data_9BM0
# 
_entry.id   9BM0 
# 
_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   9BM0         pdb_00009bm0 10.2210/pdb9bm0/pdb 
WWPDB D_1000283515 ?            ?                   
EMDB  EMD-44683    ?            ?                   
# 
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                        9BM0 
_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-2 of motor domain from full-length human dynein-1 in 5mM ATP' 
_pdbx_database_related.db_id          EMD-44683 
_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 ? ? ? ? 
5 water       nat water                                18.015     3 ? ? ? ? 
# 
_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  
5 water                       HOH 
# 
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 
HOH non-polymer         . WATER                       ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 ?    ?   ?   A . n 
A 1 1328 ASP 1328 1328 ?    ?   ?   A . n 
A 1 1329 LEU 1329 1329 ?    ?   ?   A . n 
A 1 1330 LYS 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 ?    ?   ?   A . n 
A 1 1332 VAL 1332 1332 ?    ?   ?   A . n 
A 1 1333 TRP 1333 1333 ?    ?   ?   A . n 
A 1 1334 SER 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 SER 1337 1337 ?    ?   ?   A . n 
A 1 1338 LYS 1338 1338 ?    ?   ?   A . n 
A 1 1339 VAL 1339 1339 ?    ?   ?   A . n 
A 1 1340 TRP 1340 1340 ?    ?   ?   A . n 
A 1 1341 GLU 1341 1341 ?    ?   ?   A . n 
A 1 1342 GLN 1342 1342 ?    ?   ?   A . n 
A 1 1343 ILE 1343 1343 ?    ?   ?   A . n 
A 1 1344 ASP 1344 1344 ?    ?   ?   A . n 
A 1 1345 GLN 1345 1345 ?    ?   ?   A . n 
A 1 1346 MET 1346 1346 ?    ?   ?   A . n 
A 1 1347 LYS 1347 1347 ?    ?   ?   A . n 
A 1 1348 GLU 1348 1348 ?    ?   ?   A . n 
A 1 1349 GLN 1349 1349 ?    ?   ?   A . n 
A 1 1350 PRO 1350 1350 ?    ?   ?   A . n 
A 1 1351 TRP 1351 1351 ?    ?   ?   A . n 
A 1 1352 VAL 1352 1352 ?    ?   ?   A . n 
A 1 1353 SER 1353 1353 ?    ?   ?   A . n 
A 1 1354 VAL 1354 1354 ?    ?   ?   A . n 
A 1 1355 GLN 1355 1355 ?    ?   ?   A . n 
A 1 1356 PRO 1356 1356 ?    ?   ?   A . n 
A 1 1357 ARG 1357 1357 ?    ?   ?   A . n 
A 1 1358 LYS 1358 1358 ?    ?   ?   A . n 
A 1 1359 LEU 1359 1359 ?    ?   ?   A . n 
A 1 1360 ARG 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLN 1361 1361 ?    ?   ?   A . n 
A 1 1362 ASN 1362 1362 ?    ?   ?   A . n 
A 1 1363 LEU 1363 1363 ?    ?   ?   A . n 
A 1 1364 ASP 1364 1364 ?    ?   ?   A . n 
A 1 1365 ALA 1365 1365 ?    ?   ?   A . n 
A 1 1366 LEU 1366 1366 ?    ?   ?   A . n 
A 1 1367 LEU 1367 1367 ?    ?   ?   A . n 
A 1 1368 ASN 1368 1368 ?    ?   ?   A . n 
A 1 1369 GLN 1369 1369 ?    ?   ?   A . n 
A 1 1370 LEU 1370 1370 ?    ?   ?   A . n 
A 1 1371 LYS 1371 1371 ?    ?   ?   A . n 
A 1 1372 SER 1372 1372 ?    ?   ?   A . n 
A 1 1373 PHE 1373 1373 ?    ?   ?   A . n 
A 1 1374 PRO 1374 1374 ?    ?   ?   A . n 
A 1 1375 ALA 1375 1375 ?    ?   ?   A . n 
A 1 1376 ARG 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 ARG 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLN 1379 1379 ?    ?   ?   A . n 
A 1 1380 TYR 1380 1380 ?    ?   ?   A . n 
A 1 1381 ALA 1381 1381 ?    ?   ?   A . n 
A 1 1382 SER 1382 1382 ?    ?   ?   A . n 
A 1 1383 TYR 1383 1383 ?    ?   ?   A . n 
A 1 1384 GLU 1384 1384 ?    ?   ?   A . n 
A 1 1385 PHE 1385 1385 ?    ?   ?   A . n 
A 1 1386 VAL 1386 1386 ?    ?   ?   A . n 
A 1 1387 GLN 1387 1387 ?    ?   ?   A . n 
A 1 1388 ARG 1388 1388 ?    ?   ?   A . n 
A 1 1389 LEU 1389 1389 ?    ?   ?   A . n 
A 1 1390 LEU 1390 1390 ?    ?   ?   A . n 
A 1 1391 LYS 1391 1391 ?    ?   ?   A . n 
A 1 1392 GLY 1392 1392 ?    ?   ?   A . n 
A 1 1393 TYR 1393 1393 ?    ?   ?   A . n 
A 1 1394 MET 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ILE 1396 1396 ?    ?   ?   A . n 
A 1 1397 ASN 1397 1397 ?    ?   ?   A . n 
A 1 1398 MET 1398 1398 ?    ?   ?   A . n 
A 1 1399 LEU 1399 1399 ?    ?   ?   A . n 
A 1 1400 VAL 1400 1400 ?    ?   ?   A . n 
A 1 1401 ILE 1401 1401 ?    ?   ?   A . n 
A 1 1402 GLU 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 LYS 1404 1404 ?    ?   ?   A . n 
A 1 1405 SER 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLU 1406 1406 ?    ?   ?   A . n 
A 1 1407 ALA 1407 1407 ?    ?   ?   A . n 
A 1 1408 LEU 1408 1408 ?    ?   ?   A . n 
A 1 1409 LYS 1409 1409 ?    ?   ?   A . n 
A 1 1410 ASP 1410 1410 ?    ?   ?   A . n 
A 1 1411 ARG 1411 1411 ?    ?   ?   A . n 
A 1 1412 HIS 1412 1412 ?    ?   ?   A . n 
A 1 1413 TRP 1413 1413 ?    ?   ?   A . n 
A 1 1414 LYS 1414 1414 ?    ?   ?   A . n 
A 1 1415 GLN 1415 1415 ?    ?   ?   A . n 
A 1 1416 LEU 1416 1416 ?    ?   ?   A . n 
A 1 1417 MET 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ARG 1419 1419 ?    ?   ?   A . n 
A 1 1420 LEU 1420 1420 ?    ?   ?   A . n 
A 1 1421 HIS 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 ASN 1423 1423 ?    ?   ?   A . n 
A 1 1424 TRP 1424 1424 ?    ?   ?   A . n 
A 1 1425 VAL 1425 1425 ?    ?   ?   A . n 
A 1 1426 VAL 1426 1426 ?    ?   ?   A . n 
A 1 1427 SER 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 LEU 1429 1429 ?    ?   ?   A . n 
A 1 1430 THR 1430 1430 ?    ?   ?   A . n 
A 1 1431 LEU 1431 1431 ?    ?   ?   A . n 
A 1 1432 GLY 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 ILE 1434 1434 ?    ?   ?   A . n 
A 1 1435 TRP 1435 1435 ?    ?   ?   A . n 
A 1 1436 ASP 1436 1436 ?    ?   ?   A . n 
A 1 1437 VAL 1437 1437 ?    ?   ?   A . n 
A 1 1438 ASP 1438 1438 ?    ?   ?   A . n 
A 1 1439 LEU 1439 1439 ?    ?   ?   A . n 
A 1 1440 GLN 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ASN 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 ALA 1444 1444 ?    ?   ?   A . n 
A 1 1445 ILE 1445 1445 ?    ?   ?   A . n 
A 1 1446 VAL 1446 1446 ?    ?   ?   A . n 
A 1 1447 LYS 1447 1447 ?    ?   ?   A . n 
A 1 1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1 1449 VAL 1449 1449 ?    ?   ?   A . n 
A 1 1450 LEU 1450 1450 ?    ?   ?   A . n 
A 1 1451 LEU 1451 1451 ?    ?   ?   A . n 
A 1 1452 VAL 1452 1452 ?    ?   ?   A . n 
A 1 1453 ALA 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLN 1454 1454 ?    ?   ?   A . n 
A 1 1455 GLY 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLU 1456 1456 ?    ?   ?   A . n 
A 1 1457 MET 1457 1457 1457 MET MET A . n 
A 1 1458 ALA 1458 1458 1458 ALA ALA A . n 
A 1 1459 LEU 1459 1459 1459 LEU LEU A . n 
A 1 1460 GLU 1460 1460 1460 GLU GLU A . n 
A 1 1461 GLU 1461 1461 1461 GLU GLU A . n 
A 1 1462 PHE 1462 1462 1462 PHE PHE A . n 
A 1 1463 LEU 1463 1463 1463 LEU LEU A . n 
A 1 1464 LYS 1464 1464 1464 LYS LYS A . n 
A 1 1465 GLN 1465 1465 1465 GLN GLN A . n 
A 1 1466 ILE 1466 1466 1466 ILE ILE A . n 
A 1 1467 ARG 1467 1467 1467 ARG ARG A . n 
A 1 1468 GLU 1468 1468 1468 GLU GLU A . n 
A 1 1469 VAL 1469 1469 1469 VAL VAL A . n 
A 1 1470 TRP 1470 1470 1470 TRP TRP A . n 
A 1 1471 ASN 1471 1471 1471 ASN ASN A . n 
A 1 1472 THR 1472 1472 1472 THR THR A . n 
A 1 1473 TYR 1473 1473 1473 TYR TYR A . n 
A 1 1474 GLU 1474 1474 1474 GLU GLU A . n 
A 1 1475 LEU 1475 1475 1475 LEU LEU A . n 
A 1 1476 ASP 1476 1476 1476 ASP ASP A . n 
A 1 1477 LEU 1477 1477 1477 LEU LEU A . n 
A 1 1478 VAL 1478 1478 1478 VAL VAL A . n 
A 1 1479 ASN 1479 1479 1479 ASN ASN A . n 
A 1 1480 TYR 1480 1480 1480 TYR TYR A . n 
A 1 1481 GLN 1481 1481 1481 GLN GLN A . n 
A 1 1482 ASN 1482 1482 1482 ASN ASN A . n 
A 1 1483 LYS 1483 1483 1483 LYS LYS A . n 
A 1 1484 CYS 1484 1484 1484 CYS CYS A . n 
A 1 1485 ARG 1485 1485 1485 ARG ARG A . n 
A 1 1486 LEU 1486 1486 1486 LEU LEU A . n 
A 1 1487 ILE 1487 1487 1487 ILE ILE A . n 
A 1 1488 ARG 1488 1488 1488 ARG ARG A . n 
A 1 1489 GLY 1489 1489 1489 GLY GLY A . n 
A 1 1490 TRP 1490 1490 1490 TRP TRP A . n 
A 1 1491 ASP 1491 1491 1491 ASP ASP A . n 
A 1 1492 ASP 1492 1492 1492 ASP ASP A . n 
A 1 1493 LEU 1493 1493 1493 LEU LEU A . n 
A 1 1494 PHE 1494 1494 1494 PHE PHE A . n 
A 1 1495 ASN 1495 1495 1495 ASN ASN A . n 
A 1 1496 LYS 1496 1496 1496 LYS LYS A . n 
A 1 1497 VAL 1497 1497 1497 VAL VAL A . n 
A 1 1498 LYS 1498 1498 1498 LYS LYS A . n 
A 1 1499 GLU 1499 1499 1499 GLU GLU A . n 
A 1 1500 HIS 1500 1500 1500 HIS HIS A . n 
A 1 1501 ILE 1501 1501 1501 ILE ILE A . n 
A 1 1502 ASN 1502 1502 1502 ASN ASN A . n 
A 1 1503 SER 1503 1503 1503 SER SER A . n 
A 1 1504 VAL 1504 1504 1504 VAL VAL A . n 
A 1 1505 SER 1505 1505 1505 SER SER A . n 
A 1 1506 ALA 1506 1506 1506 ALA ALA A . n 
A 1 1507 MET 1507 1507 1507 MET MET A . n 
A 1 1508 LYS 1508 1508 1508 LYS LYS A . n 
A 1 1509 LEU 1509 1509 1509 LEU LEU A . n 
A 1 1510 SER 1510 1510 1510 SER SER A . n 
A 1 1511 PRO 1511 1511 1511 PRO PRO A . n 
A 1 1512 TYR 1512 1512 1512 TYR TYR A . n 
A 1 1513 TYR 1513 1513 1513 TYR TYR A . n 
A 1 1514 LYS 1514 1514 1514 LYS LYS A . n 
A 1 1515 VAL 1515 1515 1515 VAL VAL A . n 
A 1 1516 PHE 1516 1516 1516 PHE PHE A . n 
A 1 1517 GLU 1517 1517 1517 GLU GLU A . n 
A 1 1518 GLU 1518 1518 1518 GLU GLU A . n 
A 1 1519 ASP 1519 1519 1519 ASP ASP A . n 
A 1 1520 ALA 1520 1520 1520 ALA ALA A . n 
A 1 1521 LEU 1521 1521 1521 LEU LEU A . n 
A 1 1522 SER 1522 1522 1522 SER SER A . n 
A 1 1523 TRP 1523 1523 1523 TRP TRP A . n 
A 1 1524 GLU 1524 1524 1524 GLU GLU A . n 
A 1 1525 ASP 1525 1525 1525 ASP ASP A . n 
A 1 1526 LYS 1526 1526 1526 LYS LYS A . n 
A 1 1527 LEU 1527 1527 1527 LEU LEU A . n 
A 1 1528 ASN 1528 1528 1528 ASN ASN A . n 
A 1 1529 ARG 1529 1529 1529 ARG ARG A . n 
A 1 1530 ILE 1530 1530 1530 ILE ILE A . n 
A 1 1531 MET 1531 1531 1531 MET MET A . n 
A 1 1532 ALA 1532 1532 1532 ALA ALA A . n 
A 1 1533 LEU 1533 1533 1533 LEU LEU A . n 
A 1 1534 PHE 1534 1534 1534 PHE PHE A . n 
A 1 1535 ASP 1535 1535 1535 ASP ASP A . n 
A 1 1536 VAL 1536 1536 1536 VAL VAL A . n 
A 1 1537 TRP 1537 1537 1537 TRP TRP A . n 
A 1 1538 ILE 1538 1538 1538 ILE ILE A . n 
A 1 1539 ASP 1539 1539 1539 ASP ASP A . n 
A 1 1540 VAL 1540 1540 1540 VAL VAL A . n 
A 1 1541 GLN 1541 1541 1541 GLN GLN A . n 
A 1 1542 ARG 1542 1542 1542 ARG ARG A . n 
A 1 1543 ARG 1543 1543 1543 ARG ARG A . n 
A 1 1544 TRP 1544 1544 1544 TRP TRP A . n 
A 1 1545 VAL 1545 1545 1545 VAL VAL A . n 
A 1 1546 TYR 1546 1546 1546 TYR TYR A . n 
A 1 1547 LEU 1547 1547 1547 LEU LEU A . n 
A 1 1548 GLU 1548 1548 1548 GLU GLU A . n 
A 1 1549 GLY 1549 1549 1549 GLY GLY A . n 
A 1 1550 ILE 1550 1550 1550 ILE ILE A . n 
A 1 1551 PHE 1551 1551 1551 PHE PHE A . n 
A 1 1552 THR 1552 1552 1552 THR THR A . n 
A 1 1553 GLY 1553 1553 1553 GLY GLY A . n 
A 1 1554 SER 1554 1554 1554 SER SER A . n 
A 1 1555 ALA 1555 1555 1555 ALA ALA A . n 
A 1 1556 ASP 1556 1556 1556 ASP ASP A . n 
A 1 1557 ILE 1557 1557 1557 ILE ILE A . n 
A 1 1558 LYS 1558 1558 1558 LYS LYS A . n 
A 1 1559 HIS 1559 1559 1559 HIS HIS A . n 
A 1 1560 LEU 1560 1560 1560 LEU LEU A . n 
A 1 1561 LEU 1561 1561 1561 LEU LEU A . n 
A 1 1562 PRO 1562 1562 1562 PRO PRO A . n 
A 1 1563 VAL 1563 1563 1563 VAL VAL A . n 
A 1 1564 GLU 1564 1564 1564 GLU GLU A . n 
A 1 1565 THR 1565 1565 1565 THR THR A . n 
A 1 1566 GLN 1566 1566 1566 GLN GLN A . n 
A 1 1567 ARG 1567 1567 1567 ARG ARG A . n 
A 1 1568 PHE 1568 1568 1568 PHE PHE A . n 
A 1 1569 GLN 1569 1569 1569 GLN GLN A . n 
A 1 1570 SER 1570 1570 1570 SER SER A . n 
A 1 1571 ILE 1571 1571 1571 ILE ILE A . n 
A 1 1572 SER 1572 1572 1572 SER SER A . n 
A 1 1573 THR 1573 1573 1573 THR THR A . n 
A 1 1574 GLU 1574 1574 1574 GLU GLU A . n 
A 1 1575 PHE 1575 1575 1575 PHE PHE A . n 
A 1 1576 LEU 1576 1576 1576 LEU LEU A . n 
A 1 1577 ALA 1577 1577 1577 ALA ALA A . n 
A 1 1578 LEU 1578 1578 1578 LEU LEU A . n 
A 1 1579 MET 1579 1579 1579 MET MET A . n 
A 1 1580 LYS 1580 1580 1580 LYS LYS A . n 
A 1 1581 LYS 1581 1581 1581 LYS LYS A . n 
A 1 1582 VAL 1582 1582 1582 VAL VAL A . n 
A 1 1583 SER 1583 1583 1583 SER SER A . n 
A 1 1584 LYS 1584 1584 1584 LYS LYS A . n 
A 1 1585 SER 1585 1585 1585 SER SER A . n 
A 1 1586 PRO 1586 1586 1586 PRO PRO A . n 
A 1 1587 LEU 1587 1587 1587 LEU LEU A . n 
A 1 1588 VAL 1588 1588 1588 VAL VAL A . n 
A 1 1589 MET 1589 1589 1589 MET MET A . n 
A 1 1590 ASP 1590 1590 1590 ASP ASP A . n 
A 1 1591 VAL 1591 1591 1591 VAL VAL A . n 
A 1 1592 LEU 1592 1592 1592 LEU LEU A . n 
A 1 1593 ASN 1593 1593 1593 ASN ASN A . n 
A 1 1594 ILE 1594 1594 1594 ILE ILE A . n 
A 1 1595 GLN 1595 1595 1595 GLN GLN A . n 
A 1 1596 GLY 1596 1596 1596 GLY GLY A . n 
A 1 1597 VAL 1597 1597 1597 VAL VAL A . n 
A 1 1598 GLN 1598 1598 1598 GLN GLN A . n 
A 1 1599 ARG 1599 1599 1599 ARG ARG A . n 
A 1 1600 SER 1600 1600 1600 SER SER A . n 
A 1 1601 LEU 1601 1601 1601 LEU LEU A . n 
A 1 1602 GLU 1602 1602 1602 GLU GLU A . n 
A 1 1603 ARG 1603 1603 1603 ARG ARG A . n 
A 1 1604 LEU 1604 1604 1604 LEU LEU A . n 
A 1 1605 ALA 1605 1605 1605 ALA ALA A . n 
A 1 1606 ASP 1606 1606 1606 ASP ASP A . n 
A 1 1607 LEU 1607 1607 1607 LEU LEU A . n 
A 1 1608 LEU 1608 1608 1608 LEU LEU A . n 
A 1 1609 GLY 1609 1609 1609 GLY GLY A . n 
A 1 1610 LYS 1610 1610 1610 LYS LYS A . n 
A 1 1611 ILE 1611 1611 1611 ILE ILE A . n 
A 1 1612 GLN 1612 1612 1612 GLN GLN A . n 
A 1 1613 LYS 1613 1613 1613 LYS LYS A . n 
A 1 1614 ALA 1614 1614 1614 ALA ALA A . n 
A 1 1615 LEU 1615 1615 1615 LEU LEU A . n 
A 1 1616 GLY 1616 1616 1616 GLY GLY A . n 
A 1 1617 GLU 1617 1617 1617 GLU GLU A . n 
A 1 1618 TYR 1618 1618 1618 TYR TYR A . n 
A 1 1619 LEU 1619 1619 1619 LEU LEU A . n 
A 1 1620 GLU 1620 1620 1620 GLU GLU A . n 
A 1 1621 ARG 1621 1621 1621 ARG ARG A . n 
A 1 1622 GLU 1622 1622 1622 GLU GLU A . n 
A 1 1623 ARG 1623 1623 1623 ARG ARG A . n 
A 1 1624 SER 1624 1624 1624 SER SER A . n 
A 1 1625 SER 1625 1625 1625 SER SER A . n 
A 1 1626 PHE 1626 1626 1626 PHE PHE A . n 
A 1 1627 PRO 1627 1627 1627 PRO PRO A . n 
A 1 1628 ARG 1628 1628 1628 ARG ARG A . n 
A 1 1629 PHE 1629 1629 1629 PHE PHE A . n 
A 1 1630 TYR 1630 1630 1630 TYR TYR A . n 
A 1 1631 PHE 1631 1631 1631 PHE PHE A . n 
A 1 1632 VAL 1632 1632 1632 VAL VAL A . n 
A 1 1633 GLY 1633 1633 1633 GLY GLY A . n 
A 1 1634 ASP 1634 1634 1634 ASP ASP A . n 
A 1 1635 GLU 1635 1635 1635 GLU GLU A . n 
A 1 1636 ASP 1636 1636 1636 ASP ASP A . n 
A 1 1637 LEU 1637 1637 1637 LEU LEU A . n 
A 1 1638 LEU 1638 1638 1638 LEU LEU A . n 
A 1 1639 GLU 1639 1639 1639 GLU GLU A . n 
A 1 1640 ILE 1640 1640 1640 ILE ILE A . n 
A 1 1641 ILE 1641 1641 1641 ILE ILE A . n 
A 1 1642 GLY 1642 1642 1642 GLY GLY A . n 
A 1 1643 ASN 1643 1643 1643 ASN ASN A . n 
A 1 1644 SER 1644 1644 1644 SER SER A . n 
A 1 1645 LYS 1645 1645 1645 LYS LYS A . n 
A 1 1646 ASN 1646 1646 1646 ASN ASN A . n 
A 1 1647 VAL 1647 1647 1647 VAL VAL A . n 
A 1 1648 ALA 1648 1648 1648 ALA ALA A . n 
A 1 1649 LYS 1649 1649 1649 LYS LYS A . n 
A 1 1650 LEU 1650 1650 1650 LEU LEU A . n 
A 1 1651 GLN 1651 1651 1651 GLN GLN A . n 
A 1 1652 LYS 1652 1652 1652 LYS LYS A . n 
A 1 1653 HIS 1653 1653 1653 HIS HIS A . n 
A 1 1654 PHE 1654 1654 1654 PHE PHE A . n 
A 1 1655 LYS 1655 1655 1655 LYS LYS A . n 
A 1 1656 LYS 1656 1656 1656 LYS LYS A . n 
A 1 1657 MET 1657 1657 1657 MET MET A . n 
A 1 1658 PHE 1658 1658 1658 PHE PHE A . n 
A 1 1659 ALA 1659 1659 1659 ALA ALA A . n 
A 1 1660 GLY 1660 1660 1660 GLY GLY A . n 
A 1 1661 VAL 1661 1661 1661 VAL VAL A . n 
A 1 1662 SER 1662 1662 1662 SER SER A . n 
A 1 1663 SER 1663 1663 1663 SER SER A . n 
A 1 1664 ILE 1664 1664 1664 ILE ILE A . n 
A 1 1665 ILE 1665 1665 1665 ILE ILE A . n 
A 1 1666 LEU 1666 1666 1666 LEU LEU A . n 
A 1 1667 ASN 1667 1667 1667 ASN ASN A . n 
A 1 1668 GLU 1668 1668 1668 GLU GLU A . n 
A 1 1669 ASP 1669 1669 1669 ASP ASP A . n 
A 1 1670 ASN 1670 1670 1670 ASN ASN A . n 
A 1 1671 SER 1671 1671 1671 SER SER A . n 
A 1 1672 VAL 1672 1672 1672 VAL VAL A . n 
A 1 1673 VAL 1673 1673 1673 VAL VAL A . n 
A 1 1674 LEU 1674 1674 1674 LEU LEU A . n 
A 1 1675 GLY 1675 1675 1675 GLY GLY A . n 
A 1 1676 ILE 1676 1676 1676 ILE ILE A . n 
A 1 1677 SER 1677 1677 1677 SER SER A . n 
A 1 1678 SER 1678 1678 1678 SER SER A . n 
A 1 1679 ARG 1679 1679 1679 ARG ARG A . n 
A 1 1680 GLU 1680 1680 1680 GLU GLU A . n 
A 1 1681 GLY 1681 1681 1681 GLY GLY A . n 
A 1 1682 GLU 1682 1682 1682 GLU GLU A . n 
A 1 1683 GLU 1683 1683 1683 GLU GLU A . n 
A 1 1684 VAL 1684 1684 1684 VAL VAL A . n 
A 1 1685 MET 1685 1685 1685 MET MET A . n 
A 1 1686 PHE 1686 1686 1686 PHE PHE A . n 
A 1 1687 LYS 1687 1687 1687 LYS LYS A . n 
A 1 1688 THR 1688 1688 1688 THR THR A . n 
A 1 1689 PRO 1689 1689 1689 PRO PRO A . n 
A 1 1690 VAL 1690 1690 1690 VAL VAL A . n 
A 1 1691 SER 1691 1691 1691 SER SER A . n 
A 1 1692 ILE 1692 1692 1692 ILE ILE A . n 
A 1 1693 THR 1693 1693 1693 THR THR A . n 
A 1 1694 GLU 1694 1694 1694 GLU GLU A . n 
A 1 1695 HIS 1695 1695 1695 HIS HIS A . n 
A 1 1696 PRO 1696 1696 1696 PRO PRO A . n 
A 1 1697 LYS 1697 1697 1697 LYS LYS A . n 
A 1 1698 ILE 1698 1698 1698 ILE ILE A . n 
A 1 1699 ASN 1699 1699 1699 ASN ASN A . n 
A 1 1700 GLU 1700 1700 1700 GLU GLU A . n 
A 1 1701 TRP 1701 1701 1701 TRP TRP A . n 
A 1 1702 LEU 1702 1702 1702 LEU LEU A . n 
A 1 1703 THR 1703 1703 1703 THR THR A . n 
A 1 1704 LEU 1704 1704 1704 LEU LEU A . n 
A 1 1705 VAL 1705 1705 1705 VAL VAL A . n 
A 1 1706 GLU 1706 1706 1706 GLU GLU A . n 
A 1 1707 LYS 1707 1707 1707 LYS LYS A . n 
A 1 1708 GLU 1708 1708 1708 GLU GLU A . n 
A 1 1709 MET 1709 1709 1709 MET MET A . n 
A 1 1710 ARG 1710 1710 1710 ARG ARG A . n 
A 1 1711 VAL 1711 1711 1711 VAL VAL A . n 
A 1 1712 THR 1712 1712 1712 THR THR A . n 
A 1 1713 LEU 1713 1713 1713 LEU LEU A . n 
A 1 1714 ALA 1714 1714 1714 ALA ALA A . n 
A 1 1715 LYS 1715 1715 1715 LYS LYS A . n 
A 1 1716 LEU 1716 1716 1716 LEU LEU A . n 
A 1 1717 LEU 1717 1717 1717 LEU LEU A . n 
A 1 1718 ALA 1718 1718 1718 ALA ALA A . n 
A 1 1719 GLU 1719 1719 1719 GLU GLU A . n 
A 1 1720 SER 1720 1720 1720 SER SER A . n 
A 1 1721 VAL 1721 1721 1721 VAL VAL A . n 
A 1 1722 THR 1722 1722 1722 THR THR A . n 
A 1 1723 GLU 1723 1723 1723 GLU GLU A . n 
A 1 1724 VAL 1724 1724 1724 VAL VAL A . n 
A 1 1725 GLU 1725 1725 1725 GLU GLU A . n 
A 1 1726 ILE 1726 1726 1726 ILE ILE A . n 
A 1 1727 PHE 1727 1727 1727 PHE PHE A . n 
A 1 1728 GLY 1728 1728 1728 GLY GLY A . n 
A 1 1729 LYS 1729 1729 1729 LYS LYS A . n 
A 1 1730 ALA 1730 1730 1730 ALA ALA A . n 
A 1 1731 THR 1731 1731 1731 THR THR A . n 
A 1 1732 SER 1732 1732 1732 SER SER A . n 
A 1 1733 ILE 1733 1733 1733 ILE ILE A . n 
A 1 1734 ASP 1734 1734 1734 ASP ASP A . n 
A 1 1735 PRO 1735 1735 1735 PRO PRO A . n 
A 1 1736 ASN 1736 1736 1736 ASN ASN A . n 
A 1 1737 THR 1737 1737 1737 THR THR A . n 
A 1 1738 TYR 1738 1738 1738 TYR TYR A . n 
A 1 1739 ILE 1739 1739 1739 ILE ILE A . n 
A 1 1740 THR 1740 1740 1740 THR THR A . n 
A 1 1741 TRP 1741 1741 1741 TRP TRP A . n 
A 1 1742 ILE 1742 1742 1742 ILE ILE A . n 
A 1 1743 ASP 1743 1743 1743 ASP ASP A . n 
A 1 1744 LYS 1744 1744 1744 LYS LYS A . n 
A 1 1745 TYR 1745 1745 1745 TYR TYR A . n 
A 1 1746 GLN 1746 1746 1746 GLN GLN A . n 
A 1 1747 ALA 1747 1747 1747 ALA ALA A . n 
A 1 1748 GLN 1748 1748 1748 GLN GLN A . n 
A 1 1749 LEU 1749 1749 1749 LEU LEU A . n 
A 1 1750 VAL 1750 1750 1750 VAL VAL A . n 
A 1 1751 VAL 1751 1751 1751 VAL VAL A . n 
A 1 1752 LEU 1752 1752 1752 LEU LEU A . n 
A 1 1753 SER 1753 1753 1753 SER SER A . n 
A 1 1754 ALA 1754 1754 1754 ALA ALA A . n 
A 1 1755 GLN 1755 1755 1755 GLN GLN A . n 
A 1 1756 ILE 1756 1756 1756 ILE ILE A . n 
A 1 1757 ALA 1757 1757 1757 ALA ALA A . n 
A 1 1758 TRP 1758 1758 1758 TRP TRP A . n 
A 1 1759 SER 1759 1759 1759 SER SER A . n 
A 1 1760 GLU 1760 1760 1760 GLU GLU A . n 
A 1 1761 ASN 1761 1761 1761 ASN ASN A . n 
A 1 1762 VAL 1762 1762 1762 VAL VAL A . n 
A 1 1763 GLU 1763 1763 1763 GLU GLU A . n 
A 1 1764 THR 1764 1764 1764 THR THR A . n 
A 1 1765 ALA 1765 1765 1765 ALA ALA A . n 
A 1 1766 LEU 1766 1766 1766 LEU LEU A . n 
A 1 1767 SER 1767 1767 1767 SER SER A . n 
A 1 1768 SER 1768 1768 1768 SER SER A . n 
A 1 1769 MET 1769 1769 1769 MET MET A . n 
A 1 1770 GLY 1770 1770 1770 GLY GLY A . n 
A 1 1771 GLY 1771 1771 1771 GLY GLY A . n 
A 1 1772 GLY 1772 1772 1772 GLY GLY A . n 
A 1 1773 GLY 1773 1773 1773 GLY GLY A . n 
A 1 1774 ASP 1774 1774 1774 ASP ASP A . n 
A 1 1775 ALA 1775 1775 1775 ALA ALA A . n 
A 1 1776 ALA 1776 1776 1776 ALA ALA A . n 
A 1 1777 PRO 1777 1777 1777 PRO PRO A . n 
A 1 1778 LEU 1778 1778 1778 LEU LEU A . n 
A 1 1779 HIS 1779 1779 1779 HIS HIS A . n 
A 1 1780 SER 1780 1780 1780 SER SER A . n 
A 1 1781 VAL 1781 1781 1781 VAL VAL A . n 
A 1 1782 LEU 1782 1782 1782 LEU LEU A . n 
A 1 1783 SER 1783 1783 1783 SER SER A . n 
A 1 1784 ASN 1784 1784 1784 ASN ASN A . n 
A 1 1785 VAL 1785 1785 1785 VAL VAL A . n 
A 1 1786 GLU 1786 1786 1786 GLU GLU A . n 
A 1 1787 VAL 1787 1787 1787 VAL VAL A . n 
A 1 1788 THR 1788 1788 1788 THR THR A . n 
A 1 1789 LEU 1789 1789 1789 LEU LEU A . n 
A 1 1790 ASN 1790 1790 1790 ASN ASN A . n 
A 1 1791 VAL 1791 1791 1791 VAL VAL A . n 
A 1 1792 LEU 1792 1792 1792 LEU LEU A . n 
A 1 1793 ALA 1793 1793 1793 ALA ALA A . n 
A 1 1794 ASP 1794 1794 1794 ASP ASP A . n 
A 1 1795 SER 1795 1795 1795 SER SER A . n 
A 1 1796 VAL 1796 1796 1796 VAL VAL A . n 
A 1 1797 LEU 1797 1797 1797 LEU LEU A . n 
A 1 1798 MET 1798 1798 1798 MET MET A . n 
A 1 1799 GLU 1799 1799 1799 GLU GLU A . n 
A 1 1800 GLN 1800 1800 1800 GLN GLN A . n 
A 1 1801 PRO 1801 1801 1801 PRO PRO A . n 
A 1 1802 PRO 1802 1802 1802 PRO PRO A . n 
A 1 1803 LEU 1803 1803 1803 LEU LEU A . n 
A 1 1804 ARG 1804 1804 1804 ARG ARG A . n 
A 1 1805 ARG 1805 1805 1805 ARG ARG A . n 
A 1 1806 ARG 1806 1806 1806 ARG ARG A . n 
A 1 1807 LYS 1807 1807 1807 LYS LYS A . n 
A 1 1808 LEU 1808 1808 1808 LEU LEU A . n 
A 1 1809 GLU 1809 1809 1809 GLU GLU A . n 
A 1 1810 HIS 1810 1810 1810 HIS HIS A . n 
A 1 1811 LEU 1811 1811 1811 LEU LEU A . n 
A 1 1812 ILE 1812 1812 1812 ILE ILE A . n 
A 1 1813 THR 1813 1813 1813 THR THR A . n 
A 1 1814 GLU 1814 1814 1814 GLU GLU A . n 
A 1 1815 LEU 1815 1815 1815 LEU LEU A . n 
A 1 1816 VAL 1816 1816 1816 VAL VAL A . n 
A 1 1817 HIS 1817 1817 1817 HIS HIS A . n 
A 1 1818 GLN 1818 1818 1818 GLN GLN A . n 
A 1 1819 ARG 1819 1819 1819 ARG ARG A . n 
A 1 1820 ASP 1820 1820 1820 ASP ASP A . n 
A 1 1821 VAL 1821 1821 1821 VAL VAL A . n 
A 1 1822 THR 1822 1822 1822 THR THR A . n 
A 1 1823 ARG 1823 1823 1823 ARG ARG A . n 
A 1 1824 SER 1824 1824 1824 SER SER A . n 
A 1 1825 LEU 1825 1825 1825 LEU LEU A . n 
A 1 1826 ILE 1826 1826 1826 ILE ILE A . n 
A 1 1827 LYS 1827 1827 1827 LYS LYS A . n 
A 1 1828 SER 1828 1828 1828 SER SER A . n 
A 1 1829 LYS 1829 1829 1829 LYS LYS A . n 
A 1 1830 ILE 1830 1830 1830 ILE ILE A . n 
A 1 1831 ASP 1831 1831 1831 ASP ASP A . n 
A 1 1832 ASN 1832 1832 1832 ASN ASN A . n 
A 1 1833 ALA 1833 1833 1833 ALA ALA A . n 
A 1 1834 LYS 1834 1834 1834 LYS LYS A . n 
A 1 1835 SER 1835 1835 1835 SER SER A . n 
A 1 1836 PHE 1836 1836 1836 PHE PHE A . n 
A 1 1837 GLU 1837 1837 1837 GLU GLU A . n 
A 1 1838 TRP 1838 1838 1838 TRP TRP A . n 
A 1 1839 LEU 1839 1839 1839 LEU LEU A . n 
A 1 1840 SER 1840 1840 1840 SER SER A . n 
A 1 1841 GLN 1841 1841 1841 GLN GLN A . n 
A 1 1842 MET 1842 1842 1842 MET MET A . n 
A 1 1843 ARG 1843 1843 1843 ARG ARG A . n 
A 1 1844 PHE 1844 1844 1844 PHE PHE A . n 
A 1 1845 TYR 1845 1845 1845 TYR TYR A . n 
A 1 1846 PHE 1846 1846 1846 PHE PHE A . n 
A 1 1847 ASP 1847 1847 1847 ASP ASP A . n 
A 1 1848 PRO 1848 1848 1848 PRO PRO A . n 
A 1 1849 LYS 1849 1849 1849 LYS LYS A . n 
A 1 1850 GLN 1850 1850 1850 GLN GLN A . n 
A 1 1851 THR 1851 1851 1851 THR THR A . n 
A 1 1852 ASP 1852 1852 1852 ASP ASP A . n 
A 1 1853 VAL 1853 1853 1853 VAL VAL A . n 
A 1 1854 LEU 1854 1854 1854 LEU LEU A . n 
A 1 1855 GLN 1855 1855 1855 GLN GLN A . n 
A 1 1856 GLN 1856 1856 1856 GLN GLN A . n 
A 1 1857 LEU 1857 1857 1857 LEU LEU A . n 
A 1 1858 SER 1858 1858 1858 SER SER A . n 
A 1 1859 ILE 1859 1859 1859 ILE ILE A . n 
A 1 1860 GLN 1860 1860 1860 GLN GLN A . n 
A 1 1861 MET 1861 1861 1861 MET MET A . n 
A 1 1862 ALA 1862 1862 1862 ALA ALA A . n 
A 1 1863 ASN 1863 1863 1863 ASN ASN A . n 
A 1 1864 ALA 1864 1864 1864 ALA ALA A . n 
A 1 1865 LYS 1865 1865 1865 LYS LYS A . n 
A 1 1866 PHE 1866 1866 1866 PHE PHE A . n 
A 1 1867 ASN 1867 1867 1867 ASN ASN A . n 
A 1 1868 TYR 1868 1868 1868 TYR TYR A . n 
A 1 1869 GLY 1869 1869 1869 GLY GLY A . n 
A 1 1870 PHE 1870 1870 1870 PHE PHE A . n 
A 1 1871 GLU 1871 1871 1871 GLU GLU A . n 
A 1 1872 TYR 1872 1872 1872 TYR TYR A . n 
A 1 1873 LEU 1873 1873 1873 LEU LEU A . n 
A 1 1874 GLY 1874 1874 1874 GLY GLY A . n 
A 1 1875 VAL 1875 1875 1875 VAL VAL A . n 
A 1 1876 GLN 1876 1876 1876 GLN GLN A . n 
A 1 1877 ASP 1877 1877 1877 ASP ASP A . n 
A 1 1878 LYS 1878 1878 1878 LYS LYS A . n 
A 1 1879 LEU 1879 1879 1879 LEU LEU A . n 
A 1 1880 VAL 1880 1880 1880 VAL VAL A . n 
A 1 1881 GLN 1881 1881 1881 GLN GLN A . n 
A 1 1882 THR 1882 1882 1882 THR THR A . n 
A 1 1883 PRO 1883 1883 1883 PRO PRO A . n 
A 1 1884 LEU 1884 1884 1884 LEU LEU A . n 
A 1 1885 THR 1885 1885 1885 THR THR A . n 
A 1 1886 ASP 1886 1886 1886 ASP ASP A . n 
A 1 1887 ARG 1887 1887 1887 ARG ARG A . n 
A 1 1888 CYS 1888 1888 1888 CYS CYS A . n 
A 1 1889 TYR 1889 1889 1889 TYR TYR A . n 
A 1 1890 LEU 1890 1890 1890 LEU LEU A . n 
A 1 1891 THR 1891 1891 1891 THR THR A . n 
A 1 1892 MET 1892 1892 1892 MET MET A . n 
A 1 1893 THR 1893 1893 1893 THR THR A . n 
A 1 1894 GLN 1894 1894 1894 GLN GLN A . n 
A 1 1895 ALA 1895 1895 1895 ALA ALA A . n 
A 1 1896 LEU 1896 1896 1896 LEU LEU A . n 
A 1 1897 GLU 1897 1897 1897 GLU GLU A . n 
A 1 1898 ALA 1898 1898 1898 ALA ALA A . n 
A 1 1899 ARG 1899 1899 1899 ARG ARG A . n 
A 1 1900 LEU 1900 1900 1900 LEU LEU A . n 
A 1 1901 GLY 1901 1901 1901 GLY GLY A . n 
A 1 1902 GLY 1902 1902 1902 GLY GLY A . n 
A 1 1903 SER 1903 1903 1903 SER SER A . n 
A 1 1904 PRO 1904 1904 1904 PRO PRO A . n 
A 1 1905 PHE 1905 1905 1905 PHE PHE A . n 
A 1 1906 GLY 1906 1906 1906 GLY GLY A . n 
A 1 1907 PRO 1907 1907 1907 PRO PRO A . n 
A 1 1908 ALA 1908 1908 1908 ALA ALA A . n 
A 1 1909 GLY 1909 1909 1909 GLY GLY A . n 
A 1 1910 THR 1910 1910 1910 THR THR A . n 
A 1 1911 GLY 1911 1911 1911 GLY GLY A . n 
A 1 1912 LYS 1912 1912 1912 LYS LYS A . n 
A 1 1913 THR 1913 1913 1913 THR THR A . n 
A 1 1914 GLU 1914 1914 1914 GLU GLU A . n 
A 1 1915 SER 1915 1915 1915 SER SER A . n 
A 1 1916 VAL 1916 1916 1916 VAL VAL A . n 
A 1 1917 LYS 1917 1917 1917 LYS LYS A . n 
A 1 1918 ALA 1918 1918 1918 ALA ALA A . n 
A 1 1919 LEU 1919 1919 1919 LEU LEU A . n 
A 1 1920 GLY 1920 1920 1920 GLY GLY A . n 
A 1 1921 HIS 1921 1921 1921 HIS HIS A . n 
A 1 1922 GLN 1922 1922 1922 GLN GLN A . n 
A 1 1923 LEU 1923 1923 1923 LEU LEU A . n 
A 1 1924 GLY 1924 1924 1924 GLY GLY A . n 
A 1 1925 ARG 1925 1925 1925 ARG ARG A . n 
A 1 1926 PHE 1926 1926 1926 PHE PHE A . n 
A 1 1927 VAL 1927 1927 1927 VAL VAL A . n 
A 1 1928 LEU 1928 1928 1928 LEU LEU A . n 
A 1 1929 VAL 1929 1929 1929 VAL VAL A . n 
A 1 1930 PHE 1930 1930 1930 PHE PHE A . n 
A 1 1931 ASN 1931 1931 1931 ASN ASN A . n 
A 1 1932 CYS 1932 1932 1932 CYS CYS A . n 
A 1 1933 ASP 1933 1933 1933 ASP ASP A . n 
A 1 1934 GLU 1934 1934 1934 GLU GLU A . n 
A 1 1935 THR 1935 1935 1935 THR THR A . n 
A 1 1936 PHE 1936 1936 1936 PHE PHE A . n 
A 1 1937 ASP 1937 1937 1937 ASP ASP A . n 
A 1 1938 PHE 1938 1938 1938 PHE PHE A . n 
A 1 1939 GLN 1939 1939 1939 GLN GLN A . n 
A 1 1940 ALA 1940 1940 1940 ALA ALA A . n 
A 1 1941 MET 1941 1941 1941 MET MET A . n 
A 1 1942 GLY 1942 1942 1942 GLY GLY A . n 
A 1 1943 ARG 1943 1943 1943 ARG ARG A . n 
A 1 1944 ILE 1944 1944 1944 ILE ILE A . n 
A 1 1945 PHE 1945 1945 1945 PHE PHE A . n 
A 1 1946 VAL 1946 1946 1946 VAL VAL A . n 
A 1 1947 GLY 1947 1947 1947 GLY GLY A . n 
A 1 1948 LEU 1948 1948 1948 LEU LEU A . n 
A 1 1949 CYS 1949 1949 1949 CYS CYS A . n 
A 1 1950 GLN 1950 1950 1950 GLN GLN A . n 
A 1 1951 VAL 1951 1951 1951 VAL VAL A . n 
A 1 1952 GLY 1952 1952 1952 GLY GLY A . n 
A 1 1953 ALA 1953 1953 1953 ALA ALA A . n 
A 1 1954 TRP 1954 1954 1954 TRP TRP A . n 
A 1 1955 GLY 1955 1955 1955 GLY GLY A . n 
A 1 1956 CYS 1956 1956 1956 CYS CYS A . n 
A 1 1957 PHE 1957 1957 1957 PHE PHE A . n 
A 1 1958 ASP 1958 1958 1958 ASP ASP A . n 
A 1 1959 GLU 1959 1959 1959 GLU GLU A . n 
A 1 1960 PHE 1960 1960 1960 PHE PHE A . n 
A 1 1961 ASN 1961 1961 1961 ASN ASN A . n 
A 1 1962 ARG 1962 1962 1962 ARG ARG A . n 
A 1 1963 LEU 1963 1963 1963 LEU LEU A . n 
A 1 1964 GLU 1964 1964 1964 GLU GLU A . n 
A 1 1965 GLU 1965 1965 1965 GLU GLU A . n 
A 1 1966 ARG 1966 1966 1966 ARG ARG A . n 
A 1 1967 MET 1967 1967 1967 MET MET A . n 
A 1 1968 LEU 1968 1968 1968 LEU LEU A . n 
A 1 1969 SER 1969 1969 1969 SER SER A . n 
A 1 1970 ALA 1970 1970 1970 ALA ALA A . n 
A 1 1971 VAL 1971 1971 1971 VAL VAL A . n 
A 1 1972 SER 1972 1972 1972 SER SER A . n 
A 1 1973 GLN 1973 1973 1973 GLN GLN A . n 
A 1 1974 GLN 1974 1974 1974 GLN GLN A . n 
A 1 1975 VAL 1975 1975 1975 VAL VAL A . n 
A 1 1976 GLN 1976 1976 1976 GLN GLN A . n 
A 1 1977 CYS 1977 1977 1977 CYS CYS A . n 
A 1 1978 ILE 1978 1978 1978 ILE ILE A . n 
A 1 1979 GLN 1979 1979 1979 GLN GLN A . n 
A 1 1980 GLU 1980 1980 1980 GLU GLU A . n 
A 1 1981 ALA 1981 1981 1981 ALA ALA A . n 
A 1 1982 LEU 1982 1982 1982 LEU LEU A . n 
A 1 1983 ARG 1983 1983 1983 ARG ARG A . n 
A 1 1984 GLU 1984 1984 1984 GLU GLU A . n 
A 1 1985 HIS 1985 1985 1985 HIS HIS A . n 
A 1 1986 SER 1986 1986 1986 SER SER A . n 
A 1 1987 ASN 1987 1987 1987 ASN ASN A . n 
A 1 1988 PRO 1988 1988 1988 PRO PRO A . n 
A 1 1989 ASN 1989 1989 1989 ASN ASN A . n 
A 1 1990 TYR 1990 1990 1990 TYR TYR A . n 
A 1 1991 ASP 1991 1991 1991 ASP ASP A . n 
A 1 1992 LYS 1992 1992 1992 LYS LYS A . n 
A 1 1993 THR 1993 1993 1993 THR THR A . n 
A 1 1994 SER 1994 1994 1994 SER SER A . n 
A 1 1995 ALA 1995 1995 1995 ALA ALA A . n 
A 1 1996 PRO 1996 1996 1996 PRO PRO A . n 
A 1 1997 ILE 1997 1997 1997 ILE ILE A . n 
A 1 1998 THR 1998 1998 1998 THR THR A . n 
A 1 1999 CYS 1999 1999 1999 CYS CYS A . n 
A 1 2000 GLU 2000 2000 2000 GLU GLU A . n 
A 1 2001 LEU 2001 2001 2001 LEU LEU A . n 
A 1 2002 LEU 2002 2002 2002 LEU LEU A . n 
A 1 2003 ASN 2003 2003 2003 ASN ASN A . n 
A 1 2004 LYS 2004 2004 2004 LYS LYS A . n 
A 1 2005 GLN 2005 2005 2005 GLN GLN A . n 
A 1 2006 VAL 2006 2006 2006 VAL VAL A . n 
A 1 2007 LYS 2007 2007 2007 LYS LYS A . n 
A 1 2008 VAL 2008 2008 2008 VAL VAL A . n 
A 1 2009 SER 2009 2009 2009 SER SER A . n 
A 1 2010 PRO 2010 2010 2010 PRO PRO A . n 
A 1 2011 ASP 2011 2011 2011 ASP ASP A . n 
A 1 2012 MET 2012 2012 2012 MET MET A . n 
A 1 2013 ALA 2013 2013 2013 ALA ALA A . n 
A 1 2014 ILE 2014 2014 2014 ILE ILE A . n 
A 1 2015 PHE 2015 2015 2015 PHE PHE A . n 
A 1 2016 ILE 2016 2016 2016 ILE ILE A . n 
A 1 2017 THR 2017 2017 2017 THR THR A . n 
A 1 2018 MET 2018 2018 2018 MET MET A . n 
A 1 2019 ASN 2019 2019 2019 ASN ASN A . n 
A 1 2020 PRO 2020 2020 2020 PRO PRO A . n 
A 1 2021 GLY 2021 2021 2021 GLY GLY A . n 
A 1 2022 TYR 2022 2022 2022 TYR TYR A . n 
A 1 2023 ALA 2023 2023 2023 ALA ALA A . n 
A 1 2024 GLY 2024 2024 2024 GLY GLY A . n 
A 1 2025 ARG 2025 2025 2025 ARG ARG A . n 
A 1 2026 SER 2026 2026 2026 SER SER A . n 
A 1 2027 ASN 2027 2027 2027 ASN ASN A . n 
A 1 2028 LEU 2028 2028 2028 LEU LEU A . n 
A 1 2029 PRO 2029 2029 2029 PRO PRO A . n 
A 1 2030 ASP 2030 2030 2030 ASP ASP A . n 
A 1 2031 ASN 2031 2031 2031 ASN ASN A . n 
A 1 2032 LEU 2032 2032 2032 LEU LEU A . n 
A 1 2033 LYS 2033 2033 2033 LYS LYS A . n 
A 1 2034 LYS 2034 2034 2034 LYS LYS A . n 
A 1 2035 LEU 2035 2035 2035 LEU LEU A . n 
A 1 2036 PHE 2036 2036 2036 PHE PHE A . n 
A 1 2037 ARG 2037 2037 2037 ARG ARG A . n 
A 1 2038 SER 2038 2038 2038 SER SER A . n 
A 1 2039 LEU 2039 2039 2039 LEU LEU A . n 
A 1 2040 ALA 2040 2040 2040 ALA ALA A . n 
A 1 2041 MET 2041 2041 2041 MET MET A . n 
A 1 2042 THR 2042 2042 2042 THR THR A . n 
A 1 2043 LYS 2043 2043 2043 LYS LYS A . n 
A 1 2044 PRO 2044 2044 2044 PRO PRO A . n 
A 1 2045 ASP 2045 2045 2045 ASP ASP A . n 
A 1 2046 ARG 2046 2046 2046 ARG ARG A . n 
A 1 2047 GLN 2047 2047 2047 GLN GLN A . n 
A 1 2048 LEU 2048 2048 2048 LEU LEU A . n 
A 1 2049 ILE 2049 2049 2049 ILE ILE A . n 
A 1 2050 ALA 2050 2050 2050 ALA ALA A . n 
A 1 2051 GLN 2051 2051 2051 GLN GLN A . n 
A 1 2052 VAL 2052 2052 2052 VAL VAL A . n 
A 1 2053 MET 2053 2053 2053 MET MET A . n 
A 1 2054 LEU 2054 2054 2054 LEU LEU A . n 
A 1 2055 TYR 2055 2055 2055 TYR TYR A . n 
A 1 2056 SER 2056 2056 2056 SER SER A . n 
A 1 2057 GLN 2057 2057 2057 GLN GLN A . n 
A 1 2058 GLY 2058 2058 2058 GLY GLY A . n 
A 1 2059 PHE 2059 2059 2059 PHE PHE A . n 
A 1 2060 ARG 2060 2060 2060 ARG ARG A . n 
A 1 2061 THR 2061 2061 2061 THR THR A . n 
A 1 2062 ALA 2062 2062 2062 ALA ALA A . n 
A 1 2063 GLU 2063 2063 2063 GLU GLU A . n 
A 1 2064 VAL 2064 2064 2064 VAL VAL A . n 
A 1 2065 LEU 2065 2065 2065 LEU LEU A . n 
A 1 2066 ALA 2066 2066 2066 ALA ALA A . n 
A 1 2067 ASN 2067 2067 2067 ASN ASN A . n 
A 1 2068 LYS 2068 2068 2068 LYS LYS A . n 
A 1 2069 ILE 2069 2069 2069 ILE ILE A . n 
A 1 2070 VAL 2070 2070 2070 VAL VAL A . n 
A 1 2071 PRO 2071 2071 2071 PRO PRO A . n 
A 1 2072 PHE 2072 2072 2072 PHE PHE A . n 
A 1 2073 PHE 2073 2073 2073 PHE PHE A . n 
A 1 2074 LYS 2074 2074 2074 LYS LYS A . n 
A 1 2075 LEU 2075 2075 2075 LEU LEU A . n 
A 1 2076 CYS 2076 2076 2076 CYS CYS A . n 
A 1 2077 ASP 2077 2077 2077 ASP ASP A . n 
A 1 2078 GLU 2078 2078 2078 GLU GLU A . n 
A 1 2079 GLN 2079 2079 2079 GLN GLN A . n 
A 1 2080 LEU 2080 2080 2080 LEU LEU A . n 
A 1 2081 SER 2081 2081 2081 SER SER A . n 
A 1 2082 SER 2082 2082 2082 SER SER A . n 
A 1 2083 GLN 2083 2083 2083 GLN GLN A . n 
A 1 2084 SER 2084 2084 2084 SER SER A . n 
A 1 2085 HIS 2085 2085 2085 HIS HIS A . n 
A 1 2086 TYR 2086 2086 2086 TYR TYR A . n 
A 1 2087 ASP 2087 2087 2087 ASP ASP A . n 
A 1 2088 PHE 2088 2088 2088 PHE PHE A . n 
A 1 2089 GLY 2089 2089 2089 GLY GLY A . n 
A 1 2090 LEU 2090 2090 2090 LEU LEU A . n 
A 1 2091 ARG 2091 2091 2091 ARG ARG A . n 
A 1 2092 ALA 2092 2092 2092 ALA ALA A . n 
A 1 2093 LEU 2093 2093 2093 LEU LEU A . n 
A 1 2094 LYS 2094 2094 2094 LYS LYS A . n 
A 1 2095 SER 2095 2095 2095 SER SER A . n 
A 1 2096 VAL 2096 2096 2096 VAL VAL A . n 
A 1 2097 LEU 2097 2097 2097 LEU LEU A . n 
A 1 2098 VAL 2098 2098 2098 VAL VAL A . n 
A 1 2099 SER 2099 2099 2099 SER SER A . n 
A 1 2100 ALA 2100 2100 2100 ALA ALA A . n 
A 1 2101 GLY 2101 2101 2101 GLY GLY A . n 
A 1 2102 ASN 2102 2102 2102 ASN ASN A . n 
A 1 2103 VAL 2103 2103 2103 VAL VAL A . n 
A 1 2104 LYS 2104 2104 2104 LYS LYS A . n 
A 1 2105 ARG 2105 2105 2105 ARG ARG A . n 
A 1 2106 GLU 2106 2106 2106 GLU GLU A . n 
A 1 2107 ARG 2107 2107 2107 ARG ARG A . n 
A 1 2108 ILE 2108 2108 2108 ILE ILE A . n 
A 1 2109 GLN 2109 2109 2109 GLN GLN A . n 
A 1 2110 LYS 2110 2110 2110 LYS LYS A . n 
A 1 2111 ILE 2111 2111 2111 ILE ILE A . n 
A 1 2112 LYS 2112 2112 2112 LYS LYS A . n 
A 1 2113 ARG 2113 2113 2113 ARG ARG A . n 
A 1 2114 GLU 2114 2114 2114 GLU GLU A . n 
A 1 2115 LYS 2115 2115 2115 LYS LYS A . n 
A 1 2116 GLU 2116 2116 2116 GLU GLU A . n 
A 1 2117 GLU 2117 2117 2117 GLU GLU A . n 
A 1 2118 ARG 2118 2118 2118 ARG ARG A . n 
A 1 2119 GLY 2119 2119 2119 GLY GLY A . n 
A 1 2120 GLU 2120 2120 2120 GLU GLU A . n 
A 1 2121 ALA 2121 2121 2121 ALA ALA A . n 
A 1 2122 VAL 2122 2122 2122 VAL VAL A . n 
A 1 2123 ASP 2123 2123 2123 ASP ASP A . n 
A 1 2124 GLU 2124 2124 2124 GLU GLU A . n 
A 1 2125 GLY 2125 2125 2125 GLY GLY A . n 
A 1 2126 GLU 2126 2126 2126 GLU GLU A . n 
A 1 2127 ILE 2127 2127 2127 ILE ILE A . n 
A 1 2128 ALA 2128 2128 2128 ALA ALA A . n 
A 1 2129 GLU 2129 2129 2129 GLU GLU A . n 
A 1 2130 ASN 2130 2130 2130 ASN ASN A . n 
A 1 2131 LEU 2131 2131 2131 LEU LEU A . n 
A 1 2132 PRO 2132 2132 2132 PRO PRO A . n 
A 1 2133 GLU 2133 2133 2133 GLU GLU A . n 
A 1 2134 GLN 2134 2134 2134 GLN GLN A . n 
A 1 2135 GLU 2135 2135 2135 GLU GLU A . n 
A 1 2136 ILE 2136 2136 2136 ILE ILE A . n 
A 1 2137 LEU 2137 2137 2137 LEU LEU A . n 
A 1 2138 ILE 2138 2138 2138 ILE ILE A . n 
A 1 2139 GLN 2139 2139 2139 GLN GLN A . n 
A 1 2140 SER 2140 2140 2140 SER SER A . n 
A 1 2141 VAL 2141 2141 2141 VAL VAL A . n 
A 1 2142 CYS 2142 2142 2142 CYS CYS A . n 
A 1 2143 GLU 2143 2143 2143 GLU GLU A . n 
A 1 2144 THR 2144 2144 2144 THR THR A . n 
A 1 2145 MET 2145 2145 2145 MET MET A . n 
A 1 2146 VAL 2146 2146 2146 VAL VAL A . n 
A 1 2147 PRO 2147 2147 2147 PRO PRO A . n 
A 1 2148 LYS 2148 2148 2148 LYS LYS A . n 
A 1 2149 LEU 2149 2149 2149 LEU LEU A . n 
A 1 2150 VAL 2150 2150 2150 VAL VAL A . n 
A 1 2151 ALA 2151 2151 2151 ALA ALA A . n 
A 1 2152 GLU 2152 2152 2152 GLU GLU A . n 
A 1 2153 ASP 2153 2153 2153 ASP ASP A . n 
A 1 2154 ILE 2154 2154 2154 ILE ILE A . n 
A 1 2155 PRO 2155 2155 2155 PRO PRO A . n 
A 1 2156 LEU 2156 2156 2156 LEU LEU A . n 
A 1 2157 LEU 2157 2157 2157 LEU LEU A . n 
A 1 2158 PHE 2158 2158 2158 PHE PHE A . n 
A 1 2159 SER 2159 2159 2159 SER SER A . n 
A 1 2160 LEU 2160 2160 2160 LEU LEU A . n 
A 1 2161 LEU 2161 2161 2161 LEU LEU A . n 
A 1 2162 SER 2162 2162 2162 SER SER A . n 
A 1 2163 ASP 2163 2163 2163 ASP ASP A . n 
A 1 2164 VAL 2164 2164 2164 VAL VAL A . n 
A 1 2165 PHE 2165 2165 2165 PHE PHE A . n 
A 1 2166 PRO 2166 2166 2166 PRO PRO A . n 
A 1 2167 GLY 2167 2167 2167 GLY GLY A . n 
A 1 2168 VAL 2168 2168 2168 VAL VAL A . n 
A 1 2169 GLN 2169 2169 2169 GLN GLN A . n 
A 1 2170 TYR 2170 2170 2170 TYR TYR A . n 
A 1 2171 HIS 2171 2171 2171 HIS HIS A . n 
A 1 2172 ARG 2172 2172 2172 ARG ARG A . n 
A 1 2173 GLY 2173 2173 2173 GLY GLY A . n 
A 1 2174 GLU 2174 2174 2174 GLU GLU A . n 
A 1 2175 MET 2175 2175 2175 MET MET A . n 
A 1 2176 THR 2176 2176 2176 THR THR A . n 
A 1 2177 ALA 2177 2177 2177 ALA ALA A . n 
A 1 2178 LEU 2178 2178 2178 LEU LEU A . n 
A 1 2179 ARG 2179 2179 2179 ARG ARG A . n 
A 1 2180 GLU 2180 2180 2180 GLU GLU A . n 
A 1 2181 GLU 2181 2181 2181 GLU GLU A . n 
A 1 2182 LEU 2182 2182 2182 LEU LEU A . n 
A 1 2183 LYS 2183 2183 2183 LYS LYS A . n 
A 1 2184 LYS 2184 2184 2184 LYS LYS A . n 
A 1 2185 VAL 2185 2185 2185 VAL VAL A . n 
A 1 2186 CYS 2186 2186 2186 CYS CYS A . n 
A 1 2187 GLN 2187 2187 2187 GLN GLN A . n 
A 1 2188 GLU 2188 2188 2188 GLU GLU A . n 
A 1 2189 MET 2189 2189 2189 MET MET A . n 
A 1 2190 TYR 2190 2190 2190 TYR TYR A . n 
A 1 2191 LEU 2191 2191 2191 LEU LEU A . n 
A 1 2192 THR 2192 2192 2192 THR THR A . n 
A 1 2193 TYR 2193 2193 2193 TYR TYR A . n 
A 1 2194 GLY 2194 2194 2194 GLY GLY A . n 
A 1 2195 ASP 2195 2195 2195 ASP ASP A . n 
A 1 2196 GLY 2196 2196 2196 GLY GLY A . n 
A 1 2197 GLU 2197 2197 2197 GLU GLU A . n 
A 1 2198 GLU 2198 2198 2198 GLU GLU A . n 
A 1 2199 VAL 2199 2199 2199 VAL VAL A . n 
A 1 2200 GLY 2200 2200 2200 GLY GLY A . n 
A 1 2201 GLY 2201 2201 2201 GLY GLY A . n 
A 1 2202 MET 2202 2202 2202 MET MET A . n 
A 1 2203 TRP 2203 2203 2203 TRP TRP A . n 
A 1 2204 VAL 2204 2204 2204 VAL VAL A . n 
A 1 2205 GLU 2205 2205 2205 GLU GLU A . n 
A 1 2206 LYS 2206 2206 2206 LYS LYS A . n 
A 1 2207 VAL 2207 2207 2207 VAL VAL A . n 
A 1 2208 LEU 2208 2208 2208 LEU LEU A . n 
A 1 2209 GLN 2209 2209 2209 GLN GLN A . n 
A 1 2210 LEU 2210 2210 2210 LEU LEU A . n 
A 1 2211 TYR 2211 2211 2211 TYR TYR A . n 
A 1 2212 GLN 2212 2212 2212 GLN GLN A . n 
A 1 2213 ILE 2213 2213 2213 ILE ILE A . n 
A 1 2214 THR 2214 2214 2214 THR THR A . n 
A 1 2215 GLN 2215 2215 2215 GLN GLN A . n 
A 1 2216 ILE 2216 2216 2216 ILE ILE A . n 
A 1 2217 ASN 2217 2217 2217 ASN ASN A . n 
A 1 2218 HIS 2218 2218 2218 HIS HIS A . n 
A 1 2219 GLY 2219 2219 2219 GLY GLY A . n 
A 1 2220 LEU 2220 2220 2220 LEU LEU A . n 
A 1 2221 MET 2221 2221 2221 MET MET A . n 
A 1 2222 MET 2222 2222 2222 MET MET A . n 
A 1 2223 VAL 2223 2223 2223 VAL VAL A . n 
A 1 2224 GLY 2224 2224 2224 GLY GLY A . n 
A 1 2225 PRO 2225 2225 2225 PRO PRO A . n 
A 1 2226 SER 2226 2226 2226 SER SER A . n 
A 1 2227 GLY 2227 2227 2227 GLY GLY A . n 
A 1 2228 SER 2228 2228 2228 SER SER A . n 
A 1 2229 GLY 2229 2229 2229 GLY GLY A . n 
A 1 2230 LYS 2230 2230 2230 LYS LYS A . n 
A 1 2231 SER 2231 2231 2231 SER SER A . n 
A 1 2232 MET 2232 2232 2232 MET MET A . n 
A 1 2233 ALA 2233 2233 2233 ALA ALA A . n 
A 1 2234 TRP 2234 2234 2234 TRP TRP A . n 
A 1 2235 ARG 2235 2235 2235 ARG ARG A . n 
A 1 2236 VAL 2236 2236 2236 VAL VAL A . n 
A 1 2237 LEU 2237 2237 2237 LEU LEU A . n 
A 1 2238 LEU 2238 2238 2238 LEU LEU A . n 
A 1 2239 LYS 2239 2239 2239 LYS LYS A . n 
A 1 2240 ALA 2240 2240 2240 ALA ALA A . n 
A 1 2241 LEU 2241 2241 2241 LEU LEU A . n 
A 1 2242 GLU 2242 2242 2242 GLU GLU A . n 
A 1 2243 ARG 2243 2243 2243 ARG ARG A . n 
A 1 2244 LEU 2244 2244 2244 LEU LEU A . n 
A 1 2245 GLU 2245 2245 2245 GLU GLU A . n 
A 1 2246 GLY 2246 2246 2246 GLY GLY A . n 
A 1 2247 VAL 2247 2247 2247 VAL VAL A . n 
A 1 2248 GLU 2248 2248 2248 GLU GLU A . n 
A 1 2249 GLY 2249 2249 2249 GLY GLY A . n 
A 1 2250 VAL 2250 2250 2250 VAL VAL A . n 
A 1 2251 ALA 2251 2251 2251 ALA ALA A . n 
A 1 2252 HIS 2252 2252 2252 HIS HIS A . n 
A 1 2253 ILE 2253 2253 2253 ILE ILE A . n 
A 1 2254 ILE 2254 2254 2254 ILE ILE A . n 
A 1 2255 ASP 2255 2255 2255 ASP ASP A . n 
A 1 2256 PRO 2256 2256 2256 PRO PRO A . n 
A 1 2257 LYS 2257 2257 2257 LYS LYS A . n 
A 1 2258 ALA 2258 2258 2258 ALA ALA A . n 
A 1 2259 ILE 2259 2259 2259 ILE ILE A . n 
A 1 2260 SER 2260 2260 2260 SER SER A . n 
A 1 2261 LYS 2261 2261 2261 LYS LYS A . n 
A 1 2262 ASP 2262 2262 2262 ASP ASP A . n 
A 1 2263 HIS 2263 2263 2263 HIS HIS A . n 
A 1 2264 LEU 2264 2264 2264 LEU LEU A . n 
A 1 2265 TYR 2265 2265 2265 TYR TYR A . n 
A 1 2266 GLY 2266 2266 2266 GLY GLY A . n 
A 1 2267 THR 2267 2267 2267 THR THR A . n 
A 1 2268 LEU 2268 2268 2268 LEU LEU A . n 
A 1 2269 ASP 2269 2269 2269 ASP ASP A . n 
A 1 2270 PRO 2270 2270 2270 PRO PRO A . n 
A 1 2271 ASN 2271 2271 2271 ASN ASN A . n 
A 1 2272 THR 2272 2272 2272 THR THR A . n 
A 1 2273 ARG 2273 2273 2273 ARG ARG A . n 
A 1 2274 GLU 2274 2274 2274 GLU GLU A . n 
A 1 2275 TRP 2275 2275 2275 TRP TRP A . n 
A 1 2276 THR 2276 2276 2276 THR THR A . n 
A 1 2277 ASP 2277 2277 2277 ASP ASP A . n 
A 1 2278 GLY 2278 2278 2278 GLY GLY A . n 
A 1 2279 LEU 2279 2279 2279 LEU LEU A . n 
A 1 2280 PHE 2280 2280 2280 PHE PHE A . n 
A 1 2281 THR 2281 2281 2281 THR THR A . n 
A 1 2282 HIS 2282 2282 2282 HIS HIS A . n 
A 1 2283 VAL 2283 2283 2283 VAL VAL A . n 
A 1 2284 LEU 2284 2284 2284 LEU LEU A . n 
A 1 2285 ARG 2285 2285 2285 ARG ARG A . n 
A 1 2286 LYS 2286 2286 2286 LYS LYS A . n 
A 1 2287 ILE 2287 2287 2287 ILE ILE A . n 
A 1 2288 ILE 2288 2288 2288 ILE ILE A . n 
A 1 2289 ASP 2289 2289 2289 ASP ASP A . n 
A 1 2290 SER 2290 2290 2290 SER SER A . n 
A 1 2291 VAL 2291 2291 2291 VAL VAL A . n 
A 1 2292 ARG 2292 2292 2292 ARG ARG A . n 
A 1 2293 GLY 2293 2293 2293 GLY GLY A . n 
A 1 2294 GLU 2294 2294 2294 GLU GLU A . n 
A 1 2295 LEU 2295 2295 2295 LEU LEU A . n 
A 1 2296 GLN 2296 2296 2296 GLN GLN A . n 
A 1 2297 LYS 2297 2297 2297 LYS LYS A . n 
A 1 2298 ARG 2298 2298 2298 ARG ARG A . n 
A 1 2299 GLN 2299 2299 2299 GLN GLN A . n 
A 1 2300 TRP 2300 2300 2300 TRP TRP A . n 
A 1 2301 ILE 2301 2301 2301 ILE ILE A . n 
A 1 2302 VAL 2302 2302 2302 VAL VAL A . n 
A 1 2303 PHE 2303 2303 2303 PHE PHE A . n 
A 1 2304 ASP 2304 2304 2304 ASP ASP A . n 
A 1 2305 GLY 2305 2305 2305 GLY GLY A . n 
A 1 2306 ASP 2306 2306 2306 ASP ASP A . n 
A 1 2307 VAL 2307 2307 2307 VAL VAL A . n 
A 1 2308 ASP 2308 2308 2308 ASP ASP A . n 
A 1 2309 PRO 2309 2309 2309 PRO PRO A . n 
A 1 2310 GLU 2310 2310 2310 GLU GLU A . n 
A 1 2311 TRP 2311 2311 2311 TRP TRP A . n 
A 1 2312 VAL 2312 2312 2312 VAL VAL A . n 
A 1 2313 GLU 2313 2313 2313 GLU GLU A . n 
A 1 2314 ASN 2314 2314 2314 ASN ASN A . n 
A 1 2315 LEU 2315 2315 2315 LEU LEU A . n 
A 1 2316 ASN 2316 2316 2316 ASN ASN A . n 
A 1 2317 SER 2317 2317 2317 SER SER A . n 
A 1 2318 VAL 2318 2318 2318 VAL VAL A . n 
A 1 2319 LEU 2319 2319 2319 LEU LEU A . n 
A 1 2320 ASP 2320 2320 2320 ASP ASP A . n 
A 1 2321 ASP 2321 2321 2321 ASP ASP A . n 
A 1 2322 ASN 2322 2322 2322 ASN ASN A . n 
A 1 2323 LYS 2323 2323 2323 LYS LYS A . n 
A 1 2324 LEU 2324 2324 2324 LEU LEU A . n 
A 1 2325 LEU 2325 2325 2325 LEU LEU A . n 
A 1 2326 THR 2326 2326 2326 THR THR A . n 
A 1 2327 LEU 2327 2327 2327 LEU LEU A . n 
A 1 2328 PRO 2328 2328 2328 PRO PRO A . n 
A 1 2329 ASN 2329 2329 2329 ASN ASN A . n 
A 1 2330 GLY 2330 2330 2330 GLY GLY A . n 
A 1 2331 GLU 2331 2331 2331 GLU GLU A . n 
A 1 2332 ARG 2332 2332 2332 ARG ARG A . n 
A 1 2333 LEU 2333 2333 2333 LEU LEU A . n 
A 1 2334 SER 2334 2334 2334 SER SER A . n 
A 1 2335 LEU 2335 2335 2335 LEU LEU A . n 
A 1 2336 PRO 2336 2336 2336 PRO PRO A . n 
A 1 2337 PRO 2337 2337 2337 PRO PRO A . n 
A 1 2338 ASN 2338 2338 2338 ASN ASN A . n 
A 1 2339 VAL 2339 2339 2339 VAL VAL A . n 
A 1 2340 ARG 2340 2340 2340 ARG ARG A . n 
A 1 2341 ILE 2341 2341 2341 ILE ILE A . n 
A 1 2342 MET 2342 2342 2342 MET MET A . n 
A 1 2343 PHE 2343 2343 2343 PHE PHE A . n 
A 1 2344 GLU 2344 2344 2344 GLU GLU A . n 
A 1 2345 VAL 2345 2345 2345 VAL VAL A . n 
A 1 2346 GLN 2346 2346 2346 GLN GLN A . n 
A 1 2347 ASP 2347 2347 2347 ASP ASP A . n 
A 1 2348 LEU 2348 2348 2348 LEU LEU A . n 
A 1 2349 LYS 2349 2349 2349 LYS LYS A . n 
A 1 2350 TYR 2350 2350 2350 TYR TYR A . n 
A 1 2351 ALA 2351 2351 2351 ALA ALA A . n 
A 1 2352 THR 2352 2352 2352 THR THR A . n 
A 1 2353 LEU 2353 2353 2353 LEU LEU A . n 
A 1 2354 ALA 2354 2354 2354 ALA ALA A . n 
A 1 2355 THR 2355 2355 2355 THR THR A . n 
A 1 2356 VAL 2356 2356 2356 VAL VAL A . n 
A 1 2357 SER 2357 2357 2357 SER SER A . n 
A 1 2358 ARG 2358 2358 2358 ARG ARG A . n 
A 1 2359 CYS 2359 2359 2359 CYS CYS A . n 
A 1 2360 GLY 2360 2360 2360 GLY GLY A . n 
A 1 2361 MET 2361 2361 2361 MET MET A . n 
A 1 2362 VAL 2362 2362 2362 VAL VAL A . n 
A 1 2363 TRP 2363 2363 2363 TRP TRP A . n 
A 1 2364 PHE 2364 2364 2364 PHE PHE A . n 
A 1 2365 SER 2365 2365 2365 SER SER A . n 
A 1 2366 GLU 2366 2366 2366 GLU GLU A . n 
A 1 2367 ASP 2367 2367 2367 ASP ASP A . n 
A 1 2368 VAL 2368 2368 2368 VAL VAL A . n 
A 1 2369 LEU 2369 2369 2369 LEU LEU A . n 
A 1 2370 SER 2370 2370 2370 SER SER A . n 
A 1 2371 THR 2371 2371 2371 THR THR A . n 
A 1 2372 ASP 2372 2372 2372 ASP ASP A . n 
A 1 2373 MET 2373 2373 2373 MET MET A . n 
A 1 2374 ILE 2374 2374 2374 ILE ILE A . n 
A 1 2375 PHE 2375 2375 2375 PHE PHE A . n 
A 1 2376 ASN 2376 2376 2376 ASN ASN A . n 
A 1 2377 ASN 2377 2377 2377 ASN ASN A . n 
A 1 2378 PHE 2378 2378 2378 PHE PHE A . n 
A 1 2379 LEU 2379 2379 2379 LEU LEU A . n 
A 1 2380 ALA 2380 2380 2380 ALA ALA A . n 
A 1 2381 ARG 2381 2381 2381 ARG ARG A . n 
A 1 2382 LEU 2382 2382 2382 LEU LEU A . n 
A 1 2383 ARG 2383 2383 2383 ARG ARG A . n 
A 1 2384 SER 2384 2384 2384 SER SER A . n 
A 1 2385 ILE 2385 2385 2385 ILE ILE A . n 
A 1 2386 PRO 2386 2386 2386 PRO PRO A . n 
A 1 2387 LEU 2387 2387 2387 LEU LEU A . n 
A 1 2388 ASP 2388 2388 2388 ASP ASP A . n 
A 1 2389 GLU 2389 2389 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 . 
H 5 HOH 1 4801 2    HOH HOH A . 
H 5 HOH 2 4802 3    HOH HOH A . 
H 5 HOH 3 4803 1    HOH HOH 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                   9BM0 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BM0 
_struct.title                        'State-2 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        9BM0 
_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 ? 
H N N 5 ? 
# 
_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              9BM0 
_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,H 
# 
_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 MET A 1457 ? TYR A 1473 ? MET A 1457 TYR A 1473 1 ? 17 
HELX_P HELX_P2   AA2 GLY A 1489 ? SER A 1510 ? GLY A 1489 SER A 1510 1 ? 22 
HELX_P HELX_P3   AA3 PRO A 1511 ? VAL A 1515 ? PRO A 1511 VAL A 1515 5 ? 5  
HELX_P HELX_P4   AA4 PHE A 1516 ? SER A 1554 ? PHE A 1516 SER A 1554 1 ? 39 
HELX_P HELX_P5   AA5 ALA A 1555 ? LEU A 1561 ? ALA A 1555 LEU A 1561 1 ? 7  
HELX_P HELX_P6   AA6 LEU A 1561 ? SER A 1585 ? LEU A 1561 SER A 1585 1 ? 25 
HELX_P HELX_P7   AA7 LEU A 1587 ? ASN A 1593 ? LEU A 1587 ASN A 1593 1 ? 7  
HELX_P HELX_P8   AA8 GLY A 1596 ? ALA A 1614 ? GLY A 1596 ALA A 1614 1 ? 19 
HELX_P HELX_P9   AA9 LEU A 1615 ? PHE A 1626 ? LEU A 1615 PHE A 1626 1 ? 12 
HELX_P HELX_P10  AB1 PRO A 1627 ? VAL A 1632 ? PRO A 1627 VAL A 1632 5 ? 6  
HELX_P HELX_P11  AB2 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P12  AB3 SER A 1644 ? LYS A 1645 ? SER A 1644 LYS A 1645 5 ? 2  
HELX_P HELX_P13  AB4 ASN A 1646 ? GLN A 1651 ? ASN A 1646 GLN A 1651 5 ? 6  
HELX_P HELX_P14  AB5 HIS A 1653 ? PHE A 1658 ? HIS A 1653 PHE A 1658 1 ? 6  
HELX_P HELX_P15  AB6 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P16  AB7 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P17  AB8 GLN A 1746 ? MET A 1769 ? GLN A 1746 MET A 1769 1 ? 24 
HELX_P HELX_P18  AB9 GLY A 1770 ? GLY A 1772 ? GLY A 1770 GLY A 1772 5 ? 3  
HELX_P HELX_P19  AC1 PRO A 1777 ? MET A 1798 ? PRO A 1777 MET A 1798 1 ? 22 
HELX_P HELX_P20  AC2 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P21  AC3 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P22  AC4 ASP A 1852 ? GLN A 1855 ? ASP A 1852 GLN A 1855 5 ? 4  
HELX_P HELX_P23  AC5 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P24  AC6 GLY A 1911 ? LEU A 1923 ? GLY A 1911 LEU A 1923 1 ? 13 
HELX_P HELX_P25  AC7 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P26  AC8 PHE A 1960 ? LEU A 1963 ? PHE A 1960 LEU A 1963 5 ? 4  
HELX_P HELX_P27  AC9 GLU A 1964 ? ASN A 1987 ? GLU A 1964 ASN A 1987 1 ? 24 
HELX_P HELX_P28  AD1 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P29  AD2 ASP A 2045 ? GLY A 2058 ? ASP A 2045 GLY A 2058 1 ? 14 
HELX_P HELX_P30  AD3 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P31  AD4 GLY A 2089 ? ARG A 2118 ? GLY A 2089 ARG A 2118 1 ? 30 
HELX_P HELX_P32  AD5 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P33  AD6 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P34  AD7 GLU A 2152 ? PHE A 2165 ? GLU A 2152 PHE A 2165 1 ? 14 
HELX_P HELX_P35  AD8 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P36  AD9 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P37  AE1 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P38  AE2 ASP A 2255 ? ILE A 2259 ? ASP A 2255 ILE A 2259 5 ? 5  
HELX_P HELX_P39  AE3 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P40  AE4 GLY A 2278 ? SER A 2290 ? GLY A 2278 SER A 2290 1 ? 13 
HELX_P HELX_P41  AE5 ASP A 2308 ? GLU A 2313 ? ASP A 2308 GLU A 2313 1 ? 6  
HELX_P HELX_P42  AE6 LEU A 2315 ? ASP A 2320 ? LEU A 2315 ASP A 2320 1 ? 6  
HELX_P HELX_P43  AE7 THR A 2352 ? ARG A 2358 ? THR A 2352 ARG A 2358 1 ? 7  
HELX_P HELX_P44  AE8 SER A 2370 ? ILE A 2385 ? SER A 2370 ILE A 2385 1 ? 16 
HELX_P HELX_P45  AE9 PRO A 2411 ? GLN A 2424 ? PRO A 2411 GLN A 2424 1 ? 14 
HELX_P HELX_P46  AF1 GLY A 2431 ? PHE A 2441 ? GLY A 2431 PHE A 2441 1 ? 11 
HELX_P HELX_P47  AF2 THR A 2450 ? HIS A 2476 ? THR A 2450 HIS A 2476 1 ? 27 
HELX_P HELX_P48  AF3 GLN A 2482 ? GLY A 2504 ? GLN A 2482 GLY A 2504 1 ? 23 
HELX_P HELX_P49  AF4 ARG A 2507 ? THR A 2522 ? ARG A 2507 THR A 2522 1 ? 16 
HELX_P HELX_P50  AF5 PRO A 2533 ? ILE A 2535 ? PRO A 2533 ILE A 2535 5 ? 3  
HELX_P HELX_P51  AF6 GLN A 2549 ? VAL A 2552 ? GLN A 2549 VAL A 2552 5 ? 4  
HELX_P HELX_P52  AF7 GLU A 2558 ? VAL A 2562 ? GLU A 2558 VAL A 2562 5 ? 5  
HELX_P HELX_P53  AF8 THR A 2571 ? GLU A 2587 ? THR A 2571 GLU A 2587 1 ? 17 
HELX_P HELX_P54  AF9 GLY A 2600 ? ARG A 2610 ? GLY A 2600 ARG A 2610 1 ? 11 
HELX_P HELX_P55  AG1 THR A 2627 ? TYR A 2638 ? THR A 2627 TYR A 2638 1 ? 12 
HELX_P HELX_P56  AG2 GLN A 2677 ? HIS A 2689 ? GLN A 2677 HIS A 2689 1 ? 13 
HELX_P HELX_P57  AG3 SER A 2724 ? ARG A 2729 ? SER A 2724 ARG A 2729 1 ? 6  
HELX_P HELX_P58  AG4 GLY A 2740 ? LEU A 2756 ? GLY A 2740 LEU A 2756 1 ? 17 
HELX_P HELX_P59  AG5 ARG A 2757 ? LEU A 2758 ? ARG A 2757 LEU A 2758 5 ? 2  
HELX_P HELX_P60  AG6 ILE A 2759 ? THR A 2764 ? ILE A 2759 THR A 2764 5 ? 6  
HELX_P HELX_P61  AG7 TYR A 2765 ? PHE A 2784 ? TYR A 2765 PHE A 2784 1 ? 20 
HELX_P HELX_P62  AG8 SER A 2795 ? ARG A 2811 ? SER A 2795 ARG A 2811 1 ? 17 
HELX_P HELX_P63  AG9 PRO A 2817 ? GLN A 2834 ? PRO A 2817 GLN A 2834 1 ? 18 
HELX_P HELX_P64  AH1 GLU A 2839 ? PHE A 2858 ? GLU A 2839 PHE A 2858 1 ? 20 
HELX_P HELX_P65  AH2 ASP A 2862 ? MET A 2867 ? ASP A 2862 MET A 2867 1 ? 6  
HELX_P HELX_P66  AH3 ASP A 2885 ? GLU A 2904 ? ASP A 2885 GLU A 2904 1 ? 20 
HELX_P HELX_P67  AH4 PHE A 2912 ? ARG A 2927 ? PHE A 2912 ARG A 2927 1 ? 16 
HELX_P HELX_P68  AH5 GLY A 2942 ? ASN A 2954 ? GLY A 2942 ASN A 2954 1 ? 13 
HELX_P HELX_P69  AH6 THR A 2968 ? CYS A 2985 ? THR A 2968 CYS A 2985 1 ? 18 
HELX_P HELX_P70  AH7 SER A 2997 ? VAL A 2999 ? SER A 2997 VAL A 2999 5 ? 3  
HELX_P HELX_P71  AH8 ASP A 3001 ? GLY A 3015 ? ASP A 3001 GLY A 3015 1 ? 15 
HELX_P HELX_P72  AH9 GLY A 3023 ? GLY A 3041 ? GLY A 3023 GLY A 3041 1 ? 19 
HELX_P HELX_P73  AI1 SER A 3046 ? ASN A 3061 ? SER A 3046 ASN A 3061 1 ? 16 
HELX_P HELX_P74  AI2 SER A 3071 ? SER A 3082 ? SER A 3071 SER A 3082 1 ? 12 
HELX_P HELX_P75  AI3 PRO A 3083 ? PHE A 3086 ? PRO A 3083 PHE A 3086 5 ? 4  
HELX_P HELX_P76  AI4 SER A 3098 ? THR A 3110 ? SER A 3098 THR A 3110 1 ? 13 
HELX_P HELX_P77  AI5 SER A 3138 ? ARG A 3164 ? SER A 3138 ARG A 3164 1 ? 27 
HELX_P HELX_P78  AI6 THR A 3172 ? LYS A 3241 ? THR A 3172 LYS A 3241 1 ? 70 
HELX_P HELX_P79  AI7 GLU A 3450 ? ALA A 3517 ? GLU A 3450 ALA A 3517 1 ? 68 
HELX_P HELX_P80  AI8 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P81  AI9 ALA A 3548 ? LEU A 3553 ? ALA A 3548 LEU A 3553 1 ? 6  
HELX_P HELX_P82  AJ1 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P83  AJ2 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P84  AJ3 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P85  AJ4 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P86  AJ5 ASP A 3637 ? TYR A 3641 ? ASP A 3637 TYR A 3641 5 ? 5  
HELX_P HELX_P87  AJ6 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P88  AJ7 LEU A 3645 ? ARG A 3651 ? LEU A 3645 ARG A 3651 1 ? 7  
HELX_P HELX_P89  AJ8 PRO A 3689 ? VAL A 3696 ? PRO A 3689 VAL A 3696 1 ? 8  
HELX_P HELX_P90  AJ9 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P91  AK1 ARG A 3721 ? VAL A 3756 ? ARG A 3721 VAL A 3756 1 ? 36 
HELX_P HELX_P92  AK2 ASP A 3763 ? LEU A 3818 ? ASP A 3763 LEU A 3818 1 ? 56 
HELX_P HELX_P93  AK3 LYS A 3819 ? ILE A 3821 ? LYS A 3819 ILE A 3821 5 ? 3  
HELX_P HELX_P94  AK4 SER A 3828 ? GLU A 3842 ? SER A 3828 GLU A 3842 1 ? 15 
HELX_P HELX_P95  AK5 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P96  AK6 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P97  AK7 GLY A 3874 ? MET A 3875 ? GLY A 3874 MET A 3875 5 ? 2  
HELX_P HELX_P98  AK8 LEU A 3876 ? GLN A 3878 ? LEU A 3876 GLN A 3878 5 ? 3  
HELX_P HELX_P99  AK9 ASP A 3879 ? GLY A 3894 ? ASP A 3879 GLY A 3894 1 ? 16 
HELX_P HELX_P100 AL1 TYR A 3901 ? GLY A 3911 ? TYR A 3901 GLY A 3911 1 ? 11 
HELX_P HELX_P101 AL2 ASN A 3912 ? ILE A 3914 ? ASN A 3912 ILE A 3914 5 ? 3  
HELX_P HELX_P102 AL3 SER A 3917 ? THR A 3921 ? SER A 3917 THR A 3921 5 ? 5  
HELX_P HELX_P103 AL4 THR A 3928 ? SER A 3939 ? THR A 3928 SER A 3939 1 ? 12 
HELX_P HELX_P104 AL5 CYS A 3940 ? LYS A 3945 ? CYS A 3940 LYS A 3945 5 ? 6  
HELX_P HELX_P105 AL6 ASP A 3946 ? ALA A 3953 ? ASP A 3946 ALA A 3953 1 ? 8  
HELX_P HELX_P106 AL7 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P107 AL8 SER A 3965 ? VAL A 3970 ? SER A 3965 VAL A 3970 5 ? 6  
HELX_P HELX_P108 AL9 THR A 3981 ? ARG A 3997 ? THR A 3981 ARG A 3997 1 ? 17 
HELX_P HELX_P109 AM1 ARG A 4000 ? LEU A 4013 ? ARG A 4000 LEU A 4013 1 ? 14 
HELX_P HELX_P110 AM2 MET A 4018 ? GLN A 4023 ? MET A 4018 GLN A 4023 5 ? 6  
HELX_P HELX_P111 AM3 ASP A 4026 ? GLU A 4034 ? ASP A 4026 GLU A 4034 1 ? 9  
HELX_P HELX_P112 AM4 ALA A 4051 ? GLN A 4062 ? ALA A 4051 GLN A 4062 1 ? 12 
HELX_P HELX_P113 AM5 SER A 4073 ? GLY A 4091 ? SER A 4073 GLY A 4091 1 ? 19 
HELX_P HELX_P114 AM6 ASN A 4098 ? LEU A 4101 ? ASN A 4098 LEU A 4101 5 ? 4  
HELX_P HELX_P115 AM7 ALA A 4102 ? SER A 4115 ? ALA A 4102 SER A 4115 1 ? 14 
HELX_P HELX_P116 AM8 PRO A 4135 ? GLY A 4142 ? PRO A 4135 GLY A 4142 1 ? 8  
HELX_P HELX_P117 AM9 GLY A 4152 ? ILE A 4164 ? GLY A 4152 ILE A 4164 1 ? 13 
HELX_P HELX_P118 AN1 PRO A 4165 ? CYS A 4170 ? PRO A 4165 CYS A 4170 1 ? 6  
HELX_P HELX_P119 AN2 GLU A 4175 ? ARG A 4195 ? GLU A 4175 ARG A 4195 1 ? 21 
HELX_P HELX_P120 AN3 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P121 AN4 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P122 AN5 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P123 AN6 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P124 AN7 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P125 AN8 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P126 AN9 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
HELX_P HELX_P127 AO1 PRO A 4324 ? ALA A 4327 ? PRO A 4324 ALA A 4327 5 ? 4  
HELX_P HELX_P128 AO2 GLU A 4328 ? MET A 4346 ? GLU A 4328 MET A 4346 1 ? 19 
HELX_P HELX_P129 AO3 ALA A 4375 ? ILE A 4391 ? ALA A 4375 ILE A 4391 1 ? 17 
HELX_P HELX_P130 AO4 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P131 AO5 THR A 4445 ? LYS A 4457 ? THR A 4445 LYS A 4457 1 ? 13 
HELX_P HELX_P132 AO6 THR A 4474 ? SER A 4498 ? THR A 4474 SER A 4498 1 ? 25 
HELX_P HELX_P133 AO7 GLY A 4500 ? ILE A 4507 ? GLY A 4500 ILE A 4507 1 ? 8  
HELX_P HELX_P134 AO8 VAL A 4516 ? SER A 4533 ? VAL A 4516 SER A 4533 1 ? 18 
HELX_P HELX_P135 AO9 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P136 AP1 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 ? ? ? ? ? ? ? 1.958 ? ? 
metalc2 metalc ? ? A SER 2231 OG  ? ? ? 1_555 G MG  . MG ? ? A SER 2231 A MG  4706 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc3 metalc ? ? A GLU 2344 OE2 ? ? ? 1_555 G MG  . MG ? ? A GLU 2344 A MG  4706 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc4 metalc ? ? B ADP .    O3B ? ? ? 1_555 F MG  . MG ? ? A ADP 4701 A MG  4705 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc5 metalc ? ? C ATP .    O2G ? ? ? 1_555 G MG  . MG ? ? A ATP 4702 A MG  4706 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc6 metalc ? ? C ATP .    O2B ? ? ? 1_555 G MG  . MG ? ? A ATP 4702 A MG  4706 1_555 ? ? ? ? ? ? ? 2.646 ? ? 
metalc7 metalc ? ? F MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4705 A HOH 4801 1_555 ? ? ? ? ? ? ? 1.961 ? ? 
metalc8 metalc ? ? F MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4705 A HOH 4802 1_555 ? ? ? ? ? ? ? 1.988 ? ? 
metalc9 metalc ? ? F MG  .    MG  ? ? ? 1_555 H HOH . O  ? ? A MG  4705 A HOH 4803 1_555 ? ? ? ? ? ? ? 1.978 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O3B ? B ADP .    ? A ADP 4701 ? 1_555 103.4 ? 
2  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4801 ? 1_555 87.5  ? 
3  O3B ? B ADP .    ? A ADP 4701 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4801 ? 1_555 68.7  ? 
4  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4802 ? 1_555 136.1 ? 
5  O3B ? B ADP .    ? A ADP 4701 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4802 ? 1_555 103.1 ? 
6  O   ? H HOH .    ? A HOH 4801 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4802 ? 1_555 70.5  ? 
7  OG1 ? A THR 1913 ? A THR 1913 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4803 ? 1_555 119.3 ? 
8  O3B ? B ADP .    ? A ADP 4701 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4803 ? 1_555 117.7 ? 
9  O   ? H HOH .    ? A HOH 4801 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4803 ? 1_555 147.0 ? 
10 O   ? H HOH .    ? A HOH 4802 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O   ? H HOH .    ? A HOH 4803 ? 1_555 76.6  ? 
11 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 102.8 ? 
12 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 133.4 ? 
13 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 95.6  ? 
14 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 57.5  ? 
15 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 83.5  ? 
16 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? G MG . ? A MG 4706 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 83.2  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 2 ? 
AB5 ? 5 ? 
AB6 ? 5 ? 
AB7 ? 3 ? 
AB8 ? 5 ? 
AB9 ? 2 ? 
AC1 ? 4 ? 
AC2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB3 1 2 ? anti-parallel 
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? parallel      
AB8 3 4 ? parallel      
AB8 4 5 ? parallel      
AB9 1 2 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? parallel      
AC2 3 4 ? anti-parallel 
AC2 4 5 ? parallel      
AC2 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 1476 ? TYR A 1480 ? ASP A 1476 TYR A 1480 
AA1 2 CYS A 1484 ? ARG A 1488 ? CYS A 1484 ARG A 1488 
AA2 1 SER A 1663 ? LEU A 1666 ? SER A 1663 LEU A 1666 
AA2 2 VAL A 1672 ? SER A 1677 ? VAL A 1672 SER A 1677 
AA2 3 GLU A 1683 ? SER A 1691 ? GLU A 1683 SER A 1691 
AA3 1 MET A 1842 ? PHE A 1846 ? MET A 1842 PHE A 1846 
AA3 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA3 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA4 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA4 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA5 1 VAL A 1927 ? ASN A 1931 ? VAL A 1927 ASN A 1931 
AA5 2 TRP A 1954 ? ASP A 1958 ? TRP A 1954 ASP A 1958 
AA5 3 ALA A 2013 ? THR A 2017 ? ALA A 2013 THR A 2017 
AA6 1 THR A 1998 ? LEU A 2001 ? THR A 1998 LEU A 2001 
AA6 2 LYS A 2004 ? LYS A 2007 ? LYS A 2004 LYS A 2007 
AA7 1 GLY A 2249 ? ILE A 2254 ? GLY A 2249 ILE A 2254 
AA7 2 ARG A 2298 ? ASP A 2304 ? ARG A 2298 ASP A 2304 
AA7 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA7 4 GLY A 2219 ? VAL A 2223 ? GLY A 2219 VAL A 2223 
AA7 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA8 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA8 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA9 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA9 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AB1 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AB1 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB2 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB2 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB2 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB2 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB2 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB3 1 CYS A 2639 ? ARG A 2643 ? CYS A 2639 ARG A 2643 
AB3 2 VAL A 2648 ? PRO A 2652 ? VAL A 2648 PRO A 2652 
AB3 3 TRP A 2700 ? LEU A 2703 ? TRP A 2700 LEU A 2703 
AB3 4 GLY A 2691 ? TYR A 2693 ? GLY A 2691 TYR A 2693 
AB4 1 TYR A 2873 ? SER A 2874 ? TYR A 2873 SER A 2874 
AB4 2 ILE A 2882 ? PRO A 2883 ? ILE A 2882 PRO A 2883 
AB5 1 SER A 2957 ? TYR A 2959 ? SER A 2957 TYR A 2959 
AB5 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB5 3 LEU A 3062 ? MET A 3068 ? LEU A 3062 MET A 3068 
AB5 4 HIS A 2932 ? GLY A 2937 ? HIS A 2932 GLY A 2937 
AB5 5 CYS A 3089 ? GLY A 3095 ? CYS A 3089 GLY A 3095 
AB6 1 THR A 3610 ? SER A 3613 ? THR A 3610 SER A 3613 
AB6 2 PRO A 3632 ? GLN A 3636 ? PRO A 3632 GLN A 3636 
AB6 3 VAL A 3676 ? THR A 3681 ? VAL A 3676 THR A 3681 
AB6 4 PRO A 3587 ? ILE A 3590 ? PRO A 3587 ILE A 3590 
AB6 5 THR A 3697 ? ASN A 3700 ? THR A 3697 ASN A 3700 
AB7 1 ARG A 3654 ? THR A 3656 ? ARG A 3654 THR A 3656 
AB7 2 ARG A 3659 ? LEU A 3664 ? ARG A 3659 LEU A 3664 
AB7 3 GLN A 3667 ? ASP A 3670 ? GLN A 3667 ASP A 3670 
AB8 1 ILE A 4066 ? ALA A 4070 ? ILE A 4066 ALA A 4070 
AB8 2 TRP A 4093 ? LYS A 4097 ? TRP A 4093 LYS A 4097 
AB8 3 ARG A 4123 ? GLU A 4129 ? ARG A 4123 GLU A 4129 
AB8 4 VAL A 4041 ? SER A 4045 ? VAL A 4041 SER A 4045 
AB8 5 ARG A 4143 ? PHE A 4147 ? ARG A 4143 PHE A 4147 
AB9 1 LYS A 4283 ? ALA A 4285 ? LYS A 4283 ALA A 4285 
AB9 2 ILE A 4294 ? GLN A 4295 ? ILE A 4294 GLN A 4295 
AC1 1 VAL A 4509 ? CYS A 4510 ? VAL A 4509 CYS A 4510 
AC1 2 SER A 4557 ? THR A 4561 ? SER A 4557 THR A 4561 
AC1 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AC1 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC2 1 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
AC2 2 LYS A 4574 ? ALA A 4584 ? LYS A 4574 ALA A 4584 
AC2 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AC2 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AC2 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AC2 6 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASP A 1476 ? N ASP A 1476 O ARG A 1488 ? O ARG A 1488 
AA2 1 2 N SER A 1663 ? N SER A 1663 O SER A 1677 ? O SER A 1677 
AA2 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
AA3 1 2 N ARG A 1843 ? N ARG A 1843 O GLN A 1860 ? O GLN A 1860 
AA3 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA4 1 2 N GLY A 1901 ? N GLY A 1901 O ARG A 2037 ? O ARG A 2037 
AA5 1 2 N LEU A 1928 ? N LEU A 1928 O TRP A 1954 ? O TRP A 1954 
AA5 2 3 N PHE A 1957 ? N PHE A 1957 O PHE A 2015 ? O PHE A 2015 
AA6 1 2 N LEU A 2001 ? N LEU A 2001 O LYS A 2004 ? O LYS A 2004 
AA7 1 2 N HIS A 2252 ? N HIS A 2252 O TRP A 2300 ? O TRP A 2300 
AA7 2 3 N PHE A 2303 ? N PHE A 2303 O MET A 2342 ? O MET A 2342 
AA7 3 4 O ILE A 2341 ? O ILE A 2341 N LEU A 2220 ? N LEU A 2220 
AA7 4 5 N GLY A 2219 ? N GLY A 2219 O GLY A 2360 ? O GLY A 2360 
AA8 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA9 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB1 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB2 1 2 N GLU A 2616 ? N GLU A 2616 O VAL A 2660 ? O VAL A 2660 
AB2 2 3 N LEU A 2661 ? N LEU A 2661 O VAL A 2709 ? O VAL A 2709 
AB2 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 2593 ? N LEU A 2593 
AB2 4 5 N CYS A 2594 ? N CYS A 2594 O VAL A 2734 ? O VAL A 2734 
AB3 1 2 N ARG A 2642 ? N ARG A 2642 O VAL A 2649 ? O VAL A 2649 
AB3 2 3 N VAL A 2648 ? N VAL A 2648 O LYS A 2702 ? O LYS A 2702 
AB3 3 4 O VAL A 2701 ? O VAL A 2701 N PHE A 2692 ? N PHE A 2692 
AB4 1 2 N SER A 2874 ? N SER A 2874 O ILE A 2882 ? O ILE A 2882 
AB5 1 2 N SER A 2957 ? N SER A 2957 O ALA A 2991 ? O ALA A 2991 
AB5 2 3 N PHE A 2992 ? N PHE A 2992 O VAL A 3065 ? O VAL A 3065 
AB5 3 4 O PHE A 3066 ? O PHE A 3066 N LEU A 2933 ? N LEU A 2933 
AB5 4 5 N HIS A 2932 ? N HIS A 2932 O VAL A 3090 ? O VAL A 3090 
AB6 1 2 N THR A 3610 ? N THR A 3610 O LEU A 3634 ? O LEU A 3634 
AB6 2 3 N VAL A 3635 ? N VAL A 3635 O PHE A 3678 ? O PHE A 3678 
AB6 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB6 4 5 N LEU A 3588 ? N LEU A 3588 O THR A 3697 ? O THR A 3697 
AB7 1 2 N ARG A 3654 ? N ARG A 3654 O LEU A 3661 ? O LEU A 3661 
AB7 2 3 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB8 1 2 N THR A 4067 ? N THR A 4067 O TRP A 4093 ? O TRP A 4093 
AB8 2 3 N VAL A 4094 ? N VAL A 4094 O PHE A 4125 ? O PHE A 4125 
AB8 3 4 O LEU A 4124 ? O LEU A 4124 N VAL A 4041 ? N VAL A 4041 
AB8 4 5 N LEU A 4042 ? N LEU A 4042 O PHE A 4145 ? O PHE A 4145 
AB9 1 2 N LEU A 4284 ? N LEU A 4284 O ILE A 4294 ? O ILE A 4294 
AC1 1 2 N VAL A 4509 ? N VAL A 4509 O THR A 4561 ? O THR A 4561 
AC1 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AC1 3 4 O ARG A 4591 ? O ARG A 4591 N GLU A 4542 ? N GLU A 4542 
AC2 1 2 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
AC2 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC2 3 4 O ILE A 4619 ? O ILE A 4619 N VAL A 4609 ? N VAL A 4609 
AC2 4 5 N TYR A 4610 ? N TYR A 4610 O VAL A 4642 ? O VAL A 4642 
AC2 5 6 O ALA A 4641 ? O ALA A 4641 N GLN A 4566 ? N GLN A 4566 
# 
_pdbx_entry_details.entry_id                   9BM0 
_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 O   A GLY 3106 ? ? OG1   A THR 3110 ? ? 2.13 
2 1 OG  A SER 2317 ? ? O     A LEU 2324 ? ? 2.18 
3 1 OE1 A GLU 2174 ? ? OG1   A THR 2176 ? ? 2.19 
4 1 NZ  A LYS 2094 ? ? "O2'" A ADP 4701 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 1643 ? ? -93.85  32.21   
2 1 ALA A 1862 ? ? 58.56   -123.52 
3 1 GLU A 2587 ? ? -59.04  -0.95   
4 1 PRO A 2796 ? ? -56.53  -9.90   
5 1 SER A 3640 ? ? -108.99 41.39   
6 1 ASN A 4597 ? ? 38.58   48.47   
7 1 GLU A 4599 ? ? 61.91   -143.06 
8 1 THR A 4628 ? ? 50.84   -142.80 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 2642 ? ? 0.077 'SIDE CHAIN' 
2 1 ARG A 2753 ? ? 0.118 'SIDE CHAIN' 
3 1 ARG A 3164 ? ? 0.098 'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BM0 
_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                    9BM0 
_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                  2.8 
_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               165772 
_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-2 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                        9BM0 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             3000 
_em_imaging.calibrated_defocus_min          1200 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_em_imaging.calibrated_magnification        105000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            50 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9BM0 
_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                9BM0 
_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 GLY 2390 ? A GLY 2390 
1458 1 Y 1 A GLU 2391 ? A GLU 2391 
1459 1 Y 1 A ASP 2392 ? A ASP 2392 
1460 1 Y 1 A GLU 2393 ? A GLU 2393 
1461 1 Y 1 A ALA 2394 ? A ALA 2394 
1462 1 Y 1 A GLN 2395 ? A GLN 2395 
1463 1 Y 1 A ARG 2396 ? A ARG 2396 
1464 1 Y 1 A ARG 2397 ? A ARG 2397 
1465 1 Y 1 A ARG 2398 ? A ARG 2398 
1466 1 Y 1 A LYS 2399 ? A LYS 2399 
1467 1 Y 1 A GLY 2400 ? A GLY 2400 
1468 1 Y 1 A LYS 2401 ? A LYS 2401 
1469 1 Y 1 A GLU 2402 ? A GLU 2402 
1470 1 Y 1 A ASP 2403 ? A ASP 2403 
1471 1 Y 1 A GLU 2404 ? A GLU 2404 
1472 1 Y 1 A GLY 2405 ? A GLY 2405 
1473 1 Y 1 A GLU 2406 ? A GLU 2406 
1474 1 Y 1 A GLU 2407 ? A GLU 2407 
1475 1 Y 1 A ALA 2408 ? A ALA 2408 
1476 1 Y 1 A ALA 2409 ? A ALA 2409 
1477 1 Y 1 A MET 3243 ? A MET 3243 
1478 1 Y 1 A VAL 3244 ? A VAL 3244 
1479 1 Y 1 A LYS 3245 ? A LYS 3245 
1480 1 Y 1 A ASP 3246 ? A ASP 3246 
1481 1 Y 1 A GLN 3247 ? A GLN 3247 
1482 1 Y 1 A GLN 3248 ? A GLN 3248 
1483 1 Y 1 A GLU 3249 ? A GLU 3249 
1484 1 Y 1 A ALA 3250 ? A ALA 3250 
1485 1 Y 1 A GLU 3251 ? A GLU 3251 
1486 1 Y 1 A LYS 3252 ? A LYS 3252 
1487 1 Y 1 A LYS 3253 ? A LYS 3253 
1488 1 Y 1 A LYS 3254 ? A LYS 3254 
1489 1 Y 1 A VAL 3255 ? A VAL 3255 
1490 1 Y 1 A MET 3256 ? A MET 3256 
1491 1 Y 1 A SER 3257 ? A SER 3257 
1492 1 Y 1 A GLN 3258 ? A GLN 3258 
1493 1 Y 1 A GLU 3259 ? A GLU 3259 
1494 1 Y 1 A ILE 3260 ? A ILE 3260 
1495 1 Y 1 A GLN 3261 ? A GLN 3261 
1496 1 Y 1 A GLU 3262 ? A GLU 3262 
1497 1 Y 1 A GLN 3263 ? A GLN 3263 
1498 1 Y 1 A LEU 3264 ? A LEU 3264 
1499 1 Y 1 A HIS 3265 ? A HIS 3265 
1500 1 Y 1 A LYS 3266 ? A LYS 3266 
1501 1 Y 1 A GLN 3267 ? A GLN 3267 
1502 1 Y 1 A GLN 3268 ? A GLN 3268 
1503 1 Y 1 A GLU 3269 ? A GLU 3269 
1504 1 Y 1 A VAL 3270 ? A VAL 3270 
1505 1 Y 1 A ILE 3271 ? A ILE 3271 
1506 1 Y 1 A ALA 3272 ? A ALA 3272 
1507 1 Y 1 A ASP 3273 ? A ASP 3273 
1508 1 Y 1 A LYS 3274 ? A LYS 3274 
1509 1 Y 1 A GLN 3275 ? A GLN 3275 
1510 1 Y 1 A MET 3276 ? A MET 3276 
1511 1 Y 1 A SER 3277 ? A SER 3277 
1512 1 Y 1 A VAL 3278 ? A VAL 3278 
1513 1 Y 1 A LYS 3279 ? A LYS 3279 
1514 1 Y 1 A GLU 3280 ? A GLU 3280 
1515 1 Y 1 A ASP 3281 ? A ASP 3281 
1516 1 Y 1 A LEU 3282 ? A LEU 3282 
1517 1 Y 1 A ASP 3283 ? A ASP 3283 
1518 1 Y 1 A LYS 3284 ? A LYS 3284 
1519 1 Y 1 A VAL 3285 ? A VAL 3285 
1520 1 Y 1 A GLU 3286 ? A GLU 3286 
1521 1 Y 1 A PRO 3287 ? A PRO 3287 
1522 1 Y 1 A ALA 3288 ? A ALA 3288 
1523 1 Y 1 A VAL 3289 ? A VAL 3289 
1524 1 Y 1 A ILE 3290 ? A ILE 3290 
1525 1 Y 1 A GLU 3291 ? A GLU 3291 
1526 1 Y 1 A ALA 3292 ? A ALA 3292 
1527 1 Y 1 A GLN 3293 ? A GLN 3293 
1528 1 Y 1 A ASN 3294 ? A ASN 3294 
1529 1 Y 1 A ALA 3295 ? A ALA 3295 
1530 1 Y 1 A VAL 3296 ? A VAL 3296 
1531 1 Y 1 A LYS 3297 ? A LYS 3297 
1532 1 Y 1 A SER 3298 ? A SER 3298 
1533 1 Y 1 A ILE 3299 ? A ILE 3299 
1534 1 Y 1 A LYS 3300 ? A LYS 3300 
1535 1 Y 1 A LYS 3301 ? A LYS 3301 
1536 1 Y 1 A GLN 3302 ? A GLN 3302 
1537 1 Y 1 A HIS 3303 ? A HIS 3303 
1538 1 Y 1 A LEU 3304 ? A LEU 3304 
1539 1 Y 1 A VAL 3305 ? A VAL 3305 
1540 1 Y 1 A GLU 3306 ? A GLU 3306 
1541 1 Y 1 A VAL 3307 ? A VAL 3307 
1542 1 Y 1 A ARG 3308 ? A ARG 3308 
1543 1 Y 1 A SER 3309 ? A SER 3309 
1544 1 Y 1 A MET 3310 ? A MET 3310 
1545 1 Y 1 A ALA 3311 ? A ALA 3311 
1546 1 Y 1 A ASN 3312 ? A ASN 3312 
1547 1 Y 1 A PRO 3313 ? A PRO 3313 
1548 1 Y 1 A PRO 3314 ? A PRO 3314 
1549 1 Y 1 A ALA 3315 ? A ALA 3315 
1550 1 Y 1 A ALA 3316 ? A ALA 3316 
1551 1 Y 1 A VAL 3317 ? A VAL 3317 
1552 1 Y 1 A LYS 3318 ? A LYS 3318 
1553 1 Y 1 A LEU 3319 ? A LEU 3319 
1554 1 Y 1 A ALA 3320 ? A ALA 3320 
1555 1 Y 1 A LEU 3321 ? A LEU 3321 
1556 1 Y 1 A GLU 3322 ? A GLU 3322 
1557 1 Y 1 A SER 3323 ? A SER 3323 
1558 1 Y 1 A ILE 3324 ? A ILE 3324 
1559 1 Y 1 A CYS 3325 ? A CYS 3325 
1560 1 Y 1 A LEU 3326 ? A LEU 3326 
1561 1 Y 1 A LEU 3327 ? A LEU 3327 
1562 1 Y 1 A LEU 3328 ? A LEU 3328 
1563 1 Y 1 A GLY 3329 ? A GLY 3329 
1564 1 Y 1 A GLU 3330 ? A GLU 3330 
1565 1 Y 1 A SER 3331 ? A SER 3331 
1566 1 Y 1 A THR 3332 ? A THR 3332 
1567 1 Y 1 A THR 3333 ? A THR 3333 
1568 1 Y 1 A ASP 3334 ? A ASP 3334 
1569 1 Y 1 A TRP 3335 ? A TRP 3335 
1570 1 Y 1 A LYS 3336 ? A LYS 3336 
1571 1 Y 1 A GLN 3337 ? A GLN 3337 
1572 1 Y 1 A ILE 3338 ? A ILE 3338 
1573 1 Y 1 A ARG 3339 ? A ARG 3339 
1574 1 Y 1 A SER 3340 ? A SER 3340 
1575 1 Y 1 A ILE 3341 ? A ILE 3341 
1576 1 Y 1 A ILE 3342 ? A ILE 3342 
1577 1 Y 1 A MET 3343 ? A MET 3343 
1578 1 Y 1 A ARG 3344 ? A ARG 3344 
1579 1 Y 1 A GLU 3345 ? A GLU 3345 
1580 1 Y 1 A ASN 3346 ? A ASN 3346 
1581 1 Y 1 A PHE 3347 ? A PHE 3347 
1582 1 Y 1 A ILE 3348 ? A ILE 3348 
1583 1 Y 1 A PRO 3349 ? A PRO 3349 
1584 1 Y 1 A THR 3350 ? A THR 3350 
1585 1 Y 1 A ILE 3351 ? A ILE 3351 
1586 1 Y 1 A VAL 3352 ? A VAL 3352 
1587 1 Y 1 A ASN 3353 ? A ASN 3353 
1588 1 Y 1 A PHE 3354 ? A PHE 3354 
1589 1 Y 1 A SER 3355 ? A SER 3355 
1590 1 Y 1 A ALA 3356 ? A ALA 3356 
1591 1 Y 1 A GLU 3357 ? A GLU 3357 
1592 1 Y 1 A GLU 3358 ? A GLU 3358 
1593 1 Y 1 A ILE 3359 ? A ILE 3359 
1594 1 Y 1 A SER 3360 ? A SER 3360 
1595 1 Y 1 A ASP 3361 ? A ASP 3361 
1596 1 Y 1 A ALA 3362 ? A ALA 3362 
1597 1 Y 1 A ILE 3363 ? A ILE 3363 
1598 1 Y 1 A ARG 3364 ? A ARG 3364 
1599 1 Y 1 A GLU 3365 ? A GLU 3365 
1600 1 Y 1 A LYS 3366 ? A LYS 3366 
1601 1 Y 1 A MET 3367 ? A MET 3367 
1602 1 Y 1 A LYS 3368 ? A LYS 3368 
1603 1 Y 1 A LYS 3369 ? A LYS 3369 
1604 1 Y 1 A ASN 3370 ? A ASN 3370 
1605 1 Y 1 A TYR 3371 ? A TYR 3371 
1606 1 Y 1 A MET 3372 ? A MET 3372 
1607 1 Y 1 A SER 3373 ? A SER 3373 
1608 1 Y 1 A ASN 3374 ? A ASN 3374 
1609 1 Y 1 A PRO 3375 ? A PRO 3375 
1610 1 Y 1 A SER 3376 ? A SER 3376 
1611 1 Y 1 A TYR 3377 ? A TYR 3377 
1612 1 Y 1 A ASN 3378 ? A ASN 3378 
1613 1 Y 1 A TYR 3379 ? A TYR 3379 
1614 1 Y 1 A GLU 3380 ? A GLU 3380 
1615 1 Y 1 A ILE 3381 ? A ILE 3381 
1616 1 Y 1 A VAL 3382 ? A VAL 3382 
1617 1 Y 1 A ASN 3383 ? A ASN 3383 
1618 1 Y 1 A ARG 3384 ? A ARG 3384 
1619 1 Y 1 A ALA 3385 ? A ALA 3385 
1620 1 Y 1 A SER 3386 ? A SER 3386 
1621 1 Y 1 A LEU 3387 ? A LEU 3387 
1622 1 Y 1 A ALA 3388 ? A ALA 3388 
1623 1 Y 1 A CYS 3389 ? A CYS 3389 
1624 1 Y 1 A GLY 3390 ? A GLY 3390 
1625 1 Y 1 A PRO 3391 ? A PRO 3391 
1626 1 Y 1 A MET 3392 ? A MET 3392 
1627 1 Y 1 A VAL 3393 ? A VAL 3393 
1628 1 Y 1 A LYS 3394 ? A LYS 3394 
1629 1 Y 1 A TRP 3395 ? A TRP 3395 
1630 1 Y 1 A ALA 3396 ? A ALA 3396 
1631 1 Y 1 A ILE 3397 ? A ILE 3397 
1632 1 Y 1 A ALA 3398 ? A ALA 3398 
1633 1 Y 1 A GLN 3399 ? A GLN 3399 
1634 1 Y 1 A LEU 3400 ? A LEU 3400 
1635 1 Y 1 A ASN 3401 ? A ASN 3401 
1636 1 Y 1 A TYR 3402 ? A TYR 3402 
1637 1 Y 1 A ALA 3403 ? A ALA 3403 
1638 1 Y 1 A ASP 3404 ? A ASP 3404 
1639 1 Y 1 A MET 3405 ? A MET 3405 
1640 1 Y 1 A LEU 3406 ? A LEU 3406 
1641 1 Y 1 A LYS 3407 ? A LYS 3407 
1642 1 Y 1 A ARG 3408 ? A ARG 3408 
1643 1 Y 1 A VAL 3409 ? A VAL 3409 
1644 1 Y 1 A GLU 3410 ? A GLU 3410 
1645 1 Y 1 A PRO 3411 ? A PRO 3411 
1646 1 Y 1 A LEU 3412 ? A LEU 3412 
1647 1 Y 1 A ARG 3413 ? A ARG 3413 
1648 1 Y 1 A ASN 3414 ? A ASN 3414 
1649 1 Y 1 A GLU 3415 ? A GLU 3415 
1650 1 Y 1 A LEU 3416 ? A LEU 3416 
1651 1 Y 1 A GLN 3417 ? A GLN 3417 
1652 1 Y 1 A LYS 3418 ? A LYS 3418 
1653 1 Y 1 A LEU 3419 ? A LEU 3419 
1654 1 Y 1 A GLU 3420 ? A GLU 3420 
1655 1 Y 1 A ASP 3421 ? A ASP 3421 
1656 1 Y 1 A ASP 3422 ? A ASP 3422 
1657 1 Y 1 A ALA 3423 ? A ALA 3423 
1658 1 Y 1 A LYS 3424 ? A LYS 3424 
1659 1 Y 1 A ASP 3425 ? A ASP 3425 
1660 1 Y 1 A ASN 3426 ? A ASN 3426 
1661 1 Y 1 A GLN 3427 ? A GLN 3427 
1662 1 Y 1 A GLN 3428 ? A GLN 3428 
1663 1 Y 1 A LYS 3429 ? A LYS 3429 
1664 1 Y 1 A ALA 3430 ? A ALA 3430 
1665 1 Y 1 A ASN 3431 ? A ASN 3431 
1666 1 Y 1 A GLU 3432 ? A GLU 3432 
1667 1 Y 1 A VAL 3433 ? A VAL 3433 
1668 1 Y 1 A GLU 3434 ? A GLU 3434 
1669 1 Y 1 A GLN 3435 ? A GLN 3435 
1670 1 Y 1 A MET 3436 ? A MET 3436 
1671 1 Y 1 A ILE 3437 ? A ILE 3437 
1672 1 Y 1 A ARG 3438 ? A ARG 3438 
1673 1 Y 1 A ASP 3439 ? A ASP 3439 
1674 1 Y 1 A LEU 3440 ? A LEU 3440 
1675 1 Y 1 A GLU 3441 ? A GLU 3441 
1676 1 Y 1 A ALA 3442 ? A ALA 3442 
1677 1 Y 1 A SER 3443 ? A SER 3443 
1678 1 Y 1 A ILE 3444 ? A ILE 3444 
1679 1 Y 1 A ALA 3445 ? A ALA 3445 
1680 1 Y 1 A ARG 3446 ? A ARG 3446 
1681 1 Y 1 A TYR 3447 ? A TYR 3447 
1682 1 Y 1 A LYS 3448 ? A LYS 3448 
1683 1 Y 1 A MET 4348 ? A MET 4348 
1684 1 Y 1 A LEU 4349 ? A LEU 4349 
1685 1 Y 1 A GLU 4350 ? A GLU 4350 
1686 1 Y 1 A ASP 4351 ? A ASP 4351 
1687 1 Y 1 A GLU 4352 ? A GLU 4352 
1688 1 Y 1 A ASP 4353 ? A ASP 4353 
1689 1 Y 1 A ASP 4354 ? A ASP 4354 
1690 1 Y 1 A LEU 4355 ? A LEU 4355 
1691 1 Y 1 A ALA 4356 ? A ALA 4356 
1692 1 Y 1 A TYR 4357 ? A TYR 4357 
1693 1 Y 1 A ALA 4358 ? A ALA 4358 
1694 1 Y 1 A GLU 4359 ? A GLU 4359 
1695 1 Y 1 A THR 4360 ? A THR 4360 
1696 1 Y 1 A GLU 4361 ? A GLU 4361 
1697 1 Y 1 A LYS 4362 ? A LYS 4362 
1698 1 Y 1 A LYS 4363 ? A LYS 4363 
1699 1 Y 1 A THR 4364 ? A THR 4364 
1700 1 Y 1 A ARG 4365 ? A ARG 4365 
1701 1 Y 1 A THR 4366 ? A THR 4366 
1702 1 Y 1 A ASP 4367 ? A ASP 4367 
1703 1 Y 1 A SER 4368 ? A SER 4368 
1704 1 Y 1 A THR 4369 ? A THR 4369 
1705 1 Y 1 A SER 4370 ? A SER 4370 
1706 1 Y 1 A ASP 4371 ? A ASP 4371 
1707 1 Y 1 A GLY 4372 ? A GLY 4372 
1708 1 Y 1 A ARG 4373 ? A ARG 4373 
1709 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 
HOH O      O  N N 247 
HOH H1     H  N N 248 
HOH H2     H  N N 249 
ILE N      N  N N 250 
ILE CA     C  N S 251 
ILE C      C  N N 252 
ILE O      O  N N 253 
ILE CB     C  N S 254 
ILE CG1    C  N N 255 
ILE CG2    C  N N 256 
ILE CD1    C  N N 257 
ILE OXT    O  N N 258 
ILE H      H  N N 259 
ILE H2     H  N N 260 
ILE HA     H  N N 261 
ILE HB     H  N N 262 
ILE HG12   H  N N 263 
ILE HG13   H  N N 264 
ILE HG21   H  N N 265 
ILE HG22   H  N N 266 
ILE HG23   H  N N 267 
ILE HD11   H  N N 268 
ILE HD12   H  N N 269 
ILE HD13   H  N N 270 
ILE HXT    H  N N 271 
LEU N      N  N N 272 
LEU CA     C  N S 273 
LEU C      C  N N 274 
LEU O      O  N N 275 
LEU CB     C  N N 276 
LEU CG     C  N N 277 
LEU CD1    C  N N 278 
LEU CD2    C  N N 279 
LEU OXT    O  N N 280 
LEU H      H  N N 281 
LEU H2     H  N N 282 
LEU HA     H  N N 283 
LEU HB2    H  N N 284 
LEU HB3    H  N N 285 
LEU HG     H  N N 286 
LEU HD11   H  N N 287 
LEU HD12   H  N N 288 
LEU HD13   H  N N 289 
LEU HD21   H  N N 290 
LEU HD22   H  N N 291 
LEU HD23   H  N N 292 
LEU HXT    H  N N 293 
LYS N      N  N N 294 
LYS CA     C  N S 295 
LYS C      C  N N 296 
LYS O      O  N N 297 
LYS CB     C  N N 298 
LYS CG     C  N N 299 
LYS CD     C  N N 300 
LYS CE     C  N N 301 
LYS NZ     N  N N 302 
LYS OXT    O  N N 303 
LYS H      H  N N 304 
LYS H2     H  N N 305 
LYS HA     H  N N 306 
LYS HB2    H  N N 307 
LYS HB3    H  N N 308 
LYS HG2    H  N N 309 
LYS HG3    H  N N 310 
LYS HD2    H  N N 311 
LYS HD3    H  N N 312 
LYS HE2    H  N N 313 
LYS HE3    H  N N 314 
LYS HZ1    H  N N 315 
LYS HZ2    H  N N 316 
LYS HZ3    H  N N 317 
LYS HXT    H  N N 318 
MET N      N  N N 319 
MET CA     C  N S 320 
MET C      C  N N 321 
MET O      O  N N 322 
MET CB     C  N N 323 
MET CG     C  N N 324 
MET SD     S  N N 325 
MET CE     C  N N 326 
MET OXT    O  N N 327 
MET H      H  N N 328 
MET H2     H  N N 329 
MET HA     H  N N 330 
MET HB2    H  N N 331 
MET HB3    H  N N 332 
MET HG2    H  N N 333 
MET HG3    H  N N 334 
MET HE1    H  N N 335 
MET HE2    H  N N 336 
MET HE3    H  N N 337 
MET HXT    H  N N 338 
MG  MG     MG N N 339 
PHE N      N  N N 340 
PHE CA     C  N S 341 
PHE C      C  N N 342 
PHE O      O  N N 343 
PHE CB     C  N N 344 
PHE CG     C  Y N 345 
PHE CD1    C  Y N 346 
PHE CD2    C  Y N 347 
PHE CE1    C  Y N 348 
PHE CE2    C  Y N 349 
PHE CZ     C  Y N 350 
PHE OXT    O  N N 351 
PHE H      H  N N 352 
PHE H2     H  N N 353 
PHE HA     H  N N 354 
PHE HB2    H  N N 355 
PHE HB3    H  N N 356 
PHE HD1    H  N N 357 
PHE HD2    H  N N 358 
PHE HE1    H  N N 359 
PHE HE2    H  N N 360 
PHE HZ     H  N N 361 
PHE HXT    H  N N 362 
PRO N      N  N N 363 
PRO CA     C  N S 364 
PRO C      C  N N 365 
PRO O      O  N N 366 
PRO CB     C  N N 367 
PRO CG     C  N N 368 
PRO CD     C  N N 369 
PRO OXT    O  N N 370 
PRO H      H  N N 371 
PRO HA     H  N N 372 
PRO HB2    H  N N 373 
PRO HB3    H  N N 374 
PRO HG2    H  N N 375 
PRO HG3    H  N N 376 
PRO HD2    H  N N 377 
PRO HD3    H  N N 378 
PRO HXT    H  N N 379 
SER N      N  N N 380 
SER CA     C  N S 381 
SER C      C  N N 382 
SER O      O  N N 383 
SER CB     C  N N 384 
SER OG     O  N N 385 
SER OXT    O  N N 386 
SER H      H  N N 387 
SER H2     H  N N 388 
SER HA     H  N N 389 
SER HB2    H  N N 390 
SER HB3    H  N N 391 
SER HG     H  N N 392 
SER HXT    H  N N 393 
THR N      N  N N 394 
THR CA     C  N S 395 
THR C      C  N N 396 
THR O      O  N N 397 
THR CB     C  N R 398 
THR OG1    O  N N 399 
THR CG2    C  N N 400 
THR OXT    O  N N 401 
THR H      H  N N 402 
THR H2     H  N N 403 
THR HA     H  N N 404 
THR HB     H  N N 405 
THR HG1    H  N N 406 
THR HG21   H  N N 407 
THR HG22   H  N N 408 
THR HG23   H  N N 409 
THR HXT    H  N N 410 
TRP N      N  N N 411 
TRP CA     C  N S 412 
TRP C      C  N N 413 
TRP O      O  N N 414 
TRP CB     C  N N 415 
TRP CG     C  Y N 416 
TRP CD1    C  Y N 417 
TRP CD2    C  Y N 418 
TRP NE1    N  Y N 419 
TRP CE2    C  Y N 420 
TRP CE3    C  Y N 421 
TRP CZ2    C  Y N 422 
TRP CZ3    C  Y N 423 
TRP CH2    C  Y N 424 
TRP OXT    O  N N 425 
TRP H      H  N N 426 
TRP H2     H  N N 427 
TRP HA     H  N N 428 
TRP HB2    H  N N 429 
TRP HB3    H  N N 430 
TRP HD1    H  N N 431 
TRP HE1    H  N N 432 
TRP HE3    H  N N 433 
TRP HZ2    H  N N 434 
TRP HZ3    H  N N 435 
TRP HH2    H  N N 436 
TRP HXT    H  N N 437 
TYR N      N  N N 438 
TYR CA     C  N S 439 
TYR C      C  N N 440 
TYR O      O  N N 441 
TYR CB     C  N N 442 
TYR CG     C  Y N 443 
TYR CD1    C  Y N 444 
TYR CD2    C  Y N 445 
TYR CE1    C  Y N 446 
TYR CE2    C  Y N 447 
TYR CZ     C  Y N 448 
TYR OH     O  N N 449 
TYR OXT    O  N N 450 
TYR H      H  N N 451 
TYR H2     H  N N 452 
TYR HA     H  N N 453 
TYR HB2    H  N N 454 
TYR HB3    H  N N 455 
TYR HD1    H  N N 456 
TYR HD2    H  N N 457 
TYR HE1    H  N N 458 
TYR HE2    H  N N 459 
TYR HH     H  N N 460 
TYR HXT    H  N N 461 
VAL N      N  N N 462 
VAL CA     C  N S 463 
VAL C      C  N N 464 
VAL O      O  N N 465 
VAL CB     C  N N 466 
VAL CG1    C  N N 467 
VAL CG2    C  N N 468 
VAL OXT    O  N N 469 
VAL H      H  N N 470 
VAL H2     H  N N 471 
VAL HA     H  N N 472 
VAL HB     H  N N 473 
VAL HG11   H  N N 474 
VAL HG12   H  N N 475 
VAL HG13   H  N N 476 
VAL HG21   H  N N 477 
VAL HG22   H  N N 478 
VAL HG23   H  N N 479 
VAL HXT    H  N N 480 
# 
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 
HOH O     H1     sing N N 243 
HOH O     H2     sing N N 244 
ILE N     CA     sing N N 245 
ILE N     H      sing N N 246 
ILE N     H2     sing N N 247 
ILE CA    C      sing N N 248 
ILE CA    CB     sing N N 249 
ILE CA    HA     sing N N 250 
ILE C     O      doub N N 251 
ILE C     OXT    sing N N 252 
ILE CB    CG1    sing N N 253 
ILE CB    CG2    sing N N 254 
ILE CB    HB     sing N N 255 
ILE CG1   CD1    sing N N 256 
ILE CG1   HG12   sing N N 257 
ILE CG1   HG13   sing N N 258 
ILE CG2   HG21   sing N N 259 
ILE CG2   HG22   sing N N 260 
ILE CG2   HG23   sing N N 261 
ILE CD1   HD11   sing N N 262 
ILE CD1   HD12   sing N N 263 
ILE CD1   HD13   sing N N 264 
ILE OXT   HXT    sing N N 265 
LEU N     CA     sing N N 266 
LEU N     H      sing N N 267 
LEU N     H2     sing N N 268 
LEU CA    C      sing N N 269 
LEU CA    CB     sing N N 270 
LEU CA    HA     sing N N 271 
LEU C     O      doub N N 272 
LEU C     OXT    sing N N 273 
LEU CB    CG     sing N N 274 
LEU CB    HB2    sing N N 275 
LEU CB    HB3    sing N N 276 
LEU CG    CD1    sing N N 277 
LEU CG    CD2    sing N N 278 
LEU CG    HG     sing N N 279 
LEU CD1   HD11   sing N N 280 
LEU CD1   HD12   sing N N 281 
LEU CD1   HD13   sing N N 282 
LEU CD2   HD21   sing N N 283 
LEU CD2   HD22   sing N N 284 
LEU CD2   HD23   sing N N 285 
LEU OXT   HXT    sing N N 286 
LYS N     CA     sing N N 287 
LYS N     H      sing N N 288 
LYS N     H2     sing N N 289 
LYS CA    C      sing N N 290 
LYS CA    CB     sing N N 291 
LYS CA    HA     sing N N 292 
LYS C     O      doub N N 293 
LYS C     OXT    sing N N 294 
LYS CB    CG     sing N N 295 
LYS CB    HB2    sing N N 296 
LYS CB    HB3    sing N N 297 
LYS CG    CD     sing N N 298 
LYS CG    HG2    sing N N 299 
LYS CG    HG3    sing N N 300 
LYS CD    CE     sing N N 301 
LYS CD    HD2    sing N N 302 
LYS CD    HD3    sing N N 303 
LYS CE    NZ     sing N N 304 
LYS CE    HE2    sing N N 305 
LYS CE    HE3    sing N N 306 
LYS NZ    HZ1    sing N N 307 
LYS NZ    HZ2    sing N N 308 
LYS NZ    HZ3    sing N N 309 
LYS OXT   HXT    sing N N 310 
MET N     CA     sing N N 311 
MET N     H      sing N N 312 
MET N     H2     sing N N 313 
MET CA    C      sing N N 314 
MET CA    CB     sing N N 315 
MET CA    HA     sing N N 316 
MET C     O      doub N N 317 
MET C     OXT    sing N N 318 
MET CB    CG     sing N N 319 
MET CB    HB2    sing N N 320 
MET CB    HB3    sing N N 321 
MET CG    SD     sing N N 322 
MET CG    HG2    sing N N 323 
MET CG    HG3    sing N N 324 
MET SD    CE     sing N N 325 
MET CE    HE1    sing N N 326 
MET CE    HE2    sing N N 327 
MET CE    HE3    sing N N 328 
MET OXT   HXT    sing N N 329 
PHE N     CA     sing N N 330 
PHE N     H      sing N N 331 
PHE N     H2     sing N N 332 
PHE CA    C      sing N N 333 
PHE CA    CB     sing N N 334 
PHE CA    HA     sing N N 335 
PHE C     O      doub N N 336 
PHE C     OXT    sing N N 337 
PHE CB    CG     sing N N 338 
PHE CB    HB2    sing N N 339 
PHE CB    HB3    sing N N 340 
PHE CG    CD1    doub Y N 341 
PHE CG    CD2    sing Y N 342 
PHE CD1   CE1    sing Y N 343 
PHE CD1   HD1    sing N N 344 
PHE CD2   CE2    doub Y N 345 
PHE CD2   HD2    sing N N 346 
PHE CE1   CZ     doub Y N 347 
PHE CE1   HE1    sing N N 348 
PHE CE2   CZ     sing Y N 349 
PHE CE2   HE2    sing N N 350 
PHE CZ    HZ     sing N N 351 
PHE OXT   HXT    sing N N 352 
PRO N     CA     sing N N 353 
PRO N     CD     sing N N 354 
PRO N     H      sing N N 355 
PRO CA    C      sing N N 356 
PRO CA    CB     sing N N 357 
PRO CA    HA     sing N N 358 
PRO C     O      doub N N 359 
PRO C     OXT    sing N N 360 
PRO CB    CG     sing N N 361 
PRO CB    HB2    sing N N 362 
PRO CB    HB3    sing N N 363 
PRO CG    CD     sing N N 364 
PRO CG    HG2    sing N N 365 
PRO CG    HG3    sing N N 366 
PRO CD    HD2    sing N N 367 
PRO CD    HD3    sing N N 368 
PRO OXT   HXT    sing N N 369 
SER N     CA     sing N N 370 
SER N     H      sing N N 371 
SER N     H2     sing N N 372 
SER CA    C      sing N N 373 
SER CA    CB     sing N N 374 
SER CA    HA     sing N N 375 
SER C     O      doub N N 376 
SER C     OXT    sing N N 377 
SER CB    OG     sing N N 378 
SER CB    HB2    sing N N 379 
SER CB    HB3    sing N N 380 
SER OG    HG     sing N N 381 
SER OXT   HXT    sing N N 382 
THR N     CA     sing N N 383 
THR N     H      sing N N 384 
THR N     H2     sing N N 385 
THR CA    C      sing N N 386 
THR CA    CB     sing N N 387 
THR CA    HA     sing N N 388 
THR C     O      doub N N 389 
THR C     OXT    sing N N 390 
THR CB    OG1    sing N N 391 
THR CB    CG2    sing N N 392 
THR CB    HB     sing N N 393 
THR OG1   HG1    sing N N 394 
THR CG2   HG21   sing N N 395 
THR CG2   HG22   sing N N 396 
THR CG2   HG23   sing N N 397 
THR OXT   HXT    sing N N 398 
TRP N     CA     sing N N 399 
TRP N     H      sing N N 400 
TRP N     H2     sing N N 401 
TRP CA    C      sing N N 402 
TRP CA    CB     sing N N 403 
TRP CA    HA     sing N N 404 
TRP C     O      doub N N 405 
TRP C     OXT    sing N N 406 
TRP CB    CG     sing N N 407 
TRP CB    HB2    sing N N 408 
TRP CB    HB3    sing N N 409 
TRP CG    CD1    doub Y N 410 
TRP CG    CD2    sing Y N 411 
TRP CD1   NE1    sing Y N 412 
TRP CD1   HD1    sing N N 413 
TRP CD2   CE2    doub Y N 414 
TRP CD2   CE3    sing Y N 415 
TRP NE1   CE2    sing Y N 416 
TRP NE1   HE1    sing N N 417 
TRP CE2   CZ2    sing Y N 418 
TRP CE3   CZ3    doub Y N 419 
TRP CE3   HE3    sing N N 420 
TRP CZ2   CH2    doub Y N 421 
TRP CZ2   HZ2    sing N N 422 
TRP CZ3   CH2    sing Y N 423 
TRP CZ3   HZ3    sing N N 424 
TRP CH2   HH2    sing N N 425 
TRP OXT   HXT    sing N N 426 
TYR N     CA     sing N N 427 
TYR N     H      sing N N 428 
TYR N     H2     sing N N 429 
TYR CA    C      sing N N 430 
TYR CA    CB     sing N N 431 
TYR CA    HA     sing N N 432 
TYR C     O      doub N N 433 
TYR C     OXT    sing N N 434 
TYR CB    CG     sing N N 435 
TYR CB    HB2    sing N N 436 
TYR CB    HB3    sing N N 437 
TYR CG    CD1    doub Y N 438 
TYR CG    CD2    sing Y N 439 
TYR CD1   CE1    sing Y N 440 
TYR CD1   HD1    sing N N 441 
TYR CD2   CE2    doub Y N 442 
TYR CD2   HD2    sing N N 443 
TYR CE1   CZ     doub Y N 444 
TYR CE1   HE1    sing N N 445 
TYR CE2   CZ     sing Y N 446 
TYR CE2   HE2    sing N N 447 
TYR CZ    OH     sing N N 448 
TYR OH    HH     sing N N 449 
TYR OXT   HXT    sing N N 450 
VAL N     CA     sing N N 451 
VAL N     H      sing N N 452 
VAL N     H2     sing N N 453 
VAL CA    C      sing N N 454 
VAL CA    CB     sing N N 455 
VAL CA    HA     sing N N 456 
VAL C     O      doub N N 457 
VAL C     OXT    sing N N 458 
VAL CB    CG1    sing N N 459 
VAL CB    CG2    sing N N 460 
VAL CB    HB     sing N N 461 
VAL CG1   HG11   sing N N 462 
VAL CG1   HG12   sing N N 463 
VAL CG1   HG13   sing N N 464 
VAL CG2   HG21   sing N N 465 
VAL CG2   HG22   sing N N 466 
VAL CG2   HG23   sing N N 467 
VAL OXT   HXT    sing N N 468 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BM0 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-2 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                    9BM0 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . MET A 1 1457 ? 147.803 235.544 165.608 1.00 115.87 ? 1457 MET A N     1 
ATOM   2     C  CA    . MET A 1 1457 ? 146.404 235.889 165.387 1.00 117.40 ? 1457 MET A CA    1 
ATOM   3     C  C     . MET A 1 1457 ? 145.829 235.109 164.210 1.00 117.97 ? 1457 MET A C     1 
ATOM   4     O  O     . MET A 1 1457 ? 144.612 234.997 164.062 1.00 113.93 ? 1457 MET A O     1 
ATOM   5     C  CB    . MET A 1 1457 ? 146.253 237.393 165.154 1.00 117.51 ? 1457 MET A CB    1 
ATOM   6     C  CG    . MET A 1 1457 ? 146.717 238.247 166.325 1.00 116.97 ? 1457 MET A CG    1 
ATOM   7     S  SD    . MET A 1 1457 ? 148.434 238.777 166.181 1.00 116.98 ? 1457 MET A SD    1 
ATOM   8     C  CE    . MET A 1 1457 ? 148.729 239.415 167.829 1.00 105.96 ? 1457 MET A CE    1 
ATOM   9     N  N     . ALA A 1 1458 ? 146.717 234.567 163.372 1.00 119.26 ? 1458 ALA A N     1 
ATOM   10    C  CA    . ALA A 1 1458 ? 146.273 233.699 162.288 1.00 113.61 ? 1458 ALA A CA    1 
ATOM   11    C  C     . ALA A 1 1458 ? 145.687 232.399 162.823 1.00 113.74 ? 1458 ALA A C     1 
ATOM   12    O  O     . ALA A 1 1458 ? 144.988 231.686 162.094 1.00 114.51 ? 1458 ALA A O     1 
ATOM   13    C  CB    . ALA A 1 1458 ? 147.432 233.409 161.334 1.00 105.70 ? 1458 ALA A CB    1 
ATOM   14    N  N     . LEU A 1 1459 ? 145.964 232.076 164.089 1.00 112.77 ? 1459 LEU A N     1 
ATOM   15    C  CA    . LEU A 1 1459 ? 145.404 230.875 164.699 1.00 111.24 ? 1459 LEU A CA    1 
ATOM   16    C  C     . LEU A 1 1459 ? 143.882 230.935 164.734 1.00 113.05 ? 1459 LEU A C     1 
ATOM   17    O  O     . LEU A 1 1459 ? 143.206 229.935 164.465 1.00 112.12 ? 1459 LEU A O     1 
ATOM   18    C  CB    . LEU A 1 1459 ? 145.963 230.702 166.112 1.00 109.42 ? 1459 LEU A CB    1 
ATOM   19    C  CG    . LEU A 1 1459 ? 147.395 230.189 166.277 1.00 110.23 ? 1459 LEU A CG    1 
ATOM   20    C  CD1   . LEU A 1 1459 ? 148.394 231.320 166.109 1.00 111.35 ? 1459 LEU A CD1   1 
ATOM   21    C  CD2   . LEU A 1 1459 ? 147.568 229.540 167.640 1.00 110.07 ? 1459 LEU A CD2   1 
ATOM   22    N  N     . GLU A 1 1460 ? 143.328 232.103 165.070 1.00 111.99 ? 1460 GLU A N     1 
ATOM   23    C  CA    . GLU A 1 1460 ? 141.878 232.244 165.164 1.00 108.94 ? 1460 GLU A CA    1 
ATOM   24    C  C     . GLU A 1 1460 ? 141.208 232.037 163.810 1.00 110.24 ? 1460 GLU A C     1 
ATOM   25    O  O     . GLU A 1 1460 ? 140.151 231.400 163.724 1.00 107.13 ? 1460 GLU A O     1 
ATOM   26    C  CB    . GLU A 1 1460 ? 141.528 233.618 165.736 1.00 105.40 ? 1460 GLU A CB    1 
ATOM   27    C  CG    . GLU A 1 1460 ? 140.043 233.862 165.934 1.00 106.57 ? 1460 GLU A CG    1 
ATOM   28    C  CD    . GLU A 1 1460 ? 139.744 235.286 166.360 1.00 108.56 ? 1460 GLU A CD    1 
ATOM   29    O  OE1   . GLU A 1 1460 ? 139.993 236.212 165.559 1.00 107.61 ? 1460 GLU A OE1   1 
ATOM   30    O  OE2   . GLU A 1 1460 ? 139.268 235.480 167.498 1.00 105.06 ? 1460 GLU A OE2   1 
ATOM   31    N  N     . GLU A 1 1461 ? 141.804 232.573 162.741 1.00 112.38 ? 1461 GLU A N     1 
ATOM   32    C  CA    . GLU A 1 1461 ? 141.229 232.400 161.411 1.00 109.89 ? 1461 GLU A CA    1 
ATOM   33    C  C     . GLU A 1 1461 ? 141.218 230.933 160.998 1.00 107.33 ? 1461 GLU A C     1 
ATOM   34    O  O     . GLU A 1 1461 ? 140.239 230.453 160.416 1.00 107.18 ? 1461 GLU A O     1 
ATOM   35    C  CB    . GLU A 1 1461 ? 141.994 233.242 160.389 1.00 110.74 ? 1461 GLU A CB    1 
ATOM   36    C  CG    . GLU A 1 1461 ? 142.253 234.680 160.818 1.00 112.79 ? 1461 GLU A CG    1 
ATOM   37    C  CD    . GLU A 1 1461 ? 141.074 235.299 161.547 1.00 113.61 ? 1461 GLU A CD    1 
ATOM   38    O  OE1   . GLU A 1 1461 ? 139.977 235.374 160.954 1.00 111.97 ? 1461 GLU A OE1   1 
ATOM   39    O  OE2   . GLU A 1 1461 ? 141.245 235.710 162.714 1.00 113.09 ? 1461 GLU A OE2   1 
ATOM   40    N  N     . PHE A 1 1462 ? 142.299 230.205 161.291 1.00 108.46 ? 1462 PHE A N     1 
ATOM   41    C  CA    . PHE A 1 1462 ? 142.333 228.778 160.981 1.00 106.40 ? 1462 PHE A CA    1 
ATOM   42    C  C     . PHE A 1 1462 ? 141.261 228.021 161.754 1.00 105.14 ? 1462 PHE A C     1 
ATOM   43    O  O     . PHE A 1 1462 ? 140.635 227.100 161.217 1.00 103.49 ? 1462 PHE A O     1 
ATOM   44    C  CB    . PHE A 1 1462 ? 143.720 228.205 161.276 1.00 101.33 ? 1462 PHE A CB    1 
ATOM   45    C  CG    . PHE A 1 1462 ? 144.713 228.413 160.167 1.00 104.89 ? 1462 PHE A CG    1 
ATOM   46    C  CD1   . PHE A 1 1462 ? 145.028 229.687 159.726 1.00 106.94 ? 1462 PHE A CD1   1 
ATOM   47    C  CD2   . PHE A 1 1462 ? 145.331 227.330 159.564 1.00 103.13 ? 1462 PHE A CD2   1 
ATOM   48    C  CE1   . PHE A 1 1462 ? 145.940 229.879 158.705 1.00 103.59 ? 1462 PHE A CE1   1 
ATOM   49    C  CE2   . PHE A 1 1462 ? 146.244 227.514 158.542 1.00 101.14 ? 1462 PHE A CE2   1 
ATOM   50    C  CZ    . PHE A 1 1462 ? 146.549 228.790 158.112 1.00 99.17  ? 1462 PHE A CZ    1 
ATOM   51    N  N     . LEU A 1 1463 ? 141.040 228.392 163.017 1.00 104.04 ? 1463 LEU A N     1 
ATOM   52    C  CA    . LEU A 1 1463 ? 139.942 227.802 163.775 1.00 102.78 ? 1463 LEU A CA    1 
ATOM   53    C  C     . LEU A 1 1463 ? 138.597 228.154 163.154 1.00 101.53 ? 1463 LEU A C     1 
ATOM   54    O  O     . LEU A 1 1463 ? 137.697 227.309 163.083 1.00 102.09 ? 1463 LEU A O     1 
ATOM   55    C  CB    . LEU A 1 1463 ? 140.001 228.266 165.231 1.00 102.67 ? 1463 LEU A CB    1 
ATOM   56    C  CG    . LEU A 1 1463 ? 141.133 227.690 166.084 1.00 103.05 ? 1463 LEU A CG    1 
ATOM   57    C  CD1   . LEU A 1 1463 ? 140.773 227.748 167.559 1.00 96.71  ? 1463 LEU A CD1   1 
ATOM   58    C  CD2   . LEU A 1 1463 ? 141.449 226.262 165.665 1.00 96.48  ? 1463 LEU A CD2   1 
ATOM   59    N  N     . LYS A 1 1464 ? 138.440 229.401 162.703 1.00 101.66 ? 1464 LYS A N     1 
ATOM   60    C  CA    . LYS A 1 1464 ? 137.200 229.796 162.044 1.00 100.87 ? 1464 LYS A CA    1 
ATOM   61    C  C     . LYS A 1 1464 ? 137.025 229.067 160.718 1.00 101.94 ? 1464 LYS A C     1 
ATOM   62    O  O     . LYS A 1 1464 ? 135.908 228.674 160.360 1.00 100.04 ? 1464 LYS A O     1 
ATOM   63    C  CB    . LYS A 1 1464 ? 137.174 231.310 161.836 1.00 100.34 ? 1464 LYS A CB    1 
ATOM   64    C  CG    . LYS A 1 1464 ? 135.822 231.851 161.400 1.00 98.85  ? 1464 LYS A CG    1 
ATOM   65    C  CD    . LYS A 1 1464 ? 134.702 231.295 162.266 1.00 98.01  ? 1464 LYS A CD    1 
ATOM   66    C  CE    . LYS A 1 1464 ? 133.337 231.692 161.728 1.00 98.23  ? 1464 LYS A CE    1 
ATOM   67    N  NZ    . LYS A 1 1464 ? 132.232 231.002 162.450 1.00 97.07  ? 1464 LYS A NZ    1 
ATOM   68    N  N     . GLN A 1 1465 ? 138.116 228.886 159.968 1.00 103.07 ? 1465 GLN A N     1 
ATOM   69    C  CA    . GLN A 1 1465 ? 138.042 228.134 158.719 1.00 100.08 ? 1465 GLN A CA    1 
ATOM   70    C  C     . GLN A 1 1465 ? 137.600 226.698 158.970 1.00 97.99  ? 1465 GLN A C     1 
ATOM   71    O  O     . GLN A 1 1465 ? 136.705 226.184 158.290 1.00 95.34  ? 1465 GLN A O     1 
ATOM   72    C  CB    . GLN A 1 1465 ? 139.394 228.158 158.004 1.00 96.69  ? 1465 GLN A CB    1 
ATOM   73    C  CG    . GLN A 1 1465 ? 139.787 229.509 157.435 1.00 99.77  ? 1465 GLN A CG    1 
ATOM   74    C  CD    . GLN A 1 1465 ? 141.268 229.594 157.122 1.00 101.71 ? 1465 GLN A CD    1 
ATOM   75    O  OE1   . GLN A 1 1465 ? 141.961 230.501 157.582 1.00 103.96 ? 1465 GLN A OE1   1 
ATOM   76    N  NE2   . GLN A 1 1465 ? 141.762 228.643 156.337 1.00 92.00  ? 1465 GLN A NE2   1 
ATOM   77    N  N     . ILE A 1 1466 ? 138.215 226.038 159.954 1.00 96.75  ? 1466 ILE A N     1 
ATOM   78    C  CA    . ILE A 1 1466 ? 137.846 224.662 160.276 1.00 92.89  ? 1466 ILE A CA    1 
ATOM   79    C  C     . ILE A 1 1466 ? 136.401 224.597 160.752 1.00 95.13  ? 1466 ILE A C     1 
ATOM   80    O  O     . ILE A 1 1466 ? 135.658 223.669 160.409 1.00 94.42  ? 1466 ILE A O     1 
ATOM   81    C  CB    . ILE A 1 1466 ? 138.821 224.082 161.319 1.00 90.25  ? 1466 ILE A CB    1 
ATOM   82    C  CG1   . ILE A 1 1466 ? 140.203 223.878 160.695 1.00 90.21  ? 1466 ILE A CG1   1 
ATOM   83    C  CG2   . ILE A 1 1466 ? 138.293 222.775 161.891 1.00 86.27  ? 1466 ILE A CG2   1 
ATOM   84    C  CD1   . ILE A 1 1466 ? 141.325 223.796 161.705 1.00 85.38  ? 1466 ILE A CD1   1 
ATOM   85    N  N     . ARG A 1 1467 ? 135.977 225.585 161.545 1.00 96.88  ? 1467 ARG A N     1 
ATOM   86    C  CA    . ARG A 1 1467 ? 134.591 225.627 161.999 1.00 95.75  ? 1467 ARG A CA    1 
ATOM   87    C  C     . ARG A 1 1467 ? 133.628 225.763 160.826 1.00 95.97  ? 1467 ARG A C     1 
ATOM   88    O  O     . ARG A 1 1467 ? 132.590 225.093 160.785 1.00 95.19  ? 1467 ARG A O     1 
ATOM   89    C  CB    . ARG A 1 1467 ? 134.402 226.779 162.986 1.00 96.33  ? 1467 ARG A CB    1 
ATOM   90    C  CG    . ARG A 1 1467 ? 132.960 227.005 163.417 1.00 95.55  ? 1467 ARG A CG    1 
ATOM   91    C  CD    . ARG A 1 1467 ? 132.781 228.008 164.574 1.00 90.73  ? 1467 ARG A CD    1 
ATOM   92    N  NE    . ARG A 1 1467 ? 133.628 227.772 165.740 1.00 92.63  ? 1467 ARG A NE    1 
ATOM   93    C  CZ    . ARG A 1 1467 ? 134.881 228.188 165.877 1.00 96.75  ? 1467 ARG A CZ    1 
ATOM   94    N  NH1   . ARG A 1 1467 ? 135.466 228.942 164.960 1.00 97.88  ? 1467 ARG A NH1   1 
ATOM   95    N  NH2   . ARG A 1 1467 ? 135.558 227.857 166.973 1.00 97.04  ? 1467 ARG A NH2   1 
ATOM   96    N  N     . GLU A 1 1468 ? 133.957 226.624 159.860 1.00 97.36  ? 1468 GLU A N     1 
ATOM   97    C  CA    . GLU A 1 1468 ? 133.082 226.810 158.706 1.00 96.53  ? 1468 GLU A CA    1 
ATOM   98    C  C     . GLU A 1 1468 ? 133.025 225.558 157.841 1.00 94.16  ? 1468 GLU A C     1 
ATOM   99    O  O     . GLU A 1 1468 ? 131.966 225.223 157.295 1.00 92.37  ? 1468 GLU A O     1 
ATOM   100   C  CB    . GLU A 1 1468 ? 133.543 228.013 157.883 1.00 95.95  ? 1468 GLU A CB    1 
ATOM   101   C  CG    . GLU A 1 1468 ? 133.253 229.359 158.532 1.00 101.55 ? 1468 GLU A CG    1 
ATOM   102   C  CD    . GLU A 1 1468 ? 131.779 229.725 158.493 1.00 102.64 ? 1468 GLU A CD    1 
ATOM   103   O  OE1   . GLU A 1 1468 ? 131.012 229.056 157.769 1.00 101.60 ? 1468 GLU A OE1   1 
ATOM   104   O  OE2   . GLU A 1 1468 ? 131.387 230.685 159.190 1.00 102.11 ? 1468 GLU A OE2   1 
ATOM   105   N  N     . VAL A 1 1469 ? 134.153 224.858 157.692 1.00 94.14  ? 1469 VAL A N     1 
ATOM   106   C  CA    . VAL A 1 1469 ? 134.165 223.635 156.892 1.00 90.52  ? 1469 VAL A CA    1 
ATOM   107   C  C     . VAL A 1 1469 ? 133.257 222.580 157.509 1.00 88.09  ? 1469 VAL A C     1 
ATOM   108   O  O     . VAL A 1 1469 ? 132.453 221.949 156.813 1.00 90.60  ? 1469 VAL A O     1 
ATOM   109   C  CB    . VAL A 1 1469 ? 135.605 223.114 156.724 1.00 86.88  ? 1469 VAL A CB    1 
ATOM   110   C  CG1   . VAL A 1 1469 ? 135.601 221.773 156.011 1.00 82.02  ? 1469 VAL A CG1   1 
ATOM   111   C  CG2   . VAL A 1 1469 ? 136.441 224.114 155.946 1.00 88.38  ? 1469 VAL A CG2   1 
ATOM   112   N  N     . TRP A 1 1470 ? 133.356 222.382 158.825 1.00 88.54  ? 1470 TRP A N     1 
ATOM   113   C  CA    . TRP A 1 1470 ? 132.575 221.329 159.464 1.00 86.89  ? 1470 TRP A CA    1 
ATOM   114   C  C     . TRP A 1 1470 ? 131.109 221.717 159.609 1.00 89.03  ? 1470 TRP A C     1 
ATOM   115   O  O     . TRP A 1 1470 ? 130.242 220.839 159.674 1.00 89.19  ? 1470 TRP A O     1 
ATOM   116   C  CB    . TRP A 1 1470 ? 133.178 220.980 160.824 1.00 81.22  ? 1470 TRP A CB    1 
ATOM   117   C  CG    . TRP A 1 1470 ? 134.440 220.175 160.716 1.00 81.38  ? 1470 TRP A CG    1 
ATOM   118   C  CD1   . TRP A 1 1470 ? 135.657 220.490 161.244 1.00 83.83  ? 1470 TRP A CD1   1 
ATOM   119   C  CD2   . TRP A 1 1470 ? 134.612 218.929 160.027 1.00 79.46  ? 1470 TRP A CD2   1 
ATOM   120   N  NE1   . TRP A 1 1470 ? 136.575 219.518 160.932 1.00 81.49  ? 1470 TRP A NE1   1 
ATOM   121   C  CE2   . TRP A 1 1470 ? 135.959 218.548 160.186 1.00 76.67  ? 1470 TRP A CE2   1 
ATOM   122   C  CE3   . TRP A 1 1470 ? 133.758 218.098 159.296 1.00 78.72  ? 1470 TRP A CE3   1 
ATOM   123   C  CZ2   . TRP A 1 1470 ? 136.471 217.374 159.640 1.00 75.34  ? 1470 TRP A CZ2   1 
ATOM   124   C  CZ3   . TRP A 1 1470 ? 134.268 216.934 158.755 1.00 75.58  ? 1470 TRP A CZ3   1 
ATOM   125   C  CH2   . TRP A 1 1470 ? 135.612 216.583 158.930 1.00 74.40  ? 1470 TRP A CH2   1 
ATOM   126   N  N     . ASN A 1 1471 ? 130.810 223.017 159.662 1.00 92.40  ? 1471 ASN A N     1 
ATOM   127   C  CA    . ASN A 1 1471 ? 129.415 223.443 159.684 1.00 92.27  ? 1471 ASN A CA    1 
ATOM   128   C  C     . ASN A 1 1471 ? 128.764 223.299 158.315 1.00 87.42  ? 1471 ASN A C     1 
ATOM   129   O  O     . ASN A 1 1471 ? 127.533 223.257 158.216 1.00 83.28  ? 1471 ASN A O     1 
ATOM   130   C  CB    . ASN A 1 1471 ? 129.308 224.888 160.174 1.00 91.59  ? 1471 ASN A CB    1 
ATOM   131   C  CG    . ASN A 1 1471 ? 129.693 225.040 161.633 1.00 94.69  ? 1471 ASN A CG    1 
ATOM   132   O  OD1   . ASN A 1 1471 ? 130.131 224.084 162.274 1.00 93.35  ? 1471 ASN A OD1   1 
ATOM   133   N  ND2   . ASN A 1 1471 ? 129.529 226.245 162.166 1.00 93.81  ? 1471 ASN A ND2   1 
ATOM   134   N  N     . THR A 1 1472 ? 129.567 223.225 157.253 1.00 87.75  ? 1472 THR A N     1 
ATOM   135   C  CA    . THR A 1 1472 ? 129.058 223.066 155.899 1.00 87.62  ? 1472 THR A CA    1 
ATOM   136   C  C     . THR A 1 1472 ? 129.294 221.674 155.328 1.00 84.89  ? 1472 THR A C     1 
ATOM   137   O  O     . THR A 1 1472 ? 128.629 221.303 154.354 1.00 81.77  ? 1472 THR A O     1 
ATOM   138   C  CB    . THR A 1 1472 ? 129.692 224.106 154.966 1.00 88.73  ? 1472 THR A CB    1 
ATOM   139   O  OG1   . THR A 1 1472 ? 131.120 224.014 155.044 1.00 91.46  ? 1472 THR A OG1   1 
ATOM   140   C  CG2   . THR A 1 1472 ? 129.256 225.510 155.359 1.00 86.24  ? 1472 THR A CG2   1 
ATOM   141   N  N     . TYR A 1 1473 ? 130.219 220.904 155.897 1.00 84.89  ? 1473 TYR A N     1 
ATOM   142   C  CA    . TYR A 1 1473 ? 130.488 219.562 155.398 1.00 78.97  ? 1473 TYR A CA    1 
ATOM   143   C  C     . TYR A 1 1473 ? 129.291 218.656 155.655 1.00 79.98  ? 1473 TYR A C     1 
ATOM   144   O  O     . TYR A 1 1473 ? 128.712 218.666 156.745 1.00 80.01  ? 1473 TYR A O     1 
ATOM   145   C  CB    . TYR A 1 1473 ? 131.738 218.986 156.063 1.00 77.31  ? 1473 TYR A CB    1 
ATOM   146   C  CG    . TYR A 1 1473 ? 132.435 217.912 155.256 1.00 75.00  ? 1473 TYR A CG    1 
ATOM   147   C  CD1   . TYR A 1 1473 ? 131.867 216.656 155.095 1.00 73.82  ? 1473 TYR A CD1   1 
ATOM   148   C  CD2   . TYR A 1 1473 ? 133.666 218.154 154.659 1.00 75.66  ? 1473 TYR A CD2   1 
ATOM   149   C  CE1   . TYR A 1 1473 ? 132.501 215.674 154.359 1.00 71.99  ? 1473 TYR A CE1   1 
ATOM   150   C  CE2   . TYR A 1 1473 ? 134.308 217.177 153.922 1.00 72.59  ? 1473 TYR A CE2   1 
ATOM   151   C  CZ    . TYR A 1 1473 ? 133.721 215.939 153.776 1.00 68.78  ? 1473 TYR A CZ    1 
ATOM   152   O  OH    . TYR A 1 1473 ? 134.356 214.961 153.044 1.00 55.18  ? 1473 TYR A OH    1 
ATOM   153   N  N     . GLU A 1 1474 ? 128.918 217.876 154.644 1.00 78.98  ? 1474 GLU A N     1 
ATOM   154   C  CA    . GLU A 1 1474 ? 127.836 216.913 154.754 1.00 75.72  ? 1474 GLU A CA    1 
ATOM   155   C  C     . GLU A 1 1474 ? 128.292 215.577 154.190 1.00 73.06  ? 1474 GLU A C     1 
ATOM   156   O  O     . GLU A 1 1474 ? 129.121 215.521 153.276 1.00 69.42  ? 1474 GLU A O     1 
ATOM   157   C  CB    . GLU A 1 1474 ? 126.577 217.391 154.019 1.00 74.98  ? 1474 GLU A CB    1 
ATOM   158   C  CG    . GLU A 1 1474 ? 125.783 218.443 154.775 1.00 81.67  ? 1474 GLU A CG    1 
ATOM   159   C  CD    . GLU A 1 1474 ? 124.457 218.759 154.113 1.00 83.75  ? 1474 GLU A CD    1 
ATOM   160   O  OE1   . GLU A 1 1474 ? 124.210 218.247 153.001 1.00 84.08  ? 1474 GLU A OE1   1 
ATOM   161   O  OE2   . GLU A 1 1474 ? 123.661 219.517 154.705 1.00 84.82  ? 1474 GLU A OE2   1 
ATOM   162   N  N     . LEU A 1 1475 ? 127.748 214.499 154.747 1.00 73.28  ? 1475 LEU A N     1 
ATOM   163   C  CA    . LEU A 1 1475 ? 128.077 213.162 154.272 1.00 64.83  ? 1475 LEU A CA    1 
ATOM   164   C  C     . LEU A 1 1475 ? 127.489 212.958 152.882 1.00 65.14  ? 1475 LEU A C     1 
ATOM   165   O  O     . LEU A 1 1475 ? 126.275 213.083 152.689 1.00 68.74  ? 1475 LEU A O     1 
ATOM   166   C  CB    . LEU A 1 1475 ? 127.546 212.110 155.241 1.00 61.61  ? 1475 LEU A CB    1 
ATOM   167   C  CG    . LEU A 1 1475 ? 128.332 211.911 156.539 1.00 59.57  ? 1475 LEU A CG    1 
ATOM   168   C  CD1   . LEU A 1 1475 ? 127.533 211.077 157.528 1.00 61.81  ? 1475 LEU A CD1   1 
ATOM   169   C  CD2   . LEU A 1 1475 ? 129.682 211.271 156.262 1.00 56.19  ? 1475 LEU A CD2   1 
ATOM   170   N  N     . ASP A 1 1476 ? 128.346 212.646 151.913 1.00 62.83  ? 1476 ASP A N     1 
ATOM   171   C  CA    . ASP A 1 1476 ? 127.893 212.408 150.546 1.00 63.15  ? 1476 ASP A CA    1 
ATOM   172   C  C     . ASP A 1 1476 ? 127.130 211.091 150.500 1.00 60.25  ? 1476 ASP A C     1 
ATOM   173   O  O     . ASP A 1 1476 ? 127.715 210.017 150.675 1.00 58.55  ? 1476 ASP A O     1 
ATOM   174   C  CB    . ASP A 1 1476 ? 129.080 212.392 149.589 1.00 63.65  ? 1476 ASP A CB    1 
ATOM   175   C  CG    . ASP A 1 1476 ? 128.666 212.596 148.145 1.00 67.37  ? 1476 ASP A CG    1 
ATOM   176   O  OD1   . ASP A 1 1476 ? 127.493 212.949 147.905 1.00 67.14  ? 1476 ASP A OD1   1 
ATOM   177   O  OD2   . ASP A 1 1476 ? 129.515 212.403 147.249 1.00 67.75  ? 1476 ASP A OD2   1 
ATOM   178   N  N     . LEU A 1 1477 ? 125.824 211.170 150.265 1.00 56.95  ? 1477 LEU A N     1 
ATOM   179   C  CA    . LEU A 1 1477 ? 124.943 210.013 150.307 1.00 61.62  ? 1477 LEU A CA    1 
ATOM   180   C  C     . LEU A 1 1477 ? 124.493 209.643 148.901 1.00 65.37  ? 1477 LEU A C     1 
ATOM   181   O  O     . LEU A 1 1477 ? 124.049 210.502 148.133 1.00 65.02  ? 1477 LEU A O     1 
ATOM   182   C  CB    . LEU A 1 1477 ? 123.722 210.286 151.191 1.00 58.71  ? 1477 LEU A CB    1 
ATOM   183   C  CG    . LEU A 1 1477 ? 123.947 210.438 152.700 1.00 59.16  ? 1477 LEU A CG    1 
ATOM   184   C  CD1   . LEU A 1 1477 ? 122.757 209.897 153.474 1.00 63.50  ? 1477 LEU A CD1   1 
ATOM   185   C  CD2   . LEU A 1 1477 ? 125.225 209.741 153.146 1.00 56.85  ? 1477 LEU A CD2   1 
ATOM   186   N  N     . VAL A 1 1478 ? 124.612 208.360 148.570 1.00 64.10  ? 1478 VAL A N     1 
ATOM   187   C  CA    . VAL A 1 1478 ? 124.167 207.826 147.290 1.00 63.35  ? 1478 VAL A CA    1 
ATOM   188   C  C     . VAL A 1 1478 ? 123.226 206.659 147.559 1.00 64.81  ? 1478 VAL A C     1 
ATOM   189   O  O     . VAL A 1 1478 ? 123.442 205.875 148.490 1.00 65.59  ? 1478 VAL A O     1 
ATOM   190   C  CB    . VAL A 1 1478 ? 125.356 207.399 146.398 1.00 62.93  ? 1478 VAL A CB    1 
ATOM   191   C  CG1   . VAL A 1 1478 ? 126.082 206.192 146.980 1.00 60.35  ? 1478 VAL A CG1   1 
ATOM   192   C  CG2   . VAL A 1 1478 ? 124.884 207.113 144.980 1.00 63.87  ? 1478 VAL A CG2   1 
ATOM   193   N  N     . ASN A 1 1479 ? 122.162 206.569 146.766 1.00 64.73  ? 1479 ASN A N     1 
ATOM   194   C  CA    . ASN A 1 1479 ? 121.170 205.524 146.964 1.00 67.21  ? 1479 ASN A CA    1 
ATOM   195   C  C     . ASN A 1 1479 ? 121.754 204.152 146.643 1.00 66.90  ? 1479 ASN A C     1 
ATOM   196   O  O     . ASN A 1 1479 ? 122.664 204.012 145.821 1.00 67.33  ? 1479 ASN A O     1 
ATOM   197   C  CB    . ASN A 1 1479 ? 119.932 205.792 146.105 1.00 65.52  ? 1479 ASN A CB    1 
ATOM   198   C  CG    . ASN A 1 1479 ? 120.097 205.320 144.673 1.00 70.35  ? 1479 ASN A CG    1 
ATOM   199   O  OD1   . ASN A 1 1479 ? 121.131 205.548 144.045 1.00 68.61  ? 1479 ASN A OD1   1 
ATOM   200   N  ND2   . ASN A 1 1479 ? 119.072 204.658 144.149 1.00 69.95  ? 1479 ASN A ND2   1 
ATOM   201   N  N     . TYR A 1 1480 ? 121.225 203.131 147.316 1.00 64.53  ? 1480 TYR A N     1 
ATOM   202   C  CA    . TYR A 1 1480 ? 121.687 201.751 147.166 1.00 63.86  ? 1480 TYR A CA    1 
ATOM   203   C  C     . TYR A 1 1480 ? 120.461 200.870 146.941 1.00 66.90  ? 1480 TYR A C     1 
ATOM   204   O  O     . TYR A 1 1480 ? 119.843 200.398 147.899 1.00 65.24  ? 1480 TYR A O     1 
ATOM   205   C  CB    . TYR A 1 1480 ? 122.498 201.308 148.384 1.00 58.13  ? 1480 TYR A CB    1 
ATOM   206   C  CG    . TYR A 1 1480 ? 122.904 199.850 148.367 1.00 55.64  ? 1480 TYR A CG    1 
ATOM   207   C  CD1   . TYR A 1 1480 ? 122.222 198.909 149.127 1.00 59.52  ? 1480 TYR A CD1   1 
ATOM   208   C  CD2   . TYR A 1 1480 ? 123.967 199.413 147.588 1.00 46.96  ? 1480 TYR A CD2   1 
ATOM   209   C  CE1   . TYR A 1 1480 ? 122.588 197.577 149.115 1.00 55.32  ? 1480 TYR A CE1   1 
ATOM   210   C  CE2   . TYR A 1 1480 ? 124.340 198.083 147.570 1.00 48.13  ? 1480 TYR A CE2   1 
ATOM   211   C  CZ    . TYR A 1 1480 ? 123.647 197.170 148.334 1.00 53.22  ? 1480 TYR A CZ    1 
ATOM   212   O  OH    . TYR A 1 1480 ? 124.014 195.844 148.319 1.00 51.02  ? 1480 TYR A OH    1 
ATOM   213   N  N     . GLN A 1 1481 ? 120.111 200.669 145.668 1.00 65.84  ? 1481 GLN A N     1 
ATOM   214   C  CA    . GLN A 1 1481 ? 119.032 199.763 145.270 1.00 65.38  ? 1481 GLN A CA    1 
ATOM   215   C  C     . GLN A 1 1481 ? 117.707 200.136 145.932 1.00 68.60  ? 1481 GLN A C     1 
ATOM   216   O  O     . GLN A 1 1481 ? 116.903 199.270 146.285 1.00 69.50  ? 1481 GLN A O     1 
ATOM   217   C  CB    . GLN A 1 1481 ? 119.401 198.308 145.569 1.00 67.47  ? 1481 GLN A CB    1 
ATOM   218   C  CG    . GLN A 1 1481 ? 120.772 197.907 145.050 1.00 62.62  ? 1481 GLN A CG    1 
ATOM   219   C  CD    . GLN A 1 1481 ? 121.228 196.561 145.576 1.00 62.53  ? 1481 GLN A CD    1 
ATOM   220   O  OE1   . GLN A 1 1481 ? 120.523 195.912 146.347 1.00 61.40  ? 1481 GLN A OE1   1 
ATOM   221   N  NE2   . GLN A 1 1481 ? 122.416 196.137 145.162 1.00 57.22  ? 1481 GLN A NE2   1 
ATOM   222   N  N     . ASN A 1 1482 ? 117.481 201.442 146.102 1.00 65.31  ? 1482 ASN A N     1 
ATOM   223   C  CA    . ASN A 1 1482 ? 116.250 201.973 146.691 1.00 67.44  ? 1482 ASN A CA    1 
ATOM   224   C  C     . ASN A 1 1482 ? 115.991 201.407 148.084 1.00 66.81  ? 1482 ASN A C     1 
ATOM   225   O  O     . ASN A 1 1482 ? 114.840 201.235 148.493 1.00 68.59  ? 1482 ASN A O     1 
ATOM   226   C  CB    . ASN A 1 1482 ? 115.043 201.722 145.782 1.00 66.97  ? 1482 ASN A CB    1 
ATOM   227   C  CG    . ASN A 1 1482 ? 115.357 201.957 144.319 1.00 66.46  ? 1482 ASN A CG    1 
ATOM   228   O  OD1   . ASN A 1 1482 ? 115.660 203.077 143.909 1.00 63.05  ? 1482 ASN A OD1   1 
ATOM   229   N  ND2   . ASN A 1 1482 ? 115.284 200.898 143.521 1.00 64.74  ? 1482 ASN A ND2   1 
ATOM   230   N  N     . LYS A 1 1483 ? 117.058 201.112 148.824 1.00 64.58  ? 1483 LYS A N     1 
ATOM   231   C  CA    . LYS A 1 1483 ? 116.948 200.592 150.181 1.00 64.69  ? 1483 LYS A CA    1 
ATOM   232   C  C     . LYS A 1 1483 ? 117.386 201.597 151.236 1.00 67.79  ? 1483 LYS A C     1 
ATOM   233   O  O     . LYS A 1 1483 ? 116.778 201.667 152.308 1.00 65.59  ? 1483 LYS A O     1 
ATOM   234   C  CB    . LYS A 1 1483 ? 117.774 199.310 150.325 1.00 65.85  ? 1483 LYS A CB    1 
ATOM   235   C  CG    . LYS A 1 1483 ? 117.372 198.206 149.362 1.00 66.94  ? 1483 LYS A CG    1 
ATOM   236   C  CD    . LYS A 1 1483 ? 118.478 197.176 149.204 1.00 66.62  ? 1483 LYS A CD    1 
ATOM   237   C  CE    . LYS A 1 1483 ? 118.001 195.974 148.404 1.00 68.94  ? 1483 LYS A CE    1 
ATOM   238   N  NZ    . LYS A 1 1483 ? 117.084 195.107 149.194 1.00 65.87  ? 1483 LYS A NZ    1 
ATOM   239   N  N     . CYS A 1 1484 ? 118.420 202.378 150.955 1.00 65.58  ? 1484 CYS A N     1 
ATOM   240   C  CA    . CYS A 1 1484 ? 118.932 203.388 151.877 1.00 57.00  ? 1484 CYS A CA    1 
ATOM   241   C  C     . CYS A 1 1484 ? 119.760 204.376 151.064 1.00 60.11  ? 1484 CYS A C     1 
ATOM   242   O  O     . CYS A 1 1484 ? 119.753 204.348 149.828 1.00 62.12  ? 1484 CYS A O     1 
ATOM   243   C  CB    . CYS A 1 1484 ? 119.755 202.754 152.999 1.00 60.67  ? 1484 CYS A CB    1 
ATOM   244   S  SG    . CYS A 1 1484 ? 120.680 201.282 152.503 1.00 72.56  ? 1484 CYS A SG    1 
ATOM   245   N  N     . ARG A 1 1485 ? 120.475 205.254 151.762 1.00 60.60  ? 1485 ARG A N     1 
ATOM   246   C  CA    . ARG A 1 1485 ? 121.421 206.183 151.150 1.00 61.35  ? 1485 ARG A CA    1 
ATOM   247   C  C     . ARG A 1 1485 ? 122.773 205.955 151.816 1.00 60.98  ? 1485 ARG A C     1 
ATOM   248   O  O     . ARG A 1 1485 ? 123.041 206.491 152.896 1.00 64.46  ? 1485 ARG A O     1 
ATOM   249   C  CB    . ARG A 1 1485 ? 120.958 207.628 151.301 1.00 64.23  ? 1485 ARG A CB    1 
ATOM   250   C  CG    . ARG A 1 1485 ? 119.634 207.933 150.626 1.00 63.49  ? 1485 ARG A CG    1 
ATOM   251   C  CD    . ARG A 1 1485 ? 119.843 208.813 149.405 1.00 67.20  ? 1485 ARG A CD    1 
ATOM   252   N  NE    . ARG A 1 1485 ? 120.533 210.053 149.738 1.00 71.00  ? 1485 ARG A NE    1 
ATOM   253   C  CZ    . ARG A 1 1485 ? 119.966 211.092 150.335 1.00 68.25  ? 1485 ARG A CZ    1 
ATOM   254   N  NH1   . ARG A 1 1485 ? 118.687 211.082 150.675 1.00 69.90  ? 1485 ARG A NH1   1 
ATOM   255   N  NH2   . ARG A 1 1485 ? 120.700 212.170 150.597 1.00 59.91  ? 1485 ARG A NH2   1 
ATOM   256   N  N     . LEU A 1 1486 ? 123.621 205.160 151.171 1.00 60.48  ? 1486 LEU A N     1 
ATOM   257   C  CA    . LEU A 1 1486 ? 124.906 204.793 151.743 1.00 53.89  ? 1486 LEU A CA    1 
ATOM   258   C  C     . LEU A 1 1486 ? 125.882 205.962 151.685 1.00 51.81  ? 1486 LEU A C     1 
ATOM   259   O  O     . LEU A 1 1486 ? 125.814 206.817 150.798 1.00 51.99  ? 1486 LEU A O     1 
ATOM   260   C  CB    . LEU A 1 1486 ? 125.490 203.590 151.004 1.00 53.11  ? 1486 LEU A CB    1 
ATOM   261   C  CG    . LEU A 1 1486 ? 124.790 202.255 151.257 1.00 52.30  ? 1486 LEU A CG    1 
ATOM   262   C  CD1   . LEU A 1 1486 ? 125.639 201.115 150.735 1.00 47.69  ? 1486 LEU A CD1   1 
ATOM   263   C  CD2   . LEU A 1 1486 ? 124.491 202.071 152.738 1.00 52.46  ? 1486 LEU A CD2   1 
ATOM   264   N  N     . ILE A 1 1487 ? 126.800 205.989 152.652 1.00 50.52  ? 1487 ILE A N     1 
ATOM   265   C  CA    . ILE A 1 1487 ? 127.806 207.040 152.702 1.00 50.57  ? 1487 ILE A CA    1 
ATOM   266   C  C     . ILE A 1 1487 ? 128.841 206.811 151.610 1.00 53.57  ? 1487 ILE A C     1 
ATOM   267   O  O     . ILE A 1 1487 ? 129.330 205.690 151.412 1.00 52.14  ? 1487 ILE A O     1 
ATOM   268   C  CB    . ILE A 1 1487 ? 128.463 207.090 154.092 1.00 43.44  ? 1487 ILE A CB    1 
ATOM   269   C  CG1   . ILE A 1 1487 ? 127.400 207.257 155.179 1.00 48.78  ? 1487 ILE A CG1   1 
ATOM   270   C  CG2   . ILE A 1 1487 ? 129.484 208.213 154.163 1.00 45.22  ? 1487 ILE A CG2   1 
ATOM   271   C  CD1   . ILE A 1 1487 ? 127.968 207.391 156.574 1.00 50.76  ? 1487 ILE A CD1   1 
ATOM   272   N  N     . ARG A 1 1488 ? 129.180 207.879 150.892 1.00 55.02  ? 1488 ARG A N     1 
ATOM   273   C  CA    . ARG A 1 1488 ? 130.136 207.825 149.798 1.00 52.96  ? 1488 ARG A CA    1 
ATOM   274   C  C     . ARG A 1 1488 ? 131.181 208.914 149.991 1.00 57.72  ? 1488 ARG A C     1 
ATOM   275   O  O     . ARG A 1 1488 ? 130.899 209.973 150.558 1.00 63.33  ? 1488 ARG A O     1 
ATOM   276   C  CB    . ARG A 1 1488 ? 129.437 207.996 148.439 1.00 57.19  ? 1488 ARG A CB    1 
ATOM   277   C  CG    . ARG A 1 1488 ? 130.346 207.823 147.234 1.00 60.56  ? 1488 ARG A CG    1 
ATOM   278   C  CD    . ARG A 1 1488 ? 129.574 207.973 145.935 1.00 65.02  ? 1488 ARG A CD    1 
ATOM   279   N  NE    . ARG A 1 1488 ? 128.831 209.227 145.887 1.00 68.10  ? 1488 ARG A NE    1 
ATOM   280   C  CZ    . ARG A 1 1488 ? 127.942 209.535 144.953 1.00 72.56  ? 1488 ARG A CZ    1 
ATOM   281   N  NH1   . ARG A 1 1488 ? 127.664 208.704 143.962 1.00 68.02  ? 1488 ARG A NH1   1 
ATOM   282   N  NH2   . ARG A 1 1488 ? 127.317 210.708 145.014 1.00 72.42  ? 1488 ARG A NH2   1 
ATOM   283   N  N     . GLY A 1 1489 ? 132.396 208.641 149.523 1.00 56.83  ? 1489 GLY A N     1 
ATOM   284   C  CA    . GLY A 1 1489 ? 133.473 209.606 149.627 1.00 54.59  ? 1489 GLY A CA    1 
ATOM   285   C  C     . GLY A 1 1489 ? 134.199 209.540 150.953 1.00 56.12  ? 1489 GLY A C     1 
ATOM   286   O  O     . GLY A 1 1489 ? 134.419 210.567 151.601 1.00 54.85  ? 1489 GLY A O     1 
ATOM   287   N  N     . TRP A 1 1490 ? 134.570 208.327 151.369 1.00 53.95  ? 1490 TRP A N     1 
ATOM   288   C  CA    . TRP A 1 1490 ? 135.282 208.159 152.632 1.00 49.16  ? 1490 TRP A CA    1 
ATOM   289   C  C     . TRP A 1 1490 ? 136.653 208.821 152.590 1.00 53.69  ? 1490 TRP A C     1 
ATOM   290   O  O     . TRP A 1 1490 ? 137.102 209.392 153.591 1.00 58.84  ? 1490 TRP A O     1 
ATOM   291   C  CB    . TRP A 1 1490 ? 135.422 206.675 152.965 1.00 49.70  ? 1490 TRP A CB    1 
ATOM   292   C  CG    . TRP A 1 1490 ? 134.120 205.959 153.132 1.00 50.95  ? 1490 TRP A CG    1 
ATOM   293   C  CD1   . TRP A 1 1490 ? 133.510 205.148 152.222 1.00 49.29  ? 1490 TRP A CD1   1 
ATOM   294   C  CD2   . TRP A 1 1490 ? 133.275 205.975 154.287 1.00 45.26  ? 1490 TRP A CD2   1 
ATOM   295   N  NE1   . TRP A 1 1490 ? 132.332 204.663 152.735 1.00 46.77  ? 1490 TRP A NE1   1 
ATOM   296   C  CE2   . TRP A 1 1490 ? 132.165 205.156 154.003 1.00 42.85  ? 1490 TRP A CE2   1 
ATOM   297   C  CE3   . TRP A 1 1490 ? 133.347 206.605 155.533 1.00 45.77  ? 1490 TRP A CE3   1 
ATOM   298   C  CZ2   . TRP A 1 1490 ? 131.136 204.949 154.918 1.00 39.68  ? 1490 TRP A CZ2   1 
ATOM   299   C  CZ3   . TRP A 1 1490 ? 132.324 206.399 156.440 1.00 46.75  ? 1490 TRP A CZ3   1 
ATOM   300   C  CH2   . TRP A 1 1490 ? 131.233 205.579 156.127 1.00 42.60  ? 1490 TRP A CH2   1 
ATOM   301   N  N     . ASP A 1 1491 ? 137.335 208.749 151.443 1.00 56.05  ? 1491 ASP A N     1 
ATOM   302   C  CA    . ASP A 1 1491 ? 138.697 209.268 151.355 1.00 56.32  ? 1491 ASP A CA    1 
ATOM   303   C  C     . ASP A 1 1491 ? 138.746 210.770 151.613 1.00 62.30  ? 1491 ASP A C     1 
ATOM   304   O  O     . ASP A 1 1491 ? 139.624 211.252 152.337 1.00 64.78  ? 1491 ASP A O     1 
ATOM   305   C  CB    . ASP A 1 1491 ? 139.301 208.921 149.992 1.00 61.54  ? 1491 ASP A CB    1 
ATOM   306   C  CG    . ASP A 1 1491 ? 138.530 209.526 148.829 1.00 66.17  ? 1491 ASP A CG    1 
ATOM   307   O  OD1   . ASP A 1 1491 ? 137.491 210.180 149.060 1.00 63.70  ? 1491 ASP A OD1   1 
ATOM   308   O  OD2   . ASP A 1 1491 ? 138.969 209.344 147.674 1.00 68.56  ? 1491 ASP A OD2   1 
ATOM   309   N  N     . ASP A 1 1492 ? 137.811 211.526 151.033 1.00 63.63  ? 1492 ASP A N     1 
ATOM   310   C  CA    . ASP A 1 1492 ? 137.761 212.961 151.294 1.00 63.63  ? 1492 ASP A CA    1 
ATOM   311   C  C     . ASP A 1 1492 ? 137.462 213.240 152.760 1.00 60.12  ? 1492 ASP A C     1 
ATOM   312   O  O     . ASP A 1 1492 ? 138.038 214.156 153.358 1.00 60.53  ? 1492 ASP A O     1 
ATOM   313   C  CB    . ASP A 1 1492 ? 136.715 213.624 150.398 1.00 67.59  ? 1492 ASP A CB    1 
ATOM   314   C  CG    . ASP A 1 1492 ? 136.966 213.374 148.925 1.00 76.83  ? 1492 ASP A CG    1 
ATOM   315   O  OD1   . ASP A 1 1492 ? 138.059 213.735 148.438 1.00 77.49  ? 1492 ASP A OD1   1 
ATOM   316   O  OD2   . ASP A 1 1492 ? 136.071 212.818 148.255 1.00 74.04  ? 1492 ASP A OD2   1 
ATOM   317   N  N     . LEU A 1 1493 ? 136.557 212.459 153.353 1.00 58.01  ? 1493 LEU A N     1 
ATOM   318   C  CA    . LEU A 1 1493 ? 136.221 212.633 154.762 1.00 55.26  ? 1493 LEU A CA    1 
ATOM   319   C  C     . LEU A 1 1493 ? 137.426 212.370 155.657 1.00 59.94  ? 1493 LEU A C     1 
ATOM   320   O  O     . LEU A 1 1493 ? 137.711 213.145 156.578 1.00 62.48  ? 1493 LEU A O     1 
ATOM   321   C  CB    . LEU A 1 1493 ? 135.061 211.708 155.126 1.00 48.68  ? 1493 LEU A CB    1 
ATOM   322   C  CG    . LEU A 1 1493 ? 134.353 211.916 156.462 1.00 48.20  ? 1493 LEU A CG    1 
ATOM   323   C  CD1   . LEU A 1 1493 ? 133.165 212.844 156.313 1.00 55.79  ? 1493 LEU A CD1   1 
ATOM   324   C  CD2   . LEU A 1 1493 ? 133.910 210.570 156.990 1.00 48.59  ? 1493 LEU A CD2   1 
ATOM   325   N  N     . PHE A 1 1494 ? 138.148 211.276 155.402 1.00 60.32  ? 1494 PHE A N     1 
ATOM   326   C  CA    . PHE A 1 1494 ? 139.294 210.938 156.240 1.00 60.34  ? 1494 PHE A CA    1 
ATOM   327   C  C     . PHE A 1 1494 ? 140.447 211.912 156.029 1.00 64.13  ? 1494 PHE A C     1 
ATOM   328   O  O     . PHE A 1 1494 ? 141.129 212.294 156.987 1.00 69.28  ? 1494 PHE A O     1 
ATOM   329   C  CB    . PHE A 1 1494 ? 139.741 209.502 155.966 1.00 56.71  ? 1494 PHE A CB    1 
ATOM   330   C  CG    . PHE A 1 1494 ? 138.759 208.465 156.428 1.00 52.87  ? 1494 PHE A CG    1 
ATOM   331   C  CD1   . PHE A 1 1494 ? 138.210 208.531 157.698 1.00 52.92  ? 1494 PHE A CD1   1 
ATOM   332   C  CD2   . PHE A 1 1494 ? 138.387 207.422 155.597 1.00 52.80  ? 1494 PHE A CD2   1 
ATOM   333   C  CE1   . PHE A 1 1494 ? 137.305 207.579 158.128 1.00 46.49  ? 1494 PHE A CE1   1 
ATOM   334   C  CE2   . PHE A 1 1494 ? 137.483 206.467 156.022 1.00 51.96  ? 1494 PHE A CE2   1 
ATOM   335   C  CZ    . PHE A 1 1494 ? 136.942 206.546 157.289 1.00 46.84  ? 1494 PHE A CZ    1 
ATOM   336   N  N     . ASN A 1 1495 ? 140.688 212.318 154.779 1.00 64.88  ? 1495 ASN A N     1 
ATOM   337   C  CA    . ASN A 1 1495 ? 141.775 213.253 154.505 1.00 65.85  ? 1495 ASN A CA    1 
ATOM   338   C  C     . ASN A 1 1495 ? 141.521 214.608 155.154 1.00 63.41  ? 1495 ASN A C     1 
ATOM   339   O  O     . ASN A 1 1495 ? 142.445 215.228 155.694 1.00 67.07  ? 1495 ASN A O     1 
ATOM   340   C  CB    . ASN A 1 1495 ? 141.970 213.408 152.997 1.00 64.73  ? 1495 ASN A CB    1 
ATOM   341   C  CG    . ASN A 1 1495 ? 142.489 212.144 152.344 1.00 64.93  ? 1495 ASN A CG    1 
ATOM   342   O  OD1   . ASN A 1 1495 ? 142.863 211.189 153.025 1.00 62.48  ? 1495 ASN A OD1   1 
ATOM   343   N  ND2   . ASN A 1 1495 ? 142.514 212.131 151.017 1.00 63.23  ? 1495 ASN A ND2   1 
ATOM   344   N  N     . LYS A 1 1496 ? 140.276 215.087 155.106 1.00 65.18  ? 1496 LYS A N     1 
ATOM   345   C  CA    . LYS A 1 1496 ? 139.949 216.360 155.741 1.00 69.11  ? 1496 LYS A CA    1 
ATOM   346   C  C     . LYS A 1 1496 ? 140.169 216.296 157.247 1.00 68.84  ? 1496 LYS A C     1 
ATOM   347   O  O     . LYS A 1 1496 ? 140.670 217.252 157.851 1.00 75.18  ? 1496 LYS A O     1 
ATOM   348   C  CB    . LYS A 1 1496 ? 138.505 216.751 155.423 1.00 67.94  ? 1496 LYS A CB    1 
ATOM   349   C  CG    . LYS A 1 1496 ? 138.082 218.092 156.002 1.00 68.42  ? 1496 LYS A CG    1 
ATOM   350   C  CD    . LYS A 1 1496 ? 138.900 219.233 155.420 1.00 77.48  ? 1496 LYS A CD    1 
ATOM   351   C  CE    . LYS A 1 1496 ? 138.621 219.420 153.939 1.00 74.99  ? 1496 LYS A CE    1 
ATOM   352   N  NZ    . LYS A 1 1496 ? 139.448 220.513 153.359 1.00 71.43  ? 1496 LYS A NZ    1 
ATOM   353   N  N     . VAL A 1 1497 ? 139.796 215.177 157.870 1.00 64.32  ? 1497 VAL A N     1 
ATOM   354   C  CA    . VAL A 1 1497 ? 140.006 215.017 159.305 1.00 63.91  ? 1497 VAL A CA    1 
ATOM   355   C  C     . VAL A 1 1497 ? 141.495 214.998 159.627 1.00 70.99  ? 1497 VAL A C     1 
ATOM   356   O  O     . VAL A 1 1497 ? 141.949 215.653 160.574 1.00 72.12  ? 1497 VAL A O     1 
ATOM   357   C  CB    . VAL A 1 1497 ? 139.299 213.744 159.806 1.00 63.87  ? 1497 VAL A CB    1 
ATOM   358   C  CG1   . VAL A 1 1497 ? 139.724 213.417 161.226 1.00 65.69  ? 1497 VAL A CG1   1 
ATOM   359   C  CG2   . VAL A 1 1497 ? 137.797 213.911 159.718 1.00 65.70  ? 1497 VAL A CG2   1 
ATOM   360   N  N     . LYS A 1 1498 ? 142.280 214.254 158.843 1.00 69.97  ? 1498 LYS A N     1 
ATOM   361   C  CA    . LYS A 1 1498 ? 143.719 214.193 159.079 1.00 70.30  ? 1498 LYS A CA    1 
ATOM   362   C  C     . LYS A 1 1498 ? 144.371 215.557 158.897 1.00 77.19  ? 1498 LYS A C     1 
ATOM   363   O  O     . LYS A 1 1498 ? 145.224 215.956 159.698 1.00 81.28  ? 1498 LYS A O     1 
ATOM   364   C  CB    . LYS A 1 1498 ? 144.364 213.168 158.145 1.00 74.86  ? 1498 LYS A CB    1 
ATOM   365   C  CG    . LYS A 1 1498 ? 144.084 211.727 158.520 1.00 79.41  ? 1498 LYS A CG    1 
ATOM   366   C  CD    . LYS A 1 1498 ? 144.714 210.762 157.533 1.00 76.40  ? 1498 LYS A CD    1 
ATOM   367   C  CE    . LYS A 1 1498 ? 144.543 209.326 157.995 1.00 77.10  ? 1498 LYS A CE    1 
ATOM   368   N  NZ    . LYS A 1 1498 ? 143.109 208.936 158.063 1.00 70.57  ? 1498 LYS A NZ    1 
ATOM   369   N  N     . GLU A 1 1499 ? 143.982 216.287 157.849 1.00 76.72  ? 1499 GLU A N     1 
ATOM   370   C  CA    . GLU A 1 1499 ? 144.566 217.603 157.608 1.00 78.55  ? 1499 GLU A CA    1 
ATOM   371   C  C     . GLU A 1 1499 ? 144.243 218.565 158.745 1.00 81.04  ? 1499 GLU A C     1 
ATOM   372   O  O     . GLU A 1 1499 ? 145.099 219.354 159.164 1.00 83.81  ? 1499 GLU A O     1 
ATOM   373   C  CB    . GLU A 1 1499 ? 144.072 218.158 156.271 1.00 76.36  ? 1499 GLU A CB    1 
ATOM   374   C  CG    . GLU A 1 1499 ? 143.944 219.672 156.228 1.00 79.63  ? 1499 GLU A CG    1 
ATOM   375   C  CD    . GLU A 1 1499 ? 143.992 220.221 154.818 1.00 79.36  ? 1499 GLU A CD    1 
ATOM   376   O  OE1   . GLU A 1 1499 ? 143.393 221.290 154.575 1.00 78.75  ? 1499 GLU A OE1   1 
ATOM   377   O  OE2   . GLU A 1 1499 ? 144.631 219.586 153.953 1.00 80.15  ? 1499 GLU A OE2   1 
ATOM   378   N  N     . HIS A 1 1500 ? 143.015 218.510 159.263 1.00 79.16  ? 1500 HIS A N     1 
ATOM   379   C  CA    . HIS A 1 1500 ? 142.637 219.406 160.350 1.00 80.95  ? 1500 HIS A CA    1 
ATOM   380   C  C     . HIS A 1 1500 ? 143.295 219.000 161.663 1.00 81.67  ? 1500 HIS A C     1 
ATOM   381   O  O     . HIS A 1 1500 ? 143.667 219.863 162.466 1.00 87.69  ? 1500 HIS A O     1 
ATOM   382   C  CB    . HIS A 1 1500 ? 141.116 219.443 160.491 1.00 78.44  ? 1500 HIS A CB    1 
ATOM   383   C  CG    . HIS A 1 1500 ? 140.435 220.274 159.448 1.00 77.74  ? 1500 HIS A CG    1 
ATOM   384   N  ND1   . HIS A 1 1500 ? 139.087 220.556 159.483 1.00 78.77  ? 1500 HIS A ND1   1 
ATOM   385   C  CD2   . HIS A 1 1500 ? 140.918 220.885 158.341 1.00 79.91  ? 1500 HIS A CD2   1 
ATOM   386   C  CE1   . HIS A 1 1500 ? 138.769 221.305 158.442 1.00 84.92  ? 1500 HIS A CE1   1 
ATOM   387   N  NE2   . HIS A 1 1500 ? 139.862 221.519 157.733 1.00 83.74  ? 1500 HIS A NE2   1 
ATOM   388   N  N     . ILE A 1 1501 ? 143.452 217.694 161.902 1.00 77.80  ? 1501 ILE A N     1 
ATOM   389   C  CA    . ILE A 1 1501 ? 144.116 217.241 163.123 1.00 81.98  ? 1501 ILE A CA    1 
ATOM   390   C  C     . ILE A 1 1501 ? 145.570 217.695 163.140 1.00 85.80  ? 1501 ILE A C     1 
ATOM   391   O  O     . ILE A 1 1501 ? 146.071 218.185 164.160 1.00 86.77  ? 1501 ILE A O     1 
ATOM   392   C  CB    . ILE A 1 1501 ? 143.998 215.713 163.270 1.00 75.11  ? 1501 ILE A CB    1 
ATOM   393   C  CG1   . ILE A 1 1501 ? 142.580 215.322 163.687 1.00 73.78  ? 1501 ILE A CG1   1 
ATOM   394   C  CG2   . ILE A 1 1501 ? 145.010 215.188 164.277 1.00 70.47  ? 1501 ILE A CG2   1 
ATOM   395   C  CD1   . ILE A 1 1501 ? 142.335 213.830 163.677 1.00 66.39  ? 1501 ILE A CD1   1 
ATOM   396   N  N     . ASN A 1 1502 ? 146.269 217.542 162.013 1.00 86.26  ? 1502 ASN A N     1 
ATOM   397   C  CA    . ASN A 1 1502 ? 147.647 218.015 161.932 1.00 87.29  ? 1502 ASN A CA    1 
ATOM   398   C  C     . ASN A 1 1502 ? 147.720 219.527 162.099 1.00 89.94  ? 1502 ASN A C     1 
ATOM   399   O  O     . ASN A 1 1502 ? 148.645 220.045 162.736 1.00 93.24  ? 1502 ASN A O     1 
ATOM   400   C  CB    . ASN A 1 1502 ? 148.276 217.585 160.607 1.00 85.17  ? 1502 ASN A CB    1 
ATOM   401   C  CG    . ASN A 1 1502 ? 148.154 216.095 160.361 1.00 87.36  ? 1502 ASN A CG    1 
ATOM   402   O  OD1   . ASN A 1 1502 ? 148.095 215.301 161.301 1.00 86.90  ? 1502 ASN A OD1   1 
ATOM   403   N  ND2   . ASN A 1 1502 ? 148.114 215.706 159.092 1.00 87.32  ? 1502 ASN A ND2   1 
ATOM   404   N  N     . SER A 1 1503 ? 146.756 220.253 161.528 1.00 87.45  ? 1503 SER A N     1 
ATOM   405   C  CA    . SER A 1 1503 ? 146.698 221.696 161.740 1.00 86.59  ? 1503 SER A CA    1 
ATOM   406   C  C     . SER A 1 1503 ? 146.447 222.025 163.206 1.00 93.95  ? 1503 SER A C     1 
ATOM   407   O  O     . SER A 1 1503 ? 147.050 222.956 163.753 1.00 96.00  ? 1503 SER A O     1 
ATOM   408   C  CB    . SER A 1 1503 ? 145.616 222.315 160.856 1.00 79.29  ? 1503 SER A CB    1 
ATOM   409   O  OG    . SER A 1 1503 ? 144.325 222.051 161.375 1.00 88.23  ? 1503 SER A OG    1 
ATOM   410   N  N     . VAL A 1 1504 ? 145.539 221.274 163.836 1.00 92.52  ? 1504 VAL A N     1 
ATOM   411   C  CA    . VAL A 1 1504 ? 145.206 221.521 165.273 1.00 91.17  ? 1504 VAL A CA    1 
ATOM   412   C  C     . VAL A 1 1504 ? 146.507 221.460 166.089 1.00 95.11  ? 1504 VAL A C     1 
ATOM   413   O  O     . VAL A 1 1504 ? 146.672 222.292 167.004 1.00 98.28  ? 1504 VAL A O     1 
ATOM   414   C  CB    . VAL A 1 1504 ? 144.161 220.523 165.808 1.00 89.41  ? 1504 VAL A CB    1 
ATOM   415   C  CG1   . VAL A 1 1504 ? 144.075 220.549 167.329 1.00 89.47  ? 1504 VAL A CG1   1 
ATOM   416   C  CG2   . VAL A 1 1504 ? 142.788 220.753 165.190 1.00 85.39  ? 1504 VAL A CG2   1 
ATOM   417   N  N     . SER A 1 1505 ? 147.388 220.511 165.763 1.00 96.42  ? 1505 SER A N     1 
ATOM   418   C  CA    . SER A 1 1505 ? 148.675 220.368 166.493 1.00 96.55  ? 1505 SER A CA    1 
ATOM   419   C  C     . SER A 1 1505 ? 149.583 221.569 166.198 1.00 98.55  ? 1505 SER A C     1 
ATOM   420   O  O     . SER A 1 1505 ? 150.271 222.031 167.135 1.00 100.83 ? 1505 SER A O     1 
ATOM   421   C  CB    . SER A 1 1505 ? 149.352 219.073 166.133 1.00 93.83  ? 1505 SER A CB    1 
ATOM   422   O  OG    . SER A 1 1505 ? 148.490 217.968 166.369 1.00 93.84  ? 1505 SER A OG    1 
ATOM   423   N  N     . ALA A 1 1506 ? 149.575 222.059 164.955 1.00 98.65  ? 1506 ALA A N     1 
ATOM   424   C  CA    . ALA A 1 1506 ? 150.478 223.169 164.563 1.00 99.78  ? 1506 ALA A CA    1 
ATOM   425   C  C     . ALA A 1 1506 ? 150.229 224.402 165.436 1.00 105.29 ? 1506 ALA A C     1 
ATOM   426   O  O     . ALA A 1 1506 ? 151.214 225.011 165.906 1.00 108.93 ? 1506 ALA A O     1 
ATOM   427   C  CB    . ALA A 1 1506 ? 150.287 223.487 163.096 1.00 90.19  ? 1506 ALA A CB    1 
ATOM   428   N  N     . MET A 1 1507 ? 148.961 224.764 165.645 1.00 104.74 ? 1507 MET A N     1 
ATOM   429   C  CA    . MET A 1 1507 ? 148.641 225.990 166.423 1.00 105.07 ? 1507 MET A CA    1 
ATOM   430   C  C     . MET A 1 1507 ? 149.203 225.839 167.846 1.00 108.58 ? 1507 MET A C     1 
ATOM   431   O  O     . MET A 1 1507 ? 149.681 226.850 168.405 1.00 111.39 ? 1507 MET A O     1 
ATOM   432   C  CB    . MET A 1 1507 ? 147.128 226.234 166.472 1.00 105.63 ? 1507 MET A CB    1 
ATOM   433   C  CG    . MET A 1 1507 ? 146.359 225.198 167.266 1.00 102.97 ? 1507 MET A CG    1 
ATOM   434   S  SD    . MET A 1 1507 ? 144.594 225.217 166.895 1.00 101.76 ? 1507 MET A SD    1 
ATOM   435   C  CE    . MET A 1 1507 ? 144.651 224.956 165.117 1.00 89.97  ? 1507 MET A CE    1 
ATOM   436   N  N     . LYS A 1 1508 ? 149.156 224.624 168.398 1.00 108.83 ? 1508 LYS A N     1 
ATOM   437   C  CA    . LYS A 1 1508 ? 149.674 224.375 169.768 1.00 108.97 ? 1508 LYS A CA    1 
ATOM   438   C  C     . LYS A 1 1508 ? 151.169 224.720 169.810 1.00 110.35 ? 1508 LYS A C     1 
ATOM   439   O  O     . LYS A 1 1508 ? 151.628 225.245 170.848 1.00 110.09 ? 1508 LYS A O     1 
ATOM   440   C  CB    . LYS A 1 1508 ? 149.433 222.913 170.157 1.00 104.76 ? 1508 LYS A CB    1 
ATOM   441   C  CG    . LYS A 1 1508 ? 148.014 222.427 169.908 1.00 103.92 ? 1508 LYS A CG    1 
ATOM   442   C  CD    . LYS A 1 1508 ? 147.819 220.943 170.188 1.00 97.87  ? 1508 LYS A CD    1 
ATOM   443   C  CE    . LYS A 1 1508 ? 146.415 220.504 169.925 1.00 96.55  ? 1508 LYS A CE    1 
ATOM   444   N  NZ    . LYS A 1 1508 ? 146.260 219.061 170.118 1.00 92.95  ? 1508 LYS A NZ    1 
ATOM   445   N  N     . LEU A 1 1509 ? 151.891 224.444 168.721 1.00 112.83 ? 1509 LEU A N     1 
ATOM   446   C  CA    . LEU A 1 1509 ? 153.355 224.698 168.684 1.00 114.27 ? 1509 LEU A CA    1 
ATOM   447   C  C     . LEU A 1 1509 ? 153.625 226.181 168.980 1.00 113.99 ? 1509 LEU A C     1 
ATOM   448   O  O     . LEU A 1 1509 ? 154.565 226.467 169.752 1.00 110.89 ? 1509 LEU A O     1 
ATOM   449   C  CB    . LEU A 1 1509 ? 153.894 224.288 167.315 1.00 111.07 ? 1509 LEU A CB    1 
ATOM   450   C  CG    . LEU A 1 1509 ? 153.453 222.911 166.811 1.00 108.40 ? 1509 LEU A CG    1 
ATOM   451   C  CD1   . LEU A 1 1509 ? 154.064 222.601 165.456 1.00 100.71 ? 1509 LEU A CD1   1 
ATOM   452   C  CD2   . LEU A 1 1509 ? 153.792 221.824 167.816 1.00 105.11 ? 1509 LEU A CD2   1 
ATOM   453   N  N     . SER A 1 1510 ? 152.830 227.081 168.394 1.00 116.81 ? 1510 SER A N     1 
ATOM   454   C  CA    . SER A 1 1510 ? 153.039 228.540 168.588 1.00 117.17 ? 1510 SER A CA    1 
ATOM   455   C  C     . SER A 1 1510 ? 152.774 228.924 170.050 1.00 119.14 ? 1510 SER A C     1 
ATOM   456   O  O     . SER A 1 1510 ? 151.904 228.283 170.681 1.00 116.22 ? 1510 SER A O     1 
ATOM   457   C  CB    . SER A 1 1510 ? 152.164 229.340 167.659 1.00 112.38 ? 1510 SER A CB    1 
ATOM   458   O  OG    . SER A 1 1510 ? 150.796 229.212 168.021 1.00 110.16 ? 1510 SER A OG    1 
ATOM   459   N  N     . PRO A 1 1511 ? 153.465 229.941 170.613 1.00 121.11 ? 1511 PRO A N     1 
ATOM   460   C  CA    . PRO A 1 1511 ? 153.180 230.408 171.980 1.00 121.10 ? 1511 PRO A CA    1 
ATOM   461   C  C     . PRO A 1 1511 ? 151.812 231.051 172.117 1.00 117.24 ? 1511 PRO A C     1 
ATOM   462   O  O     . PRO A 1 1511 ? 151.280 231.136 173.231 1.00 113.33 ? 1511 PRO A O     1 
ATOM   463   C  CB    . PRO A 1 1511 ? 154.315 231.404 172.249 1.00 117.35 ? 1511 PRO A CB    1 
ATOM   464   C  CG    . PRO A 1 1511 ? 154.701 231.900 170.896 1.00 113.67 ? 1511 PRO A CG    1 
ATOM   465   C  CD    . PRO A 1 1511 ? 154.515 230.739 169.958 1.00 113.95 ? 1511 PRO A CD    1 
ATOM   466   N  N     . TYR A 1 1512 ? 151.225 231.510 171.010 1.00 117.67 ? 1512 TYR A N     1 
ATOM   467   C  CA    . TYR A 1 1512 ? 149.905 232.129 171.058 1.00 116.91 ? 1512 TYR A CA    1 
ATOM   468   C  C     . TYR A 1 1512 ? 148.797 231.106 171.268 1.00 113.92 ? 1512 TYR A C     1 
ATOM   469   O  O     . TYR A 1 1512 ? 147.630 231.488 171.406 1.00 109.45 ? 1512 TYR A O     1 
ATOM   470   C  CB    . TYR A 1 1512 ? 149.651 232.921 169.772 1.00 117.99 ? 1512 TYR A CB    1 
ATOM   471   C  CG    . TYR A 1 1512 ? 150.532 234.142 169.616 1.00 120.14 ? 1512 TYR A CG    1 
ATOM   472   C  CD1   . TYR A 1 1512 ? 151.254 234.646 170.691 1.00 118.70 ? 1512 TYR A CD1   1 
ATOM   473   C  CD2   . TYR A 1 1512 ? 150.641 234.792 168.393 1.00 117.91 ? 1512 TYR A CD2   1 
ATOM   474   C  CE1   . TYR A 1 1512 ? 152.059 235.761 170.553 1.00 118.94 ? 1512 TYR A CE1   1 
ATOM   475   C  CE2   . TYR A 1 1512 ? 151.443 235.909 168.246 1.00 121.69 ? 1512 TYR A CE2   1 
ATOM   476   C  CZ    . TYR A 1 1512 ? 152.150 236.389 169.329 1.00 122.60 ? 1512 TYR A CZ    1 
ATOM   477   O  OH    . TYR A 1 1512 ? 152.949 237.500 169.185 1.00 115.42 ? 1512 TYR A OH    1 
ATOM   478   N  N     . TYR A 1 1513 ? 149.136 229.818 171.289 1.00 113.95 ? 1513 TYR A N     1 
ATOM   479   C  CA    . TYR A 1 1513 ? 148.169 228.740 171.458 1.00 112.63 ? 1513 TYR A CA    1 
ATOM   480   C  C     . TYR A 1 1513 ? 147.383 228.864 172.760 1.00 110.69 ? 1513 TYR A C     1 
ATOM   481   O  O     . TYR A 1 1513 ? 146.248 228.386 172.849 1.00 110.74 ? 1513 TYR A O     1 
ATOM   482   C  CB    . TYR A 1 1513 ? 148.890 227.390 171.400 1.00 111.31 ? 1513 TYR A CB    1 
ATOM   483   C  CG    . TYR A 1 1513 ? 148.055 226.207 171.829 1.00 110.82 ? 1513 TYR A CG    1 
ATOM   484   C  CD1   . TYR A 1 1513 ? 146.940 225.817 171.100 1.00 109.79 ? 1513 TYR A CD1   1 
ATOM   485   C  CD2   . TYR A 1 1513 ? 148.386 225.476 172.962 1.00 107.62 ? 1513 TYR A CD2   1 
ATOM   486   C  CE1   . TYR A 1 1513 ? 146.176 224.734 171.490 1.00 106.59 ? 1513 TYR A CE1   1 
ATOM   487   C  CE2   . TYR A 1 1513 ? 147.629 224.392 173.358 1.00 107.97 ? 1513 TYR A CE2   1 
ATOM   488   C  CZ    . TYR A 1 1513 ? 146.526 224.025 172.619 1.00 106.74 ? 1513 TYR A CZ    1 
ATOM   489   O  OH    . TYR A 1 1513 ? 145.769 222.946 173.010 1.00 103.62 ? 1513 TYR A OH    1 
ATOM   490   N  N     . LYS A 1 1514 ? 147.972 229.512 173.769 1.00 109.07 ? 1514 LYS A N     1 
ATOM   491   C  CA    . LYS A 1 1514 ? 147.348 229.560 175.088 1.00 105.36 ? 1514 LYS A CA    1 
ATOM   492   C  C     . LYS A 1 1514 ? 146.011 230.295 175.063 1.00 104.16 ? 1514 LYS A C     1 
ATOM   493   O  O     . LYS A 1 1514 ? 145.049 229.866 175.709 1.00 100.20 ? 1514 LYS A O     1 
ATOM   494   C  CB    . LYS A 1 1514 ? 148.297 230.217 176.092 1.00 99.36  ? 1514 LYS A CB    1 
ATOM   495   C  CG    . LYS A 1 1514 ? 147.770 230.237 177.520 1.00 97.87  ? 1514 LYS A CG    1 
ATOM   496   C  CD    . LYS A 1 1514 ? 147.285 228.861 177.950 1.00 98.82  ? 1514 LYS A CD    1 
ATOM   497   C  CE    . LYS A 1 1514 ? 146.551 228.924 179.280 1.00 97.80  ? 1514 LYS A CE    1 
ATOM   498   N  NZ    . LYS A 1 1514 ? 146.014 227.594 179.684 1.00 91.85  ? 1514 LYS A NZ    1 
ATOM   499   N  N     . VAL A 1 1515 ? 145.932 231.406 174.326 1.00 106.41 ? 1515 VAL A N     1 
ATOM   500   C  CA    . VAL A 1 1515 ? 144.714 232.210 174.324 1.00 107.29 ? 1515 VAL A CA    1 
ATOM   501   C  C     . VAL A 1 1515 ? 143.539 231.457 173.711 1.00 106.82 ? 1515 VAL A C     1 
ATOM   502   O  O     . VAL A 1 1515 ? 142.387 231.700 174.087 1.00 105.37 ? 1515 VAL A O     1 
ATOM   503   C  CB    . VAL A 1 1515 ? 144.962 233.557 173.604 1.00 107.28 ? 1515 VAL A CB    1 
ATOM   504   C  CG1   . VAL A 1 1515 ? 145.157 233.353 172.112 1.00 107.37 ? 1515 VAL A CG1   1 
ATOM   505   C  CG2   . VAL A 1 1515 ? 143.823 234.531 173.878 1.00 105.61 ? 1515 VAL A CG2   1 
ATOM   506   N  N     . PHE A 1 1516 ? 143.797 230.539 172.780 1.00 107.39 ? 1516 PHE A N     1 
ATOM   507   C  CA    . PHE A 1 1516 ? 142.757 229.701 172.200 1.00 105.36 ? 1516 PHE A CA    1 
ATOM   508   C  C     . PHE A 1 1516 ? 142.903 228.233 172.572 1.00 103.94 ? 1516 PHE A C     1 
ATOM   509   O  O     . PHE A 1 1516 ? 142.369 227.374 171.863 1.00 103.71 ? 1516 PHE A O     1 
ATOM   510   C  CB    . PHE A 1 1516 ? 142.748 229.834 170.671 1.00 105.26 ? 1516 PHE A CB    1 
ATOM   511   C  CG    . PHE A 1 1516 ? 142.846 231.250 170.179 1.00 105.89 ? 1516 PHE A CG    1 
ATOM   512   C  CD1   . PHE A 1 1516 ? 141.943 232.211 170.602 1.00 105.02 ? 1516 PHE A CD1   1 
ATOM   513   C  CD2   . PHE A 1 1516 ? 143.832 231.615 169.277 1.00 106.31 ? 1516 PHE A CD2   1 
ATOM   514   C  CE1   . PHE A 1 1516 ? 142.029 233.513 170.144 1.00 105.38 ? 1516 PHE A CE1   1 
ATOM   515   C  CE2   . PHE A 1 1516 ? 143.923 232.914 168.815 1.00 107.37 ? 1516 PHE A CE2   1 
ATOM   516   C  CZ    . PHE A 1 1516 ? 143.021 233.864 169.249 1.00 106.66 ? 1516 PHE A CZ    1 
ATOM   517   N  N     . GLU A 1 1517 ? 143.611 227.921 173.660 1.00 104.11 ? 1517 GLU A N     1 
ATOM   518   C  CA    . GLU A 1 1517 ? 143.926 226.533 173.987 1.00 101.39 ? 1517 GLU A CA    1 
ATOM   519   C  C     . GLU A 1 1517 ? 142.670 225.721 174.282 1.00 101.56 ? 1517 GLU A C     1 
ATOM   520   O  O     . GLU A 1 1517 ? 142.493 224.614 173.762 1.00 101.99 ? 1517 GLU A O     1 
ATOM   521   C  CB    . GLU A 1 1517 ? 144.890 226.488 175.174 1.00 102.71 ? 1517 GLU A CB    1 
ATOM   522   C  CG    . GLU A 1 1517 ? 145.060 225.106 175.782 1.00 105.38 ? 1517 GLU A CG    1 
ATOM   523   C  CD    . GLU A 1 1517 ? 146.071 225.087 176.911 1.00 107.63 ? 1517 GLU A CD    1 
ATOM   524   O  OE1   . GLU A 1 1517 ? 145.849 225.785 177.922 1.00 106.83 ? 1517 GLU A OE1   1 
ATOM   525   O  OE2   . GLU A 1 1517 ? 147.089 224.374 176.787 1.00 108.08 ? 1517 GLU A OE2   1 
ATOM   526   N  N     . GLU A 1 1518 ? 141.784 226.258 175.125 1.00 99.46  ? 1518 GLU A N     1 
ATOM   527   C  CA    . GLU A 1 1518 ? 140.596 225.510 175.524 1.00 98.69  ? 1518 GLU A CA    1 
ATOM   528   C  C     . GLU A 1 1518 ? 139.693 225.230 174.328 1.00 99.93  ? 1518 GLU A C     1 
ATOM   529   O  O     . GLU A 1 1518 ? 139.184 224.115 174.164 1.00 99.47  ? 1518 GLU A O     1 
ATOM   530   C  CB    . GLU A 1 1518 ? 139.835 226.271 176.611 1.00 96.41  ? 1518 GLU A CB    1 
ATOM   531   C  CG    . GLU A 1 1518 ? 138.404 225.795 176.814 1.00 97.24  ? 1518 GLU A CG    1 
ATOM   532   C  CD    . GLU A 1 1518 ? 137.545 226.815 177.535 1.00 98.94  ? 1518 GLU A CD    1 
ATOM   533   O  OE1   . GLU A 1 1518 ? 137.380 227.934 177.006 1.00 97.46  ? 1518 GLU A OE1   1 
ATOM   534   O  OE2   . GLU A 1 1518 ? 137.036 226.496 178.630 1.00 102.22 ? 1518 GLU A OE2   1 
ATOM   535   N  N     . ASP A 1 1519 ? 139.483 226.237 173.478 1.00 98.27  ? 1519 ASP A N     1 
ATOM   536   C  CA    . ASP A 1 1519 ? 138.668 226.036 172.284 1.00 99.10  ? 1519 ASP A CA    1 
ATOM   537   C  C     . ASP A 1 1519 ? 139.350 225.079 171.313 1.00 98.52  ? 1519 ASP A C     1 
ATOM   538   O  O     . ASP A 1 1519 ? 138.695 224.240 170.685 1.00 95.56  ? 1519 ASP A O     1 
ATOM   539   C  CB    . ASP A 1 1519 ? 138.379 227.378 171.612 1.00 100.66 ? 1519 ASP A CB    1 
ATOM   540   C  CG    . ASP A 1 1519 ? 137.533 227.233 170.363 1.00 102.61 ? 1519 ASP A CG    1 
ATOM   541   O  OD1   . ASP A 1 1519 ? 136.403 226.711 170.468 1.00 97.32  ? 1519 ASP A OD1   1 
ATOM   542   O  OD2   . ASP A 1 1519 ? 137.996 227.641 169.278 1.00 101.83 ? 1519 ASP A OD2   1 
ATOM   543   N  N     . ALA A 1 1520 ? 140.673 225.198 171.172 1.00 99.60  ? 1520 ALA A N     1 
ATOM   544   C  CA    . ALA A 1 1520 ? 141.414 224.262 170.333 1.00 94.64  ? 1520 ALA A CA    1 
ATOM   545   C  C     . ALA A 1 1520 ? 141.363 222.850 170.903 1.00 94.00  ? 1520 ALA A C     1 
ATOM   546   O  O     . ALA A 1 1520 ? 141.193 221.878 170.158 1.00 90.90  ? 1520 ALA A O     1 
ATOM   547   C  CB    . ALA A 1 1520 ? 142.861 224.725 170.180 1.00 89.82  ? 1520 ALA A CB    1 
ATOM   548   N  N     . LEU A 1 1521 ? 141.516 222.718 172.223 1.00 95.20  ? 1521 LEU A N     1 
ATOM   549   C  CA    . LEU A 1 1521 ? 141.425 221.405 172.854 1.00 92.44  ? 1521 LEU A CA    1 
ATOM   550   C  C     . LEU A 1 1521 ? 140.032 220.814 172.684 1.00 89.86  ? 1521 LEU A C     1 
ATOM   551   O  O     . LEU A 1 1521 ? 139.877 219.609 172.457 1.00 85.40  ? 1521 LEU A O     1 
ATOM   552   C  CB    . LEU A 1 1521 ? 141.793 221.506 174.336 1.00 94.50  ? 1521 LEU A CB    1 
ATOM   553   C  CG    . LEU A 1 1521 ? 143.287 221.481 174.669 1.00 98.15  ? 1521 LEU A CG    1 
ATOM   554   C  CD1   . LEU A 1 1521 ? 143.503 221.393 176.172 1.00 90.33  ? 1521 LEU A CD1   1 
ATOM   555   C  CD2   . LEU A 1 1521 ? 143.977 220.328 173.956 1.00 90.02  ? 1521 LEU A CD2   1 
ATOM   556   N  N     . SER A 1 1522 ? 139.001 221.653 172.800 1.00 92.47  ? 1522 SER A N     1 
ATOM   557   C  CA    . SER A 1 1522 ? 137.636 221.184 172.584 1.00 92.08  ? 1522 SER A CA    1 
ATOM   558   C  C     . SER A 1 1522 ? 137.436 220.729 171.143 1.00 86.86  ? 1522 SER A C     1 
ATOM   559   O  O     . SER A 1 1522 ? 136.654 219.812 170.870 1.00 83.32  ? 1522 SER A O     1 
ATOM   560   C  CB    . SER A 1 1522 ? 136.640 222.288 172.947 1.00 96.37  ? 1522 SER A CB    1 
ATOM   561   O  OG    . SER A 1 1522 ? 136.612 223.299 171.954 1.00 96.42  ? 1522 SER A OG    1 
ATOM   562   N  N     . TRP A 1 1523 ? 138.137 221.368 170.203 1.00 88.54  ? 1523 TRP A N     1 
ATOM   563   C  CA    . TRP A 1 1523 ? 138.025 220.977 168.801 1.00 87.90  ? 1523 TRP A CA    1 
ATOM   564   C  C     . TRP A 1 1523 ? 138.623 219.597 168.559 1.00 83.68  ? 1523 TRP A C     1 
ATOM   565   O  O     . TRP A 1 1523 ? 137.982 218.731 167.952 1.00 76.78  ? 1523 TRP A O     1 
ATOM   566   C  CB    . TRP A 1 1523 ? 138.695 222.022 167.908 1.00 89.17  ? 1523 TRP A CB    1 
ATOM   567   C  CG    . TRP A 1 1523 ? 137.721 222.954 167.260 1.00 90.01  ? 1523 TRP A CG    1 
ATOM   568   C  CD1   . TRP A 1 1523 ? 137.614 224.299 167.460 1.00 93.04  ? 1523 TRP A CD1   1 
ATOM   569   C  CD2   . TRP A 1 1523 ? 136.724 222.612 166.291 1.00 88.05  ? 1523 TRP A CD2   1 
ATOM   570   N  NE1   . TRP A 1 1523 ? 136.604 224.814 166.684 1.00 93.58  ? 1523 TRP A NE1   1 
ATOM   571   C  CE2   . TRP A 1 1523 ? 136.043 223.798 165.955 1.00 91.81  ? 1523 TRP A CE2   1 
ATOM   572   C  CE3   . TRP A 1 1523 ? 136.339 221.416 165.676 1.00 85.78  ? 1523 TRP A CE3   1 
ATOM   573   C  CZ2   . TRP A 1 1523 ? 134.999 223.824 165.034 1.00 93.24  ? 1523 TRP A CZ2   1 
ATOM   574   C  CZ3   . TRP A 1 1523 ? 135.302 221.444 164.763 1.00 88.39  ? 1523 TRP A CZ3   1 
ATOM   575   C  CH2   . TRP A 1 1523 ? 134.644 222.639 164.450 1.00 91.67  ? 1523 TRP A CH2   1 
ATOM   576   N  N     . GLU A 1 1524 ? 139.849 219.366 169.043 1.00 83.25  ? 1524 GLU A N     1 
ATOM   577   C  CA    . GLU A 1 1524 ? 140.530 218.106 168.754 1.00 76.41  ? 1524 GLU A CA    1 
ATOM   578   C  C     . GLU A 1 1524 ? 139.758 216.918 169.313 1.00 70.51  ? 1524 GLU A C     1 
ATOM   579   O  O     . GLU A 1 1524 ? 139.845 215.806 168.780 1.00 69.77  ? 1524 GLU A O     1 
ATOM   580   C  CB    . GLU A 1 1524 ? 141.958 218.131 169.302 1.00 76.41  ? 1524 GLU A CB    1 
ATOM   581   C  CG    . GLU A 1 1524 ? 142.067 218.011 170.812 1.00 82.97  ? 1524 GLU A CG    1 
ATOM   582   C  CD    . GLU A 1 1524 ? 143.271 217.198 171.245 1.00 87.06  ? 1524 GLU A CD    1 
ATOM   583   O  OE1   . GLU A 1 1524 ? 143.134 216.384 172.182 1.00 82.83  ? 1524 GLU A OE1   1 
ATOM   584   O  OE2   . GLU A 1 1524 ? 144.354 217.372 170.648 1.00 93.53  ? 1524 GLU A OE2   1 
ATOM   585   N  N     . ASP A 1 1525 ? 138.994 217.133 170.386 1.00 70.85  ? 1525 ASP A N     1 
ATOM   586   C  CA    . ASP A 1 1525 ? 138.128 216.077 170.898 1.00 69.35  ? 1525 ASP A CA    1 
ATOM   587   C  C     . ASP A 1 1525 ? 137.057 215.712 169.877 1.00 69.07  ? 1525 ASP A C     1 
ATOM   588   O  O     . ASP A 1 1525 ? 136.722 214.535 169.703 1.00 65.52  ? 1525 ASP A O     1 
ATOM   589   C  CB    . ASP A 1 1525 ? 137.495 216.514 172.218 1.00 72.80  ? 1525 ASP A CB    1 
ATOM   590   C  CG    . ASP A 1 1525 ? 136.558 215.469 172.791 1.00 75.21  ? 1525 ASP A CG    1 
ATOM   591   O  OD1   . ASP A 1 1525 ? 137.006 214.324 173.010 1.00 76.00  ? 1525 ASP A OD1   1 
ATOM   592   O  OD2   . ASP A 1 1525 ? 135.376 215.794 173.025 1.00 72.02  ? 1525 ASP A OD2   1 
ATOM   593   N  N     . LYS A 1 1526 ? 136.511 216.715 169.185 1.00 73.78  ? 1526 LYS A N     1 
ATOM   594   C  CA    . LYS A 1 1526 ? 135.436 216.462 168.231 1.00 67.18  ? 1526 LYS A CA    1 
ATOM   595   C  C     . LYS A 1 1526 ? 135.948 215.731 166.993 1.00 61.46  ? 1526 LYS A C     1 
ATOM   596   O  O     . LYS A 1 1526 ? 135.309 214.790 166.509 1.00 61.31  ? 1526 LYS A O     1 
ATOM   597   C  CB    . LYS A 1 1526 ? 134.758 217.777 167.845 1.00 73.00  ? 1526 LYS A CB    1 
ATOM   598   C  CG    . LYS A 1 1526 ? 133.979 218.422 168.982 1.00 72.39  ? 1526 LYS A CG    1 
ATOM   599   C  CD    . LYS A 1 1526 ? 133.049 219.514 168.476 1.00 73.09  ? 1526 LYS A CD    1 
ATOM   600   C  CE    . LYS A 1 1526 ? 133.826 220.729 168.006 1.00 78.56  ? 1526 LYS A CE    1 
ATOM   601   N  NZ    . LYS A 1 1526 ? 132.925 221.849 167.622 1.00 78.68  ? 1526 LYS A NZ    1 
ATOM   602   N  N     . LEU A 1 1527 ? 137.097 216.155 166.458 1.00 60.51  ? 1527 LEU A N     1 
ATOM   603   C  CA    . LEU A 1 1527 ? 137.646 215.487 165.280 1.00 60.20  ? 1527 LEU A CA    1 
ATOM   604   C  C     . LEU A 1 1527 ? 138.064 214.057 165.600 1.00 60.37  ? 1527 LEU A C     1 
ATOM   605   O  O     . LEU A 1 1527 ? 137.926 213.155 164.766 1.00 59.48  ? 1527 LEU A O     1 
ATOM   606   C  CB    . LEU A 1 1527 ? 138.824 216.276 164.704 1.00 62.12  ? 1527 LEU A CB    1 
ATOM   607   C  CG    . LEU A 1 1527 ? 138.647 217.770 164.427 1.00 68.16  ? 1527 LEU A CG    1 
ATOM   608   C  CD1   . LEU A 1 1527 ? 139.577 218.605 165.288 1.00 70.23  ? 1527 LEU A CD1   1 
ATOM   609   C  CD2   . LEU A 1 1527 ? 138.868 218.067 162.955 1.00 69.19  ? 1527 LEU A CD2   1 
ATOM   610   N  N     . ASN A 1 1528 ? 138.592 213.833 166.805 1.00 60.27  ? 1528 ASN A N     1 
ATOM   611   C  CA    . ASN A 1 1528 ? 138.935 212.475 167.218 1.00 54.32  ? 1528 ASN A CA    1 
ATOM   612   C  C     . ASN A 1 1528 ? 137.691 211.599 167.297 1.00 54.94  ? 1528 ASN A C     1 
ATOM   613   O  O     . ASN A 1 1528 ? 137.722 210.422 166.920 1.00 55.81  ? 1528 ASN A O     1 
ATOM   614   C  CB    . ASN A 1 1528 ? 139.672 212.501 168.557 1.00 57.32  ? 1528 ASN A CB    1 
ATOM   615   C  CG    . ASN A 1 1528 ? 141.060 213.102 168.446 1.00 56.29  ? 1528 ASN A CG    1 
ATOM   616   O  OD1   . ASN A 1 1528 ? 141.695 213.036 167.394 1.00 59.87  ? 1528 ASN A OD1   1 
ATOM   617   N  ND2   . ASN A 1 1528 ? 141.536 213.698 169.533 1.00 55.24  ? 1528 ASN A ND2   1 
ATOM   618   N  N     . ARG A 1 1529 ? 136.583 212.157 167.792 1.00 54.60  ? 1529 ARG A N     1 
ATOM   619   C  CA    . ARG A 1 1529 ? 135.323 211.420 167.799 1.00 54.27  ? 1529 ARG A CA    1 
ATOM   620   C  C     . ARG A 1 1529 ? 134.836 211.156 166.379 1.00 54.54  ? 1529 ARG A C     1 
ATOM   621   O  O     . ARG A 1 1529 ? 134.298 210.083 166.084 1.00 60.79  ? 1529 ARG A O     1 
ATOM   622   C  CB    . ARG A 1 1529 ? 134.264 212.183 168.596 1.00 58.76  ? 1529 ARG A CB    1 
ATOM   623   C  CG    . ARG A 1 1529 ? 134.550 212.284 170.083 1.00 57.20  ? 1529 ARG A CG    1 
ATOM   624   C  CD    . ARG A 1 1529 ? 133.682 213.350 170.731 1.00 57.21  ? 1529 ARG A CD    1 
ATOM   625   N  NE    . ARG A 1 1529 ? 132.271 213.162 170.419 1.00 58.74  ? 1529 ARG A NE    1 
ATOM   626   C  CZ    . ARG A 1 1529 ? 131.403 214.150 170.245 1.00 61.50  ? 1529 ARG A CZ    1 
ATOM   627   N  NH1   . ARG A 1 1529 ? 131.772 215.417 170.336 1.00 63.59  ? 1529 ARG A NH1   1 
ATOM   628   N  NH2   . ARG A 1 1529 ? 130.135 213.859 169.971 1.00 61.50  ? 1529 ARG A NH2   1 
ATOM   629   N  N     . ILE A 1 1530 ? 135.005 212.136 165.487 1.00 53.24  ? 1530 ILE A N     1 
ATOM   630   C  CA    . ILE A 1 1530 ? 134.619 211.948 164.088 1.00 54.25  ? 1530 ILE A CA    1 
ATOM   631   C  C     . ILE A 1 1530 ? 135.447 210.830 163.467 1.00 54.06  ? 1530 ILE A C     1 
ATOM   632   O  O     . ILE A 1 1530 ? 134.923 209.946 162.779 1.00 52.83  ? 1530 ILE A O     1 
ATOM   633   C  CB    . ILE A 1 1530 ? 134.767 213.263 163.303 1.00 52.93  ? 1530 ILE A CB    1 
ATOM   634   C  CG1   . ILE A 1 1530 ? 133.471 214.069 163.353 1.00 54.38  ? 1530 ILE A CG1   1 
ATOM   635   C  CG2   . ILE A 1 1530 ? 135.117 212.988 161.854 1.00 50.97  ? 1530 ILE A CG2   1 
ATOM   636   C  CD1   . ILE A 1 1530 ? 133.566 215.419 162.678 1.00 59.90  ? 1530 ILE A CD1   1 
ATOM   637   N  N     . MET A 1 1531 ? 136.759 210.854 163.712 1.00 56.58  ? 1531 MET A N     1 
ATOM   638   C  CA    . MET A 1 1531 ? 137.633 209.805 163.197 1.00 48.54  ? 1531 MET A CA    1 
ATOM   639   C  C     . MET A 1 1531 ? 137.278 208.449 163.794 1.00 50.39  ? 1531 MET A C     1 
ATOM   640   O  O     . MET A 1 1531 ? 137.241 207.436 163.088 1.00 53.64  ? 1531 MET A O     1 
ATOM   641   C  CB    . MET A 1 1531 ? 139.094 210.153 163.484 1.00 50.21  ? 1531 MET A CB    1 
ATOM   642   C  CG    . MET A 1 1531 ? 140.092 209.257 162.773 1.00 55.25  ? 1531 MET A CG    1 
ATOM   643   S  SD    . MET A 1 1531 ? 140.233 209.628 161.017 1.00 70.33  ? 1531 MET A SD    1 
ATOM   644   C  CE    . MET A 1 1531 ? 141.842 210.408 160.977 1.00 63.73  ? 1531 MET A CE    1 
ATOM   645   N  N     . ALA A 1 1532 ? 137.017 208.414 165.103 1.00 48.31  ? 1532 ALA A N     1 
ATOM   646   C  CA    . ALA A 1 1532 ? 136.685 207.155 165.763 1.00 51.95  ? 1532 ALA A CA    1 
ATOM   647   C  C     . ALA A 1 1532 ? 135.370 206.586 165.243 1.00 52.68  ? 1532 ALA A C     1 
ATOM   648   O  O     . ALA A 1 1532 ? 135.248 205.377 165.017 1.00 55.24  ? 1532 ALA A O     1 
ATOM   649   C  CB    . ALA A 1 1532 ? 136.622 207.359 167.278 1.00 51.42  ? 1532 ALA A CB    1 
ATOM   650   N  N     . LEU A 1 1533 ? 134.370 207.449 165.051 1.00 49.40  ? 1533 LEU A N     1 
ATOM   651   C  CA    . LEU A 1 1533 ? 133.070 206.985 164.577 1.00 50.54  ? 1533 LEU A CA    1 
ATOM   652   C  C     . LEU A 1 1533 ? 133.161 206.444 163.156 1.00 48.29  ? 1533 LEU A C     1 
ATOM   653   O  O     . LEU A 1 1533 ? 132.628 205.370 162.851 1.00 51.20  ? 1533 LEU A O     1 
ATOM   654   C  CB    . LEU A 1 1533 ? 132.050 208.122 164.653 1.00 53.66  ? 1533 LEU A CB    1 
ATOM   655   C  CG    . LEU A 1 1533 ? 130.615 207.758 164.268 1.00 51.04  ? 1533 LEU A CG    1 
ATOM   656   C  CD1   . LEU A 1 1533 ? 130.053 206.708 165.212 1.00 49.50  ? 1533 LEU A CD1   1 
ATOM   657   C  CD2   . LEU A 1 1533 ? 129.732 208.996 164.244 1.00 53.12  ? 1533 LEU A CD2   1 
ATOM   658   N  N     . PHE A 1 1534 ? 133.835 207.174 162.271 1.00 48.46  ? 1534 PHE A N     1 
ATOM   659   C  CA    . PHE A 1 1534 ? 133.905 206.803 160.865 1.00 44.28  ? 1534 PHE A CA    1 
ATOM   660   C  C     . PHE A 1 1534 ? 134.988 205.776 160.566 1.00 45.48  ? 1534 PHE A C     1 
ATOM   661   O  O     . PHE A 1 1534 ? 135.002 205.226 159.459 1.00 43.70  ? 1534 PHE A O     1 
ATOM   662   C  CB    . PHE A 1 1534 ? 134.110 208.056 160.013 1.00 43.74  ? 1534 PHE A CB    1 
ATOM   663   C  CG    . PHE A 1 1534 ? 132.936 208.991 160.037 1.00 49.07  ? 1534 PHE A CG    1 
ATOM   664   C  CD1   . PHE A 1 1534 ? 131.652 208.510 159.840 1.00 50.23  ? 1534 PHE A CD1   1 
ATOM   665   C  CD2   . PHE A 1 1534 ? 133.110 210.341 160.284 1.00 52.03  ? 1534 PHE A CD2   1 
ATOM   666   C  CE1   . PHE A 1 1534 ? 130.567 209.362 159.867 1.00 50.30  ? 1534 PHE A CE1   1 
ATOM   667   C  CE2   . PHE A 1 1534 ? 132.029 211.197 160.312 1.00 53.59  ? 1534 PHE A CE2   1 
ATOM   668   C  CZ    . PHE A 1 1534 ? 130.756 210.707 160.105 1.00 54.49  ? 1534 PHE A CZ    1 
ATOM   669   N  N     . ASP A 1 1535 ? 135.890 205.499 161.509 1.00 48.57  ? 1535 ASP A N     1 
ATOM   670   C  CA    . ASP A 1 1535 ? 136.788 204.362 161.355 1.00 47.66  ? 1535 ASP A CA    1 
ATOM   671   C  C     . ASP A 1 1535 ? 136.063 203.037 161.532 1.00 44.84  ? 1535 ASP A C     1 
ATOM   672   O  O     . ASP A 1 1535 ? 136.600 201.992 161.147 1.00 52.71  ? 1535 ASP A O     1 
ATOM   673   C  CB    . ASP A 1 1535 ? 137.945 204.453 162.352 1.00 50.14  ? 1535 ASP A CB    1 
ATOM   674   C  CG    . ASP A 1 1535 ? 139.217 204.983 161.721 1.00 56.56  ? 1535 ASP A CG    1 
ATOM   675   O  OD1   . ASP A 1 1535 ? 139.127 205.904 160.881 1.00 54.39  ? 1535 ASP A OD1   1 
ATOM   676   O  OD2   . ASP A 1 1535 ? 140.307 204.477 162.062 1.00 60.80  ? 1535 ASP A OD2   1 
ATOM   677   N  N     . VAL A 1 1536 ? 134.866 203.061 162.105 1.00 39.75  ? 1536 VAL A N     1 
ATOM   678   C  CA    . VAL A 1 1536 ? 134.039 201.872 162.266 1.00 43.58  ? 1536 VAL A CA    1 
ATOM   679   C  C     . VAL A 1 1536 ? 132.904 201.848 161.252 1.00 42.00  ? 1536 VAL A C     1 
ATOM   680   O  O     . VAL A 1 1536 ? 132.507 200.783 160.780 1.00 41.89  ? 1536 VAL A O     1 
ATOM   681   C  CB    . VAL A 1 1536 ? 133.501 201.793 163.713 1.00 43.74  ? 1536 VAL A CB    1 
ATOM   682   C  CG1   . VAL A 1 1536 ? 132.891 200.428 163.984 1.00 47.74  ? 1536 VAL A CG1   1 
ATOM   683   C  CG2   . VAL A 1 1536 ? 134.605 202.102 164.710 1.00 44.78  ? 1536 VAL A CG2   1 
ATOM   684   N  N     . TRP A 1 1537 ? 132.379 203.023 160.899 1.00 41.30  ? 1537 TRP A N     1 
ATOM   685   C  CA    . TRP A 1 1537 ? 131.213 203.094 160.023 1.00 40.24  ? 1537 TRP A CA    1 
ATOM   686   C  C     . TRP A 1 1537 ? 131.517 202.532 158.640 1.00 38.67  ? 1537 TRP A C     1 
ATOM   687   O  O     . TRP A 1 1537 ? 130.683 201.846 158.038 1.00 38.37  ? 1537 TRP A O     1 
ATOM   688   C  CB    . TRP A 1 1537 ? 130.723 204.539 159.925 1.00 44.46  ? 1537 TRP A CB    1 
ATOM   689   C  CG    . TRP A 1 1537 ? 129.271 204.664 159.565 1.00 48.74  ? 1537 TRP A CG    1 
ATOM   690   C  CD1   . TRP A 1 1537 ? 128.599 203.966 158.605 1.00 45.57  ? 1537 TRP A CD1   1 
ATOM   691   C  CD2   . TRP A 1 1537 ? 128.312 205.538 160.171 1.00 54.62  ? 1537 TRP A CD2   1 
ATOM   692   N  NE1   . TRP A 1 1537 ? 127.281 204.354 158.571 1.00 48.13  ? 1537 TRP A NE1   1 
ATOM   693   C  CE2   . TRP A 1 1537 ? 127.079 205.318 159.524 1.00 53.44  ? 1537 TRP A CE2   1 
ATOM   694   C  CE3   . TRP A 1 1537 ? 128.375 206.486 161.196 1.00 54.36  ? 1537 TRP A CE3   1 
ATOM   695   C  CZ2   . TRP A 1 1537 ? 125.921 206.011 159.868 1.00 52.93  ? 1537 TRP A CZ2   1 
ATOM   696   C  CZ3   . TRP A 1 1537 ? 127.225 207.173 161.536 1.00 53.80  ? 1537 TRP A CZ3   1 
ATOM   697   C  CH2   . TRP A 1 1537 ? 126.015 206.932 160.875 1.00 56.80  ? 1537 TRP A CH2   1 
ATOM   698   N  N     . ILE A 1 1538 ? 132.711 202.817 158.118 1.00 40.80  ? 1538 ILE A N     1 
ATOM   699   C  CA    . ILE A 1 1538 ? 133.079 202.327 156.790 1.00 37.54  ? 1538 ILE A CA    1 
ATOM   700   C  C     . ILE A 1 1538 ? 133.141 200.803 156.795 1.00 39.29  ? 1538 ILE A C     1 
ATOM   701   O  O     . ILE A 1 1538 ? 132.744 200.139 155.830 1.00 42.17  ? 1538 ILE A O     1 
ATOM   702   C  CB    . ILE A 1 1538 ? 134.406 202.955 156.329 1.00 37.28  ? 1538 ILE A CB    1 
ATOM   703   C  CG1   . ILE A 1 1538 ? 134.860 202.349 155.000 1.00 42.85  ? 1538 ILE A CG1   1 
ATOM   704   C  CG2   . ILE A 1 1538 ? 135.483 202.791 157.391 1.00 41.13  ? 1538 ILE A CG2   1 
ATOM   705   C  CD1   . ILE A 1 1538 ? 135.949 203.141 154.314 1.00 40.62  ? 1538 ILE A CD1   1 
ATOM   706   N  N     . ASP A 1 1539 ? 133.637 200.228 157.892 1.00 38.85  ? 1539 ASP A N     1 
ATOM   707   C  CA    . ASP A 1 1539 ? 133.654 198.775 158.028 1.00 38.99  ? 1539 ASP A CA    1 
ATOM   708   C  C     . ASP A 1 1539 ? 132.241 198.217 158.163 1.00 36.40  ? 1539 ASP A C     1 
ATOM   709   O  O     . ASP A 1 1539 ? 131.910 197.183 157.572 1.00 37.48  ? 1539 ASP A O     1 
ATOM   710   C  CB    . ASP A 1 1539 ? 134.510 198.374 159.230 1.00 42.11  ? 1539 ASP A CB    1 
ATOM   711   C  CG    . ASP A 1 1539 ? 135.922 197.988 158.837 1.00 52.95  ? 1539 ASP A CG    1 
ATOM   712   O  OD1   . ASP A 1 1539 ? 136.215 197.953 157.624 1.00 50.58  ? 1539 ASP A OD1   1 
ATOM   713   O  OD2   . ASP A 1 1539 ? 136.738 197.714 159.743 1.00 59.55  ? 1539 ASP A OD2   1 
ATOM   714   N  N     . VAL A 1 1540 ? 131.394 198.891 158.946 1.00 35.85  ? 1540 VAL A N     1 
ATOM   715   C  CA    . VAL A 1 1540 ? 130.024 198.420 159.155 1.00 34.25  ? 1540 VAL A CA    1 
ATOM   716   C  C     . VAL A 1 1540 ? 129.236 198.481 157.853 1.00 35.71  ? 1540 VAL A C     1 
ATOM   717   O  O     . VAL A 1 1540 ? 128.517 197.542 157.491 1.00 36.93  ? 1540 VAL A O     1 
ATOM   718   C  CB    . VAL A 1 1540 ? 129.334 199.232 160.265 1.00 37.19  ? 1540 VAL A CB    1 
ATOM   719   C  CG1   . VAL A 1 1540 ? 127.869 198.846 160.368 1.00 37.52  ? 1540 VAL A CG1   1 
ATOM   720   C  CG2   . VAL A 1 1540 ? 130.029 199.009 161.594 1.00 38.49  ? 1540 VAL A CG2   1 
ATOM   721   N  N     . GLN A 1 1541 ? 129.359 199.597 157.130 1.00 32.86  ? 1541 GLN A N     1 
ATOM   722   C  CA    . GLN A 1 1541 ? 128.615 199.758 155.885 1.00 27.53  ? 1541 GLN A CA    1 
ATOM   723   C  C     . GLN A 1 1541 ? 129.035 198.720 154.852 1.00 31.14  ? 1541 GLN A C     1 
ATOM   724   O  O     . GLN A 1 1541 ? 128.189 198.084 154.216 1.00 37.34  ? 1541 GLN A O     1 
ATOM   725   C  CB    . GLN A 1 1541 ? 128.809 201.172 155.335 1.00 30.67  ? 1541 GLN A CB    1 
ATOM   726   C  CG    . GLN A 1 1541 ? 128.126 201.409 153.998 1.00 33.18  ? 1541 GLN A CG    1 
ATOM   727   C  CD    . GLN A 1 1541 ? 128.148 202.865 153.581 1.00 42.73  ? 1541 GLN A CD    1 
ATOM   728   O  OE1   . GLN A 1 1541 ? 127.530 203.714 154.221 1.00 48.99  ? 1541 GLN A OE1   1 
ATOM   729   N  NE2   . GLN A 1 1541 ? 128.864 203.161 152.503 1.00 40.74  ? 1541 GLN A NE2   1 
ATOM   730   N  N     . ARG A 1 1542 ? 130.345 198.527 154.683 1.00 34.25  ? 1542 ARG A N     1 
ATOM   731   C  CA    . ARG A 1 1542 ? 130.834 197.550 153.715 1.00 31.35  ? 1542 ARG A CA    1 
ATOM   732   C  C     . ARG A 1 1542 ? 130.394 196.141 154.090 1.00 33.80  ? 1542 ARG A C     1 
ATOM   733   O  O     . ARG A 1 1542 ? 129.992 195.351 153.229 1.00 35.77  ? 1542 ARG A O     1 
ATOM   734   C  CB    . ARG A 1 1542 ? 132.358 197.626 153.614 1.00 32.38  ? 1542 ARG A CB    1 
ATOM   735   C  CG    . ARG A 1 1542 ? 132.968 196.556 152.723 1.00 39.46  ? 1542 ARG A CG    1 
ATOM   736   C  CD    . ARG A 1 1542 ? 134.464 196.758 152.554 1.00 40.19  ? 1542 ARG A CD    1 
ATOM   737   N  NE    . ARG A 1 1542 ? 135.126 197.019 153.826 1.00 40.59  ? 1542 ARG A NE    1 
ATOM   738   C  CZ    . ARG A 1 1542 ? 135.407 196.089 154.729 1.00 43.95  ? 1542 ARG A CZ    1 
ATOM   739   N  NH1   . ARG A 1 1542 ? 135.107 194.817 154.528 1.00 40.92  ? 1542 ARG A NH1   1 
ATOM   740   N  NH2   . ARG A 1 1542 ? 136.007 196.445 155.861 1.00 41.66  ? 1542 ARG A NH2   1 
ATOM   741   N  N     . ARG A 1 1543 ? 130.465 195.812 155.381 1.00 34.36  ? 1543 ARG A N     1 
ATOM   742   C  CA    . ARG A 1 1543 ? 130.032 194.498 155.843 1.00 30.00  ? 1543 ARG A CA    1 
ATOM   743   C  C     . ARG A 1 1543 ? 128.548 194.285 155.575 1.00 32.22  ? 1543 ARG A C     1 
ATOM   744   O  O     . ARG A 1 1543 ? 128.125 193.194 155.177 1.00 34.52  ? 1543 ARG A O     1 
ATOM   745   C  CB    . ARG A 1 1543 ? 130.341 194.341 157.333 1.00 30.84  ? 1543 ARG A CB    1 
ATOM   746   C  CG    . ARG A 1 1543 ? 130.755 192.938 157.739 1.00 35.01  ? 1543 ARG A CG    1 
ATOM   747   C  CD    . ARG A 1 1543 ? 131.557 192.950 159.029 1.00 41.41  ? 1543 ARG A CD    1 
ATOM   748   N  NE    . ARG A 1 1543 ? 132.809 193.682 158.882 1.00 46.70  ? 1543 ARG A NE    1 
ATOM   749   C  CZ    . ARG A 1 1543 ? 133.982 193.116 158.636 1.00 48.15  ? 1543 ARG A CZ    1 
ATOM   750   N  NH1   . ARG A 1 1543 ? 134.103 191.805 158.507 1.00 49.26  ? 1543 ARG A NH1   1 
ATOM   751   N  NH2   . ARG A 1 1543 ? 135.061 193.884 158.516 1.00 45.79  ? 1543 ARG A NH2   1 
ATOM   752   N  N     . TRP A 1 1544 ? 127.740 195.325 155.788 1.00 32.86  ? 1544 TRP A N     1 
ATOM   753   C  CA    . TRP A 1 1544 ? 126.302 195.203 155.575 1.00 31.75  ? 1544 TRP A CA    1 
ATOM   754   C  C     . TRP A 1 1544 ? 125.968 195.018 154.099 1.00 33.50  ? 1544 TRP A C     1 
ATOM   755   O  O     . TRP A 1 1544 ? 124.987 194.347 153.759 1.00 38.86  ? 1544 TRP A O     1 
ATOM   756   C  CB    . TRP A 1 1544 ? 125.585 196.431 156.136 1.00 36.37  ? 1544 TRP A CB    1 
ATOM   757   C  CG    . TRP A 1 1544 ? 124.098 196.389 155.965 1.00 37.37  ? 1544 TRP A CG    1 
ATOM   758   C  CD1   . TRP A 1 1544 ? 123.196 195.779 156.787 1.00 34.69  ? 1544 TRP A CD1   1 
ATOM   759   C  CD2   . TRP A 1 1544 ? 123.338 196.982 154.906 1.00 36.17  ? 1544 TRP A CD2   1 
ATOM   760   N  NE1   . TRP A 1 1544 ? 121.922 195.955 156.305 1.00 38.45  ? 1544 TRP A NE1   1 
ATOM   761   C  CE2   . TRP A 1 1544 ? 121.982 196.690 155.151 1.00 35.54  ? 1544 TRP A CE2   1 
ATOM   762   C  CE3   . TRP A 1 1544 ? 123.674 197.731 153.774 1.00 38.75  ? 1544 TRP A CE3   1 
ATOM   763   C  CZ2   . TRP A 1 1544 ? 120.962 197.121 154.307 1.00 40.18  ? 1544 TRP A CZ2   1 
ATOM   764   C  CZ3   . TRP A 1 1544 ? 122.660 198.157 152.937 1.00 41.70  ? 1544 TRP A CZ3   1 
ATOM   765   C  CH2   . TRP A 1 1544 ? 121.320 197.851 153.207 1.00 46.03  ? 1544 TRP A CH2   1 
ATOM   766   N  N     . VAL A 1 1545 ? 126.770 195.608 153.207 1.00 32.55  ? 1545 VAL A N     1 
ATOM   767   C  CA    . VAL A 1 1545 ? 126.454 195.580 151.777 1.00 31.85  ? 1545 VAL A CA    1 
ATOM   768   C  C     . VAL A 1 1545 ? 126.483 194.153 151.245 1.00 35.41  ? 1545 VAL A C     1 
ATOM   769   O  O     . VAL A 1 1545 ? 125.535 193.690 150.599 1.00 43.89  ? 1545 VAL A O     1 
ATOM   770   C  CB    . VAL A 1 1545 ? 127.419 196.484 150.991 1.00 35.72  ? 1545 VAL A CB    1 
ATOM   771   C  CG1   . VAL A 1 1545 ? 127.277 196.234 149.500 1.00 42.44  ? 1545 VAL A CG1   1 
ATOM   772   C  CG2   . VAL A 1 1545 ? 127.145 197.938 151.298 1.00 35.80  ? 1545 VAL A CG2   1 
ATOM   773   N  N     . TYR A 1 1546 ? 127.574 193.429 151.509 1.00 32.34  ? 1546 TYR A N     1 
ATOM   774   C  CA    . TYR A 1 1546 ? 127.681 192.078 150.968 1.00 34.41  ? 1546 TYR A CA    1 
ATOM   775   C  C     . TYR A 1 1546 ? 126.920 191.068 151.816 1.00 32.66  ? 1546 TYR A C     1 
ATOM   776   O  O     . TYR A 1 1546 ? 126.591 189.980 151.332 1.00 40.43  ? 1546 TYR A O     1 
ATOM   777   C  CB    . TYR A 1 1546 ? 129.154 191.683 150.800 1.00 34.10  ? 1546 TYR A CB    1 
ATOM   778   C  CG    . TYR A 1 1546 ? 129.971 191.529 152.069 1.00 30.37  ? 1546 TYR A CG    1 
ATOM   779   C  CD1   . TYR A 1 1546 ? 129.806 190.435 152.909 1.00 32.85  ? 1546 TYR A CD1   1 
ATOM   780   C  CD2   . TYR A 1 1546 ? 130.934 192.470 152.406 1.00 29.46  ? 1546 TYR A CD2   1 
ATOM   781   C  CE1   . TYR A 1 1546 ? 130.562 190.296 154.058 1.00 31.59  ? 1546 TYR A CE1   1 
ATOM   782   C  CE2   . TYR A 1 1546 ? 131.695 192.337 153.551 1.00 28.26  ? 1546 TYR A CE2   1 
ATOM   783   C  CZ    . TYR A 1 1546 ? 131.504 191.250 154.373 1.00 31.77  ? 1546 TYR A CZ    1 
ATOM   784   O  OH    . TYR A 1 1546 ? 132.261 191.116 155.514 1.00 44.11  ? 1546 TYR A OH    1 
ATOM   785   N  N     . LEU A 1 1547 ? 126.631 191.402 153.074 1.00 33.01  ? 1547 LEU A N     1 
ATOM   786   C  CA    . LEU A 1 1547 ? 125.761 190.544 153.871 1.00 34.61  ? 1547 LEU A CA    1 
ATOM   787   C  C     . LEU A 1 1547 ? 124.308 190.688 153.434 1.00 36.60  ? 1547 LEU A C     1 
ATOM   788   O  O     . LEU A 1 1547 ? 123.544 189.716 153.461 1.00 38.53  ? 1547 LEU A O     1 
ATOM   789   C  CB    . LEU A 1 1547 ? 125.917 190.867 155.356 1.00 31.69  ? 1547 LEU A CB    1 
ATOM   790   C  CG    . LEU A 1 1547 ? 126.967 190.050 156.112 1.00 37.84  ? 1547 LEU A CG    1 
ATOM   791   C  CD1   . LEU A 1 1547 ? 127.325 190.718 157.431 1.00 41.27  ? 1547 LEU A CD1   1 
ATOM   792   C  CD2   . LEU A 1 1547 ? 126.490 188.625 156.336 1.00 38.55  ? 1547 LEU A CD2   1 
ATOM   793   N  N     . GLU A 1 1548 ? 123.909 191.897 153.030 1.00 35.84  ? 1548 GLU A N     1 
ATOM   794   C  CA    . GLU A 1 1548 ? 122.550 192.109 152.541 1.00 38.81  ? 1548 GLU A CA    1 
ATOM   795   C  C     . GLU A 1 1548 ? 122.303 191.341 151.249 1.00 41.62  ? 1548 GLU A C     1 
ATOM   796   O  O     . GLU A 1 1548 ? 121.251 190.716 151.075 1.00 47.53  ? 1548 GLU A O     1 
ATOM   797   C  CB    . GLU A 1 1548 ? 122.292 193.602 152.335 1.00 38.52  ? 1548 GLU A CB    1 
ATOM   798   C  CG    . GLU A 1 1548 ? 120.840 194.009 152.505 1.00 45.77  ? 1548 GLU A CG    1 
ATOM   799   C  CD    . GLU A 1 1548 ? 120.072 193.976 151.200 1.00 54.47  ? 1548 GLU A CD    1 
ATOM   800   O  OE1   . GLU A 1 1548 ? 120.714 193.986 150.129 1.00 53.70  ? 1548 GLU A OE1   1 
ATOM   801   O  OE2   . GLU A 1 1548 ? 118.824 193.938 151.244 1.00 60.00  ? 1548 GLU A OE2   1 
ATOM   802   N  N     . GLY A 1 1549 ? 123.268 191.376 150.327 1.00 37.33  ? 1549 GLY A N     1 
ATOM   803   C  CA    . GLY A 1 1549 ? 123.116 190.671 149.067 1.00 36.18  ? 1549 GLY A CA    1 
ATOM   804   C  C     . GLY A 1 1549 ? 123.115 189.164 149.207 1.00 36.94  ? 1549 GLY A C     1 
ATOM   805   O  O     . GLY A 1 1549 ? 122.710 188.462 148.275 1.00 42.53  ? 1549 GLY A O     1 
ATOM   806   N  N     . ILE A 1 1550 ? 123.556 188.650 150.352 1.00 33.43  ? 1550 ILE A N     1 
ATOM   807   C  CA    . ILE A 1 1550 ? 123.564 187.211 150.576 1.00 36.50  ? 1550 ILE A CA    1 
ATOM   808   C  C     . ILE A 1 1550 ? 122.246 186.726 151.175 1.00 43.11  ? 1550 ILE A C     1 
ATOM   809   O  O     . ILE A 1 1550 ? 121.723 185.688 150.755 1.00 51.17  ? 1550 ILE A O     1 
ATOM   810   C  CB    . ILE A 1 1550 ? 124.760 186.832 151.466 1.00 38.79  ? 1550 ILE A CB    1 
ATOM   811   C  CG1   . ILE A 1 1550 ? 125.982 186.535 150.600 1.00 39.56  ? 1550 ILE A CG1   1 
ATOM   812   C  CG2   . ILE A 1 1550 ? 124.435 185.631 152.345 1.00 38.35  ? 1550 ILE A CG2   1 
ATOM   813   C  CD1   . ILE A 1 1550 ? 127.255 186.384 151.380 1.00 35.75  ? 1550 ILE A CD1   1 
ATOM   814   N  N     . PHE A 1 1551 ? 121.687 187.463 152.131 1.00 45.88  ? 1551 PHE A N     1 
ATOM   815   C  CA    . PHE A 1 1551 ? 120.432 187.096 152.771 1.00 46.60  ? 1551 PHE A CA    1 
ATOM   816   C  C     . PHE A 1 1551 ? 119.213 187.509 151.958 1.00 48.16  ? 1551 PHE A C     1 
ATOM   817   O  O     . PHE A 1 1551 ? 118.088 187.179 152.344 1.00 52.76  ? 1551 PHE A O     1 
ATOM   818   C  CB    . PHE A 1 1551 ? 120.354 187.717 154.169 1.00 40.12  ? 1551 PHE A CB    1 
ATOM   819   C  CG    . PHE A 1 1551 ? 121.245 187.052 155.176 1.00 39.25  ? 1551 PHE A CG    1 
ATOM   820   C  CD1   . PHE A 1 1551 ? 120.942 185.794 155.665 1.00 40.33  ? 1551 PHE A CD1   1 
ATOM   821   C  CD2   . PHE A 1 1551 ? 122.389 187.685 155.632 1.00 38.98  ? 1551 PHE A CD2   1 
ATOM   822   C  CE1   . PHE A 1 1551 ? 121.762 185.179 156.591 1.00 47.38  ? 1551 PHE A CE1   1 
ATOM   823   C  CE2   . PHE A 1 1551 ? 123.212 187.076 156.557 1.00 36.02  ? 1551 PHE A CE2   1 
ATOM   824   C  CZ    . PHE A 1 1551 ? 122.898 185.821 157.037 1.00 43.14  ? 1551 PHE A CZ    1 
ATOM   825   N  N     . THR A 1 1552 ? 119.407 188.218 150.849 1.00 45.09  ? 1552 THR A N     1 
ATOM   826   C  CA    . THR A 1 1552 ? 118.311 188.641 149.987 1.00 54.28  ? 1552 THR A CA    1 
ATOM   827   C  C     . THR A 1 1552 ? 118.411 188.050 148.590 1.00 59.51  ? 1552 THR A C     1 
ATOM   828   O  O     . THR A 1 1552 ? 117.405 187.576 148.049 1.00 64.79  ? 1552 THR A O     1 
ATOM   829   C  CB    . THR A 1 1552 ? 118.266 190.176 149.903 1.00 54.66  ? 1552 THR A CB    1 
ATOM   830   O  OG1   . THR A 1 1552 ? 118.307 190.729 151.224 1.00 54.47  ? 1552 THR A OG1   1 
ATOM   831   C  CG2   . THR A 1 1552 ? 116.994 190.636 149.207 1.00 55.33  ? 1552 THR A CG2   1 
ATOM   832   N  N     . GLY A 1 1553 ? 119.602 188.066 147.988 1.00 57.18  ? 1553 GLY A N     1 
ATOM   833   C  CA    . GLY A 1 1553 ? 119.760 187.503 146.658 1.00 56.89  ? 1553 GLY A CA    1 
ATOM   834   C  C     . GLY A 1 1553 ? 119.561 186.002 146.610 1.00 62.16  ? 1553 GLY A C     1 
ATOM   835   O  O     . GLY A 1 1553 ? 118.997 185.480 145.644 1.00 62.03  ? 1553 GLY A O     1 
ATOM   836   N  N     . SER A 1 1554 ? 120.013 185.291 147.638 1.00 62.53  ? 1554 SER A N     1 
ATOM   837   C  CA    . SER A 1 1554 ? 119.910 183.839 147.698 1.00 69.81  ? 1554 SER A CA    1 
ATOM   838   C  C     . SER A 1 1554 ? 118.664 183.443 148.480 1.00 76.10  ? 1554 SER A C     1 
ATOM   839   O  O     . SER A 1 1554 ? 118.301 184.106 149.457 1.00 74.76  ? 1554 SER A O     1 
ATOM   840   C  CB    . SER A 1 1554 ? 121.154 183.231 148.346 1.00 69.93  ? 1554 SER A CB    1 
ATOM   841   O  OG    . SER A 1 1554 ? 121.279 183.645 149.696 1.00 71.65  ? 1554 SER A OG    1 
ATOM   842   N  N     . ALA A 1 1555 ? 118.014 182.364 148.046 1.00 79.36  ? 1555 ALA A N     1 
ATOM   843   C  CA    . ALA A 1 1555 ? 116.813 181.870 148.704 1.00 85.18  ? 1555 ALA A CA    1 
ATOM   844   C  C     . ALA A 1 1555 ? 117.058 180.647 149.576 1.00 87.90  ? 1555 ALA A C     1 
ATOM   845   O  O     . ALA A 1 1555 ? 116.262 180.387 150.486 1.00 90.34  ? 1555 ALA A O     1 
ATOM   846   C  CB    . ALA A 1 1555 ? 115.736 181.534 147.665 1.00 79.01  ? 1555 ALA A CB    1 
ATOM   847   N  N     . ASP A 1 1556 ? 118.129 179.892 149.325 1.00 89.35  ? 1556 ASP A N     1 
ATOM   848   C  CA    . ASP A 1 1556 ? 118.373 178.669 150.081 1.00 92.52  ? 1556 ASP A CA    1 
ATOM   849   C  C     . ASP A 1 1556 ? 118.879 178.940 151.492 1.00 90.58  ? 1556 ASP A C     1 
ATOM   850   O  O     . ASP A 1 1556 ? 118.775 178.058 152.351 1.00 87.18  ? 1556 ASP A O     1 
ATOM   851   C  CB    . ASP A 1 1556 ? 119.375 177.783 149.339 1.00 93.37  ? 1556 ASP A CB    1 
ATOM   852   C  CG    . ASP A 1 1556 ? 118.745 177.036 148.180 1.00 99.89  ? 1556 ASP A CG    1 
ATOM   853   O  OD1   . ASP A 1 1556 ? 117.767 177.552 147.599 1.00 97.97  ? 1556 ASP A OD1   1 
ATOM   854   O  OD2   . ASP A 1 1556 ? 119.228 175.933 147.850 1.00 102.45 ? 1556 ASP A OD2   1 
ATOM   855   N  N     . ILE A 1 1557 ? 119.423 180.131 151.752 1.00 87.69  ? 1557 ILE A N     1 
ATOM   856   C  CA    . ILE A 1 1557 ? 120.011 180.396 153.061 1.00 80.27  ? 1557 ILE A CA    1 
ATOM   857   C  C     . ILE A 1 1557 ? 118.932 180.559 154.126 1.00 79.15  ? 1557 ILE A C     1 
ATOM   858   O  O     . ILE A 1 1557 ? 119.183 180.309 155.312 1.00 80.39  ? 1557 ILE A O     1 
ATOM   859   C  CB    . ILE A 1 1557 ? 120.938 181.626 152.991 1.00 69.65  ? 1557 ILE A CB    1 
ATOM   860   C  CG1   . ILE A 1 1557 ? 121.870 181.660 154.204 1.00 65.54  ? 1557 ILE A CG1   1 
ATOM   861   C  CG2   . ILE A 1 1557 ? 120.133 182.914 152.890 1.00 62.12  ? 1557 ILE A CG2   1 
ATOM   862   C  CD1   . ILE A 1 1557 ? 122.895 182.769 154.156 1.00 55.27  ? 1557 ILE A CD1   1 
ATOM   863   N  N     . LYS A 1 1558 ? 117.723 180.973 153.737 1.00 77.91  ? 1558 LYS A N     1 
ATOM   864   C  CA    . LYS A 1 1558 ? 116.663 181.152 154.725 1.00 81.00  ? 1558 LYS A CA    1 
ATOM   865   C  C     . LYS A 1 1558 ? 116.217 179.815 155.307 1.00 86.74  ? 1558 LYS A C     1 
ATOM   866   O  O     . LYS A 1 1558 ? 115.910 179.725 156.502 1.00 80.84  ? 1558 LYS A O     1 
ATOM   867   C  CB    . LYS A 1 1558 ? 115.486 181.915 154.109 1.00 83.25  ? 1558 LYS A CB    1 
ATOM   868   C  CG    . LYS A 1 1558 ? 114.617 181.118 153.149 1.00 89.02  ? 1558 LYS A CG    1 
ATOM   869   C  CD    . LYS A 1 1558 ? 113.678 182.027 152.373 1.00 90.79  ? 1558 LYS A CD    1 
ATOM   870   C  CE    . LYS A 1 1558 ? 112.477 182.430 153.214 1.00 90.40  ? 1558 LYS A CE    1 
ATOM   871   N  NZ    . LYS A 1 1558 ? 111.251 182.603 152.387 1.00 83.97  ? 1558 LYS A NZ    1 
ATOM   872   N  N     . HIS A 1 1559 ? 116.171 178.764 154.484 1.00 89.43  ? 1559 HIS A N     1 
ATOM   873   C  CA    . HIS A 1 1559 ? 115.870 177.434 155.002 1.00 86.49  ? 1559 HIS A CA    1 
ATOM   874   C  C     . HIS A 1 1559 ? 117.080 176.817 155.694 1.00 84.26  ? 1559 HIS A C     1 
ATOM   875   O  O     . HIS A 1 1559 ? 116.936 176.155 156.727 1.00 82.97  ? 1559 HIS A O     1 
ATOM   876   C  CB    . HIS A 1 1559 ? 115.384 176.522 153.874 1.00 86.63  ? 1559 HIS A CB    1 
ATOM   877   C  CG    . HIS A 1 1559 ? 114.511 177.210 152.871 1.00 95.91  ? 1559 HIS A CG    1 
ATOM   878   N  ND1   . HIS A 1 1559 ? 115.017 177.883 151.780 1.00 99.35  ? 1559 HIS A ND1   1 
ATOM   879   C  CD2   . HIS A 1 1559 ? 113.164 177.324 152.791 1.00 98.95  ? 1559 HIS A CD2   1 
ATOM   880   C  CE1   . HIS A 1 1559 ? 114.020 178.384 151.072 1.00 98.67  ? 1559 HIS A CE1   1 
ATOM   881   N  NE2   . HIS A 1 1559 ? 112.885 178.059 151.665 1.00 103.15 ? 1559 HIS A NE2   1 
ATOM   882   N  N     . LEU A 1 1560 ? 118.276 177.026 155.139 1.00 84.98  ? 1560 LEU A N     1 
ATOM   883   C  CA    . LEU A 1 1560 ? 119.474 176.407 155.699 1.00 84.45  ? 1560 LEU A CA    1 
ATOM   884   C  C     . LEU A 1 1560 ? 119.877 177.056 157.016 1.00 82.46  ? 1560 LEU A C     1 
ATOM   885   O  O     . LEU A 1 1560 ? 120.211 176.359 157.981 1.00 79.32  ? 1560 LEU A O     1 
ATOM   886   C  CB    . LEU A 1 1560 ? 120.622 176.489 154.695 1.00 79.91  ? 1560 LEU A CB    1 
ATOM   887   C  CG    . LEU A 1 1560 ? 121.683 175.393 154.791 1.00 78.94  ? 1560 LEU A CG    1 
ATOM   888   C  CD1   . LEU A 1 1560 ? 121.064 174.020 154.583 1.00 75.63  ? 1560 LEU A CD1   1 
ATOM   889   C  CD2   . LEU A 1 1560 ? 122.796 175.646 153.791 1.00 72.58  ? 1560 LEU A CD2   1 
ATOM   890   N  N     . LEU A 1 1561 ? 119.853 178.384 157.077 1.00 80.07  ? 1561 LEU A N     1 
ATOM   891   C  CA    . LEU A 1 1561 ? 120.328 179.130 158.243 1.00 79.72  ? 1561 LEU A CA    1 
ATOM   892   C  C     . LEU A 1 1561 ? 119.249 180.116 158.664 1.00 82.23  ? 1561 LEU A C     1 
ATOM   893   O  O     . LEU A 1 1561 ? 119.372 181.329 158.453 1.00 80.42  ? 1561 LEU A O     1 
ATOM   894   C  CB    . LEU A 1 1561 ? 121.646 179.842 157.928 1.00 77.48  ? 1561 LEU A CB    1 
ATOM   895   C  CG    . LEU A 1 1561 ? 122.828 178.910 157.652 1.00 76.13  ? 1561 LEU A CG    1 
ATOM   896   C  CD1   . LEU A 1 1561 ? 124.054 179.685 157.196 1.00 67.28  ? 1561 LEU A CD1   1 
ATOM   897   C  CD2   . LEU A 1 1561 ? 123.149 178.078 158.884 1.00 77.62  ? 1561 LEU A CD2   1 
ATOM   898   N  N     . PRO A 1 1562 ? 118.165 179.625 159.273 1.00 84.15  ? 1562 PRO A N     1 
ATOM   899   C  CA    . PRO A 1 1562 ? 117.037 180.507 159.599 1.00 80.20  ? 1562 PRO A CA    1 
ATOM   900   C  C     . PRO A 1 1562 ? 117.282 181.363 160.831 1.00 78.04  ? 1562 PRO A C     1 
ATOM   901   O  O     . PRO A 1 1562 ? 116.753 182.475 160.933 1.00 73.96  ? 1562 PRO A O     1 
ATOM   902   C  CB    . PRO A 1 1562 ? 115.878 179.524 159.834 1.00 81.99  ? 1562 PRO A CB    1 
ATOM   903   C  CG    . PRO A 1 1562 ? 116.385 178.173 159.376 1.00 79.89  ? 1562 PRO A CG    1 
ATOM   904   C  CD    . PRO A 1 1562 ? 117.859 178.222 159.587 1.00 82.49  ? 1562 PRO A CD    1 
ATOM   905   N  N     . VAL A 1 1563 ? 118.075 180.852 161.775 1.00 79.15  ? 1563 VAL A N     1 
ATOM   906   C  CA    . VAL A 1 1563 ? 118.218 181.519 163.066 1.00 79.87  ? 1563 VAL A CA    1 
ATOM   907   C  C     . VAL A 1 1563 ? 118.919 182.865 162.910 1.00 78.59  ? 1563 VAL A C     1 
ATOM   908   O  O     . VAL A 1 1563 ? 118.453 183.885 163.431 1.00 76.42  ? 1563 VAL A O     1 
ATOM   909   C  CB    . VAL A 1 1563 ? 118.941 180.601 164.072 1.00 79.98  ? 1563 VAL A CB    1 
ATOM   910   C  CG1   . VAL A 1 1563 ? 120.271 180.106 163.517 1.00 76.82  ? 1563 VAL A CG1   1 
ATOM   911   C  CG2   . VAL A 1 1563 ? 119.146 181.326 165.395 1.00 71.03  ? 1563 VAL A CG2   1 
ATOM   912   N  N     . GLU A 1 1564 ? 120.038 182.899 162.184 1.00 76.86  ? 1564 GLU A N     1 
ATOM   913   C  CA    . GLU A 1 1564 ? 120.749 184.161 162.020 1.00 75.97  ? 1564 GLU A CA    1 
ATOM   914   C  C     . GLU A 1 1564 ? 120.335 184.922 160.767 1.00 72.10  ? 1564 GLU A C     1 
ATOM   915   O  O     . GLU A 1 1564 ? 120.796 186.051 160.571 1.00 67.14  ? 1564 GLU A O     1 
ATOM   916   C  CB    . GLU A 1 1564 ? 122.265 183.933 162.030 1.00 74.90  ? 1564 GLU A CB    1 
ATOM   917   C  CG    . GLU A 1 1564 ? 122.888 183.556 160.701 1.00 73.76  ? 1564 GLU A CG    1 
ATOM   918   C  CD    . GLU A 1 1564 ? 122.799 182.073 160.411 1.00 79.31  ? 1564 GLU A CD    1 
ATOM   919   O  OE1   . GLU A 1 1564 ? 121.879 181.408 160.931 1.00 81.55  ? 1564 GLU A OE1   1 
ATOM   920   O  OE2   . GLU A 1 1564 ? 123.671 181.568 159.678 1.00 76.57  ? 1564 GLU A OE2   1 
ATOM   921   N  N     . THR A 1 1565 ? 119.482 184.341 159.919 1.00 68.71  ? 1565 THR A N     1 
ATOM   922   C  CA    . THR A 1 1565 ? 118.801 185.148 158.911 1.00 63.82  ? 1565 THR A CA    1 
ATOM   923   C  C     . THR A 1 1565 ? 117.866 186.148 159.577 1.00 64.42  ? 1565 THR A C     1 
ATOM   924   O  O     . THR A 1 1565 ? 117.820 187.324 159.194 1.00 64.18  ? 1565 THR A O     1 
ATOM   925   C  CB    . THR A 1 1565 ? 118.034 184.248 157.940 1.00 67.85  ? 1565 THR A CB    1 
ATOM   926   O  OG1   . THR A 1 1565 ? 118.932 183.735 156.949 1.00 71.26  ? 1565 THR A OG1   1 
ATOM   927   C  CG2   . THR A 1 1565 ? 116.920 185.020 157.247 1.00 62.69  ? 1565 THR A CG2   1 
ATOM   928   N  N     . GLN A 1 1566 ? 117.122 185.699 160.592 1.00 66.95  ? 1566 GLN A N     1 
ATOM   929   C  CA    . GLN A 1 1566 ? 116.319 186.618 161.391 1.00 69.26  ? 1566 GLN A CA    1 
ATOM   930   C  C     . GLN A 1 1566 ? 117.203 187.571 162.185 1.00 65.43  ? 1566 GLN A C     1 
ATOM   931   O  O     . GLN A 1 1566 ? 116.860 188.746 162.355 1.00 61.31  ? 1566 GLN A O     1 
ATOM   932   C  CB    . GLN A 1 1566 ? 115.396 185.837 162.325 1.00 74.11  ? 1566 GLN A CB    1 
ATOM   933   C  CG    . GLN A 1 1566 ? 114.337 185.017 161.608 1.00 79.46  ? 1566 GLN A CG    1 
ATOM   934   C  CD    . GLN A 1 1566 ? 113.382 185.876 160.803 1.00 82.10  ? 1566 GLN A CD    1 
ATOM   935   O  OE1   . GLN A 1 1566 ? 113.408 185.867 159.572 1.00 80.61  ? 1566 GLN A OE1   1 
ATOM   936   N  NE2   . GLN A 1 1566 ? 112.533 186.626 161.495 1.00 79.09  ? 1566 GLN A NE2   1 
ATOM   937   N  N     . ARG A 1 1567 ? 118.340 187.079 162.688 1.00 63.45  ? 1567 ARG A N     1 
ATOM   938   C  CA    . ARG A 1 1567 ? 119.277 187.954 163.387 1.00 59.35  ? 1567 ARG A CA    1 
ATOM   939   C  C     . ARG A 1 1567 ? 119.768 189.065 162.470 1.00 61.08  ? 1567 ARG A C     1 
ATOM   940   O  O     . ARG A 1 1567 ? 119.858 190.227 162.879 1.00 62.42  ? 1567 ARG A O     1 
ATOM   941   C  CB    . ARG A 1 1567 ? 120.459 187.148 163.927 1.00 62.88  ? 1567 ARG A CB    1 
ATOM   942   C  CG    . ARG A 1 1567 ? 120.111 186.159 165.025 1.00 67.65  ? 1567 ARG A CG    1 
ATOM   943   C  CD    . ARG A 1 1567 ? 121.338 185.832 165.866 1.00 66.29  ? 1567 ARG A CD    1 
ATOM   944   N  NE    . ARG A 1 1567 ? 121.134 184.672 166.727 1.00 79.67  ? 1567 ARG A NE    1 
ATOM   945   C  CZ    . ARG A 1 1567 ? 120.364 184.659 167.806 1.00 87.39  ? 1567 ARG A CZ    1 
ATOM   946   N  NH1   . ARG A 1 1567 ? 119.709 185.739 168.202 1.00 87.18  ? 1567 ARG A NH1   1 
ATOM   947   N  NH2   . ARG A 1 1567 ? 120.252 183.537 168.510 1.00 86.03  ? 1567 ARG A NH2   1 
ATOM   948   N  N     . PHE A 1 1568 ? 120.088 188.725 161.217 1.00 61.20  ? 1568 PHE A N     1 
ATOM   949   C  CA    . PHE A 1 1568 ? 120.510 189.752 160.271 1.00 55.29  ? 1568 PHE A CA    1 
ATOM   950   C  C     . PHE A 1 1568 ? 119.383 190.725 159.958 1.00 55.06  ? 1568 PHE A C     1 
ATOM   951   O  O     . PHE A 1 1568 ? 119.635 191.921 159.780 1.00 55.68  ? 1568 PHE A O     1 
ATOM   952   C  CB    . PHE A 1 1568 ? 121.029 189.126 158.979 1.00 50.10  ? 1568 PHE A CB    1 
ATOM   953   C  CG    . PHE A 1 1568 ? 121.451 190.141 157.955 1.00 46.34  ? 1568 PHE A CG    1 
ATOM   954   C  CD1   . PHE A 1 1568 ? 122.655 190.812 158.083 1.00 41.19  ? 1568 PHE A CD1   1 
ATOM   955   C  CD2   . PHE A 1 1568 ? 120.636 190.436 156.874 1.00 40.08  ? 1568 PHE A CD2   1 
ATOM   956   C  CE1   . PHE A 1 1568 ? 123.042 191.753 157.151 1.00 40.43  ? 1568 PHE A CE1   1 
ATOM   957   C  CE2   . PHE A 1 1568 ? 121.019 191.376 155.937 1.00 41.06  ? 1568 PHE A CE2   1 
ATOM   958   C  CZ    . PHE A 1 1568 ? 122.224 192.035 156.076 1.00 43.38  ? 1568 PHE A CZ    1 
ATOM   959   N  N     . GLN A 1 1569 ? 118.144 190.238 159.878 1.00 53.84  ? 1569 GLN A N     1 
ATOM   960   C  CA    . GLN A 1 1569 ? 117.021 191.132 159.619 1.00 56.05  ? 1569 GLN A CA    1 
ATOM   961   C  C     . GLN A 1 1569 ? 116.850 192.136 160.753 1.00 61.19  ? 1569 GLN A C     1 
ATOM   962   O  O     . GLN A 1 1569 ? 116.475 193.291 160.519 1.00 61.67  ? 1569 GLN A O     1 
ATOM   963   C  CB    . GLN A 1 1569 ? 115.742 190.319 159.416 1.00 58.25  ? 1569 GLN A CB    1 
ATOM   964   C  CG    . GLN A 1 1569 ? 114.522 191.150 159.060 1.00 61.80  ? 1569 GLN A CG    1 
ATOM   965   C  CD    . GLN A 1 1569 ? 114.686 191.888 157.746 1.00 68.99  ? 1569 GLN A CD    1 
ATOM   966   O  OE1   . GLN A 1 1569 ? 114.911 193.099 157.723 1.00 63.48  ? 1569 GLN A OE1   1 
ATOM   967   N  NE2   . GLN A 1 1569 ? 114.576 191.160 156.640 1.00 67.96  ? 1569 GLN A NE2   1 
ATOM   968   N  N     . SER A 1 1570 ? 117.118 191.711 161.990 1.00 64.82  ? 1570 SER A N     1 
ATOM   969   C  CA    . SER A 1 1570 ? 117.006 192.617 163.128 1.00 60.09  ? 1570 SER A CA    1 
ATOM   970   C  C     . SER A 1 1570 ? 118.064 193.713 163.070 1.00 58.27  ? 1570 SER A C     1 
ATOM   971   O  O     . SER A 1 1570 ? 117.747 194.903 163.187 1.00 61.25  ? 1570 SER A O     1 
ATOM   972   C  CB    . SER A 1 1570 ? 117.117 191.828 164.434 1.00 63.24  ? 1570 SER A CB    1 
ATOM   973   O  OG    . SER A 1 1570 ? 116.329 190.652 164.386 1.00 64.02  ? 1570 SER A OG    1 
ATOM   974   N  N     . ILE A 1 1571 ? 119.331 193.333 162.884 1.00 56.78  ? 1571 ILE A N     1 
ATOM   975   C  CA    . ILE A 1 1571 ? 120.394 194.333 162.824 1.00 55.70  ? 1571 ILE A CA    1 
ATOM   976   C  C     . ILE A 1 1571 ? 120.253 195.191 161.574 1.00 54.15  ? 1571 ILE A C     1 
ATOM   977   O  O     . ILE A 1 1571 ? 120.531 196.396 161.606 1.00 54.26  ? 1571 ILE A O     1 
ATOM   978   C  CB    . ILE A 1 1571 ? 121.781 193.664 162.904 1.00 53.35  ? 1571 ILE A CB    1 
ATOM   979   C  CG1   . ILE A 1 1571 ? 122.885 194.649 162.521 1.00 55.27  ? 1571 ILE A CG1   1 
ATOM   980   C  CG2   . ILE A 1 1571 ? 121.860 192.471 161.995 1.00 50.82  ? 1571 ILE A CG2   1 
ATOM   981   C  CD1   . ILE A 1 1571 ? 124.228 194.316 163.117 1.00 53.30  ? 1571 ILE A CD1   1 
ATOM   982   N  N     . SER A 1 1572 ? 119.815 194.598 160.459 1.00 51.98  ? 1572 SER A N     1 
ATOM   983   C  CA    . SER A 1 1572 ? 119.588 195.387 159.253 1.00 51.16  ? 1572 SER A CA    1 
ATOM   984   C  C     . SER A 1 1572 ? 118.565 196.486 159.503 1.00 58.28  ? 1572 SER A C     1 
ATOM   985   O  O     . SER A 1 1572 ? 118.825 197.657 159.210 1.00 61.14  ? 1572 SER A O     1 
ATOM   986   C  CB    . SER A 1 1572 ? 119.137 194.484 158.106 1.00 50.67  ? 1572 SER A CB    1 
ATOM   987   O  OG    . SER A 1 1572 ? 119.059 195.203 156.889 1.00 50.70  ? 1572 SER A OG    1 
ATOM   988   N  N     . THR A 1 1573 ? 117.414 196.135 160.087 1.00 59.99  ? 1573 THR A N     1 
ATOM   989   C  CA    . THR A 1 1573 ? 116.388 197.135 160.372 1.00 56.87  ? 1573 THR A CA    1 
ATOM   990   C  C     . THR A 1 1573 ? 116.945 198.273 161.219 1.00 58.59  ? 1573 THR A C     1 
ATOM   991   O  O     . THR A 1 1573 ? 116.546 199.432 161.057 1.00 60.28  ? 1573 THR A O     1 
ATOM   992   C  CB    . THR A 1 1573 ? 115.194 196.483 161.071 1.00 56.56  ? 1573 THR A CB    1 
ATOM   993   O  OG1   . THR A 1 1573 ? 115.658 195.455 161.955 1.00 61.78  ? 1573 THR A OG1   1 
ATOM   994   C  CG2   . THR A 1 1573 ? 114.245 195.878 160.048 1.00 52.43  ? 1573 THR A CG2   1 
ATOM   995   N  N     . GLU A 1 1574 ? 117.869 197.959 162.130 1.00 57.82  ? 1574 GLU A N     1 
ATOM   996   C  CA    . GLU A 1 1574 ? 118.566 199.008 162.865 1.00 56.36  ? 1574 GLU A CA    1 
ATOM   997   C  C     . GLU A 1 1574 ? 119.440 199.843 161.937 1.00 57.07  ? 1574 GLU A C     1 
ATOM   998   O  O     . GLU A 1 1574 ? 119.565 201.060 162.118 1.00 62.26  ? 1574 GLU A O     1 
ATOM   999   C  CB    . GLU A 1 1574 ? 119.406 198.393 163.985 1.00 58.04  ? 1574 GLU A CB    1 
ATOM   1000  C  CG    . GLU A 1 1574 ? 118.625 197.479 164.914 1.00 63.40  ? 1574 GLU A CG    1 
ATOM   1001  C  CD    . GLU A 1 1574 ? 119.406 197.106 166.158 1.00 71.16  ? 1574 GLU A CD    1 
ATOM   1002  O  OE1   . GLU A 1 1574 ? 120.646 197.258 166.151 1.00 71.49  ? 1574 GLU A OE1   1 
ATOM   1003  O  OE2   . GLU A 1 1574 ? 118.780 196.657 167.141 1.00 71.82  ? 1574 GLU A OE2   1 
ATOM   1004  N  N     . PHE A 1 1575 ? 120.060 199.205 160.940 1.00 58.05  ? 1575 PHE A N     1 
ATOM   1005  C  CA    . PHE A 1 1575 ? 120.959 199.925 160.043 1.00 51.38  ? 1575 PHE A CA    1 
ATOM   1006  C  C     . PHE A 1 1575 ? 120.195 200.890 159.141 1.00 53.22  ? 1575 PHE A C     1 
ATOM   1007  O  O     . PHE A 1 1575 ? 120.606 202.044 158.975 1.00 57.74  ? 1575 PHE A O     1 
ATOM   1008  C  CB    . PHE A 1 1575 ? 121.776 198.936 159.212 1.00 42.28  ? 1575 PHE A CB    1 
ATOM   1009  C  CG    . PHE A 1 1575 ? 122.834 199.584 158.366 1.00 43.67  ? 1575 PHE A CG    1 
ATOM   1010  C  CD1   . PHE A 1 1575 ? 124.045 199.961 158.922 1.00 45.95  ? 1575 PHE A CD1   1 
ATOM   1011  C  CD2   . PHE A 1 1575 ? 122.621 199.815 157.018 1.00 44.54  ? 1575 PHE A CD2   1 
ATOM   1012  C  CE1   . PHE A 1 1575 ? 125.023 200.559 158.151 1.00 38.19  ? 1575 PHE A CE1   1 
ATOM   1013  C  CE2   . PHE A 1 1575 ? 123.596 200.411 156.240 1.00 46.33  ? 1575 PHE A CE2   1 
ATOM   1014  C  CZ    . PHE A 1 1575 ? 124.798 200.784 156.808 1.00 42.23  ? 1575 PHE A CZ    1 
ATOM   1015  N  N     . LEU A 1 1576 ? 119.086 200.439 158.545 1.00 54.55  ? 1576 LEU A N     1 
ATOM   1016  C  CA    . LEU A 1 1576 ? 118.271 201.348 157.741 1.00 57.99  ? 1576 LEU A CA    1 
ATOM   1017  C  C     . LEU A 1 1576 ? 117.696 202.474 158.590 1.00 59.44  ? 1576 LEU A C     1 
ATOM   1018  O  O     . LEU A 1 1576 ? 117.602 203.618 158.129 1.00 59.08  ? 1576 LEU A O     1 
ATOM   1019  C  CB    . LEU A 1 1576 ? 117.142 200.598 157.024 1.00 61.35  ? 1576 LEU A CB    1 
ATOM   1020  C  CG    . LEU A 1 1576 ? 117.375 199.542 155.931 1.00 56.50  ? 1576 LEU A CG    1 
ATOM   1021  C  CD1   . LEU A 1 1576 ? 118.159 200.140 154.781 1.00 53.43  ? 1576 LEU A CD1   1 
ATOM   1022  C  CD2   . LEU A 1 1576 ? 118.030 198.267 156.408 1.00 51.56  ? 1576 LEU A CD2   1 
ATOM   1023  N  N     . ALA A 1 1577 ? 117.354 202.164 159.843 1.00 59.69  ? 1577 ALA A N     1 
ATOM   1024  C  CA    . ALA A 1 1577 ? 116.876 203.224 160.761 1.00 62.07  ? 1577 ALA A CA    1 
ATOM   1025  C  C     . ALA A 1 1577 ? 117.975 204.279 160.908 1.00 62.80  ? 1577 ALA A C     1 
ATOM   1026  O  O     . ALA A 1 1577 ? 117.703 205.480 160.696 1.00 62.95  ? 1577 ALA A O     1 
ATOM   1027  C  CB    . ALA A 1 1577 ? 116.505 202.621 162.096 1.00 58.47  ? 1577 ALA A CB    1 
ATOM   1028  N  N     . LEU A 1 1578 ? 119.190 203.838 161.242 1.00 58.22  ? 1578 LEU A N     1 
ATOM   1029  C  CA    . LEU A 1 1578 ? 120.329 204.778 161.406 1.00 56.60  ? 1578 LEU A CA    1 
ATOM   1030  C  C     . LEU A 1 1578 ? 120.557 205.542 160.092 1.00 55.17  ? 1578 LEU A C     1 
ATOM   1031  O  O     . LEU A 1 1578 ? 120.755 206.774 160.153 1.00 58.19  ? 1578 LEU A O     1 
ATOM   1032  C  CB    . LEU A 1 1578 ? 121.571 203.992 161.820 1.00 53.93  ? 1578 LEU A CB    1 
ATOM   1033  C  CG    . LEU A 1 1578 ? 122.898 204.754 161.755 1.00 56.03  ? 1578 LEU A CG    1 
ATOM   1034  C  CD1   . LEU A 1 1578 ? 122.937 205.886 162.767 1.00 56.73  ? 1578 LEU A CD1   1 
ATOM   1035  C  CD2   . LEU A 1 1578 ? 124.075 203.815 161.948 1.00 56.03  ? 1578 LEU A CD2   1 
ATOM   1036  N  N     . MET A 1 1579 ? 120.523 204.840 158.956 1.00 54.32  ? 1579 MET A N     1 
ATOM   1037  C  CA    . MET A 1 1579 ? 120.806 205.491 157.650 1.00 57.94  ? 1579 MET A CA    1 
ATOM   1038  C  C     . MET A 1 1579 ? 119.767 206.593 157.381 1.00 59.17  ? 1579 MET A C     1 
ATOM   1039  O  O     . MET A 1 1579 ? 120.171 207.686 156.933 1.00 61.53  ? 1579 MET A O     1 
ATOM   1040  C  CB    . MET A 1 1579 ? 120.790 204.471 156.506 1.00 56.86  ? 1579 MET A CB    1 
ATOM   1041  C  CG    . MET A 1 1579 ? 121.856 203.400 156.630 1.00 58.19  ? 1579 MET A CG    1 
ATOM   1042  S  SD    . MET A 1 1579 ? 123.467 204.070 157.089 1.00 65.84  ? 1579 MET A SD    1 
ATOM   1043  C  CE    . MET A 1 1579 ? 123.845 205.087 155.655 1.00 52.70  ? 1579 MET A CE    1 
ATOM   1044  N  N     . LYS A 1 1580 ? 118.487 206.311 157.642 1.00 59.50  ? 1580 LYS A N     1 
ATOM   1045  C  CA    . LYS A 1 1580 ? 117.417 207.309 157.381 1.00 60.85  ? 1580 LYS A CA    1 
ATOM   1046  C  C     . LYS A 1 1580 ? 117.643 208.523 158.298 1.00 65.31  ? 1580 LYS A C     1 
ATOM   1047  O  O     . LYS A 1 1580 ? 117.418 209.662 157.837 1.00 64.60  ? 1580 LYS A O     1 
ATOM   1048  C  CB    . LYS A 1 1580 ? 116.022 206.699 157.570 1.00 58.39  ? 1580 LYS A CB    1 
ATOM   1049  C  CG    . LYS A 1 1580 ? 115.588 206.463 159.008 1.00 60.66  ? 1580 LYS A CG    1 
ATOM   1050  C  CD    . LYS A 1 1580 ? 114.286 205.680 159.122 1.00 65.96  ? 1580 LYS A CD    1 
ATOM   1051  C  CE    . LYS A 1 1580 ? 114.370 204.342 158.460 1.00 72.04  ? 1580 LYS A CE    1 
ATOM   1052  N  NZ    . LYS A 1 1580 ? 113.131 203.578 158.622 1.00 68.70  ? 1580 LYS A NZ    1 
ATOM   1053  N  N     . LYS A 1 1581 ? 118.074 208.284 159.541 1.00 65.71  ? 1581 LYS A N     1 
ATOM   1054  C  CA    . LYS A 1 1581 ? 118.376 209.405 160.469 1.00 63.37  ? 1581 LYS A CA    1 
ATOM   1055  C  C     . LYS A 1 1581 ? 119.502 210.252 159.860 1.00 62.27  ? 1581 LYS A C     1 
ATOM   1056  O  O     . LYS A 1 1581 ? 119.368 211.495 159.841 1.00 67.25  ? 1581 LYS A O     1 
ATOM   1057  C  CB    . LYS A 1 1581 ? 118.791 208.880 161.847 1.00 58.80  ? 1581 LYS A CB    1 
ATOM   1058  C  CG    . LYS A 1 1581 ? 117.786 207.958 162.520 1.00 56.89  ? 1581 LYS A CG    1 
ATOM   1059  C  CD    . LYS A 1 1581 ? 118.225 207.525 163.913 1.00 58.79  ? 1581 LYS A CD    1 
ATOM   1060  C  CE    . LYS A 1 1581 ? 119.599 206.937 163.917 1.00 57.87  ? 1581 LYS A CE    1 
ATOM   1061  N  NZ    . LYS A 1 1581 ? 119.997 206.493 165.255 1.00 52.85  ? 1581 LYS A NZ    1 
ATOM   1062  N  N     . VAL A 1 1582 ? 120.559 209.597 159.372 1.00 63.82  ? 1582 VAL A N     1 
ATOM   1063  C  CA    . VAL A 1 1582 ? 121.685 210.329 158.718 1.00 63.77  ? 1582 VAL A CA    1 
ATOM   1064  C  C     . VAL A 1 1582 ? 121.125 211.066 157.493 1.00 67.83  ? 1582 VAL A C     1 
ATOM   1065  O  O     . VAL A 1 1582 ? 121.552 212.214 157.245 1.00 73.41  ? 1582 VAL A O     1 
ATOM   1066  C  CB    . VAL A 1 1582 ? 122.819 209.366 158.322 1.00 57.35  ? 1582 VAL A CB    1 
ATOM   1067  C  CG1   . VAL A 1 1582 ? 123.936 210.080 157.571 1.00 58.77  ? 1582 VAL A CG1   1 
ATOM   1068  C  CG2   . VAL A 1 1582 ? 123.371 208.617 159.529 1.00 56.22  ? 1582 VAL A CG2   1 
ATOM   1069  N  N     . SER A 1 1583 ? 120.206 210.427 156.765 1.00 66.43  ? 1583 SER A N     1 
ATOM   1070  C  CA    . SER A 1 1583 ? 119.591 211.062 155.571 1.00 68.75  ? 1583 SER A CA    1 
ATOM   1071  C  C     . SER A 1 1583 ? 118.847 212.338 155.991 1.00 75.59  ? 1583 SER A C     1 
ATOM   1072  O  O     . SER A 1 1583 ? 119.106 213.398 155.382 1.00 72.44  ? 1583 SER A O     1 
ATOM   1073  C  CB    . SER A 1 1583 ? 118.674 210.104 154.856 1.00 68.61  ? 1583 SER A CB    1 
ATOM   1074  O  OG    . SER A 1 1583 ? 118.133 210.699 153.686 1.00 73.60  ? 1583 SER A OG    1 
ATOM   1075  N  N     . LYS A 1 1584 ? 117.964 212.238 156.991 1.00 78.43  ? 1584 LYS A N     1 
ATOM   1076  C  CA    . LYS A 1 1584 ? 117.195 213.403 157.416 1.00 76.40  ? 1584 LYS A CA    1 
ATOM   1077  C  C     . LYS A 1 1584 ? 118.105 214.604 157.650 1.00 73.15  ? 1584 LYS A C     1 
ATOM   1078  O  O     . LYS A 1 1584 ? 117.807 215.720 157.209 1.00 75.33  ? 1584 LYS A O     1 
ATOM   1079  C  CB    . LYS A 1 1584 ? 116.406 213.077 158.686 1.00 72.23  ? 1584 LYS A CB    1 
ATOM   1080  C  CG    . LYS A 1 1584 ? 115.366 211.976 158.530 1.00 76.42  ? 1584 LYS A CG    1 
ATOM   1081  C  CD    . LYS A 1 1584 ? 114.187 212.422 157.680 1.00 79.80  ? 1584 LYS A CD    1 
ATOM   1082  C  CE    . LYS A 1 1584 ? 113.152 211.313 157.551 1.00 72.55  ? 1584 LYS A CE    1 
ATOM   1083  N  NZ    . LYS A 1 1584 ? 112.772 210.748 158.876 1.00 63.46  ? 1584 LYS A NZ    1 
ATOM   1084  N  N     . SER A 1 1585 ? 119.223 214.391 158.344 1.00 71.05  ? 1585 SER A N     1 
ATOM   1085  C  CA    . SER A 1 1585 ? 120.188 215.446 158.648 1.00 74.00  ? 1585 SER A CA    1 
ATOM   1086  C  C     . SER A 1 1585 ? 121.574 214.965 158.244 1.00 74.19  ? 1585 SER A C     1 
ATOM   1087  O  O     . SER A 1 1585 ? 122.272 214.309 159.031 1.00 72.22  ? 1585 SER A O     1 
ATOM   1088  C  CB    . SER A 1 1585 ? 120.140 215.828 160.126 1.00 75.83  ? 1585 SER A CB    1 
ATOM   1089  O  OG    . SER A 1 1585 ? 120.343 214.697 160.955 1.00 79.36  ? 1585 SER A OG    1 
ATOM   1090  N  N     . PRO A 1 1586 ? 122.010 215.271 157.022 1.00 71.75  ? 1586 PRO A N     1 
ATOM   1091  C  CA    . PRO A 1 1586 ? 123.317 214.801 156.546 1.00 70.95  ? 1586 PRO A CA    1 
ATOM   1092  C  C     . PRO A 1 1586 ? 124.513 215.550 157.114 1.00 73.98  ? 1586 PRO A C     1 
ATOM   1093  O  O     . PRO A 1 1586 ? 125.635 215.307 156.663 1.00 71.03  ? 1586 PRO A O     1 
ATOM   1094  C  CB    . PRO A 1 1586 ? 123.214 215.016 155.028 1.00 70.94  ? 1586 PRO A CB    1 
ATOM   1095  C  CG    . PRO A 1 1586 ? 122.289 216.167 154.884 1.00 69.40  ? 1586 PRO A CG    1 
ATOM   1096  C  CD    . PRO A 1 1586 ? 121.286 216.041 155.995 1.00 69.13  ? 1586 PRO A CD    1 
ATOM   1097  N  N     . LEU A 1 1587 ? 124.314 216.448 158.075 1.00 78.42  ? 1587 LEU A N     1 
ATOM   1098  C  CA    . LEU A 1 1587 ? 125.434 217.156 158.680 1.00 77.02  ? 1587 LEU A CA    1 
ATOM   1099  C  C     . LEU A 1 1587 ? 126.303 216.196 159.484 1.00 74.87  ? 1587 LEU A C     1 
ATOM   1100  O  O     . LEU A 1 1587 ? 125.798 215.340 160.216 1.00 77.43  ? 1587 LEU A O     1 
ATOM   1101  C  CB    . LEU A 1 1587 ? 124.929 218.285 159.578 1.00 80.09  ? 1587 LEU A CB    1 
ATOM   1102  C  CG    . LEU A 1 1587 ? 125.838 219.508 159.717 1.00 84.37  ? 1587 LEU A CG    1 
ATOM   1103  C  CD1   . LEU A 1 1587 ? 126.171 220.092 158.352 1.00 82.90  ? 1587 LEU A CD1   1 
ATOM   1104  C  CD2   . LEU A 1 1587 ? 125.197 220.557 160.613 1.00 76.30  ? 1587 LEU A CD2   1 
ATOM   1105  N  N     . VAL A 1 1588 ? 127.622 216.343 159.341 1.00 76.21  ? 1588 VAL A N     1 
ATOM   1106  C  CA    . VAL A 1 1588 ? 128.550 215.469 160.051 1.00 75.94  ? 1588 VAL A CA    1 
ATOM   1107  C  C     . VAL A 1 1588 ? 128.449 215.683 161.556 1.00 77.32  ? 1588 VAL A C     1 
ATOM   1108  O  O     . VAL A 1 1588 ? 128.419 214.721 162.333 1.00 73.89  ? 1588 VAL A O     1 
ATOM   1109  C  CB    . VAL A 1 1588 ? 129.986 215.690 159.545 1.00 71.50  ? 1588 VAL A CB    1 
ATOM   1110  C  CG1   . VAL A 1 1588 ? 130.846 214.477 159.850 1.00 63.30  ? 1588 VAL A CG1   1 
ATOM   1111  C  CG2   . VAL A 1 1588 ? 129.981 215.979 158.056 1.00 71.00  ? 1588 VAL A CG2   1 
ATOM   1112  N  N     . MET A 1 1589 ? 128.403 216.944 161.992 1.00 77.52  ? 1589 MET A N     1 
ATOM   1113  C  CA    . MET A 1 1589 ? 128.278 217.227 163.418 1.00 79.07  ? 1589 MET A CA    1 
ATOM   1114  C  C     . MET A 1 1589 ? 126.944 216.736 163.965 1.00 78.37  ? 1589 MET A C     1 
ATOM   1115  O  O     . MET A 1 1589 ? 126.877 216.235 165.093 1.00 82.80  ? 1589 MET A O     1 
ATOM   1116  C  CB    . MET A 1 1589 ? 128.443 218.725 163.675 1.00 82.96  ? 1589 MET A CB    1 
ATOM   1117  C  CG    . MET A 1 1589 ? 129.660 219.342 163.005 1.00 88.03  ? 1589 MET A CG    1 
ATOM   1118  S  SD    . MET A 1 1589 ? 131.218 218.932 163.817 1.00 99.71  ? 1589 MET A SD    1 
ATOM   1119  C  CE    . MET A 1 1589 ? 130.711 218.841 165.534 1.00 81.61  ? 1589 MET A CE    1 
ATOM   1120  N  N     . ASP A 1 1590 ? 125.871 216.875 163.183 1.00 75.59  ? 1590 ASP A N     1 
ATOM   1121  C  CA    . ASP A 1 1590 ? 124.571 216.380 163.625 1.00 75.23  ? 1590 ASP A CA    1 
ATOM   1122  C  C     . ASP A 1 1590 ? 124.583 214.863 163.768 1.00 73.30  ? 1590 ASP A C     1 
ATOM   1123  O  O     . ASP A 1 1590 ? 123.965 214.314 164.687 1.00 74.42  ? 1590 ASP A O     1 
ATOM   1124  C  CB    . ASP A 1 1590 ? 123.477 216.833 162.659 1.00 76.44  ? 1590 ASP A CB    1 
ATOM   1125  C  CG    . ASP A 1 1590 ? 122.183 217.176 163.370 1.00 80.52  ? 1590 ASP A CG    1 
ATOM   1126  O  OD1   . ASP A 1 1590 ? 121.163 217.400 162.685 1.00 76.35  ? 1590 ASP A OD1   1 
ATOM   1127  O  OD2   . ASP A 1 1590 ? 122.186 217.212 164.618 1.00 81.74  ? 1590 ASP A OD2   1 
ATOM   1128  N  N     . VAL A 1 1591 ? 125.275 214.169 162.861 1.00 72.96  ? 1591 VAL A N     1 
ATOM   1129  C  CA    . VAL A 1 1591 ? 125.435 212.723 162.991 1.00 70.28  ? 1591 VAL A CA    1 
ATOM   1130  C  C     . VAL A 1 1591 ? 126.219 212.386 164.253 1.00 69.25  ? 1591 VAL A C     1 
ATOM   1131  O  O     . VAL A 1 1591 ? 125.866 211.459 164.993 1.00 71.35  ? 1591 VAL A O     1 
ATOM   1132  C  CB    . VAL A 1 1591 ? 126.108 212.145 161.731 1.00 67.89  ? 1591 VAL A CB    1 
ATOM   1133  C  CG1   . VAL A 1 1591 ? 126.563 210.715 161.976 1.00 65.13  ? 1591 VAL A CG1   1 
ATOM   1134  C  CG2   . VAL A 1 1591 ? 125.158 212.209 160.546 1.00 64.96  ? 1591 VAL A CG2   1 
ATOM   1135  N  N     . LEU A 1 1592 ? 127.291 213.137 164.522 1.00 68.45  ? 1592 LEU A N     1 
ATOM   1136  C  CA    . LEU A 1 1592 ? 128.082 212.900 165.726 1.00 69.86  ? 1592 LEU A CA    1 
ATOM   1137  C  C     . LEU A 1 1592 ? 127.277 213.142 166.995 1.00 74.28  ? 1592 LEU A C     1 
ATOM   1138  O  O     . LEU A 1 1592 ? 127.561 212.533 168.032 1.00 72.06  ? 1592 LEU A O     1 
ATOM   1139  C  CB    . LEU A 1 1592 ? 129.326 213.788 165.727 1.00 64.40  ? 1592 LEU A CB    1 
ATOM   1140  C  CG    . LEU A 1 1592 ? 130.461 213.318 166.641 1.00 62.58  ? 1592 LEU A CG    1 
ATOM   1141  C  CD1   . LEU A 1 1592 ? 130.716 211.828 166.468 1.00 61.16  ? 1592 LEU A CD1   1 
ATOM   1142  C  CD2   . LEU A 1 1592 ? 131.728 214.124 166.412 1.00 58.12  ? 1592 LEU A CD2   1 
ATOM   1143  N  N     . ASN A 1 1593 ? 126.276 214.016 166.936 1.00 74.98  ? 1593 ASN A N     1 
ATOM   1144  C  CA    . ASN A 1 1593 ? 125.483 214.366 168.105 1.00 75.35  ? 1593 ASN A CA    1 
ATOM   1145  C  C     . ASN A 1 1593 ? 124.357 213.378 168.377 1.00 73.67  ? 1593 ASN A C     1 
ATOM   1146  O  O     . ASN A 1 1593 ? 123.624 213.553 169.356 1.00 73.77  ? 1593 ASN A O     1 
ATOM   1147  C  CB    . ASN A 1 1593 ? 124.909 215.777 167.947 1.00 77.54  ? 1593 ASN A CB    1 
ATOM   1148  C  CG    . ASN A 1 1593 ? 125.981 216.849 167.994 1.00 78.12  ? 1593 ASN A CG    1 
ATOM   1149  O  OD1   . ASN A 1 1593 ? 127.173 216.549 168.073 1.00 71.73  ? 1593 ASN A OD1   1 
ATOM   1150  N  ND2   . ASN A 1 1593 ? 125.562 218.108 167.946 1.00 82.90  ? 1593 ASN A ND2   1 
ATOM   1151  N  N     . ILE A 1 1594 ? 124.198 212.353 167.536 1.00 71.97  ? 1594 ILE A N     1 
ATOM   1152  C  CA    . ILE A 1 1594 ? 123.212 211.316 167.808 1.00 72.96  ? 1594 ILE A CA    1 
ATOM   1153  C  C     . ILE A 1 1594 ? 123.617 210.565 169.066 1.00 74.58  ? 1594 ILE A C     1 
ATOM   1154  O  O     . ILE A 1 1594 ? 124.771 210.140 169.211 1.00 72.77  ? 1594 ILE A O     1 
ATOM   1155  C  CB    . ILE A 1 1594 ? 123.081 210.372 166.603 1.00 70.02  ? 1594 ILE A CB    1 
ATOM   1156  C  CG1   . ILE A 1 1594 ? 122.528 211.126 165.392 1.00 65.96  ? 1594 ILE A CG1   1 
ATOM   1157  C  CG2   . ILE A 1 1594 ? 122.195 209.183 166.945 1.00 66.27  ? 1594 ILE A CG2   1 
ATOM   1158  C  CD1   . ILE A 1 1594 ? 122.346 210.260 164.165 1.00 58.62  ? 1594 ILE A CD1   1 
ATOM   1159  N  N     . GLN A 1 1595 ? 122.671 210.407 169.988 1.00 76.88  ? 1595 GLN A N     1 
ATOM   1160  C  CA    . GLN A 1 1595 ? 122.971 209.785 171.271 1.00 80.12  ? 1595 GLN A CA    1 
ATOM   1161  C  C     . GLN A 1 1595 ? 123.370 208.326 171.080 1.00 80.92  ? 1595 GLN A C     1 
ATOM   1162  O  O     . GLN A 1 1595 ? 122.716 207.579 170.345 1.00 79.90  ? 1595 GLN A O     1 
ATOM   1163  C  CB    . GLN A 1 1595 ? 121.775 209.900 172.224 1.00 75.58  ? 1595 GLN A CB    1 
ATOM   1164  C  CG    . GLN A 1 1595 ? 120.529 209.075 171.877 1.00 82.17  ? 1595 GLN A CG    1 
ATOM   1165  C  CD    . GLN A 1 1595 ? 120.006 209.320 170.474 1.00 87.19  ? 1595 GLN A CD    1 
ATOM   1166  O  OE1   . GLN A 1 1595 ? 119.795 210.463 170.069 1.00 85.07  ? 1595 GLN A OE1   1 
ATOM   1167  N  NE2   . GLN A 1 1595 ? 119.796 208.244 169.724 1.00 85.35  ? 1595 GLN A NE2   1 
ATOM   1168  N  N     . GLY A 1 1596 ? 124.463 207.931 171.730 1.00 80.81  ? 1596 GLY A N     1 
ATOM   1169  C  CA    . GLY A 1 1596 ? 124.943 206.562 171.646 1.00 76.88  ? 1596 GLY A CA    1 
ATOM   1170  C  C     . GLY A 1 1596 ? 125.286 206.102 170.247 1.00 71.87  ? 1596 GLY A C     1 
ATOM   1171  O  O     . GLY A 1 1596 ? 125.198 204.905 169.958 1.00 72.30  ? 1596 GLY A O     1 
ATOM   1172  N  N     . VAL A 1 1597 ? 125.675 207.025 169.365 1.00 68.61  ? 1597 VAL A N     1 
ATOM   1173  C  CA    . VAL A 1 1597 ? 125.979 206.645 167.988 1.00 65.18  ? 1597 VAL A CA    1 
ATOM   1174  C  C     . VAL A 1 1597 ? 127.275 205.842 167.923 1.00 59.46  ? 1597 VAL A C     1 
ATOM   1175  O  O     . VAL A 1 1597 ? 127.414 204.933 167.095 1.00 63.73  ? 1597 VAL A O     1 
ATOM   1176  C  CB    . VAL A 1 1597 ? 126.010 207.890 167.078 1.00 64.34  ? 1597 VAL A CB    1 
ATOM   1177  C  CG1   . VAL A 1 1597 ? 127.374 208.568 167.091 1.00 61.91  ? 1597 VAL A CG1   1 
ATOM   1178  C  CG2   . VAL A 1 1597 ? 125.612 207.515 165.659 1.00 56.69  ? 1597 VAL A CG2   1 
ATOM   1179  N  N     . GLN A 1 1598 ? 128.243 206.158 168.787 1.00 57.16  ? 1598 GLN A N     1 
ATOM   1180  C  CA    . GLN A 1 1598 ? 129.490 205.399 168.808 1.00 59.31  ? 1598 GLN A CA    1 
ATOM   1181  C  C     . GLN A 1 1598 ? 129.259 203.986 169.329 1.00 65.24  ? 1598 GLN A C     1 
ATOM   1182  O  O     . GLN A 1 1598 ? 129.791 203.014 168.781 1.00 66.23  ? 1598 GLN A O     1 
ATOM   1183  C  CB    . GLN A 1 1598 ? 130.534 206.127 169.655 1.00 57.98  ? 1598 GLN A CB    1 
ATOM   1184  C  CG    . GLN A 1 1598 ? 131.908 205.476 169.639 1.00 60.63  ? 1598 GLN A CG    1 
ATOM   1185  C  CD    . GLN A 1 1598 ? 132.685 205.781 168.373 1.00 62.10  ? 1598 GLN A CD    1 
ATOM   1186  O  OE1   . GLN A 1 1598 ? 133.005 206.935 168.089 1.00 57.16  ? 1598 GLN A OE1   1 
ATOM   1187  N  NE2   . GLN A 1 1598 ? 132.994 204.743 167.604 1.00 61.80  ? 1598 GLN A NE2   1 
ATOM   1188  N  N     . ARG A 1 1599 ? 128.467 203.856 170.396 1.00 64.58  ? 1599 ARG A N     1 
ATOM   1189  C  CA    . ARG A 1 1599 ? 128.148 202.534 170.924 1.00 64.00  ? 1599 ARG A CA    1 
ATOM   1190  C  C     . ARG A 1 1599 ? 127.305 201.735 169.940 1.00 64.23  ? 1599 ARG A C     1 
ATOM   1191  O  O     . ARG A 1 1599 ? 127.491 200.521 169.793 1.00 65.34  ? 1599 ARG A O     1 
ATOM   1192  C  CB    . ARG A 1 1599 ? 127.424 202.662 172.263 1.00 67.73  ? 1599 ARG A CB    1 
ATOM   1193  C  CG    . ARG A 1 1599 ? 127.371 201.372 173.063 1.00 68.70  ? 1599 ARG A CG    1 
ATOM   1194  C  CD    . ARG A 1 1599 ? 126.086 201.282 173.867 1.00 72.13  ? 1599 ARG A CD    1 
ATOM   1195  N  NE    . ARG A 1 1599 ? 125.025 200.622 173.116 1.00 79.26  ? 1599 ARG A NE    1 
ATOM   1196  C  CZ    . ARG A 1 1599 ? 124.048 201.258 172.484 1.00 80.96  ? 1599 ARG A CZ    1 
ATOM   1197  N  NH1   . ARG A 1 1599 ? 123.964 202.578 172.490 1.00 80.06  ? 1599 ARG A NH1   1 
ATOM   1198  N  NH2   . ARG A 1 1599 ? 123.132 200.551 171.827 1.00 74.55  ? 1599 ARG A NH2   1 
ATOM   1199  N  N     . SER A 1 1600 ? 126.363 202.398 169.264 1.00 62.78  ? 1600 SER A N     1 
ATOM   1200  C  CA    . SER A 1 1600 ? 125.510 201.702 168.307 1.00 61.16  ? 1600 SER A CA    1 
ATOM   1201  C  C     . SER A 1 1600 ? 126.326 201.132 167.154 1.00 59.43  ? 1600 SER A C     1 
ATOM   1202  O  O     . SER A 1 1600 ? 126.101 199.993 166.730 1.00 62.34  ? 1600 SER A O     1 
ATOM   1203  C  CB    . SER A 1 1600 ? 124.428 202.645 167.782 1.00 62.61  ? 1600 SER A CB    1 
ATOM   1204  O  OG    . SER A 1 1600 ? 123.821 203.365 168.841 1.00 67.27  ? 1600 SER A OG    1 
ATOM   1205  N  N     . LEU A 1 1601 ? 127.281 201.908 166.636 1.00 59.12  ? 1601 LEU A N     1 
ATOM   1206  C  CA    . LEU A 1 1601 ? 128.094 201.432 165.522 1.00 57.56  ? 1601 LEU A CA    1 
ATOM   1207  C  C     . LEU A 1 1601 ? 128.944 200.235 165.929 1.00 58.61  ? 1601 LEU A C     1 
ATOM   1208  O  O     . LEU A 1 1601 ? 129.059 199.260 165.177 1.00 56.35  ? 1601 LEU A O     1 
ATOM   1209  C  CB    . LEU A 1 1601 ? 128.983 202.558 164.995 1.00 55.24  ? 1601 LEU A CB    1 
ATOM   1210  C  CG    . LEU A 1 1601 ? 128.453 203.370 163.813 1.00 50.93  ? 1601 LEU A CG    1 
ATOM   1211  C  CD1   . LEU A 1 1601 ? 128.762 202.660 162.512 1.00 46.06  ? 1601 LEU A CD1   1 
ATOM   1212  C  CD2   . LEU A 1 1601 ? 126.968 203.639 163.938 1.00 52.30  ? 1601 LEU A CD2   1 
ATOM   1213  N  N     . GLU A 1 1602 ? 129.550 200.295 167.117 1.00 56.62  ? 1602 GLU A N     1 
ATOM   1214  C  CA    . GLU A 1 1602 ? 130.368 199.184 167.589 1.00 55.60  ? 1602 GLU A CA    1 
ATOM   1215  C  C     . GLU A 1 1602 ? 129.525 197.934 167.810 1.00 59.02  ? 1602 GLU A C     1 
ATOM   1216  O  O     . GLU A 1 1602 ? 129.972 196.817 167.523 1.00 62.29  ? 1602 GLU A O     1 
ATOM   1217  C  CB    . GLU A 1 1602 ? 131.097 199.581 168.871 1.00 58.93  ? 1602 GLU A CB    1 
ATOM   1218  C  CG    . GLU A 1 1602 ? 132.267 200.525 168.644 1.00 59.73  ? 1602 GLU A CG    1 
ATOM   1219  C  CD    . GLU A 1 1602 ? 132.991 200.876 169.928 1.00 68.89  ? 1602 GLU A CD    1 
ATOM   1220  O  OE1   . GLU A 1 1602 ? 133.136 202.082 170.219 1.00 67.88  ? 1602 GLU A OE1   1 
ATOM   1221  O  OE2   . GLU A 1 1602 ? 133.413 199.947 170.648 1.00 72.54  ? 1602 GLU A OE2   1 
ATOM   1222  N  N     . ARG A 1 1603 ? 128.305 198.100 168.326 1.00 55.03  ? 1603 ARG A N     1 
ATOM   1223  C  CA    . ARG A 1 1603 ? 127.415 196.956 168.488 1.00 56.18  ? 1603 ARG A CA    1 
ATOM   1224  C  C     . ARG A 1 1603 ? 127.007 196.385 167.136 1.00 59.79  ? 1603 ARG A C     1 
ATOM   1225  O  O     . ARG A 1 1603 ? 126.886 195.164 166.983 1.00 61.25  ? 1603 ARG A O     1 
ATOM   1226  C  CB    . ARG A 1 1603 ? 126.183 197.350 169.301 1.00 63.56  ? 1603 ARG A CB    1 
ATOM   1227  C  CG    . ARG A 1 1603 ? 125.400 196.163 169.841 1.00 64.73  ? 1603 ARG A CG    1 
ATOM   1228  C  CD    . ARG A 1 1603 ? 124.138 196.605 170.561 1.00 65.30  ? 1603 ARG A CD    1 
ATOM   1229  N  NE    . ARG A 1 1603 ? 123.357 197.548 169.770 1.00 68.53  ? 1603 ARG A NE    1 
ATOM   1230  C  CZ    . ARG A 1 1603 ? 122.412 197.197 168.910 1.00 68.84  ? 1603 ARG A CZ    1 
ATOM   1231  N  NH1   . ARG A 1 1603 ? 122.103 195.928 168.702 1.00 66.19  ? 1603 ARG A NH1   1 
ATOM   1232  N  NH2   . ARG A 1 1603 ? 121.757 198.144 168.243 1.00 73.43  ? 1603 ARG A NH2   1 
ATOM   1233  N  N     . LEU A 1 1604 ? 126.782 197.253 166.146 1.00 62.14  ? 1604 LEU A N     1 
ATOM   1234  C  CA    . LEU A 1 1604 ? 126.511 196.775 164.795 1.00 59.10  ? 1604 LEU A CA    1 
ATOM   1235  C  C     . LEU A 1 1604 ? 127.706 196.010 164.239 1.00 55.70  ? 1604 LEU A C     1 
ATOM   1236  O  O     . LEU A 1 1604 ? 127.544 194.945 163.632 1.00 54.99  ? 1604 LEU A O     1 
ATOM   1237  C  CB    . LEU A 1 1604 ? 126.158 197.947 163.878 1.00 54.28  ? 1604 LEU A CB    1 
ATOM   1238  C  CG    . LEU A 1 1604 ? 124.856 198.709 164.139 1.00 55.51  ? 1604 LEU A CG    1 
ATOM   1239  C  CD1   . LEU A 1 1604 ? 124.747 199.911 163.212 1.00 52.91  ? 1604 LEU A CD1   1 
ATOM   1240  C  CD2   . LEU A 1 1604 ? 123.646 197.810 163.994 1.00 56.64  ? 1604 LEU A CD2   1 
ATOM   1241  N  N     . ALA A 1 1605 ? 128.916 196.539 164.442 1.00 50.93  ? 1605 ALA A N     1 
ATOM   1242  C  CA    . ALA A 1 1605 ? 130.116 195.863 163.957 1.00 49.54  ? 1605 ALA A CA    1 
ATOM   1243  C  C     . ALA A 1 1605 ? 130.312 194.519 164.644 1.00 53.19  ? 1605 ALA A C     1 
ATOM   1244  O  O     . ALA A 1 1605 ? 130.668 193.528 163.995 1.00 53.27  ? 1605 ALA A O     1 
ATOM   1245  C  CB    . ALA A 1 1605 ? 131.340 196.754 164.166 1.00 47.94  ? 1605 ALA A CB    1 
ATOM   1246  N  N     . ASP A 1 1606 ? 130.094 194.467 165.959 1.00 57.45  ? 1606 ASP A N     1 
ATOM   1247  C  CA    . ASP A 1 1606 ? 130.255 193.215 166.692 1.00 59.98  ? 1606 ASP A CA    1 
ATOM   1248  C  C     . ASP A 1 1606 ? 129.244 192.174 166.228 1.00 55.96  ? 1606 ASP A C     1 
ATOM   1249  O  O     . ASP A 1 1606 ? 129.585 191.000 166.040 1.00 56.42  ? 1606 ASP A O     1 
ATOM   1250  C  CB    . ASP A 1 1606 ? 130.120 193.464 168.193 1.00 62.26  ? 1606 ASP A CB    1 
ATOM   1251  C  CG    . ASP A 1 1606 ? 131.423 193.900 168.831 1.00 72.19  ? 1606 ASP A CG    1 
ATOM   1252  O  OD1   . ASP A 1 1606 ? 132.420 194.065 168.098 1.00 73.52  ? 1606 ASP A OD1   1 
ATOM   1253  O  OD2   . ASP A 1 1606 ? 131.450 194.076 170.068 1.00 77.87  ? 1606 ASP A OD2   1 
ATOM   1254  N  N     . LEU A 1 1607 ? 127.988 192.585 166.044 1.00 53.28  ? 1607 LEU A N     1 
ATOM   1255  C  CA    . LEU A 1 1607 ? 126.963 191.644 165.604 1.00 54.13  ? 1607 LEU A CA    1 
ATOM   1256  C  C     . LEU A 1 1607 ? 127.216 191.175 164.176 1.00 53.69  ? 1607 LEU A C     1 
ATOM   1257  O  O     . LEU A 1 1607 ? 127.127 189.976 163.892 1.00 53.17  ? 1607 LEU A O     1 
ATOM   1258  C  CB    . LEU A 1 1607 ? 125.573 192.271 165.727 1.00 56.83  ? 1607 LEU A CB    1 
ATOM   1259  C  CG    . LEU A 1 1607 ? 124.823 192.192 167.064 1.00 54.71  ? 1607 LEU A CG    1 
ATOM   1260  C  CD1   . LEU A 1 1607 ? 125.751 192.283 168.268 1.00 51.86  ? 1607 LEU A CD1   1 
ATOM   1261  C  CD2   . LEU A 1 1607 ? 123.748 193.268 167.134 1.00 61.08  ? 1607 LEU A CD2   1 
ATOM   1262  N  N     . LEU A 1 1608 ? 127.547 192.098 163.268 1.00 55.37  ? 1608 LEU A N     1 
ATOM   1263  C  CA    . LEU A 1 1608 ? 127.811 191.711 161.884 1.00 50.08  ? 1608 LEU A CA    1 
ATOM   1264  C  C     . LEU A 1 1608 ? 128.948 190.700 161.800 1.00 48.63  ? 1608 LEU A C     1 
ATOM   1265  O  O     . LEU A 1 1608 ? 128.937 189.814 160.939 1.00 52.16  ? 1608 LEU A O     1 
ATOM   1266  C  CB    . LEU A 1 1608 ? 128.128 192.944 161.037 1.00 44.57  ? 1608 LEU A CB    1 
ATOM   1267  C  CG    . LEU A 1 1608 ? 126.964 193.869 160.675 1.00 44.42  ? 1608 LEU A CG    1 
ATOM   1268  C  CD1   . LEU A 1 1608 ? 127.433 194.984 159.754 1.00 37.04  ? 1608 LEU A CD1   1 
ATOM   1269  C  CD2   . LEU A 1 1608 ? 125.829 193.086 160.034 1.00 45.40  ? 1608 LEU A CD2   1 
ATOM   1270  N  N     . GLY A 1 1609 ? 129.939 190.817 162.686 1.00 43.15  ? 1609 GLY A N     1 
ATOM   1271  C  CA    . GLY A 1 1609 ? 131.008 189.833 162.714 1.00 49.09  ? 1609 GLY A CA    1 
ATOM   1272  C  C     . GLY A 1 1609 ? 130.518 188.447 163.088 1.00 54.67  ? 1609 GLY A C     1 
ATOM   1273  O  O     . GLY A 1 1609 ? 130.971 187.446 162.527 1.00 56.00  ? 1609 GLY A O     1 
ATOM   1274  N  N     . LYS A 1 1610 ? 129.589 188.369 164.045 1.00 54.38  ? 1610 LYS A N     1 
ATOM   1275  C  CA    . LYS A 1 1610 ? 129.071 187.072 164.470 1.00 53.04  ? 1610 LYS A CA    1 
ATOM   1276  C  C     . LYS A 1 1610 ? 128.286 186.388 163.356 1.00 50.81  ? 1610 LYS A C     1 
ATOM   1277  O  O     . LYS A 1 1610 ? 128.447 185.184 163.125 1.00 53.31  ? 1610 LYS A O     1 
ATOM   1278  C  CB    . LYS A 1 1610 ? 128.208 187.241 165.721 1.00 52.46  ? 1610 LYS A CB    1 
ATOM   1279  C  CG    . LYS A 1 1610 ? 128.939 187.903 166.880 1.00 51.42  ? 1610 LYS A CG    1 
ATOM   1280  C  CD    . LYS A 1 1610 ? 128.170 187.780 168.187 1.00 59.70  ? 1610 LYS A CD    1 
ATOM   1281  C  CE    . LYS A 1 1610 ? 126.674 187.954 167.980 1.00 62.48  ? 1610 LYS A CE    1 
ATOM   1282  N  NZ    . LYS A 1 1610 ? 126.025 188.602 169.153 1.00 62.78  ? 1610 LYS A NZ    1 
ATOM   1283  N  N     . ILE A 1 1611 ? 127.428 187.135 162.656 1.00 46.08  ? 1611 ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 1611 ? 126.715 186.566 161.513 1.00 48.19  ? 1611 ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 1611 ? 127.690 186.208 160.398 1.00 47.83  ? 1611 ILE A C     1 
ATOM   1286  O  O     . ILE A 1 1611 ? 127.582 185.141 159.780 1.00 50.78  ? 1611 ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 1611 ? 125.599 187.511 161.013 1.00 44.76  ? 1611 ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 1611 ? 124.429 187.658 162.011 1.00 53.34  ? 1611 ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 1611 ? 125.078 187.055 159.657 1.00 43.65  ? 1611 ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 1611 ? 124.728 188.192 163.391 1.00 52.65  ? 1611 ILE A CD1   1 
ATOM   1291  N  N     . GLN A 1 1612 ? 128.659 187.085 160.123 1.00 50.05  ? 1612 GLN A N     1 
ATOM   1292  C  CA    . GLN A 1 1612 ? 129.637 186.795 159.077 1.00 45.08  ? 1612 GLN A CA    1 
ATOM   1293  C  C     . GLN A 1 1612 ? 130.460 185.557 159.417 1.00 46.20  ? 1612 GLN A C     1 
ATOM   1294  O  O     . GLN A 1 1612 ? 130.725 184.720 158.546 1.00 45.61  ? 1612 GLN A O     1 
ATOM   1295  C  CB    . GLN A 1 1612 ? 130.547 188.004 158.855 1.00 42.35  ? 1612 GLN A CB    1 
ATOM   1296  C  CG    . GLN A 1 1612 ? 131.912 187.659 158.286 1.00 50.15  ? 1612 GLN A CG    1 
ATOM   1297  C  CD    . GLN A 1 1612 ? 132.753 188.884 158.000 1.00 49.71  ? 1612 GLN A CD    1 
ATOM   1298  O  OE1   . GLN A 1 1612 ? 132.250 190.006 157.992 1.00 48.30  ? 1612 GLN A OE1   1 
ATOM   1299  N  NE2   . GLN A 1 1612 ? 134.042 188.676 157.766 1.00 47.98  ? 1612 GLN A NE2   1 
ATOM   1300  N  N     . LYS A 1 1613 ? 130.869 185.421 160.680 1.00 51.01  ? 1613 LYS A N     1 
ATOM   1301  C  CA    . LYS A 1 1613 ? 131.593 184.229 161.101 1.00 52.37  ? 1613 LYS A CA    1 
ATOM   1302  C  C     . LYS A 1 1613 ? 130.718 182.982 161.083 1.00 48.33  ? 1613 LYS A C     1 
ATOM   1303  O  O     . LYS A 1 1613 ? 131.251 181.868 161.066 1.00 50.37  ? 1613 LYS A O     1 
ATOM   1304  C  CB    . LYS A 1 1613 ? 132.175 184.431 162.501 1.00 51.20  ? 1613 LYS A CB    1 
ATOM   1305  C  CG    . LYS A 1 1613 ? 133.681 184.632 162.527 1.00 58.76  ? 1613 LYS A CG    1 
ATOM   1306  C  CD    . LYS A 1 1613 ? 134.059 186.048 162.132 1.00 62.02  ? 1613 LYS A CD    1 
ATOM   1307  C  CE    . LYS A 1 1613 ? 135.482 186.373 162.554 1.00 65.34  ? 1613 LYS A CE    1 
ATOM   1308  N  NZ    . LYS A 1 1613 ? 135.624 186.425 164.036 1.00 67.57  ? 1613 LYS A NZ    1 
ATOM   1309  N  N     . ALA A 1 1614 ? 129.394 183.141 161.084 1.00 47.16  ? 1614 ALA A N     1 
ATOM   1310  C  CA    . ALA A 1 1614 ? 128.462 182.020 161.095 1.00 46.15  ? 1614 ALA A CA    1 
ATOM   1311  C  C     . ALA A 1 1614 ? 127.929 181.694 159.704 1.00 45.55  ? 1614 ALA A C     1 
ATOM   1312  O  O     . ALA A 1 1614 ? 126.809 181.190 159.570 1.00 47.98  ? 1614 ALA A O     1 
ATOM   1313  C  CB    . ALA A 1 1614 ? 127.305 182.301 162.054 1.00 46.10  ? 1614 ALA A CB    1 
ATOM   1314  N  N     . LEU A 1 1615 ? 128.712 181.976 158.662 1.00 45.28  ? 1615 LEU A N     1 
ATOM   1315  C  CA    . LEU A 1 1615 ? 128.320 181.690 157.287 1.00 44.33  ? 1615 LEU A CA    1 
ATOM   1316  C  C     . LEU A 1 1615 ? 129.293 180.716 156.633 1.00 44.89  ? 1615 LEU A C     1 
ATOM   1317  O  O     . LEU A 1 1615 ? 129.353 180.618 155.405 1.00 47.37  ? 1615 LEU A O     1 
ATOM   1318  C  CB    . LEU A 1 1615 ? 128.222 182.978 156.469 1.00 42.87  ? 1615 LEU A CB    1 
ATOM   1319  C  CG    . LEU A 1 1615 ? 126.968 183.833 156.671 1.00 36.97  ? 1615 LEU A CG    1 
ATOM   1320  C  CD1   . LEU A 1 1615 ? 126.819 184.848 155.550 1.00 36.91  ? 1615 LEU A CD1   1 
ATOM   1321  C  CD2   . LEU A 1 1615 ? 125.728 182.961 156.770 1.00 45.94  ? 1615 LEU A CD2   1 
ATOM   1322  N  N     . GLY A 1 1616 ? 130.063 179.989 157.446 1.00 44.34  ? 1616 GLY A N     1 
ATOM   1323  C  CA    . GLY A 1 1616 ? 131.064 179.088 156.897 1.00 41.20  ? 1616 GLY A CA    1 
ATOM   1324  C  C     . GLY A 1 1616 ? 130.465 177.934 156.114 1.00 43.33  ? 1616 GLY A C     1 
ATOM   1325  O  O     . GLY A 1 1616 ? 130.969 177.571 155.048 1.00 49.42  ? 1616 GLY A O     1 
ATOM   1326  N  N     . GLU A 1 1617 ? 129.391 177.335 156.635 1.00 43.11  ? 1617 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1617 ? 128.765 176.210 155.944 1.00 47.41  ? 1617 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1617 ? 128.180 176.641 154.605 1.00 43.79  ? 1617 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1617 ? 128.261 175.900 153.619 1.00 47.05  ? 1617 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1617 ? 127.685 175.579 156.825 1.00 51.22  ? 1617 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1617 ? 128.084 175.270 158.275 1.00 52.58  ? 1617 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1617 ? 129.571 175.002 158.476 1.00 61.81  ? 1617 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1617 ? 130.153 175.588 159.412 1.00 63.70  ? 1617 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1617 ? 130.148 174.177 157.734 1.00 62.31  ? 1617 GLU A OE2   1 
ATOM   1335  N  N     . TYR A 1 1618 ? 127.577 177.830 154.555 1.00 39.43  ? 1618 TYR A N     1 
ATOM   1336  C  CA    . TYR A 1 1618 ? 127.068 178.345 153.289 1.00 42.38  ? 1618 TYR A CA    1 
ATOM   1337  C  C     . TYR A 1 1618 ? 128.196 178.563 152.289 1.00 42.98  ? 1618 TYR A C     1 
ATOM   1338  O  O     . TYR A 1 1618 ? 128.046 178.270 151.097 1.00 45.58  ? 1618 TYR A O     1 
ATOM   1339  C  CB    . TYR A 1 1618 ? 126.297 179.643 153.526 1.00 40.75  ? 1618 TYR A CB    1 
ATOM   1340  C  CG    . TYR A 1 1618 ? 125.679 180.222 152.275 1.00 44.28  ? 1618 TYR A CG    1 
ATOM   1341  C  CD1   . TYR A 1 1618 ? 126.199 181.367 151.688 1.00 40.48  ? 1618 TYR A CD1   1 
ATOM   1342  C  CD2   . TYR A 1 1618 ? 124.583 179.618 151.676 1.00 44.88  ? 1618 TYR A CD2   1 
ATOM   1343  C  CE1   . TYR A 1 1618 ? 125.641 181.899 150.544 1.00 45.76  ? 1618 TYR A CE1   1 
ATOM   1344  C  CE2   . TYR A 1 1618 ? 124.017 180.142 150.531 1.00 52.24  ? 1618 TYR A CE2   1 
ATOM   1345  C  CZ    . TYR A 1 1618 ? 124.551 181.282 149.969 1.00 53.81  ? 1618 TYR A CZ    1 
ATOM   1346  O  OH    . TYR A 1 1618 ? 123.993 181.809 148.828 1.00 57.71  ? 1618 TYR A OH    1 
ATOM   1347  N  N     . LEU A 1 1619 ? 129.335 179.080 152.757 1.00 40.23  ? 1619 LEU A N     1 
ATOM   1348  C  CA    . LEU A 1 1619 ? 130.455 179.344 151.860 1.00 37.40  ? 1619 LEU A CA    1 
ATOM   1349  C  C     . LEU A 1 1619 ? 131.032 178.053 151.290 1.00 41.22  ? 1619 LEU A C     1 
ATOM   1350  O  O     . LEU A 1 1619 ? 131.407 178.001 150.113 1.00 41.02  ? 1619 LEU A O     1 
ATOM   1351  C  CB    . LEU A 1 1619 ? 131.532 180.146 152.591 1.00 35.79  ? 1619 LEU A CB    1 
ATOM   1352  C  CG    . LEU A 1 1619 ? 131.182 181.614 152.843 1.00 37.54  ? 1619 LEU A CG    1 
ATOM   1353  C  CD1   . LEU A 1 1619 ? 132.388 182.382 153.347 1.00 36.48  ? 1619 LEU A CD1   1 
ATOM   1354  C  CD2   . LEU A 1 1619 ? 130.629 182.257 151.582 1.00 38.42  ? 1619 LEU A CD2   1 
ATOM   1355  N  N     . GLU A 1 1620 ? 131.112 177.001 152.108 1.00 40.49  ? 1620 GLU A N     1 
ATOM   1356  C  CA    . GLU A 1 1620 ? 131.634 175.726 151.623 1.00 37.76  ? 1620 GLU A CA    1 
ATOM   1357  C  C     . GLU A 1 1620 ? 130.754 175.151 150.519 1.00 39.62  ? 1620 GLU A C     1 
ATOM   1358  O  O     . GLU A 1 1620 ? 131.259 174.576 149.548 1.00 47.39  ? 1620 GLU A O     1 
ATOM   1359  C  CB    . GLU A 1 1620 ? 131.765 174.737 152.779 1.00 41.06  ? 1620 GLU A CB    1 
ATOM   1360  C  CG    . GLU A 1 1620 ? 133.117 174.776 153.470 1.00 47.36  ? 1620 GLU A CG    1 
ATOM   1361  C  CD    . GLU A 1 1620 ? 134.240 174.306 152.569 1.00 47.63  ? 1620 GLU A CD    1 
ATOM   1362  O  OE1   . GLU A 1 1620 ? 134.108 173.218 151.969 1.00 54.32  ? 1620 GLU A OE1   1 
ATOM   1363  O  OE2   . GLU A 1 1620 ? 135.261 175.019 152.470 1.00 39.65  ? 1620 GLU A OE2   1 
ATOM   1364  N  N     . ARG A 1 1621 ? 129.431 175.281 150.661 1.00 37.43  ? 1621 ARG A N     1 
ATOM   1365  C  CA    . ARG A 1 1621 ? 128.520 174.807 149.622 1.00 39.95  ? 1621 ARG A CA    1 
ATOM   1366  C  C     . ARG A 1 1621 ? 128.686 175.603 148.334 1.00 41.72  ? 1621 ARG A C     1 
ATOM   1367  O  O     . ARG A 1 1621 ? 128.643 175.038 147.234 1.00 42.23  ? 1621 ARG A O     1 
ATOM   1368  C  CB    . ARG A 1 1621 ? 127.075 174.888 150.110 1.00 47.47  ? 1621 ARG A CB    1 
ATOM   1369  C  CG    . ARG A 1 1621 ? 126.709 173.908 151.206 1.00 49.65  ? 1621 ARG A CG    1 
ATOM   1370  C  CD    . ARG A 1 1621 ? 125.268 174.060 151.735 1.00 59.52  ? 1621 ARG A CD    1 
ATOM   1371  N  NE    . ARG A 1 1621 ? 124.195 173.978 150.743 1.00 68.84  ? 1621 ARG A NE    1 
ATOM   1372  C  CZ    . ARG A 1 1621 ? 123.803 174.956 149.932 1.00 66.38  ? 1621 ARG A CZ    1 
ATOM   1373  N  NH1   . ARG A 1 1621 ? 124.303 176.178 150.022 1.00 59.11  ? 1621 ARG A NH1   1 
ATOM   1374  N  NH2   . ARG A 1 1621 ? 122.853 174.711 149.035 1.00 68.55  ? 1621 ARG A NH2   1 
ATOM   1375  N  N     . GLU A 1 1622 ? 128.861 176.920 148.450 1.00 39.66  ? 1622 GLU A N     1 
ATOM   1376  C  CA    . GLU A 1 1622 ? 128.992 177.758 147.263 1.00 36.43  ? 1622 GLU A CA    1 
ATOM   1377  C  C     . GLU A 1 1622 ? 130.266 177.428 146.492 1.00 39.49  ? 1622 GLU A C     1 
ATOM   1378  O  O     . GLU A 1 1622 ? 130.303 177.552 145.262 1.00 40.60  ? 1622 GLU A O     1 
ATOM   1379  C  CB    . GLU A 1 1622 ? 128.960 179.233 147.662 1.00 42.82  ? 1622 GLU A CB    1 
ATOM   1380  C  CG    . GLU A 1 1622 ? 127.566 179.773 147.986 1.00 45.99  ? 1622 GLU A CG    1 
ATOM   1381  C  CD    . GLU A 1 1622 ? 126.730 180.062 146.751 1.00 52.99  ? 1622 GLU A CD    1 
ATOM   1382  O  OE1   . GLU A 1 1622 ? 127.107 179.616 145.648 1.00 53.16  ? 1622 GLU A OE1   1 
ATOM   1383  O  OE2   . GLU A 1 1622 ? 125.697 180.752 146.881 1.00 50.66  ? 1622 GLU A OE2   1 
ATOM   1384  N  N     . ARG A 1 1623 ? 131.323 177.012 147.197 1.00 36.91  ? 1623 ARG A N     1 
ATOM   1385  C  CA    . ARG A 1 1623 ? 132.559 176.630 146.522 1.00 27.12  ? 1623 ARG A CA    1 
ATOM   1386  C  C     . ARG A 1 1623 ? 132.341 175.427 145.613 1.00 34.44  ? 1623 ARG A C     1 
ATOM   1387  O  O     . ARG A 1 1623 ? 132.964 175.320 144.550 1.00 38.12  ? 1623 ARG A O     1 
ATOM   1388  C  CB    . ARG A 1 1623 ? 133.651 176.333 147.549 1.00 26.30  ? 1623 ARG A CB    1 
ATOM   1389  C  CG    . ARG A 1 1623 ? 134.142 177.549 148.312 1.00 25.58  ? 1623 ARG A CG    1 
ATOM   1390  C  CD    . ARG A 1 1623 ? 134.898 177.129 149.560 1.00 28.29  ? 1623 ARG A CD    1 
ATOM   1391  N  NE    . ARG A 1 1623 ? 134.954 178.190 150.558 1.00 27.36  ? 1623 ARG A NE    1 
ATOM   1392  C  CZ    . ARG A 1 1623 ? 135.764 179.238 150.498 1.00 28.63  ? 1623 ARG A CZ    1 
ATOM   1393  N  NH1   . ARG A 1 1623 ? 136.617 179.397 149.500 1.00 27.80  ? 1623 ARG A NH1   1 
ATOM   1394  N  NH2   . ARG A 1 1623 ? 135.718 180.148 151.467 1.00 32.82  ? 1623 ARG A NH2   1 
ATOM   1395  N  N     . SER A 1 1624 ? 131.467 174.503 146.020 1.00 37.37  ? 1624 SER A N     1 
ATOM   1396  C  CA    . SER A 1 1624 ? 131.168 173.349 145.180 1.00 36.55  ? 1624 SER A CA    1 
ATOM   1397  C  C     . SER A 1 1624 ? 130.451 173.756 143.900 1.00 35.79  ? 1624 SER A C     1 
ATOM   1398  O  O     . SER A 1 1624 ? 130.646 173.129 142.853 1.00 37.09  ? 1624 SER A O     1 
ATOM   1399  C  CB    . SER A 1 1624 ? 130.329 172.335 145.958 1.00 36.81  ? 1624 SER A CB    1 
ATOM   1400  O  OG    . SER A 1 1624 ? 131.152 171.351 146.560 1.00 39.70  ? 1624 SER A OG    1 
ATOM   1401  N  N     . SER A 1 1625 ? 129.614 174.794 143.965 1.00 38.97  ? 1625 SER A N     1 
ATOM   1402  C  CA    . SER A 1 1625 ? 128.908 175.256 142.773 1.00 38.01  ? 1625 SER A CA    1 
ATOM   1403  C  C     . SER A 1 1625 ? 129.879 175.825 141.745 1.00 33.01  ? 1625 SER A C     1 
ATOM   1404  O  O     . SER A 1 1625 ? 129.836 175.458 140.565 1.00 35.87  ? 1625 SER A O     1 
ATOM   1405  C  CB    . SER A 1 1625 ? 127.858 176.297 143.160 1.00 39.88  ? 1625 SER A CB    1 
ATOM   1406  O  OG    . SER A 1 1625 ? 128.469 177.497 143.601 1.00 43.48  ? 1625 SER A OG    1 
ATOM   1407  N  N     . PHE A 1 1626 ? 130.758 176.723 142.173 1.00 34.22  ? 1626 PHE A N     1 
ATOM   1408  C  CA    . PHE A 1 1626 ? 131.793 177.285 141.306 1.00 30.21  ? 1626 PHE A CA    1 
ATOM   1409  C  C     . PHE A 1 1626 ? 133.152 176.880 141.858 1.00 28.15  ? 1626 PHE A C     1 
ATOM   1410  O  O     . PHE A 1 1626 ? 133.612 177.471 142.854 1.00 27.28  ? 1626 PHE A O     1 
ATOM   1411  C  CB    . PHE A 1 1626 ? 131.674 178.806 141.220 1.00 27.16  ? 1626 PHE A CB    1 
ATOM   1412  C  CG    . PHE A 1 1626 ? 132.517 179.420 140.140 1.00 27.27  ? 1626 PHE A CG    1 
ATOM   1413  C  CD1   . PHE A 1 1626 ? 132.365 179.028 138.820 1.00 31.72  ? 1626 PHE A CD1   1 
ATOM   1414  C  CD2   . PHE A 1 1626 ? 133.462 180.386 140.442 1.00 21.95  ? 1626 PHE A CD2   1 
ATOM   1415  C  CE1   . PHE A 1 1626 ? 133.137 179.589 137.822 1.00 22.09  ? 1626 PHE A CE1   1 
ATOM   1416  C  CE2   . PHE A 1 1626 ? 134.237 180.950 139.448 1.00 18.91  ? 1626 PHE A CE2   1 
ATOM   1417  C  CZ    . PHE A 1 1626 ? 134.074 180.550 138.137 1.00 19.88  ? 1626 PHE A CZ    1 
ATOM   1418  N  N     . PRO A 1 1627 ? 133.825 175.895 141.257 1.00 26.20  ? 1627 PRO A N     1 
ATOM   1419  C  CA    . PRO A 1 1627 ? 135.017 175.315 141.901 1.00 26.11  ? 1627 PRO A CA    1 
ATOM   1420  C  C     . PRO A 1 1627 ? 136.147 176.301 142.144 1.00 26.03  ? 1627 PRO A C     1 
ATOM   1421  O  O     . PRO A 1 1627 ? 136.918 176.113 143.093 1.00 24.47  ? 1627 PRO A O     1 
ATOM   1422  C  CB    . PRO A 1 1627 ? 135.435 174.208 140.922 1.00 23.65  ? 1627 PRO A CB    1 
ATOM   1423  C  CG    . PRO A 1 1627 ? 134.819 174.589 139.618 1.00 25.56  ? 1627 PRO A CG    1 
ATOM   1424  C  CD    . PRO A 1 1627 ? 133.533 175.270 139.958 1.00 25.71  ? 1627 PRO A CD    1 
ATOM   1425  N  N     . ARG A 1 1628 ? 136.278 177.344 141.321 1.00 26.90  ? 1628 ARG A N     1 
ATOM   1426  C  CA    . ARG A 1 1628 ? 137.373 178.291 141.502 1.00 18.18  ? 1628 ARG A CA    1 
ATOM   1427  C  C     . ARG A 1 1628 ? 137.249 179.089 142.792 1.00 21.54  ? 1628 ARG A C     1 
ATOM   1428  O  O     . ARG A 1 1628 ? 138.217 179.742 143.196 1.00 20.38  ? 1628 ARG A O     1 
ATOM   1429  C  CB    . ARG A 1 1628 ? 137.460 179.240 140.306 1.00 18.55  ? 1628 ARG A CB    1 
ATOM   1430  C  CG    . ARG A 1 1628 ? 137.780 178.545 138.995 1.00 17.53  ? 1628 ARG A CG    1 
ATOM   1431  C  CD    . ARG A 1 1628 ? 138.070 179.546 137.892 1.00 14.73  ? 1628 ARG A CD    1 
ATOM   1432  N  NE    . ARG A 1 1628 ? 138.418 178.885 136.640 1.00 20.65  ? 1628 ARG A NE    1 
ATOM   1433  C  CZ    . ARG A 1 1628 ? 139.618 178.929 136.078 1.00 18.74  ? 1628 ARG A CZ    1 
ATOM   1434  N  NH1   . ARG A 1 1628 ? 140.615 179.601 136.630 1.00 18.58  ? 1628 ARG A NH1   1 
ATOM   1435  N  NH2   . ARG A 1 1628 ? 139.823 178.282 134.935 1.00 20.75  ? 1628 ARG A NH2   1 
ATOM   1436  N  N     . PHE A 1 1629 ? 136.084 179.058 143.445 1.00 26.48  ? 1629 PHE A N     1 
ATOM   1437  C  CA    . PHE A 1 1629 ? 135.934 179.727 144.732 1.00 19.83  ? 1629 PHE A CA    1 
ATOM   1438  C  C     . PHE A 1 1629 ? 136.756 179.061 145.828 1.00 18.13  ? 1629 PHE A C     1 
ATOM   1439  O  O     . PHE A 1 1629 ? 136.937 179.653 146.897 1.00 21.09  ? 1629 PHE A O     1 
ATOM   1440  C  CB    . PHE A 1 1629 ? 134.461 179.765 145.138 1.00 20.57  ? 1629 PHE A CB    1 
ATOM   1441  C  CG    . PHE A 1 1629 ? 133.658 180.797 144.401 1.00 22.42  ? 1629 PHE A CG    1 
ATOM   1442  C  CD1   . PHE A 1 1629 ? 134.269 181.917 143.864 1.00 22.93  ? 1629 PHE A CD1   1 
ATOM   1443  C  CD2   . PHE A 1 1629 ? 132.290 180.648 144.246 1.00 25.09  ? 1629 PHE A CD2   1 
ATOM   1444  C  CE1   . PHE A 1 1629 ? 133.532 182.867 143.186 1.00 23.94  ? 1629 PHE A CE1   1 
ATOM   1445  C  CE2   . PHE A 1 1629 ? 131.548 181.594 143.570 1.00 21.21  ? 1629 PHE A CE2   1 
ATOM   1446  C  CZ    . PHE A 1 1629 ? 132.170 182.705 143.039 1.00 21.61  ? 1629 PHE A CZ    1 
ATOM   1447  N  N     . TYR A 1 1630 ? 137.258 177.847 145.587 1.00 16.37  ? 1630 TYR A N     1 
ATOM   1448  C  CA    . TYR A 1 1630 ? 138.085 177.166 146.576 1.00 16.14  ? 1630 TYR A CA    1 
ATOM   1449  C  C     . TYR A 1 1630 ? 139.409 177.877 146.813 1.00 18.38  ? 1630 TYR A C     1 
ATOM   1450  O  O     . TYR A 1 1630 ? 140.093 177.579 147.798 1.00 21.68  ? 1630 TYR A O     1 
ATOM   1451  C  CB    . TYR A 1 1630 ? 138.347 175.724 146.138 1.00 14.87  ? 1630 TYR A CB    1 
ATOM   1452  C  CG    . TYR A 1 1630 ? 137.284 174.746 146.580 1.00 19.24  ? 1630 TYR A CG    1 
ATOM   1453  C  CD1   . TYR A 1 1630 ? 137.230 174.297 147.890 1.00 17.22  ? 1630 TYR A CD1   1 
ATOM   1454  C  CD2   . TYR A 1 1630 ? 136.337 174.270 145.684 1.00 21.29  ? 1630 TYR A CD2   1 
ATOM   1455  C  CE1   . TYR A 1 1630 ? 136.261 173.403 148.298 1.00 21.16  ? 1630 TYR A CE1   1 
ATOM   1456  C  CE2   . TYR A 1 1630 ? 135.365 173.376 146.083 1.00 22.89  ? 1630 TYR A CE2   1 
ATOM   1457  C  CZ    . TYR A 1 1630 ? 135.331 172.946 147.391 1.00 24.50  ? 1630 TYR A CZ    1 
ATOM   1458  O  OH    . TYR A 1 1630 ? 134.365 172.055 147.795 1.00 27.16  ? 1630 TYR A OH    1 
ATOM   1459  N  N     . PHE A 1 1631 ? 139.786 178.806 145.937 1.00 19.57  ? 1631 PHE A N     1 
ATOM   1460  C  CA    . PHE A 1 1631 ? 141.025 179.559 146.066 1.00 15.52  ? 1631 PHE A CA    1 
ATOM   1461  C  C     . PHE A 1 1631 ? 140.792 180.972 146.581 1.00 19.56  ? 1631 PHE A C     1 
ATOM   1462  O  O     . PHE A 1 1631 ? 141.677 181.824 146.456 1.00 25.06  ? 1631 PHE A O     1 
ATOM   1463  C  CB    . PHE A 1 1631 ? 141.752 179.600 144.721 1.00 16.46  ? 1631 PHE A CB    1 
ATOM   1464  C  CG    . PHE A 1 1631 ? 141.836 178.263 144.044 1.00 17.73  ? 1631 PHE A CG    1 
ATOM   1465  C  CD1   . PHE A 1 1631 ? 142.209 177.134 144.754 1.00 16.02  ? 1631 PHE A CD1   1 
ATOM   1466  C  CD2   . PHE A 1 1631 ? 141.533 178.134 142.700 1.00 17.53  ? 1631 PHE A CD2   1 
ATOM   1467  C  CE1   . PHE A 1 1631 ? 142.282 175.903 144.136 1.00 14.53  ? 1631 PHE A CE1   1 
ATOM   1468  C  CE2   . PHE A 1 1631 ? 141.606 176.906 142.075 1.00 18.08  ? 1631 PHE A CE2   1 
ATOM   1469  C  CZ    . PHE A 1 1631 ? 141.981 175.788 142.794 1.00 15.38  ? 1631 PHE A CZ    1 
ATOM   1470  N  N     . VAL A 1 1632 ? 139.622 181.236 147.156 1.00 25.39  ? 1632 VAL A N     1 
ATOM   1471  C  CA    . VAL A 1 1632 ? 139.259 182.550 147.671 1.00 20.55  ? 1632 VAL A CA    1 
ATOM   1472  C  C     . VAL A 1 1632 ? 138.871 182.393 149.134 1.00 24.21  ? 1632 VAL A C     1 
ATOM   1473  O  O     . VAL A 1 1632 ? 138.112 181.482 149.485 1.00 31.89  ? 1632 VAL A O     1 
ATOM   1474  C  CB    . VAL A 1 1632 ? 138.110 183.175 146.858 1.00 22.72  ? 1632 VAL A CB    1 
ATOM   1475  C  CG1   . VAL A 1 1632 ? 137.631 184.458 147.508 1.00 29.43  ? 1632 VAL A CG1   1 
ATOM   1476  C  CG2   . VAL A 1 1632 ? 138.556 183.436 145.430 1.00 22.81  ? 1632 VAL A CG2   1 
ATOM   1477  N  N     . GLY A 1 1633 ? 139.395 183.273 149.982 1.00 26.70  ? 1633 GLY A N     1 
ATOM   1478  C  CA    . GLY A 1 1633 ? 139.115 183.201 151.399 1.00 25.52  ? 1633 GLY A CA    1 
ATOM   1479  C  C     . GLY A 1 1633 ? 137.673 183.543 151.725 1.00 30.16  ? 1633 GLY A C     1 
ATOM   1480  O  O     . GLY A 1 1633 ? 136.906 184.040 150.900 1.00 33.67  ? 1633 GLY A O     1 
ATOM   1481  N  N     . ASP A 1 1634 ? 137.302 183.259 152.976 1.00 33.48  ? 1634 ASP A N     1 
ATOM   1482  C  CA    . ASP A 1 1634 ? 135.931 183.492 153.417 1.00 34.67  ? 1634 ASP A CA    1 
ATOM   1483  C  C     . ASP A 1 1634 ? 135.584 184.976 153.397 1.00 35.05  ? 1634 ASP A C     1 
ATOM   1484  O  O     . ASP A 1 1634 ? 134.448 185.350 153.083 1.00 34.25  ? 1634 ASP A O     1 
ATOM   1485  C  CB    . ASP A 1 1634 ? 135.724 182.909 154.814 1.00 32.45  ? 1634 ASP A CB    1 
ATOM   1486  C  CG    . ASP A 1 1634 ? 135.487 181.412 154.790 1.00 38.41  ? 1634 ASP A CG    1 
ATOM   1487  O  OD1   . ASP A 1 1634 ? 136.025 180.738 153.888 1.00 36.40  ? 1634 ASP A OD1   1 
ATOM   1488  O  OD2   . ASP A 1 1634 ? 134.761 180.909 155.673 1.00 39.16  ? 1634 ASP A OD2   1 
ATOM   1489  N  N     . GLU A 1 1635 ? 136.546 185.835 153.742 1.00 34.41  ? 1635 GLU A N     1 
ATOM   1490  C  CA    . GLU A 1 1635 ? 136.300 187.274 153.725 1.00 36.95  ? 1635 GLU A CA    1 
ATOM   1491  C  C     . GLU A 1 1635 ? 135.929 187.753 152.327 1.00 35.50  ? 1635 GLU A C     1 
ATOM   1492  O  O     . GLU A 1 1635 ? 134.948 188.484 152.146 1.00 31.79  ? 1635 GLU A O     1 
ATOM   1493  C  CB    . GLU A 1 1635 ? 137.536 188.020 154.232 1.00 43.48  ? 1635 GLU A CB    1 
ATOM   1494  C  CG    . GLU A 1 1635 ? 137.921 187.702 155.666 1.00 54.47  ? 1635 GLU A CG    1 
ATOM   1495  C  CD    . GLU A 1 1635 ? 136.929 188.250 156.670 1.00 61.02  ? 1635 GLU A CD    1 
ATOM   1496  O  OE1   . GLU A 1 1635 ? 136.348 189.324 156.407 1.00 54.33  ? 1635 GLU A OE1   1 
ATOM   1497  O  OE2   . GLU A 1 1635 ? 136.731 187.609 157.723 1.00 61.91  ? 1635 GLU A OE2   1 
ATOM   1498  N  N     . ASP A 1 1636 ? 136.706 187.346 151.321 1.00 36.90  ? 1636 ASP A N     1 
ATOM   1499  C  CA    . ASP A 1 1636 ? 136.465 187.816 149.962 1.00 34.85  ? 1636 ASP A CA    1 
ATOM   1500  C  C     . ASP A 1 1636 ? 135.295 187.095 149.305 1.00 34.43  ? 1636 ASP A C     1 
ATOM   1501  O  O     . ASP A 1 1636 ? 134.592 187.688 148.479 1.00 36.83  ? 1636 ASP A O     1 
ATOM   1502  C  CB    . ASP A 1 1636 ? 137.731 187.656 149.124 1.00 36.76  ? 1636 ASP A CB    1 
ATOM   1503  C  CG    . ASP A 1 1636 ? 138.968 188.150 149.845 1.00 39.52  ? 1636 ASP A CG    1 
ATOM   1504  O  OD1   . ASP A 1 1636 ? 138.972 189.315 150.293 1.00 35.92  ? 1636 ASP A OD1   1 
ATOM   1505  O  OD2   . ASP A 1 1636 ? 139.937 187.371 149.965 1.00 36.41  ? 1636 ASP A OD2   1 
ATOM   1506  N  N     . LEU A 1 1637 ? 135.077 185.821 149.644 1.00 29.88  ? 1637 LEU A N     1 
ATOM   1507  C  CA    . LEU A 1 1637 ? 133.968 185.081 149.048 1.00 29.04  ? 1637 LEU A CA    1 
ATOM   1508  C  C     . LEU A 1 1637 ? 132.628 185.700 149.422 1.00 30.22  ? 1637 LEU A C     1 
ATOM   1509  O  O     . LEU A 1 1637 ? 131.727 185.797 148.581 1.00 34.27  ? 1637 LEU A O     1 
ATOM   1510  C  CB    . LEU A 1 1637 ? 134.020 183.614 149.471 1.00 33.57  ? 1637 LEU A CB    1 
ATOM   1511  C  CG    . LEU A 1 1637 ? 133.033 182.686 148.758 1.00 25.92  ? 1637 LEU A CG    1 
ATOM   1512  C  CD1   . LEU A 1 1637 ? 133.122 182.865 147.253 1.00 25.76  ? 1637 LEU A CD1   1 
ATOM   1513  C  CD2   . LEU A 1 1637 ? 133.275 181.239 149.141 1.00 28.75  ? 1637 LEU A CD2   1 
ATOM   1514  N  N     . LEU A 1 1638 ? 132.480 186.126 150.679 1.00 31.49  ? 1638 LEU A N     1 
ATOM   1515  C  CA    . LEU A 1 1638 ? 131.265 186.826 151.084 1.00 27.60  ? 1638 LEU A CA    1 
ATOM   1516  C  C     . LEU A 1 1638 ? 131.094 188.118 150.297 1.00 30.59  ? 1638 LEU A C     1 
ATOM   1517  O  O     . LEU A 1 1638 ? 129.974 188.485 149.923 1.00 36.70  ? 1638 LEU A O     1 
ATOM   1518  C  CB    . LEU A 1 1638 ? 131.304 187.116 152.584 1.00 30.33  ? 1638 LEU A CB    1 
ATOM   1519  C  CG    . LEU A 1 1638 ? 131.247 185.920 153.535 1.00 34.60  ? 1638 LEU A CG    1 
ATOM   1520  C  CD1   . LEU A 1 1638 ? 131.578 186.355 154.948 1.00 32.11  ? 1638 LEU A CD1   1 
ATOM   1521  C  CD2   . LEU A 1 1638 ? 129.886 185.256 153.494 1.00 34.94  ? 1638 LEU A CD2   1 
ATOM   1522  N  N     . GLU A 1 1639 ? 132.198 188.822 150.041 1.00 31.74  ? 1639 GLU A N     1 
ATOM   1523  C  CA    . GLU A 1 1639 ? 132.134 190.048 149.253 1.00 31.06  ? 1639 GLU A CA    1 
ATOM   1524  C  C     . GLU A 1 1639 ? 131.704 189.764 147.819 1.00 36.06  ? 1639 GLU A C     1 
ATOM   1525  O  O     . GLU A 1 1639 ? 130.932 190.531 147.233 1.00 41.89  ? 1639 GLU A O     1 
ATOM   1526  C  CB    . GLU A 1 1639 ? 133.489 190.755 149.279 1.00 31.07  ? 1639 GLU A CB    1 
ATOM   1527  C  CG    . GLU A 1 1639 ? 133.406 192.268 149.190 1.00 38.37  ? 1639 GLU A CG    1 
ATOM   1528  C  CD    . GLU A 1 1639 ? 134.632 192.879 148.543 1.00 46.59  ? 1639 GLU A CD    1 
ATOM   1529  O  OE1   . GLU A 1 1639 ? 135.625 193.122 149.261 1.00 46.55  ? 1639 GLU A OE1   1 
ATOM   1530  O  OE2   . GLU A 1 1639 ? 134.605 193.113 147.317 1.00 36.09  ? 1639 GLU A OE2   1 
ATOM   1531  N  N     . ILE A 1 1640 ? 132.195 188.669 147.236 1.00 35.71  ? 1640 ILE A N     1 
ATOM   1532  C  CA    . ILE A 1 1640 ? 131.851 188.347 145.854 1.00 34.52  ? 1640 ILE A CA    1 
ATOM   1533  C  C     . ILE A 1 1640 ? 130.378 187.975 145.741 1.00 34.71  ? 1640 ILE A C     1 
ATOM   1534  O  O     . ILE A 1 1640 ? 129.666 188.455 144.851 1.00 37.78  ? 1640 ILE A O     1 
ATOM   1535  C  CB    . ILE A 1 1640 ? 132.757 187.221 145.323 1.00 35.60  ? 1640 ILE A CB    1 
ATOM   1536  C  CG1   . ILE A 1 1640 ? 134.195 187.717 145.168 1.00 32.19  ? 1640 ILE A CG1   1 
ATOM   1537  C  CG2   . ILE A 1 1640 ? 132.236 186.696 143.995 1.00 30.00  ? 1640 ILE A CG2   1 
ATOM   1538  C  CD1   . ILE A 1 1640 ? 135.193 186.604 144.957 1.00 30.42  ? 1640 ILE A CD1   1 
ATOM   1539  N  N     . ILE A 1 1641 ? 129.900 187.111 146.639 1.00 32.78  ? 1641 ILE A N     1 
ATOM   1540  C  CA    . ILE A 1 1641 ? 128.518 186.647 146.563 1.00 32.78  ? 1641 ILE A CA    1 
ATOM   1541  C  C     . ILE A 1 1641 ? 127.553 187.799 146.818 1.00 35.96  ? 1641 ILE A C     1 
ATOM   1542  O  O     . ILE A 1 1641 ? 126.551 187.960 146.110 1.00 38.37  ? 1641 ILE A O     1 
ATOM   1543  C  CB    . ILE A 1 1641 ? 128.286 185.490 147.553 1.00 30.59  ? 1641 ILE A CB    1 
ATOM   1544  C  CG1   . ILE A 1 1641 ? 129.221 184.318 147.247 1.00 33.85  ? 1641 ILE A CG1   1 
ATOM   1545  C  CG2   . ILE A 1 1641 ? 126.846 185.017 147.483 1.00 35.94  ? 1641 ILE A CG2   1 
ATOM   1546  C  CD1   . ILE A 1 1641 ? 129.016 183.696 145.893 1.00 31.26  ? 1641 ILE A CD1   1 
ATOM   1547  N  N     . GLY A 1 1642 ? 127.839 188.616 147.833 1.00 31.84  ? 1642 GLY A N     1 
ATOM   1548  C  CA    . GLY A 1 1642 ? 126.942 189.710 148.167 1.00 33.82  ? 1642 GLY A CA    1 
ATOM   1549  C  C     . GLY A 1 1642 ? 126.907 190.799 147.111 1.00 37.24  ? 1642 GLY A C     1 
ATOM   1550  O  O     . GLY A 1 1642 ? 125.852 191.381 146.843 1.00 40.65  ? 1642 GLY A O     1 
ATOM   1551  N  N     . ASN A 1 1643 ? 128.055 191.094 146.500 1.00 36.00  ? 1643 ASN A N     1 
ATOM   1552  C  CA    . ASN A 1 1643 ? 128.167 192.155 145.507 1.00 41.68  ? 1643 ASN A CA    1 
ATOM   1553  C  C     . ASN A 1 1643 ? 127.998 191.634 144.085 1.00 45.93  ? 1643 ASN A C     1 
ATOM   1554  O  O     . ASN A 1 1643 ? 128.614 192.160 143.153 1.00 50.08  ? 1643 ASN A O     1 
ATOM   1555  C  CB    . ASN A 1 1643 ? 129.504 192.879 145.653 1.00 42.21  ? 1643 ASN A CB    1 
ATOM   1556  C  CG    . ASN A 1 1643 ? 129.555 193.765 146.881 1.00 42.61  ? 1643 ASN A CG    1 
ATOM   1557  O  OD1   . ASN A 1 1643 ? 130.284 193.485 147.832 1.00 39.60  ? 1643 ASN A OD1   1 
ATOM   1558  N  ND2   . ASN A 1 1643 ? 128.781 194.842 146.864 1.00 44.92  ? 1643 ASN A ND2   1 
ATOM   1559  N  N     . SER A 1 1644 ? 127.179 190.596 143.904 1.00 43.39  ? 1644 SER A N     1 
ATOM   1560  C  CA    . SER A 1 1644 ? 126.938 190.070 142.564 1.00 47.06  ? 1644 SER A CA    1 
ATOM   1561  C  C     . SER A 1 1644 ? 126.228 191.093 141.687 1.00 52.57  ? 1644 SER A C     1 
ATOM   1562  O  O     . SER A 1 1644 ? 126.526 191.209 140.492 1.00 58.01  ? 1644 SER A O     1 
ATOM   1563  C  CB    . SER A 1 1644 ? 126.126 188.778 142.649 1.00 47.68  ? 1644 SER A CB    1 
ATOM   1564  O  OG    . SER A 1 1644 ? 124.827 189.025 143.159 1.00 52.69  ? 1644 SER A OG    1 
ATOM   1565  N  N     . LYS A 1 1645 ? 125.279 191.839 142.260 1.00 49.43  ? 1645 LYS A N     1 
ATOM   1566  C  CA    . LYS A 1 1645 ? 124.535 192.822 141.478 1.00 48.33  ? 1645 LYS A CA    1 
ATOM   1567  C  C     . LYS A 1 1645 ? 125.444 193.927 140.953 1.00 53.39  ? 1645 LYS A C     1 
ATOM   1568  O  O     . LYS A 1 1645 ? 125.349 194.315 139.783 1.00 54.24  ? 1645 LYS A O     1 
ATOM   1569  C  CB    . LYS A 1 1645 ? 123.407 193.419 142.320 1.00 47.38  ? 1645 LYS A CB    1 
ATOM   1570  C  CG    . LYS A 1 1645 ? 122.268 192.458 142.613 1.00 49.26  ? 1645 LYS A CG    1 
ATOM   1571  C  CD    . LYS A 1 1645 ? 121.166 193.145 143.401 1.00 47.62  ? 1645 LYS A CD    1 
ATOM   1572  C  CE    . LYS A 1 1645 ? 120.034 192.185 143.722 1.00 50.04  ? 1645 LYS A CE    1 
ATOM   1573  N  NZ    . LYS A 1 1645 ? 118.952 192.848 144.500 1.00 52.61  ? 1645 LYS A NZ    1 
ATOM   1574  N  N     . ASN A 1 1646 ? 126.332 194.444 141.799 1.00 52.85  ? 1646 ASN A N     1 
ATOM   1575  C  CA    . ASN A 1 1646 ? 127.220 195.546 141.428 1.00 51.42  ? 1646 ASN A CA    1 
ATOM   1576  C  C     . ASN A 1 1646 ? 128.606 194.955 141.182 1.00 51.90  ? 1646 ASN A C     1 
ATOM   1577  O  O     . ASN A 1 1646 ? 129.338 194.616 142.112 1.00 52.22  ? 1646 ASN A O     1 
ATOM   1578  C  CB    . ASN A 1 1646 ? 127.228 196.622 142.508 1.00 51.07  ? 1646 ASN A CB    1 
ATOM   1579  C  CG    . ASN A 1 1646 ? 128.498 197.443 142.505 1.00 55.60  ? 1646 ASN A CG    1 
ATOM   1580  O  OD1   . ASN A 1 1646 ? 129.321 197.333 143.411 1.00 54.17  ? 1646 ASN A OD1   1 
ATOM   1581  N  ND2   . ASN A 1 1646 ? 128.667 198.271 141.481 1.00 55.31  ? 1646 ASN A ND2   1 
ATOM   1582  N  N     . VAL A 1 1647 ? 128.966 194.840 139.901 1.00 51.92  ? 1647 VAL A N     1 
ATOM   1583  C  CA    . VAL A 1 1647 ? 130.160 194.101 139.510 1.00 45.36  ? 1647 VAL A CA    1 
ATOM   1584  C  C     . VAL A 1 1647 ? 131.435 194.916 139.710 1.00 44.84  ? 1647 VAL A C     1 
ATOM   1585  O  O     . VAL A 1 1647 ? 132.533 194.347 139.724 1.00 46.28  ? 1647 VAL A O     1 
ATOM   1586  C  CB    . VAL A 1 1647 ? 130.009 193.636 138.047 1.00 42.24  ? 1647 VAL A CB    1 
ATOM   1587  C  CG1   . VAL A 1 1647 ? 131.104 192.652 137.665 1.00 44.16  ? 1647 VAL A CG1   1 
ATOM   1588  C  CG2   . VAL A 1 1647 ? 128.636 193.019 137.829 1.00 38.55  ? 1647 VAL A CG2   1 
ATOM   1589  N  N     . ALA A 1 1648 ? 131.320 196.235 139.885 1.00 46.23  ? 1648 ALA A N     1 
ATOM   1590  C  CA    . ALA A 1 1648 ? 132.502 197.087 139.975 1.00 44.51  ? 1648 ALA A CA    1 
ATOM   1591  C  C     . ALA A 1 1648 ? 133.426 196.700 141.125 1.00 44.38  ? 1648 ALA A C     1 
ATOM   1592  O  O     . ALA A 1 1648 ? 134.636 196.932 141.033 1.00 38.91  ? 1648 ALA A O     1 
ATOM   1593  C  CB    . ALA A 1 1648 ? 132.085 198.551 140.117 1.00 45.72  ? 1648 ALA A CB    1 
ATOM   1594  N  N     . LYS A 1 1649 ? 132.891 196.119 142.199 1.00 46.07  ? 1649 LYS A N     1 
ATOM   1595  C  CA    . LYS A 1 1649 ? 133.722 195.681 143.313 1.00 44.24  ? 1649 LYS A CA    1 
ATOM   1596  C  C     . LYS A 1 1649 ? 134.309 194.291 143.108 1.00 42.12  ? 1649 LYS A C     1 
ATOM   1597  O  O     . LYS A 1 1649 ? 135.136 193.861 143.920 1.00 41.75  ? 1649 LYS A O     1 
ATOM   1598  C  CB    . LYS A 1 1649 ? 132.917 195.704 144.615 1.00 47.67  ? 1649 LYS A CB    1 
ATOM   1599  C  CG    . LYS A 1 1649 ? 132.067 196.948 144.795 1.00 49.45  ? 1649 LYS A CG    1 
ATOM   1600  C  CD    . LYS A 1 1649 ? 131.979 197.356 146.256 1.00 52.89  ? 1649 LYS A CD    1 
ATOM   1601  C  CE    . LYS A 1 1649 ? 133.285 197.962 146.742 1.00 59.19  ? 1649 LYS A CE    1 
ATOM   1602  N  NZ    . LYS A 1 1649 ? 133.319 198.080 148.226 1.00 59.29  ? 1649 LYS A NZ    1 
ATOM   1603  N  N     . LEU A 1 1650 ? 133.908 193.585 142.054 1.00 39.60  ? 1650 LEU A N     1 
ATOM   1604  C  CA    . LEU A 1 1650 ? 134.402 192.242 141.784 1.00 32.90  ? 1650 LEU A CA    1 
ATOM   1605  C  C     . LEU A 1 1650 ? 135.742 192.231 141.062 1.00 32.44  ? 1650 LEU A C     1 
ATOM   1606  O  O     . LEU A 1 1650 ? 136.363 191.168 140.963 1.00 33.51  ? 1650 LEU A O     1 
ATOM   1607  C  CB    . LEU A 1 1650 ? 133.380 191.465 140.949 1.00 33.18  ? 1650 LEU A CB    1 
ATOM   1608  C  CG    . LEU A 1 1650 ? 132.098 191.033 141.659 1.00 35.03  ? 1650 LEU A CG    1 
ATOM   1609  C  CD1   . LEU A 1 1650 ? 131.397 189.947 140.866 1.00 38.53  ? 1650 LEU A CD1   1 
ATOM   1610  C  CD2   . LEU A 1 1650 ? 132.405 190.562 143.067 1.00 35.28  ? 1650 LEU A CD2   1 
ATOM   1611  N  N     . GLN A 1 1651 ? 136.203 193.382 140.568 1.00 31.19  ? 1651 GLN A N     1 
ATOM   1612  C  CA    . GLN A 1 1651 ? 137.369 193.400 139.692 1.00 30.17  ? 1651 GLN A CA    1 
ATOM   1613  C  C     . GLN A 1 1651 ? 138.651 193.037 140.431 1.00 29.55  ? 1651 GLN A C     1 
ATOM   1614  O  O     . GLN A 1 1651 ? 139.591 192.523 139.816 1.00 34.41  ? 1651 GLN A O     1 
ATOM   1615  C  CB    . GLN A 1 1651 ? 137.504 194.772 139.034 1.00 28.54  ? 1651 GLN A CB    1 
ATOM   1616  C  CG    . GLN A 1 1651 ? 136.231 195.251 138.355 1.00 32.77  ? 1651 GLN A CG    1 
ATOM   1617  C  CD    . GLN A 1 1651 ? 136.077 194.708 136.949 1.00 25.83  ? 1651 GLN A CD    1 
ATOM   1618  O  OE1   . GLN A 1 1651 ? 136.829 193.834 136.523 1.00 26.69  ? 1651 GLN A OE1   1 
ATOM   1619  N  NE2   . GLN A 1 1651 ? 135.095 195.224 136.220 1.00 28.13  ? 1651 GLN A NE2   1 
ATOM   1620  N  N     . LYS A 1 1652 ? 138.714 193.286 141.737 1.00 27.63  ? 1652 LYS A N     1 
ATOM   1621  C  CA    . LYS A 1 1652 ? 139.922 192.988 142.495 1.00 28.99  ? 1652 LYS A CA    1 
ATOM   1622  C  C     . LYS A 1 1652 ? 139.986 191.543 142.972 1.00 28.40  ? 1652 LYS A C     1 
ATOM   1623  O  O     . LYS A 1 1652 ? 140.970 191.166 143.616 1.00 27.83  ? 1652 LYS A O     1 
ATOM   1624  C  CB    . LYS A 1 1652 ? 140.043 193.933 143.693 1.00 27.45  ? 1652 LYS A CB    1 
ATOM   1625  C  CG    . LYS A 1 1652 ? 138.934 193.797 144.719 1.00 27.97  ? 1652 LYS A CG    1 
ATOM   1626  C  CD    . LYS A 1 1652 ? 139.171 194.731 145.893 1.00 32.27  ? 1652 LYS A CD    1 
ATOM   1627  C  CE    . LYS A 1 1652 ? 138.079 194.602 146.940 1.00 34.22  ? 1652 LYS A CE    1 
ATOM   1628  N  NZ    . LYS A 1 1652 ? 138.310 195.519 148.091 1.00 28.16  ? 1652 LYS A NZ    1 
ATOM   1629  N  N     . HIS A 1 1653 ? 138.973 190.729 142.674 1.00 25.43  ? 1653 HIS A N     1 
ATOM   1630  C  CA    . HIS A 1 1653 ? 138.945 189.339 143.104 1.00 26.52  ? 1653 HIS A CA    1 
ATOM   1631  C  C     . HIS A 1 1653 ? 139.171 188.343 141.975 1.00 25.06  ? 1653 HIS A C     1 
ATOM   1632  O  O     . HIS A 1 1653 ? 139.469 187.177 142.257 1.00 25.79  ? 1653 HIS A O     1 
ATOM   1633  C  CB    . HIS A 1 1653 ? 137.610 189.024 143.793 1.00 31.10  ? 1653 HIS A CB    1 
ATOM   1634  C  CG    . HIS A 1 1653 ? 137.318 189.900 144.970 1.00 29.74  ? 1653 HIS A CG    1 
ATOM   1635  N  ND1   . HIS A 1 1653 ? 137.993 189.787 146.166 1.00 28.90  ? 1653 HIS A ND1   1 
ATOM   1636  C  CD2   . HIS A 1 1653 ? 136.423 190.902 145.137 1.00 29.61  ? 1653 HIS A CD2   1 
ATOM   1637  C  CE1   . HIS A 1 1653 ? 137.528 190.683 147.018 1.00 29.62  ? 1653 HIS A CE1   1 
ATOM   1638  N  NE2   . HIS A 1 1653 ? 136.574 191.372 146.418 1.00 31.49  ? 1653 HIS A NE2   1 
ATOM   1639  N  N     . PHE A 1 1654 ? 139.035 188.761 140.714 1.00 26.20  ? 1654 PHE A N     1 
ATOM   1640  C  CA    . PHE A 1 1654 ? 139.250 187.846 139.598 1.00 23.16  ? 1654 PHE A CA    1 
ATOM   1641  C  C     . PHE A 1 1654 ? 140.685 187.347 139.520 1.00 25.05  ? 1654 PHE A C     1 
ATOM   1642  O  O     . PHE A 1 1654 ? 140.921 186.261 138.981 1.00 26.38  ? 1654 PHE A O     1 
ATOM   1643  C  CB    . PHE A 1 1654 ? 138.867 188.516 138.278 1.00 25.18  ? 1654 PHE A CB    1 
ATOM   1644  C  CG    . PHE A 1 1654 ? 137.391 188.721 138.109 1.00 27.16  ? 1654 PHE A CG    1 
ATOM   1645  C  CD1   . PHE A 1 1654 ? 136.550 187.643 137.894 1.00 27.36  ? 1654 PHE A CD1   1 
ATOM   1646  C  CD2   . PHE A 1 1654 ? 136.846 189.991 138.157 1.00 27.46  ? 1654 PHE A CD2   1 
ATOM   1647  C  CE1   . PHE A 1 1654 ? 135.191 187.829 137.737 1.00 24.61  ? 1654 PHE A CE1   1 
ATOM   1648  C  CE2   . PHE A 1 1654 ? 135.488 190.183 138.001 1.00 28.84  ? 1654 PHE A CE2   1 
ATOM   1649  C  CZ    . PHE A 1 1654 ? 134.660 189.100 137.790 1.00 30.93  ? 1654 PHE A CZ    1 
ATOM   1650  N  N     . LYS A 1 1655 ? 141.645 188.112 140.043 1.00 22.81  ? 1655 LYS A N     1 
ATOM   1651  C  CA    . LYS A 1 1655 ? 143.040 187.693 140.011 1.00 21.17  ? 1655 LYS A CA    1 
ATOM   1652  C  C     . LYS A 1 1655 ? 143.292 186.457 140.867 1.00 18.03  ? 1655 LYS A C     1 
ATOM   1653  O  O     . LYS A 1 1655 ? 144.154 185.642 140.521 1.00 18.16  ? 1655 LYS A O     1 
ATOM   1654  C  CB    . LYS A 1 1655 ? 143.933 188.855 140.455 1.00 19.77  ? 1655 LYS A CB    1 
ATOM   1655  C  CG    . LYS A 1 1655 ? 145.281 188.457 141.029 1.00 25.49  ? 1655 LYS A CG    1 
ATOM   1656  C  CD    . LYS A 1 1655 ? 145.529 189.145 142.360 1.00 27.66  ? 1655 LYS A CD    1 
ATOM   1657  C  CE    . LYS A 1 1655 ? 145.348 190.649 142.242 1.00 23.10  ? 1655 LYS A CE    1 
ATOM   1658  N  NZ    . LYS A 1 1655 ? 145.421 191.324 143.565 1.00 31.55  ? 1655 LYS A NZ    1 
ATOM   1659  N  N     . LYS A 1 1656 ? 142.547 186.287 141.958 1.00 16.86  ? 1656 LYS A N     1 
ATOM   1660  C  CA    . LYS A 1 1656 ? 142.722 185.136 142.833 1.00 18.71  ? 1656 LYS A CA    1 
ATOM   1661  C  C     . LYS A 1 1656 ? 142.114 183.855 142.277 1.00 18.63  ? 1656 LYS A C     1 
ATOM   1662  O  O     . LYS A 1 1656 ? 142.485 182.766 142.729 1.00 20.23  ? 1656 LYS A O     1 
ATOM   1663  C  CB    . LYS A 1 1656 ? 142.116 185.425 144.210 1.00 20.50  ? 1656 LYS A CB    1 
ATOM   1664  C  CG    . LYS A 1 1656 ? 142.310 186.856 144.672 1.00 23.71  ? 1656 LYS A CG    1 
ATOM   1665  C  CD    . LYS A 1 1656 ? 141.492 187.160 145.913 1.00 21.17  ? 1656 LYS A CD    1 
ATOM   1666  C  CE    . LYS A 1 1656 ? 141.522 188.646 146.226 1.00 26.38  ? 1656 LYS A CE    1 
ATOM   1667  N  NZ    . LYS A 1 1656 ? 140.670 188.993 147.393 1.00 20.96  ? 1656 LYS A NZ    1 
ATOM   1668  N  N     . MET A 1 1657 ? 141.195 183.951 141.315 1.00 17.34  ? 1657 MET A N     1 
ATOM   1669  C  CA    . MET A 1 1657 ? 140.537 182.769 140.775 1.00 19.05  ? 1657 MET A CA    1 
ATOM   1670  C  C     . MET A 1 1657 ? 140.997 182.399 139.372 1.00 18.75  ? 1657 MET A C     1 
ATOM   1671  O  O     . MET A 1 1657 ? 140.612 181.335 138.876 1.00 17.15  ? 1657 MET A O     1 
ATOM   1672  C  CB    . MET A 1 1657 ? 139.015 182.961 140.762 1.00 21.23  ? 1657 MET A CB    1 
ATOM   1673  C  CG    . MET A 1 1657 ? 138.498 183.957 141.784 1.00 25.98  ? 1657 MET A CG    1 
ATOM   1674  S  SD    . MET A 1 1657 ? 136.704 184.123 141.727 1.00 36.81  ? 1657 MET A SD    1 
ATOM   1675  C  CE    . MET A 1 1657 ? 136.531 185.711 140.923 1.00 25.87  ? 1657 MET A CE    1 
ATOM   1676  N  N     . PHE A 1 1658 ? 141.800 183.238 138.724 1.00 21.54  ? 1658 PHE A N     1 
ATOM   1677  C  CA    . PHE A 1 1658 ? 142.257 182.979 137.368 1.00 16.92  ? 1658 PHE A CA    1 
ATOM   1678  C  C     . PHE A 1 1658 ? 143.757 183.216 137.266 1.00 18.18  ? 1658 PHE A C     1 
ATOM   1679  O  O     . PHE A 1 1658 ? 144.349 183.956 138.055 1.00 21.91  ? 1658 PHE A O     1 
ATOM   1680  C  CB    . PHE A 1 1658 ? 141.522 183.852 136.346 1.00 15.71  ? 1658 PHE A CB    1 
ATOM   1681  C  CG    . PHE A 1 1658 ? 140.051 183.568 136.247 1.00 18.52  ? 1658 PHE A CG    1 
ATOM   1682  C  CD1   . PHE A 1 1658 ? 139.152 184.174 137.108 1.00 19.68  ? 1658 PHE A CD1   1 
ATOM   1683  C  CD2   . PHE A 1 1658 ? 139.566 182.692 135.291 1.00 16.96  ? 1658 PHE A CD2   1 
ATOM   1684  C  CE1   . PHE A 1 1658 ? 137.798 183.914 137.015 1.00 15.49  ? 1658 PHE A CE1   1 
ATOM   1685  C  CE2   . PHE A 1 1658 ? 138.215 182.427 135.193 1.00 15.70  ? 1658 PHE A CE2   1 
ATOM   1686  C  CZ    . PHE A 1 1658 ? 137.330 183.038 136.056 1.00 19.61  ? 1658 PHE A CZ    1 
ATOM   1687  N  N     . ALA A 1 1659 ? 144.368 182.564 136.273 1.00 18.01  ? 1659 ALA A N     1 
ATOM   1688  C  CA    . ALA A 1 1659 ? 145.808 182.690 136.071 1.00 14.88  ? 1659 ALA A CA    1 
ATOM   1689  C  C     . ALA A 1 1659 ? 146.179 184.073 135.549 1.00 17.62  ? 1659 ALA A C     1 
ATOM   1690  O  O     . ALA A 1 1659 ? 147.097 184.717 136.069 1.00 25.61  ? 1659 ALA A O     1 
ATOM   1691  C  CB    . ALA A 1 1659 ? 146.299 181.607 135.110 1.00 14.97  ? 1659 ALA A CB    1 
ATOM   1692  N  N     . GLY A 1 1660 ? 145.475 184.548 134.525 1.00 15.62  ? 1660 GLY A N     1 
ATOM   1693  C  CA    . GLY A 1 1660 ? 145.849 185.791 133.881 1.00 16.72  ? 1660 GLY A CA    1 
ATOM   1694  C  C     . GLY A 1 1660 ? 144.725 186.795 133.748 1.00 18.08  ? 1660 GLY A C     1 
ATOM   1695  O  O     . GLY A 1 1660 ? 144.913 187.869 133.170 1.00 23.23  ? 1660 GLY A O     1 
ATOM   1696  N  N     . VAL A 1 1661 ? 143.551 186.462 134.278 1.00 17.20  ? 1661 VAL A N     1 
ATOM   1697  C  CA    . VAL A 1 1661 ? 142.401 187.358 134.249 1.00 19.62  ? 1661 VAL A CA    1 
ATOM   1698  C  C     . VAL A 1 1661 ? 142.439 188.197 135.522 1.00 22.52  ? 1661 VAL A C     1 
ATOM   1699  O  O     . VAL A 1 1661 ? 142.245 187.687 136.627 1.00 26.86  ? 1661 VAL A O     1 
ATOM   1700  C  CB    . VAL A 1 1661 ? 141.085 186.594 134.112 1.00 20.25  ? 1661 VAL A CB    1 
ATOM   1701  C  CG1   . VAL A 1 1661 ? 140.009 187.508 133.579 1.00 21.99  ? 1661 VAL A CG1   1 
ATOM   1702  C  CG2   . VAL A 1 1661 ? 141.263 185.405 133.185 1.00 23.27  ? 1661 VAL A CG2   1 
ATOM   1703  N  N     . SER A 1 1662 ? 142.692 189.494 135.363 1.00 21.17  ? 1662 SER A N     1 
ATOM   1704  C  CA    . SER A 1 1662 ? 142.671 190.420 136.485 1.00 23.76  ? 1662 SER A CA    1 
ATOM   1705  C  C     . SER A 1 1662 ? 141.397 191.248 136.542 1.00 29.97  ? 1662 SER A C     1 
ATOM   1706  O  O     . SER A 1 1662 ? 141.015 191.695 137.628 1.00 34.40  ? 1662 SER A O     1 
ATOM   1707  C  CB    . SER A 1 1662 ? 143.881 191.358 136.423 1.00 23.12  ? 1662 SER A CB    1 
ATOM   1708  O  OG    . SER A 1 1662 ? 143.700 192.355 135.433 1.00 28.29  ? 1662 SER A OG    1 
ATOM   1709  N  N     . SER A 1 1663 ? 140.735 191.462 135.407 1.00 27.40  ? 1663 SER A N     1 
ATOM   1710  C  CA    . SER A 1 1663 ? 139.503 192.237 135.367 1.00 22.25  ? 1663 SER A CA    1 
ATOM   1711  C  C     . SER A 1 1663 ? 138.672 191.771 134.182 1.00 25.86  ? 1663 SER A C     1 
ATOM   1712  O  O     . SER A 1 1663 ? 139.180 191.136 133.254 1.00 32.38  ? 1663 SER A O     1 
ATOM   1713  C  CB    . SER A 1 1663 ? 139.787 193.740 135.271 1.00 26.58  ? 1663 SER A CB    1 
ATOM   1714  O  OG    . SER A 1 1663 ? 140.221 194.094 133.971 1.00 31.06  ? 1663 SER A OG    1 
ATOM   1715  N  N     . ILE A 1 1664 ? 137.381 192.094 134.227 1.00 27.88  ? 1664 ILE A N     1 
ATOM   1716  C  CA    . ILE A 1 1664 ? 136.447 191.738 133.167 1.00 28.15  ? 1664 ILE A CA    1 
ATOM   1717  C  C     . ILE A 1 1664 ? 135.937 193.015 132.515 1.00 30.87  ? 1664 ILE A C     1 
ATOM   1718  O  O     . ILE A 1 1664 ? 135.942 194.092 133.120 1.00 29.91  ? 1664 ILE A O     1 
ATOM   1719  C  CB    . ILE A 1 1664 ? 135.271 190.884 133.689 1.00 28.73  ? 1664 ILE A CB    1 
ATOM   1720  C  CG1   . ILE A 1 1664 ? 134.562 191.590 134.845 1.00 26.78  ? 1664 ILE A CG1   1 
ATOM   1721  C  CG2   . ILE A 1 1664 ? 135.759 189.511 134.121 1.00 29.66  ? 1664 ILE A CG2   1 
ATOM   1722  C  CD1   . ILE A 1 1664 ? 133.152 191.098 135.076 1.00 28.11  ? 1664 ILE A CD1   1 
ATOM   1723  N  N     . ILE A 1 1665 ? 135.493 192.888 131.267 1.00 31.71  ? 1665 ILE A N     1 
ATOM   1724  C  CA    . ILE A 1 1665 ? 135.008 194.016 130.480 1.00 30.85  ? 1665 ILE A CA    1 
ATOM   1725  C  C     . ILE A 1 1665 ? 133.495 193.913 130.360 1.00 36.05  ? 1665 ILE A C     1 
ATOM   1726  O  O     . ILE A 1 1665 ? 132.965 192.869 129.958 1.00 33.69  ? 1665 ILE A O     1 
ATOM   1727  C  CB    . ILE A 1 1665 ? 135.672 194.052 129.094 1.00 30.15  ? 1665 ILE A CB    1 
ATOM   1728  C  CG1   . ILE A 1 1665 ? 137.102 194.579 129.211 1.00 32.25  ? 1665 ILE A CG1   1 
ATOM   1729  C  CG2   . ILE A 1 1665 ? 134.864 194.909 128.130 1.00 34.42  ? 1665 ILE A CG2   1 
ATOM   1730  C  CD1   . ILE A 1 1665 ? 138.121 193.742 128.482 1.00 33.43  ? 1665 ILE A CD1   1 
ATOM   1731  N  N     . LEU A 1 1666 ? 132.799 194.990 130.708 1.00 37.63  ? 1666 LEU A N     1 
ATOM   1732  C  CA    . LEU A 1 1666 ? 131.347 195.030 130.684 1.00 40.20  ? 1666 LEU A CA    1 
ATOM   1733  C  C     . LEU A 1 1666 ? 130.871 196.164 129.785 1.00 44.65  ? 1666 LEU A C     1 
ATOM   1734  O  O     . LEU A 1 1666 ? 131.629 197.068 129.424 1.00 42.76  ? 1666 LEU A O     1 
ATOM   1735  C  CB    . LEU A 1 1666 ? 130.776 195.209 132.095 1.00 41.22  ? 1666 LEU A CB    1 
ATOM   1736  C  CG    . LEU A 1 1666 ? 131.212 194.210 133.165 1.00 38.44  ? 1666 LEU A CG    1 
ATOM   1737  C  CD1   . LEU A 1 1666 ? 131.608 194.950 134.432 1.00 33.12  ? 1666 LEU A CD1   1 
ATOM   1738  C  CD2   . LEU A 1 1666 ? 130.097 193.221 133.443 1.00 39.94  ? 1666 LEU A CD2   1 
ATOM   1739  N  N     . ASN A 1 1667 ? 129.591 196.105 129.426 1.00 48.81  ? 1667 ASN A N     1 
ATOM   1740  C  CA    . ASN A 1 1667 ? 128.957 197.181 128.676 1.00 44.66  ? 1667 ASN A CA    1 
ATOM   1741  C  C     . ASN A 1 1667 ? 128.640 198.324 129.639 1.00 51.82  ? 1667 ASN A C     1 
ATOM   1742  O  O     . ASN A 1 1667 ? 128.986 198.281 130.823 1.00 51.43  ? 1667 ASN A O     1 
ATOM   1743  C  CB    . ASN A 1 1667 ? 127.722 196.658 127.948 1.00 44.17  ? 1667 ASN A CB    1 
ATOM   1744  C  CG    . ASN A 1 1667 ? 126.742 195.970 128.877 1.00 49.17  ? 1667 ASN A CG    1 
ATOM   1745  O  OD1   . ASN A 1 1667 ? 127.028 195.754 130.055 1.00 52.91  ? 1667 ASN A OD1   1 
ATOM   1746  N  ND2   . ASN A 1 1667 ? 125.582 195.607 128.345 1.00 49.05  ? 1667 ASN A ND2   1 
ATOM   1747  N  N     . GLU A 1 1668 ? 127.978 199.373 129.145 1.00 54.54  ? 1668 GLU A N     1 
ATOM   1748  C  CA    . GLU A 1 1668 ? 127.699 200.511 130.014 1.00 53.51  ? 1668 GLU A CA    1 
ATOM   1749  C  C     . GLU A 1 1668 ? 126.494 200.256 130.914 1.00 55.32  ? 1668 GLU A C     1 
ATOM   1750  O  O     . GLU A 1 1668 ? 126.211 201.066 131.804 1.00 58.35  ? 1668 GLU A O     1 
ATOM   1751  C  CB    . GLU A 1 1668 ? 127.534 201.796 129.187 1.00 54.03  ? 1668 GLU A CB    1 
ATOM   1752  C  CG    . GLU A 1 1668 ? 126.115 202.205 128.775 1.00 59.56  ? 1668 GLU A CG    1 
ATOM   1753  C  CD    . GLU A 1 1668 ? 125.344 201.143 128.000 1.00 63.97  ? 1668 GLU A CD    1 
ATOM   1754  O  OE1   . GLU A 1 1668 ? 125.968 200.217 127.438 1.00 59.14  ? 1668 GLU A OE1   1 
ATOM   1755  O  OE2   . GLU A 1 1668 ? 124.098 201.236 127.952 1.00 59.29  ? 1668 GLU A OE2   1 
ATOM   1756  N  N     . ASP A 1 1669 ? 125.767 199.152 130.703 1.00 53.67  ? 1669 ASP A N     1 
ATOM   1757  C  CA    . ASP A 1 1669 ? 124.770 198.727 131.680 1.00 49.05  ? 1669 ASP A CA    1 
ATOM   1758  C  C     . ASP A 1 1669 ? 125.375 197.910 132.808 1.00 49.58  ? 1669 ASP A C     1 
ATOM   1759  O  O     . ASP A 1 1669 ? 124.712 197.712 133.830 1.00 52.60  ? 1669 ASP A O     1 
ATOM   1760  C  CB    . ASP A 1 1669 ? 123.669 197.883 131.034 1.00 50.83  ? 1669 ASP A CB    1 
ATOM   1761  C  CG    . ASP A 1 1669 ? 123.122 198.496 129.777 1.00 58.48  ? 1669 ASP A CG    1 
ATOM   1762  O  OD1   . ASP A 1 1669 ? 123.916 198.742 128.851 1.00 59.62  ? 1669 ASP A OD1   1 
ATOM   1763  O  OD2   . ASP A 1 1669 ? 121.901 198.745 129.726 1.00 61.16  ? 1669 ASP A OD2   1 
ATOM   1764  N  N     . ASN A 1 1670 ? 126.612 197.439 132.642 1.00 49.14  ? 1670 ASN A N     1 
ATOM   1765  C  CA    . ASN A 1 1670 ? 127.201 196.423 133.515 1.00 47.88  ? 1670 ASN A CA    1 
ATOM   1766  C  C     . ASN A 1 1670 ? 126.305 195.187 133.598 1.00 46.26  ? 1670 ASN A C     1 
ATOM   1767  O  O     . ASN A 1 1670 ? 126.163 194.565 134.652 1.00 45.31  ? 1670 ASN A O     1 
ATOM   1768  C  CB    . ASN A 1 1670 ? 127.506 196.981 134.907 1.00 45.88  ? 1670 ASN A CB    1 
ATOM   1769  C  CG    . ASN A 1 1670 ? 128.611 198.008 134.882 1.00 50.44  ? 1670 ASN A CG    1 
ATOM   1770  O  OD1   . ASN A 1 1670 ? 129.064 198.413 133.813 1.00 52.53  ? 1670 ASN A OD1   1 
ATOM   1771  N  ND2   . ASN A 1 1670 ? 129.078 198.412 136.056 1.00 53.06  ? 1670 ASN A ND2   1 
ATOM   1772  N  N     . SER A 1 1671 ? 125.702 194.819 132.464 1.00 45.59  ? 1671 SER A N     1 
ATOM   1773  C  CA    . SER A 1 1671 ? 124.833 193.653 132.393 1.00 45.69  ? 1671 SER A CA    1 
ATOM   1774  C  C     . SER A 1 1671 ? 125.343 192.563 131.463 1.00 44.52  ? 1671 SER A C     1 
ATOM   1775  O  O     . SER A 1 1671 ? 124.829 191.440 131.518 1.00 41.73  ? 1671 SER A O     1 
ATOM   1776  C  CB    . SER A 1 1671 ? 123.422 194.054 131.937 1.00 47.56  ? 1671 SER A CB    1 
ATOM   1777  O  OG    . SER A 1 1671 ? 123.459 194.729 130.692 1.00 43.39  ? 1671 SER A OG    1 
ATOM   1778  N  N     . VAL A 1 1672 ? 126.314 192.861 130.603 1.00 43.59  ? 1672 VAL A N     1 
ATOM   1779  C  CA    . VAL A 1 1672 ? 126.861 191.902 129.652 1.00 40.08  ? 1672 VAL A CA    1 
ATOM   1780  C  C     . VAL A 1 1672 ? 128.377 191.932 129.769 1.00 40.44  ? 1672 VAL A C     1 
ATOM   1781  O  O     . VAL A 1 1672 ? 128.983 193.010 129.747 1.00 44.44  ? 1672 VAL A O     1 
ATOM   1782  C  CB    . VAL A 1 1672 ? 126.422 192.215 128.208 1.00 36.84  ? 1672 VAL A CB    1 
ATOM   1783  C  CG1   . VAL A 1 1672 ? 127.033 191.218 127.241 1.00 40.18  ? 1672 VAL A CG1   1 
ATOM   1784  C  CG2   . VAL A 1 1672 ? 124.906 192.199 128.095 1.00 32.91  ? 1672 VAL A CG2   1 
ATOM   1785  N  N     . VAL A 1 1673 ? 128.988 190.758 129.894 1.00 32.86  ? 1673 VAL A N     1 
ATOM   1786  C  CA    . VAL A 1 1673 ? 130.439 190.640 129.973 1.00 33.11  ? 1673 VAL A CA    1 
ATOM   1787  C  C     . VAL A 1 1673 ? 130.968 190.489 128.551 1.00 33.14  ? 1673 VAL A C     1 
ATOM   1788  O  O     . VAL A 1 1673 ? 130.777 189.451 127.913 1.00 32.62  ? 1673 VAL A O     1 
ATOM   1789  C  CB    . VAL A 1 1673 ? 130.863 189.460 130.856 1.00 30.39  ? 1673 VAL A CB    1 
ATOM   1790  C  CG1   . VAL A 1 1673 ? 132.376 189.312 130.854 1.00 30.36  ? 1673 VAL A CG1   1 
ATOM   1791  C  CG2   . VAL A 1 1673 ? 130.346 189.648 132.273 1.00 28.47  ? 1673 VAL A CG2   1 
ATOM   1792  N  N     . LEU A 1 1674 ? 131.632 191.533 128.050 1.00 31.34  ? 1674 LEU A N     1 
ATOM   1793  C  CA    . LEU A 1 1674 ? 132.124 191.528 126.679 1.00 31.74  ? 1674 LEU A CA    1 
ATOM   1794  C  C     . LEU A 1 1674 ? 133.471 190.835 126.532 1.00 31.77  ? 1674 LEU A C     1 
ATOM   1795  O  O     . LEU A 1 1674 ? 133.869 190.523 125.405 1.00 31.89  ? 1674 LEU A O     1 
ATOM   1796  C  CB    . LEU A 1 1674 ? 132.229 192.961 126.152 1.00 37.80  ? 1674 LEU A CB    1 
ATOM   1797  C  CG    . LEU A 1 1674 ? 130.939 193.782 126.138 1.00 38.25  ? 1674 LEU A CG    1 
ATOM   1798  C  CD1   . LEU A 1 1674 ? 131.183 195.147 125.515 1.00 37.88  ? 1674 LEU A CD1   1 
ATOM   1799  C  CD2   . LEU A 1 1674 ? 129.843 193.039 125.394 1.00 36.83  ? 1674 LEU A CD2   1 
ATOM   1800  N  N     . GLY A 1 1675 ? 134.176 190.585 127.630 1.00 32.28  ? 1675 GLY A N     1 
ATOM   1801  C  CA    . GLY A 1 1675 ? 135.474 189.945 127.538 1.00 24.00  ? 1675 GLY A CA    1 
ATOM   1802  C  C     . GLY A 1 1675 ? 136.222 190.043 128.851 1.00 28.28  ? 1675 GLY A C     1 
ATOM   1803  O  O     . GLY A 1 1675 ? 135.639 190.345 129.893 1.00 34.34  ? 1675 GLY A O     1 
ATOM   1804  N  N     . ILE A 1 1676 ? 137.528 189.781 128.778 1.00 32.09  ? 1676 ILE A N     1 
ATOM   1805  C  CA    . ILE A 1 1676 ? 138.394 189.757 129.946 1.00 25.03  ? 1676 ILE A CA    1 
ATOM   1806  C  C     . ILE A 1 1676 ? 139.623 190.612 129.669 1.00 22.13  ? 1676 ILE A C     1 
ATOM   1807  O  O     . ILE A 1 1676 ? 139.961 190.907 128.521 1.00 27.23  ? 1676 ILE A O     1 
ATOM   1808  C  CB    . ILE A 1 1676 ? 138.817 188.323 130.325 1.00 23.83  ? 1676 ILE A CB    1 
ATOM   1809  C  CG1   . ILE A 1 1676 ? 139.416 187.611 129.113 1.00 23.68  ? 1676 ILE A CG1   1 
ATOM   1810  C  CG2   . ILE A 1 1676 ? 137.629 187.542 130.862 1.00 20.46  ? 1676 ILE A CG2   1 
ATOM   1811  C  CD1   . ILE A 1 1676 ? 139.807 186.180 129.383 1.00 23.60  ? 1676 ILE A CD1   1 
ATOM   1812  N  N     . SER A 1 1677 ? 140.294 191.011 130.748 1.00 24.48  ? 1677 SER A N     1 
ATOM   1813  C  CA    . SER A 1 1677 ? 141.503 191.814 130.655 1.00 30.05  ? 1677 SER A CA    1 
ATOM   1814  C  C     . SER A 1 1677 ? 142.533 191.289 131.644 1.00 28.86  ? 1677 SER A C     1 
ATOM   1815  O  O     . SER A 1 1677 ? 142.196 190.667 132.654 1.00 29.49  ? 1677 SER A O     1 
ATOM   1816  C  CB    . SER A 1 1677 ? 141.218 193.299 130.919 1.00 30.08  ? 1677 SER A CB    1 
ATOM   1817  O  OG    . SER A 1 1677 ? 142.415 194.058 130.908 1.00 34.26  ? 1677 SER A OG    1 
ATOM   1818  N  N     . SER A 1 1678 ? 143.800 191.547 131.340 1.00 28.80  ? 1678 SER A N     1 
ATOM   1819  C  CA    . SER A 1 1678 ? 144.918 191.130 132.172 1.00 31.90  ? 1678 SER A CA    1 
ATOM   1820  C  C     . SER A 1 1678 ? 145.482 192.324 132.931 1.00 32.96  ? 1678 SER A C     1 
ATOM   1821  O  O     . SER A 1 1678 ? 145.085 193.473 132.721 1.00 39.66  ? 1678 SER A O     1 
ATOM   1822  C  CB    . SER A 1 1678 ? 146.011 190.470 131.322 1.00 31.73  ? 1678 SER A CB    1 
ATOM   1823  O  OG    . SER A 1 1678 ? 146.559 191.390 130.396 1.00 32.99  ? 1678 SER A OG    1 
ATOM   1824  N  N     . ARG A 1 1679 ? 146.424 192.034 133.832 1.00 26.78  ? 1679 ARG A N     1 
ATOM   1825  C  CA    . ARG A 1 1679 ? 147.047 193.091 134.620 1.00 35.41  ? 1679 ARG A CA    1 
ATOM   1826  C  C     . ARG A 1 1679 ? 147.911 194.016 133.772 1.00 37.21  ? 1679 ARG A C     1 
ATOM   1827  O  O     . ARG A 1 1679 ? 148.237 195.120 134.219 1.00 43.11  ? 1679 ARG A O     1 
ATOM   1828  C  CB    . ARG A 1 1679 ? 147.881 192.485 135.751 1.00 36.07  ? 1679 ARG A CB    1 
ATOM   1829  C  CG    . ARG A 1 1679 ? 148.956 191.517 135.288 1.00 42.81  ? 1679 ARG A CG    1 
ATOM   1830  C  CD    . ARG A 1 1679 ? 150.114 191.467 136.272 1.00 46.89  ? 1679 ARG A CD    1 
ATOM   1831  N  NE    . ARG A 1 1679 ? 149.763 190.745 137.489 1.00 65.11  ? 1679 ARG A NE    1 
ATOM   1832  C  CZ    . ARG A 1 1679 ? 150.106 189.490 137.741 1.00 68.14  ? 1679 ARG A CZ    1 
ATOM   1833  N  NH1   . ARG A 1 1679 ? 150.816 188.781 136.879 1.00 60.02  ? 1679 ARG A NH1   1 
ATOM   1834  N  NH2   . ARG A 1 1679 ? 149.726 188.931 138.886 1.00 58.31  ? 1679 ARG A NH2   1 
ATOM   1835  N  N     . GLU A 1 1680 ? 148.287 193.593 132.568 1.00 36.00  ? 1680 GLU A N     1 
ATOM   1836  C  CA    . GLU A 1 1680 ? 149.051 194.426 131.650 1.00 33.47  ? 1680 GLU A CA    1 
ATOM   1837  C  C     . GLU A 1 1680 ? 148.166 195.208 130.688 1.00 38.84  ? 1680 GLU A C     1 
ATOM   1838  O  O     . GLU A 1 1680 ? 148.691 195.929 129.833 1.00 37.76  ? 1680 GLU A O     1 
ATOM   1839  C  CB    . GLU A 1 1680 ? 150.039 193.568 130.854 1.00 33.69  ? 1680 GLU A CB    1 
ATOM   1840  C  CG    . GLU A 1 1680 ? 151.066 192.846 131.710 1.00 40.24  ? 1680 GLU A CG    1 
ATOM   1841  C  CD    . GLU A 1 1680 ? 150.610 191.460 132.120 1.00 42.54  ? 1680 GLU A CD    1 
ATOM   1842  O  OE1   . GLU A 1 1680 ? 149.571 190.998 131.605 1.00 40.63  ? 1680 GLU A OE1   1 
ATOM   1843  O  OE2   . GLU A 1 1680 ? 151.292 190.832 132.957 1.00 45.85  ? 1680 GLU A OE2   1 
ATOM   1844  N  N     . GLY A 1 1681 ? 146.845 195.085 130.805 1.00 39.55  ? 1681 GLY A N     1 
ATOM   1845  C  CA    . GLY A 1 1681 ? 145.924 195.773 129.930 1.00 36.93  ? 1681 GLY A CA    1 
ATOM   1846  C  C     . GLY A 1 1681 ? 145.534 195.016 128.679 1.00 34.04  ? 1681 GLY A C     1 
ATOM   1847  O  O     . GLY A 1 1681 ? 144.676 195.498 127.928 1.00 40.55  ? 1681 GLY A O     1 
ATOM   1848  N  N     . GLU A 1 1682 ? 146.133 193.856 128.426 1.00 29.02  ? 1682 GLU A N     1 
ATOM   1849  C  CA    . GLU A 1 1682 ? 145.761 193.061 127.264 1.00 30.42  ? 1682 GLU A CA    1 
ATOM   1850  C  C     . GLU A 1 1682 ? 144.344 192.528 127.423 1.00 33.58  ? 1682 GLU A C     1 
ATOM   1851  O  O     . GLU A 1 1682 ? 143.973 192.005 128.478 1.00 36.74  ? 1682 GLU A O     1 
ATOM   1852  C  CB    . GLU A 1 1682 ? 146.744 191.908 127.073 1.00 30.33  ? 1682 GLU A CB    1 
ATOM   1853  C  CG    . GLU A 1 1682 ? 146.622 191.200 125.736 1.00 25.41  ? 1682 GLU A CG    1 
ATOM   1854  C  CD    . GLU A 1 1682 ? 147.515 189.980 125.644 1.00 27.65  ? 1682 GLU A CD    1 
ATOM   1855  O  OE1   . GLU A 1 1682 ? 147.213 188.970 126.313 1.00 32.94  ? 1682 GLU A OE1   1 
ATOM   1856  O  OE2   . GLU A 1 1682 ? 148.521 190.032 124.905 1.00 29.70  ? 1682 GLU A OE2   1 
ATOM   1857  N  N     . GLU A 1 1683 ? 143.549 192.656 126.364 1.00 25.03  ? 1683 GLU A N     1 
ATOM   1858  C  CA    . GLU A 1 1683 ? 142.133 192.327 126.403 1.00 27.93  ? 1683 GLU A CA    1 
ATOM   1859  C  C     . GLU A 1 1683 ? 141.818 191.210 125.420 1.00 27.45  ? 1683 GLU A C     1 
ATOM   1860  O  O     . GLU A 1 1683 ? 142.403 191.138 124.335 1.00 32.86  ? 1683 GLU A O     1 
ATOM   1861  C  CB    . GLU A 1 1683 ? 141.273 193.551 126.075 1.00 32.39  ? 1683 GLU A CB    1 
ATOM   1862  C  CG    . GLU A 1 1683 ? 141.425 194.703 127.050 1.00 38.15  ? 1683 GLU A CG    1 
ATOM   1863  C  CD    . GLU A 1 1683 ? 141.088 196.040 126.420 1.00 51.54  ? 1683 GLU A CD    1 
ATOM   1864  O  OE1   . GLU A 1 1683 ? 141.466 196.260 125.250 1.00 54.63  ? 1683 GLU A OE1   1 
ATOM   1865  O  OE2   . GLU A 1 1683 ? 140.443 196.871 127.093 1.00 56.57  ? 1683 GLU A OE2   1 
ATOM   1866  N  N     . VAL A 1 1684 ? 140.892 190.340 125.812 1.00 23.32  ? 1684 VAL A N     1 
ATOM   1867  C  CA    . VAL A 1 1684 ? 140.338 189.313 124.939 1.00 20.58  ? 1684 VAL A CA    1 
ATOM   1868  C  C     . VAL A 1 1684 ? 138.846 189.580 124.821 1.00 28.79  ? 1684 VAL A C     1 
ATOM   1869  O  O     . VAL A 1 1684 ? 138.138 189.628 125.834 1.00 32.76  ? 1684 VAL A O     1 
ATOM   1870  C  CB    . VAL A 1 1684 ? 140.598 187.897 125.473 1.00 21.03  ? 1684 VAL A CB    1 
ATOM   1871  C  CG1   . VAL A 1 1684 ? 140.009 186.863 124.532 1.00 26.52  ? 1684 VAL A CG1   1 
ATOM   1872  C  CG2   . VAL A 1 1684 ? 142.080 187.670 125.654 1.00 21.47  ? 1684 VAL A CG2   1 
ATOM   1873  N  N     . MET A 1 1685 ? 138.369 189.753 123.593 1.00 26.66  ? 1685 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1685 ? 136.972 190.068 123.334 1.00 24.71  ? 1685 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1685 ? 136.222 188.774 123.045 1.00 28.51  ? 1685 MET A C     1 
ATOM   1876  O  O     . MET A 1 1685 ? 136.582 188.036 122.122 1.00 37.31  ? 1685 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1685 ? 136.843 191.043 122.165 1.00 32.72  ? 1685 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1685 ? 137.277 192.464 122.495 1.00 37.47  ? 1685 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1685 ? 136.451 193.148 123.945 1.00 49.37  ? 1685 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1685 ? 134.735 193.026 123.447 1.00 33.11  ? 1685 MET A CE    1 
ATOM   1881  N  N     . PHE A 1 1686 ? 135.189 188.501 123.838 1.00 29.70  ? 1686 PHE A N     1 
ATOM   1882  C  CA    . PHE A 1 1686 ? 134.420 187.276 123.674 1.00 29.32  ? 1686 PHE A CA    1 
ATOM   1883  C  C     . PHE A 1 1686 ? 133.661 187.288 122.354 1.00 31.32  ? 1686 PHE A C     1 
ATOM   1884  O  O     . PHE A 1 1686 ? 133.066 188.298 121.968 1.00 32.67  ? 1686 PHE A O     1 
ATOM   1885  C  CB    . PHE A 1 1686 ? 133.440 187.101 124.835 1.00 25.48  ? 1686 PHE A CB    1 
ATOM   1886  C  CG    . PHE A 1 1686 ? 134.095 186.750 126.143 1.00 25.12  ? 1686 PHE A CG    1 
ATOM   1887  C  CD1   . PHE A 1 1686 ? 135.436 186.412 126.198 1.00 30.95  ? 1686 PHE A CD1   1 
ATOM   1888  C  CD2   . PHE A 1 1686 ? 133.362 186.754 127.318 1.00 29.13  ? 1686 PHE A CD2   1 
ATOM   1889  C  CE1   . PHE A 1 1686 ? 136.034 186.087 127.401 1.00 31.09  ? 1686 PHE A CE1   1 
ATOM   1890  C  CE2   . PHE A 1 1686 ? 133.955 186.430 128.523 1.00 26.33  ? 1686 PHE A CE2   1 
ATOM   1891  C  CZ    . PHE A 1 1686 ? 135.292 186.096 128.564 1.00 24.23  ? 1686 PHE A CZ    1 
ATOM   1892  N  N     . LYS A 1 1687 ? 133.689 186.151 121.655 1.00 30.12  ? 1687 LYS A N     1 
ATOM   1893  C  CA    . LYS A 1 1687 ? 132.901 186.021 120.435 1.00 30.15  ? 1687 LYS A CA    1 
ATOM   1894  C  C     . LYS A 1 1687 ? 131.416 185.915 120.755 1.00 35.92  ? 1687 LYS A C     1 
ATOM   1895  O  O     . LYS A 1 1687 ? 130.572 186.393 119.988 1.00 40.76  ? 1687 LYS A O     1 
ATOM   1896  C  CB    . LYS A 1 1687 ? 133.371 184.809 119.632 1.00 30.05  ? 1687 LYS A CB    1 
ATOM   1897  C  CG    . LYS A 1 1687 ? 134.845 184.488 119.807 1.00 30.46  ? 1687 LYS A CG    1 
ATOM   1898  C  CD    . LYS A 1 1687 ? 135.722 185.493 119.077 1.00 32.28  ? 1687 LYS A CD    1 
ATOM   1899  C  CE    . LYS A 1 1687 ? 136.071 185.014 117.677 1.00 35.14  ? 1687 LYS A CE    1 
ATOM   1900  N  NZ    . LYS A 1 1687 ? 137.120 185.865 117.050 1.00 33.87  ? 1687 LYS A NZ    1 
ATOM   1901  N  N     . THR A 1 1688 ? 131.081 185.292 121.881 1.00 35.42  ? 1688 THR A N     1 
ATOM   1902  C  CA    . THR A 1 1688 ? 129.707 185.232 122.380 1.00 34.59  ? 1688 THR A CA    1 
ATOM   1903  C  C     . THR A 1 1688 ? 129.660 185.920 123.735 1.00 37.30  ? 1688 THR A C     1 
ATOM   1904  O  O     . THR A 1 1688 ? 130.043 185.317 124.754 1.00 37.93  ? 1688 THR A O     1 
ATOM   1905  C  CB    . THR A 1 1688 ? 129.221 183.788 122.492 1.00 34.94  ? 1688 THR A CB    1 
ATOM   1906  O  OG1   . THR A 1 1688 ? 129.459 183.104 121.255 1.00 40.56  ? 1688 THR A OG1   1 
ATOM   1907  C  CG2   . THR A 1 1688 ? 127.734 183.752 122.809 1.00 31.91  ? 1688 THR A CG2   1 
ATOM   1908  N  N     . PRO A 1 1689 ? 129.219 187.176 123.802 1.00 37.98  ? 1689 PRO A N     1 
ATOM   1909  C  CA    . PRO A 1 1689 ? 129.195 187.881 125.089 1.00 34.65  ? 1689 PRO A CA    1 
ATOM   1910  C  C     . PRO A 1 1689 ? 128.265 187.202 126.085 1.00 33.93  ? 1689 PRO A C     1 
ATOM   1911  O  O     . PRO A 1 1689 ? 127.208 186.681 125.724 1.00 38.69  ? 1689 PRO A O     1 
ATOM   1912  C  CB    . PRO A 1 1689 ? 128.697 189.282 124.717 1.00 37.80  ? 1689 PRO A CB    1 
ATOM   1913  C  CG    . PRO A 1 1689 ? 128.953 189.410 123.250 1.00 35.67  ? 1689 PRO A CG    1 
ATOM   1914  C  CD    . PRO A 1 1689 ? 128.777 188.034 122.692 1.00 35.48  ? 1689 PRO A CD    1 
ATOM   1915  N  N     . VAL A 1 1690 ? 128.674 187.215 127.349 1.00 34.49  ? 1690 VAL A N     1 
ATOM   1916  C  CA    . VAL A 1 1690 ? 127.893 186.622 128.428 1.00 33.44  ? 1690 VAL A CA    1 
ATOM   1917  C  C     . VAL A 1 1690 ? 127.043 187.709 129.069 1.00 37.97  ? 1690 VAL A C     1 
ATOM   1918  O  O     . VAL A 1 1690 ? 127.571 188.709 129.571 1.00 40.43  ? 1690 VAL A O     1 
ATOM   1919  C  CB    . VAL A 1 1690 ? 128.808 185.953 129.467 1.00 30.11  ? 1690 VAL A CB    1 
ATOM   1920  C  CG1   . VAL A 1 1690 ? 127.998 185.488 130.664 1.00 34.03  ? 1690 VAL A CG1   1 
ATOM   1921  C  CG2   . VAL A 1 1690 ? 129.560 184.791 128.841 1.00 32.21  ? 1690 VAL A CG2   1 
ATOM   1922  N  N     . SER A 1 1691 ? 125.729 187.514 129.059 1.00 40.79  ? 1691 SER A N     1 
ATOM   1923  C  CA    . SER A 1 1691 ? 124.788 188.479 129.611 1.00 42.54  ? 1691 SER A CA    1 
ATOM   1924  C  C     . SER A 1 1691 ? 124.442 188.095 131.043 1.00 43.32  ? 1691 SER A C     1 
ATOM   1925  O  O     . SER A 1 1691 ? 123.993 186.974 131.300 1.00 44.86  ? 1691 SER A O     1 
ATOM   1926  C  CB    . SER A 1 1691 ? 123.521 188.553 128.759 1.00 44.96  ? 1691 SER A CB    1 
ATOM   1927  O  OG    . SER A 1 1691 ? 122.473 187.796 129.336 1.00 48.65  ? 1691 SER A OG    1 
ATOM   1928  N  N     . ILE A 1 1692 ? 124.650 189.031 131.970 1.00 44.80  ? 1692 ILE A N     1 
ATOM   1929  C  CA    . ILE A 1 1692 ? 124.375 188.760 133.377 1.00 40.59  ? 1692 ILE A CA    1 
ATOM   1930  C  C     . ILE A 1 1692 ? 122.877 188.787 133.660 1.00 45.77  ? 1692 ILE A C     1 
ATOM   1931  O  O     . ILE A 1 1692 ? 122.414 188.164 134.622 1.00 50.06  ? 1692 ILE A O     1 
ATOM   1932  C  CB    . ILE A 1 1692 ? 125.138 189.758 134.264 1.00 36.04  ? 1692 ILE A CB    1 
ATOM   1933  C  CG1   . ILE A 1 1692 ? 126.579 189.911 133.772 1.00 36.36  ? 1692 ILE A CG1   1 
ATOM   1934  C  CG2   . ILE A 1 1692 ? 125.117 189.316 135.718 1.00 36.08  ? 1692 ILE A CG2   1 
ATOM   1935  C  CD1   . ILE A 1 1692 ? 127.457 190.737 134.685 1.00 33.28  ? 1692 ILE A CD1   1 
ATOM   1936  N  N     . THR A 1 1693 ? 122.099 189.500 132.843 1.00 47.83  ? 1693 THR A N     1 
ATOM   1937  C  CA    . THR A 1 1693 ? 120.654 189.542 133.049 1.00 47.35  ? 1693 THR A CA    1 
ATOM   1938  C  C     . THR A 1 1693 ? 120.030 188.163 132.870 1.00 48.63  ? 1693 THR A C     1 
ATOM   1939  O  O     . THR A 1 1693 ? 119.147 187.768 133.641 1.00 50.53  ? 1693 THR A O     1 
ATOM   1940  C  CB    . THR A 1 1693 ? 120.014 190.546 132.092 1.00 48.77  ? 1693 THR A CB    1 
ATOM   1941  O  OG1   . THR A 1 1693 ? 120.428 190.260 130.750 1.00 48.38  ? 1693 THR A OG1   1 
ATOM   1942  C  CG2   . THR A 1 1693 ? 120.430 191.964 132.453 1.00 46.42  ? 1693 THR A CG2   1 
ATOM   1943  N  N     . GLU A 1 1694 ? 120.475 187.416 131.857 1.00 46.97  ? 1694 GLU A N     1 
ATOM   1944  C  CA    . GLU A 1 1694 ? 119.935 186.080 131.628 1.00 48.49  ? 1694 GLU A CA    1 
ATOM   1945  C  C     . GLU A 1 1694 ? 120.353 185.106 132.722 1.00 48.60  ? 1694 GLU A C     1 
ATOM   1946  O  O     . GLU A 1 1694 ? 119.625 184.150 133.009 1.00 48.91  ? 1694 GLU A O     1 
ATOM   1947  C  CB    . GLU A 1 1694 ? 120.379 185.561 130.261 1.00 52.53  ? 1694 GLU A CB    1 
ATOM   1948  C  CG    . GLU A 1 1694 ? 119.381 184.630 129.594 1.00 56.98  ? 1694 GLU A CG    1 
ATOM   1949  C  CD    . GLU A 1 1694 ? 119.463 184.677 128.081 1.00 65.12  ? 1694 GLU A CD    1 
ATOM   1950  O  OE1   . GLU A 1 1694 ? 120.592 184.677 127.545 1.00 58.53  ? 1694 GLU A OE1   1 
ATOM   1951  O  OE2   . GLU A 1 1694 ? 118.399 184.714 127.427 1.00 69.18  ? 1694 GLU A OE2   1 
ATOM   1952  N  N     . HIS A 1 1695 ? 121.512 185.328 133.339 1.00 47.55  ? 1695 HIS A N     1 
ATOM   1953  C  CA    . HIS A 1 1695 ? 122.046 184.450 134.379 1.00 47.54  ? 1695 HIS A CA    1 
ATOM   1954  C  C     . HIS A 1 1695 ? 122.403 185.305 135.586 1.00 49.92  ? 1695 HIS A C     1 
ATOM   1955  O  O     . HIS A 1 1695 ? 123.581 185.607 135.823 1.00 52.60  ? 1695 HIS A O     1 
ATOM   1956  C  CB    . HIS A 1 1695 ? 123.253 183.665 133.866 1.00 41.79  ? 1695 HIS A CB    1 
ATOM   1957  C  CG    . HIS A 1 1695 ? 123.062 183.095 132.495 1.00 50.58  ? 1695 HIS A CG    1 
ATOM   1958  N  ND1   . HIS A 1 1695 ? 122.559 181.830 132.279 1.00 50.64  ? 1695 HIS A ND1   1 
ATOM   1959  C  CD2   . HIS A 1 1695 ? 123.296 183.620 131.270 1.00 46.77  ? 1695 HIS A CD2   1 
ATOM   1960  C  CE1   . HIS A 1 1695 ? 122.497 181.599 130.980 1.00 45.34  ? 1695 HIS A CE1   1 
ATOM   1961  N  NE2   . HIS A 1 1695 ? 122.939 182.670 130.345 1.00 44.08  ? 1695 HIS A NE2   1 
ATOM   1962  N  N     . PRO A 1 1696 ? 121.404 185.726 136.366 1.00 44.50  ? 1696 PRO A N     1 
ATOM   1963  C  CA    . PRO A 1 1696 ? 121.685 186.620 137.502 1.00 43.53  ? 1696 PRO A CA    1 
ATOM   1964  C  C     . PRO A 1 1696 ? 122.601 186.014 138.550 1.00 49.31  ? 1696 PRO A C     1 
ATOM   1965  O  O     . PRO A 1 1696 ? 123.334 186.757 139.216 1.00 55.65  ? 1696 PRO A O     1 
ATOM   1966  C  CB    . PRO A 1 1696 ? 120.289 186.910 138.075 1.00 52.80  ? 1696 PRO A CB    1 
ATOM   1967  C  CG    . PRO A 1 1696 ? 119.329 186.537 136.983 1.00 50.38  ? 1696 PRO A CG    1 
ATOM   1968  C  CD    . PRO A 1 1696 ? 119.972 185.403 136.259 1.00 44.38  ? 1696 PRO A CD    1 
ATOM   1969  N  N     . LYS A 1 1697 ? 122.576 184.695 138.727 1.00 44.26  ? 1697 LYS A N     1 
ATOM   1970  C  CA    . LYS A 1 1697 ? 123.392 184.065 139.757 1.00 41.64  ? 1697 LYS A CA    1 
ATOM   1971  C  C     . LYS A 1 1697 ? 124.875 184.275 139.476 1.00 40.05  ? 1697 LYS A C     1 
ATOM   1972  O  O     . LYS A 1 1697 ? 125.339 184.131 138.342 1.00 40.40  ? 1697 LYS A O     1 
ATOM   1973  C  CB    . LYS A 1 1697 ? 123.078 182.572 139.846 1.00 47.85  ? 1697 LYS A CB    1 
ATOM   1974  C  CG    . LYS A 1 1697 ? 121.715 182.263 140.441 1.00 50.41  ? 1697 LYS A CG    1 
ATOM   1975  C  CD    . LYS A 1 1697 ? 121.607 180.801 140.843 1.00 55.67  ? 1697 LYS A CD    1 
ATOM   1976  C  CE    . LYS A 1 1697 ? 122.608 180.452 141.933 1.00 52.76  ? 1697 LYS A CE    1 
ATOM   1977  N  NZ    . LYS A 1 1697 ? 122.664 181.491 142.998 1.00 48.84  ? 1697 LYS A NZ    1 
ATOM   1978  N  N     . ILE A 1 1698 ? 125.619 184.614 140.531 1.00 40.94  ? 1698 ILE A N     1 
ATOM   1979  C  CA    . ILE A 1 1698 ? 127.041 184.917 140.386 1.00 34.44  ? 1698 ILE A CA    1 
ATOM   1980  C  C     . ILE A 1 1698 ? 127.811 183.686 139.922 1.00 34.96  ? 1698 ILE A C     1 
ATOM   1981  O  O     . ILE A 1 1698 ? 128.688 183.771 139.054 1.00 33.46  ? 1698 ILE A O     1 
ATOM   1982  C  CB    . ILE A 1 1698 ? 127.602 185.487 141.704 1.00 41.20  ? 1698 ILE A CB    1 
ATOM   1983  C  CG1   . ILE A 1 1698 ? 129.076 185.865 141.548 1.00 35.97  ? 1698 ILE A CG1   1 
ATOM   1984  C  CG2   . ILE A 1 1698 ? 127.374 184.528 142.864 1.00 42.41  ? 1698 ILE A CG2   1 
ATOM   1985  C  CD1   . ILE A 1 1698 ? 129.309 187.008 140.601 1.00 35.57  ? 1698 ILE A CD1   1 
ATOM   1986  N  N     . ASN A 1 1699 ? 127.493 182.520 140.489 1.00 38.99  ? 1699 ASN A N     1 
ATOM   1987  C  CA    . ASN A 1 1699 ? 128.219 181.307 140.130 1.00 33.67  ? 1699 ASN A CA    1 
ATOM   1988  C  C     . ASN A 1 1699 ? 127.823 180.806 138.746 1.00 32.66  ? 1699 ASN A C     1 
ATOM   1989  O  O     . ASN A 1 1699 ? 128.559 180.029 138.127 1.00 35.54  ? 1699 ASN A O     1 
ATOM   1990  C  CB    . ASN A 1 1699 ? 127.988 180.227 141.189 1.00 33.83  ? 1699 ASN A CB    1 
ATOM   1991  C  CG    . ASN A 1 1699 ? 126.518 179.899 141.384 1.00 44.95  ? 1699 ASN A CG    1 
ATOM   1992  O  OD1   . ASN A 1 1699 ? 125.653 180.390 140.658 1.00 49.72  ? 1699 ASN A OD1   1 
ATOM   1993  N  ND2   . ASN A 1 1699 ? 126.230 179.066 142.376 1.00 43.26  ? 1699 ASN A ND2   1 
ATOM   1994  N  N     . GLU A 1 1700 ? 126.666 181.240 138.243 1.00 32.79  ? 1700 GLU A N     1 
ATOM   1995  C  CA    . GLU A 1 1700 ? 126.201 180.757 136.947 1.00 33.16  ? 1700 GLU A CA    1 
ATOM   1996  C  C     . GLU A 1 1700 ? 126.919 181.461 135.801 1.00 31.37  ? 1700 GLU A C     1 
ATOM   1997  O  O     . GLU A 1 1700 ? 127.471 180.809 134.907 1.00 31.27  ? 1700 GLU A O     1 
ATOM   1998  C  CB    . GLU A 1 1700 ? 124.687 180.939 136.833 1.00 39.87  ? 1700 GLU A CB    1 
ATOM   1999  C  CG    . GLU A 1 1700 ? 124.103 180.431 135.526 1.00 46.44  ? 1700 GLU A CG    1 
ATOM   2000  C  CD    . GLU A 1 1700 ? 122.598 180.595 135.457 1.00 58.07  ? 1700 GLU A CD    1 
ATOM   2001  O  OE1   . GLU A 1 1700 ? 121.960 180.695 136.526 1.00 54.21  ? 1700 GLU A OE1   1 
ATOM   2002  O  OE2   . GLU A 1 1700 ? 122.053 180.621 134.333 1.00 60.78  ? 1700 GLU A OE2   1 
ATOM   2003  N  N     . TRP A 1 1701 ? 126.921 182.798 135.804 1.00 27.72  ? 1701 TRP A N     1 
ATOM   2004  C  CA    . TRP A 1 1701 ? 127.532 183.529 134.700 1.00 30.24  ? 1701 TRP A CA    1 
ATOM   2005  C  C     . TRP A 1 1701 ? 129.049 183.573 134.801 1.00 28.11  ? 1701 TRP A C     1 
ATOM   2006  O  O     . TRP A 1 1701 ? 129.716 183.823 133.791 1.00 29.81  ? 1701 TRP A O     1 
ATOM   2007  C  CB    . TRP A 1 1701 ? 126.948 184.947 134.608 1.00 35.75  ? 1701 TRP A CB    1 
ATOM   2008  C  CG    . TRP A 1 1701 ? 127.328 185.914 135.700 1.00 29.38  ? 1701 TRP A CG    1 
ATOM   2009  C  CD1   . TRP A 1 1701 ? 126.525 186.352 136.711 1.00 29.43  ? 1701 TRP A CD1   1 
ATOM   2010  C  CD2   . TRP A 1 1701 ? 128.556 186.649 135.823 1.00 30.65  ? 1701 TRP A CD2   1 
ATOM   2011  N  NE1   . TRP A 1 1701 ? 127.193 187.262 137.491 1.00 30.69  ? 1701 TRP A NE1   1 
ATOM   2012  C  CE2   . TRP A 1 1701 ? 128.440 187.467 136.963 1.00 28.18  ? 1701 TRP A CE2   1 
ATOM   2013  C  CE3   . TRP A 1 1701 ? 129.750 186.676 135.094 1.00 34.37  ? 1701 TRP A CE3   1 
ATOM   2014  C  CZ2   . TRP A 1 1701 ? 129.471 188.302 137.391 1.00 27.20  ? 1701 TRP A CZ2   1 
ATOM   2015  C  CZ3   . TRP A 1 1701 ? 130.772 187.501 135.523 1.00 30.29  ? 1701 TRP A CZ3   1 
ATOM   2016  C  CH2   . TRP A 1 1701 ? 130.626 188.303 136.661 1.00 27.28  ? 1701 TRP A CH2   1 
ATOM   2017  N  N     . LEU A 1 1702 ? 129.608 183.334 135.989 1.00 25.31  ? 1702 LEU A N     1 
ATOM   2018  C  CA    . LEU A 1 1702 ? 131.053 183.163 136.100 1.00 22.29  ? 1702 LEU A CA    1 
ATOM   2019  C  C     . LEU A 1 1702 ? 131.513 181.909 135.368 1.00 24.33  ? 1702 LEU A C     1 
ATOM   2020  O  O     . LEU A 1 1702 ? 132.563 181.913 134.717 1.00 26.89  ? 1702 LEU A O     1 
ATOM   2021  C  CB    . LEU A 1 1702 ? 131.471 183.111 137.569 1.00 23.04  ? 1702 LEU A CB    1 
ATOM   2022  C  CG    . LEU A 1 1702 ? 131.925 184.435 138.182 1.00 22.13  ? 1702 LEU A CG    1 
ATOM   2023  C  CD1   . LEU A 1 1702 ? 132.269 184.259 139.651 1.00 21.18  ? 1702 LEU A CD1   1 
ATOM   2024  C  CD2   . LEU A 1 1702 ? 133.113 184.982 137.418 1.00 21.63  ? 1702 LEU A CD2   1 
ATOM   2025  N  N     . THR A 1 1703 ? 130.742 180.824 135.474 1.00 25.55  ? 1703 THR A N     1 
ATOM   2026  C  CA    . THR A 1 1703 ? 131.059 179.613 134.724 1.00 26.49  ? 1703 THR A CA    1 
ATOM   2027  C  C     . THR A 1 1703 ? 130.982 179.864 133.224 1.00 24.54  ? 1703 THR A C     1 
ATOM   2028  O  O     . THR A 1 1703 ? 131.821 179.374 132.460 1.00 27.35  ? 1703 THR A O     1 
ATOM   2029  C  CB    . THR A 1 1703 ? 130.112 178.483 135.129 1.00 25.29  ? 1703 THR A CB    1 
ATOM   2030  O  OG1   . THR A 1 1703 ? 130.071 178.380 136.558 1.00 28.92  ? 1703 THR A OG1   1 
ATOM   2031  C  CG2   . THR A 1 1703 ? 130.581 177.161 134.549 1.00 17.22  ? 1703 THR A CG2   1 
ATOM   2032  N  N     . LEU A 1 1704 ? 129.976 180.624 132.786 1.00 24.33  ? 1704 LEU A N     1 
ATOM   2033  C  CA    . LEU A 1 1704 ? 129.864 180.965 131.372 1.00 22.58  ? 1704 LEU A CA    1 
ATOM   2034  C  C     . LEU A 1 1704 ? 131.035 181.829 130.919 1.00 22.81  ? 1704 LEU A C     1 
ATOM   2035  O  O     . LEU A 1 1704 ? 131.531 181.674 129.797 1.00 25.91  ? 1704 LEU A O     1 
ATOM   2036  C  CB    . LEU A 1 1704 ? 128.537 181.675 131.109 1.00 26.54  ? 1704 LEU A CB    1 
ATOM   2037  C  CG    . LEU A 1 1704 ? 127.327 180.761 130.922 1.00 24.17  ? 1704 LEU A CG    1 
ATOM   2038  C  CD1   . LEU A 1 1704 ? 126.040 181.519 131.188 1.00 28.06  ? 1704 LEU A CD1   1 
ATOM   2039  C  CD2   . LEU A 1 1704 ? 127.320 180.161 129.526 1.00 24.32  ? 1704 LEU A CD2   1 
ATOM   2040  N  N     . VAL A 1 1705 ? 131.483 182.751 131.775 1.00 22.98  ? 1705 VAL A N     1 
ATOM   2041  C  CA    . VAL A 1 1705 ? 132.636 183.582 131.438 1.00 21.19  ? 1705 VAL A CA    1 
ATOM   2042  C  C     . VAL A 1 1705 ? 133.885 182.723 131.292 1.00 21.49  ? 1705 VAL A C     1 
ATOM   2043  O  O     . VAL A 1 1705 ? 134.663 182.888 130.344 1.00 24.58  ? 1705 VAL A O     1 
ATOM   2044  C  CB    . VAL A 1 1705 ? 132.823 184.687 132.495 1.00 20.16  ? 1705 VAL A CB    1 
ATOM   2045  C  CG1   . VAL A 1 1705 ? 134.244 185.225 132.465 1.00 21.58  ? 1705 VAL A CG1   1 
ATOM   2046  C  CG2   . VAL A 1 1705 ? 131.824 185.809 132.267 1.00 27.37  ? 1705 VAL A CG2   1 
ATOM   2047  N  N     . GLU A 1 1706 ? 134.095 181.791 132.224 1.00 24.27  ? 1706 GLU A N     1 
ATOM   2048  C  CA    . GLU A 1 1706 ? 135.234 180.884 132.122 1.00 20.69  ? 1706 GLU A CA    1 
ATOM   2049  C  C     . GLU A 1 1706 ? 135.130 180.007 130.880 1.00 23.32  ? 1706 GLU A C     1 
ATOM   2050  O  O     . GLU A 1 1706 ? 136.122 179.804 130.169 1.00 23.13  ? 1706 GLU A O     1 
ATOM   2051  C  CB    . GLU A 1 1706 ? 135.331 180.023 133.381 1.00 23.24  ? 1706 GLU A CB    1 
ATOM   2052  C  CG    . GLU A 1 1706 ? 136.174 178.770 133.219 1.00 25.62  ? 1706 GLU A CG    1 
ATOM   2053  C  CD    . GLU A 1 1706 ? 136.193 177.918 134.472 1.00 32.45  ? 1706 GLU A CD    1 
ATOM   2054  O  OE1   . GLU A 1 1706 ? 135.122 177.740 135.088 1.00 33.64  ? 1706 GLU A OE1   1 
ATOM   2055  O  OE2   . GLU A 1 1706 ? 137.279 177.422 134.839 1.00 33.03  ? 1706 GLU A OE2   1 
ATOM   2056  N  N     . LYS A 1 1707 ? 133.935 179.479 130.602 1.00 24.39  ? 1707 LYS A N     1 
ATOM   2057  C  CA    . LYS A 1 1707 ? 133.745 178.665 129.406 1.00 20.79  ? 1707 LYS A CA    1 
ATOM   2058  C  C     . LYS A 1 1707 ? 133.965 179.482 128.140 1.00 23.01  ? 1707 LYS A C     1 
ATOM   2059  O  O     . LYS A 1 1707 ? 134.595 179.007 127.188 1.00 27.70  ? 1707 LYS A O     1 
ATOM   2060  C  CB    . LYS A 1 1707 ? 132.347 178.048 129.407 1.00 22.98  ? 1707 LYS A CB    1 
ATOM   2061  C  CG    . LYS A 1 1707 ? 132.270 176.695 128.720 1.00 32.99  ? 1707 LYS A CG    1 
ATOM   2062  C  CD    . LYS A 1 1707 ? 131.279 176.719 127.570 1.00 34.22  ? 1707 LYS A CD    1 
ATOM   2063  C  CE    . LYS A 1 1707 ? 131.493 175.541 126.633 1.00 40.15  ? 1707 LYS A CE    1 
ATOM   2064  N  NZ    . LYS A 1 1707 ? 130.574 175.588 125.463 1.00 40.54  ? 1707 LYS A NZ    1 
ATOM   2065  N  N     . GLU A 1 1708 ? 133.449 180.713 128.108 1.00 22.85  ? 1708 GLU A N     1 
ATOM   2066  C  CA    . GLU A 1 1708 ? 133.647 181.566 126.941 1.00 20.74  ? 1708 GLU A CA    1 
ATOM   2067  C  C     . GLU A 1 1708 ? 135.107 181.966 126.780 1.00 22.72  ? 1708 GLU A C     1 
ATOM   2068  O  O     . GLU A 1 1708 ? 135.578 182.135 125.650 1.00 24.78  ? 1708 GLU A O     1 
ATOM   2069  C  CB    . GLU A 1 1708 ? 132.765 182.810 127.042 1.00 24.85  ? 1708 GLU A CB    1 
ATOM   2070  C  CG    . GLU A 1 1708 ? 132.637 183.591 125.745 1.00 30.29  ? 1708 GLU A CG    1 
ATOM   2071  C  CD    . GLU A 1 1708 ? 132.361 182.701 124.549 1.00 37.15  ? 1708 GLU A CD    1 
ATOM   2072  O  OE1   . GLU A 1 1708 ? 131.361 181.955 124.581 1.00 35.93  ? 1708 GLU A OE1   1 
ATOM   2073  O  OE2   . GLU A 1 1708 ? 133.144 182.750 123.577 1.00 36.51  ? 1708 GLU A OE2   1 
ATOM   2074  N  N     . MET A 1 1709 ? 135.833 182.119 127.890 1.00 21.11  ? 1709 MET A N     1 
ATOM   2075  C  CA    . MET A 1 1709 ? 137.244 182.486 127.820 1.00 17.99  ? 1709 MET A CA    1 
ATOM   2076  C  C     . MET A 1 1709 ? 138.051 181.430 127.076 1.00 18.46  ? 1709 MET A C     1 
ATOM   2077  O  O     . MET A 1 1709 ? 138.916 181.756 126.254 1.00 24.42  ? 1709 MET A O     1 
ATOM   2078  C  CB    . MET A 1 1709 ? 137.793 182.698 129.231 1.00 20.16  ? 1709 MET A CB    1 
ATOM   2079  C  CG    . MET A 1 1709 ? 139.306 182.624 129.336 1.00 21.03  ? 1709 MET A CG    1 
ATOM   2080  S  SD    . MET A 1 1709 ? 139.854 182.200 131.000 1.00 25.20  ? 1709 MET A SD    1 
ATOM   2081  C  CE    . MET A 1 1709 ? 139.890 180.414 130.899 1.00 16.51  ? 1709 MET A CE    1 
ATOM   2082  N  N     . ARG A 1 1710 ? 137.783 180.153 127.353 1.00 19.50  ? 1710 ARG A N     1 
ATOM   2083  C  CA    . ARG A 1 1710 ? 138.487 179.083 126.655 1.00 15.66  ? 1710 ARG A CA    1 
ATOM   2084  C  C     . ARG A 1 1710 ? 138.097 179.034 125.183 1.00 17.54  ? 1710 ARG A C     1 
ATOM   2085  O  O     . ARG A 1 1710 ? 138.957 178.875 124.310 1.00 20.02  ? 1710 ARG A O     1 
ATOM   2086  C  CB    . ARG A 1 1710 ? 138.196 177.744 127.329 1.00 13.23  ? 1710 ARG A CB    1 
ATOM   2087  C  CG    . ARG A 1 1710 ? 138.767 177.618 128.727 1.00 12.27  ? 1710 ARG A CG    1 
ATOM   2088  C  CD    . ARG A 1 1710 ? 138.552 176.223 129.279 1.00 14.74  ? 1710 ARG A CD    1 
ATOM   2089  N  NE    . ARG A 1 1710 ? 139.265 176.017 130.533 1.00 24.87  ? 1710 ARG A NE    1 
ATOM   2090  C  CZ    . ARG A 1 1710 ? 138.681 175.699 131.681 1.00 28.62  ? 1710 ARG A CZ    1 
ATOM   2091  N  NH1   . ARG A 1 1710 ? 137.370 175.545 131.770 1.00 23.06  ? 1710 ARG A NH1   1 
ATOM   2092  N  NH2   . ARG A 1 1710 ? 139.432 175.531 132.766 1.00 24.61  ? 1710 ARG A NH2   1 
ATOM   2093  N  N     . VAL A 1 1711 ? 136.801 179.165 124.891 1.00 18.83  ? 1711 VAL A N     1 
ATOM   2094  C  CA    . VAL A 1 1711 ? 136.328 179.045 123.515 1.00 18.65  ? 1711 VAL A CA    1 
ATOM   2095  C  C     . VAL A 1 1711 ? 136.854 180.191 122.658 1.00 21.57  ? 1711 VAL A C     1 
ATOM   2096  O  O     . VAL A 1 1711 ? 137.305 179.978 121.526 1.00 23.90  ? 1711 VAL A O     1 
ATOM   2097  C  CB    . VAL A 1 1711 ? 134.791 178.972 123.487 1.00 19.73  ? 1711 VAL A CB    1 
ATOM   2098  C  CG1   . VAL A 1 1711 ? 134.280 179.060 122.061 1.00 20.91  ? 1711 VAL A CG1   1 
ATOM   2099  C  CG2   . VAL A 1 1711 ? 134.312 177.692 124.148 1.00 23.37  ? 1711 VAL A CG2   1 
ATOM   2100  N  N     . THR A 1 1712 ? 136.809 181.421 123.177 1.00 22.28  ? 1712 THR A N     1 
ATOM   2101  C  CA    . THR A 1 1712 ? 137.254 182.561 122.381 1.00 19.16  ? 1712 THR A CA    1 
ATOM   2102  C  C     . THR A 1 1712 ? 138.754 182.511 122.115 1.00 18.34  ? 1712 THR A C     1 
ATOM   2103  O  O     . THR A 1 1712 ? 139.208 182.971 121.062 1.00 23.08  ? 1712 THR A O     1 
ATOM   2104  C  CB    . THR A 1 1712 ? 136.865 183.878 123.063 1.00 26.08  ? 1712 THR A CB    1 
ATOM   2105  O  OG1   . THR A 1 1712 ? 137.096 184.970 122.164 1.00 30.51  ? 1712 THR A OG1   1 
ATOM   2106  C  CG2   . THR A 1 1712 ? 137.663 184.102 124.338 1.00 26.73  ? 1712 THR A CG2   1 
ATOM   2107  N  N     . LEU A 1 1713 ? 139.536 181.960 123.047 1.00 16.60  ? 1713 LEU A N     1 
ATOM   2108  C  CA    . LEU A 1 1713 ? 140.965 181.798 122.805 1.00 14.77  ? 1713 LEU A CA    1 
ATOM   2109  C  C     . LEU A 1 1713 ? 141.223 180.741 121.740 1.00 16.91  ? 1713 LEU A C     1 
ATOM   2110  O  O     . LEU A 1 1713 ? 142.110 180.903 120.894 1.00 17.64  ? 1713 LEU A O     1 
ATOM   2111  C  CB    . LEU A 1 1713 ? 141.679 181.440 124.108 1.00 13.75  ? 1713 LEU A CB    1 
ATOM   2112  C  CG    . LEU A 1 1713 ? 142.114 182.614 124.985 1.00 13.02  ? 1713 LEU A CG    1 
ATOM   2113  C  CD1   . LEU A 1 1713 ? 142.941 182.125 126.161 1.00 13.09  ? 1713 LEU A CD1   1 
ATOM   2114  C  CD2   . LEU A 1 1713 ? 142.887 183.634 124.171 1.00 19.13  ? 1713 LEU A CD2   1 
ATOM   2115  N  N     . ALA A 1 1714 ? 140.460 179.645 121.771 1.00 15.02  ? 1714 ALA A N     1 
ATOM   2116  C  CA    . ALA A 1 1714 ? 140.620 178.599 120.767 1.00 10.84  ? 1714 ALA A CA    1 
ATOM   2117  C  C     . ALA A 1 1714 ? 140.254 179.104 119.377 1.00 15.45  ? 1714 ALA A C     1 
ATOM   2118  O  O     . ALA A 1 1714 ? 140.938 178.793 118.396 1.00 17.96  ? 1714 ALA A O     1 
ATOM   2119  C  CB    . ALA A 1 1714 ? 139.773 177.383 121.137 1.00 13.18  ? 1714 ALA A CB    1 
ATOM   2120  N  N     . LYS A 1 1715 ? 139.172 179.880 119.272 1.00 15.64  ? 1715 LYS A N     1 
ATOM   2121  C  CA    . LYS A 1 1715 ? 138.770 180.410 117.974 1.00 15.16  ? 1715 LYS A CA    1 
ATOM   2122  C  C     . LYS A 1 1715 ? 139.760 181.451 117.469 1.00 16.74  ? 1715 LYS A C     1 
ATOM   2123  O  O     . LYS A 1 1715 ? 140.056 181.502 116.270 1.00 19.16  ? 1715 LYS A O     1 
ATOM   2124  C  CB    . LYS A 1 1715 ? 137.361 180.997 118.061 1.00 21.45  ? 1715 LYS A CB    1 
ATOM   2125  C  CG    . LYS A 1 1715 ? 136.276 179.957 118.283 1.00 21.26  ? 1715 LYS A CG    1 
ATOM   2126  C  CD    . LYS A 1 1715 ? 134.900 180.598 118.340 1.00 27.28  ? 1715 LYS A CD    1 
ATOM   2127  C  CE    . LYS A 1 1715 ? 133.807 179.548 118.451 1.00 30.32  ? 1715 LYS A CE    1 
ATOM   2128  N  NZ    . LYS A 1 1715 ? 132.453 180.160 118.541 1.00 26.55  ? 1715 LYS A NZ    1 
ATOM   2129  N  N     . LEU A 1 1716 ? 140.280 182.292 118.367 1.00 17.74  ? 1716 LEU A N     1 
ATOM   2130  C  CA    . LEU A 1 1716 ? 141.318 183.239 117.971 1.00 18.10  ? 1716 LEU A CA    1 
ATOM   2131  C  C     . LEU A 1 1716 ? 142.593 182.517 117.558 1.00 17.47  ? 1716 LEU A C     1 
ATOM   2132  O  O     . LEU A 1 1716 ? 143.288 182.955 116.634 1.00 21.84  ? 1716 LEU A O     1 
ATOM   2133  C  CB    . LEU A 1 1716 ? 141.601 184.221 119.107 1.00 17.78  ? 1716 LEU A CB    1 
ATOM   2134  C  CG    . LEU A 1 1716 ? 140.570 185.324 119.350 1.00 21.13  ? 1716 LEU A CG    1 
ATOM   2135  C  CD1   . LEU A 1 1716 ? 140.843 186.021 120.672 1.00 24.46  ? 1716 LEU A CD1   1 
ATOM   2136  C  CD2   . LEU A 1 1716 ? 140.575 186.320 118.203 1.00 22.41  ? 1716 LEU A CD2   1 
ATOM   2137  N  N     . LEU A 1 1717 ? 142.923 181.416 118.237 1.00 16.02  ? 1717 LEU A N     1 
ATOM   2138  C  CA    . LEU A 1 1717 ? 144.098 180.638 117.858 1.00 15.68  ? 1717 LEU A CA    1 
ATOM   2139  C  C     . LEU A 1 1717 ? 143.950 180.071 116.452 1.00 20.84  ? 1717 LEU A C     1 
ATOM   2140  O  O     . LEU A 1 1717 ? 144.912 180.061 115.675 1.00 26.61  ? 1717 LEU A O     1 
ATOM   2141  C  CB    . LEU A 1 1717 ? 144.335 179.518 118.871 1.00 14.81  ? 1717 LEU A CB    1 
ATOM   2142  C  CG    . LEU A 1 1717 ? 145.383 178.466 118.505 1.00 14.59  ? 1717 LEU A CG    1 
ATOM   2143  C  CD1   . LEU A 1 1717 ? 146.782 179.033 118.658 1.00 15.12  ? 1717 LEU A CD1   1 
ATOM   2144  C  CD2   . LEU A 1 1717 ? 145.212 177.219 119.354 1.00 11.55  ? 1717 LEU A CD2   1 
ATOM   2145  N  N     . ALA A 1 1718 ? 142.751 179.599 116.106 1.00 17.49  ? 1718 ALA A N     1 
ATOM   2146  C  CA    . ALA A 1 1718 ? 142.508 179.098 114.757 1.00 16.20  ? 1718 ALA A CA    1 
ATOM   2147  C  C     . ALA A 1 1718 ? 142.703 180.198 113.722 1.00 21.34  ? 1718 ALA A C     1 
ATOM   2148  O  O     . ALA A 1 1718 ? 143.292 179.971 112.659 1.00 25.19  ? 1718 ALA A O     1 
ATOM   2149  C  CB    . ALA A 1 1718 ? 141.101 178.510 114.662 1.00 18.84  ? 1718 ALA A CB    1 
ATOM   2150  N  N     . GLU A 1 1719 ? 142.207 181.402 114.017 1.00 23.30  ? 1719 GLU A N     1 
ATOM   2151  C  CA    . GLU A 1 1719 ? 142.409 182.528 113.111 1.00 24.46  ? 1719 GLU A CA    1 
ATOM   2152  C  C     . GLU A 1 1719 ? 143.884 182.894 113.007 1.00 25.81  ? 1719 GLU A C     1 
ATOM   2153  O  O     . GLU A 1 1719 ? 144.381 183.197 111.916 1.00 30.14  ? 1719 GLU A O     1 
ATOM   2154  C  CB    . GLU A 1 1719 ? 141.591 183.731 113.578 1.00 23.23  ? 1719 GLU A CB    1 
ATOM   2155  C  CG    . GLU A 1 1719 ? 140.098 183.603 113.332 1.00 28.97  ? 1719 GLU A CG    1 
ATOM   2156  C  CD    . GLU A 1 1719 ? 139.271 184.127 114.489 1.00 36.38  ? 1719 GLU A CD    1 
ATOM   2157  O  OE1   . GLU A 1 1719 ? 139.699 185.111 115.129 1.00 34.56  ? 1719 GLU A OE1   1 
ATOM   2158  O  OE2   . GLU A 1 1719 ? 138.195 183.554 114.759 1.00 32.57  ? 1719 GLU A OE2   1 
ATOM   2159  N  N     . SER A 1 1720 ? 144.599 182.875 114.134 1.00 24.09  ? 1720 SER A N     1 
ATOM   2160  C  CA    . SER A 1 1720 ? 146.014 183.230 114.117 1.00 21.98  ? 1720 SER A CA    1 
ATOM   2161  C  C     . SER A 1 1720 ? 146.843 182.182 113.385 1.00 27.68  ? 1720 SER A C     1 
ATOM   2162  O  O     . SER A 1 1720 ? 147.817 182.522 112.705 1.00 30.61  ? 1720 SER A O     1 
ATOM   2163  C  CB    . SER A 1 1720 ? 146.525 183.417 115.545 1.00 24.32  ? 1720 SER A CB    1 
ATOM   2164  O  OG    . SER A 1 1720 ? 147.900 183.755 115.551 1.00 26.23  ? 1720 SER A OG    1 
ATOM   2165  N  N     . VAL A 1 1721 ? 146.476 180.905 113.516 1.00 30.42  ? 1721 VAL A N     1 
ATOM   2166  C  CA    . VAL A 1 1721 ? 147.203 179.848 112.814 1.00 27.82  ? 1721 VAL A CA    1 
ATOM   2167  C  C     . VAL A 1 1721 ? 147.085 180.037 111.308 1.00 28.87  ? 1721 VAL A C     1 
ATOM   2168  O  O     . VAL A 1 1721 ? 148.076 179.951 110.574 1.00 34.12  ? 1721 VAL A O     1 
ATOM   2169  C  CB    . VAL A 1 1721 ? 146.702 178.461 113.254 1.00 22.03  ? 1721 VAL A CB    1 
ATOM   2170  C  CG1   . VAL A 1 1721 ? 147.149 177.399 112.266 1.00 27.04  ? 1721 VAL A CG1   1 
ATOM   2171  C  CG2   . VAL A 1 1721 ? 147.218 178.132 114.642 1.00 21.68  ? 1721 VAL A CG2   1 
ATOM   2172  N  N     . THR A 1 1722 ? 145.871 180.313 110.827 1.00 30.09  ? 1722 THR A N     1 
ATOM   2173  C  CA    . THR A 1 1722 ? 145.681 180.566 109.402 1.00 32.89  ? 1722 THR A CA    1 
ATOM   2174  C  C     . THR A 1 1722 ? 146.503 181.767 108.948 1.00 35.40  ? 1722 THR A C     1 
ATOM   2175  O  O     . THR A 1 1722 ? 147.093 181.753 107.861 1.00 42.13  ? 1722 THR A O     1 
ATOM   2176  C  CB    . THR A 1 1722 ? 144.195 180.777 109.104 1.00 30.73  ? 1722 THR A CB    1 
ATOM   2177  O  OG1   . THR A 1 1722 ? 143.517 179.515 109.132 1.00 35.78  ? 1722 THR A OG1   1 
ATOM   2178  C  CG2   . THR A 1 1722 ? 143.998 181.416 107.736 1.00 32.14  ? 1722 THR A CG2   1 
ATOM   2179  N  N     . GLU A 1 1723 ? 146.568 182.809 109.779 1.00 32.54  ? 1723 GLU A N     1 
ATOM   2180  C  CA    . GLU A 1 1723 ? 147.347 183.991 109.430 1.00 32.41  ? 1723 GLU A CA    1 
ATOM   2181  C  C     . GLU A 1 1723 ? 148.844 183.700 109.438 1.00 35.45  ? 1723 GLU A C     1 
ATOM   2182  O  O     . GLU A 1 1723 ? 149.576 184.167 108.558 1.00 37.92  ? 1723 GLU A O     1 
ATOM   2183  C  CB    . GLU A 1 1723 ? 147.018 185.131 110.393 1.00 32.68  ? 1723 GLU A CB    1 
ATOM   2184  C  CG    . GLU A 1 1723 ? 147.105 186.514 109.777 1.00 34.78  ? 1723 GLU A CG    1 
ATOM   2185  C  CD    . GLU A 1 1723 ? 146.442 187.572 110.637 1.00 36.51  ? 1723 GLU A CD    1 
ATOM   2186  O  OE1   . GLU A 1 1723 ? 145.427 187.256 111.291 1.00 31.41  ? 1723 GLU A OE1   1 
ATOM   2187  O  OE2   . GLU A 1 1723 ? 146.936 188.719 110.659 1.00 40.56  ? 1723 GLU A OE2   1 
ATOM   2188  N  N     . VAL A 1 1724 ? 149.321 182.930 110.422 1.00 37.67  ? 1724 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 1724 ? 150.758 182.689 110.553 1.00 37.32  ? 1724 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 1724 ? 151.271 181.668 109.550 1.00 39.25  ? 1724 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 1724 ? 152.486 181.592 109.326 1.00 45.89  ? 1724 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 1724 ? 151.103 182.249 111.990 1.00 33.48  ? 1724 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 1724 ? 150.617 180.833 112.260 1.00 29.31  ? 1724 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 1724 ? 152.597 182.396 112.276 1.00 29.29  ? 1724 VAL A CG2   1 
ATOM   2195  N  N     . GLU A 1 1725 ? 150.383 180.889 108.924 1.00 42.41  ? 1725 GLU A N     1 
ATOM   2196  C  CA    . GLU A 1 1725 ? 150.811 179.988 107.859 1.00 46.32  ? 1725 GLU A CA    1 
ATOM   2197  C  C     . GLU A 1 1725 ? 151.411 180.739 106.680 1.00 48.83  ? 1725 GLU A C     1 
ATOM   2198  O  O     . GLU A 1 1725 ? 152.189 180.155 105.919 1.00 53.93  ? 1725 GLU A O     1 
ATOM   2199  C  CB    . GLU A 1 1725 ? 149.639 179.130 107.375 1.00 49.02  ? 1725 GLU A CB    1 
ATOM   2200  C  CG    . GLU A 1 1725 ? 149.146 178.097 108.376 1.00 44.79  ? 1725 GLU A CG    1 
ATOM   2201  C  CD    . GLU A 1 1725 ? 149.926 176.801 108.312 1.00 50.82  ? 1725 GLU A CD    1 
ATOM   2202  O  OE1   . GLU A 1 1725 ? 150.282 176.373 107.194 1.00 55.37  ? 1725 GLU A OE1   1 
ATOM   2203  O  OE2   . GLU A 1 1725 ? 150.182 176.208 109.381 1.00 50.10  ? 1725 GLU A OE2   1 
ATOM   2204  N  N     . ILE A 1 1726 ? 151.060 182.014 106.506 1.00 51.22  ? 1726 ILE A N     1 
ATOM   2205  C  CA    . ILE A 1 1726 ? 151.654 182.813 105.439 1.00 51.74  ? 1726 ILE A CA    1 
ATOM   2206  C  C     . ILE A 1 1726 ? 153.116 183.111 105.749 1.00 47.90  ? 1726 ILE A C     1 
ATOM   2207  O  O     . ILE A 1 1726 ? 153.986 183.008 104.877 1.00 51.76  ? 1726 ILE A O     1 
ATOM   2208  C  CB    . ILE A 1 1726 ? 150.846 184.105 105.226 1.00 47.88  ? 1726 ILE A CB    1 
ATOM   2209  C  CG1   . ILE A 1 1726 ? 149.369 183.776 104.998 1.00 41.74  ? 1726 ILE A CG1   1 
ATOM   2210  C  CG2   . ILE A 1 1726 ? 151.409 184.902 104.061 1.00 47.43  ? 1726 ILE A CG2   1 
ATOM   2211  C  CD1   . ILE A 1 1726 ? 149.126 182.824 103.849 1.00 38.14  ? 1726 ILE A CD1   1 
ATOM   2212  N  N     . PHE A 1 1727 ? 153.406 183.490 106.997 1.00 44.71  ? 1727 PHE A N     1 
ATOM   2213  C  CA    . PHE A 1 1727 ? 154.788 183.754 107.387 1.00 47.97  ? 1727 PHE A CA    1 
ATOM   2214  C  C     . PHE A 1 1727 ? 155.635 182.492 107.297 1.00 55.01  ? 1727 PHE A C     1 
ATOM   2215  O  O     . PHE A 1 1727 ? 156.797 182.544 106.878 1.00 64.72  ? 1727 PHE A O     1 
ATOM   2216  C  CB    . PHE A 1 1727 ? 154.830 184.342 108.796 1.00 42.82  ? 1727 PHE A CB    1 
ATOM   2217  C  CG    . PHE A 1 1727 ? 153.919 185.518 108.985 1.00 43.75  ? 1727 PHE A CG    1 
ATOM   2218  C  CD1   . PHE A 1 1727 ? 153.913 186.558 108.069 1.00 34.98  ? 1727 PHE A CD1   1 
ATOM   2219  C  CD2   . PHE A 1 1727 ? 153.061 185.583 110.069 1.00 39.06  ? 1727 PHE A CD2   1 
ATOM   2220  C  CE1   . PHE A 1 1727 ? 153.076 187.642 108.234 1.00 31.39  ? 1727 PHE A CE1   1 
ATOM   2221  C  CE2   . PHE A 1 1727 ? 152.220 186.666 110.240 1.00 33.38  ? 1727 PHE A CE2   1 
ATOM   2222  C  CZ    . PHE A 1 1727 ? 152.228 187.696 109.321 1.00 33.48  ? 1727 PHE A CZ    1 
ATOM   2223  N  N     . GLY A 1 1728 ? 155.077 181.352 107.694 1.00 50.47  ? 1728 GLY A N     1 
ATOM   2224  C  CA    . GLY A 1 1728 ? 155.720 180.088 107.403 1.00 49.92  ? 1728 GLY A CA    1 
ATOM   2225  C  C     . GLY A 1 1728 ? 155.707 179.798 105.915 1.00 60.59  ? 1728 GLY A C     1 
ATOM   2226  O  O     . GLY A 1 1728 ? 154.868 180.300 105.166 1.00 62.34  ? 1728 GLY A O     1 
ATOM   2227  N  N     . LYS A 1 1729 ? 156.669 178.984 105.480 1.00 62.32  ? 1729 LYS A N     1 
ATOM   2228  C  CA    . LYS A 1 1729 ? 156.826 178.635 104.066 1.00 69.13  ? 1729 LYS A CA    1 
ATOM   2229  C  C     . LYS A 1 1729 ? 157.042 179.874 103.202 1.00 70.88  ? 1729 LYS A C     1 
ATOM   2230  O  O     . LYS A 1 1729 ? 156.674 179.896 102.025 1.00 68.49  ? 1729 LYS A O     1 
ATOM   2231  C  CB    . LYS A 1 1729 ? 155.626 177.830 103.554 1.00 62.23  ? 1729 LYS A CB    1 
ATOM   2232  C  CG    . LYS A 1 1729 ? 155.354 176.550 104.325 1.00 61.96  ? 1729 LYS A CG    1 
ATOM   2233  C  CD    . LYS A 1 1729 ? 153.955 176.027 104.037 1.00 66.96  ? 1729 LYS A CD    1 
ATOM   2234  C  CE    . LYS A 1 1729 ? 153.872 175.387 102.661 1.00 66.68  ? 1729 LYS A CE    1 
ATOM   2235  N  NZ    . LYS A 1 1729 ? 152.561 174.715 102.443 1.00 54.52  ? 1729 LYS A NZ    1 
ATOM   2236  N  N     . ALA A 1 1730 ? 157.635 180.917 103.779 1.00 65.98  ? 1730 ALA A N     1 
ATOM   2237  C  CA    . ALA A 1 1730 ? 157.887 182.172 103.085 1.00 63.69  ? 1730 ALA A CA    1 
ATOM   2238  C  C     . ALA A 1 1730 ? 159.373 182.491 103.145 1.00 62.90  ? 1730 ALA A C     1 
ATOM   2239  O  O     . ALA A 1 1730 ? 159.992 182.387 104.210 1.00 59.47  ? 1730 ALA A O     1 
ATOM   2240  C  CB    . ALA A 1 1730 ? 157.074 183.317 103.697 1.00 56.46  ? 1730 ALA A CB    1 
ATOM   2241  N  N     . THR A 1 1731 ? 159.941 182.878 102.001 1.00 61.13  ? 1731 THR A N     1 
ATOM   2242  C  CA    . THR A 1 1731 ? 161.365 183.192 101.954 1.00 59.20  ? 1731 THR A CA    1 
ATOM   2243  C  C     . THR A 1 1731 ? 161.662 184.528 102.625 1.00 60.13  ? 1731 THR A C     1 
ATOM   2244  O  O     . THR A 1 1731 ? 162.671 184.665 103.326 1.00 58.92  ? 1731 THR A O     1 
ATOM   2245  C  CB    . THR A 1 1731 ? 161.853 183.200 100.506 1.00 62.28  ? 1731 THR A CB    1 
ATOM   2246  O  OG1   . THR A 1 1731 ? 161.251 184.295 99.804  1.00 66.18  ? 1731 THR A OG1   1 
ATOM   2247  C  CG2   . THR A 1 1731 ? 161.481 181.897 99.815  1.00 61.02  ? 1731 THR A CG2   1 
ATOM   2248  N  N     . SER A 1 1732 ? 160.802 185.521 102.422 1.00 66.56  ? 1732 SER A N     1 
ATOM   2249  C  CA    . SER A 1 1732 ? 160.966 186.842 103.010 1.00 65.11  ? 1732 SER A CA    1 
ATOM   2250  C  C     . SER A 1 1732 ? 159.675 187.260 103.699 1.00 62.98  ? 1732 SER A C     1 
ATOM   2251  O  O     . SER A 1 1732 ? 158.578 187.010 103.188 1.00 66.81  ? 1732 SER A O     1 
ATOM   2252  C  CB    . SER A 1 1732 ? 161.352 187.878 101.950 1.00 66.27  ? 1732 SER A CB    1 
ATOM   2253  O  OG    . SER A 1 1732 ? 160.288 188.097 101.040 1.00 66.01  ? 1732 SER A OG    1 
ATOM   2254  N  N     . ILE A 1 1733 ? 159.810 187.896 104.859 1.00 54.55  ? 1733 ILE A N     1 
ATOM   2255  C  CA    . ILE A 1 1733 ? 158.675 188.346 105.656 1.00 55.06  ? 1733 ILE A CA    1 
ATOM   2256  C  C     . ILE A 1 1733 ? 158.763 189.856 105.816 1.00 54.08  ? 1733 ILE A C     1 
ATOM   2257  O  O     . ILE A 1 1733 ? 159.803 190.382 106.230 1.00 52.92  ? 1733 ILE A O     1 
ATOM   2258  C  CB    . ILE A 1 1733 ? 158.634 187.654 107.031 1.00 54.52  ? 1733 ILE A CB    1 
ATOM   2259  C  CG1   . ILE A 1 1733 ? 158.879 186.153 106.881 1.00 53.69  ? 1733 ILE A CG1   1 
ATOM   2260  C  CG2   . ILE A 1 1733 ? 157.305 187.919 107.722 1.00 52.67  ? 1733 ILE A CG2   1 
ATOM   2261  C  CD1   . ILE A 1 1733 ? 158.868 185.406 108.189 1.00 44.93  ? 1733 ILE A CD1   1 
ATOM   2262  N  N     . ASP A 1 1734 ? 157.680 190.545 105.485 1.00 53.16  ? 1734 ASP A N     1 
ATOM   2263  C  CA    . ASP A 1 1734 ? 157.607 191.987 105.691 1.00 49.37  ? 1734 ASP A CA    1 
ATOM   2264  C  C     . ASP A 1 1734 ? 157.520 192.283 107.182 1.00 46.22  ? 1734 ASP A C     1 
ATOM   2265  O  O     . ASP A 1 1734 ? 156.629 191.750 107.857 1.00 46.72  ? 1734 ASP A O     1 
ATOM   2266  C  CB    . ASP A 1 1734 ? 156.397 192.565 104.962 1.00 48.31  ? 1734 ASP A CB    1 
ATOM   2267  C  CG    . ASP A 1 1734 ? 156.464 194.073 104.824 1.00 48.52  ? 1734 ASP A CG    1 
ATOM   2268  O  OD1   . ASP A 1 1734 ? 157.581 194.627 104.856 1.00 49.72  ? 1734 ASP A OD1   1 
ATOM   2269  O  OD2   . ASP A 1 1734 ? 155.396 194.706 104.686 1.00 43.32  ? 1734 ASP A OD2   1 
ATOM   2270  N  N     . PRO A 1 1735 ? 158.419 193.099 107.742 1.00 49.10  ? 1735 PRO A N     1 
ATOM   2271  C  CA    . PRO A 1 1735 ? 158.318 193.412 109.178 1.00 48.30  ? 1735 PRO A CA    1 
ATOM   2272  C  C     . PRO A 1 1735 ? 157.001 194.062 109.565 1.00 41.29  ? 1735 PRO A C     1 
ATOM   2273  O  O     . PRO A 1 1735 ? 156.473 193.780 110.647 1.00 39.47  ? 1735 PRO A O     1 
ATOM   2274  C  CB    . PRO A 1 1735 ? 159.509 194.353 109.413 1.00 46.12  ? 1735 PRO A CB    1 
ATOM   2275  C  CG    . PRO A 1 1735 ? 160.468 194.034 108.316 1.00 44.13  ? 1735 PRO A CG    1 
ATOM   2276  C  CD    . PRO A 1 1735 ? 159.625 193.680 107.129 1.00 44.12  ? 1735 PRO A CD    1 
ATOM   2277  N  N     . ASN A 1 1736 ? 156.453 194.926 108.708 1.00 41.27  ? 1736 ASN A N     1 
ATOM   2278  C  CA    . ASN A 1 1736 ? 155.193 195.588 109.032 1.00 38.39  ? 1736 ASN A CA    1 
ATOM   2279  C  C     . ASN A 1 1736 ? 154.041 194.593 109.088 1.00 37.55  ? 1736 ASN A C     1 
ATOM   2280  O  O     . ASN A 1 1736 ? 153.171 194.690 109.962 1.00 38.14  ? 1736 ASN A O     1 
ATOM   2281  C  CB    . ASN A 1 1736 ? 154.904 196.691 108.015 1.00 41.69  ? 1736 ASN A CB    1 
ATOM   2282  C  CG    . ASN A 1 1736 ? 156.114 197.560 107.741 1.00 39.51  ? 1736 ASN A CG    1 
ATOM   2283  O  OD1   . ASN A 1 1736 ? 156.949 197.235 106.898 1.00 42.12  ? 1736 ASN A OD1   1 
ATOM   2284  N  ND2   . ASN A 1 1736 ? 156.217 198.673 108.459 1.00 38.93  ? 1736 ASN A ND2   1 
ATOM   2285  N  N     . THR A 1 1737 ? 154.012 193.635 108.158 1.00 36.27  ? 1737 THR A N     1 
ATOM   2286  C  CA    . THR A 1 1737 ? 152.975 192.609 108.187 1.00 37.56  ? 1737 THR A CA    1 
ATOM   2287  C  C     . THR A 1 1737 ? 153.103 191.732 109.426 1.00 32.07  ? 1737 THR A C     1 
ATOM   2288  O  O     . THR A 1 1737 ? 152.098 191.389 110.061 1.00 27.59  ? 1737 THR A O     1 
ATOM   2289  C  CB    . THR A 1 1737 ? 153.041 191.757 106.920 1.00 35.78  ? 1737 THR A CB    1 
ATOM   2290  O  OG1   . THR A 1 1737 ? 153.118 192.612 105.771 1.00 40.26  ? 1737 THR A OG1   1 
ATOM   2291  C  CG2   . THR A 1 1737 ? 151.808 190.874 106.806 1.00 31.42  ? 1737 THR A CG2   1 
ATOM   2292  N  N     . TYR A 1 1738 ? 154.332 191.351 109.780 1.00 31.66  ? 1738 TYR A N     1 
ATOM   2293  C  CA    . TYR A 1 1738 ? 154.539 190.516 110.959 1.00 28.40  ? 1738 TYR A CA    1 
ATOM   2294  C  C     . TYR A 1 1738 ? 154.166 191.259 112.236 1.00 29.24  ? 1738 TYR A C     1 
ATOM   2295  O  O     . TYR A 1 1738 ? 153.560 190.680 113.145 1.00 30.42  ? 1738 TYR A O     1 
ATOM   2296  C  CB    . TYR A 1 1738 ? 155.991 190.044 111.020 1.00 29.13  ? 1738 TYR A CB    1 
ATOM   2297  C  CG    . TYR A 1 1738 ? 156.172 188.738 111.755 1.00 28.02  ? 1738 TYR A CG    1 
ATOM   2298  C  CD1   . TYR A 1 1738 ? 155.650 187.557 111.248 1.00 29.63  ? 1738 TYR A CD1   1 
ATOM   2299  C  CD2   . TYR A 1 1738 ? 156.852 188.686 112.963 1.00 23.70  ? 1738 TYR A CD2   1 
ATOM   2300  C  CE1   . TYR A 1 1738 ? 155.810 186.359 111.917 1.00 32.95  ? 1738 TYR A CE1   1 
ATOM   2301  C  CE2   . TYR A 1 1738 ? 157.012 187.493 113.639 1.00 25.15  ? 1738 TYR A CE2   1 
ATOM   2302  C  CZ    . TYR A 1 1738 ? 156.491 186.334 113.113 1.00 29.72  ? 1738 TYR A CZ    1 
ATOM   2303  O  OH    . TYR A 1 1738 ? 156.652 185.145 113.785 1.00 28.19  ? 1738 TYR A OH    1 
ATOM   2304  N  N     . ILE A 1 1739 ? 154.527 192.541 112.326 1.00 27.42  ? 1739 ILE A N     1 
ATOM   2305  C  CA    . ILE A 1 1739 ? 154.216 193.324 113.518 1.00 27.34  ? 1739 ILE A CA    1 
ATOM   2306  C  C     . ILE A 1 1739 ? 152.708 193.480 113.678 1.00 30.92  ? 1739 ILE A C     1 
ATOM   2307  O  O     . ILE A 1 1739 ? 152.176 193.389 114.792 1.00 27.93  ? 1739 ILE A O     1 
ATOM   2308  C  CB    . ILE A 1 1739 ? 154.931 194.687 113.460 1.00 29.50  ? 1739 ILE A CB    1 
ATOM   2309  C  CG1   . ILE A 1 1739 ? 156.425 194.518 113.745 1.00 27.06  ? 1739 ILE A CG1   1 
ATOM   2310  C  CG2   . ILE A 1 1739 ? 154.312 195.667 114.442 1.00 28.17  ? 1739 ILE A CG2   1 
ATOM   2311  C  CD1   . ILE A 1 1739 ? 156.723 193.913 115.095 1.00 32.65  ? 1739 ILE A CD1   1 
ATOM   2312  N  N     . THR A 1 1740 ? 151.995 193.709 112.572 1.00 31.34  ? 1740 THR A N     1 
ATOM   2313  C  CA    . THR A 1 1740 ? 150.543 193.835 112.639 1.00 29.24  ? 1740 THR A CA    1 
ATOM   2314  C  C     . THR A 1 1740 ? 149.903 192.553 113.159 1.00 25.33  ? 1740 THR A C     1 
ATOM   2315  O  O     . THR A 1 1740 ? 148.953 192.600 113.950 1.00 27.30  ? 1740 THR A O     1 
ATOM   2316  C  CB    . THR A 1 1740 ? 149.983 194.194 111.261 1.00 30.83  ? 1740 THR A CB    1 
ATOM   2317  O  OG1   . THR A 1 1740 ? 150.602 195.398 110.791 1.00 36.83  ? 1740 THR A OG1   1 
ATOM   2318  C  CG2   . THR A 1 1740 ? 148.478 194.401 111.332 1.00 28.04  ? 1740 THR A CG2   1 
ATOM   2319  N  N     . TRP A 1 1741 ? 150.408 191.398 112.722 1.00 21.52  ? 1741 TRP A N     1 
ATOM   2320  C  CA    . TRP A 1 1741 ? 149.902 190.127 113.228 1.00 23.47  ? 1741 TRP A CA    1 
ATOM   2321  C  C     . TRP A 1 1741 ? 150.162 189.981 114.723 1.00 24.93  ? 1741 TRP A C     1 
ATOM   2322  O  O     . TRP A 1 1741 ? 149.308 189.480 115.464 1.00 25.05  ? 1741 TRP A O     1 
ATOM   2323  C  CB    . TRP A 1 1741 ? 150.535 188.968 112.458 1.00 20.27  ? 1741 TRP A CB    1 
ATOM   2324  C  CG    . TRP A 1 1741 ? 150.310 187.635 113.097 1.00 22.43  ? 1741 TRP A CG    1 
ATOM   2325  C  CD1   . TRP A 1 1741 ? 149.179 186.875 113.031 1.00 22.04  ? 1741 TRP A CD1   1 
ATOM   2326  C  CD2   . TRP A 1 1741 ? 151.240 186.901 113.900 1.00 22.19  ? 1741 TRP A CD2   1 
ATOM   2327  N  NE1   . TRP A 1 1741 ? 149.346 185.714 113.745 1.00 26.03  ? 1741 TRP A NE1   1 
ATOM   2328  C  CE2   . TRP A 1 1741 ? 150.603 185.705 114.288 1.00 21.63  ? 1741 TRP A CE2   1 
ATOM   2329  C  CE3   . TRP A 1 1741 ? 152.548 187.138 114.329 1.00 21.21  ? 1741 TRP A CE3   1 
ATOM   2330  C  CZ2   . TRP A 1 1741 ? 151.231 184.751 115.083 1.00 19.46  ? 1741 TRP A CZ2   1 
ATOM   2331  C  CZ3   . TRP A 1 1741 ? 153.169 186.191 115.118 1.00 19.75  ? 1741 TRP A CZ3   1 
ATOM   2332  C  CH2   . TRP A 1 1741 ? 152.510 185.012 115.488 1.00 19.88  ? 1741 TRP A CH2   1 
ATOM   2333  N  N     . ILE A 1 1742 ? 151.342 190.406 115.182 1.00 22.48  ? 1742 ILE A N     1 
ATOM   2334  C  CA    . ILE A 1 1742 ? 151.690 190.275 116.595 1.00 19.73  ? 1742 ILE A CA    1 
ATOM   2335  C  C     . ILE A 1 1742 ? 150.747 191.106 117.457 1.00 26.80  ? 1742 ILE A C     1 
ATOM   2336  O  O     . ILE A 1 1742 ? 150.230 190.636 118.478 1.00 27.15  ? 1742 ILE A O     1 
ATOM   2337  C  CB    . ILE A 1 1742 ? 153.160 190.672 116.823 1.00 23.68  ? 1742 ILE A CB    1 
ATOM   2338  C  CG1   . ILE A 1 1742 ? 154.093 189.565 116.333 1.00 21.42  ? 1742 ILE A CG1   1 
ATOM   2339  C  CG2   . ILE A 1 1742 ? 153.416 190.973 118.292 1.00 24.02  ? 1742 ILE A CG2   1 
ATOM   2340  C  CD1   . ILE A 1 1742 ? 155.530 190.004 116.189 1.00 25.50  ? 1742 ILE A CD1   1 
ATOM   2341  N  N     . ASP A 1 1743 ? 150.507 192.357 117.056 1.00 28.22  ? 1743 ASP A N     1 
ATOM   2342  C  CA    . ASP A 1 1743 ? 149.644 193.235 117.840 1.00 25.59  ? 1743 ASP A CA    1 
ATOM   2343  C  C     . ASP A 1 1743 ? 148.192 192.775 117.815 1.00 24.55  ? 1743 ASP A C     1 
ATOM   2344  O  O     . ASP A 1 1743 ? 147.437 193.064 118.751 1.00 26.24  ? 1743 ASP A O     1 
ATOM   2345  C  CB    . ASP A 1 1743 ? 149.752 194.670 117.325 1.00 25.93  ? 1743 ASP A CB    1 
ATOM   2346  C  CG    . ASP A 1 1743 ? 150.887 195.437 117.972 1.00 36.61  ? 1743 ASP A CG    1 
ATOM   2347  O  OD1   . ASP A 1 1743 ? 151.262 195.100 119.115 1.00 38.32  ? 1743 ASP A OD1   1 
ATOM   2348  O  OD2   . ASP A 1 1743 ? 151.405 196.379 117.336 1.00 35.85  ? 1743 ASP A OD2   1 
ATOM   2349  N  N     . LYS A 1 1744 ? 147.783 192.069 116.760 1.00 21.55  ? 1744 LYS A N     1 
ATOM   2350  C  CA    . LYS A 1 1744 ? 146.389 191.655 116.637 1.00 19.50  ? 1744 LYS A CA    1 
ATOM   2351  C  C     . LYS A 1 1744 ? 146.016 190.612 117.684 1.00 19.34  ? 1744 LYS A C     1 
ATOM   2352  O  O     . LYS A 1 1744 ? 144.902 190.634 118.219 1.00 22.19  ? 1744 LYS A O     1 
ATOM   2353  C  CB    . LYS A 1 1744 ? 146.127 191.119 115.230 1.00 22.36  ? 1744 LYS A CB    1 
ATOM   2354  C  CG    . LYS A 1 1744 ? 144.706 190.631 115.002 1.00 21.10  ? 1744 LYS A CG    1 
ATOM   2355  C  CD    . LYS A 1 1744 ? 144.448 190.345 113.531 1.00 23.89  ? 1744 LYS A CD    1 
ATOM   2356  C  CE    . LYS A 1 1744 ? 143.123 189.629 113.334 1.00 23.91  ? 1744 LYS A CE    1 
ATOM   2357  N  NZ    . LYS A 1 1744 ? 141.990 190.397 113.916 1.00 32.21  ? 1744 LYS A NZ    1 
ATOM   2358  N  N     . TYR A 1 1745 ? 146.929 189.699 117.995 1.00 19.66  ? 1745 TYR A N     1 
ATOM   2359  C  CA    . TYR A 1 1745 ? 146.630 188.551 118.837 1.00 15.08  ? 1745 TYR A CA    1 
ATOM   2360  C  C     . TYR A 1 1745 ? 147.355 188.659 120.173 1.00 18.38  ? 1745 TYR A C     1 
ATOM   2361  O  O     . TYR A 1 1745 ? 148.321 189.409 120.332 1.00 23.09  ? 1745 TYR A O     1 
ATOM   2362  C  CB    . TYR A 1 1745 ? 147.006 187.249 118.120 1.00 15.04  ? 1745 TYR A CB    1 
ATOM   2363  C  CG    . TYR A 1 1745 ? 146.175 186.990 116.885 1.00 20.42  ? 1745 TYR A CG    1 
ATOM   2364  C  CD1   . TYR A 1 1745 ? 144.914 186.421 116.978 1.00 21.59  ? 1745 TYR A CD1   1 
ATOM   2365  C  CD2   . TYR A 1 1745 ? 146.650 187.325 115.625 1.00 21.32  ? 1745 TYR A CD2   1 
ATOM   2366  C  CE1   . TYR A 1 1745 ? 144.151 186.187 115.850 1.00 21.03  ? 1745 TYR A CE1   1 
ATOM   2367  C  CE2   . TYR A 1 1745 ? 145.894 187.094 114.492 1.00 22.41  ? 1745 TYR A CE2   1 
ATOM   2368  C  CZ    . TYR A 1 1745 ? 144.646 186.526 114.611 1.00 22.27  ? 1745 TYR A CZ    1 
ATOM   2369  O  OH    . TYR A 1 1745 ? 143.890 186.295 113.485 1.00 30.23  ? 1745 TYR A OH    1 
ATOM   2370  N  N     . GLN A 1 1746 ? 146.866 187.886 121.139 1.00 18.24  ? 1746 GLN A N     1 
ATOM   2371  C  CA    . GLN A 1 1746 ? 147.381 187.940 122.497 1.00 15.63  ? 1746 GLN A CA    1 
ATOM   2372  C  C     . GLN A 1 1746 ? 148.780 187.333 122.574 1.00 16.46  ? 1746 GLN A C     1 
ATOM   2373  O  O     . GLN A 1 1746 ? 149.236 186.631 121.668 1.00 21.23  ? 1746 GLN A O     1 
ATOM   2374  C  CB    . GLN A 1 1746 ? 146.437 187.214 123.455 1.00 20.30  ? 1746 GLN A CB    1 
ATOM   2375  C  CG    . GLN A 1 1746 ? 145.166 187.989 123.777 1.00 25.70  ? 1746 GLN A CG    1 
ATOM   2376  C  CD    . GLN A 1 1746 ? 144.171 187.997 122.629 1.00 22.55  ? 1746 GLN A CD    1 
ATOM   2377  O  OE1   . GLN A 1 1746 ? 144.306 187.238 121.670 1.00 18.78  ? 1746 GLN A OE1   1 
ATOM   2378  N  NE2   . GLN A 1 1746 ? 143.168 188.863 122.721 1.00 25.00  ? 1746 GLN A NE2   1 
ATOM   2379  N  N     . ALA A 1 1747 ? 149.460 187.616 123.688 1.00 16.41  ? 1747 ALA A N     1 
ATOM   2380  C  CA    . ALA A 1 1747 ? 150.858 187.222 123.836 1.00 12.85  ? 1747 ALA A CA    1 
ATOM   2381  C  C     . ALA A 1 1747 ? 151.025 185.708 123.779 1.00 16.47  ? 1747 ALA A C     1 
ATOM   2382  O  O     . ALA A 1 1747 ? 151.938 185.198 123.120 1.00 19.33  ? 1747 ALA A O     1 
ATOM   2383  C  CB    . ALA A 1 1747 ? 151.419 187.777 125.146 1.00 16.67  ? 1747 ALA A CB    1 
ATOM   2384  N  N     . GLN A 1 1748 ? 150.152 184.969 124.466 1.00 14.18  ? 1748 GLN A N     1 
ATOM   2385  C  CA    . GLN A 1 1748 ? 150.292 183.516 124.487 1.00 10.76  ? 1748 GLN A CA    1 
ATOM   2386  C  C     . GLN A 1 1748 ? 149.859 182.890 123.168 1.00 12.64  ? 1748 GLN A C     1 
ATOM   2387  O  O     . GLN A 1 1748 ? 150.260 181.763 122.855 1.00 14.21  ? 1748 GLN A O     1 
ATOM   2388  C  CB    . GLN A 1 1748 ? 149.495 182.926 125.652 1.00 9.54   ? 1748 GLN A CB    1 
ATOM   2389  C  CG    . GLN A 1 1748 ? 148.018 182.719 125.372 1.00 9.77   ? 1748 GLN A CG    1 
ATOM   2390  C  CD    . GLN A 1 1748 ? 147.271 182.170 126.572 1.00 10.55  ? 1748 GLN A CD    1 
ATOM   2391  O  OE1   . GLN A 1 1748 ? 147.056 182.873 127.558 1.00 11.76  ? 1748 GLN A OE1   1 
ATOM   2392  N  NE2   . GLN A 1 1748 ? 146.875 180.905 126.496 1.00 14.14  ? 1748 GLN A NE2   1 
ATOM   2393  N  N     . LEU A 1 1749 ? 149.044 183.599 122.384 1.00 14.16  ? 1749 LEU A N     1 
ATOM   2394  C  CA    . LEU A 1 1749 ? 148.583 183.050 121.113 1.00 11.77  ? 1749 LEU A CA    1 
ATOM   2395  C  C     . LEU A 1 1749 ? 149.650 183.164 120.030 1.00 13.84  ? 1749 LEU A C     1 
ATOM   2396  O  O     . LEU A 1 1749 ? 149.805 182.253 119.209 1.00 16.51  ? 1749 LEU A O     1 
ATOM   2397  C  CB    . LEU A 1 1749 ? 147.295 183.746 120.678 1.00 13.54  ? 1749 LEU A CB    1 
ATOM   2398  C  CG    . LEU A 1 1749 ? 146.042 183.359 121.465 1.00 13.12  ? 1749 LEU A CG    1 
ATOM   2399  C  CD1   . LEU A 1 1749 ? 144.795 183.855 120.759 1.00 14.57  ? 1749 LEU A CD1   1 
ATOM   2400  C  CD2   . LEU A 1 1749 ? 145.979 181.854 121.671 1.00 15.14  ? 1749 LEU A CD2   1 
ATOM   2401  N  N     . VAL A 1 1750 ? 150.392 184.274 120.007 1.00 12.99  ? 1750 VAL A N     1 
ATOM   2402  C  CA    . VAL A 1 1750 ? 151.411 184.454 118.976 1.00 13.25  ? 1750 VAL A CA    1 
ATOM   2403  C  C     . VAL A 1 1750 ? 152.550 183.457 119.161 1.00 10.98  ? 1750 VAL A C     1 
ATOM   2404  O  O     . VAL A 1 1750 ? 153.129 182.970 118.183 1.00 12.83  ? 1750 VAL A O     1 
ATOM   2405  C  CB    . VAL A 1 1750 ? 151.908 185.914 118.950 1.00 15.19  ? 1750 VAL A CB    1 
ATOM   2406  C  CG1   . VAL A 1 1750 ? 150.729 186.868 118.918 1.00 14.67  ? 1750 VAL A CG1   1 
ATOM   2407  C  CG2   . VAL A 1 1750 ? 152.794 186.223 120.148 1.00 17.67  ? 1750 VAL A CG2   1 
ATOM   2408  N  N     . VAL A 1 1751 ? 152.889 183.133 120.411 1.00 10.22  ? 1751 VAL A N     1 
ATOM   2409  C  CA    . VAL A 1 1751 ? 153.913 182.122 120.659 1.00 10.09  ? 1751 VAL A CA    1 
ATOM   2410  C  C     . VAL A 1 1751 ? 153.389 180.740 120.297 1.00 9.16   ? 1751 VAL A C     1 
ATOM   2411  O  O     . VAL A 1 1751 ? 154.101 179.924 119.699 1.00 12.06  ? 1751 VAL A O     1 
ATOM   2412  C  CB    . VAL A 1 1751 ? 154.387 182.187 122.123 1.00 7.30   ? 1751 VAL A CB    1 
ATOM   2413  C  CG1   . VAL A 1 1751 ? 155.371 181.069 122.412 1.00 9.96   ? 1751 VAL A CG1   1 
ATOM   2414  C  CG2   . VAL A 1 1751 ? 155.012 183.540 122.415 1.00 12.06  ? 1751 VAL A CG2   1 
ATOM   2415  N  N     . LEU A 1 1752 ? 152.133 180.457 120.651 1.00 8.63   ? 1752 LEU A N     1 
ATOM   2416  C  CA    . LEU A 1 1752 ? 151.545 179.158 120.342 1.00 8.35   ? 1752 LEU A CA    1 
ATOM   2417  C  C     . LEU A 1 1752 ? 151.429 178.943 118.838 1.00 10.54  ? 1752 LEU A C     1 
ATOM   2418  O  O     . LEU A 1 1752 ? 151.731 177.855 118.335 1.00 11.62  ? 1752 LEU A O     1 
ATOM   2419  C  CB    . LEU A 1 1752 ? 150.175 179.040 121.010 1.00 10.49  ? 1752 LEU A CB    1 
ATOM   2420  C  CG    . LEU A 1 1752 ? 149.672 177.639 121.349 1.00 7.45   ? 1752 LEU A CG    1 
ATOM   2421  C  CD1   . LEU A 1 1752 ? 150.724 176.862 122.120 1.00 6.03   ? 1752 LEU A CD1   1 
ATOM   2422  C  CD2   . LEU A 1 1752 ? 148.383 177.736 122.140 1.00 6.30   ? 1752 LEU A CD2   1 
ATOM   2423  N  N     . SER A 1 1753 ? 150.991 179.969 118.104 1.00 11.05  ? 1753 SER A N     1 
ATOM   2424  C  CA    . SER A 1 1753 ? 150.851 179.836 116.657 1.00 9.53   ? 1753 SER A CA    1 
ATOM   2425  C  C     . SER A 1 1753 ? 152.205 179.650 115.986 1.00 10.74  ? 1753 SER A C     1 
ATOM   2426  O  O     . SER A 1 1753 ? 152.340 178.843 115.058 1.00 14.14  ? 1753 SER A O     1 
ATOM   2427  C  CB    . SER A 1 1753 ? 150.128 181.055 116.086 1.00 15.90  ? 1753 SER A CB    1 
ATOM   2428  O  OG    . SER A 1 1753 ? 150.452 182.225 116.814 1.00 17.10  ? 1753 SER A OG    1 
ATOM   2429  N  N     . ALA A 1 1754 ? 153.221 180.389 116.439 1.00 9.59   ? 1754 ALA A N     1 
ATOM   2430  C  CA    . ALA A 1 1754 ? 154.568 180.184 115.918 1.00 7.25   ? 1754 ALA A CA    1 
ATOM   2431  C  C     . ALA A 1 1754 ? 155.072 178.786 116.250 1.00 10.54  ? 1754 ALA A C     1 
ATOM   2432  O  O     . ALA A 1 1754 ? 155.796 178.172 115.458 1.00 14.63  ? 1754 ALA A O     1 
ATOM   2433  C  CB    . ALA A 1 1754 ? 155.515 181.245 116.477 1.00 10.01  ? 1754 ALA A CB    1 
ATOM   2434  N  N     . GLN A 1 1755 ? 154.703 178.272 117.426 1.00 8.91   ? 1755 GLN A N     1 
ATOM   2435  C  CA    . GLN A 1 1755 ? 155.031 176.896 117.776 1.00 7.24   ? 1755 GLN A CA    1 
ATOM   2436  C  C     . GLN A 1 1755 ? 154.344 175.913 116.839 1.00 8.17   ? 1755 GLN A C     1 
ATOM   2437  O  O     . GLN A 1 1755 ? 154.947 174.920 116.415 1.00 12.58  ? 1755 GLN A O     1 
ATOM   2438  C  CB    . GLN A 1 1755 ? 154.628 176.621 119.224 1.00 7.43   ? 1755 GLN A CB    1 
ATOM   2439  C  CG    . GLN A 1 1755 ? 155.780 176.643 120.196 1.00 8.32   ? 1755 GLN A CG    1 
ATOM   2440  C  CD    . GLN A 1 1755 ? 155.376 177.171 121.554 1.00 9.41   ? 1755 GLN A CD    1 
ATOM   2441  O  OE1   . GLN A 1 1755 ? 154.193 177.369 121.828 1.00 10.99  ? 1755 GLN A OE1   1 
ATOM   2442  N  NE2   . GLN A 1 1755 ? 156.359 177.425 122.406 1.00 11.82  ? 1755 GLN A NE2   1 
ATOM   2443  N  N     . ILE A 1 1756 ? 153.075 176.167 116.515 1.00 9.07   ? 1756 ILE A N     1 
ATOM   2444  C  CA    . ILE A 1 1756 ? 152.336 175.273 115.629 1.00 9.95   ? 1756 ILE A CA    1 
ATOM   2445  C  C     . ILE A 1 1756 ? 152.922 175.311 114.225 1.00 10.55  ? 1756 ILE A C     1 
ATOM   2446  O  O     . ILE A 1 1756 ? 153.164 174.266 113.609 1.00 13.10  ? 1756 ILE A O     1 
ATOM   2447  C  CB    . ILE A 1 1756 ? 150.841 175.642 115.629 1.00 11.10  ? 1756 ILE A CB    1 
ATOM   2448  C  CG1   . ILE A 1 1756 ? 150.212 175.327 116.987 1.00 11.69  ? 1756 ILE A CG1   1 
ATOM   2449  C  CG2   . ILE A 1 1756 ? 150.109 174.900 114.525 1.00 10.28  ? 1756 ILE A CG2   1 
ATOM   2450  C  CD1   . ILE A 1 1756 ? 148.917 176.064 117.240 1.00 13.23  ? 1756 ILE A CD1   1 
ATOM   2451  N  N     . ALA A 1 1757 ? 153.176 176.514 113.704 1.00 11.54  ? 1757 ALA A N     1 
ATOM   2452  C  CA    . ALA A 1 1757 ? 153.661 176.646 112.333 1.00 13.22  ? 1757 ALA A CA    1 
ATOM   2453  C  C     . ALA A 1 1757 ? 155.018 175.977 112.156 1.00 13.81  ? 1757 ALA A C     1 
ATOM   2454  O  O     . ALA A 1 1757 ? 155.266 175.318 111.139 1.00 16.09  ? 1757 ALA A O     1 
ATOM   2455  C  CB    . ALA A 1 1757 ? 153.735 178.122 111.943 1.00 18.23  ? 1757 ALA A CB    1 
ATOM   2456  N  N     . TRP A 1 1758 ? 155.912 176.140 113.132 1.00 11.21  ? 1758 TRP A N     1 
ATOM   2457  C  CA    . TRP A 1 1758 ? 157.224 175.507 113.048 1.00 10.05  ? 1758 TRP A CA    1 
ATOM   2458  C  C     . TRP A 1 1758 ? 157.111 173.989 113.125 1.00 11.17  ? 1758 TRP A C     1 
ATOM   2459  O  O     . TRP A 1 1758 ? 157.821 173.270 112.413 1.00 13.67  ? 1758 TRP A O     1 
ATOM   2460  C  CB    . TRP A 1 1758 ? 158.129 176.037 114.157 1.00 11.15  ? 1758 TRP A CB    1 
ATOM   2461  C  CG    . TRP A 1 1758 ? 159.422 175.299 114.287 1.00 10.12  ? 1758 TRP A CG    1 
ATOM   2462  C  CD1   . TRP A 1 1758 ? 160.552 175.486 113.547 1.00 9.09   ? 1758 TRP A CD1   1 
ATOM   2463  C  CD2   . TRP A 1 1758 ? 159.720 174.253 115.217 1.00 9.23   ? 1758 TRP A CD2   1 
ATOM   2464  N  NE1   . TRP A 1 1758 ? 161.536 174.621 113.957 1.00 11.26  ? 1758 TRP A NE1   1 
ATOM   2465  C  CE2   . TRP A 1 1758 ? 161.050 173.853 114.982 1.00 8.79   ? 1758 TRP A CE2   1 
ATOM   2466  C  CE3   . TRP A 1 1758 ? 158.991 173.615 116.225 1.00 8.55   ? 1758 TRP A CE3   1 
ATOM   2467  C  CZ2   . TRP A 1 1758 ? 161.666 172.845 115.718 1.00 11.77  ? 1758 TRP A CZ2   1 
ATOM   2468  C  CZ3   . TRP A 1 1758 ? 159.602 172.617 116.954 1.00 8.19   ? 1758 TRP A CZ3   1 
ATOM   2469  C  CH2   . TRP A 1 1758 ? 160.927 172.240 116.697 1.00 11.80  ? 1758 TRP A CH2   1 
ATOM   2470  N  N     . SER A 1 1759 ? 156.226 173.484 113.988 1.00 10.11  ? 1759 SER A N     1 
ATOM   2471  C  CA    . SER A 1 1759 ? 156.081 172.041 114.144 1.00 9.94   ? 1759 SER A CA    1 
ATOM   2472  C  C     . SER A 1 1759 ? 155.572 171.388 112.863 1.00 15.58  ? 1759 SER A C     1 
ATOM   2473  O  O     . SER A 1 1759 ? 156.075 170.335 112.454 1.00 20.38  ? 1759 SER A O     1 
ATOM   2474  C  CB    . SER A 1 1759 ? 155.145 171.731 115.311 1.00 12.96  ? 1759 SER A CB    1 
ATOM   2475  O  OG    . SER A 1 1759 ? 155.620 172.307 116.515 1.00 14.04  ? 1759 SER A OG    1 
ATOM   2476  N  N     . GLU A 1 1760 ? 154.571 171.994 112.218 1.00 16.57  ? 1760 GLU A N     1 
ATOM   2477  C  CA    . GLU A 1 1760 ? 154.056 171.436 110.971 1.00 13.97  ? 1760 GLU A CA    1 
ATOM   2478  C  C     . GLU A 1 1760 ? 155.098 171.506 109.861 1.00 22.15  ? 1760 GLU A C     1 
ATOM   2479  O  O     . GLU A 1 1760 ? 155.194 170.591 109.036 1.00 31.71  ? 1760 GLU A O     1 
ATOM   2480  C  CB    . GLU A 1 1760 ? 152.776 172.159 110.548 1.00 17.65  ? 1760 GLU A CB    1 
ATOM   2481  C  CG    . GLU A 1 1760 ? 151.754 172.342 111.659 1.00 26.36  ? 1760 GLU A CG    1 
ATOM   2482  C  CD    . GLU A 1 1760 ? 150.670 171.282 111.642 1.00 35.21  ? 1760 GLU A CD    1 
ATOM   2483  O  OE1   . GLU A 1 1760 ? 150.588 170.499 112.611 1.00 31.10  ? 1760 GLU A OE1   1 
ATOM   2484  O  OE2   . GLU A 1 1760 ? 149.899 171.233 110.661 1.00 37.98  ? 1760 GLU A OE2   1 
ATOM   2485  N  N     . ASN A 1 1761 ? 155.881 172.588 109.820 1.00 20.84  ? 1761 ASN A N     1 
ATOM   2486  C  CA    . ASN A 1 1761 ? 156.912 172.715 108.795 1.00 19.92  ? 1761 ASN A CA    1 
ATOM   2487  C  C     . ASN A 1 1761 ? 157.962 171.620 108.927 1.00 22.70  ? 1761 ASN A C     1 
ATOM   2488  O  O     . ASN A 1 1761 ? 158.393 171.039 107.925 1.00 28.84  ? 1761 ASN A O     1 
ATOM   2489  C  CB    . ASN A 1 1761 ? 157.563 174.095 108.875 1.00 18.84  ? 1761 ASN A CB    1 
ATOM   2490  C  CG    . ASN A 1 1761 ? 156.694 175.185 108.281 1.00 31.13  ? 1761 ASN A CG    1 
ATOM   2491  O  OD1   . ASN A 1 1761 ? 155.535 174.952 107.938 1.00 31.53  ? 1761 ASN A OD1   1 
ATOM   2492  N  ND2   . ASN A 1 1761 ? 157.250 176.384 108.156 1.00 36.54  ? 1761 ASN A ND2   1 
ATOM   2493  N  N     . VAL A 1 1762 ? 158.389 171.329 110.157 1.00 21.20  ? 1762 VAL A N     1 
ATOM   2494  C  CA    . VAL A 1 1762 ? 159.339 170.243 110.375 1.00 18.20  ? 1762 VAL A CA    1 
ATOM   2495  C  C     . VAL A 1 1762 ? 158.703 168.903 110.024 1.00 22.24  ? 1762 VAL A C     1 
ATOM   2496  O  O     . VAL A 1 1762 ? 159.333 168.049 109.389 1.00 31.37  ? 1762 VAL A O     1 
ATOM   2497  C  CB    . VAL A 1 1762 ? 159.851 170.266 111.827 1.00 13.51  ? 1762 VAL A CB    1 
ATOM   2498  C  CG1   . VAL A 1 1762 ? 160.742 169.065 112.094 1.00 16.46  ? 1762 VAL A CG1   1 
ATOM   2499  C  CG2   . VAL A 1 1762 ? 160.595 171.559 112.107 1.00 13.75  ? 1762 VAL A CG2   1 
ATOM   2500  N  N     . GLU A 1 1763 ? 157.448 168.698 110.431 1.00 23.42  ? 1763 GLU A N     1 
ATOM   2501  C  CA    . GLU A 1 1763 ? 156.749 167.463 110.093 1.00 25.25  ? 1763 GLU A CA    1 
ATOM   2502  C  C     . GLU A 1 1763 ? 156.578 167.321 108.586 1.00 28.97  ? 1763 GLU A C     1 
ATOM   2503  O  O     . GLU A 1 1763 ? 156.743 166.226 108.035 1.00 35.20  ? 1763 GLU A O     1 
ATOM   2504  C  CB    . GLU A 1 1763 ? 155.390 167.422 110.793 1.00 22.43  ? 1763 GLU A CB    1 
ATOM   2505  C  CG    . GLU A 1 1763 ? 154.821 166.025 110.971 1.00 25.56  ? 1763 GLU A CG    1 
ATOM   2506  C  CD    . GLU A 1 1763 ? 155.220 165.396 112.290 1.00 32.02  ? 1763 GLU A CD    1 
ATOM   2507  O  OE1   . GLU A 1 1763 ? 155.983 166.031 113.047 1.00 29.32  ? 1763 GLU A OE1   1 
ATOM   2508  O  OE2   . GLU A 1 1763 ? 154.769 164.267 112.570 1.00 33.87  ? 1763 GLU A OE2   1 
ATOM   2509  N  N     . THR A 1 1764 ? 156.237 168.417 107.904 1.00 26.71  ? 1764 THR A N     1 
ATOM   2510  C  CA    . THR A 1 1764 ? 156.141 168.381 106.448 1.00 26.66  ? 1764 THR A CA    1 
ATOM   2511  C  C     . THR A 1 1764 ? 157.495 168.086 105.815 1.00 31.14  ? 1764 THR A C     1 
ATOM   2512  O  O     . THR A 1 1764 ? 157.591 167.281 104.881 1.00 37.03  ? 1764 THR A O     1 
ATOM   2513  C  CB    . THR A 1 1764 ? 155.585 169.705 105.923 1.00 29.90  ? 1764 THR A CB    1 
ATOM   2514  O  OG1   . THR A 1 1764 ? 154.322 169.976 106.544 1.00 35.37  ? 1764 THR A OG1   1 
ATOM   2515  C  CG2   . THR A 1 1764 ? 155.401 169.647 104.415 1.00 26.77  ? 1764 THR A CG2   1 
ATOM   2516  N  N     . ALA A 1 1765 ? 158.555 168.728 106.314 1.00 29.92  ? 1765 ALA A N     1 
ATOM   2517  C  CA    . ALA A 1 1765 ? 159.885 168.513 105.753 1.00 29.46  ? 1765 ALA A CA    1 
ATOM   2518  C  C     . ALA A 1 1765 ? 160.356 167.081 105.969 1.00 36.50  ? 1765 ALA A C     1 
ATOM   2519  O  O     . ALA A 1 1765 ? 160.921 166.463 105.059 1.00 42.18  ? 1765 ALA A O     1 
ATOM   2520  C  CB    . ALA A 1 1765 ? 160.878 169.501 106.366 1.00 29.84  ? 1765 ALA A CB    1 
ATOM   2521  N  N     . LEU A 1 1766 ? 160.130 166.534 107.166 1.00 36.33  ? 1766 LEU A N     1 
ATOM   2522  C  CA    . LEU A 1 1766 ? 160.592 165.179 107.454 1.00 34.70  ? 1766 LEU A CA    1 
ATOM   2523  C  C     . LEU A 1 1766 ? 159.843 164.149 106.621 1.00 41.16  ? 1766 LEU A C     1 
ATOM   2524  O  O     . LEU A 1 1766 ? 160.402 163.104 106.266 1.00 46.29  ? 1766 LEU A O     1 
ATOM   2525  C  CB    . LEU A 1 1766 ? 160.444 164.878 108.944 1.00 28.93  ? 1766 LEU A CB    1 
ATOM   2526  C  CG    . LEU A 1 1766 ? 161.487 165.539 109.846 1.00 31.55  ? 1766 LEU A CG    1 
ATOM   2527  C  CD1   . LEU A 1 1766 ? 161.036 165.522 111.297 1.00 22.47  ? 1766 LEU A CD1   1 
ATOM   2528  C  CD2   . LEU A 1 1766 ? 162.835 164.861 109.683 1.00 32.10  ? 1766 LEU A CD2   1 
ATOM   2529  N  N     . SER A 1 1767 ? 158.575 164.419 106.305 1.00 40.65  ? 1767 SER A N     1 
ATOM   2530  C  CA    . SER A 1 1767 ? 157.831 163.529 105.420 1.00 40.80  ? 1767 SER A CA    1 
ATOM   2531  C  C     . SER A 1 1767 ? 158.438 163.516 104.024 1.00 47.67  ? 1767 SER A C     1 
ATOM   2532  O  O     . SER A 1 1767 ? 158.476 162.471 103.364 1.00 50.89  ? 1767 SER A O     1 
ATOM   2533  C  CB    . SER A 1 1767 ? 156.362 163.950 105.366 1.00 40.41  ? 1767 SER A CB    1 
ATOM   2534  O  OG    . SER A 1 1767 ? 155.556 162.919 104.825 1.00 49.08  ? 1767 SER A OG    1 
ATOM   2535  N  N     . SER A 1 1768 ? 158.915 164.672 103.557 1.00 45.91  ? 1768 SER A N     1 
ATOM   2536  C  CA    . SER A 1 1768 ? 159.564 164.737 102.251 1.00 43.35  ? 1768 SER A CA    1 
ATOM   2537  C  C     . SER A 1 1768 ? 160.871 163.954 102.242 1.00 49.04  ? 1768 SER A C     1 
ATOM   2538  O  O     . SER A 1 1768 ? 161.208 163.309 101.242 1.00 61.06  ? 1768 SER A O     1 
ATOM   2539  C  CB    . SER A 1 1768 ? 159.807 166.194 101.860 1.00 49.57  ? 1768 SER A CB    1 
ATOM   2540  O  OG    . SER A 1 1768 ? 158.595 166.835 101.499 1.00 47.22  ? 1768 SER A OG    1 
ATOM   2541  N  N     . MET A 1 1769 ? 161.622 163.998 103.343 1.00 49.14  ? 1769 MET A N     1 
ATOM   2542  C  CA    . MET A 1 1769 ? 162.891 163.286 103.437 1.00 50.64  ? 1769 MET A CA    1 
ATOM   2543  C  C     . MET A 1 1769 ? 162.729 161.828 103.839 1.00 63.06  ? 1769 MET A C     1 
ATOM   2544  O  O     . MET A 1 1769 ? 163.739 161.137 104.012 1.00 67.86  ? 1769 MET A O     1 
ATOM   2545  C  CB    . MET A 1 1769 ? 163.820 163.983 104.434 1.00 45.79  ? 1769 MET A CB    1 
ATOM   2546  C  CG    . MET A 1 1769 ? 163.883 165.488 104.277 1.00 52.43  ? 1769 MET A CG    1 
ATOM   2547  S  SD    . MET A 1 1769 ? 164.707 166.306 105.655 1.00 55.75  ? 1769 MET A SD    1 
ATOM   2548  C  CE    . MET A 1 1769 ? 166.293 165.474 105.636 1.00 47.82  ? 1769 MET A CE    1 
ATOM   2549  N  N     . GLY A 1 1770 ? 161.497 161.347 103.995 1.00 62.43  ? 1770 GLY A N     1 
ATOM   2550  C  CA    . GLY A 1 1770 ? 161.252 159.987 104.435 1.00 68.77  ? 1770 GLY A CA    1 
ATOM   2551  C  C     . GLY A 1 1770 ? 161.840 158.924 103.530 1.00 82.57  ? 1770 GLY A C     1 
ATOM   2552  O  O     . GLY A 1 1770 ? 162.077 157.794 103.966 1.00 83.91  ? 1770 GLY A O     1 
ATOM   2553  N  N     . GLY A 1 1771 ? 162.082 159.273 102.265 1.00 78.81  ? 1771 GLY A N     1 
ATOM   2554  C  CA    . GLY A 1 1771 ? 162.684 158.331 101.338 1.00 82.15  ? 1771 GLY A CA    1 
ATOM   2555  C  C     . GLY A 1 1771 ? 164.168 158.118 101.549 1.00 87.17  ? 1771 GLY A C     1 
ATOM   2556  O  O     . GLY A 1 1771 ? 164.741 157.197 100.957 1.00 87.69  ? 1771 GLY A O     1 
ATOM   2557  N  N     . GLY A 1 1772 ? 164.803 158.945 102.376 1.00 84.13  ? 1772 GLY A N     1 
ATOM   2558  C  CA    . GLY A 1 1772 ? 166.218 158.800 102.655 1.00 83.14  ? 1772 GLY A CA    1 
ATOM   2559  C  C     . GLY A 1 1772 ? 167.108 159.526 101.667 1.00 88.66  ? 1772 GLY A C     1 
ATOM   2560  O  O     . GLY A 1 1772 ? 167.862 160.427 102.046 1.00 83.76  ? 1772 GLY A O     1 
ATOM   2561  N  N     . GLY A 1 1773 ? 167.027 159.143 100.395 1.00 90.77  ? 1773 GLY A N     1 
ATOM   2562  C  CA    . GLY A 1 1773 ? 167.831 159.744 99.353  1.00 89.15  ? 1773 GLY A CA    1 
ATOM   2563  C  C     . GLY A 1 1773 ? 167.309 161.044 98.791  1.00 94.57  ? 1773 GLY A C     1 
ATOM   2564  O  O     . GLY A 1 1773 ? 167.923 161.605 97.879  1.00 92.91  ? 1773 GLY A O     1 
ATOM   2565  N  N     . ASP A 1 1774 ? 166.190 161.544 99.307  1.00 93.17  ? 1774 ASP A N     1 
ATOM   2566  C  CA    . ASP A 1 1774 ? 165.598 162.773 98.801  1.00 90.51  ? 1774 ASP A CA    1 
ATOM   2567  C  C     . ASP A 1 1774 ? 166.423 163.982 99.242  1.00 86.28  ? 1774 ASP A C     1 
ATOM   2568  O  O     . ASP A 1 1774 ? 167.464 163.864 99.894  1.00 80.14  ? 1774 ASP A O     1 
ATOM   2569  C  CB    . ASP A 1 1774 ? 164.152 162.895 99.275  1.00 79.64  ? 1774 ASP A CB    1 
ATOM   2570  C  CG    . ASP A 1 1774 ? 163.264 161.798 98.724  1.00 82.19  ? 1774 ASP A CG    1 
ATOM   2571  O  OD1   . ASP A 1 1774 ? 163.553 161.298 97.616  1.00 84.48  ? 1774 ASP A OD1   1 
ATOM   2572  O  OD2   . ASP A 1 1774 ? 162.279 161.432 99.399  1.00 74.58  ? 1774 ASP A OD2   1 
ATOM   2573  N  N     . ALA A 1 1775 ? 165.939 165.167 98.878  1.00 84.29  ? 1775 ALA A N     1 
ATOM   2574  C  CA    . ALA A 1 1775 ? 166.602 166.407 99.248  1.00 71.34  ? 1775 ALA A CA    1 
ATOM   2575  C  C     . ALA A 1 1775 ? 166.389 166.694 100.733 1.00 68.35  ? 1775 ALA A C     1 
ATOM   2576  O  O     . ALA A 1 1775 ? 165.831 165.887 101.482 1.00 60.27  ? 1775 ALA A O     1 
ATOM   2577  C  CB    . ALA A 1 1775 ? 166.092 167.560 98.386  1.00 57.68  ? 1775 ALA A CB    1 
ATOM   2578  N  N     . ALA A 1 1776 ? 166.840 167.872 101.167 1.00 66.78  ? 1776 ALA A N     1 
ATOM   2579  C  CA    . ALA A 1 1776 ? 166.767 168.280 102.569 1.00 51.31  ? 1776 ALA A CA    1 
ATOM   2580  C  C     . ALA A 1 1776 ? 166.000 169.592 102.677 1.00 52.92  ? 1776 ALA A C     1 
ATOM   2581  O  O     . ALA A 1 1776 ? 166.605 170.674 102.734 1.00 42.42  ? 1776 ALA A O     1 
ATOM   2582  C  CB    . ALA A 1 1776 ? 168.165 168.414 103.171 1.00 40.02  ? 1776 ALA A CB    1 
ATOM   2583  N  N     . PRO A 1 1777 ? 164.666 169.546 102.706 1.00 55.43  ? 1777 PRO A N     1 
ATOM   2584  C  CA    . PRO A 1 1777 ? 163.885 170.753 103.001 1.00 42.22  ? 1777 PRO A CA    1 
ATOM   2585  C  C     . PRO A 1 1777 ? 163.959 171.193 104.454 1.00 36.94  ? 1777 PRO A C     1 
ATOM   2586  O  O     . PRO A 1 1777 ? 163.331 172.197 104.809 1.00 34.37  ? 1777 PRO A O     1 
ATOM   2587  C  CB    . PRO A 1 1777 ? 162.453 170.338 102.626 1.00 40.68  ? 1777 PRO A CB    1 
ATOM   2588  C  CG    . PRO A 1 1777 ? 162.445 168.859 102.742 1.00 45.53  ? 1777 PRO A CG    1 
ATOM   2589  C  CD    . PRO A 1 1777 ? 163.809 168.412 102.321 1.00 52.27  ? 1777 PRO A CD    1 
ATOM   2590  N  N     . LEU A 1 1778 ? 164.694 170.468 105.302 1.00 34.63  ? 1778 LEU A N     1 
ATOM   2591  C  CA    . LEU A 1 1778 ? 164.926 170.933 106.665 1.00 32.15  ? 1778 LEU A CA    1 
ATOM   2592  C  C     . LEU A 1 1778 ? 165.704 172.241 106.679 1.00 33.78  ? 1778 LEU A C     1 
ATOM   2593  O  O     . LEU A 1 1778 ? 165.551 173.045 107.606 1.00 35.04  ? 1778 LEU A O     1 
ATOM   2594  C  CB    . LEU A 1 1778 ? 165.669 169.863 107.465 1.00 31.68  ? 1778 LEU A CB    1 
ATOM   2595  C  CG    . LEU A 1 1778 ? 164.841 168.947 108.367 1.00 30.09  ? 1778 LEU A CG    1 
ATOM   2596  C  CD1   . LEU A 1 1778 ? 165.696 168.404 109.500 1.00 25.97  ? 1778 LEU A CD1   1 
ATOM   2597  C  CD2   . LEU A 1 1778 ? 163.627 169.677 108.917 1.00 28.66  ? 1778 LEU A CD2   1 
ATOM   2598  N  N     . HIS A 1 1779 ? 166.545 172.469 105.666 1.00 34.99  ? 1779 HIS A N     1 
ATOM   2599  C  CA    . HIS A 1 1779 ? 167.257 173.738 105.565 1.00 34.10  ? 1779 HIS A CA    1 
ATOM   2600  C  C     . HIS A 1 1779 ? 166.299 174.896 105.323 1.00 30.64  ? 1779 HIS A C     1 
ATOM   2601  O  O     . HIS A 1 1779 ? 166.530 176.005 105.818 1.00 31.37  ? 1779 HIS A O     1 
ATOM   2602  C  CB    . HIS A 1 1779 ? 168.302 173.667 104.451 1.00 32.68  ? 1779 HIS A CB    1 
ATOM   2603  C  CG    . HIS A 1 1779 ? 169.554 172.947 104.844 1.00 33.33  ? 1779 HIS A CG    1 
ATOM   2604  N  ND1   . HIS A 1 1779 ? 169.963 171.780 104.235 1.00 35.86  ? 1779 HIS A ND1   1 
ATOM   2605  C  CD2   . HIS A 1 1779 ? 170.485 173.226 105.786 1.00 31.65  ? 1779 HIS A CD2   1 
ATOM   2606  C  CE1   . HIS A 1 1779 ? 171.093 171.372 104.784 1.00 35.95  ? 1779 HIS A CE1   1 
ATOM   2607  N  NE2   . HIS A 1 1779 ? 171.432 172.232 105.728 1.00 35.84  ? 1779 HIS A NE2   1 
ATOM   2608  N  N     . SER A 1 1780 ? 165.228 174.665 104.559 1.00 33.28  ? 1780 SER A N     1 
ATOM   2609  C  CA    . SER A 1 1780 ? 164.225 175.706 104.358 1.00 29.95  ? 1780 SER A CA    1 
ATOM   2610  C  C     . SER A 1 1780 ? 163.546 176.070 105.672 1.00 28.23  ? 1780 SER A C     1 
ATOM   2611  O  O     . SER A 1 1780 ? 163.248 177.244 105.922 1.00 31.30  ? 1780 SER A O     1 
ATOM   2612  C  CB    . SER A 1 1780 ? 163.194 175.259 103.323 1.00 27.53  ? 1780 SER A CB    1 
ATOM   2613  O  OG    . SER A 1 1780 ? 162.812 173.911 103.526 1.00 36.97  ? 1780 SER A OG    1 
ATOM   2614  N  N     . VAL A 1 1781 ? 163.288 175.074 106.522 1.00 26.22  ? 1781 VAL A N     1 
ATOM   2615  C  CA    . VAL A 1 1781 ? 162.719 175.347 107.839 1.00 23.25  ? 1781 VAL A CA    1 
ATOM   2616  C  C     . VAL A 1 1781 ? 163.690 176.168 108.678 1.00 27.43  ? 1781 VAL A C     1 
ATOM   2617  O  O     . VAL A 1 1781 ? 163.291 177.114 109.368 1.00 30.24  ? 1781 VAL A O     1 
ATOM   2618  C  CB    . VAL A 1 1781 ? 162.337 174.031 108.541 1.00 23.39  ? 1781 VAL A CB    1 
ATOM   2619  C  CG1   . VAL A 1 1781 ? 161.407 174.306 109.711 1.00 19.88  ? 1781 VAL A CG1   1 
ATOM   2620  C  CG2   . VAL A 1 1781 ? 161.691 173.072 107.556 1.00 29.16  ? 1781 VAL A CG2   1 
ATOM   2621  N  N     . LEU A 1 1782 ? 164.978 175.814 108.640 1.00 27.79  ? 1782 LEU A N     1 
ATOM   2622  C  CA    . LEU A 1 1782 ? 165.974 176.561 109.403 1.00 24.30  ? 1782 LEU A CA    1 
ATOM   2623  C  C     . LEU A 1 1782 ? 166.090 177.998 108.910 1.00 25.28  ? 1782 LEU A C     1 
ATOM   2624  O  O     . LEU A 1 1782 ? 166.144 178.935 109.715 1.00 31.42  ? 1782 LEU A O     1 
ATOM   2625  C  CB    . LEU A 1 1782 ? 167.329 175.860 109.328 1.00 24.41  ? 1782 LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1 1782 ? 168.464 176.508 110.125 1.00 25.50  ? 1782 LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1 1782 ? 168.151 176.490 111.613 1.00 25.38  ? 1782 LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1 1782 ? 169.787 175.816 109.842 1.00 29.24  ? 1782 LEU A CD2   1 
ATOM   2629  N  N     . SER A 1 1783 ? 166.131 178.193 107.589 1.00 25.14  ? 1783 SER A N     1 
ATOM   2630  C  CA    . SER A 1 1783 ? 166.269 179.541 107.045 1.00 27.06  ? 1783 SER A CA    1 
ATOM   2631  C  C     . SER A 1 1783 ? 165.050 180.396 107.367 1.00 28.14  ? 1783 SER A C     1 
ATOM   2632  O  O     . SER A 1 1783 ? 165.182 181.586 107.673 1.00 31.28  ? 1783 SER A O     1 
ATOM   2633  C  CB    . SER A 1 1783 ? 166.501 179.481 105.536 1.00 27.26  ? 1783 SER A CB    1 
ATOM   2634  O  OG    . SER A 1 1783 ? 165.769 178.422 104.949 1.00 29.20  ? 1783 SER A OG    1 
ATOM   2635  N  N     . ASN A 1 1784 ? 163.854 179.806 107.301 1.00 27.20  ? 1784 ASN A N     1 
ATOM   2636  C  CA    . ASN A 1 1784 ? 162.644 180.551 107.637 1.00 28.41  ? 1784 ASN A CA    1 
ATOM   2637  C  C     . ASN A 1 1784 ? 162.670 180.997 109.094 1.00 29.01  ? 1784 ASN A C     1 
ATOM   2638  O  O     . ASN A 1 1784 ? 162.264 182.120 109.415 1.00 30.47  ? 1784 ASN A O     1 
ATOM   2639  C  CB    . ASN A 1 1784 ? 161.409 179.697 107.337 1.00 29.54  ? 1784 ASN A CB    1 
ATOM   2640  C  CG    . ASN A 1 1784 ? 160.107 180.347 107.788 1.00 41.92  ? 1784 ASN A CG    1 
ATOM   2641  O  OD1   . ASN A 1 1784 ? 159.876 180.566 108.978 1.00 44.91  ? 1784 ASN A OD1   1 
ATOM   2642  N  ND2   . ASN A 1 1784 ? 159.248 180.663 106.826 1.00 46.67  ? 1784 ASN A ND2   1 
ATOM   2643  N  N     . VAL A 1 1785 ? 163.138 180.125 109.990 1.00 28.86  ? 1785 VAL A N     1 
ATOM   2644  C  CA    . VAL A 1 1785 ? 163.293 180.508 111.391 1.00 25.36  ? 1785 VAL A CA    1 
ATOM   2645  C  C     . VAL A 1 1785 ? 164.320 181.625 111.524 1.00 28.90  ? 1785 VAL A C     1 
ATOM   2646  O  O     . VAL A 1 1785 ? 164.106 182.603 112.252 1.00 31.86  ? 1785 VAL A O     1 
ATOM   2647  C  CB    . VAL A 1 1785 ? 163.673 179.281 112.240 1.00 24.07  ? 1785 VAL A CB    1 
ATOM   2648  C  CG1   . VAL A 1 1785 ? 164.143 179.707 113.622 1.00 23.41  ? 1785 VAL A CG1   1 
ATOM   2649  C  CG2   . VAL A 1 1785 ? 162.498 178.322 112.346 1.00 22.81  ? 1785 VAL A CG2   1 
ATOM   2650  N  N     . GLU A 1 1786 ? 165.448 181.502 110.820 1.00 27.28  ? 1786 GLU A N     1 
ATOM   2651  C  CA    . GLU A 1 1786 ? 166.484 182.528 110.889 1.00 26.81  ? 1786 GLU A CA    1 
ATOM   2652  C  C     . GLU A 1 1786 ? 166.002 183.848 110.299 1.00 30.21  ? 1786 GLU A C     1 
ATOM   2653  O  O     . GLU A 1 1786 ? 166.311 184.920 110.832 1.00 31.86  ? 1786 GLU A O     1 
ATOM   2654  C  CB    . GLU A 1 1786 ? 167.747 182.049 110.174 1.00 27.35  ? 1786 GLU A CB    1 
ATOM   2655  C  CG    . GLU A 1 1786 ? 168.450 180.895 110.867 1.00 32.38  ? 1786 GLU A CG    1 
ATOM   2656  C  CD    . GLU A 1 1786 ? 169.725 181.323 111.563 1.00 48.90  ? 1786 GLU A CD    1 
ATOM   2657  O  OE1   . GLU A 1 1786 ? 169.699 182.347 112.279 1.00 51.19  ? 1786 GLU A OE1   1 
ATOM   2658  O  OE2   . GLU A 1 1786 ? 170.755 180.637 111.394 1.00 45.55  ? 1786 GLU A OE2   1 
ATOM   2659  N  N     . VAL A 1 1787 ? 165.254 183.792 109.195 1.00 30.74  ? 1787 VAL A N     1 
ATOM   2660  C  CA    . VAL A 1 1787 ? 164.707 185.010 108.602 1.00 28.22  ? 1787 VAL A CA    1 
ATOM   2661  C  C     . VAL A 1 1787 ? 163.733 185.675 109.566 1.00 28.17  ? 1787 VAL A C     1 
ATOM   2662  O  O     . VAL A 1 1787 ? 163.773 186.893 109.780 1.00 30.29  ? 1787 VAL A O     1 
ATOM   2663  C  CB    . VAL A 1 1787 ? 164.042 184.698 107.249 1.00 27.54  ? 1787 VAL A CB    1 
ATOM   2664  C  CG1   . VAL A 1 1787 ? 163.138 185.843 106.820 1.00 34.85  ? 1787 VAL A CG1   1 
ATOM   2665  C  CG2   . VAL A 1 1787 ? 165.100 184.434 106.190 1.00 29.56  ? 1787 VAL A CG2   1 
ATOM   2666  N  N     . THR A 1 1788 ? 162.843 184.881 110.167 1.00 28.83  ? 1788 THR A N     1 
ATOM   2667  C  CA    . THR A 1 1788 ? 161.891 185.430 111.127 1.00 29.66  ? 1788 THR A CA    1 
ATOM   2668  C  C     . THR A 1 1788 ? 162.600 185.970 112.363 1.00 28.74  ? 1788 THR A C     1 
ATOM   2669  O  O     . THR A 1 1788 ? 162.208 187.009 112.907 1.00 30.86  ? 1788 THR A O     1 
ATOM   2670  C  CB    . THR A 1 1788 ? 160.866 184.367 111.521 1.00 26.48  ? 1788 THR A CB    1 
ATOM   2671  O  OG1   . THR A 1 1788 ? 160.451 183.644 110.356 1.00 33.10  ? 1788 THR A OG1   1 
ATOM   2672  C  CG2   . THR A 1 1788 ? 159.652 185.016 112.163 1.00 23.76  ? 1788 THR A CG2   1 
ATOM   2673  N  N     . LEU A 1 1789 ? 163.644 185.276 112.822 1.00 24.89  ? 1789 LEU A N     1 
ATOM   2674  C  CA    . LEU A 1 1789 ? 164.377 185.732 113.998 1.00 21.42  ? 1789 LEU A CA    1 
ATOM   2675  C  C     . LEU A 1 1789 ? 165.125 187.030 113.718 1.00 24.66  ? 1789 LEU A C     1 
ATOM   2676  O  O     . LEU A 1 1789 ? 165.290 187.863 114.617 1.00 28.37  ? 1789 LEU A O     1 
ATOM   2677  C  CB    . LEU A 1 1789 ? 165.341 184.642 114.466 1.00 18.86  ? 1789 LEU A CB    1 
ATOM   2678  C  CG    . LEU A 1 1789 ? 165.803 184.706 115.921 1.00 17.10  ? 1789 LEU A CG    1 
ATOM   2679  C  CD1   . LEU A 1 1789 ? 164.617 184.850 116.858 1.00 14.26  ? 1789 LEU A CD1   1 
ATOM   2680  C  CD2   . LEU A 1 1789 ? 166.615 183.473 116.273 1.00 15.92  ? 1789 LEU A CD2   1 
ATOM   2681  N  N     . ASN A 1 1790 ? 165.590 187.217 112.480 1.00 29.79  ? 1790 ASN A N     1 
ATOM   2682  C  CA    . ASN A 1 1790 ? 166.258 188.465 112.126 1.00 27.59  ? 1790 ASN A CA    1 
ATOM   2683  C  C     . ASN A 1 1790 ? 165.293 189.642 112.184 1.00 29.91  ? 1790 ASN A C     1 
ATOM   2684  O  O     . ASN A 1 1790 ? 165.650 190.725 112.663 1.00 31.76  ? 1790 ASN A O     1 
ATOM   2685  C  CB    . ASN A 1 1790 ? 166.883 188.350 110.736 1.00 30.64  ? 1790 ASN A CB    1 
ATOM   2686  C  CG    . ASN A 1 1790 ? 168.093 189.248 110.566 1.00 43.26  ? 1790 ASN A CG    1 
ATOM   2687  O  OD1   . ASN A 1 1790 ? 168.075 190.188 109.772 1.00 41.62  ? 1790 ASN A OD1   1 
ATOM   2688  N  ND2   . ASN A 1 1790 ? 169.151 188.963 111.316 1.00 40.55  ? 1790 ASN A ND2   1 
ATOM   2689  N  N     . VAL A 1 1791 ? 164.066 189.449 111.697 1.00 32.04  ? 1791 VAL A N     1 
ATOM   2690  C  CA    . VAL A 1 1791 ? 163.046 190.488 111.811 1.00 28.57  ? 1791 VAL A CA    1 
ATOM   2691  C  C     . VAL A 1 1791 ? 162.725 190.752 113.276 1.00 30.28  ? 1791 VAL A C     1 
ATOM   2692  O  O     . VAL A 1 1791 ? 162.533 191.901 113.691 1.00 31.34  ? 1791 VAL A O     1 
ATOM   2693  C  CB    . VAL A 1 1791 ? 161.787 190.090 111.016 1.00 30.58  ? 1791 VAL A CB    1 
ATOM   2694  C  CG1   . VAL A 1 1791 ? 160.710 191.156 111.149 1.00 31.40  ? 1791 VAL A CG1   1 
ATOM   2695  C  CG2   . VAL A 1 1791 ? 162.133 189.851 109.555 1.00 30.31  ? 1791 VAL A CG2   1 
ATOM   2696  N  N     . LEU A 1 1792 ? 162.658 189.688 114.079 1.00 26.75  ? 1792 LEU A N     1 
ATOM   2697  C  CA    . LEU A 1 1792 ? 162.390 189.840 115.506 1.00 23.84  ? 1792 LEU A CA    1 
ATOM   2698  C  C     . LEU A 1 1792 ? 163.491 190.632 116.197 1.00 24.34  ? 1792 LEU A C     1 
ATOM   2699  O  O     . LEU A 1 1792 ? 163.210 191.520 117.011 1.00 29.73  ? 1792 LEU A O     1 
ATOM   2700  C  CB    . LEU A 1 1792 ? 162.242 188.463 116.148 1.00 24.79  ? 1792 LEU A CB    1 
ATOM   2701  C  CG    . LEU A 1 1792 ? 160.825 188.008 116.473 1.00 18.49  ? 1792 LEU A CG    1 
ATOM   2702  C  CD1   . LEU A 1 1792 ? 159.992 188.008 115.217 1.00 19.66  ? 1792 LEU A CD1   1 
ATOM   2703  C  CD2   . LEU A 1 1792 ? 160.875 186.621 117.064 1.00 17.82  ? 1792 LEU A CD2   1 
ATOM   2704  N  N     . ALA A 1 1793 ? 164.753 190.321 115.890 1.00 24.92  ? 1793 ALA A N     1 
ATOM   2705  C  CA    . ALA A 1 1793 ? 165.861 191.058 116.487 1.00 23.27  ? 1793 ALA A CA    1 
ATOM   2706  C  C     . ALA A 1 1793 ? 165.853 192.516 116.048 1.00 30.37  ? 1793 ALA A C     1 
ATOM   2707  O  O     . ALA A 1 1793 ? 166.113 193.415 116.857 1.00 36.04  ? 1793 ALA A O     1 
ATOM   2708  C  CB    . ALA A 1 1793 ? 167.189 190.395 116.126 1.00 22.08  ? 1793 ALA A CB    1 
ATOM   2709  N  N     . ASP A 1 1794 ? 165.559 192.769 114.771 1.00 30.59  ? 1794 ASP A N     1 
ATOM   2710  C  CA    . ASP A 1 1794 ? 165.514 194.140 114.275 1.00 32.30  ? 1794 ASP A CA    1 
ATOM   2711  C  C     . ASP A 1 1794 ? 164.410 194.941 114.954 1.00 36.21  ? 1794 ASP A C     1 
ATOM   2712  O  O     . ASP A 1 1794 ? 164.611 196.106 115.317 1.00 38.44  ? 1794 ASP A O     1 
ATOM   2713  C  CB    . ASP A 1 1794 ? 165.320 194.141 112.758 1.00 34.72  ? 1794 ASP A CB    1 
ATOM   2714  C  CG    . ASP A 1 1794 ? 166.576 193.738 112.010 1.00 41.71  ? 1794 ASP A CG    1 
ATOM   2715  O  OD1   . ASP A 1 1794 ? 166.459 193.279 110.854 1.00 37.05  ? 1794 ASP A OD1   1 
ATOM   2716  O  OD2   . ASP A 1 1794 ? 167.679 193.879 112.577 1.00 48.98  ? 1794 ASP A OD2   1 
ATOM   2717  N  N     . SER A 1 1795 ? 163.252 194.306 115.152 1.00 37.37  ? 1795 SER A N     1 
ATOM   2718  C  CA    . SER A 1 1795 ? 162.105 194.995 115.802 1.00 37.87  ? 1795 SER A CA    1 
ATOM   2719  C  C     . SER A 1 1795 ? 162.479 195.397 117.236 1.00 35.91  ? 1795 SER A C     1 
ATOM   2720  O  O     . SER A 1 1795 ? 162.112 196.514 117.653 1.00 44.08  ? 1795 SER A O     1 
ATOM   2721  C  CB    . SER A 1 1795 ? 160.873 194.130 115.781 1.00 33.38  ? 1795 SER A CB    1 
ATOM   2722  O  OG    . SER A 1 1795 ? 160.540 193.754 114.451 1.00 35.47  ? 1795 SER A OG    1 
ATOM   2723  N  N     . VAL A 1 1796 ? 163.173 194.516 117.961 1.00 31.85  ? 1796 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1796 ? 163.548 194.803 119.379 1.00 33.86  ? 1796 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1796 ? 164.547 195.971 119.410 1.00 37.38  ? 1796 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1796 ? 164.461 196.797 120.343 1.00 40.83  ? 1796 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1796 ? 164.115 193.554 120.080 1.00 32.53  ? 1796 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1796 ? 164.772 193.899 121.411 1.00 28.96  ? 1796 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1796 ? 163.047 192.484 120.269 1.00 29.31  ? 1796 VAL A CG2   1 
ATOM   2730  N  N     . LEU A 1 1797 ? 165.448 196.037 118.425 1.00 37.31  ? 1797 LEU A N     1 
ATOM   2731  C  CA    . LEU A 1 1797 ? 166.474 197.112 118.390 1.00 34.03  ? 1797 LEU A CA    1 
ATOM   2732  C  C     . LEU A 1 1797 ? 165.773 198.480 118.376 1.00 37.53  ? 1797 LEU A C     1 
ATOM   2733  O  O     . LEU A 1 1797 ? 166.282 199.413 119.033 1.00 43.95  ? 1797 LEU A O     1 
ATOM   2734  C  CB    . LEU A 1 1797 ? 167.379 196.927 117.174 1.00 29.16  ? 1797 LEU A CB    1 
ATOM   2735  C  CG    . LEU A 1 1797 ? 168.178 195.621 117.132 1.00 35.91  ? 1797 LEU A CG    1 
ATOM   2736  C  CD1   . LEU A 1 1797 ? 169.097 195.575 115.924 1.00 38.83  ? 1797 LEU A CD1   1 
ATOM   2737  C  CD2   . LEU A 1 1797 ? 168.963 195.422 118.416 1.00 37.24  ? 1797 LEU A CD2   1 
ATOM   2738  N  N     . MET A 1 1798 ? 164.652 198.590 117.657 1.00 42.77  ? 1798 MET A N     1 
ATOM   2739  C  CA    . MET A 1 1798 ? 163.890 199.865 117.605 1.00 45.27  ? 1798 MET A CA    1 
ATOM   2740  C  C     . MET A 1 1798 ? 162.900 199.910 118.781 1.00 44.77  ? 1798 MET A C     1 
ATOM   2741  O  O     . MET A 1 1798 ? 162.551 198.829 119.304 1.00 41.53  ? 1798 MET A O     1 
ATOM   2742  C  CB    . MET A 1 1798 ? 163.136 199.998 116.277 1.00 42.13  ? 1798 MET A CB    1 
ATOM   2743  C  CG    . MET A 1 1798 ? 162.008 199.002 116.106 1.00 41.16  ? 1798 MET A CG    1 
ATOM   2744  S  SD    . MET A 1 1798 ? 161.396 198.908 114.412 1.00 70.21  ? 1798 MET A SD    1 
ATOM   2745  C  CE    . MET A 1 1798 ? 162.859 198.281 113.576 1.00 45.68  ? 1798 MET A CE    1 
ATOM   2746  N  N     . GLU A 1 1799 ? 162.470 201.112 119.176 1.00 49.14  ? 1799 GLU A N     1 
ATOM   2747  C  CA    . GLU A 1 1799 ? 161.529 201.263 120.318 1.00 48.94  ? 1799 GLU A CA    1 
ATOM   2748  C  C     . GLU A 1 1799 ? 160.198 200.571 119.984 1.00 51.42  ? 1799 GLU A C     1 
ATOM   2749  O  O     . GLU A 1 1799 ? 159.785 200.621 118.804 1.00 50.54  ? 1799 GLU A O     1 
ATOM   2750  C  CB    . GLU A 1 1799 ? 161.314 202.744 120.635 1.00 52.61  ? 1799 GLU A CB    1 
ATOM   2751  C  CG    . GLU A 1 1799 ? 160.234 202.992 121.684 1.00 56.21  ? 1799 GLU A CG    1 
ATOM   2752  C  CD    . GLU A 1 1799 ? 160.567 202.496 123.080 1.00 64.77  ? 1799 GLU A CD    1 
ATOM   2753  O  OE1   . GLU A 1 1799 ? 159.709 202.650 123.974 1.00 64.62  ? 1799 GLU A OE1   1 
ATOM   2754  O  OE2   . GLU A 1 1799 ? 161.679 201.963 123.278 1.00 65.55  ? 1799 GLU A OE2   1 
ATOM   2755  N  N     . GLN A 1 1800 ? 159.560 199.952 120.982 1.00 45.48  ? 1800 GLN A N     1 
ATOM   2756  C  CA    . GLN A 1 1800 ? 158.271 199.246 120.763 1.00 42.20  ? 1800 GLN A CA    1 
ATOM   2757  C  C     . GLN A 1 1800 ? 157.335 199.512 121.951 1.00 44.13  ? 1800 GLN A C     1 
ATOM   2758  O  O     . GLN A 1 1800 ? 157.851 199.759 123.064 1.00 40.87  ? 1800 GLN A O     1 
ATOM   2759  C  CB    . GLN A 1 1800 ? 158.507 197.741 120.626 1.00 36.16  ? 1800 GLN A CB    1 
ATOM   2760  C  CG    . GLN A 1 1800 ? 159.432 197.347 119.480 1.00 38.02  ? 1800 GLN A CG    1 
ATOM   2761  C  CD    . GLN A 1 1800 ? 158.830 197.587 118.113 1.00 38.69  ? 1800 GLN A CD    1 
ATOM   2762  O  OE1   . GLN A 1 1800 ? 157.709 198.088 117.981 1.00 46.15  ? 1800 GLN A OE1   1 
ATOM   2763  N  NE2   . GLN A 1 1800 ? 159.575 197.230 117.078 1.00 39.11  ? 1800 GLN A NE2   1 
ATOM   2764  N  N     . PRO A 1 1801 ? 155.995 199.474 121.776 1.00 39.50  ? 1801 PRO A N     1 
ATOM   2765  C  CA    . PRO A 1 1801 ? 155.083 199.628 122.902 1.00 29.71  ? 1801 PRO A CA    1 
ATOM   2766  C  C     . PRO A 1 1801 ? 155.399 198.520 123.889 1.00 34.17  ? 1801 PRO A C     1 
ATOM   2767  O  O     . PRO A 1 1801 ? 155.769 197.416 123.439 1.00 32.06  ? 1801 PRO A O     1 
ATOM   2768  C  CB    . PRO A 1 1801 ? 153.694 199.479 122.276 1.00 29.56  ? 1801 PRO A CB    1 
ATOM   2769  C  CG    . PRO A 1 1801 ? 153.916 199.766 120.806 1.00 39.15  ? 1801 PRO A CG    1 
ATOM   2770  C  CD    . PRO A 1 1801 ? 155.322 199.280 120.504 1.00 35.25  ? 1801 PRO A CD    1 
ATOM   2771  N  N     . PRO A 1 1802 ? 155.276 198.727 125.220 1.00 34.60  ? 1802 PRO A N     1 
ATOM   2772  C  CA    . PRO A 1 1802 ? 155.690 197.695 126.188 1.00 28.10  ? 1802 PRO A CA    1 
ATOM   2773  C  C     . PRO A 1 1802 ? 155.027 196.345 125.975 1.00 25.01  ? 1802 PRO A C     1 
ATOM   2774  O  O     . PRO A 1 1802 ? 155.679 195.310 126.161 1.00 26.72  ? 1802 PRO A O     1 
ATOM   2775  C  CB    . PRO A 1 1802 ? 155.301 198.313 127.540 1.00 26.25  ? 1802 PRO A CB    1 
ATOM   2776  C  CG    . PRO A 1 1802 ? 155.238 199.782 127.284 1.00 32.18  ? 1802 PRO A CG    1 
ATOM   2777  C  CD    . PRO A 1 1802 ? 154.734 199.924 125.883 1.00 30.82  ? 1802 PRO A CD    1 
ATOM   2778  N  N     . LEU A 1 1803 ? 153.751 196.320 125.589 1.00 23.47  ? 1803 LEU A N     1 
ATOM   2779  C  CA    . LEU A 1 1803 ? 153.079 195.045 125.361 1.00 24.77  ? 1803 LEU A CA    1 
ATOM   2780  C  C     . LEU A 1 1803 ? 153.659 194.326 124.150 1.00 24.79  ? 1803 LEU A C     1 
ATOM   2781  O  O     . LEU A 1 1803 ? 153.912 193.116 124.195 1.00 24.91  ? 1803 LEU A O     1 
ATOM   2782  C  CB    . LEU A 1 1803 ? 151.575 195.261 125.192 1.00 28.49  ? 1803 LEU A CB    1 
ATOM   2783  C  CG    . LEU A 1 1803 ? 150.737 193.982 125.165 1.00 17.17  ? 1803 LEU A CG    1 
ATOM   2784  C  CD1   . LEU A 1 1803 ? 150.783 193.284 126.513 1.00 20.82  ? 1803 LEU A CD1   1 
ATOM   2785  C  CD2   . LEU A 1 1803 ? 149.303 194.285 124.766 1.00 19.98  ? 1803 LEU A CD2   1 
ATOM   2786  N  N     . ARG A 1 1804 ? 153.879 195.056 123.054 1.00 23.74  ? 1804 ARG A N     1 
ATOM   2787  C  CA    . ARG A 1 1804 ? 154.478 194.446 121.872 1.00 23.43  ? 1804 ARG A CA    1 
ATOM   2788  C  C     . ARG A 1 1804 ? 155.920 194.035 122.130 1.00 22.93  ? 1804 ARG A C     1 
ATOM   2789  O  O     . ARG A 1 1804 ? 156.391 193.038 121.570 1.00 24.09  ? 1804 ARG A O     1 
ATOM   2790  C  CB    . ARG A 1 1804 ? 154.403 195.406 120.685 1.00 27.43  ? 1804 ARG A CB    1 
ATOM   2791  C  CG    . ARG A 1 1804 ? 154.822 194.787 119.362 1.00 29.94  ? 1804 ARG A CG    1 
ATOM   2792  C  CD    . ARG A 1 1804 ? 155.249 195.850 118.368 1.00 31.89  ? 1804 ARG A CD    1 
ATOM   2793  N  NE    . ARG A 1 1804 ? 154.119 196.637 117.890 1.00 32.69  ? 1804 ARG A NE    1 
ATOM   2794  C  CZ    . ARG A 1 1804 ? 154.231 197.763 117.200 1.00 36.54  ? 1804 ARG A CZ    1 
ATOM   2795  N  NH1   . ARG A 1 1804 ? 155.413 198.268 116.887 1.00 36.88  ? 1804 ARG A NH1   1 
ATOM   2796  N  NH2   . ARG A 1 1804 ? 153.128 198.398 116.811 1.00 40.27  ? 1804 ARG A NH2   1 
ATOM   2797  N  N     . ARG A 1 1805 ? 156.637 194.789 122.967 1.00 24.98  ? 1805 ARG A N     1 
ATOM   2798  C  CA    . ARG A 1 1805 ? 158.011 194.427 123.296 1.00 20.49  ? 1805 ARG A CA    1 
ATOM   2799  C  C     . ARG A 1 1805 ? 158.073 193.078 123.999 1.00 21.59  ? 1805 ARG A C     1 
ATOM   2800  O  O     . ARG A 1 1805 ? 158.904 192.231 123.656 1.00 21.80  ? 1805 ARG A O     1 
ATOM   2801  C  CB    . ARG A 1 1805 ? 158.645 195.514 124.163 1.00 23.71  ? 1805 ARG A CB    1 
ATOM   2802  C  CG    . ARG A 1 1805 ? 160.132 195.711 123.927 1.00 26.28  ? 1805 ARG A CG    1 
ATOM   2803  C  CD    . ARG A 1 1805 ? 160.788 196.403 125.111 1.00 22.50  ? 1805 ARG A CD    1 
ATOM   2804  N  NE    . ARG A 1 1805 ? 160.547 195.691 126.361 1.00 29.22  ? 1805 ARG A NE    1 
ATOM   2805  C  CZ    . ARG A 1 1805 ? 159.916 196.208 127.406 1.00 31.50  ? 1805 ARG A CZ    1 
ATOM   2806  N  NH1   . ARG A 1 1805 ? 159.444 197.443 127.388 1.00 33.15  ? 1805 ARG A NH1   1 
ATOM   2807  N  NH2   . ARG A 1 1805 ? 159.754 195.465 128.498 1.00 27.41  ? 1805 ARG A NH2   1 
ATOM   2808  N  N     . ARG A 1 1806 ? 157.190 192.853 124.976 1.00 25.79  ? 1806 ARG A N     1 
ATOM   2809  C  CA    . ARG A 1 1806 ? 157.182 191.576 125.683 1.00 20.34  ? 1806 ARG A CA    1 
ATOM   2810  C  C     . ARG A 1 1806 ? 156.794 190.434 124.753 1.00 15.62  ? 1806 ARG A C     1 
ATOM   2811  O  O     . ARG A 1 1806 ? 157.308 189.317 124.887 1.00 16.56  ? 1806 ARG A O     1 
ATOM   2812  C  CB    . ARG A 1 1806 ? 156.239 191.644 126.884 1.00 22.89  ? 1806 ARG A CB    1 
ATOM   2813  C  CG    . ARG A 1 1806 ? 156.573 192.763 127.855 1.00 23.95  ? 1806 ARG A CG    1 
ATOM   2814  C  CD    . ARG A 1 1806 ? 157.288 192.243 129.092 1.00 33.39  ? 1806 ARG A CD    1 
ATOM   2815  N  NE    . ARG A 1 1806 ? 156.484 191.289 129.846 1.00 37.68  ? 1806 ARG A NE    1 
ATOM   2816  C  CZ    . ARG A 1 1806 ? 155.552 191.629 130.725 1.00 43.73  ? 1806 ARG A CZ    1 
ATOM   2817  N  NH1   . ARG A 1 1806 ? 155.265 192.897 130.972 1.00 39.92  ? 1806 ARG A NH1   1 
ATOM   2818  N  NH2   . ARG A 1 1806 ? 154.894 190.675 131.377 1.00 40.28  ? 1806 ARG A NH2   1 
ATOM   2819  N  N     . LYS A 1 1807 ? 155.887 190.692 123.809 1.00 16.30  ? 1807 LYS A N     1 
ATOM   2820  C  CA    . LYS A 1 1807 ? 155.545 189.677 122.817 1.00 15.29  ? 1807 LYS A CA    1 
ATOM   2821  C  C     . LYS A 1 1807 ? 156.750 189.323 121.956 1.00 18.23  ? 1807 LYS A C     1 
ATOM   2822  O  O     . LYS A 1 1807 ? 156.974 188.148 121.641 1.00 22.56  ? 1807 LYS A O     1 
ATOM   2823  C  CB    . LYS A 1 1807 ? 154.389 190.161 121.943 1.00 17.87  ? 1807 LYS A CB    1 
ATOM   2824  C  CG    . LYS A 1 1807 ? 153.041 190.183 122.639 1.00 14.63  ? 1807 LYS A CG    1 
ATOM   2825  C  CD    . LYS A 1 1807 ? 151.941 190.567 121.667 1.00 15.70  ? 1807 LYS A CD    1 
ATOM   2826  C  CE    . LYS A 1 1807 ? 150.626 190.808 122.382 1.00 19.46  ? 1807 LYS A CE    1 
ATOM   2827  N  NZ    . LYS A 1 1807 ? 149.574 191.288 121.446 1.00 18.96  ? 1807 LYS A NZ    1 
ATOM   2828  N  N     . LEU A 1 1808 ? 157.534 190.328 121.560 1.00 18.14  ? 1808 LEU A N     1 
ATOM   2829  C  CA    . LEU A 1 1808 ? 158.714 190.067 120.742 1.00 13.97  ? 1808 LEU A CA    1 
ATOM   2830  C  C     . LEU A 1 1808 ? 159.757 189.261 121.508 1.00 16.56  ? 1808 LEU A C     1 
ATOM   2831  O  O     . LEU A 1 1808 ? 160.382 188.354 120.947 1.00 19.93  ? 1808 LEU A O     1 
ATOM   2832  C  CB    . LEU A 1 1808 ? 159.308 191.383 120.242 1.00 18.86  ? 1808 LEU A CB    1 
ATOM   2833  C  CG    . LEU A 1 1808 ? 158.486 192.126 119.186 1.00 17.80  ? 1808 LEU A CG    1 
ATOM   2834  C  CD1   . LEU A 1 1808 ? 158.987 193.551 119.016 1.00 25.04  ? 1808 LEU A CD1   1 
ATOM   2835  C  CD2   . LEU A 1 1808 ? 158.526 191.381 117.865 1.00 18.66  ? 1808 LEU A CD2   1 
ATOM   2836  N  N     . GLU A 1 1809 ? 159.964 189.578 122.790 1.00 16.45  ? 1809 GLU A N     1 
ATOM   2837  C  CA    . GLU A 1 1809 ? 160.932 188.826 123.585 1.00 12.50  ? 1809 GLU A CA    1 
ATOM   2838  C  C     . GLU A 1 1809 ? 160.506 187.374 123.748 1.00 14.25  ? 1809 GLU A C     1 
ATOM   2839  O  O     . GLU A 1 1809 ? 161.341 186.464 123.686 1.00 16.26  ? 1809 GLU A O     1 
ATOM   2840  C  CB    . GLU A 1 1809 ? 161.127 189.484 124.951 1.00 15.01  ? 1809 GLU A CB    1 
ATOM   2841  C  CG    . GLU A 1 1809 ? 161.434 190.968 124.895 1.00 22.28  ? 1809 GLU A CG    1 
ATOM   2842  C  CD    . GLU A 1 1809 ? 161.444 191.611 126.267 1.00 32.06  ? 1809 GLU A CD    1 
ATOM   2843  O  OE1   . GLU A 1 1809 ? 160.422 192.220 126.647 1.00 30.42  ? 1809 GLU A OE1   1 
ATOM   2844  O  OE2   . GLU A 1 1809 ? 162.474 191.509 126.966 1.00 35.70  ? 1809 GLU A OE2   1 
ATOM   2845  N  N     . HIS A 1 1810 ? 159.212 187.135 123.974 1.00 14.27  ? 1810 HIS A N     1 
ATOM   2846  C  CA    . HIS A 1 1810 ? 158.720 185.763 124.043 1.00 13.69  ? 1810 HIS A CA    1 
ATOM   2847  C  C     . HIS A 1 1810 ? 158.907 185.050 122.711 1.00 12.32  ? 1810 HIS A C     1 
ATOM   2848  O  O     . HIS A 1 1810 ? 159.311 183.882 122.673 1.00 15.00  ? 1810 HIS A O     1 
ATOM   2849  C  CB    . HIS A 1 1810 ? 157.248 185.743 124.454 1.00 13.59  ? 1810 HIS A CB    1 
ATOM   2850  C  CG    . HIS A 1 1810 ? 156.982 186.350 125.797 1.00 14.42  ? 1810 HIS A CG    1 
ATOM   2851  N  ND1   . HIS A 1 1810 ? 157.982 186.847 126.603 1.00 19.68  ? 1810 HIS A ND1   1 
ATOM   2852  C  CD2   . HIS A 1 1810 ? 155.825 186.531 126.477 1.00 16.12  ? 1810 HIS A CD2   1 
ATOM   2853  C  CE1   . HIS A 1 1810 ? 157.453 187.314 127.720 1.00 23.30  ? 1810 HIS A CE1   1 
ATOM   2854  N  NE2   . HIS A 1 1810 ? 156.146 187.134 127.669 1.00 20.70  ? 1810 HIS A NE2   1 
ATOM   2855  N  N     . LEU A 1 1811 ? 158.612 185.739 121.607 1.00 14.41  ? 1811 LEU A N     1 
ATOM   2856  C  CA    . LEU A 1 1811 ? 158.788 185.137 120.290 1.00 14.50  ? 1811 LEU A CA    1 
ATOM   2857  C  C     . LEU A 1 1811 ? 160.261 184.893 119.988 1.00 12.43  ? 1811 LEU A C     1 
ATOM   2858  O  O     . LEU A 1 1811 ? 160.616 183.878 119.376 1.00 14.50  ? 1811 LEU A O     1 
ATOM   2859  C  CB    . LEU A 1 1811 ? 158.152 186.022 119.220 1.00 11.09  ? 1811 LEU A CB    1 
ATOM   2860  C  CG    . LEU A 1 1811 ? 156.667 185.783 118.948 1.00 10.07  ? 1811 LEU A CG    1 
ATOM   2861  C  CD1   . LEU A 1 1811 ? 156.153 186.753 117.898 1.00 18.11  ? 1811 LEU A CD1   1 
ATOM   2862  C  CD2   . LEU A 1 1811 ? 156.422 184.345 118.523 1.00 10.47  ? 1811 LEU A CD2   1 
ATOM   2863  N  N     . ILE A 1 1812 ? 161.134 185.816 120.399 1.00 11.09  ? 1812 ILE A N     1 
ATOM   2864  C  CA    . ILE A 1 1812 ? 162.570 185.613 120.220 1.00 10.57  ? 1812 ILE A CA    1 
ATOM   2865  C  C     . ILE A 1 1812 ? 163.031 184.388 120.996 1.00 11.17  ? 1812 ILE A C     1 
ATOM   2866  O  O     . ILE A 1 1812 ? 163.795 183.561 120.483 1.00 13.12  ? 1812 ILE A O     1 
ATOM   2867  C  CB    . ILE A 1 1812 ? 163.350 186.874 120.639 1.00 11.76  ? 1812 ILE A CB    1 
ATOM   2868  C  CG1   . ILE A 1 1812 ? 163.234 187.957 119.569 1.00 12.75  ? 1812 ILE A CG1   1 
ATOM   2869  C  CG2   . ILE A 1 1812 ? 164.813 186.547 120.886 1.00 15.77  ? 1812 ILE A CG2   1 
ATOM   2870  C  CD1   . ILE A 1 1812 ? 163.905 189.251 119.947 1.00 17.36  ? 1812 ILE A CD1   1 
ATOM   2871  N  N     . THR A 1 1813 ? 162.563 184.244 122.237 1.00 12.00  ? 1813 THR A N     1 
ATOM   2872  C  CA    . THR A 1 1813 ? 162.961 183.105 123.058 1.00 10.40  ? 1813 THR A CA    1 
ATOM   2873  C  C     . THR A 1 1813 ? 162.542 181.793 122.408 1.00 9.70   ? 1813 THR A C     1 
ATOM   2874  O  O     . THR A 1 1813 ? 163.301 180.817 122.403 1.00 9.83   ? 1813 THR A O     1 
ATOM   2875  C  CB    . THR A 1 1813 ? 162.356 183.231 124.457 1.00 10.84  ? 1813 THR A CB    1 
ATOM   2876  O  OG1   . THR A 1 1813 ? 162.670 184.517 125.003 1.00 13.95  ? 1813 THR A OG1   1 
ATOM   2877  C  CG2   . THR A 1 1813 ? 162.910 182.155 125.377 1.00 9.48   ? 1813 THR A CG2   1 
ATOM   2878  N  N     . GLU A 1 1814 ? 161.331 181.753 121.852 1.00 10.74  ? 1814 GLU A N     1 
ATOM   2879  C  CA    . GLU A 1 1814 ? 160.843 180.528 121.230 1.00 10.91  ? 1814 GLU A CA    1 
ATOM   2880  C  C     . GLU A 1 1814 ? 161.630 180.181 119.973 1.00 12.84  ? 1814 GLU A C     1 
ATOM   2881  O  O     . GLU A 1 1814 ? 161.999 179.020 119.764 1.00 15.72  ? 1814 GLU A O     1 
ATOM   2882  C  CB    . GLU A 1 1814 ? 159.359 180.664 120.904 1.00 15.63  ? 1814 GLU A CB    1 
ATOM   2883  C  CG    . GLU A 1 1814 ? 158.551 179.462 121.319 1.00 19.94  ? 1814 GLU A CG    1 
ATOM   2884  C  CD    . GLU A 1 1814 ? 158.626 178.345 120.301 1.00 24.72  ? 1814 GLU A CD    1 
ATOM   2885  O  OE1   . GLU A 1 1814 ? 158.304 178.595 119.120 1.00 26.25  ? 1814 GLU A OE1   1 
ATOM   2886  O  OE2   . GLU A 1 1814 ? 159.010 177.218 120.679 1.00 22.15  ? 1814 GLU A OE2   1 
ATOM   2887  N  N     . LEU A 1 1815 ? 161.900 181.173 119.123 1.00 12.72  ? 1815 LEU A N     1 
ATOM   2888  C  CA    . LEU A 1 1815 ? 162.553 180.893 117.849 1.00 9.55   ? 1815 LEU A CA    1 
ATOM   2889  C  C     . LEU A 1 1815 ? 164.037 180.591 118.012 1.00 10.30  ? 1815 LEU A C     1 
ATOM   2890  O  O     . LEU A 1 1815 ? 164.617 179.904 117.165 1.00 14.72  ? 1815 LEU A O     1 
ATOM   2891  C  CB    . LEU A 1 1815 ? 162.347 182.062 116.885 1.00 12.93  ? 1815 LEU A CB    1 
ATOM   2892  C  CG    . LEU A 1 1815 ? 161.117 181.980 115.978 1.00 13.10  ? 1815 LEU A CG    1 
ATOM   2893  C  CD1   . LEU A 1 1815 ? 159.828 182.146 116.762 1.00 14.50  ? 1815 LEU A CD1   1 
ATOM   2894  C  CD2   . LEU A 1 1815 ? 161.209 183.018 114.878 1.00 18.87  ? 1815 LEU A CD2   1 
ATOM   2895  N  N     . VAL A 1 1816 ? 164.669 181.095 119.074 1.00 10.50  ? 1816 VAL A N     1 
ATOM   2896  C  CA    . VAL A 1 1816 ? 166.030 180.665 119.385 1.00 12.17  ? 1816 VAL A CA    1 
ATOM   2897  C  C     . VAL A 1 1816 ? 166.041 179.184 119.737 1.00 12.85  ? 1816 VAL A C     1 
ATOM   2898  O  O     . VAL A 1 1816 ? 166.929 178.433 119.314 1.00 11.73  ? 1816 VAL A O     1 
ATOM   2899  C  CB    . VAL A 1 1816 ? 166.626 181.529 120.512 1.00 9.27   ? 1816 VAL A CB    1 
ATOM   2900  C  CG1   . VAL A 1 1816 ? 167.948 180.952 120.983 1.00 12.99  ? 1816 VAL A CG1   1 
ATOM   2901  C  CG2   . VAL A 1 1816 ? 166.831 182.952 120.029 1.00 9.17   ? 1816 VAL A CG2   1 
ATOM   2902  N  N     . HIS A 1 1817 ? 165.050 178.739 120.512 1.00 10.93  ? 1817 HIS A N     1 
ATOM   2903  C  CA    . HIS A 1 1817 ? 164.910 177.315 120.797 1.00 8.69   ? 1817 HIS A CA    1 
ATOM   2904  C  C     . HIS A 1 1817 ? 164.632 176.524 119.525 1.00 10.67  ? 1817 HIS A C     1 
ATOM   2905  O  O     . HIS A 1 1817 ? 165.193 175.441 119.324 1.00 12.14  ? 1817 HIS A O     1 
ATOM   2906  C  CB    . HIS A 1 1817 ? 163.796 177.095 121.819 1.00 8.03   ? 1817 HIS A CB    1 
ATOM   2907  C  CG    . HIS A 1 1817 ? 163.474 175.654 122.064 1.00 7.63   ? 1817 HIS A CG    1 
ATOM   2908  N  ND1   . HIS A 1 1817 ? 164.421 174.737 122.464 1.00 9.57   ? 1817 HIS A ND1   1 
ATOM   2909  C  CD2   . HIS A 1 1817 ? 162.308 174.973 121.969 1.00 7.08   ? 1817 HIS A CD2   1 
ATOM   2910  C  CE1   . HIS A 1 1817 ? 163.853 173.552 122.601 1.00 10.67  ? 1817 HIS A CE1   1 
ATOM   2911  N  NE2   . HIS A 1 1817 ? 162.571 173.669 122.308 1.00 8.52   ? 1817 HIS A NE2   1 
ATOM   2912  N  N     . GLN A 1 1818 ? 163.765 177.050 118.656 1.00 9.43   ? 1818 GLN A N     1 
ATOM   2913  C  CA    . GLN A 1 1818 ? 163.458 176.363 117.405 1.00 9.21   ? 1818 GLN A CA    1 
ATOM   2914  C  C     . GLN A 1 1818 ? 164.683 176.281 116.505 1.00 11.87  ? 1818 GLN A C     1 
ATOM   2915  O  O     . GLN A 1 1818 ? 164.912 175.258 115.848 1.00 15.27  ? 1818 GLN A O     1 
ATOM   2916  C  CB    . GLN A 1 1818 ? 162.315 177.073 116.685 1.00 10.69  ? 1818 GLN A CB    1 
ATOM   2917  C  CG    . GLN A 1 1818 ? 160.995 177.028 117.425 1.00 11.02  ? 1818 GLN A CG    1 
ATOM   2918  C  CD    . GLN A 1 1818 ? 159.881 177.701 116.654 1.00 13.21  ? 1818 GLN A CD    1 
ATOM   2919  O  OE1   . GLN A 1 1818 ? 160.129 178.432 115.695 1.00 18.79  ? 1818 GLN A OE1   1 
ATOM   2920  N  NE2   . GLN A 1 1818 ? 158.644 177.461 117.071 1.00 13.99  ? 1818 GLN A NE2   1 
ATOM   2921  N  N     . ARG A 1 1819 ? 165.475 177.353 116.451 1.00 11.19  ? 1819 ARG A N     1 
ATOM   2922  C  CA    . ARG A 1 1819 ? 166.695 177.331 115.651 1.00 11.59  ? 1819 ARG A CA    1 
ATOM   2923  C  C     . ARG A 1 1819 ? 167.687 176.308 116.188 1.00 15.38  ? 1819 ARG A C     1 
ATOM   2924  O  O     . ARG A 1 1819 ? 168.330 175.590 115.414 1.00 22.91  ? 1819 ARG A O     1 
ATOM   2925  C  CB    . ARG A 1 1819 ? 167.316 178.727 115.613 1.00 17.90  ? 1819 ARG A CB    1 
ATOM   2926  C  CG    . ARG A 1 1819 ? 168.644 178.807 114.882 1.00 23.39  ? 1819 ARG A CG    1 
ATOM   2927  C  CD    . ARG A 1 1819 ? 169.365 180.100 115.213 1.00 24.66  ? 1819 ARG A CD    1 
ATOM   2928  N  NE    . ARG A 1 1819 ? 169.691 180.198 116.630 1.00 28.22  ? 1819 ARG A NE    1 
ATOM   2929  C  CZ    . ARG A 1 1819 ? 170.099 181.309 117.228 1.00 28.19  ? 1819 ARG A CZ    1 
ATOM   2930  N  NH1   . ARG A 1 1819 ? 170.245 182.441 116.558 1.00 29.16  ? 1819 ARG A NH1   1 
ATOM   2931  N  NH2   . ARG A 1 1819 ? 170.366 181.285 118.530 1.00 18.48  ? 1819 ARG A NH2   1 
ATOM   2932  N  N     . ASP A 1 1820 ? 167.823 176.226 117.513 1.00 16.34  ? 1820 ASP A N     1 
ATOM   2933  C  CA    . ASP A 1 1820 ? 168.720 175.239 118.106 1.00 13.45  ? 1820 ASP A CA    1 
ATOM   2934  C  C     . ASP A 1 1820 ? 168.243 173.819 117.824 1.00 17.91  ? 1820 ASP A C     1 
ATOM   2935  O  O     . ASP A 1 1820 ? 169.053 172.930 117.537 1.00 24.52  ? 1820 ASP A O     1 
ATOM   2936  C  CB    . ASP A 1 1820 ? 168.839 175.478 119.611 1.00 15.49  ? 1820 ASP A CB    1 
ATOM   2937  C  CG    . ASP A 1 1820 ? 169.544 176.780 119.941 1.00 30.29  ? 1820 ASP A CG    1 
ATOM   2938  O  OD1   . ASP A 1 1820 ? 169.816 177.025 121.136 1.00 30.25  ? 1820 ASP A OD1   1 
ATOM   2939  O  OD2   . ASP A 1 1820 ? 169.822 177.562 119.007 1.00 29.00  ? 1820 ASP A OD2   1 
ATOM   2940  N  N     . VAL A 1 1821 ? 166.931 173.586 117.909 1.00 18.86  ? 1821 VAL A N     1 
ATOM   2941  C  CA    . VAL A 1 1821 ? 166.391 172.253 117.649 1.00 14.82  ? 1821 VAL A CA    1 
ATOM   2942  C  C     . VAL A 1 1821 ? 166.557 171.884 116.181 1.00 17.26  ? 1821 VAL A C     1 
ATOM   2943  O  O     . VAL A 1 1821 ? 166.968 170.764 115.850 1.00 23.46  ? 1821 VAL A O     1 
ATOM   2944  C  CB    . VAL A 1 1821 ? 164.917 172.180 118.089 1.00 13.78  ? 1821 VAL A CB    1 
ATOM   2945  C  CG1   . VAL A 1 1821 ? 164.247 170.944 117.511 1.00 16.95  ? 1821 VAL A CG1   1 
ATOM   2946  C  CG2   . VAL A 1 1821 ? 164.820 172.176 119.602 1.00 12.15  ? 1821 VAL A CG2   1 
ATOM   2947  N  N     . THR A 1 1822 ? 166.240 172.815 115.278 1.00 14.14  ? 1822 THR A N     1 
ATOM   2948  C  CA    . THR A 1 1822 ? 166.342 172.525 113.852 1.00 14.72  ? 1822 THR A CA    1 
ATOM   2949  C  C     . THR A 1 1822 ? 167.789 172.286 113.439 1.00 24.84  ? 1822 THR A C     1 
ATOM   2950  O  O     . THR A 1 1822 ? 168.068 171.407 112.615 1.00 30.33  ? 1822 THR A O     1 
ATOM   2951  C  CB    . THR A 1 1822 ? 165.730 173.665 113.038 1.00 19.73  ? 1822 THR A CB    1 
ATOM   2952  O  OG1   . THR A 1 1822 ? 164.393 173.910 113.492 1.00 21.27  ? 1822 THR A OG1   1 
ATOM   2953  C  CG2   . THR A 1 1822 ? 165.691 173.303 111.561 1.00 22.89  ? 1822 THR A CG2   1 
ATOM   2954  N  N     . ARG A 1 1823 ? 168.723 173.058 114.000 1.00 24.00  ? 1823 ARG A N     1 
ATOM   2955  C  CA    . ARG A 1 1823 ? 170.137 172.814 113.740 1.00 20.69  ? 1823 ARG A CA    1 
ATOM   2956  C  C     . ARG A 1 1823 ? 170.553 171.435 114.233 1.00 26.97  ? 1823 ARG A C     1 
ATOM   2957  O  O     . ARG A 1 1823 ? 171.326 170.734 113.568 1.00 30.57  ? 1823 ARG A O     1 
ATOM   2958  C  CB    . ARG A 1 1823 ? 170.988 173.897 114.402 1.00 22.50  ? 1823 ARG A CB    1 
ATOM   2959  C  CG    . ARG A 1 1823 ? 171.022 175.215 113.648 1.00 26.10  ? 1823 ARG A CG    1 
ATOM   2960  C  CD    . ARG A 1 1823 ? 171.779 176.270 114.435 1.00 21.41  ? 1823 ARG A CD    1 
ATOM   2961  N  NE    . ARG A 1 1823 ? 171.900 177.521 113.696 1.00 28.22  ? 1823 ARG A NE    1 
ATOM   2962  C  CZ    . ARG A 1 1823 ? 172.366 178.650 114.210 1.00 36.13  ? 1823 ARG A CZ    1 
ATOM   2963  N  NH1   . ARG A 1 1823 ? 172.767 178.723 115.469 1.00 36.69  ? 1823 ARG A NH1   1 
ATOM   2964  N  NH2   . ARG A 1 1823 ? 172.429 179.735 113.443 1.00 42.02  ? 1823 ARG A NH2   1 
ATOM   2965  N  N     . SER A 1 1824 ? 170.054 171.031 115.404 1.00 26.54  ? 1824 SER A N     1 
ATOM   2966  C  CA    . SER A 1 1824 ? 170.356 169.701 115.922 1.00 24.58  ? 1824 SER A CA    1 
ATOM   2967  C  C     . SER A 1 1824 ? 169.796 168.613 115.013 1.00 28.76  ? 1824 SER A C     1 
ATOM   2968  O  O     . SER A 1 1824 ? 170.450 167.589 114.784 1.00 37.26  ? 1824 SER A O     1 
ATOM   2969  C  CB    . SER A 1 1824 ? 169.805 169.554 117.340 1.00 27.41  ? 1824 SER A CB    1 
ATOM   2970  O  OG    . SER A 1 1824 ? 169.895 168.213 117.786 1.00 38.06  ? 1824 SER A OG    1 
ATOM   2971  N  N     . LEU A 1 1825 ? 168.582 168.814 114.494 1.00 25.23  ? 1825 LEU A N     1 
ATOM   2972  C  CA    . LEU A 1 1825 ? 167.989 167.831 113.592 1.00 26.05  ? 1825 LEU A CA    1 
ATOM   2973  C  C     . LEU A 1 1825 ? 168.805 167.688 112.314 1.00 30.75  ? 1825 LEU A C     1 
ATOM   2974  O  O     . LEU A 1 1825 ? 169.012 166.573 111.822 1.00 30.77  ? 1825 LEU A O     1 
ATOM   2975  C  CB    . LEU A 1 1825 ? 166.548 168.221 113.264 1.00 24.24  ? 1825 LEU A CB    1 
ATOM   2976  C  CG    . LEU A 1 1825 ? 165.497 167.982 114.349 1.00 21.91  ? 1825 LEU A CG    1 
ATOM   2977  C  CD1   . LEU A 1 1825 ? 164.101 168.194 113.789 1.00 18.36  ? 1825 LEU A CD1   1 
ATOM   2978  C  CD2   . LEU A 1 1825 ? 165.635 166.590 114.939 1.00 22.52  ? 1825 LEU A CD2   1 
ATOM   2979  N  N     . ILE A 1 1826 ? 169.265 168.809 111.754 1.00 31.37  ? 1826 ILE A N     1 
ATOM   2980  C  CA    . ILE A 1 1826 ? 170.103 168.756 110.561 1.00 30.26  ? 1826 ILE A CA    1 
ATOM   2981  C  C     . ILE A 1 1826 ? 171.438 168.093 110.873 1.00 31.92  ? 1826 ILE A C     1 
ATOM   2982  O  O     . ILE A 1 1826 ? 171.931 167.262 110.100 1.00 37.56  ? 1826 ILE A O     1 
ATOM   2983  C  CB    . ILE A 1 1826 ? 170.291 170.170 109.981 1.00 27.23  ? 1826 ILE A CB    1 
ATOM   2984  C  CG1   . ILE A 1 1826 ? 168.955 170.720 109.481 1.00 29.58  ? 1826 ILE A CG1   1 
ATOM   2985  C  CG2   . ILE A 1 1826 ? 171.315 170.159 108.858 1.00 28.46  ? 1826 ILE A CG2   1 
ATOM   2986  C  CD1   . ILE A 1 1826 ? 169.007 172.175 109.077 1.00 28.53  ? 1826 ILE A CD1   1 
ATOM   2987  N  N     . LYS A 1 1827 ? 172.044 168.445 112.011 1.00 33.17  ? 1827 LYS A N     1 
ATOM   2988  C  CA    . LYS A 1 1827 ? 173.335 167.870 112.375 1.00 35.42  ? 1827 LYS A CA    1 
ATOM   2989  C  C     . LYS A 1 1827 ? 173.231 166.374 112.642 1.00 38.71  ? 1827 LYS A C     1 
ATOM   2990  O  O     . LYS A 1 1827 ? 174.214 165.644 112.468 1.00 42.72  ? 1827 LYS A O     1 
ATOM   2991  C  CB    . LYS A 1 1827 ? 173.903 168.590 113.598 1.00 36.70  ? 1827 LYS A CB    1 
ATOM   2992  C  CG    . LYS A 1 1827 ? 175.407 168.803 113.549 1.00 43.77  ? 1827 LYS A CG    1 
ATOM   2993  C  CD    . LYS A 1 1827 ? 175.999 168.898 114.945 1.00 52.12  ? 1827 LYS A CD    1 
ATOM   2994  C  CE    . LYS A 1 1827 ? 176.030 167.539 115.626 1.00 55.39  ? 1827 LYS A CE    1 
ATOM   2995  N  NZ    . LYS A 1 1827 ? 176.902 166.576 114.899 1.00 52.39  ? 1827 LYS A NZ    1 
ATOM   2996  N  N     . SER A 1 1828 ? 172.061 165.900 113.061 1.00 37.73  ? 1828 SER A N     1 
ATOM   2997  C  CA    . SER A 1 1828 ? 171.842 164.484 113.319 1.00 39.74  ? 1828 SER A CA    1 
ATOM   2998  C  C     . SER A 1 1828 ? 171.414 163.715 112.077 1.00 37.72  ? 1828 SER A C     1 
ATOM   2999  O  O     . SER A 1 1828 ? 171.192 162.503 112.167 1.00 39.31  ? 1828 SER A O     1 
ATOM   3000  C  CB    . SER A 1 1828 ? 170.792 164.304 114.421 1.00 37.67  ? 1828 SER A CB    1 
ATOM   3001  O  OG    . SER A 1 1828 ? 171.265 164.803 115.660 1.00 39.40  ? 1828 SER A OG    1 
ATOM   3002  N  N     . LYS A 1 1829 ? 171.299 164.386 110.929 1.00 35.70  ? 1829 LYS A N     1 
ATOM   3003  C  CA    . LYS A 1 1829 ? 170.899 163.756 109.669 1.00 39.98  ? 1829 LYS A CA    1 
ATOM   3004  C  C     . LYS A 1 1829 ? 169.560 163.035 109.813 1.00 38.82  ? 1829 LYS A C     1 
ATOM   3005  O  O     . LYS A 1 1829 ? 169.404 161.874 109.428 1.00 41.27  ? 1829 LYS A O     1 
ATOM   3006  C  CB    . LYS A 1 1829 ? 171.986 162.804 109.162 1.00 43.27  ? 1829 LYS A CB    1 
ATOM   3007  C  CG    . LYS A 1 1829 ? 173.228 163.504 108.632 1.00 44.18  ? 1829 LYS A CG    1 
ATOM   3008  C  CD    . LYS A 1 1829 ? 173.400 163.286 107.136 1.00 46.39  ? 1829 LYS A CD    1 
ATOM   3009  C  CE    . LYS A 1 1829 ? 172.263 163.912 106.343 1.00 51.23  ? 1829 LYS A CE    1 
ATOM   3010  N  NZ    . LYS A 1 1829 ? 172.254 163.450 104.928 1.00 50.50  ? 1829 LYS A NZ    1 
ATOM   3011  N  N     . ILE A 1 1830 ? 168.586 163.737 110.384 1.00 37.23  ? 1830 ILE A N     1 
ATOM   3012  C  CA    . ILE A 1 1830 ? 167.261 163.170 110.603 1.00 34.42  ? 1830 ILE A CA    1 
ATOM   3013  C  C     . ILE A 1 1830 ? 166.470 163.240 109.304 1.00 39.53  ? 1830 ILE A C     1 
ATOM   3014  O  O     . ILE A 1 1830 ? 166.361 164.306 108.686 1.00 44.87  ? 1830 ILE A O     1 
ATOM   3015  C  CB    . ILE A 1 1830 ? 166.533 163.911 111.735 1.00 33.91  ? 1830 ILE A CB    1 
ATOM   3016  C  CG1   . ILE A 1 1830 ? 167.350 163.839 113.022 1.00 33.35  ? 1830 ILE A CG1   1 
ATOM   3017  C  CG2   . ILE A 1 1830 ? 165.161 163.307 111.966 1.00 31.25  ? 1830 ILE A CG2   1 
ATOM   3018  C  CD1   . ILE A 1 1830 ? 167.576 162.437 113.504 1.00 35.16  ? 1830 ILE A CD1   1 
ATOM   3019  N  N     . ASP A 1 1831 ? 165.917 162.102 108.885 1.00 43.95  ? 1831 ASP A N     1 
ATOM   3020  C  CA    . ASP A 1 1831 ? 165.113 162.033 107.676 1.00 43.91  ? 1831 ASP A CA    1 
ATOM   3021  C  C     . ASP A 1 1831 ? 163.728 161.441 107.892 1.00 40.54  ? 1831 ASP A C     1 
ATOM   3022  O  O     . ASP A 1 1831 ? 162.907 161.489 106.970 1.00 48.53  ? 1831 ASP A O     1 
ATOM   3023  C  CB    . ASP A 1 1831 ? 165.838 161.216 106.594 1.00 44.84  ? 1831 ASP A CB    1 
ATOM   3024  C  CG    . ASP A 1 1831 ? 166.287 159.857 107.093 1.00 50.28  ? 1831 ASP A CG    1 
ATOM   3025  O  OD1   . ASP A 1 1831 ? 166.158 159.595 108.307 1.00 52.08  ? 1831 ASP A OD1   1 
ATOM   3026  O  OD2   . ASP A 1 1831 ? 166.767 159.050 106.270 1.00 60.07  ? 1831 ASP A OD2   1 
ATOM   3027  N  N     . ASN A 1 1832 ? 163.443 160.892 109.069 1.00 36.22  ? 1832 ASN A N     1 
ATOM   3028  C  CA    . ASN A 1 1832 ? 162.162 160.266 109.361 1.00 33.25  ? 1832 ASN A CA    1 
ATOM   3029  C  C     . ASN A 1 1832 ? 161.439 161.060 110.440 1.00 32.06  ? 1832 ASN A C     1 
ATOM   3030  O  O     . ASN A 1 1832 ? 162.047 161.446 111.444 1.00 31.40  ? 1832 ASN A O     1 
ATOM   3031  C  CB    . ASN A 1 1832 ? 162.352 158.817 109.811 1.00 32.92  ? 1832 ASN A CB    1 
ATOM   3032  C  CG    . ASN A 1 1832 ? 161.058 158.033 109.808 1.00 37.12  ? 1832 ASN A CG    1 
ATOM   3033  O  OD1   . ASN A 1 1832 ? 160.134 158.341 109.055 1.00 39.71  ? 1832 ASN A OD1   1 
ATOM   3034  N  ND2   . ASN A 1 1832 ? 160.984 157.010 110.651 1.00 36.38  ? 1832 ASN A ND2   1 
ATOM   3035  N  N     . ALA A 1 1833 ? 160.144 161.299 110.229 1.00 29.08  ? 1833 ALA A N     1 
ATOM   3036  C  CA    . ALA A 1 1833 ? 159.333 161.994 111.220 1.00 26.93  ? 1833 ALA A CA    1 
ATOM   3037  C  C     . ALA A 1 1833 ? 159.070 161.151 112.460 1.00 29.71  ? 1833 ALA A C     1 
ATOM   3038  O  O     . ALA A 1 1833 ? 158.650 161.703 113.484 1.00 30.85  ? 1833 ALA A O     1 
ATOM   3039  C  CB    . ALA A 1 1833 ? 158.005 162.429 110.601 1.00 28.29  ? 1833 ALA A CB    1 
ATOM   3040  N  N     . LYS A 1 1834 ? 159.301 159.843 112.397 1.00 29.03  ? 1834 LYS A N     1 
ATOM   3041  C  CA    . LYS A 1 1834 ? 159.121 158.958 113.539 1.00 23.83  ? 1834 LYS A CA    1 
ATOM   3042  C  C     . LYS A 1 1834 ? 160.406 158.732 114.323 1.00 20.38  ? 1834 LYS A C     1 
ATOM   3043  O  O     . LYS A 1 1834 ? 160.410 157.920 115.254 1.00 24.11  ? 1834 LYS A O     1 
ATOM   3044  C  CB    . LYS A 1 1834 ? 158.555 157.611 113.080 1.00 28.19  ? 1834 LYS A CB    1 
ATOM   3045  C  CG    . LYS A 1 1834 ? 157.334 157.726 112.184 1.00 36.26  ? 1834 LYS A CG    1 
ATOM   3046  C  CD    . LYS A 1 1834 ? 156.186 158.401 112.914 1.00 33.56  ? 1834 LYS A CD    1 
ATOM   3047  C  CE    . LYS A 1 1834 ? 155.653 157.526 114.037 1.00 37.43  ? 1834 LYS A CE    1 
ATOM   3048  N  NZ    . LYS A 1 1834 ? 154.476 158.142 114.708 1.00 41.53  ? 1834 LYS A NZ    1 
ATOM   3049  N  N     . SER A 1 1835 ? 161.493 159.410 113.965 1.00 21.10  ? 1835 SER A N     1 
ATOM   3050  C  CA    . SER A 1 1835 ? 162.725 159.299 114.731 1.00 20.83  ? 1835 SER A CA    1 
ATOM   3051  C  C     . SER A 1 1835 ? 162.551 159.940 116.101 1.00 17.28  ? 1835 SER A C     1 
ATOM   3052  O  O     . SER A 1 1835 ? 161.926 160.996 116.235 1.00 19.35  ? 1835 SER A O     1 
ATOM   3053  C  CB    . SER A 1 1835 ? 163.882 159.959 113.984 1.00 23.25  ? 1835 SER A CB    1 
ATOM   3054  O  OG    . SER A 1 1835 ? 165.048 159.999 114.787 1.00 23.68  ? 1835 SER A OG    1 
ATOM   3055  N  N     . PHE A 1 1836 ? 163.105 159.290 117.127 1.00 19.81  ? 1836 PHE A N     1 
ATOM   3056  C  CA    . PHE A 1 1836 ? 162.973 159.801 118.485 1.00 16.09  ? 1836 PHE A CA    1 
ATOM   3057  C  C     . PHE A 1 1836 ? 163.666 161.142 118.676 1.00 15.13  ? 1836 PHE A C     1 
ATOM   3058  O  O     . PHE A 1 1836 ? 163.263 161.912 119.552 1.00 13.41  ? 1836 PHE A O     1 
ATOM   3059  C  CB    . PHE A 1 1836 ? 163.518 158.790 119.492 1.00 14.88  ? 1836 PHE A CB    1 
ATOM   3060  C  CG    . PHE A 1 1836 ? 163.104 159.070 120.905 1.00 13.28  ? 1836 PHE A CG    1 
ATOM   3061  C  CD1   . PHE A 1 1836 ? 161.810 158.812 121.323 1.00 12.87  ? 1836 PHE A CD1   1 
ATOM   3062  C  CD2   . PHE A 1 1836 ? 164.004 159.598 121.813 1.00 11.23  ? 1836 PHE A CD2   1 
ATOM   3063  C  CE1   . PHE A 1 1836 ? 161.423 159.071 122.621 1.00 13.08  ? 1836 PHE A CE1   1 
ATOM   3064  C  CE2   . PHE A 1 1836 ? 163.623 159.859 123.113 1.00 11.61  ? 1836 PHE A CE2   1 
ATOM   3065  C  CZ    . PHE A 1 1836 ? 162.331 159.595 123.517 1.00 13.13  ? 1836 PHE A CZ    1 
ATOM   3066  N  N     . GLU A 1 1837 ? 164.692 161.443 117.877 1.00 18.63  ? 1837 GLU A N     1 
ATOM   3067  C  CA    . GLU A 1 1837 ? 165.330 162.751 117.967 1.00 20.50  ? 1837 GLU A CA    1 
ATOM   3068  C  C     . GLU A 1 1837 ? 164.382 163.867 117.545 1.00 24.89  ? 1837 GLU A C     1 
ATOM   3069  O  O     . GLU A 1 1837 ? 164.639 165.042 117.832 1.00 28.65  ? 1837 GLU A O     1 
ATOM   3070  C  CB    . GLU A 1 1837 ? 166.611 162.759 117.133 1.00 19.11  ? 1837 GLU A CB    1 
ATOM   3071  C  CG    . GLU A 1 1837 ? 167.676 161.818 117.686 1.00 30.32  ? 1837 GLU A CG    1 
ATOM   3072  C  CD    . GLU A 1 1837 ? 167.737 160.488 116.958 1.00 43.38  ? 1837 GLU A CD    1 
ATOM   3073  O  OE1   . GLU A 1 1837 ? 167.329 159.469 117.554 1.00 44.12  ? 1837 GLU A OE1   1 
ATOM   3074  O  OE2   . GLU A 1 1837 ? 168.207 160.450 115.804 1.00 43.72  ? 1837 GLU A OE2   1 
ATOM   3075  N  N     . TRP A 1 1838 ? 163.287 163.523 116.868 1.00 18.84  ? 1838 TRP A N     1 
ATOM   3076  C  CA    . TRP A 1 1838 ? 162.187 164.449 116.637 1.00 11.98  ? 1838 TRP A CA    1 
ATOM   3077  C  C     . TRP A 1 1838 ? 161.015 164.224 117.580 1.00 15.57  ? 1838 TRP A C     1 
ATOM   3078  O  O     . TRP A 1 1838 ? 160.357 165.193 117.973 1.00 15.17  ? 1838 TRP A O     1 
ATOM   3079  C  CB    . TRP A 1 1838 ? 161.695 164.344 115.188 1.00 15.48  ? 1838 TRP A CB    1 
ATOM   3080  C  CG    . TRP A 1 1838 ? 160.446 165.133 114.901 1.00 13.78  ? 1838 TRP A CG    1 
ATOM   3081  C  CD1   . TRP A 1 1838 ? 159.277 164.651 114.387 1.00 15.02  ? 1838 TRP A CD1   1 
ATOM   3082  C  CD2   . TRP A 1 1838 ? 160.240 166.536 115.114 1.00 10.64  ? 1838 TRP A CD2   1 
ATOM   3083  N  NE1   . TRP A 1 1838 ? 158.359 165.664 114.263 1.00 13.50  ? 1838 TRP A NE1   1 
ATOM   3084  C  CE2   . TRP A 1 1838 ? 158.925 166.832 114.702 1.00 11.15  ? 1838 TRP A CE2   1 
ATOM   3085  C  CE3   . TRP A 1 1838 ? 161.040 167.570 115.609 1.00 12.31  ? 1838 TRP A CE3   1 
ATOM   3086  C  CZ2   . TRP A 1 1838 ? 158.392 168.116 114.774 1.00 14.15  ? 1838 TRP A CZ2   1 
ATOM   3087  C  CZ3   . TRP A 1 1838 ? 160.508 168.844 115.679 1.00 11.43  ? 1838 TRP A CZ3   1 
ATOM   3088  C  CH2   . TRP A 1 1838 ? 159.197 169.106 115.264 1.00 11.56  ? 1838 TRP A CH2   1 
ATOM   3089  N  N     . LEU A 1 1839 ? 160.743 162.973 117.959 1.00 14.76  ? 1839 LEU A N     1 
ATOM   3090  C  CA    . LEU A 1 1839 ? 159.619 162.701 118.850 1.00 10.83  ? 1839 LEU A CA    1 
ATOM   3091  C  C     . LEU A 1 1839 ? 159.910 163.132 120.281 1.00 10.54  ? 1839 LEU A C     1 
ATOM   3092  O  O     . LEU A 1 1839 ? 158.980 163.470 121.021 1.00 16.53  ? 1839 LEU A O     1 
ATOM   3093  C  CB    . LEU A 1 1839 ? 159.253 161.218 118.808 1.00 11.41  ? 1839 LEU A CB    1 
ATOM   3094  C  CG    . LEU A 1 1839 ? 158.699 160.701 117.481 1.00 13.36  ? 1839 LEU A CG    1 
ATOM   3095  C  CD1   . LEU A 1 1839 ? 158.496 159.197 117.535 1.00 15.92  ? 1839 LEU A CD1   1 
ATOM   3096  C  CD2   . LEU A 1 1839 ? 157.401 161.408 117.131 1.00 15.31  ? 1839 LEU A CD2   1 
ATOM   3097  N  N     . SER A 1 1840 ? 161.179 163.131 120.691 1.00 10.69  ? 1840 SER A N     1 
ATOM   3098  C  CA    . SER A 1 1840 ? 161.523 163.603 122.027 1.00 11.23  ? 1840 SER A CA    1 
ATOM   3099  C  C     . SER A 1 1840 ? 161.280 165.095 122.199 1.00 11.68  ? 1840 SER A C     1 
ATOM   3100  O  O     . SER A 1 1840 ? 161.157 165.557 123.338 1.00 14.70  ? 1840 SER A O     1 
ATOM   3101  C  CB    . SER A 1 1840 ? 162.983 163.278 122.347 1.00 12.27  ? 1840 SER A CB    1 
ATOM   3102  O  OG    . SER A 1 1840 ? 163.844 163.723 121.314 1.00 16.30  ? 1840 SER A OG    1 
ATOM   3103  N  N     . GLN A 1 1841 ? 161.207 165.850 121.108 1.00 12.99  ? 1841 GLN A N     1 
ATOM   3104  C  CA    . GLN A 1 1841 ? 160.876 167.261 121.183 1.00 11.72  ? 1841 GLN A CA    1 
ATOM   3105  C  C     . GLN A 1 1841 ? 159.383 167.435 121.448 1.00 11.23  ? 1841 GLN A C     1 
ATOM   3106  O  O     . GLN A 1 1841 ? 158.582 166.509 121.301 1.00 12.76  ? 1841 GLN A O     1 
ATOM   3107  C  CB    . GLN A 1 1841 ? 161.272 167.975 119.891 1.00 10.75  ? 1841 GLN A CB    1 
ATOM   3108  C  CG    . GLN A 1 1841 ? 162.692 167.689 119.432 1.00 16.68  ? 1841 GLN A CG    1 
ATOM   3109  C  CD    . GLN A 1 1841 ? 163.733 168.152 120.431 1.00 18.77  ? 1841 GLN A CD    1 
ATOM   3110  O  OE1   . GLN A 1 1841 ? 163.611 169.225 121.019 1.00 19.85  ? 1841 GLN A OE1   1 
ATOM   3111  N  NE2   . GLN A 1 1841 ? 164.762 167.338 120.633 1.00 17.58  ? 1841 GLN A NE2   1 
ATOM   3112  N  N     . MET A 1 1842 ? 159.011 168.646 121.849 1.00 9.56   ? 1842 MET A N     1 
ATOM   3113  C  CA    . MET A 1 1842 ? 157.613 168.986 122.079 1.00 6.94   ? 1842 MET A CA    1 
ATOM   3114  C  C     . MET A 1 1842 ? 157.043 169.581 120.798 1.00 8.82   ? 1842 MET A C     1 
ATOM   3115  O  O     . MET A 1 1842 ? 157.489 170.638 120.340 1.00 10.34  ? 1842 MET A O     1 
ATOM   3116  C  CB    . MET A 1 1842 ? 157.476 169.948 123.254 1.00 6.92   ? 1842 MET A CB    1 
ATOM   3117  C  CG    . MET A 1 1842 ? 156.072 170.469 123.449 1.00 9.26   ? 1842 MET A CG    1 
ATOM   3118  S  SD    . MET A 1 1842 ? 155.604 170.417 125.181 1.00 32.50  ? 1842 MET A SD    1 
ATOM   3119  C  CE    . MET A 1 1842 ? 156.485 171.849 125.773 1.00 13.23  ? 1842 MET A CE    1 
ATOM   3120  N  N     . ARG A 1 1843 ? 156.053 168.903 120.226 1.00 9.48   ? 1843 ARG A N     1 
ATOM   3121  C  CA    . ARG A 1 1843 ? 155.523 169.223 118.910 1.00 8.12   ? 1843 ARG A CA    1 
ATOM   3122  C  C     . ARG A 1 1843 ? 154.059 169.618 119.022 1.00 10.73  ? 1843 ARG A C     1 
ATOM   3123  O  O     . ARG A 1 1843 ? 153.329 169.105 119.876 1.00 9.17   ? 1843 ARG A O     1 
ATOM   3124  C  CB    . ARG A 1 1843 ? 155.691 168.032 117.968 1.00 13.01  ? 1843 ARG A CB    1 
ATOM   3125  C  CG    . ARG A 1 1843 ? 156.958 167.242 118.251 1.00 11.28  ? 1843 ARG A CG    1 
ATOM   3126  C  CD    . ARG A 1 1843 ? 157.031 165.959 117.450 1.00 11.55  ? 1843 ARG A CD    1 
ATOM   3127  N  NE    . ARG A 1 1843 ? 155.946 165.042 117.776 1.00 14.47  ? 1843 ARG A NE    1 
ATOM   3128  C  CZ    . ARG A 1 1843 ? 155.911 164.276 118.858 1.00 13.19  ? 1843 ARG A CZ    1 
ATOM   3129  N  NH1   . ARG A 1 1843 ? 156.870 164.319 119.767 1.00 9.76   ? 1843 ARG A NH1   1 
ATOM   3130  N  NH2   . ARG A 1 1843 ? 154.886 163.447 119.032 1.00 14.60  ? 1843 ARG A NH2   1 
ATOM   3131  N  N     . PHE A 1 1844 ? 153.638 170.534 118.155 1.00 18.56  ? 1844 PHE A N     1 
ATOM   3132  C  CA    . PHE A 1 1844 ? 152.316 171.142 118.219 1.00 11.89  ? 1844 PHE A CA    1 
ATOM   3133  C  C     . PHE A 1 1844 ? 151.578 170.859 116.919 1.00 13.31  ? 1844 PHE A C     1 
ATOM   3134  O  O     . PHE A 1 1844 ? 152.018 171.288 115.847 1.00 18.73  ? 1844 PHE A O     1 
ATOM   3135  C  CB    . PHE A 1 1844 ? 152.427 172.648 118.465 1.00 9.06   ? 1844 PHE A CB    1 
ATOM   3136  C  CG    . PHE A 1 1844 ? 153.194 173.002 119.708 1.00 8.44   ? 1844 PHE A CG    1 
ATOM   3137  C  CD1   . PHE A 1 1844 ? 154.578 172.944 119.728 1.00 8.94   ? 1844 PHE A CD1   1 
ATOM   3138  C  CD2   . PHE A 1 1844 ? 152.532 173.386 120.859 1.00 7.42   ? 1844 PHE A CD2   1 
ATOM   3139  C  CE1   . PHE A 1 1844 ? 155.283 173.258 120.868 1.00 9.90   ? 1844 PHE A CE1   1 
ATOM   3140  C  CE2   . PHE A 1 1844 ? 153.231 173.704 122.004 1.00 7.79   ? 1844 PHE A CE2   1 
ATOM   3141  C  CZ    . PHE A 1 1844 ? 154.609 173.640 122.007 1.00 11.03  ? 1844 PHE A CZ    1 
ATOM   3142  N  N     . TYR A 1 1845 ? 150.458 170.149 117.015 1.00 15.83  ? 1845 TYR A N     1 
ATOM   3143  C  CA    . TYR A 1 1845 ? 149.668 169.759 115.855 1.00 17.76  ? 1845 TYR A CA    1 
ATOM   3144  C  C     . TYR A 1 1845 ? 148.303 170.425 115.924 1.00 20.13  ? 1845 TYR A C     1 
ATOM   3145  O  O     . TYR A 1 1845 ? 147.633 170.373 116.961 1.00 22.06  ? 1845 TYR A O     1 
ATOM   3146  C  CB    . TYR A 1 1845 ? 149.517 168.238 115.779 1.00 14.97  ? 1845 TYR A CB    1 
ATOM   3147  C  CG    . TYR A 1 1845 ? 150.835 167.503 115.703 1.00 23.10  ? 1845 TYR A CG    1 
ATOM   3148  C  CD1   . TYR A 1 1845 ? 151.784 167.839 114.747 1.00 27.18  ? 1845 TYR A CD1   1 
ATOM   3149  C  CD2   . TYR A 1 1845 ? 151.133 166.479 116.590 1.00 23.87  ? 1845 TYR A CD2   1 
ATOM   3150  C  CE1   . TYR A 1 1845 ? 152.991 167.173 114.674 1.00 26.51  ? 1845 TYR A CE1   1 
ATOM   3151  C  CE2   . TYR A 1 1845 ? 152.338 165.808 116.526 1.00 20.98  ? 1845 TYR A CE2   1 
ATOM   3152  C  CZ    . TYR A 1 1845 ? 153.263 166.159 115.566 1.00 24.13  ? 1845 TYR A CZ    1 
ATOM   3153  O  OH    . TYR A 1 1845 ? 154.464 165.493 115.497 1.00 25.09  ? 1845 TYR A OH    1 
ATOM   3154  N  N     . PHE A 1 1846 ? 147.895 171.043 114.820 1.00 18.13  ? 1846 PHE A N     1 
ATOM   3155  C  CA    . PHE A 1 1846 ? 146.616 171.732 114.722 1.00 20.86  ? 1846 PHE A CA    1 
ATOM   3156  C  C     . PHE A 1 1846 ? 145.734 171.020 113.707 1.00 29.41  ? 1846 PHE A C     1 
ATOM   3157  O  O     . PHE A 1 1846 ? 146.189 170.685 112.609 1.00 30.17  ? 1846 PHE A O     1 
ATOM   3158  C  CB    . PHE A 1 1846 ? 146.813 173.195 114.322 1.00 23.09  ? 1846 PHE A CB    1 
ATOM   3159  C  CG    . PHE A 1 1846 ? 145.665 174.084 114.699 1.00 22.64  ? 1846 PHE A CG    1 
ATOM   3160  C  CD1   . PHE A 1 1846 ? 145.374 174.334 116.029 1.00 23.44  ? 1846 PHE A CD1   1 
ATOM   3161  C  CD2   . PHE A 1 1846 ? 144.879 174.672 113.723 1.00 25.43  ? 1846 PHE A CD2   1 
ATOM   3162  C  CE1   . PHE A 1 1846 ? 144.318 175.152 116.379 1.00 27.28  ? 1846 PHE A CE1   1 
ATOM   3163  C  CE2   . PHE A 1 1846 ? 143.822 175.491 114.066 1.00 29.44  ? 1846 PHE A CE2   1 
ATOM   3164  C  CZ    . PHE A 1 1846 ? 143.541 175.731 115.396 1.00 30.63  ? 1846 PHE A CZ    1 
ATOM   3165  N  N     . ASP A 1 1847 ? 144.474 170.789 114.079 1.00 29.77  ? 1847 ASP A N     1 
ATOM   3166  C  CA    . ASP A 1 1847 ? 143.488 170.138 113.217 1.00 32.77  ? 1847 ASP A CA    1 
ATOM   3167  C  C     . ASP A 1 1847 ? 142.292 171.068 113.066 1.00 39.16  ? 1847 ASP A C     1 
ATOM   3168  O  O     . ASP A 1 1847 ? 141.345 171.013 113.866 1.00 44.58  ? 1847 ASP A O     1 
ATOM   3169  C  CB    . ASP A 1 1847 ? 143.064 168.786 113.787 1.00 34.69  ? 1847 ASP A CB    1 
ATOM   3170  C  CG    . ASP A 1 1847 ? 142.321 167.937 112.776 1.00 41.94  ? 1847 ASP A CG    1 
ATOM   3171  O  OD1   . ASP A 1 1847 ? 142.265 168.332 111.593 1.00 46.05  ? 1847 ASP A OD1   1 
ATOM   3172  O  OD2   . ASP A 1 1847 ? 141.791 166.875 113.165 1.00 44.17  ? 1847 ASP A OD2   1 
ATOM   3173  N  N     . PRO A 1 1848 ? 142.294 171.944 112.058 1.00 38.21  ? 1848 PRO A N     1 
ATOM   3174  C  CA    . PRO A 1 1848 ? 141.146 172.845 111.866 1.00 41.38  ? 1848 PRO A CA    1 
ATOM   3175  C  C     . PRO A 1 1848 ? 139.850 172.124 111.541 1.00 42.67  ? 1848 PRO A C     1 
ATOM   3176  O  O     . PRO A 1 1848 ? 138.773 172.697 111.746 1.00 40.83  ? 1848 PRO A O     1 
ATOM   3177  C  CB    . PRO A 1 1848 ? 141.594 173.741 110.703 1.00 38.04  ? 1848 PRO A CB    1 
ATOM   3178  C  CG    . PRO A 1 1848 ? 142.622 172.935 109.981 1.00 32.72  ? 1848 PRO A CG    1 
ATOM   3179  C  CD    . PRO A 1 1848 ? 143.333 172.141 111.035 1.00 33.77  ? 1848 PRO A CD    1 
ATOM   3180  N  N     . LYS A 1 1849 ? 139.915 170.889 111.042 1.00 43.71  ? 1849 LYS A N     1 
ATOM   3181  C  CA    . LYS A 1 1849 ? 138.714 170.142 110.693 1.00 46.79  ? 1849 LYS A CA    1 
ATOM   3182  C  C     . LYS A 1 1849 ? 137.966 169.606 111.906 1.00 46.95  ? 1849 LYS A C     1 
ATOM   3183  O  O     . LYS A 1 1849 ? 136.833 169.136 111.752 1.00 55.56  ? 1849 LYS A O     1 
ATOM   3184  C  CB    . LYS A 1 1849 ? 139.071 168.979 109.764 1.00 45.97  ? 1849 LYS A CB    1 
ATOM   3185  C  CG    . LYS A 1 1849 ? 139.764 169.395 108.479 1.00 49.04  ? 1849 LYS A CG    1 
ATOM   3186  C  CD    . LYS A 1 1849 ? 139.356 168.491 107.327 1.00 52.36  ? 1849 LYS A CD    1 
ATOM   3187  C  CE    . LYS A 1 1849 ? 140.562 168.043 106.518 1.00 49.28  ? 1849 LYS A CE    1 
ATOM   3188  N  NZ    . LYS A 1 1849 ? 140.762 168.884 105.306 1.00 53.27  ? 1849 LYS A NZ    1 
ATOM   3189  N  N     . GLN A 1 1850 ? 138.561 169.657 113.095 1.00 42.40  ? 1850 GLN A N     1 
ATOM   3190  C  CA    . GLN A 1 1850 ? 137.891 169.160 114.289 1.00 42.27  ? 1850 GLN A CA    1 
ATOM   3191  C  C     . GLN A 1 1850 ? 136.783 170.118 114.708 1.00 48.26  ? 1850 GLN A C     1 
ATOM   3192  O  O     . GLN A 1 1850 ? 136.995 171.332 114.793 1.00 49.88  ? 1850 GLN A O     1 
ATOM   3193  C  CB    . GLN A 1 1850 ? 138.896 168.976 115.425 1.00 40.81  ? 1850 GLN A CB    1 
ATOM   3194  C  CG    . GLN A 1 1850 ? 138.282 168.457 116.714 1.00 41.21  ? 1850 GLN A CG    1 
ATOM   3195  C  CD    . GLN A 1 1850 ? 138.875 167.130 117.146 1.00 41.48  ? 1850 GLN A CD    1 
ATOM   3196  O  OE1   . GLN A 1 1850 ? 139.674 166.531 116.426 1.00 43.80  ? 1850 GLN A OE1   1 
ATOM   3197  N  NE2   . GLN A 1 1850 ? 138.473 166.656 118.318 1.00 40.13  ? 1850 GLN A NE2   1 
ATOM   3198  N  N     . THR A 1 1851 ? 135.596 169.567 114.972 1.00 48.95  ? 1851 THR A N     1 
ATOM   3199  C  CA    . THR A 1 1851 ? 134.449 170.400 115.323 1.00 48.91  ? 1851 THR A CA    1 
ATOM   3200  C  C     . THR A 1 1851 ? 134.646 171.087 116.668 1.00 48.66  ? 1851 THR A C     1 
ATOM   3201  O  O     . THR A 1 1851 ? 134.323 172.271 116.820 1.00 44.69  ? 1851 THR A O     1 
ATOM   3202  C  CB    . THR A 1 1851 ? 133.175 169.558 115.339 1.00 49.30  ? 1851 THR A CB    1 
ATOM   3203  O  OG1   . THR A 1 1851 ? 133.474 168.249 115.842 1.00 55.53  ? 1851 THR A OG1   1 
ATOM   3204  C  CG2   . THR A 1 1851 ? 132.603 169.437 113.936 1.00 46.65  ? 1851 THR A CG2   1 
ATOM   3205  N  N     . ASP A 1 1852 ? 135.166 170.364 117.657 1.00 46.38  ? 1852 ASP A N     1 
ATOM   3206  C  CA    . ASP A 1 1852 ? 135.403 170.928 118.981 1.00 42.30  ? 1852 ASP A CA    1 
ATOM   3207  C  C     . ASP A 1 1852 ? 136.629 171.829 118.918 1.00 43.41  ? 1852 ASP A C     1 
ATOM   3208  O  O     . ASP A 1 1852 ? 137.746 171.356 118.683 1.00 46.16  ? 1852 ASP A O     1 
ATOM   3209  C  CB    . ASP A 1 1852 ? 135.585 169.818 120.011 1.00 39.52  ? 1852 ASP A CB    1 
ATOM   3210  C  CG    . ASP A 1 1852 ? 135.479 170.323 121.437 1.00 45.00  ? 1852 ASP A CG    1 
ATOM   3211  O  OD1   . ASP A 1 1852 ? 135.167 171.517 121.625 1.00 50.53  ? 1852 ASP A OD1   1 
ATOM   3212  O  OD2   . ASP A 1 1852 ? 135.702 169.524 122.369 1.00 44.57  ? 1852 ASP A OD2   1 
ATOM   3213  N  N     . VAL A 1 1853 ? 136.422 173.132 119.128 1.00 39.94  ? 1853 VAL A N     1 
ATOM   3214  C  CA    . VAL A 1 1853 ? 137.528 174.083 119.059 1.00 35.95  ? 1853 VAL A CA    1 
ATOM   3215  C  C     . VAL A 1 1853 ? 138.534 173.832 120.174 1.00 34.33  ? 1853 VAL A C     1 
ATOM   3216  O  O     . VAL A 1 1853 ? 139.732 174.094 120.008 1.00 36.43  ? 1853 VAL A O     1 
ATOM   3217  C  CB    . VAL A 1 1853 ? 136.993 175.529 119.083 1.00 35.45  ? 1853 VAL A CB    1 
ATOM   3218  C  CG1   . VAL A 1 1853 ? 135.964 175.724 117.983 1.00 38.14  ? 1853 VAL A CG1   1 
ATOM   3219  C  CG2   . VAL A 1 1853 ? 136.390 175.863 120.438 1.00 33.49  ? 1853 VAL A CG2   1 
ATOM   3220  N  N     . LEU A 1 1854 ? 138.077 173.325 121.320 1.00 32.22  ? 1854 LEU A N     1 
ATOM   3221  C  CA    . LEU A 1 1854 ? 138.980 173.031 122.425 1.00 26.70  ? 1854 LEU A CA    1 
ATOM   3222  C  C     . LEU A 1 1854 ? 139.848 171.808 122.169 1.00 30.65  ? 1854 LEU A C     1 
ATOM   3223  O  O     . LEU A 1 1854 ? 140.783 171.563 122.938 1.00 35.91  ? 1854 LEU A O     1 
ATOM   3224  C  CB    . LEU A 1 1854 ? 138.183 172.835 123.716 1.00 26.23  ? 1854 LEU A CB    1 
ATOM   3225  C  CG    . LEU A 1 1854 ? 137.390 174.043 124.218 1.00 25.29  ? 1854 LEU A CG    1 
ATOM   3226  C  CD1   . LEU A 1 1854 ? 136.973 173.846 125.665 1.00 17.20  ? 1854 LEU A CD1   1 
ATOM   3227  C  CD2   . LEU A 1 1854 ? 138.195 175.323 124.059 1.00 19.58  ? 1854 LEU A CD2   1 
ATOM   3228  N  N     . GLN A 1 1855 ? 139.564 171.039 121.118 1.00 32.03  ? 1855 GLN A N     1 
ATOM   3229  C  CA    . GLN A 1 1855 ? 140.331 169.848 120.780 1.00 28.03  ? 1855 GLN A CA    1 
ATOM   3230  C  C     . GLN A 1 1855 ? 141.109 170.001 119.480 1.00 28.92  ? 1855 GLN A C     1 
ATOM   3231  O  O     . GLN A 1 1855 ? 141.725 169.034 119.020 1.00 29.90  ? 1855 GLN A O     1 
ATOM   3232  C  CB    . GLN A 1 1855 ? 139.402 168.635 120.690 1.00 31.00  ? 1855 GLN A CB    1 
ATOM   3233  C  CG    . GLN A 1 1855 ? 138.761 168.233 122.008 1.00 32.70  ? 1855 GLN A CG    1 
ATOM   3234  C  CD    . GLN A 1 1855 ? 139.772 168.076 123.125 1.00 38.57  ? 1855 GLN A CD    1 
ATOM   3235  O  OE1   . GLN A 1 1855 ? 140.715 167.293 123.018 1.00 39.06  ? 1855 GLN A OE1   1 
ATOM   3236  N  NE2   . GLN A 1 1855 ? 139.578 168.820 124.208 1.00 35.43  ? 1855 GLN A NE2   1 
ATOM   3237  N  N     . GLN A 1 1856 ? 141.099 171.192 118.875 1.00 29.01  ? 1856 GLN A N     1 
ATOM   3238  C  CA    . GLN A 1 1856 ? 141.766 171.372 117.590 1.00 28.24  ? 1856 GLN A CA    1 
ATOM   3239  C  C     . GLN A 1 1856 ? 143.282 171.340 117.724 1.00 25.54  ? 1856 GLN A C     1 
ATOM   3240  O  O     . GLN A 1 1856 ? 143.981 171.035 116.751 1.00 28.60  ? 1856 GLN A O     1 
ATOM   3241  C  CB    . GLN A 1 1856 ? 141.330 172.687 116.944 1.00 28.06  ? 1856 GLN A CB    1 
ATOM   3242  C  CG    . GLN A 1 1856 ? 139.859 172.751 116.578 1.00 34.73  ? 1856 GLN A CG    1 
ATOM   3243  C  CD    . GLN A 1 1856 ? 139.560 173.858 115.585 1.00 41.16  ? 1856 GLN A CD    1 
ATOM   3244  O  OE1   . GLN A 1 1856 ? 140.053 174.978 115.720 1.00 39.57  ? 1856 GLN A OE1   1 
ATOM   3245  N  NE2   . GLN A 1 1856 ? 138.746 173.550 114.582 1.00 40.13  ? 1856 GLN A NE2   1 
ATOM   3246  N  N     . LEU A 1 1857 ? 143.807 171.647 118.905 1.00 22.02  ? 1857 LEU A N     1 
ATOM   3247  C  CA    . LEU A 1 1857 ? 145.243 171.715 119.134 1.00 15.99  ? 1857 LEU A CA    1 
ATOM   3248  C  C     . LEU A 1 1857 ? 145.664 170.593 120.071 1.00 18.86  ? 1857 LEU A C     1 
ATOM   3249  O  O     . LEU A 1 1857 ? 145.052 170.394 121.126 1.00 19.10  ? 1857 LEU A O     1 
ATOM   3250  C  CB    . LEU A 1 1857 ? 145.635 173.072 119.719 1.00 16.97  ? 1857 LEU A CB    1 
ATOM   3251  C  CG    . LEU A 1 1857 ? 147.067 173.189 120.236 1.00 13.33  ? 1857 LEU A CG    1 
ATOM   3252  C  CD1   . LEU A 1 1857 ? 148.062 173.019 119.100 1.00 13.11  ? 1857 LEU A CD1   1 
ATOM   3253  C  CD2   . LEU A 1 1857 ? 147.280 174.512 120.946 1.00 12.27  ? 1857 LEU A CD2   1 
ATOM   3254  N  N     . SER A 1 1858 ? 146.705 169.861 119.682 1.00 20.33  ? 1858 SER A N     1 
ATOM   3255  C  CA    . SER A 1 1858 ? 147.251 168.774 120.480 1.00 14.55  ? 1858 SER A CA    1 
ATOM   3256  C  C     . SER A 1 1858 ? 148.740 169.001 120.691 1.00 15.51  ? 1858 SER A C     1 
ATOM   3257  O  O     . SER A 1 1858 ? 149.474 169.280 119.739 1.00 19.01  ? 1858 SER A O     1 
ATOM   3258  C  CB    . SER A 1 1858 ? 147.019 167.418 119.807 1.00 17.45  ? 1858 SER A CB    1 
ATOM   3259  O  OG    . SER A 1 1858 ? 147.499 166.359 120.616 1.00 24.22  ? 1858 SER A OG    1 
ATOM   3260  N  N     . ILE A 1 1859 ? 149.181 168.880 121.940 1.00 15.74  ? 1859 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 1859 ? 150.589 169.017 122.300 1.00 9.39   ? 1859 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 1859 ? 151.125 167.620 122.572 1.00 9.43   ? 1859 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 1859 ? 150.602 166.908 123.438 1.00 12.59  ? 1859 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 1859 ? 150.800 169.924 123.525 1.00 9.09   ? 1859 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 1859 ? 149.858 171.135 123.527 1.00 9.15   ? 1859 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 1859 ? 152.245 170.397 123.583 1.00 11.43  ? 1859 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 1859 ? 149.764 171.880 122.217 1.00 12.32  ? 1859 ILE A CD1   1 
ATOM   3268  N  N     . GLN A 1 1860 ? 152.160 167.229 121.836 1.00 11.49  ? 1860 GLN A N     1 
ATOM   3269  C  CA    . GLN A 1 1860 ? 152.758 165.911 121.969 1.00 10.10  ? 1860 GLN A CA    1 
ATOM   3270  C  C     . GLN A 1 1860 ? 154.243 166.035 122.276 1.00 8.16   ? 1860 GLN A C     1 
ATOM   3271  O  O     . GLN A 1 1860 ? 154.937 166.887 121.712 1.00 10.48  ? 1860 GLN A O     1 
ATOM   3272  C  CB    . GLN A 1 1860 ? 152.559 165.079 120.699 1.00 11.81  ? 1860 GLN A CB    1 
ATOM   3273  C  CG    . GLN A 1 1860 ? 151.129 165.043 120.191 1.00 17.45  ? 1860 GLN A CG    1 
ATOM   3274  C  CD    . GLN A 1 1860 ? 150.911 163.960 119.155 1.00 25.23  ? 1860 GLN A CD    1 
ATOM   3275  O  OE1   . GLN A 1 1860 ? 151.819 163.190 118.845 1.00 24.74  ? 1860 GLN A OE1   1 
ATOM   3276  N  NE2   . GLN A 1 1860 ? 149.700 163.891 118.616 1.00 27.21  ? 1860 GLN A NE2   1 
ATOM   3277  N  N     . MET A 1 1861 ? 154.719 165.180 123.178 1.00 9.46   ? 1861 MET A N     1 
ATOM   3278  C  CA    . MET A 1 1861 ? 156.139 165.059 123.483 1.00 8.48   ? 1861 MET A CA    1 
ATOM   3279  C  C     . MET A 1 1861 ? 156.404 163.607 123.842 1.00 11.16  ? 1861 MET A C     1 
ATOM   3280  O  O     . MET A 1 1861 ? 155.832 163.096 124.809 1.00 16.42  ? 1861 MET A O     1 
ATOM   3281  C  CB    . MET A 1 1861 ? 156.549 165.990 124.627 1.00 8.16   ? 1861 MET A CB    1 
ATOM   3282  C  CG    . MET A 1 1861 ? 158.024 166.346 124.627 1.00 11.10  ? 1861 MET A CG    1 
ATOM   3283  S  SD    . MET A 1 1861 ? 158.451 167.568 125.878 1.00 14.36  ? 1861 MET A SD    1 
ATOM   3284  C  CE    . MET A 1 1861 ? 160.223 167.344 125.972 1.00 7.33   ? 1861 MET A CE    1 
ATOM   3285  N  N     . ALA A 1 1862 ? 157.263 162.949 123.061 1.00 12.55  ? 1862 ALA A N     1 
ATOM   3286  C  CA    . ALA A 1 1862 ? 157.496 161.503 123.144 1.00 11.74  ? 1862 ALA A CA    1 
ATOM   3287  C  C     . ALA A 1 1862 ? 156.158 160.816 122.902 1.00 14.35  ? 1862 ALA A C     1 
ATOM   3288  O  O     . ALA A 1 1862 ? 155.544 161.060 121.848 1.00 23.13  ? 1862 ALA A O     1 
ATOM   3289  C  CB    . ALA A 1 1862 ? 158.193 161.167 124.465 1.00 11.98  ? 1862 ALA A CB    1 
ATOM   3290  N  N     . ASN A 1 1863 ? 155.668 159.973 123.806 1.00 13.47  ? 1863 ASN A N     1 
ATOM   3291  C  CA    . ASN A 1 1863 ? 154.374 159.326 123.635 1.00 15.10  ? 1863 ASN A CA    1 
ATOM   3292  C  C     . ASN A 1 1863 ? 153.253 160.040 124.377 1.00 18.06  ? 1863 ASN A C     1 
ATOM   3293  O  O     . ASN A 1 1863 ? 152.114 159.563 124.358 1.00 23.28  ? 1863 ASN A O     1 
ATOM   3294  C  CB    . ASN A 1 1863 ? 154.447 157.867 124.098 1.00 17.60  ? 1863 ASN A CB    1 
ATOM   3295  C  CG    . ASN A 1 1863 ? 154.705 157.741 125.585 1.00 19.17  ? 1863 ASN A CG    1 
ATOM   3296  O  OD1   . ASN A 1 1863 ? 155.756 158.146 126.080 1.00 19.64  ? 1863 ASN A OD1   1 
ATOM   3297  N  ND2   . ASN A 1 1863 ? 153.745 157.176 126.306 1.00 20.75  ? 1863 ASN A ND2   1 
ATOM   3298  N  N     . ALA A 1 1864 ? 153.542 161.167 125.022 1.00 16.05  ? 1864 ALA A N     1 
ATOM   3299  C  CA    . ALA A 1 1864 ? 152.559 161.872 125.830 1.00 16.19  ? 1864 ALA A CA    1 
ATOM   3300  C  C     . ALA A 1 1864 ? 151.831 162.911 124.987 1.00 15.30  ? 1864 ALA A C     1 
ATOM   3301  O  O     . ALA A 1 1864 ? 152.465 163.754 124.345 1.00 12.41  ? 1864 ALA A O     1 
ATOM   3302  C  CB    . ALA A 1 1864 ? 153.231 162.539 127.030 1.00 16.20  ? 1864 ALA A CB    1 
ATOM   3303  N  N     . LYS A 1 1865 ? 150.502 162.849 124.998 1.00 20.17  ? 1865 LYS A N     1 
ATOM   3304  C  CA    . LYS A 1 1865 ? 149.656 163.783 124.270 1.00 13.56  ? 1865 LYS A CA    1 
ATOM   3305  C  C     . LYS A 1 1865 ? 148.845 164.607 125.258 1.00 12.52  ? 1865 LYS A C     1 
ATOM   3306  O  O     . LYS A 1 1865 ? 148.247 164.062 126.192 1.00 16.27  ? 1865 LYS A O     1 
ATOM   3307  C  CB    . LYS A 1 1865 ? 148.715 163.051 123.309 1.00 16.07  ? 1865 LYS A CB    1 
ATOM   3308  C  CG    . LYS A 1 1865 ? 149.421 162.249 122.231 1.00 21.49  ? 1865 LYS A CG    1 
ATOM   3309  C  CD    . LYS A 1 1865 ? 148.438 161.386 121.459 1.00 27.13  ? 1865 LYS A CD    1 
ATOM   3310  C  CE    . LYS A 1 1865 ? 149.140 160.575 120.383 1.00 31.53  ? 1865 LYS A CE    1 
ATOM   3311  N  NZ    . LYS A 1 1865 ? 150.147 159.643 120.960 1.00 22.89  ? 1865 LYS A NZ    1 
ATOM   3312  N  N     . PHE A 1 1866 ? 148.825 165.921 125.050 1.00 11.44  ? 1866 PHE A N     1 
ATOM   3313  C  CA    . PHE A 1 1866 ? 148.088 166.823 125.919 1.00 9.80   ? 1866 PHE A CA    1 
ATOM   3314  C  C     . PHE A 1 1866 ? 147.238 167.763 125.081 1.00 10.52  ? 1866 PHE A C     1 
ATOM   3315  O  O     . PHE A 1 1866 ? 147.605 168.134 123.963 1.00 12.02  ? 1866 PHE A O     1 
ATOM   3316  C  CB    . PHE A 1 1866 ? 149.022 167.640 126.820 1.00 9.15   ? 1866 PHE A CB    1 
ATOM   3317  C  CG    . PHE A 1 1866 ? 150.039 166.812 127.543 1.00 8.29   ? 1866 PHE A CG    1 
ATOM   3318  C  CD1   . PHE A 1 1866 ? 149.725 166.202 128.743 1.00 8.46   ? 1866 PHE A CD1   1 
ATOM   3319  C  CD2   . PHE A 1 1866 ? 151.311 166.649 127.025 1.00 12.41  ? 1866 PHE A CD2   1 
ATOM   3320  C  CE1   . PHE A 1 1866 ? 150.656 165.441 129.411 1.00 8.49   ? 1866 PHE A CE1   1 
ATOM   3321  C  CE2   . PHE A 1 1866 ? 152.248 165.889 127.690 1.00 11.12  ? 1866 PHE A CE2   1 
ATOM   3322  C  CZ    . PHE A 1 1866 ? 151.920 165.284 128.885 1.00 9.34   ? 1866 PHE A CZ    1 
ATOM   3323  N  N     . ASN A 1 1867 ? 146.092 168.140 125.637 1.00 12.63  ? 1867 ASN A N     1 
ATOM   3324  C  CA    . ASN A 1 1867 ? 145.218 169.137 125.041 1.00 11.64  ? 1867 ASN A CA    1 
ATOM   3325  C  C     . ASN A 1 1867 ? 145.451 170.475 125.727 1.00 11.12  ? 1867 ASN A C     1 
ATOM   3326  O  O     . ASN A 1 1867 ? 145.583 170.539 126.953 1.00 11.21  ? 1867 ASN A O     1 
ATOM   3327  C  CB    . ASN A 1 1867 ? 143.749 168.732 125.171 1.00 18.06  ? 1867 ASN A CB    1 
ATOM   3328  C  CG    . ASN A 1 1867 ? 143.407 167.509 124.345 1.00 31.81  ? 1867 ASN A CG    1 
ATOM   3329  O  OD1   . ASN A 1 1867 ? 142.607 166.671 124.760 1.00 32.86  ? 1867 ASN A OD1   1 
ATOM   3330  N  ND2   . ASN A 1 1867 ? 144.018 167.397 123.171 1.00 30.76  ? 1867 ASN A ND2   1 
ATOM   3331  N  N     . TYR A 1 1868 ? 145.520 171.538 124.930 1.00 8.42   ? 1868 TYR A N     1 
ATOM   3332  C  CA    . TYR A 1 1868 ? 145.678 172.870 125.494 1.00 5.85   ? 1868 TYR A CA    1 
ATOM   3333  C  C     . TYR A 1 1868 ? 144.474 173.215 126.358 1.00 6.70   ? 1868 TYR A C     1 
ATOM   3334  O  O     . TYR A 1 1868 ? 143.326 173.111 125.916 1.00 8.63   ? 1868 TYR A O     1 
ATOM   3335  C  CB    . TYR A 1 1868 ? 145.845 173.902 124.377 1.00 6.91   ? 1868 TYR A CB    1 
ATOM   3336  C  CG    . TYR A 1 1868 ? 146.592 175.148 124.797 1.00 4.24   ? 1868 TYR A CG    1 
ATOM   3337  C  CD1   . TYR A 1 1868 ? 147.964 175.128 124.992 1.00 4.37   ? 1868 TYR A CD1   1 
ATOM   3338  C  CD2   . TYR A 1 1868 ? 145.923 176.346 124.998 1.00 4.69   ? 1868 TYR A CD2   1 
ATOM   3339  C  CE1   . TYR A 1 1868 ? 148.647 176.266 125.376 1.00 3.75   ? 1868 TYR A CE1   1 
ATOM   3340  C  CE2   . TYR A 1 1868 ? 146.598 177.487 125.382 1.00 4.10   ? 1868 TYR A CE2   1 
ATOM   3341  C  CZ    . TYR A 1 1868 ? 147.959 177.441 125.570 1.00 3.17   ? 1868 TYR A CZ    1 
ATOM   3342  O  OH    . TYR A 1 1868 ? 148.637 178.576 125.952 1.00 3.53   ? 1868 TYR A OH    1 
ATOM   3343  N  N     . GLY A 1 1869 ? 144.739 173.625 127.599 1.00 6.02   ? 1869 GLY A N     1 
ATOM   3344  C  CA    . GLY A 1 1869 ? 143.660 173.987 128.499 1.00 8.45   ? 1869 GLY A CA    1 
ATOM   3345  C  C     . GLY A 1 1869 ? 142.954 175.269 128.120 1.00 10.26  ? 1869 GLY A C     1 
ATOM   3346  O  O     . GLY A 1 1869 ? 141.820 175.493 128.557 1.00 15.47  ? 1869 GLY A O     1 
ATOM   3347  N  N     . PHE A 1 1870 ? 143.604 176.114 127.318 1.00 6.97   ? 1870 PHE A N     1 
ATOM   3348  C  CA    . PHE A 1 1870 ? 143.047 177.390 126.873 1.00 7.97   ? 1870 PHE A CA    1 
ATOM   3349  C  C     . PHE A 1 1870 ? 142.669 178.284 128.048 1.00 10.98  ? 1870 PHE A C     1 
ATOM   3350  O  O     . PHE A 1 1870 ? 141.738 179.089 127.962 1.00 14.32  ? 1870 PHE A O     1 
ATOM   3351  C  CB    . PHE A 1 1870 ? 141.856 177.178 125.936 1.00 11.57  ? 1870 PHE A CB    1 
ATOM   3352  C  CG    . PHE A 1 1870 ? 142.253 176.722 124.564 1.00 10.74  ? 1870 PHE A CG    1 
ATOM   3353  C  CD1   . PHE A 1 1870 ? 142.997 177.546 123.738 1.00 7.79   ? 1870 PHE A CD1   1 
ATOM   3354  C  CD2   . PHE A 1 1870 ? 141.899 175.466 124.107 1.00 10.82  ? 1870 PHE A CD2   1 
ATOM   3355  C  CE1   . PHE A 1 1870 ? 143.371 177.130 122.479 1.00 7.48   ? 1870 PHE A CE1   1 
ATOM   3356  C  CE2   . PHE A 1 1870 ? 142.269 175.044 122.848 1.00 12.72  ? 1870 PHE A CE2   1 
ATOM   3357  C  CZ    . PHE A 1 1870 ? 143.006 175.877 122.032 1.00 10.98  ? 1870 PHE A CZ    1 
ATOM   3358  N  N     . GLU A 1 1871 ? 143.394 178.145 129.153 1.00 12.62  ? 1871 GLU A N     1 
ATOM   3359  C  CA    . GLU A 1 1871 ? 143.274 179.086 130.255 1.00 11.26  ? 1871 GLU A CA    1 
ATOM   3360  C  C     . GLU A 1 1871 ? 144.081 180.335 129.936 1.00 13.44  ? 1871 GLU A C     1 
ATOM   3361  O  O     . GLU A 1 1871 ? 145.269 180.251 129.612 1.00 18.18  ? 1871 GLU A O     1 
ATOM   3362  C  CB    . GLU A 1 1871 ? 143.767 178.446 131.552 1.00 12.79  ? 1871 GLU A CB    1 
ATOM   3363  C  CG    . GLU A 1 1871 ? 144.075 179.435 132.663 1.00 16.39  ? 1871 GLU A CG    1 
ATOM   3364  C  CD    . GLU A 1 1871 ? 142.831 179.911 133.382 1.00 23.03  ? 1871 GLU A CD    1 
ATOM   3365  O  OE1   . GLU A 1 1871 ? 141.799 179.212 133.316 1.00 31.58  ? 1871 GLU A OE1   1 
ATOM   3366  O  OE2   . GLU A 1 1871 ? 142.886 180.983 134.021 1.00 24.82  ? 1871 GLU A OE2   1 
ATOM   3367  N  N     . TYR A 1 1872 ? 143.435 181.496 130.015 1.00 13.87  ? 1872 TYR A N     1 
ATOM   3368  C  CA    . TYR A 1 1872 ? 144.107 182.750 129.692 1.00 11.47  ? 1872 TYR A CA    1 
ATOM   3369  C  C     . TYR A 1 1872 ? 145.165 183.046 130.745 1.00 12.54  ? 1872 TYR A C     1 
ATOM   3370  O  O     . TYR A 1 1872 ? 144.863 183.118 131.940 1.00 17.77  ? 1872 TYR A O     1 
ATOM   3371  C  CB    . TYR A 1 1872 ? 143.100 183.890 129.588 1.00 13.95  ? 1872 TYR A CB    1 
ATOM   3372  C  CG    . TYR A 1 1872 ? 143.731 185.185 129.137 1.00 12.51  ? 1872 TYR A CG    1 
ATOM   3373  C  CD1   . TYR A 1 1872 ? 143.918 186.233 130.025 1.00 12.67  ? 1872 TYR A CD1   1 
ATOM   3374  C  CD2   . TYR A 1 1872 ? 144.176 185.346 127.834 1.00 17.73  ? 1872 TYR A CD2   1 
ATOM   3375  C  CE1   . TYR A 1 1872 ? 144.503 187.415 129.621 1.00 17.63  ? 1872 TYR A CE1   1 
ATOM   3376  C  CE2   . TYR A 1 1872 ? 144.769 186.524 127.423 1.00 22.56  ? 1872 TYR A CE2   1 
ATOM   3377  C  CZ    . TYR A 1 1872 ? 144.927 187.554 128.319 1.00 22.06  ? 1872 TYR A CZ    1 
ATOM   3378  O  OH    . TYR A 1 1872 ? 145.515 188.729 127.910 1.00 32.51  ? 1872 TYR A OH    1 
ATOM   3379  N  N     . LEU A 1 1873 ? 146.405 183.224 130.299 1.00 9.94   ? 1873 LEU A N     1 
ATOM   3380  C  CA    . LEU A 1 1873 ? 147.535 183.449 131.185 1.00 12.02  ? 1873 LEU A CA    1 
ATOM   3381  C  C     . LEU A 1 1873 ? 148.028 184.888 131.167 1.00 16.40  ? 1873 LEU A C     1 
ATOM   3382  O  O     . LEU A 1 1873 ? 148.966 185.215 131.898 1.00 26.04  ? 1873 LEU A O     1 
ATOM   3383  C  CB    . LEU A 1 1873 ? 148.683 182.506 130.814 1.00 12.98  ? 1873 LEU A CB    1 
ATOM   3384  C  CG    . LEU A 1 1873 ? 148.301 181.033 130.660 1.00 10.33  ? 1873 LEU A CG    1 
ATOM   3385  C  CD1   . LEU A 1 1873 ? 149.046 180.398 129.497 1.00 8.47   ? 1873 LEU A CD1   1 
ATOM   3386  C  CD2   . LEU A 1 1873 ? 148.565 180.272 131.947 1.00 19.50  ? 1873 LEU A CD2   1 
ATOM   3387  N  N     . GLY A 1 1874 ? 147.419 185.754 130.366 1.00 14.70  ? 1874 GLY A N     1 
ATOM   3388  C  CA    . GLY A 1 1874 ? 147.903 187.122 130.281 1.00 19.98  ? 1874 GLY A CA    1 
ATOM   3389  C  C     . GLY A 1 1874 ? 149.241 187.171 129.573 1.00 25.67  ? 1874 GLY A C     1 
ATOM   3390  O  O     . GLY A 1 1874 ? 149.420 186.594 128.495 1.00 29.61  ? 1874 GLY A O     1 
ATOM   3391  N  N     . VAL A 1 1875 ? 150.196 187.867 130.179 1.00 24.28  ? 1875 VAL A N     1 
ATOM   3392  C  CA    . VAL A 1 1875 ? 151.548 187.989 129.646 1.00 22.91  ? 1875 VAL A CA    1 
ATOM   3393  C  C     . VAL A 1 1875 ? 152.491 187.480 130.730 1.00 25.15  ? 1875 VAL A C     1 
ATOM   3394  O  O     . VAL A 1 1875 ? 152.858 188.224 131.648 1.00 29.76  ? 1875 VAL A O     1 
ATOM   3395  C  CB    . VAL A 1 1875 ? 151.885 189.427 129.238 1.00 23.58  ? 1875 VAL A CB    1 
ATOM   3396  C  CG1   . VAL A 1 1875 ? 153.322 189.519 128.746 1.00 21.84  ? 1875 VAL A CG1   1 
ATOM   3397  C  CG2   . VAL A 1 1875 ? 150.915 189.920 128.175 1.00 24.46  ? 1875 VAL A CG2   1 
ATOM   3398  N  N     . GLN A 1 1876 ? 152.881 186.212 130.634 1.00 23.51  ? 1876 GLN A N     1 
ATOM   3399  C  CA    . GLN A 1 1876 ? 153.792 185.611 131.598 1.00 29.44  ? 1876 GLN A CA    1 
ATOM   3400  C  C     . GLN A 1 1876 ? 155.227 185.695 131.099 1.00 33.63  ? 1876 GLN A C     1 
ATOM   3401  O  O     . GLN A 1 1876 ? 155.488 185.585 129.897 1.00 32.75  ? 1876 GLN A O     1 
ATOM   3402  C  CB    . GLN A 1 1876 ? 153.422 184.150 131.863 1.00 27.17  ? 1876 GLN A CB    1 
ATOM   3403  C  CG    . GLN A 1 1876 ? 151.932 183.868 131.863 1.00 21.80  ? 1876 GLN A CG    1 
ATOM   3404  C  CD    . GLN A 1 1876 ? 151.328 183.946 133.251 1.00 26.25  ? 1876 GLN A CD    1 
ATOM   3405  O  OE1   . GLN A 1 1876 ? 150.786 184.977 133.648 1.00 28.26  ? 1876 GLN A OE1   1 
ATOM   3406  N  NE2   . GLN A 1 1876 ? 151.423 182.854 133.999 1.00 24.16  ? 1876 GLN A NE2   1 
ATOM   3407  N  N     . ASP A 1 1877 ? 156.155 185.894 132.032 1.00 33.41  ? 1877 ASP A N     1 
ATOM   3408  C  CA    . ASP A 1 1877 ? 157.574 185.953 131.699 1.00 34.21  ? 1877 ASP A CA    1 
ATOM   3409  C  C     . ASP A 1 1877 ? 158.037 184.579 131.234 1.00 32.44  ? 1877 ASP A C     1 
ATOM   3410  O  O     . ASP A 1 1877 ? 158.095 183.633 132.025 1.00 29.93  ? 1877 ASP A O     1 
ATOM   3411  C  CB    . ASP A 1 1877 ? 158.379 186.427 132.904 1.00 38.71  ? 1877 ASP A CB    1 
ATOM   3412  C  CG    . ASP A 1 1877 ? 158.823 187.870 132.775 1.00 54.40  ? 1877 ASP A CG    1 
ATOM   3413  O  OD1   . ASP A 1 1877 ? 158.996 188.338 131.630 1.00 56.35  ? 1877 ASP A OD1   1 
ATOM   3414  O  OD2   . ASP A 1 1877 ? 158.994 188.538 133.817 1.00 57.34  ? 1877 ASP A OD2   1 
ATOM   3415  N  N     . LYS A 1 1878 ? 158.363 184.467 129.950 1.00 27.12  ? 1878 LYS A N     1 
ATOM   3416  C  CA    . LYS A 1 1878 ? 158.773 183.191 129.387 1.00 20.68  ? 1878 LYS A CA    1 
ATOM   3417  C  C     . LYS A 1 1878 ? 160.157 182.795 129.888 1.00 19.73  ? 1878 LYS A C     1 
ATOM   3418  O  O     . LYS A 1 1878 ? 160.962 183.637 130.296 1.00 24.19  ? 1878 LYS A O     1 
ATOM   3419  C  CB    . LYS A 1 1878 ? 158.770 183.258 127.860 1.00 18.28  ? 1878 LYS A CB    1 
ATOM   3420  C  CG    . LYS A 1 1878 ? 157.408 183.023 127.231 1.00 22.31  ? 1878 LYS A CG    1 
ATOM   3421  C  CD    . LYS A 1 1878 ? 157.290 181.614 126.678 1.00 29.39  ? 1878 LYS A CD    1 
ATOM   3422  C  CE    . LYS A 1 1878 ? 158.211 181.409 125.486 1.00 21.94  ? 1878 LYS A CE    1 
ATOM   3423  N  NZ    . LYS A 1 1878 ? 158.077 180.041 124.911 1.00 24.14  ? 1878 LYS A NZ    1 
ATOM   3424  N  N     . LEU A 1 1879 ? 160.425 181.494 129.856 1.00 11.97  ? 1879 LEU A N     1 
ATOM   3425  C  CA    . LEU A 1 1879 ? 161.708 180.943 130.265 1.00 8.47   ? 1879 LEU A CA    1 
ATOM   3426  C  C     . LEU A 1 1879 ? 162.530 180.566 129.041 1.00 9.54   ? 1879 LEU A C     1 
ATOM   3427  O  O     . LEU A 1 1879 ? 161.981 180.196 128.000 1.00 13.78  ? 1879 LEU A O     1 
ATOM   3428  C  CB    . LEU A 1 1879 ? 161.518 179.714 131.156 1.00 8.04   ? 1879 LEU A CB    1 
ATOM   3429  C  CG    . LEU A 1 1879 ? 161.715 179.895 132.661 1.00 6.73   ? 1879 LEU A CG    1 
ATOM   3430  C  CD1   . LEU A 1 1879 ? 160.701 180.871 133.230 1.00 8.87   ? 1879 LEU A CD1   1 
ATOM   3431  C  CD2   . LEU A 1 1879 ? 161.628 178.554 133.362 1.00 5.53   ? 1879 LEU A CD2   1 
ATOM   3432  N  N     . VAL A 1 1880 ? 163.852 180.666 129.173 1.00 7.45   ? 1880 VAL A N     1 
ATOM   3433  C  CA    . VAL A 1 1880 ? 164.744 180.214 128.113 1.00 5.21   ? 1880 VAL A CA    1 
ATOM   3434  C  C     . VAL A 1 1880 ? 164.775 178.694 128.111 1.00 7.16   ? 1880 VAL A C     1 
ATOM   3435  O  O     . VAL A 1 1880 ? 165.040 178.060 129.142 1.00 8.98   ? 1880 VAL A O     1 
ATOM   3436  C  CB    . VAL A 1 1880 ? 166.149 180.805 128.301 1.00 4.78   ? 1880 VAL A CB    1 
ATOM   3437  C  CG1   . VAL A 1 1880 ? 167.107 180.233 127.272 1.00 6.86   ? 1880 VAL A CG1   1 
ATOM   3438  C  CG2   . VAL A 1 1880 ? 166.102 182.318 128.205 1.00 4.71   ? 1880 VAL A CG2   1 
ATOM   3439  N  N     . GLN A 1 1881 ? 164.505 178.097 126.951 1.00 6.76   ? 1881 GLN A N     1 
ATOM   3440  C  CA    . GLN A 1 1881 ? 164.380 176.645 126.841 1.00 6.80   ? 1881 GLN A CA    1 
ATOM   3441  C  C     . GLN A 1 1881 ? 165.776 176.033 126.780 1.00 7.93   ? 1881 GLN A C     1 
ATOM   3442  O  O     . GLN A 1 1881 ? 166.330 175.748 125.716 1.00 10.93  ? 1881 GLN A O     1 
ATOM   3443  C  CB    . GLN A 1 1881 ? 163.541 176.266 125.629 1.00 9.70   ? 1881 GLN A CB    1 
ATOM   3444  C  CG    . GLN A 1 1881 ? 163.065 174.826 125.644 1.00 9.87   ? 1881 GLN A CG    1 
ATOM   3445  C  CD    . GLN A 1 1881 ? 161.934 174.592 126.625 1.00 10.61  ? 1881 GLN A CD    1 
ATOM   3446  O  OE1   . GLN A 1 1881 ? 161.403 175.531 127.215 1.00 11.53  ? 1881 GLN A OE1   1 
ATOM   3447  N  NE2   . GLN A 1 1881 ? 161.563 173.330 126.808 1.00 10.94  ? 1881 GLN A NE2   1 
ATOM   3448  N  N     . THR A 1 1882 ? 166.349 175.834 127.960 1.00 8.82   ? 1882 THR A N     1 
ATOM   3449  C  CA    . THR A 1 1882 ? 167.657 175.222 128.107 1.00 7.18   ? 1882 THR A CA    1 
ATOM   3450  C  C     . THR A 1 1882 ? 167.551 173.704 127.997 1.00 7.76   ? 1882 THR A C     1 
ATOM   3451  O  O     . THR A 1 1882 ? 166.458 173.141 128.096 1.00 8.89   ? 1882 THR A O     1 
ATOM   3452  C  CB    . THR A 1 1882 ? 168.265 175.613 129.450 1.00 9.12   ? 1882 THR A CB    1 
ATOM   3453  O  OG1   . THR A 1 1882 ? 167.549 174.965 130.508 1.00 13.31  ? 1882 THR A OG1   1 
ATOM   3454  C  CG2   . THR A 1 1882 ? 168.194 177.119 129.644 1.00 9.19   ? 1882 THR A CG2   1 
ATOM   3455  N  N     . PRO A 1 1883 ? 168.673 173.015 127.763 1.00 8.51   ? 1883 PRO A N     1 
ATOM   3456  C  CA    . PRO A 1 1883 ? 168.633 171.544 127.779 1.00 7.44   ? 1883 PRO A CA    1 
ATOM   3457  C  C     . PRO A 1 1883 ? 168.115 170.972 129.086 1.00 9.35   ? 1883 PRO A C     1 
ATOM   3458  O  O     . PRO A 1 1883 ? 167.450 169.929 129.072 1.00 10.24  ? 1883 PRO A O     1 
ATOM   3459  C  CB    . PRO A 1 1883 ? 170.096 171.156 127.530 1.00 7.47   ? 1883 PRO A CB    1 
ATOM   3460  C  CG    . PRO A 1 1883 ? 170.647 172.289 126.751 1.00 8.63   ? 1883 PRO A CG    1 
ATOM   3461  C  CD    . PRO A 1 1883 ? 169.968 173.523 127.275 1.00 9.37   ? 1883 PRO A CD    1 
ATOM   3462  N  N     . LEU A 1 1884 ? 168.398 171.622 130.217 1.00 8.58   ? 1884 LEU A N     1 
ATOM   3463  C  CA    . LEU A 1 1884 ? 167.816 171.183 131.480 1.00 8.34   ? 1884 LEU A CA    1 
ATOM   3464  C  C     . LEU A 1 1884 ? 166.307 171.393 131.487 1.00 8.37   ? 1884 LEU A C     1 
ATOM   3465  O  O     . LEU A 1 1884 ? 165.560 170.577 132.040 1.00 9.70   ? 1884 LEU A O     1 
ATOM   3466  C  CB    . LEU A 1 1884 ? 168.473 171.923 132.646 1.00 10.87  ? 1884 LEU A CB    1 
ATOM   3467  C  CG    . LEU A 1 1884 ? 167.922 171.638 134.045 1.00 8.08   ? 1884 LEU A CG    1 
ATOM   3468  C  CD1   . LEU A 1 1884 ? 168.160 170.190 134.432 1.00 8.73   ? 1884 LEU A CD1   1 
ATOM   3469  C  CD2   . LEU A 1 1884 ? 168.549 172.570 135.065 1.00 7.43   ? 1884 LEU A CD2   1 
ATOM   3470  N  N     . THR A 1 1885 ? 165.840 172.486 130.879 1.00 7.72   ? 1885 THR A N     1 
ATOM   3471  C  CA    . THR A 1 1885 ? 164.403 172.701 130.741 1.00 7.00   ? 1885 THR A CA    1 
ATOM   3472  C  C     . THR A 1 1885 ? 163.766 171.626 129.868 1.00 7.95   ? 1885 THR A C     1 
ATOM   3473  O  O     . THR A 1 1885 ? 162.673 171.137 130.175 1.00 8.22   ? 1885 THR A O     1 
ATOM   3474  C  CB    . THR A 1 1885 ? 164.131 174.090 130.164 1.00 6.10   ? 1885 THR A CB    1 
ATOM   3475  O  OG1   . THR A 1 1885 ? 164.818 175.075 130.944 1.00 8.31   ? 1885 THR A OG1   1 
ATOM   3476  C  CG2   . THR A 1 1885 ? 162.643 174.392 130.175 1.00 7.55   ? 1885 THR A CG2   1 
ATOM   3477  N  N     . ASP A 1 1886 ? 164.432 171.251 128.773 1.00 9.28   ? 1886 ASP A N     1 
ATOM   3478  C  CA    . ASP A 1 1886 ? 163.911 170.189 127.918 1.00 6.81   ? 1886 ASP A CA    1 
ATOM   3479  C  C     . ASP A 1 1886 ? 163.879 168.857 128.654 1.00 7.25   ? 1886 ASP A C     1 
ATOM   3480  O  O     . ASP A 1 1886 ? 162.918 168.090 128.524 1.00 6.67   ? 1886 ASP A O     1 
ATOM   3481  C  CB    . ASP A 1 1886 ? 164.751 170.081 126.647 1.00 10.40  ? 1886 ASP A CB    1 
ATOM   3482  C  CG    . ASP A 1 1886 ? 164.312 171.056 125.574 1.00 22.01  ? 1886 ASP A CG    1 
ATOM   3483  O  OD1   . ASP A 1 1886 ? 163.135 171.471 125.594 1.00 18.74  ? 1886 ASP A OD1   1 
ATOM   3484  O  OD2   . ASP A 1 1886 ? 165.144 171.408 124.713 1.00 22.39  ? 1886 ASP A OD2   1 
ATOM   3485  N  N     . ARG A 1 1887 ? 164.926 168.562 129.427 1.00 6.29   ? 1887 ARG A N     1 
ATOM   3486  C  CA    . ARG A 1 1887 ? 164.933 167.344 130.230 1.00 5.77   ? 1887 ARG A CA    1 
ATOM   3487  C  C     . ARG A 1 1887 ? 163.831 167.379 131.280 1.00 5.58   ? 1887 ARG A C     1 
ATOM   3488  O  O     . ARG A 1 1887 ? 163.202 166.354 131.566 1.00 5.78   ? 1887 ARG A O     1 
ATOM   3489  C  CB    . ARG A 1 1887 ? 166.299 167.157 130.886 1.00 6.98   ? 1887 ARG A CB    1 
ATOM   3490  C  CG    . ARG A 1 1887 ? 166.528 165.771 131.459 1.00 5.96   ? 1887 ARG A CG    1 
ATOM   3491  C  CD    . ARG A 1 1887 ? 167.765 165.740 132.336 1.00 7.81   ? 1887 ARG A CD    1 
ATOM   3492  N  NE    . ARG A 1 1887 ? 168.009 164.411 132.882 1.00 11.29  ? 1887 ARG A NE    1 
ATOM   3493  C  CZ    . ARG A 1 1887 ? 169.181 163.793 132.852 1.00 11.18  ? 1887 ARG A CZ    1 
ATOM   3494  N  NH1   . ARG A 1 1887 ? 170.247 164.359 132.308 1.00 15.36  ? 1887 ARG A NH1   1 
ATOM   3495  N  NH2   . ARG A 1 1887 ? 169.288 162.578 133.380 1.00 9.62   ? 1887 ARG A NH2   1 
ATOM   3496  N  N     . CYS A 1 1888 ? 163.591 168.551 131.872 1.00 5.55   ? 1888 CYS A N     1 
ATOM   3497  C  CA    . CYS A 1 1888 ? 162.472 168.693 132.796 1.00 4.10   ? 1888 CYS A CA    1 
ATOM   3498  C  C     . CYS A 1 1888 ? 161.146 168.475 132.084 1.00 4.88   ? 1888 CYS A C     1 
ATOM   3499  O  O     . CYS A 1 1888 ? 160.276 167.753 132.583 1.00 5.55   ? 1888 CYS A O     1 
ATOM   3500  C  CB    . CYS A 1 1888 ? 162.510 170.069 133.460 1.00 6.14   ? 1888 CYS A CB    1 
ATOM   3501  S  SG    . CYS A 1 1888 ? 161.249 170.321 134.731 1.00 13.42  ? 1888 CYS A SG    1 
ATOM   3502  N  N     . TYR A 1 1889 ? 160.981 169.077 130.906 1.00 6.36   ? 1889 TYR A N     1 
ATOM   3503  C  CA    . TYR A 1 1889 ? 159.741 168.916 130.154 1.00 3.64   ? 1889 TYR A CA    1 
ATOM   3504  C  C     . TYR A 1 1889 ? 159.517 167.459 129.778 1.00 4.02   ? 1889 TYR A C     1 
ATOM   3505  O  O     . TYR A 1 1889 ? 158.396 166.948 129.865 1.00 5.88   ? 1889 TYR A O     1 
ATOM   3506  C  CB    . TYR A 1 1889 ? 159.771 169.793 128.903 1.00 4.69   ? 1889 TYR A CB    1 
ATOM   3507  C  CG    . TYR A 1 1889 ? 159.427 171.243 129.145 1.00 4.61   ? 1889 TYR A CG    1 
ATOM   3508  C  CD1   . TYR A 1 1889 ? 159.606 171.827 130.390 1.00 4.88   ? 1889 TYR A CD1   1 
ATOM   3509  C  CD2   . TYR A 1 1889 ? 158.933 172.032 128.121 1.00 6.55   ? 1889 TYR A CD2   1 
ATOM   3510  C  CE1   . TYR A 1 1889 ? 159.294 173.153 130.605 1.00 5.78   ? 1889 TYR A CE1   1 
ATOM   3511  C  CE2   . TYR A 1 1889 ? 158.622 173.356 128.326 1.00 6.32   ? 1889 TYR A CE2   1 
ATOM   3512  C  CZ    . TYR A 1 1889 ? 158.803 173.912 129.567 1.00 6.83   ? 1889 TYR A CZ    1 
ATOM   3513  O  OH    . TYR A 1 1889 ? 158.488 175.234 129.763 1.00 8.83   ? 1889 TYR A OH    1 
ATOM   3514  N  N     . LEU A 1 1890 ? 160.579 166.772 129.353 1.00 5.34   ? 1890 LEU A N     1 
ATOM   3515  C  CA    . LEU A 1 1890 ? 160.450 165.370 128.971 1.00 4.17   ? 1890 LEU A CA    1 
ATOM   3516  C  C     . LEU A 1 1890 ? 160.072 164.506 130.167 1.00 4.52   ? 1890 LEU A C     1 
ATOM   3517  O  O     . LEU A 1 1890 ? 159.186 163.649 130.074 1.00 6.80   ? 1890 LEU A O     1 
ATOM   3518  C  CB    . LEU A 1 1890 ? 161.753 164.882 128.339 1.00 4.28   ? 1890 LEU A CB    1 
ATOM   3519  C  CG    . LEU A 1 1890 ? 161.743 163.471 127.753 1.00 4.73   ? 1890 LEU A CG    1 
ATOM   3520  C  CD1   . LEU A 1 1890 ? 160.852 163.412 126.528 1.00 6.81   ? 1890 LEU A CD1   1 
ATOM   3521  C  CD2   . LEU A 1 1890 ? 163.154 163.033 127.410 1.00 7.24   ? 1890 LEU A CD2   1 
ATOM   3522  N  N     . THR A 1 1891 ? 160.731 164.724 131.306 1.00 5.16   ? 1891 THR A N     1 
ATOM   3523  C  CA    . THR A 1 1891 ? 160.465 163.898 132.479 1.00 4.28   ? 1891 THR A CA    1 
ATOM   3524  C  C     . THR A 1 1891 ? 159.087 164.186 133.063 1.00 5.56   ? 1891 THR A C     1 
ATOM   3525  O  O     . THR A 1 1891 ? 158.355 163.259 133.428 1.00 8.32   ? 1891 THR A O     1 
ATOM   3526  C  CB    . THR A 1 1891 ? 161.551 164.116 133.532 1.00 6.21   ? 1891 THR A CB    1 
ATOM   3527  O  OG1   . THR A 1 1891 ? 162.841 163.969 132.925 1.00 8.67   ? 1891 THR A OG1   1 
ATOM   3528  C  CG2   . THR A 1 1891 ? 161.414 163.102 134.653 1.00 5.98   ? 1891 THR A CG2   1 
ATOM   3529  N  N     . MET A 1 1892 ? 158.714 165.465 133.157 1.00 5.04   ? 1892 MET A N     1 
ATOM   3530  C  CA    . MET A 1 1892 ? 157.420 165.809 133.739 1.00 3.95   ? 1892 MET A CA    1 
ATOM   3531  C  C     . MET A 1 1892 ? 156.270 165.355 132.849 1.00 4.68   ? 1892 MET A C     1 
ATOM   3532  O  O     . MET A 1 1892 ? 155.233 164.906 133.351 1.00 9.47   ? 1892 MET A O     1 
ATOM   3533  C  CB    . MET A 1 1892 ? 157.339 167.312 134.000 1.00 3.15   ? 1892 MET A CB    1 
ATOM   3534  C  CG    . MET A 1 1892 ? 158.373 167.827 134.988 1.00 5.37   ? 1892 MET A CG    1 
ATOM   3535  S  SD    . MET A 1 1892 ? 158.088 167.261 136.672 1.00 20.98  ? 1892 MET A SD    1 
ATOM   3536  C  CE    . MET A 1 1892 ? 159.642 166.441 137.019 1.00 7.18   ? 1892 MET A CE    1 
ATOM   3537  N  N     . THR A 1 1893 ? 156.427 165.465 131.528 1.00 3.79   ? 1893 THR A N     1 
ATOM   3538  C  CA    . THR A 1 1893 ? 155.385 164.984 130.627 1.00 4.33   ? 1893 THR A CA    1 
ATOM   3539  C  C     . THR A 1 1893 ? 155.263 163.466 130.670 1.00 6.02   ? 1893 THR A C     1 
ATOM   3540  O  O     . THR A 1 1893 ? 154.155 162.933 130.543 1.00 8.24   ? 1893 THR A O     1 
ATOM   3541  C  CB    . THR A 1 1893 ? 155.651 165.455 129.197 1.00 6.35   ? 1893 THR A CB    1 
ATOM   3542  O  OG1   . THR A 1 1893 ? 157.022 165.214 128.858 1.00 5.88   ? 1893 THR A OG1   1 
ATOM   3543  C  CG2   . THR A 1 1893 ? 155.345 166.941 129.058 1.00 5.87   ? 1893 THR A CG2   1 
ATOM   3544  N  N     . GLN A 1 1894 ? 156.381 162.757 130.840 1.00 5.75   ? 1894 GLN A N     1 
ATOM   3545  C  CA    . GLN A 1 1894 ? 156.316 161.311 131.024 1.00 4.97   ? 1894 GLN A CA    1 
ATOM   3546  C  C     . GLN A 1 1894 ? 155.567 160.958 132.302 1.00 6.39   ? 1894 GLN A C     1 
ATOM   3547  O  O     . GLN A 1 1894 ? 154.801 159.988 132.335 1.00 8.41   ? 1894 GLN A O     1 
ATOM   3548  C  CB    . GLN A 1 1894 ? 157.725 160.718 131.043 1.00 6.36   ? 1894 GLN A CB    1 
ATOM   3549  C  CG    . GLN A 1 1894 ? 158.381 160.617 129.677 1.00 5.70   ? 1894 GLN A CG    1 
ATOM   3550  C  CD    . GLN A 1 1894 ? 157.757 159.547 128.809 1.00 8.32   ? 1894 GLN A CD    1 
ATOM   3551  O  OE1   . GLN A 1 1894 ? 157.884 158.355 129.086 1.00 7.71   ? 1894 GLN A OE1   1 
ATOM   3552  N  NE2   . GLN A 1 1894 ? 157.078 159.966 127.748 1.00 11.84  ? 1894 GLN A NE2   1 
ATOM   3553  N  N     . ALA A 1 1895 ? 155.782 161.733 133.369 1.00 6.98   ? 1895 ALA A N     1 
ATOM   3554  C  CA    . ALA A 1 1895 ? 155.024 161.531 134.599 1.00 4.82   ? 1895 ALA A CA    1 
ATOM   3555  C  C     . ALA A 1 1895 ? 153.539 161.790 134.379 1.00 5.02   ? 1895 ALA A C     1 
ATOM   3556  O  O     . ALA A 1 1895 ? 152.689 161.066 134.910 1.00 7.60   ? 1895 ALA A O     1 
ATOM   3557  C  CB    . ALA A 1 1895 ? 155.567 162.436 135.704 1.00 2.92   ? 1895 ALA A CB    1 
ATOM   3558  N  N     . LEU A 1 1896 ? 153.227 162.839 133.615 1.00 4.93   ? 1896 LEU A N     1 
ATOM   3559  C  CA    . LEU A 1 1896 ? 151.809 163.187 133.341 1.00 4.21   ? 1896 LEU A CA    1 
ATOM   3560  C  C     . LEU A 1 1896 ? 151.148 162.036 132.569 1.00 7.78   ? 1896 LEU A C     1 
ATOM   3561  O  O     . LEU A 1 1896 ? 150.005 161.668 132.917 1.00 8.97   ? 1896 LEU A O     1 
ATOM   3562  C  CB    . LEU A 1 1896 ? 151.751 164.499 132.563 1.00 4.33   ? 1896 LEU A CB    1 
ATOM   3563  C  CG    . LEU A 1 1896 ? 152.274 165.738 133.296 1.00 4.32   ? 1896 LEU A CG    1 
ATOM   3564  C  CD1   . LEU A 1 1896 ? 152.369 166.923 132.350 1.00 4.54   ? 1896 LEU A CD1   1 
ATOM   3565  C  CD2   . LEU A 1 1896 ? 151.380 166.069 134.478 1.00 4.75   ? 1896 LEU A CD2   1 
ATOM   3566  N  N     . GLU A 1 1897 ? 151.844 161.489 131.570 1.00 10.35  ? 1897 GLU A N     1 
ATOM   3567  C  CA    . GLU A 1 1897 ? 151.298 160.361 130.770 1.00 11.16  ? 1897 GLU A CA    1 
ATOM   3568  C  C     . GLU A 1 1897 ? 151.097 159.146 131.688 1.00 12.39  ? 1897 GLU A C     1 
ATOM   3569  O  O     . GLU A 1 1897 ? 150.143 158.375 131.451 1.00 16.83  ? 1897 GLU A O     1 
ATOM   3570  C  CB    . GLU A 1 1897 ? 152.247 160.039 129.615 1.00 13.84  ? 1897 GLU A CB    1 
ATOM   3571  C  CG    . GLU A 1 1897 ? 151.626 159.142 128.549 1.00 20.01  ? 1897 GLU A CG    1 
ATOM   3572  C  CD    . GLU A 1 1897 ? 150.535 159.799 127.720 1.00 33.80  ? 1897 GLU A CD    1 
ATOM   3573  O  OE1   . GLU A 1 1897 ? 150.229 160.985 127.962 1.00 30.56  ? 1897 GLU A OE1   1 
ATOM   3574  O  OE2   . GLU A 1 1897 ? 149.995 159.118 126.824 1.00 43.12  ? 1897 GLU A OE2   1 
ATOM   3575  N  N     . ALA A 1 1898 ? 151.962 158.988 132.694 1.00 9.54   ? 1898 ALA A N     1 
ATOM   3576  C  CA    . ALA A 1 1898 ? 151.862 157.842 133.629 1.00 7.80   ? 1898 ALA A CA    1 
ATOM   3577  C  C     . ALA A 1 1898 ? 150.868 158.173 134.743 1.00 11.12  ? 1898 ALA A C     1 
ATOM   3578  O  O     . ALA A 1 1898 ? 150.739 157.369 135.692 1.00 16.54  ? 1898 ALA A O     1 
ATOM   3579  C  CB    . ALA A 1 1898 ? 153.227 157.519 134.191 1.00 7.38   ? 1898 ALA A CB    1 
ATOM   3580  N  N     . ARG A 1 1899 ? 150.193 159.321 134.635 1.00 9.81   ? 1899 ARG A N     1 
ATOM   3581  C  CA    . ARG A 1 1899 ? 149.238 159.750 135.690 1.00 8.58   ? 1899 ARG A CA    1 
ATOM   3582  C  C     . ARG A 1 1899 ? 149.991 159.782 137.028 1.00 8.62   ? 1899 ARG A C     1 
ATOM   3583  O  O     . ARG A 1 1899 ? 149.422 159.325 138.042 1.00 11.62  ? 1899 ARG A O     1 
ATOM   3584  C  CB    . ARG A 1 1899 ? 148.007 158.837 135.718 1.00 13.56  ? 1899 ARG A CB    1 
ATOM   3585  C  CG    . ARG A 1 1899 ? 146.944 159.223 134.700 1.00 15.92  ? 1899 ARG A CG    1 
ATOM   3586  C  CD    . ARG A 1 1899 ? 147.500 159.287 133.287 1.00 17.07  ? 1899 ARG A CD    1 
ATOM   3587  N  NE    . ARG A 1 1899 ? 146.607 159.988 132.358 1.00 25.50  ? 1899 ARG A NE    1 
ATOM   3588  C  CZ    . ARG A 1 1899 ? 146.881 160.207 131.078 1.00 30.52  ? 1899 ARG A CZ    1 
ATOM   3589  N  NH1   . ARG A 1 1899 ? 147.982 159.712 130.543 1.00 28.85  ? 1899 ARG A NH1   1 
ATOM   3590  N  NH2   . ARG A 1 1899 ? 146.053 160.922 130.338 1.00 32.27  ? 1899 ARG A NH2   1 
ATOM   3591  N  N     . LEU A 1 1900 ? 151.223 160.295 137.016 1.00 6.85   ? 1900 LEU A N     1 
ATOM   3592  C  CA    . LEU A 1 1900 ? 152.033 160.397 138.257 1.00 5.10   ? 1900 LEU A CA    1 
ATOM   3593  C  C     . LEU A 1 1900 ? 152.461 161.859 138.438 1.00 3.44   ? 1900 LEU A C     1 
ATOM   3594  O  O     . LEU A 1 1900 ? 152.385 162.623 137.452 1.00 4.82   ? 1900 LEU A O     1 
ATOM   3595  C  CB    . LEU A 1 1900 ? 153.243 159.468 138.185 1.00 5.14   ? 1900 LEU A CB    1 
ATOM   3596  C  CG    . LEU A 1 1900 ? 152.935 157.970 138.102 1.00 6.99   ? 1900 LEU A CG    1 
ATOM   3597  C  CD1   . LEU A 1 1900 ? 154.221 157.167 138.032 1.00 8.68   ? 1900 LEU A CD1   1 
ATOM   3598  C  CD2   . LEU A 1 1900 ? 152.094 157.532 139.288 1.00 6.97   ? 1900 LEU A CD2   1 
ATOM   3599  N  N     . GLY A 1 1901 ? 152.884 162.226 139.649 1.00 3.88   ? 1901 GLY A N     1 
ATOM   3600  C  CA    . GLY A 1 1901 ? 153.309 163.611 139.922 1.00 3.20   ? 1901 GLY A CA    1 
ATOM   3601  C  C     . GLY A 1 1901 ? 154.752 163.834 139.519 1.00 2.66   ? 1901 GLY A C     1 
ATOM   3602  O  O     . GLY A 1 1901 ? 155.414 162.852 139.125 1.00 4.21   ? 1901 GLY A O     1 
ATOM   3603  N  N     . GLY A 1 1902 ? 155.224 165.080 139.608 1.00 2.18   ? 1902 GLY A N     1 
ATOM   3604  C  CA    . GLY A 1 1902 ? 156.624 165.395 139.272 1.00 1.79   ? 1902 GLY A CA    1 
ATOM   3605  C  C     . GLY A 1 1902 ? 157.366 165.943 140.473 1.00 2.37   ? 1902 GLY A C     1 
ATOM   3606  O  O     . GLY A 1 1902 ? 156.758 166.725 141.233 1.00 2.90   ? 1902 GLY A O     1 
ATOM   3607  N  N     . SER A 1 1903 ? 158.631 165.551 140.643 1.00 2.71   ? 1903 SER A N     1 
ATOM   3608  C  CA    . SER A 1 1903 ? 159.438 166.042 141.759 1.00 2.62   ? 1903 SER A CA    1 
ATOM   3609  C  C     . SER A 1 1903 ? 160.786 166.538 141.253 1.00 4.44   ? 1903 SER A C     1 
ATOM   3610  O  O     . SER A 1 1903 ? 161.802 165.842 141.369 1.00 6.66   ? 1903 SER A O     1 
ATOM   3611  C  CB    . SER A 1 1903 ? 159.631 164.957 142.819 1.00 3.74   ? 1903 SER A CB    1 
ATOM   3612  O  OG    . SER A 1 1903 ? 158.462 164.180 142.968 1.00 4.69   ? 1903 SER A OG    1 
ATOM   3613  N  N     . PRO A 1 1904 ? 160.833 167.739 140.681 1.00 4.68   ? 1904 PRO A N     1 
ATOM   3614  C  CA    . PRO A 1 1904 ? 162.134 168.368 140.430 1.00 4.89   ? 1904 PRO A CA    1 
ATOM   3615  C  C     . PRO A 1 1904 ? 162.801 168.729 141.748 1.00 5.83   ? 1904 PRO A C     1 
ATOM   3616  O  O     . PRO A 1 1904 ? 162.261 169.499 142.546 1.00 9.11   ? 1904 PRO A O     1 
ATOM   3617  C  CB    . PRO A 1 1904 ? 161.776 169.614 139.611 1.00 5.11   ? 1904 PRO A CB    1 
ATOM   3618  C  CG    . PRO A 1 1904 ? 160.348 169.883 139.939 1.00 4.56   ? 1904 PRO A CG    1 
ATOM   3619  C  CD    . PRO A 1 1904 ? 159.723 168.540 140.139 1.00 3.80   ? 1904 PRO A CD    1 
ATOM   3620  N  N     . PHE A 1 1905 ? 163.980 168.159 141.979 1.00 5.40   ? 1905 PHE A N     1 
ATOM   3621  C  CA    . PHE A 1 1905 ? 164.690 168.355 143.233 1.00 6.52   ? 1905 PHE A CA    1 
ATOM   3622  C  C     . PHE A 1 1905 ? 166.091 168.879 142.958 1.00 7.57   ? 1905 PHE A C     1 
ATOM   3623  O  O     . PHE A 1 1905 ? 166.653 168.687 141.877 1.00 10.66  ? 1905 PHE A O     1 
ATOM   3624  C  CB    . PHE A 1 1905 ? 164.748 167.058 144.062 1.00 7.02   ? 1905 PHE A CB    1 
ATOM   3625  C  CG    . PHE A 1 1905 ? 165.503 165.938 143.403 1.00 5.60   ? 1905 PHE A CG    1 
ATOM   3626  C  CD1   . PHE A 1 1905 ? 166.861 165.778 143.621 1.00 6.09   ? 1905 PHE A CD1   1 
ATOM   3627  C  CD2   . PHE A 1 1905 ? 164.852 165.040 142.576 1.00 5.30   ? 1905 PHE A CD2   1 
ATOM   3628  C  CE1   . PHE A 1 1905 ? 167.555 164.749 143.022 1.00 8.71   ? 1905 PHE A CE1   1 
ATOM   3629  C  CE2   . PHE A 1 1905 ? 165.542 164.008 141.974 1.00 6.45   ? 1905 PHE A CE2   1 
ATOM   3630  C  CZ    . PHE A 1 1905 ? 166.894 163.862 142.198 1.00 9.77   ? 1905 PHE A CZ    1 
ATOM   3631  N  N     . GLY A 1 1906 ? 166.644 169.555 143.960 1.00 8.00   ? 1906 GLY A N     1 
ATOM   3632  C  CA    . GLY A 1 1906 ? 167.959 170.138 143.859 1.00 9.82   ? 1906 GLY A CA    1 
ATOM   3633  C  C     . GLY A 1 1906 ? 168.108 171.335 144.772 1.00 11.98  ? 1906 GLY A C     1 
ATOM   3634  O  O     . GLY A 1 1906 ? 167.194 171.690 145.523 1.00 15.06  ? 1906 GLY A O     1 
ATOM   3635  N  N     . PRO A 1 1907 ? 169.268 171.984 144.728 1.00 9.97   ? 1907 PRO A N     1 
ATOM   3636  C  CA    . PRO A 1 1907 ? 169.482 173.175 145.554 1.00 11.40  ? 1907 PRO A CA    1 
ATOM   3637  C  C     . PRO A 1 1907 ? 168.639 174.345 145.068 1.00 13.02  ? 1907 PRO A C     1 
ATOM   3638  O  O     . PRO A 1 1907 ? 167.994 174.303 144.019 1.00 14.18  ? 1907 PRO A O     1 
ATOM   3639  C  CB    . PRO A 1 1907 ? 170.979 173.449 145.391 1.00 12.84  ? 1907 PRO A CB    1 
ATOM   3640  C  CG    . PRO A 1 1907 ? 171.294 172.910 144.040 1.00 10.89  ? 1907 PRO A CG    1 
ATOM   3641  C  CD    . PRO A 1 1907 ? 170.450 171.667 143.907 1.00 8.92   ? 1907 PRO A CD    1 
ATOM   3642  N  N     . ALA A 1 1908 ? 168.648 175.408 145.866 1.00 11.92  ? 1908 ALA A N     1 
ATOM   3643  C  CA    . ALA A 1 1908 ? 167.831 176.574 145.574 1.00 9.37   ? 1908 ALA A CA    1 
ATOM   3644  C  C     . ALA A 1 1908 ? 168.344 177.306 144.336 1.00 11.46  ? 1908 ALA A C     1 
ATOM   3645  O  O     . ALA A 1 1908 ? 169.528 177.257 143.991 1.00 14.14  ? 1908 ALA A O     1 
ATOM   3646  C  CB    . ALA A 1 1908 ? 167.806 177.525 146.770 1.00 11.49  ? 1908 ALA A CB    1 
ATOM   3647  N  N     . GLY A 1 1909 ? 167.423 177.994 143.665 1.00 8.46   ? 1909 GLY A N     1 
ATOM   3648  C  CA    . GLY A 1 1909 ? 167.756 178.798 142.507 1.00 7.45   ? 1909 GLY A CA    1 
ATOM   3649  C  C     . GLY A 1 1909 ? 168.240 178.013 141.306 1.00 8.99   ? 1909 GLY A C     1 
ATOM   3650  O  O     . GLY A 1 1909 ? 169.213 178.403 140.655 1.00 20.33  ? 1909 GLY A O     1 
ATOM   3651  N  N     . THR A 1 1910 ? 167.570 176.903 141.001 1.00 7.04   ? 1910 THR A N     1 
ATOM   3652  C  CA    . THR A 1 1910 ? 167.879 176.118 139.816 1.00 7.59   ? 1910 THR A CA    1 
ATOM   3653  C  C     . THR A 1 1910 ? 166.759 176.104 138.788 1.00 7.95   ? 1910 THR A C     1 
ATOM   3654  O  O     . THR A 1 1910 ? 166.869 175.379 137.793 1.00 13.87  ? 1910 THR A O     1 
ATOM   3655  C  CB    . THR A 1 1910 ? 168.222 174.669 140.198 1.00 10.96  ? 1910 THR A CB    1 
ATOM   3656  O  OG1   . THR A 1 1910 ? 167.174 174.122 141.008 1.00 14.10  ? 1910 THR A OG1   1 
ATOM   3657  C  CG2   . THR A 1 1910 ? 169.534 174.617 140.967 1.00 9.37   ? 1910 THR A CG2   1 
ATOM   3658  N  N     . GLY A 1 1911 ? 165.696 176.872 138.991 1.00 7.22   ? 1911 GLY A N     1 
ATOM   3659  C  CA    . GLY A 1 1911 ? 164.597 176.925 138.053 1.00 6.23   ? 1911 GLY A CA    1 
ATOM   3660  C  C     . GLY A 1 1911 ? 163.570 175.824 138.183 1.00 5.18   ? 1911 GLY A C     1 
ATOM   3661  O  O     . GLY A 1 1911 ? 162.844 175.571 137.217 1.00 8.55   ? 1911 GLY A O     1 
ATOM   3662  N  N     . LYS A 1 1912 ? 163.489 175.160 139.336 1.00 4.80   ? 1912 LYS A N     1 
ATOM   3663  C  CA    . LYS A 1 1912 ? 162.546 174.058 139.497 1.00 5.18   ? 1912 LYS A CA    1 
ATOM   3664  C  C     . LYS A 1 1912 ? 161.106 174.559 139.508 1.00 6.71   ? 1912 LYS A C     1 
ATOM   3665  O  O     . LYS A 1 1912 ? 160.242 174.023 138.805 1.00 7.75   ? 1912 LYS A O     1 
ATOM   3666  C  CB    . LYS A 1 1912 ? 162.862 173.291 140.780 1.00 6.17   ? 1912 LYS A CB    1 
ATOM   3667  C  CG    . LYS A 1 1912 ? 164.230 172.636 140.802 1.00 7.63   ? 1912 LYS A CG    1 
ATOM   3668  C  CD    . LYS A 1 1912 ? 164.487 171.960 142.138 1.00 7.45   ? 1912 LYS A CD    1 
ATOM   3669  C  CE    . LYS A 1 1912 ? 164.476 172.964 143.279 1.00 8.31   ? 1912 LYS A CE    1 
ATOM   3670  N  NZ    . LYS A 1 1912 ? 164.740 172.320 144.593 1.00 13.12  ? 1912 LYS A NZ    1 
ATOM   3671  N  N     . THR A 1 1913 ? 160.829 175.590 140.309 1.00 5.60   ? 1913 THR A N     1 
ATOM   3672  C  CA    . THR A 1 1913 ? 159.465 176.098 140.420 1.00 5.44   ? 1913 THR A CA    1 
ATOM   3673  C  C     . THR A 1 1913 ? 159.004 176.729 139.110 1.00 10.32  ? 1913 THR A C     1 
ATOM   3674  O  O     . THR A 1 1913 ? 157.876 176.499 138.658 1.00 12.21  ? 1913 THR A O     1 
ATOM   3675  C  CB    . THR A 1 1913 ? 159.374 177.102 141.572 1.00 7.63   ? 1913 THR A CB    1 
ATOM   3676  O  OG1   . THR A 1 1913 ? 159.281 176.392 142.813 1.00 18.80  ? 1913 THR A OG1   1 
ATOM   3677  C  CG2   . THR A 1 1913 ? 158.152 177.996 141.419 1.00 9.49   ? 1913 THR A CG2   1 
ATOM   3678  N  N     . GLU A 1 1914 ? 159.875 177.520 138.477 1.00 7.33   ? 1914 GLU A N     1 
ATOM   3679  C  CA    . GLU A 1 1914 ? 159.514 178.151 137.211 1.00 5.09   ? 1914 GLU A CA    1 
ATOM   3680  C  C     . GLU A 1 1914 ? 159.301 177.116 136.116 1.00 4.21   ? 1914 GLU A C     1 
ATOM   3681  O  O     . GLU A 1 1914 ? 158.476 177.315 135.217 1.00 6.68   ? 1914 GLU A O     1 
ATOM   3682  C  CB    . GLU A 1 1914 ? 160.589 179.154 136.797 1.00 11.01  ? 1914 GLU A CB    1 
ATOM   3683  C  CG    . GLU A 1 1914 ? 160.712 180.355 137.715 1.00 12.57  ? 1914 GLU A CG    1 
ATOM   3684  C  CD    . GLU A 1 1914 ? 159.388 181.050 137.946 1.00 15.90  ? 1914 GLU A CD    1 
ATOM   3685  O  OE1   . GLU A 1 1914 ? 158.770 181.495 136.956 1.00 15.64  ? 1914 GLU A OE1   1 
ATOM   3686  O  OE2   . GLU A 1 1914 ? 158.967 181.156 139.116 1.00 15.86  ? 1914 GLU A OE2   1 
ATOM   3687  N  N     . SER A 1 1915 ? 160.042 176.007 136.169 1.00 4.49   ? 1915 SER A N     1 
ATOM   3688  C  CA    . SER A 1 1915 ? 159.909 174.971 135.147 1.00 3.11   ? 1915 SER A CA    1 
ATOM   3689  C  C     . SER A 1 1915 ? 158.513 174.362 135.160 1.00 3.34   ? 1915 SER A C     1 
ATOM   3690  O  O     . SER A 1 1915 ? 157.933 174.088 134.104 1.00 3.12   ? 1915 SER A O     1 
ATOM   3691  C  CB    . SER A 1 1915 ? 160.970 173.891 135.357 1.00 3.21   ? 1915 SER A CB    1 
ATOM   3692  O  OG    . SER A 1 1915 ? 162.269 174.404 135.129 1.00 6.02   ? 1915 SER A OG    1 
ATOM   3693  N  N     . VAL A 1 1916 ? 157.963 174.133 136.354 1.00 4.94   ? 1916 VAL A N     1 
ATOM   3694  C  CA    . VAL A 1 1916 ? 156.622 173.564 136.460 1.00 3.07   ? 1916 VAL A CA    1 
ATOM   3695  C  C     . VAL A 1 1916 ? 155.589 174.535 135.902 1.00 3.55   ? 1916 VAL A C     1 
ATOM   3696  O  O     . VAL A 1 1916 ? 154.684 174.146 135.155 1.00 4.61   ? 1916 VAL A O     1 
ATOM   3697  C  CB    . VAL A 1 1916 ? 156.313 173.187 137.920 1.00 3.00   ? 1916 VAL A CB    1 
ATOM   3698  C  CG1   . VAL A 1 1916 ? 154.916 172.602 138.034 1.00 2.85   ? 1916 VAL A CG1   1 
ATOM   3699  C  CG2   . VAL A 1 1916 ? 157.351 172.210 138.447 1.00 4.87   ? 1916 VAL A CG2   1 
ATOM   3700  N  N     . LYS A 1 1917 ? 155.705 175.814 136.265 1.00 3.51   ? 1917 LYS A N     1 
ATOM   3701  C  CA    . LYS A 1 1917 ? 154.792 176.819 135.731 1.00 4.71   ? 1917 LYS A CA    1 
ATOM   3702  C  C     . LYS A 1 1917 ? 154.970 176.979 134.227 1.00 4.77   ? 1917 LYS A C     1 
ATOM   3703  O  O     . LYS A 1 1917 ? 153.990 177.098 133.483 1.00 7.96   ? 1917 LYS A O     1 
ATOM   3704  C  CB    . LYS A 1 1917 ? 155.005 178.156 136.439 1.00 6.33   ? 1917 LYS A CB    1 
ATOM   3705  C  CG    . LYS A 1 1917 ? 154.714 178.127 137.926 1.00 9.50   ? 1917 LYS A CG    1 
ATOM   3706  C  CD    . LYS A 1 1917 ? 154.692 179.532 138.501 1.00 14.62  ? 1917 LYS A CD    1 
ATOM   3707  C  CE    . LYS A 1 1917 ? 155.998 180.258 138.243 1.00 12.54  ? 1917 LYS A CE    1 
ATOM   3708  N  NZ    . LYS A 1 1917 ? 155.964 181.653 138.762 1.00 14.33  ? 1917 LYS A NZ    1 
ATOM   3709  N  N     . ALA A 1 1918 ? 156.221 176.983 133.762 1.00 3.73   ? 1918 ALA A N     1 
ATOM   3710  C  CA    . ALA A 1 1918 ? 156.484 177.183 132.340 1.00 3.07   ? 1918 ALA A CA    1 
ATOM   3711  C  C     . ALA A 1 1918 ? 155.888 176.059 131.504 1.00 3.79   ? 1918 ALA A C     1 
ATOM   3712  O  O     . ALA A 1 1918 ? 155.324 176.306 130.432 1.00 7.09   ? 1918 ALA A O     1 
ATOM   3713  C  CB    . ALA A 1 1918 ? 157.988 177.302 132.096 1.00 3.73   ? 1918 ALA A CB    1 
ATOM   3714  N  N     . LEU A 1 1919 ? 156.004 174.816 131.975 1.00 3.00   ? 1919 LEU A N     1 
ATOM   3715  C  CA    . LEU A 1 1919 ? 155.389 173.705 131.258 1.00 2.88   ? 1919 LEU A CA    1 
ATOM   3716  C  C     . LEU A 1 1919 ? 153.869 173.772 131.340 1.00 3.73   ? 1919 LEU A C     1 
ATOM   3717  O  O     . LEU A 1 1919 ? 153.174 173.465 130.364 1.00 6.38   ? 1919 LEU A O     1 
ATOM   3718  C  CB    . LEU A 1 1919 ? 155.901 172.375 131.809 1.00 2.96   ? 1919 LEU A CB    1 
ATOM   3719  C  CG    . LEU A 1 1919 ? 155.300 171.116 131.181 1.00 1.90   ? 1919 LEU A CG    1 
ATOM   3720  C  CD1   . LEU A 1 1919 ? 155.614 171.064 129.694 1.00 3.95   ? 1919 LEU A CD1   1 
ATOM   3721  C  CD2   . LEU A 1 1919 ? 155.803 169.868 131.880 1.00 2.41   ? 1919 LEU A CD2   1 
ATOM   3722  N  N     . GLY A 1 1920 ? 153.334 174.171 132.496 1.00 3.46   ? 1920 GLY A N     1 
ATOM   3723  C  CA    . GLY A 1 1920 ? 151.894 174.322 132.620 1.00 2.42   ? 1920 GLY A CA    1 
ATOM   3724  C  C     . GLY A 1 1920 ? 151.348 175.444 131.760 1.00 3.27   ? 1920 GLY A C     1 
ATOM   3725  O  O     . GLY A 1 1920 ? 150.292 175.305 131.137 1.00 5.48   ? 1920 GLY A O     1 
ATOM   3726  N  N     . HIS A 1 1921 ? 152.055 176.577 131.719 1.00 4.36   ? 1921 HIS A N     1 
ATOM   3727  C  CA    . HIS A 1 1921 ? 151.659 177.661 130.828 1.00 5.61   ? 1921 HIS A CA    1 
ATOM   3728  C  C     . HIS A 1 1921 ? 151.755 177.236 129.370 1.00 4.39   ? 1921 HIS A C     1 
ATOM   3729  O  O     . HIS A 1 1921 ? 150.956 177.684 128.539 1.00 6.37   ? 1921 HIS A O     1 
ATOM   3730  C  CB    . HIS A 1 1921 ? 152.527 178.897 131.074 1.00 6.54   ? 1921 HIS A CB    1 
ATOM   3731  C  CG    . HIS A 1 1921 ? 152.396 179.465 132.453 1.00 13.12  ? 1921 HIS A CG    1 
ATOM   3732  N  ND1   . HIS A 1 1921 ? 151.367 179.124 133.304 1.00 15.73  ? 1921 HIS A ND1   1 
ATOM   3733  C  CD2   . HIS A 1 1921 ? 153.166 180.350 133.129 1.00 16.55  ? 1921 HIS A CD2   1 
ATOM   3734  C  CE1   . HIS A 1 1921 ? 151.509 179.775 134.445 1.00 17.47  ? 1921 HIS A CE1   1 
ATOM   3735  N  NE2   . HIS A 1 1921 ? 152.593 180.525 134.365 1.00 17.61  ? 1921 HIS A NE2   1 
ATOM   3736  N  N     . GLN A 1 1922 ? 152.723 176.378 129.046 1.00 2.97   ? 1922 GLN A N     1 
ATOM   3737  C  CA    . GLN A 1 1922 ? 152.872 175.895 127.680 1.00 3.92   ? 1922 GLN A CA    1 
ATOM   3738  C  C     . GLN A 1 1922 ? 151.694 175.025 127.262 1.00 5.56   ? 1922 GLN A C     1 
ATOM   3739  O  O     . GLN A 1 1922 ? 151.324 175.004 126.083 1.00 7.11   ? 1922 GLN A O     1 
ATOM   3740  C  CB    . GLN A 1 1922 ? 154.181 175.120 127.552 1.00 4.89   ? 1922 GLN A CB    1 
ATOM   3741  C  CG    . GLN A 1 1922 ? 154.475 174.633 126.158 1.00 7.42   ? 1922 GLN A CG    1 
ATOM   3742  C  CD    . GLN A 1 1922 ? 155.728 175.251 125.591 1.00 10.87  ? 1922 GLN A CD    1 
ATOM   3743  O  OE1   . GLN A 1 1922 ? 156.676 175.544 126.319 1.00 14.33  ? 1922 GLN A OE1   1 
ATOM   3744  N  NE2   . GLN A 1 1922 ? 155.749 175.440 124.283 1.00 12.01  ? 1922 GLN A NE2   1 
ATOM   3745  N  N     . LEU A 1 1923 ? 151.100 174.299 128.205 1.00 4.97   ? 1923 LEU A N     1 
ATOM   3746  C  CA    . LEU A 1 1923 ? 149.908 173.503 127.951 1.00 3.53   ? 1923 LEU A CA    1 
ATOM   3747  C  C     . LEU A 1 1923 ? 148.622 174.267 128.230 1.00 4.04   ? 1923 LEU A C     1 
ATOM   3748  O  O     . LEU A 1 1923 ? 147.541 173.673 128.174 1.00 7.56   ? 1923 LEU A O     1 
ATOM   3749  C  CB    . LEU A 1 1923 ? 149.939 172.218 128.785 1.00 3.83   ? 1923 LEU A CB    1 
ATOM   3750  C  CG    . LEU A 1 1923 ? 151.214 171.380 128.690 1.00 3.36   ? 1923 LEU A CG    1 
ATOM   3751  C  CD1   . LEU A 1 1923 ? 151.333 170.442 129.878 1.00 3.09   ? 1923 LEU A CD1   1 
ATOM   3752  C  CD2   . LEU A 1 1923 ? 151.243 170.600 127.386 1.00 6.47   ? 1923 LEU A CD2   1 
ATOM   3753  N  N     . GLY A 1 1924 ? 148.712 175.559 128.524 1.00 3.25   ? 1924 GLY A N     1 
ATOM   3754  C  CA    . GLY A 1 1924 ? 147.531 176.349 128.823 1.00 4.20   ? 1924 GLY A CA    1 
ATOM   3755  C  C     . GLY A 1 1924 ? 146.850 175.948 130.111 1.00 7.40   ? 1924 GLY A C     1 
ATOM   3756  O  O     . GLY A 1 1924 ? 145.615 175.970 130.190 1.00 10.50  ? 1924 GLY A O     1 
ATOM   3757  N  N     . ARG A 1 1925 ? 147.624 175.588 131.127 1.00 7.08   ? 1925 ARG A N     1 
ATOM   3758  C  CA    . ARG A 1 1925 ? 147.094 175.123 132.397 1.00 4.82   ? 1925 ARG A CA    1 
ATOM   3759  C  C     . ARG A 1 1925 ? 147.193 176.217 133.451 1.00 6.91   ? 1925 ARG A C     1 
ATOM   3760  O  O     . ARG A 1 1925 ? 148.101 177.052 133.434 1.00 7.46   ? 1925 ARG A O     1 
ATOM   3761  C  CB    . ARG A 1 1925 ? 147.839 173.872 132.877 1.00 3.64   ? 1925 ARG A CB    1 
ATOM   3762  C  CG    . ARG A 1 1925 ? 147.786 172.709 131.904 1.00 3.06   ? 1925 ARG A CG    1 
ATOM   3763  C  CD    . ARG A 1 1925 ? 146.439 172.014 131.957 1.00 8.87   ? 1925 ARG A CD    1 
ATOM   3764  N  NE    . ARG A 1 1925 ? 146.489 170.674 131.387 1.00 11.09  ? 1925 ARG A NE    1 
ATOM   3765  C  CZ    . ARG A 1 1925 ? 146.431 170.412 130.089 1.00 11.48  ? 1925 ARG A CZ    1 
ATOM   3766  N  NH1   . ARG A 1 1925 ? 146.326 171.379 129.193 1.00 11.45  ? 1925 ARG A NH1   1 
ATOM   3767  N  NH2   . ARG A 1 1925 ? 146.479 169.147 129.680 1.00 10.96  ? 1925 ARG A NH2   1 
ATOM   3768  N  N     . PHE A 1 1926 ? 146.237 176.198 134.375 1.00 9.79   ? 1926 PHE A N     1 
ATOM   3769  C  CA    . PHE A 1 1926 ? 146.261 177.064 135.548 1.00 6.73   ? 1926 PHE A CA    1 
ATOM   3770  C  C     . PHE A 1 1926 ? 147.130 176.389 136.602 1.00 5.03   ? 1926 PHE A C     1 
ATOM   3771  O  O     . PHE A 1 1926 ? 146.726 175.390 137.205 1.00 6.22   ? 1926 PHE A O     1 
ATOM   3772  C  CB    . PHE A 1 1926 ? 144.844 177.316 136.059 1.00 10.05  ? 1926 PHE A CB    1 
ATOM   3773  C  CG    . PHE A 1 1926 ? 144.760 178.319 137.183 1.00 11.73  ? 1926 PHE A CG    1 
ATOM   3774  C  CD1   . PHE A 1 1926 ? 145.831 179.139 137.495 1.00 11.09  ? 1926 PHE A CD1   1 
ATOM   3775  C  CD2   . PHE A 1 1926 ? 143.593 178.447 137.918 1.00 11.06  ? 1926 PHE A CD2   1 
ATOM   3776  C  CE1   . PHE A 1 1926 ? 145.746 180.055 138.524 1.00 13.20  ? 1926 PHE A CE1   1 
ATOM   3777  C  CE2   . PHE A 1 1926 ? 143.500 179.364 138.946 1.00 14.86  ? 1926 PHE A CE2   1 
ATOM   3778  C  CZ    . PHE A 1 1926 ? 144.579 180.169 139.249 1.00 16.84  ? 1926 PHE A CZ    1 
ATOM   3779  N  N     . VAL A 1 1927 ? 148.322 176.931 136.820 1.00 5.99   ? 1927 VAL A N     1 
ATOM   3780  C  CA    . VAL A 1 1927 ? 149.276 176.379 137.772 1.00 4.83   ? 1927 VAL A CA    1 
ATOM   3781  C  C     . VAL A 1 1927 ? 149.197 177.200 139.049 1.00 5.04   ? 1927 VAL A C     1 
ATOM   3782  O  O     . VAL A 1 1927 ? 149.425 178.415 139.032 1.00 7.33   ? 1927 VAL A O     1 
ATOM   3783  C  CB    . VAL A 1 1927 ? 150.703 176.378 137.203 1.00 5.51   ? 1927 VAL A CB    1 
ATOM   3784  C  CG1   . VAL A 1 1927 ? 151.653 175.682 138.163 1.00 4.25   ? 1927 VAL A CG1   1 
ATOM   3785  C  CG2   . VAL A 1 1927 ? 150.729 175.705 135.841 1.00 3.97   ? 1927 VAL A CG2   1 
ATOM   3786  N  N     . LEU A 1 1928 ? 148.877 176.540 140.156 1.00 5.88   ? 1928 LEU A N     1 
ATOM   3787  C  CA    . LEU A 1 1928 ? 148.797 177.190 141.454 1.00 5.68   ? 1928 LEU A CA    1 
ATOM   3788  C  C     . LEU A 1 1928 ? 150.009 176.800 142.285 1.00 5.80   ? 1928 LEU A C     1 
ATOM   3789  O  O     . LEU A 1 1928 ? 150.253 175.612 142.520 1.00 7.61   ? 1928 LEU A O     1 
ATOM   3790  C  CB    . LEU A 1 1928 ? 147.506 176.817 142.183 1.00 5.98   ? 1928 LEU A CB    1 
ATOM   3791  C  CG    . LEU A 1 1928 ? 146.229 177.524 141.723 1.00 7.36   ? 1928 LEU A CG    1 
ATOM   3792  C  CD1   . LEU A 1 1928 ? 145.692 176.920 140.440 1.00 6.75   ? 1928 LEU A CD1   1 
ATOM   3793  C  CD2   . LEU A 1 1928 ? 145.175 177.492 142.811 1.00 10.63  ? 1928 LEU A CD2   1 
ATOM   3794  N  N     . VAL A 1 1929 ? 150.761 177.802 142.725 1.00 7.47   ? 1929 VAL A N     1 
ATOM   3795  C  CA    . VAL A 1 1929 ? 151.978 177.606 143.502 1.00 6.27   ? 1929 VAL A CA    1 
ATOM   3796  C  C     . VAL A 1 1929 ? 151.618 177.654 144.978 1.00 8.69   ? 1929 VAL A C     1 
ATOM   3797  O  O     . VAL A 1 1929 ? 150.930 178.578 145.427 1.00 11.16  ? 1929 VAL A O     1 
ATOM   3798  C  CB    . VAL A 1 1929 ? 153.032 178.669 143.153 1.00 7.91   ? 1929 VAL A CB    1 
ATOM   3799  C  CG1   . VAL A 1 1929 ? 154.185 178.623 144.134 1.00 11.37  ? 1929 VAL A CG1   1 
ATOM   3800  C  CG2   . VAL A 1 1929 ? 153.530 178.465 141.737 1.00 7.65   ? 1929 VAL A CG2   1 
ATOM   3801  N  N     . PHE A 1 1930 ? 152.072 176.656 145.731 1.00 8.84   ? 1930 PHE A N     1 
ATOM   3802  C  CA    . PHE A 1 1930 ? 151.826 176.575 147.163 1.00 7.77   ? 1930 PHE A CA    1 
ATOM   3803  C  C     . PHE A 1 1930 ? 153.155 176.461 147.892 1.00 9.63   ? 1930 PHE A C     1 
ATOM   3804  O  O     . PHE A 1 1930 ? 153.917 175.518 147.658 1.00 15.06  ? 1930 PHE A O     1 
ATOM   3805  C  CB    . PHE A 1 1930 ? 150.933 175.379 147.503 1.00 9.20   ? 1930 PHE A CB    1 
ATOM   3806  C  CG    . PHE A 1 1930 ? 149.578 175.438 146.862 1.00 7.58   ? 1930 PHE A CG    1 
ATOM   3807  C  CD1   . PHE A 1 1930 ? 148.565 176.196 147.421 1.00 5.65   ? 1930 PHE A CD1   1 
ATOM   3808  C  CD2   . PHE A 1 1930 ? 149.321 174.739 145.696 1.00 7.59   ? 1930 PHE A CD2   1 
ATOM   3809  C  CE1   . PHE A 1 1930 ? 147.321 176.254 146.832 1.00 6.47   ? 1930 PHE A CE1   1 
ATOM   3810  C  CE2   . PHE A 1 1930 ? 148.079 174.791 145.103 1.00 8.76   ? 1930 PHE A CE2   1 
ATOM   3811  C  CZ    . PHE A 1 1930 ? 147.077 175.551 145.671 1.00 8.65   ? 1930 PHE A CZ    1 
ATOM   3812  N  N     . ASN A 1 1931 ? 153.430 177.423 148.769 1.00 12.02  ? 1931 ASN A N     1 
ATOM   3813  C  CA    . ASN A 1 1931 ? 154.618 177.387 149.618 1.00 9.71   ? 1931 ASN A CA    1 
ATOM   3814  C  C     . ASN A 1 1931 ? 154.234 176.641 150.888 1.00 13.47  ? 1931 ASN A C     1 
ATOM   3815  O  O     . ASN A 1 1931 ? 153.586 177.195 151.779 1.00 18.47  ? 1931 ASN A O     1 
ATOM   3816  C  CB    . ASN A 1 1931 ? 155.121 178.796 149.911 1.00 11.70  ? 1931 ASN A CB    1 
ATOM   3817  C  CG    . ASN A 1 1931 ? 156.488 178.804 150.559 1.00 15.25  ? 1931 ASN A CG    1 
ATOM   3818  O  OD1   . ASN A 1 1931 ? 157.510 178.787 149.875 1.00 20.15  ? 1931 ASN A OD1   1 
ATOM   3819  N  ND2   . ASN A 1 1931 ? 156.515 178.830 151.885 1.00 16.65  ? 1931 ASN A ND2   1 
ATOM   3820  N  N     . CYS A 1 1932 ? 154.632 175.377 150.967 1.00 13.36  ? 1932 CYS A N     1 
ATOM   3821  C  CA    . CYS A 1 1932 ? 154.157 174.504 152.027 1.00 13.10  ? 1932 CYS A CA    1 
ATOM   3822  C  C     . CYS A 1 1932 ? 155.028 174.621 153.273 1.00 17.92  ? 1932 CYS A C     1 
ATOM   3823  O  O     . CYS A 1 1932 ? 156.222 174.924 153.201 1.00 24.36  ? 1932 CYS A O     1 
ATOM   3824  C  CB    . CYS A 1 1932 ? 154.134 173.057 151.540 1.00 16.23  ? 1932 CYS A CB    1 
ATOM   3825  S  SG    . CYS A 1 1932 ? 152.866 172.712 150.305 1.00 29.11  ? 1932 CYS A SG    1 
ATOM   3826  N  N     . ASP A 1 1933 ? 154.413 174.378 154.427 1.00 18.48  ? 1933 ASP A N     1 
ATOM   3827  C  CA    . ASP A 1 1933 ? 155.128 174.341 155.696 1.00 18.34  ? 1933 ASP A CA    1 
ATOM   3828  C  C     . ASP A 1 1933 ? 154.517 173.242 156.559 1.00 20.50  ? 1933 ASP A C     1 
ATOM   3829  O  O     . ASP A 1 1933 ? 153.716 172.430 156.087 1.00 23.70  ? 1933 ASP A O     1 
ATOM   3830  C  CB    . ASP A 1 1933 ? 155.110 175.716 156.379 1.00 21.94  ? 1933 ASP A CB    1 
ATOM   3831  C  CG    . ASP A 1 1933 ? 153.721 176.154 156.808 1.00 26.92  ? 1933 ASP A CG    1 
ATOM   3832  O  OD1   . ASP A 1 1933 ? 152.729 175.495 156.439 1.00 26.26  ? 1933 ASP A OD1   1 
ATOM   3833  O  OD2   . ASP A 1 1933 ? 153.622 177.172 157.524 1.00 28.95  ? 1933 ASP A OD2   1 
ATOM   3834  N  N     . GLU A 1 1934 ? 154.902 173.218 157.837 1.00 22.09  ? 1934 GLU A N     1 
ATOM   3835  C  CA    . GLU A 1 1934 ? 154.435 172.176 158.744 1.00 19.97  ? 1934 GLU A CA    1 
ATOM   3836  C  C     . GLU A 1 1934 ? 152.944 172.278 159.041 1.00 25.68  ? 1934 GLU A C     1 
ATOM   3837  O  O     . GLU A 1 1934 ? 152.359 171.310 159.538 1.00 30.00  ? 1934 GLU A O     1 
ATOM   3838  C  CB    . GLU A 1 1934 ? 155.232 172.225 160.047 1.00 19.80  ? 1934 GLU A CB    1 
ATOM   3839  C  CG    . GLU A 1 1934 ? 154.753 173.277 161.030 1.00 25.03  ? 1934 GLU A CG    1 
ATOM   3840  C  CD    . GLU A 1 1934 ? 155.525 174.578 160.910 1.00 31.13  ? 1934 GLU A CD    1 
ATOM   3841  O  OE1   . GLU A 1 1934 ? 156.557 174.596 160.206 1.00 33.84  ? 1934 GLU A OE1   1 
ATOM   3842  O  OE2   . GLU A 1 1934 ? 155.100 175.582 161.519 1.00 32.88  ? 1934 GLU A OE2   1 
ATOM   3843  N  N     . THR A 1 1935 ? 152.316 173.415 158.750 1.00 21.93  ? 1935 THR A N     1 
ATOM   3844  C  CA    . THR A 1 1935 ? 150.892 173.596 158.996 1.00 18.18  ? 1935 THR A CA    1 
ATOM   3845  C  C     . THR A 1 1935 ? 150.020 173.019 157.889 1.00 20.69  ? 1935 THR A C     1 
ATOM   3846  O  O     . THR A 1 1935 ? 148.792 173.029 158.020 1.00 23.02  ? 1935 THR A O     1 
ATOM   3847  C  CB    . THR A 1 1935 ? 150.571 175.083 159.179 1.00 18.21  ? 1935 THR A CB    1 
ATOM   3848  O  OG1   . THR A 1 1935 ? 150.841 175.786 157.961 1.00 21.51  ? 1935 THR A OG1   1 
ATOM   3849  C  CG2   . THR A 1 1935 ? 151.416 175.672 160.297 1.00 20.54  ? 1935 THR A CG2   1 
ATOM   3850  N  N     . PHE A 1 1936 ? 150.620 172.522 156.808 1.00 18.49  ? 1936 PHE A N     1 
ATOM   3851  C  CA    . PHE A 1 1936 ? 149.880 171.892 155.714 1.00 23.88  ? 1936 PHE A CA    1 
ATOM   3852  C  C     . PHE A 1 1936 ? 149.608 170.442 156.101 1.00 26.32  ? 1936 PHE A C     1 
ATOM   3853  O  O     . PHE A 1 1936 ? 150.328 169.513 155.725 1.00 31.91  ? 1936 PHE A O     1 
ATOM   3854  C  CB    . PHE A 1 1936 ? 150.664 171.987 154.411 1.00 22.85  ? 1936 PHE A CB    1 
ATOM   3855  C  CG    . PHE A 1 1936 ? 150.498 173.295 153.692 1.00 18.45  ? 1936 PHE A CG    1 
ATOM   3856  C  CD1   . PHE A 1 1936 ? 150.900 174.480 154.280 1.00 16.46  ? 1936 PHE A CD1   1 
ATOM   3857  C  CD2   . PHE A 1 1936 ? 149.954 173.336 152.420 1.00 21.50  ? 1936 PHE A CD2   1 
ATOM   3858  C  CE1   . PHE A 1 1936 ? 150.753 175.683 153.621 1.00 16.41  ? 1936 PHE A CE1   1 
ATOM   3859  C  CE2   . PHE A 1 1936 ? 149.806 174.536 151.754 1.00 22.31  ? 1936 PHE A CE2   1 
ATOM   3860  C  CZ    . PHE A 1 1936 ? 150.206 175.711 152.356 1.00 18.16  ? 1936 PHE A CZ    1 
ATOM   3861  N  N     . ASP A 1 1937 ? 148.543 170.247 156.873 1.00 18.91  ? 1937 ASP A N     1 
ATOM   3862  C  CA    . ASP A 1 1937 ? 148.231 168.931 157.413 1.00 18.29  ? 1937 ASP A CA    1 
ATOM   3863  C  C     . ASP A 1 1937 ? 147.329 168.168 156.445 1.00 18.67  ? 1937 ASP A C     1 
ATOM   3864  O  O     . ASP A 1 1937 ? 147.124 168.565 155.295 1.00 20.05  ? 1937 ASP A O     1 
ATOM   3865  C  CB    . ASP A 1 1937 ? 147.611 169.057 158.803 1.00 23.73  ? 1937 ASP A CB    1 
ATOM   3866  C  CG    . ASP A 1 1937 ? 146.467 170.048 158.848 1.00 28.60  ? 1937 ASP A CG    1 
ATOM   3867  O  OD1   . ASP A 1 1937 ? 146.109 170.597 157.789 1.00 27.26  ? 1937 ASP A OD1   1 
ATOM   3868  O  OD2   . ASP A 1 1937 ? 145.925 170.278 159.948 1.00 36.08  ? 1937 ASP A OD2   1 
ATOM   3869  N  N     . PHE A 1 1938 ? 146.784 167.043 156.917 1.00 18.18  ? 1938 PHE A N     1 
ATOM   3870  C  CA    . PHE A 1 1938 ? 145.972 166.181 156.065 1.00 15.01  ? 1938 PHE A CA    1 
ATOM   3871  C  C     . PHE A 1 1938 ? 144.715 166.893 155.580 1.00 15.85  ? 1938 PHE A C     1 
ATOM   3872  O  O     . PHE A 1 1938 ? 144.341 166.780 154.407 1.00 17.14  ? 1938 PHE A O     1 
ATOM   3873  C  CB    . PHE A 1 1938 ? 145.611 164.905 156.827 1.00 14.71  ? 1938 PHE A CB    1 
ATOM   3874  C  CG    . PHE A 1 1938 ? 144.743 163.955 156.053 1.00 13.16  ? 1938 PHE A CG    1 
ATOM   3875  C  CD1   . PHE A 1 1938 ? 145.288 163.132 155.084 1.00 12.63  ? 1938 PHE A CD1   1 
ATOM   3876  C  CD2   . PHE A 1 1938 ? 143.385 163.878 156.305 1.00 13.90  ? 1938 PHE A CD2   1 
ATOM   3877  C  CE1   . PHE A 1 1938 ? 144.493 162.254 154.376 1.00 13.38  ? 1938 PHE A CE1   1 
ATOM   3878  C  CE2   . PHE A 1 1938 ? 142.584 163.003 155.599 1.00 13.72  ? 1938 PHE A CE2   1 
ATOM   3879  C  CZ    . PHE A 1 1938 ? 143.140 162.189 154.632 1.00 13.20  ? 1938 PHE A CZ    1 
ATOM   3880  N  N     . GLN A 1 1939 ? 144.048 167.632 156.468 1.00 17.13  ? 1939 GLN A N     1 
ATOM   3881  C  CA    . GLN A 1 1939 ? 142.796 168.281 156.093 1.00 18.91  ? 1939 GLN A CA    1 
ATOM   3882  C  C     . GLN A 1 1939 ? 143.035 169.468 155.167 1.00 17.94  ? 1939 GLN A C     1 
ATOM   3883  O  O     . GLN A 1 1939 ? 142.309 169.648 154.182 1.00 17.81  ? 1939 GLN A O     1 
ATOM   3884  C  CB    . GLN A 1 1939 ? 142.040 168.721 157.344 1.00 23.14  ? 1939 GLN A CB    1 
ATOM   3885  C  CG    . GLN A 1 1939 ? 141.709 167.586 158.296 1.00 24.60  ? 1939 GLN A CG    1 
ATOM   3886  C  CD    . GLN A 1 1939 ? 140.345 167.744 158.932 1.00 37.30  ? 1939 GLN A CD    1 
ATOM   3887  O  OE1   . GLN A 1 1939 ? 140.231 168.027 160.125 1.00 44.67  ? 1939 GLN A OE1   1 
ATOM   3888  N  NE2   . GLN A 1 1939 ? 139.298 167.568 158.135 1.00 32.58  ? 1939 GLN A NE2   1 
ATOM   3889  N  N     . ALA A 1 1940 ? 144.038 170.296 155.472 1.00 17.62  ? 1940 ALA A N     1 
ATOM   3890  C  CA    . ALA A 1 1940 ? 144.300 171.470 154.645 1.00 13.95  ? 1940 ALA A CA    1 
ATOM   3891  C  C     . ALA A 1 1940 ? 144.760 171.076 153.248 1.00 14.84  ? 1940 ALA A C     1 
ATOM   3892  O  O     . ALA A 1 1940 ? 144.295 171.642 152.252 1.00 14.80  ? 1940 ALA A O     1 
ATOM   3893  C  CB    . ALA A 1 1940 ? 145.339 172.367 155.316 1.00 18.23  ? 1940 ALA A CB    1 
ATOM   3894  N  N     . MET A 1 1941 ? 145.672 170.107 153.152 1.00 16.12  ? 1941 MET A N     1 
ATOM   3895  C  CA    . MET A 1 1941 ? 146.156 169.683 151.843 1.00 12.54  ? 1941 MET A CA    1 
ATOM   3896  C  C     . MET A 1 1941 ? 145.074 168.943 151.068 1.00 12.80  ? 1941 MET A C     1 
ATOM   3897  O  O     . MET A 1 1941 ? 145.002 169.044 149.838 1.00 15.80  ? 1941 MET A O     1 
ATOM   3898  C  CB    . MET A 1 1941 ? 147.399 168.809 151.993 1.00 13.24  ? 1941 MET A CB    1 
ATOM   3899  C  CG    . MET A 1 1941 ? 148.696 169.592 152.085 1.00 18.75  ? 1941 MET A CG    1 
ATOM   3900  S  SD    . MET A 1 1941 ? 149.548 169.658 150.500 1.00 26.42  ? 1941 MET A SD    1 
ATOM   3901  C  CE    . MET A 1 1941 ? 149.656 167.916 150.106 1.00 23.95  ? 1941 MET A CE    1 
ATOM   3902  N  N     . GLY A 1 1942 ? 144.228 168.188 151.770 1.00 13.49  ? 1942 GLY A N     1 
ATOM   3903  C  CA    . GLY A 1 1942 ? 143.137 167.504 151.098 1.00 12.98  ? 1942 GLY A CA    1 
ATOM   3904  C  C     . GLY A 1 1942 ? 142.119 168.467 150.517 1.00 13.03  ? 1942 GLY A C     1 
ATOM   3905  O  O     . GLY A 1 1942 ? 141.569 168.227 149.439 1.00 16.97  ? 1942 GLY A O     1 
ATOM   3906  N  N     . ARG A 1 1943 ? 141.851 169.565 151.226 1.00 13.05  ? 1943 ARG A N     1 
ATOM   3907  C  CA    . ARG A 1 1943 ? 140.929 170.571 150.712 1.00 9.28   ? 1943 ARG A CA    1 
ATOM   3908  C  C     . ARG A 1 1943 ? 141.516 171.291 149.504 1.00 11.10  ? 1943 ARG A C     1 
ATOM   3909  O  O     . ARG A 1 1943 ? 140.784 171.663 148.580 1.00 13.64  ? 1943 ARG A O     1 
ATOM   3910  C  CB    . ARG A 1 1943 ? 140.574 171.566 151.815 1.00 12.18  ? 1943 ARG A CB    1 
ATOM   3911  C  CG    . ARG A 1 1943 ? 139.439 172.506 151.459 1.00 16.68  ? 1943 ARG A CG    1 
ATOM   3912  C  CD    . ARG A 1 1943 ? 139.082 173.400 152.630 1.00 17.26  ? 1943 ARG A CD    1 
ATOM   3913  N  NE    . ARG A 1 1943 ? 138.215 174.499 152.226 1.00 25.96  ? 1943 ARG A NE    1 
ATOM   3914  C  CZ    . ARG A 1 1943 ? 138.647 175.637 151.700 1.00 26.43  ? 1943 ARG A CZ    1 
ATOM   3915  N  NH1   . ARG A 1 1943 ? 139.936 175.857 151.494 1.00 24.44  ? 1943 ARG A NH1   1 
ATOM   3916  N  NH2   . ARG A 1 1943 ? 137.765 176.575 151.368 1.00 30.50  ? 1943 ARG A NH2   1 
ATOM   3917  N  N     . ILE A 1 1944 ? 142.835 171.503 149.498 1.00 10.64  ? 1944 ILE A N     1 
ATOM   3918  C  CA    . ILE A 1 1944 ? 143.490 172.095 148.334 1.00 8.68   ? 1944 ILE A CA    1 
ATOM   3919  C  C     . ILE A 1 1944 ? 143.345 171.179 147.126 1.00 10.20  ? 1944 ILE A C     1 
ATOM   3920  O  O     . ILE A 1 1944 ? 143.129 171.640 145.998 1.00 11.23  ? 1944 ILE A O     1 
ATOM   3921  C  CB    . ILE A 1 1944 ? 144.967 172.396 148.649 1.00 10.65  ? 1944 ILE A CB    1 
ATOM   3922  C  CG1   . ILE A 1 1944 ? 145.076 173.584 149.606 1.00 11.58  ? 1944 ILE A CG1   1 
ATOM   3923  C  CG2   . ILE A 1 1944 ? 145.750 172.677 147.375 1.00 7.78   ? 1944 ILE A CG2   1 
ATOM   3924  C  CD1   . ILE A 1 1944 ? 146.478 173.830 150.113 1.00 10.57  ? 1944 ILE A CD1   1 
ATOM   3925  N  N     . PHE A 1 1945 ? 143.453 169.866 147.345 1.00 8.62   ? 1945 PHE A N     1 
ATOM   3926  C  CA    . PHE A 1 1945 ? 143.270 168.911 146.256 1.00 10.21  ? 1945 PHE A CA    1 
ATOM   3927  C  C     . PHE A 1 1945 ? 141.861 168.987 145.686 1.00 13.11  ? 1945 PHE A C     1 
ATOM   3928  O  O     . PHE A 1 1945 ? 141.668 168.864 144.471 1.00 17.39  ? 1945 PHE A O     1 
ATOM   3929  C  CB    . PHE A 1 1945 ? 143.570 167.495 146.743 1.00 10.21  ? 1945 PHE A CB    1 
ATOM   3930  C  CG    . PHE A 1 1945 ? 145.031 167.216 146.937 1.00 12.62  ? 1945 PHE A CG    1 
ATOM   3931  C  CD1   . PHE A 1 1945 ? 145.988 168.011 146.330 1.00 11.96  ? 1945 PHE A CD1   1 
ATOM   3932  C  CD2   . PHE A 1 1945 ? 145.447 166.154 147.721 1.00 13.86  ? 1945 PHE A CD2   1 
ATOM   3933  C  CE1   . PHE A 1 1945 ? 147.332 167.754 146.505 1.00 12.03  ? 1945 PHE A CE1   1 
ATOM   3934  C  CE2   . PHE A 1 1945 ? 146.790 165.892 147.899 1.00 12.07  ? 1945 PHE A CE2   1 
ATOM   3935  C  CZ    . PHE A 1 1945 ? 147.733 166.693 147.291 1.00 12.83  ? 1945 PHE A CZ    1 
ATOM   3936  N  N     . VAL A 1 1946 ? 140.863 169.185 146.550 1.00 11.50  ? 1946 VAL A N     1 
ATOM   3937  C  CA    . VAL A 1 1946 ? 139.476 169.253 146.094 1.00 10.88  ? 1946 VAL A CA    1 
ATOM   3938  C  C     . VAL A 1 1946 ? 139.299 170.401 145.108 1.00 12.33  ? 1946 VAL A C     1 
ATOM   3939  O  O     . VAL A 1 1946 ? 138.672 170.246 144.054 1.00 16.37  ? 1946 VAL A O     1 
ATOM   3940  C  CB    . VAL A 1 1946 ? 138.524 169.387 147.296 1.00 12.28  ? 1946 VAL A CB    1 
ATOM   3941  C  CG1   . VAL A 1 1946 ? 137.135 169.802 146.839 1.00 12.21  ? 1946 VAL A CG1   1 
ATOM   3942  C  CG2   . VAL A 1 1946 ? 138.468 168.083 148.076 1.00 14.36  ? 1946 VAL A CG2   1 
ATOM   3943  N  N     . GLY A 1 1947 ? 139.856 171.568 145.432 1.00 12.33  ? 1947 GLY A N     1 
ATOM   3944  C  CA    . GLY A 1 1947 ? 139.759 172.696 144.519 1.00 12.60  ? 1947 GLY A CA    1 
ATOM   3945  C  C     . GLY A 1 1947 ? 140.476 172.444 143.207 1.00 15.34  ? 1947 GLY A C     1 
ATOM   3946  O  O     . GLY A 1 1947 ? 139.963 172.761 142.131 1.00 18.70  ? 1947 GLY A O     1 
ATOM   3947  N  N     . LEU A 1 1948 ? 141.678 171.870 143.280 1.00 15.18  ? 1948 LEU A N     1 
ATOM   3948  C  CA    . LEU A 1 1948 ? 142.440 171.585 142.069 1.00 13.86  ? 1948 LEU A CA    1 
ATOM   3949  C  C     . LEU A 1 1948 ? 141.746 170.540 141.204 1.00 14.19  ? 1948 LEU A C     1 
ATOM   3950  O  O     . LEU A 1 1948 ? 141.712 170.670 139.975 1.00 17.35  ? 1948 LEU A O     1 
ATOM   3951  C  CB    . LEU A 1 1948 ? 143.850 171.125 142.437 1.00 13.00  ? 1948 LEU A CB    1 
ATOM   3952  C  CG    . LEU A 1 1948 ? 144.759 172.147 143.122 1.00 10.20  ? 1948 LEU A CG    1 
ATOM   3953  C  CD1   . LEU A 1 1948 ? 146.051 171.485 143.568 1.00 10.36  ? 1948 LEU A CD1   1 
ATOM   3954  C  CD2   . LEU A 1 1948 ? 145.044 173.317 142.199 1.00 5.69   ? 1948 LEU A CD2   1 
ATOM   3955  N  N     . CYS A 1 1949 ? 141.194 169.496 141.827 1.00 15.22  ? 1949 CYS A N     1 
ATOM   3956  C  CA    . CYS A 1 1949 ? 140.558 168.425 141.063 1.00 14.82  ? 1949 CYS A CA    1 
ATOM   3957  C  C     . CYS A 1 1949 ? 139.319 168.919 140.327 1.00 17.29  ? 1949 CYS A C     1 
ATOM   3958  O  O     . CYS A 1 1949 ? 139.096 168.560 139.165 1.00 25.51  ? 1949 CYS A O     1 
ATOM   3959  C  CB    . CYS A 1 1949 ? 140.202 167.262 141.988 1.00 18.32  ? 1949 CYS A CB    1 
ATOM   3960  S  SG    . CYS A 1 1949 ? 141.623 166.328 142.585 1.00 29.26  ? 1949 CYS A SG    1 
ATOM   3961  N  N     . GLN A 1 1950 ? 138.498 169.739 140.986 1.00 17.20  ? 1950 GLN A N     1 
ATOM   3962  C  CA    . GLN A 1 1950 ? 137.270 170.210 140.353 1.00 19.20  ? 1950 GLN A CA    1 
ATOM   3963  C  C     . GLN A 1 1950 ? 137.562 171.251 139.280 1.00 20.41  ? 1950 GLN A C     1 
ATOM   3964  O  O     . GLN A 1 1950 ? 136.927 171.252 138.219 1.00 24.76  ? 1950 GLN A O     1 
ATOM   3965  C  CB    . GLN A 1 1950 ? 136.317 170.774 141.406 1.00 24.73  ? 1950 GLN A CB    1 
ATOM   3966  C  CG    . GLN A 1 1950 ? 135.957 169.797 142.510 1.00 27.55  ? 1950 GLN A CG    1 
ATOM   3967  C  CD    . GLN A 1 1950 ? 134.479 169.796 142.832 1.00 32.00  ? 1950 GLN A CD    1 
ATOM   3968  O  OE1   . GLN A 1 1950 ? 133.864 168.740 142.978 1.00 40.74  ? 1950 GLN A OE1   1 
ATOM   3969  N  NE2   . GLN A 1 1950 ? 133.898 170.984 142.945 1.00 34.30  ? 1950 GLN A NE2   1 
ATOM   3970  N  N     . VAL A 1 1951 ? 138.515 172.148 139.538 1.00 18.19  ? 1951 VAL A N     1 
ATOM   3971  C  CA    . VAL A 1 1951 ? 138.862 173.164 138.548 1.00 14.44  ? 1951 VAL A CA    1 
ATOM   3972  C  C     . VAL A 1 1951 ? 139.578 172.533 137.361 1.00 17.77  ? 1951 VAL A C     1 
ATOM   3973  O  O     . VAL A 1 1951 ? 139.290 172.853 136.202 1.00 23.40  ? 1951 VAL A O     1 
ATOM   3974  C  CB    . VAL A 1 1951 ? 139.711 174.272 139.197 1.00 13.36  ? 1951 VAL A CB    1 
ATOM   3975  C  CG1   . VAL A 1 1951 ? 140.321 175.169 138.134 1.00 13.44  ? 1951 VAL A CG1   1 
ATOM   3976  C  CG2   . VAL A 1 1951 ? 138.870 175.090 140.161 1.00 19.09  ? 1951 VAL A CG2   1 
ATOM   3977  N  N     . GLY A 1 1952 ? 140.507 171.620 137.627 1.00 16.22  ? 1952 GLY A N     1 
ATOM   3978  C  CA    . GLY A 1 1952 ? 141.362 171.094 136.584 1.00 12.27  ? 1952 GLY A CA    1 
ATOM   3979  C  C     . GLY A 1 1952 ? 142.636 171.901 136.484 1.00 9.46   ? 1952 GLY A C     1 
ATOM   3980  O  O     . GLY A 1 1952 ? 143.077 172.265 135.390 1.00 14.09  ? 1952 GLY A O     1 
ATOM   3981  N  N     . ALA A 1 1953 ? 143.232 172.189 137.636 1.00 8.36   ? 1953 ALA A N     1 
ATOM   3982  C  CA    . ALA A 1 1953 ? 144.372 173.081 137.738 1.00 6.35   ? 1953 ALA A CA    1 
ATOM   3983  C  C     . ALA A 1 1953 ? 145.593 172.329 138.250 1.00 5.29   ? 1953 ALA A C     1 
ATOM   3984  O  O     . ALA A 1 1953 ? 145.484 171.291 138.908 1.00 9.31   ? 1953 ALA A O     1 
ATOM   3985  C  CB    . ALA A 1 1953 ? 144.062 174.266 138.660 1.00 6.99   ? 1953 ALA A CB    1 
ATOM   3986  N  N     . TRP A 1 1954 ? 146.764 172.871 137.932 1.00 4.56   ? 1954 TRP A N     1 
ATOM   3987  C  CA    . TRP A 1 1954 ? 148.030 172.301 138.366 1.00 3.71   ? 1954 TRP A CA    1 
ATOM   3988  C  C     . TRP A 1 1954 ? 148.402 172.860 139.731 1.00 3.53   ? 1954 TRP A C     1 
ATOM   3989  O  O     . TRP A 1 1954 ? 148.377 174.076 139.939 1.00 5.33   ? 1954 TRP A O     1 
ATOM   3990  C  CB    . TRP A 1 1954 ? 149.137 172.604 137.358 1.00 3.57   ? 1954 TRP A CB    1 
ATOM   3991  C  CG    . TRP A 1 1954 ? 149.148 171.689 136.181 1.00 2.43   ? 1954 TRP A CG    1 
ATOM   3992  C  CD1   . TRP A 1 1954 ? 148.102 170.963 135.696 1.00 3.18   ? 1954 TRP A CD1   1 
ATOM   3993  C  CD2   . TRP A 1 1954 ? 150.266 171.394 135.339 1.00 2.10   ? 1954 TRP A CD2   1 
ATOM   3994  N  NE1   . TRP A 1 1954 ? 148.497 170.236 134.600 1.00 3.32   ? 1954 TRP A NE1   1 
ATOM   3995  C  CE2   . TRP A 1 1954 ? 149.823 170.483 134.361 1.00 2.14   ? 1954 TRP A CE2   1 
ATOM   3996  C  CE3   . TRP A 1 1954 ? 151.599 171.815 135.316 1.00 1.93   ? 1954 TRP A CE3   1 
ATOM   3997  C  CZ2   . TRP A 1 1954 ? 150.665 169.984 133.371 1.00 2.08   ? 1954 TRP A CZ2   1 
ATOM   3998  C  CZ3   . TRP A 1 1954 ? 152.432 171.318 134.335 1.00 1.50   ? 1954 TRP A CZ3   1 
ATOM   3999  C  CH2   . TRP A 1 1954 ? 151.963 170.413 133.375 1.00 1.62   ? 1954 TRP A CH2   1 
ATOM   4000  N  N     . GLY A 1 1955 ? 148.738 171.970 140.658 1.00 4.15   ? 1955 GLY A N     1 
ATOM   4001  C  CA    . GLY A 1 1955 ? 149.185 172.391 141.968 1.00 5.12   ? 1955 GLY A CA    1 
ATOM   4002  C  C     . GLY A 1 1955 ? 150.651 172.096 142.196 1.00 6.43   ? 1955 GLY A C     1 
ATOM   4003  O  O     . GLY A 1 1955 ? 151.039 170.937 142.367 1.00 7.78   ? 1955 GLY A O     1 
ATOM   4004  N  N     . CYS A 1 1956 ? 151.478 173.137 142.198 1.00 5.34   ? 1956 CYS A N     1 
ATOM   4005  C  CA    . CYS A 1 1956 ? 152.911 173.002 142.436 1.00 4.49   ? 1956 CYS A CA    1 
ATOM   4006  C  C     . CYS A 1 1956 ? 153.161 173.298 143.909 1.00 5.69   ? 1956 CYS A C     1 
ATOM   4007  O  O     . CYS A 1 1956 ? 152.984 174.429 144.367 1.00 7.36   ? 1956 CYS A O     1 
ATOM   4008  C  CB    . CYS A 1 1956 ? 153.707 173.934 141.528 1.00 7.43   ? 1956 CYS A CB    1 
ATOM   4009  S  SG    . CYS A 1 1956 ? 155.498 173.715 141.621 1.00 18.17  ? 1956 CYS A SG    1 
ATOM   4010  N  N     . PHE A 1 1957 ? 153.571 172.275 144.652 1.00 6.48   ? 1957 PHE A N     1 
ATOM   4011  C  CA    . PHE A 1 1957 ? 153.812 172.390 146.085 1.00 6.93   ? 1957 PHE A CA    1 
ATOM   4012  C  C     . PHE A 1 1957 ? 155.317 172.424 146.318 1.00 9.19   ? 1957 PHE A C     1 
ATOM   4013  O  O     . PHE A 1 1957 ? 155.974 171.379 146.341 1.00 10.63  ? 1957 PHE A O     1 
ATOM   4014  C  CB    . PHE A 1 1957 ? 153.160 171.234 146.840 1.00 6.82   ? 1957 PHE A CB    1 
ATOM   4015  C  CG    . PHE A 1 1957 ? 151.669 171.164 146.671 1.00 7.21   ? 1957 PHE A CG    1 
ATOM   4016  C  CD1   . PHE A 1 1957 ? 151.111 170.471 145.610 1.00 7.32   ? 1957 PHE A CD1   1 
ATOM   4017  C  CD2   . PHE A 1 1957 ? 150.826 171.791 147.571 1.00 6.83   ? 1957 PHE A CD2   1 
ATOM   4018  C  CE1   . PHE A 1 1957 ? 149.742 170.407 145.451 1.00 5.90   ? 1957 PHE A CE1   1 
ATOM   4019  C  CE2   . PHE A 1 1957 ? 149.455 171.730 147.418 1.00 8.68   ? 1957 PHE A CE2   1 
ATOM   4020  C  CZ    . PHE A 1 1957 ? 148.912 171.036 146.356 1.00 9.39   ? 1957 PHE A CZ    1 
ATOM   4021  N  N     . ASP A 1 1958 ? 155.858 173.624 146.494 1.00 9.91   ? 1958 ASP A N     1 
ATOM   4022  C  CA    . ASP A 1 1958 ? 157.281 173.800 146.735 1.00 12.29  ? 1958 ASP A CA    1 
ATOM   4023  C  C     . ASP A 1 1958 ? 157.578 173.713 148.225 1.00 16.85  ? 1958 ASP A C     1 
ATOM   4024  O  O     . ASP A 1 1958 ? 156.728 174.004 149.071 1.00 20.46  ? 1958 ASP A O     1 
ATOM   4025  C  CB    . ASP A 1 1958 ? 157.764 175.136 146.175 1.00 16.84  ? 1958 ASP A CB    1 
ATOM   4026  C  CG    . ASP A 1 1958 ? 157.086 175.496 144.874 1.00 21.16  ? 1958 ASP A CG    1 
ATOM   4027  O  OD1   . ASP A 1 1958 ? 157.473 174.939 143.825 1.00 15.66  ? 1958 ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A 1 1958 ? 156.161 176.329 144.901 1.00 21.10  ? 1958 ASP A OD2   1 
ATOM   4029  N  N     . GLU A 1 1959 ? 158.809 173.306 148.536 1.00 16.80  ? 1959 GLU A N     1 
ATOM   4030  C  CA    . GLU A 1 1959 ? 159.212 173.015 149.910 1.00 17.49  ? 1959 GLU A CA    1 
ATOM   4031  C  C     . GLU A 1 1959 ? 158.263 171.996 150.532 1.00 12.60  ? 1959 GLU A C     1 
ATOM   4032  O  O     . GLU A 1 1959 ? 157.858 172.108 151.690 1.00 13.09  ? 1959 GLU A O     1 
ATOM   4033  C  CB    . GLU A 1 1959 ? 159.288 174.292 150.751 1.00 24.86  ? 1959 GLU A CB    1 
ATOM   4034  C  CG    . GLU A 1 1959 ? 160.591 175.075 150.618 1.00 28.60  ? 1959 GLU A CG    1 
ATOM   4035  C  CD    . GLU A 1 1959 ? 161.105 175.141 149.193 1.00 36.19  ? 1959 GLU A CD    1 
ATOM   4036  O  OE1   . GLU A 1 1959 ? 162.060 174.402 148.869 1.00 31.00  ? 1959 GLU A OE1   1 
ATOM   4037  O  OE2   . GLU A 1 1959 ? 160.558 175.933 148.397 1.00 28.33  ? 1959 GLU A OE2   1 
ATOM   4038  N  N     . PHE A 1 1960 ? 157.901 170.988 149.736 1.00 10.25  ? 1960 PHE A N     1 
ATOM   4039  C  CA    . PHE A 1 1960 ? 156.928 169.990 150.158 1.00 10.78  ? 1960 PHE A CA    1 
ATOM   4040  C  C     . PHE A 1 1960 ? 157.495 169.042 151.207 1.00 9.71   ? 1960 PHE A C     1 
ATOM   4041  O  O     . PHE A 1 1960 ? 156.726 168.354 151.886 1.00 10.34  ? 1960 PHE A O     1 
ATOM   4042  C  CB    . PHE A 1 1960 ? 156.431 169.227 148.926 1.00 11.20  ? 1960 PHE A CB    1 
ATOM   4043  C  CG    . PHE A 1 1960 ? 155.384 168.193 149.220 1.00 8.41   ? 1960 PHE A CG    1 
ATOM   4044  C  CD1   . PHE A 1 1960 ? 154.059 168.560 149.378 1.00 7.62   ? 1960 PHE A CD1   1 
ATOM   4045  C  CD2   . PHE A 1 1960 ? 155.715 166.852 149.291 1.00 7.15   ? 1960 PHE A CD2   1 
ATOM   4046  C  CE1   . PHE A 1 1960 ? 153.093 167.612 149.635 1.00 9.80   ? 1960 PHE A CE1   1 
ATOM   4047  C  CE2   . PHE A 1 1960 ? 154.750 165.899 149.542 1.00 9.73   ? 1960 PHE A CE2   1 
ATOM   4048  C  CZ    . PHE A 1 1960 ? 153.437 166.280 149.717 1.00 12.30  ? 1960 PHE A CZ    1 
ATOM   4049  N  N     . ASN A 1 1961 ? 158.817 169.004 151.366 1.00 10.89  ? 1961 ASN A N     1 
ATOM   4050  C  CA    . ASN A 1 1961 ? 159.435 168.256 152.452 1.00 9.32   ? 1961 ASN A CA    1 
ATOM   4051  C  C     . ASN A 1 1961 ? 159.386 169.002 153.779 1.00 13.22  ? 1961 ASN A C     1 
ATOM   4052  O  O     . ASN A 1 1961 ? 159.800 168.443 154.800 1.00 20.21  ? 1961 ASN A O     1 
ATOM   4053  C  CB    . ASN A 1 1961 ? 160.885 167.908 152.104 1.00 11.10  ? 1961 ASN A CB    1 
ATOM   4054  C  CG    . ASN A 1 1961 ? 161.661 169.095 151.573 1.00 17.91  ? 1961 ASN A CG    1 
ATOM   4055  O  OD1   . ASN A 1 1961 ? 161.091 170.148 151.287 1.00 21.84  ? 1961 ASN A OD1   1 
ATOM   4056  N  ND2   . ASN A 1 1961 ? 162.972 168.933 151.438 1.00 20.67  ? 1961 ASN A ND2   1 
ATOM   4057  N  N     . ARG A 1 1962 ? 158.899 170.245 153.790 1.00 11.98  ? 1962 ARG A N     1 
ATOM   4058  C  CA    . ARG A 1 1962 ? 158.674 170.967 155.035 1.00 13.47  ? 1962 ARG A CA    1 
ATOM   4059  C  C     . ARG A 1 1962 ? 157.432 170.489 155.774 1.00 15.64  ? 1962 ARG A C     1 
ATOM   4060  O  O     . ARG A 1 1962 ? 157.216 170.900 156.919 1.00 22.29  ? 1962 ARG A O     1 
ATOM   4061  C  CB    . ARG A 1 1962 ? 158.576 172.472 154.764 1.00 15.82  ? 1962 ARG A CB    1 
ATOM   4062  C  CG    . ARG A 1 1962 ? 159.918 173.181 154.824 1.00 18.80  ? 1962 ARG A CG    1 
ATOM   4063  C  CD    . ARG A 1 1962 ? 159.873 174.585 154.241 1.00 18.81  ? 1962 ARG A CD    1 
ATOM   4064  N  NE    . ARG A 1 1962 ? 158.849 175.434 154.839 1.00 17.39  ? 1962 ARG A NE    1 
ATOM   4065  C  CZ    . ARG A 1 1962 ? 159.032 176.178 155.920 1.00 16.65  ? 1962 ARG A CZ    1 
ATOM   4066  N  NH1   . ARG A 1 1962 ? 160.169 176.148 156.596 1.00 17.45  ? 1962 ARG A NH1   1 
ATOM   4067  N  NH2   . ARG A 1 1962 ? 158.052 176.975 156.333 1.00 15.70  ? 1962 ARG A NH2   1 
ATOM   4068  N  N     . LEU A 1 1963 ? 156.618 169.642 155.151 1.00 13.81  ? 1963 LEU A N     1 
ATOM   4069  C  CA    . LEU A 1 1963 ? 155.520 168.996 155.849 1.00 11.90  ? 1963 LEU A CA    1 
ATOM   4070  C  C     . LEU A 1 1963 ? 156.061 168.009 156.877 1.00 15.10  ? 1963 LEU A C     1 
ATOM   4071  O  O     . LEU A 1 1963 ? 157.180 167.505 156.764 1.00 19.60  ? 1963 LEU A O     1 
ATOM   4072  C  CB    . LEU A 1 1963 ? 154.614 168.254 154.865 1.00 12.57  ? 1963 LEU A CB    1 
ATOM   4073  C  CG    . LEU A 1 1963 ? 153.446 168.979 154.202 1.00 15.66  ? 1963 LEU A CG    1 
ATOM   4074  C  CD1   . LEU A 1 1963 ? 153.952 169.898 153.115 1.00 15.04  ? 1963 LEU A CD1   1 
ATOM   4075  C  CD2   . LEU A 1 1963 ? 152.467 167.970 153.628 1.00 11.98  ? 1963 LEU A CD2   1 
ATOM   4076  N  N     . GLU A 1 1964 ? 155.251 167.739 157.895 1.00 19.67  ? 1964 GLU A N     1 
ATOM   4077  C  CA    . GLU A 1 1964 ? 155.606 166.710 158.861 1.00 16.98  ? 1964 GLU A CA    1 
ATOM   4078  C  C     . GLU A 1 1964 ? 155.544 165.333 158.209 1.00 15.21  ? 1964 GLU A C     1 
ATOM   4079  O  O     . GLU A 1 1964 ? 154.750 165.088 157.297 1.00 15.59  ? 1964 GLU A O     1 
ATOM   4080  C  CB    . GLU A 1 1964 ? 154.678 166.768 160.072 1.00 21.08  ? 1964 GLU A CB    1 
ATOM   4081  C  CG    . GLU A 1 1964 ? 154.778 168.065 160.855 1.00 23.59  ? 1964 GLU A CG    1 
ATOM   4082  C  CD    . GLU A 1 1964 ? 153.600 168.280 161.781 1.00 31.53  ? 1964 GLU A CD    1 
ATOM   4083  O  OE1   . GLU A 1 1964 ? 152.606 167.533 161.665 1.00 37.81  ? 1964 GLU A OE1   1 
ATOM   4084  O  OE2   . GLU A 1 1964 ? 153.667 169.198 162.625 1.00 26.94  ? 1964 GLU A OE2   1 
ATOM   4085  N  N     . GLU A 1 1965 ? 156.406 164.430 158.684 1.00 14.38  ? 1965 GLU A N     1 
ATOM   4086  C  CA    . GLU A 1 1965 ? 156.480 163.097 158.093 1.00 14.91  ? 1965 GLU A CA    1 
ATOM   4087  C  C     . GLU A 1 1965 ? 155.166 162.345 158.252 1.00 15.22  ? 1965 GLU A C     1 
ATOM   4088  O  O     . GLU A 1 1965 ? 154.748 161.613 157.347 1.00 13.21  ? 1965 GLU A O     1 
ATOM   4089  C  CB    . GLU A 1 1965 ? 157.629 162.305 158.716 1.00 16.91  ? 1965 GLU A CB    1 
ATOM   4090  C  CG    . GLU A 1 1965 ? 158.990 162.635 158.139 1.00 20.61  ? 1965 GLU A CG    1 
ATOM   4091  C  CD    . GLU A 1 1965 ? 160.022 161.566 158.432 1.00 32.25  ? 1965 GLU A CD    1 
ATOM   4092  O  OE1   . GLU A 1 1965 ? 159.740 160.378 158.170 1.00 31.33  ? 1965 GLU A OE1   1 
ATOM   4093  O  OE2   . GLU A 1 1965 ? 161.117 161.913 158.923 1.00 36.52  ? 1965 GLU A OE2   1 
ATOM   4094  N  N     . ARG A 1 1966 ? 154.505 162.504 159.400 1.00 14.59  ? 1966 ARG A N     1 
ATOM   4095  C  CA    . ARG A 1 1966 ? 153.200 161.878 159.584 1.00 14.14  ? 1966 ARG A CA    1 
ATOM   4096  C  C     . ARG A 1 1966 ? 152.178 162.452 158.610 1.00 13.10  ? 1966 ARG A C     1 
ATOM   4097  O  O     . ARG A 1 1966 ? 151.339 161.719 158.075 1.00 12.80  ? 1966 ARG A O     1 
ATOM   4098  C  CB    . ARG A 1 1966 ? 152.730 162.048 161.029 1.00 17.85  ? 1966 ARG A CB    1 
ATOM   4099  C  CG    . ARG A 1 1966 ? 152.792 163.469 161.558 1.00 20.38  ? 1966 ARG A CG    1 
ATOM   4100  C  CD    . ARG A 1 1966 ? 152.475 163.506 163.042 1.00 24.24  ? 1966 ARG A CD    1 
ATOM   4101  N  NE    . ARG A 1 1966 ? 152.023 164.825 163.468 1.00 34.31  ? 1966 ARG A NE    1 
ATOM   4102  C  CZ    . ARG A 1 1966 ? 150.757 165.143 163.701 1.00 34.12  ? 1966 ARG A CZ    1 
ATOM   4103  N  NH1   . ARG A 1 1966 ? 149.786 164.255 163.565 1.00 32.34  ? 1966 ARG A NH1   1 
ATOM   4104  N  NH2   . ARG A 1 1966 ? 150.459 166.382 164.080 1.00 30.39  ? 1966 ARG A NH2   1 
ATOM   4105  N  N     . MET A 1 1967 ? 152.234 163.764 158.370 1.00 16.98  ? 1967 MET A N     1 
ATOM   4106  C  CA    . MET A 1 1967 ? 151.357 164.371 157.374 1.00 12.87  ? 1967 MET A CA    1 
ATOM   4107  C  C     . MET A 1 1967 ? 151.711 163.902 155.969 1.00 12.54  ? 1967 MET A C     1 
ATOM   4108  O  O     . MET A 1 1967 ? 150.819 163.676 155.144 1.00 15.54  ? 1967 MET A O     1 
ATOM   4109  C  CB    . MET A 1 1967 ? 151.430 165.893 157.469 1.00 13.99  ? 1967 MET A CB    1 
ATOM   4110  C  CG    . MET A 1 1967 ? 150.606 166.480 158.602 1.00 20.16  ? 1967 MET A CG    1 
ATOM   4111  S  SD    . MET A 1 1967 ? 149.066 165.582 158.873 1.00 22.72  ? 1967 MET A SD    1 
ATOM   4112  C  CE    . MET A 1 1967 ? 148.929 165.677 160.654 1.00 22.23  ? 1967 MET A CE    1 
ATOM   4113  N  N     . LEU A 1 1968 ? 153.007 163.746 155.681 1.00 11.07  ? 1968 LEU A N     1 
ATOM   4114  C  CA    . LEU A 1 1968 ? 153.431 163.293 154.359 1.00 10.13  ? 1968 LEU A CA    1 
ATOM   4115  C  C     . LEU A 1 1968 ? 152.889 161.905 154.046 1.00 9.71   ? 1968 LEU A C     1 
ATOM   4116  O  O     . LEU A 1 1968 ? 152.456 161.638 152.919 1.00 13.08  ? 1968 LEU A O     1 
ATOM   4117  C  CB    . LEU A 1 1968 ? 154.956 163.303 154.267 1.00 12.37  ? 1968 LEU A CB    1 
ATOM   4118  C  CG    . LEU A 1 1968 ? 155.619 164.675 154.171 1.00 12.50  ? 1968 LEU A CG    1 
ATOM   4119  C  CD1   . LEU A 1 1968 ? 157.127 164.535 154.196 1.00 16.38  ? 1968 LEU A CD1   1 
ATOM   4120  C  CD2   . LEU A 1 1968 ? 155.172 165.367 152.905 1.00 8.87   ? 1968 LEU A CD2   1 
ATOM   4121  N  N     . SER A 1 1969 ? 152.918 161.001 155.026 1.00 9.37   ? 1969 SER A N     1 
ATOM   4122  C  CA    . SER A 1 1969 ? 152.339 159.678 154.823 1.00 11.51  ? 1969 SER A CA    1 
ATOM   4123  C  C     . SER A 1 1969 ? 150.834 159.764 154.609 1.00 14.74  ? 1969 SER A C     1 
ATOM   4124  O  O     . SER A 1 1969 ? 150.275 159.045 153.773 1.00 18.52  ? 1969 SER A O     1 
ATOM   4125  C  CB    . SER A 1 1969 ? 152.664 158.778 156.013 1.00 11.64  ? 1969 SER A CB    1 
ATOM   4126  O  OG    . SER A 1 1969 ? 151.612 157.863 156.261 1.00 15.81  ? 1969 SER A OG    1 
ATOM   4127  N  N     . ALA A 1 1970 ? 150.162 160.641 155.358 1.00 14.00  ? 1970 ALA A N     1 
ATOM   4128  C  CA    . ALA A 1 1970 ? 148.709 160.736 155.279 1.00 11.69  ? 1970 ALA A CA    1 
ATOM   4129  C  C     . ALA A 1 1970 ? 148.244 161.212 153.907 1.00 16.20  ? 1970 ALA A C     1 
ATOM   4130  O  O     . ALA A 1 1970 ? 147.276 160.673 153.356 1.00 18.57  ? 1970 ALA A O     1 
ATOM   4131  C  CB    . ALA A 1 1970 ? 148.188 161.666 156.374 1.00 14.37  ? 1970 ALA A CB    1 
ATOM   4132  N  N     . VAL A 1 1971 ? 148.913 162.217 153.334 1.00 14.24  ? 1971 VAL A N     1 
ATOM   4133  C  CA    . VAL A 1 1971 ? 148.459 162.755 152.056 1.00 13.44  ? 1971 VAL A CA    1 
ATOM   4134  C  C     . VAL A 1 1971 ? 148.726 161.790 150.913 1.00 11.87  ? 1971 VAL A C     1 
ATOM   4135  O  O     . VAL A 1 1971 ? 148.154 161.949 149.828 1.00 15.79  ? 1971 VAL A O     1 
ATOM   4136  C  CB    . VAL A 1 1971 ? 149.110 164.117 151.750 1.00 14.26  ? 1971 VAL A CB    1 
ATOM   4137  C  CG1   . VAL A 1 1971 ? 148.373 165.235 152.471 1.00 18.85  ? 1971 VAL A CG1   1 
ATOM   4138  C  CG2   . VAL A 1 1971 ? 150.586 164.105 152.096 1.00 15.12  ? 1971 VAL A CG2   1 
ATOM   4139  N  N     . SER A 1 1972 ? 149.590 160.793 151.122 1.00 10.57  ? 1972 SER A N     1 
ATOM   4140  C  CA    . SER A 1 1972 ? 149.848 159.806 150.080 1.00 12.18  ? 1972 SER A CA    1 
ATOM   4141  C  C     . SER A 1 1972 ? 148.580 159.062 149.688 1.00 13.79  ? 1972 SER A C     1 
ATOM   4142  O  O     . SER A 1 1972 ? 148.428 158.664 148.528 1.00 16.69  ? 1972 SER A O     1 
ATOM   4143  C  CB    . SER A 1 1972 ? 150.922 158.822 150.542 1.00 11.40  ? 1972 SER A CB    1 
ATOM   4144  O  OG    . SER A 1 1972 ? 150.434 157.988 151.578 1.00 22.37  ? 1972 SER A OG    1 
ATOM   4145  N  N     . GLN A 1 1973 ? 147.663 158.862 150.637 1.00 16.26  ? 1973 GLN A N     1 
ATOM   4146  C  CA    . GLN A 1 1973 ? 146.386 158.234 150.315 1.00 14.99  ? 1973 GLN A CA    1 
ATOM   4147  C  C     . GLN A 1 1973 ? 145.585 159.089 149.341 1.00 15.42  ? 1973 GLN A C     1 
ATOM   4148  O  O     . GLN A 1 1973 ? 144.995 158.574 148.385 1.00 16.95  ? 1973 GLN A O     1 
ATOM   4149  C  CB    . GLN A 1 1973 ? 145.586 157.989 151.595 1.00 14.98  ? 1973 GLN A CB    1 
ATOM   4150  C  CG    . GLN A 1 1973 ? 145.759 156.600 152.185 1.00 21.49  ? 1973 GLN A CG    1 
ATOM   4151  C  CD    . GLN A 1 1973 ? 145.039 156.438 153.508 1.00 21.63  ? 1973 GLN A CD    1 
ATOM   4152  O  OE1   . GLN A 1 1973 ? 144.291 155.481 153.706 1.00 21.04  ? 1973 GLN A OE1   1 
ATOM   4153  N  NE2   . GLN A 1 1973 ? 145.260 157.375 154.423 1.00 18.63  ? 1973 GLN A NE2   1 
ATOM   4154  N  N     . GLN A 1 1974 ? 145.555 160.404 149.571 1.00 15.67  ? 1974 GLN A N     1 
ATOM   4155  C  CA    . GLN A 1 1974 ? 144.787 161.288 148.699 1.00 11.75  ? 1974 GLN A CA    1 
ATOM   4156  C  C     . GLN A 1 1974 ? 145.426 161.405 147.322 1.00 14.26  ? 1974 GLN A C     1 
ATOM   4157  O  O     . GLN A 1 1974 ? 144.724 161.406 146.304 1.00 21.32  ? 1974 GLN A O     1 
ATOM   4158  C  CB    . GLN A 1 1974 ? 144.645 162.667 149.342 1.00 12.99  ? 1974 GLN A CB    1 
ATOM   4159  C  CG    . GLN A 1 1974 ? 144.372 162.629 150.832 1.00 15.67  ? 1974 GLN A CG    1 
ATOM   4160  C  CD    . GLN A 1 1974 ? 144.383 164.008 151.456 1.00 14.73  ? 1974 GLN A CD    1 
ATOM   4161  O  OE1   . GLN A 1 1974 ? 145.345 164.760 151.309 1.00 17.56  ? 1974 GLN A OE1   1 
ATOM   4162  N  NE2   . GLN A 1 1974 ? 143.308 164.350 152.156 1.00 12.51  ? 1974 GLN A NE2   1 
ATOM   4163  N  N     . VAL A 1 1975 ? 146.755 161.513 147.269 1.00 12.49  ? 1975 VAL A N     1 
ATOM   4164  C  CA    . VAL A 1 1975 ? 147.441 161.583 145.982 1.00 11.27  ? 1975 VAL A CA    1 
ATOM   4165  C  C     . VAL A 1 1975 ? 147.235 160.292 145.201 1.00 12.38  ? 1975 VAL A C     1 
ATOM   4166  O  O     . VAL A 1 1975 ? 146.965 160.314 143.994 1.00 14.24  ? 1975 VAL A O     1 
ATOM   4167  C  CB    . VAL A 1 1975 ? 148.936 161.891 146.189 1.00 10.49  ? 1975 VAL A CB    1 
ATOM   4168  C  CG1   . VAL A 1 1975 ? 149.665 161.903 144.858 1.00 9.59   ? 1975 VAL A CG1   1 
ATOM   4169  C  CG2   . VAL A 1 1975 ? 149.109 163.218 146.908 1.00 9.74   ? 1975 VAL A CG2   1 
ATOM   4170  N  N     . GLN A 1 1976 ? 147.355 159.148 145.878 1.00 15.48  ? 1976 GLN A N     1 
ATOM   4171  C  CA    . GLN A 1 1976 ? 147.134 157.864 145.221 1.00 14.22  ? 1976 GLN A CA    1 
ATOM   4172  C  C     . GLN A 1 1976 ? 145.695 157.727 144.740 1.00 17.23  ? 1976 GLN A C     1 
ATOM   4173  O  O     . GLN A 1 1976 ? 145.450 157.247 143.628 1.00 18.75  ? 1976 GLN A O     1 
ATOM   4174  C  CB    . GLN A 1 1976 ? 147.497 156.726 146.176 1.00 16.70  ? 1976 GLN A CB    1 
ATOM   4175  C  CG    . GLN A 1 1976 ? 147.198 155.340 145.646 1.00 22.52  ? 1976 GLN A CG    1 
ATOM   4176  C  CD    . GLN A 1 1976 ? 148.004 154.265 146.348 1.00 28.94  ? 1976 GLN A CD    1 
ATOM   4177  O  OE1   . GLN A 1 1976 ? 148.496 154.467 147.458 1.00 33.19  ? 1976 GLN A OE1   1 
ATOM   4178  N  NE2   . GLN A 1 1976 ? 148.148 153.114 145.700 1.00 37.33  ? 1976 GLN A NE2   1 
ATOM   4179  N  N     . CYS A 1 1977 ? 144.731 158.146 145.564 1.00 21.09  ? 1977 CYS A N     1 
ATOM   4180  C  CA    . CYS A 1 1977 ? 143.328 158.074 145.166 1.00 17.87  ? 1977 CYS A CA    1 
ATOM   4181  C  C     . CYS A 1 1977 ? 143.043 158.979 143.974 1.00 18.15  ? 1977 CYS A C     1 
ATOM   4182  O  O     . CYS A 1 1977 ? 142.288 158.604 143.069 1.00 23.33  ? 1977 CYS A O     1 
ATOM   4183  C  CB    . CYS A 1 1977 ? 142.431 158.439 146.347 1.00 21.14  ? 1977 CYS A CB    1 
ATOM   4184  S  SG    . CYS A 1 1977 ? 140.680 158.054 146.111 1.00 59.24  ? 1977 CYS A SG    1 
ATOM   4185  N  N     . ILE A 1 1978 ? 143.632 160.177 143.960 1.00 18.81  ? 1978 ILE A N     1 
ATOM   4186  C  CA    . ILE A 1 1978 ? 143.431 161.103 142.848 1.00 17.44  ? 1978 ILE A CA    1 
ATOM   4187  C  C     . ILE A 1 1978 ? 144.001 160.521 141.561 1.00 15.14  ? 1978 ILE A C     1 
ATOM   4188  O  O     . ILE A 1 1978 ? 143.379 160.604 140.494 1.00 18.23  ? 1978 ILE A O     1 
ATOM   4189  C  CB    . ILE A 1 1978 ? 144.057 162.470 143.181 1.00 13.91  ? 1978 ILE A CB    1 
ATOM   4190  C  CG1   . ILE A 1 1978 ? 143.143 163.265 144.113 1.00 16.22  ? 1978 ILE A CG1   1 
ATOM   4191  C  CG2   . ILE A 1 1978 ? 144.325 163.266 141.914 1.00 13.62  ? 1978 ILE A CG2   1 
ATOM   4192  C  CD1   . ILE A 1 1978 ? 143.806 164.479 144.716 1.00 15.99  ? 1978 ILE A CD1   1 
ATOM   4193  N  N     . GLN A 1 1979 ? 145.189 159.918 141.642 1.00 14.23  ? 1979 GLN A N     1 
ATOM   4194  C  CA    . GLN A 1 1979 ? 145.841 159.382 140.451 1.00 14.78  ? 1979 GLN A CA    1 
ATOM   4195  C  C     . GLN A 1 1979 ? 145.062 158.212 139.862 1.00 19.72  ? 1979 GLN A C     1 
ATOM   4196  O  O     . GLN A 1 1979 ? 145.018 158.045 138.638 1.00 25.05  ? 1979 GLN A O     1 
ATOM   4197  C  CB    . GLN A 1 1979 ? 147.272 158.966 140.784 1.00 14.70  ? 1979 GLN A CB    1 
ATOM   4198  C  CG    . GLN A 1 1979 ? 148.213 160.135 141.011 1.00 11.45  ? 1979 GLN A CG    1 
ATOM   4199  C  CD    . GLN A 1 1979 ? 149.598 159.692 141.432 1.00 10.29  ? 1979 GLN A CD    1 
ATOM   4200  O  OE1   . GLN A 1 1979 ? 149.908 158.501 141.430 1.00 17.46  ? 1979 GLN A OE1   1 
ATOM   4201  N  NE2   . GLN A 1 1979 ? 150.442 160.650 141.796 1.00 7.84   ? 1979 GLN A NE2   1 
ATOM   4202  N  N     . GLU A 1 1980 ? 144.450 157.385 140.714 1.00 20.94  ? 1980 GLU A N     1 
ATOM   4203  C  CA    . GLU A 1 1980 ? 143.609 156.303 140.210 1.00 23.14  ? 1980 GLU A CA    1 
ATOM   4204  C  C     . GLU A 1 1980 ? 142.410 156.846 139.444 1.00 20.80  ? 1980 GLU A C     1 
ATOM   4205  O  O     . GLU A 1 1980 ? 142.014 156.285 138.416 1.00 26.45  ? 1980 GLU A O     1 
ATOM   4206  C  CB    . GLU A 1 1980 ? 143.154 155.403 141.360 1.00 22.97  ? 1980 GLU A CB    1 
ATOM   4207  C  CG    . GLU A 1 1980 ? 144.111 154.262 141.661 1.00 29.39  ? 1980 GLU A CG    1 
ATOM   4208  C  CD    . GLU A 1 1980 ? 144.569 154.237 143.104 1.00 34.26  ? 1980 GLU A CD    1 
ATOM   4209  O  OE1   . GLU A 1 1980 ? 145.715 153.809 143.352 1.00 34.86  ? 1980 GLU A OE1   1 
ATOM   4210  O  OE2   . GLU A 1 1980 ? 143.786 154.642 143.987 1.00 30.93  ? 1980 GLU A OE2   1 
ATOM   4211  N  N     . ALA A 1 1981 ? 141.813 157.934 139.934 1.00 17.60  ? 1981 ALA A N     1 
ATOM   4212  C  CA    . ALA A 1 1981 ? 140.746 158.585 139.183 1.00 24.99  ? 1981 ALA A CA    1 
ATOM   4213  C  C     . ALA A 1 1981 ? 141.264 159.120 137.854 1.00 27.45  ? 1981 ALA A C     1 
ATOM   4214  O  O     . ALA A 1 1981 ? 140.597 158.991 136.821 1.00 32.50  ? 1981 ALA A O     1 
ATOM   4215  C  CB    . ALA A 1 1981 ? 140.128 159.710 140.013 1.00 26.14  ? 1981 ALA A CB    1 
ATOM   4216  N  N     . LEU A 1 1982 ? 142.454 159.724 137.862 1.00 26.94  ? 1982 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 1982 ? 143.051 160.204 136.620 1.00 22.13  ? 1982 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 1982 ? 143.388 159.050 135.686 1.00 26.56  ? 1982 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 1982 ? 143.183 159.146 134.470 1.00 35.21  ? 1982 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 1982 ? 144.301 161.029 136.924 1.00 17.58  ? 1982 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 1982 ? 144.069 162.456 137.422 1.00 21.23  ? 1982 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 1982 ? 145.375 163.084 137.874 1.00 17.32  ? 1982 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 1982 ? 143.417 163.298 136.339 1.00 23.59  ? 1982 LEU A CD2   1 
ATOM   4224  N  N     . ARG A 1 1983 ? 143.915 157.952 136.234 1.00 26.69  ? 1983 ARG A N     1 
ATOM   4225  C  CA    . ARG A 1 1983 ? 144.270 156.805 135.403 1.00 28.13  ? 1983 ARG A CA    1 
ATOM   4226  C  C     . ARG A 1 1983 ? 143.040 156.196 134.744 1.00 36.49  ? 1983 ARG A C     1 
ATOM   4227  O  O     . ARG A 1 1983 ? 143.071 155.843 133.559 1.00 45.01  ? 1983 ARG A O     1 
ATOM   4228  C  CB    . ARG A 1 1983 ? 145.011 155.764 136.240 1.00 24.08  ? 1983 ARG A CB    1 
ATOM   4229  C  CG    . ARG A 1 1983 ? 145.945 154.880 135.435 1.00 22.91  ? 1983 ARG A CG    1 
ATOM   4230  C  CD    . ARG A 1 1983 ? 147.067 154.333 136.298 1.00 25.07  ? 1983 ARG A CD    1 
ATOM   4231  N  NE    . ARG A 1 1983 ? 147.865 155.401 136.889 1.00 24.61  ? 1983 ARG A NE    1 
ATOM   4232  C  CZ    . ARG A 1 1983 ? 148.110 155.525 138.186 1.00 24.38  ? 1983 ARG A CZ    1 
ATOM   4233  N  NH1   . ARG A 1 1983 ? 147.631 154.662 139.066 1.00 26.77  ? 1983 ARG A NH1   1 
ATOM   4234  N  NH2   . ARG A 1 1983 ? 148.855 156.542 138.610 1.00 18.93  ? 1983 ARG A NH2   1 
ATOM   4235  N  N     . GLU A 1 1984 ? 141.944 156.062 135.494 1.00 37.55  ? 1984 GLU A N     1 
ATOM   4236  C  CA    . GLU A 1 1984 ? 140.703 155.575 134.905 1.00 43.93  ? 1984 GLU A CA    1 
ATOM   4237  C  C     . GLU A 1 1984 ? 140.064 156.605 133.983 1.00 42.23  ? 1984 GLU A C     1 
ATOM   4238  O  O     . GLU A 1 1984 ? 139.215 156.243 133.161 1.00 48.41  ? 1984 GLU A O     1 
ATOM   4239  C  CB    . GLU A 1 1984 ? 139.721 155.166 136.004 1.00 42.23  ? 1984 GLU A CB    1 
ATOM   4240  C  CG    . GLU A 1 1984 ? 138.850 156.295 136.514 1.00 41.86  ? 1984 GLU A CG    1 
ATOM   4241  C  CD    . GLU A 1 1984 ? 137.903 155.854 137.610 1.00 50.73  ? 1984 GLU A CD    1 
ATOM   4242  O  OE1   . GLU A 1 1984 ? 138.387 155.422 138.677 1.00 45.93  ? 1984 GLU A OE1   1 
ATOM   4243  O  OE2   . GLU A 1 1984 ? 136.674 155.939 137.405 1.00 63.47  ? 1984 GLU A OE2   1 
ATOM   4244  N  N     . HIS A 1 1985 ? 140.451 157.877 134.103 1.00 42.90  ? 1985 HIS A N     1 
ATOM   4245  C  CA    . HIS A 1 1985 ? 139.949 158.898 133.191 1.00 45.12  ? 1985 HIS A CA    1 
ATOM   4246  C  C     . HIS A 1 1985 ? 140.599 158.790 131.818 1.00 51.41  ? 1985 HIS A C     1 
ATOM   4247  O  O     . HIS A 1 1985 ? 139.983 159.159 130.812 1.00 55.79  ? 1985 HIS A O     1 
ATOM   4248  C  CB    . HIS A 1 1985 ? 140.190 160.287 133.783 1.00 46.87  ? 1985 HIS A CB    1 
ATOM   4249  C  CG    . HIS A 1 1985 ? 139.228 161.328 133.300 1.00 52.74  ? 1985 HIS A CG    1 
ATOM   4250  N  ND1   . HIS A 1 1985 ? 138.815 161.410 131.988 1.00 59.17  ? 1985 HIS A ND1   1 
ATOM   4251  C  CD2   . HIS A 1 1985 ? 138.605 162.336 133.954 1.00 49.84  ? 1985 HIS A CD2   1 
ATOM   4252  C  CE1   . HIS A 1 1985 ? 137.975 162.421 131.856 1.00 57.85  ? 1985 HIS A CE1   1 
ATOM   4253  N  NE2   . HIS A 1 1985 ? 137.830 162.999 133.035 1.00 57.67  ? 1985 HIS A NE2   1 
ATOM   4254  N  N     . SER A 1 1986 ? 141.835 158.293 131.757 1.00 55.70  ? 1986 SER A N     1 
ATOM   4255  C  CA    . SER A 1 1986 ? 142.560 158.211 130.496 1.00 55.86  ? 1986 SER A CA    1 
ATOM   4256  C  C     . SER A 1 1986 ? 142.225 156.961 129.693 1.00 62.41  ? 1986 SER A C     1 
ATOM   4257  O  O     . SER A 1 1986 ? 142.593 156.885 128.516 1.00 73.09  ? 1986 SER A O     1 
ATOM   4258  C  CB    . SER A 1 1986 ? 144.068 158.262 130.754 1.00 47.74  ? 1986 SER A CB    1 
ATOM   4259  O  OG    . SER A 1 1986 ? 144.564 156.989 131.127 1.00 44.77  ? 1986 SER A OG    1 
ATOM   4260  N  N     . ASN A 1 1987 ? 141.548 155.988 130.290 1.00 59.63  ? 1987 ASN A N     1 
ATOM   4261  C  CA    . ASN A 1 1987 ? 141.215 154.765 129.567 1.00 74.55  ? 1987 ASN A CA    1 
ATOM   4262  C  C     . ASN A 1 1987 ? 140.204 155.064 128.466 1.00 83.25  ? 1987 ASN A C     1 
ATOM   4263  O  O     . ASN A 1 1987 ? 139.235 155.795 128.702 1.00 80.78  ? 1987 ASN A O     1 
ATOM   4264  C  CB    . ASN A 1 1987 ? 140.663 153.705 130.518 1.00 74.05  ? 1987 ASN A CB    1 
ATOM   4265  C  CG    . ASN A 1 1987 ? 141.644 153.334 131.612 1.00 71.17  ? 1987 ASN A CG    1 
ATOM   4266  O  OD1   . ASN A 1 1987 ? 141.285 153.265 132.786 1.00 69.15  ? 1987 ASN A OD1   1 
ATOM   4267  N  ND2   . ASN A 1 1987 ? 142.893 153.095 131.230 1.00 73.36  ? 1987 ASN A ND2   1 
ATOM   4268  N  N     . PRO A 1 1988 ? 140.394 154.531 127.256 1.00 86.32  ? 1988 PRO A N     1 
ATOM   4269  C  CA    . PRO A 1 1988 ? 139.424 154.786 126.178 1.00 86.67  ? 1988 PRO A CA    1 
ATOM   4270  C  C     . PRO A 1 1988 ? 138.039 154.229 126.454 1.00 87.90  ? 1988 PRO A C     1 
ATOM   4271  O  O     . PRO A 1 1988 ? 137.065 154.724 125.874 1.00 85.25  ? 1988 PRO A O     1 
ATOM   4272  C  CB    . PRO A 1 1988 ? 140.068 154.110 124.961 1.00 87.65  ? 1988 PRO A CB    1 
ATOM   4273  C  CG    . PRO A 1 1988 ? 140.951 153.055 125.544 1.00 83.90  ? 1988 PRO A CG    1 
ATOM   4274  C  CD    . PRO A 1 1988 ? 141.476 153.628 126.828 1.00 83.07  ? 1988 PRO A CD    1 
ATOM   4275  N  N     . ASN A 1 1989 ? 137.919 153.212 127.312 1.00 87.97  ? 1989 ASN A N     1 
ATOM   4276  C  CA    . ASN A 1 1989 ? 136.609 152.634 127.598 1.00 90.00  ? 1989 ASN A CA    1 
ATOM   4277  C  C     . ASN A 1 1989 ? 135.684 153.638 128.272 1.00 93.36  ? 1989 ASN A C     1 
ATOM   4278  O  O     . ASN A 1 1989 ? 134.465 153.586 128.077 1.00 93.61  ? 1989 ASN A O     1 
ATOM   4279  C  CB    . ASN A 1 1989 ? 136.764 151.386 128.468 1.00 88.59  ? 1989 ASN A CB    1 
ATOM   4280  C  CG    . ASN A 1 1989 ? 137.768 151.577 129.587 1.00 87.29  ? 1989 ASN A CG    1 
ATOM   4281  O  OD1   . ASN A 1 1989 ? 137.597 152.437 130.451 1.00 80.84  ? 1989 ASN A OD1   1 
ATOM   4282  N  ND2   . ASN A 1 1989 ? 138.825 150.774 129.576 1.00 84.11  ? 1989 ASN A ND2   1 
ATOM   4283  N  N     . TYR A 1 1990 ? 136.238 154.550 129.068 1.00 93.83  ? 1990 TYR A N     1 
ATOM   4284  C  CA    . TYR A 1 1990 ? 135.424 155.564 129.722 1.00 94.51  ? 1990 TYR A CA    1 
ATOM   4285  C  C     . TYR A 1 1990 ? 134.848 156.533 128.697 1.00 92.07  ? 1990 TYR A C     1 
ATOM   4286  O  O     . TYR A 1 1990 ? 135.526 156.940 127.750 1.00 87.26  ? 1990 TYR A O     1 
ATOM   4287  C  CB    . TYR A 1 1990 ? 136.253 156.328 130.755 1.00 87.17  ? 1990 TYR A CB    1 
ATOM   4288  C  CG    . TYR A 1 1990 ? 135.655 157.659 131.154 1.00 86.19  ? 1990 TYR A CG    1 
ATOM   4289  C  CD1   . TYR A 1 1990 ? 134.499 157.721 131.920 1.00 86.43  ? 1990 TYR A CD1   1 
ATOM   4290  C  CD2   . TYR A 1 1990 ? 136.244 158.853 130.759 1.00 80.97  ? 1990 TYR A CD2   1 
ATOM   4291  C  CE1   . TYR A 1 1990 ? 133.948 158.935 132.286 1.00 88.14  ? 1990 TYR A CE1   1 
ATOM   4292  C  CE2   . TYR A 1 1990 ? 135.700 160.071 131.119 1.00 79.98  ? 1990 TYR A CE2   1 
ATOM   4293  C  CZ    . TYR A 1 1990 ? 134.552 160.106 131.882 1.00 85.93  ? 1990 TYR A CZ    1 
ATOM   4294  O  OH    . TYR A 1 1990 ? 134.007 161.317 132.244 1.00 80.45  ? 1990 TYR A OH    1 
ATOM   4295  N  N     . ASP A 1 1991 ? 133.584 156.899 128.891 1.00 96.06  ? 1991 ASP A N     1 
ATOM   4296  C  CA    . ASP A 1 1991 ? 132.902 157.873 128.051 1.00 96.63  ? 1991 ASP A CA    1 
ATOM   4297  C  C     . ASP A 1 1991 ? 132.391 159.006 128.927 1.00 99.33  ? 1991 ASP A C     1 
ATOM   4298  O  O     . ASP A 1 1991 ? 131.843 158.761 130.007 1.00 96.73  ? 1991 ASP A O     1 
ATOM   4299  C  CB    . ASP A 1 1991 ? 131.744 157.228 127.283 1.00 97.06  ? 1991 ASP A CB    1 
ATOM   4300  C  CG    . ASP A 1 1991 ? 130.823 156.427 128.182 1.00 98.60  ? 1991 ASP A CG    1 
ATOM   4301  O  OD1   . ASP A 1 1991 ? 131.306 155.483 128.843 1.00 94.99  ? 1991 ASP A OD1   1 
ATOM   4302  O  OD2   . ASP A 1 1991 ? 129.615 156.741 128.230 1.00 99.40  ? 1991 ASP A OD2   1 
ATOM   4303  N  N     . LYS A 1 1992 ? 132.568 160.244 128.459 1.00 98.70  ? 1992 LYS A N     1 
ATOM   4304  C  CA    . LYS A 1 1992 ? 132.140 161.402 129.237 1.00 99.75  ? 1992 LYS A CA    1 
ATOM   4305  C  C     . LYS A 1 1992 ? 130.628 161.463 129.401 1.00 100.64 ? 1992 LYS A C     1 
ATOM   4306  O  O     . LYS A 1 1992 ? 130.140 162.182 130.281 1.00 97.40  ? 1992 LYS A O     1 
ATOM   4307  C  CB    . LYS A 1 1992 ? 132.651 162.689 128.587 1.00 95.99  ? 1992 LYS A CB    1 
ATOM   4308  C  CG    . LYS A 1 1992 ? 134.167 162.815 128.577 1.00 93.83  ? 1992 LYS A CG    1 
ATOM   4309  C  CD    . LYS A 1 1992 ? 134.614 164.098 127.893 1.00 93.70  ? 1992 LYS A CD    1 
ATOM   4310  C  CE    . LYS A 1 1992 ? 134.103 164.172 126.464 1.00 91.89  ? 1992 LYS A CE    1 
ATOM   4311  N  NZ    . LYS A 1 1992 ? 134.512 165.437 125.795 1.00 92.19  ? 1992 LYS A NZ    1 
ATOM   4312  N  N     . THR A 1 1993 ? 129.875 160.731 128.577 1.00 102.37 ? 1993 THR A N     1 
ATOM   4313  C  CA    . THR A 1 1993 ? 128.424 160.697 128.722 1.00 102.05 ? 1993 THR A CA    1 
ATOM   4314  C  C     . THR A 1 1993 ? 127.985 159.975 129.989 1.00 101.41 ? 1993 THR A C     1 
ATOM   4315  O  O     . THR A 1 1993 ? 126.874 160.217 130.471 1.00 98.98  ? 1993 THR A O     1 
ATOM   4316  C  CB    . THR A 1 1993 ? 127.787 160.030 127.502 1.00 99.99  ? 1993 THR A CB    1 
ATOM   4317  O  OG1   . THR A 1 1993 ? 128.363 158.732 127.309 1.00 101.23 ? 1993 THR A OG1   1 
ATOM   4318  C  CG2   . THR A 1 1993 ? 128.018 160.871 126.255 1.00 90.88  ? 1993 THR A CG2   1 
ATOM   4319  N  N     . SER A 1 1994 ? 128.826 159.101 130.536 1.00 100.48 ? 1994 SER A N     1 
ATOM   4320  C  CA    . SER A 1 1994 ? 128.495 158.363 131.747 1.00 99.18  ? 1994 SER A CA    1 
ATOM   4321  C  C     . SER A 1 1994 ? 128.732 159.251 132.967 1.00 96.24  ? 1994 SER A C     1 
ATOM   4322  O  O     . SER A 1 1994 ? 128.925 160.465 132.857 1.00 92.57  ? 1994 SER A O     1 
ATOM   4323  C  CB    . SER A 1 1994 ? 129.302 157.069 131.814 1.00 91.93  ? 1994 SER A CB    1 
ATOM   4324  O  OG    . SER A 1 1994 ? 130.684 157.339 131.975 1.00 90.15  ? 1994 SER A OG    1 
ATOM   4325  N  N     . ALA A 1 1995 ? 128.710 158.649 134.152 1.00 92.03  ? 1995 ALA A N     1 
ATOM   4326  C  CA    . ALA A 1 1995 ? 128.953 159.406 135.370 1.00 84.77  ? 1995 ALA A CA    1 
ATOM   4327  C  C     . ALA A 1 1995 ? 130.384 159.939 135.374 1.00 86.15  ? 1995 ALA A C     1 
ATOM   4328  O  O     . ALA A 1 1995 ? 131.326 159.193 135.079 1.00 83.77  ? 1995 ALA A O     1 
ATOM   4329  C  CB    . ALA A 1 1995 ? 128.711 158.535 136.603 1.00 77.13  ? 1995 ALA A CB    1 
ATOM   4330  N  N     . PRO A 1 1996 ? 130.583 161.217 135.695 1.00 80.69  ? 1996 PRO A N     1 
ATOM   4331  C  CA    . PRO A 1 1996 ? 131.937 161.780 135.673 1.00 72.43  ? 1996 PRO A CA    1 
ATOM   4332  C  C     . PRO A 1 1996 ? 132.830 161.124 136.714 1.00 66.48  ? 1996 PRO A C     1 
ATOM   4333  O  O     . PRO A 1 1996 ? 132.368 160.643 137.751 1.00 64.37  ? 1996 PRO A O     1 
ATOM   4334  C  CB    . PRO A 1 1996 ? 131.712 163.265 135.983 1.00 69.61  ? 1996 PRO A CB    1 
ATOM   4335  C  CG    . PRO A 1 1996 ? 130.258 163.508 135.703 1.00 70.65  ? 1996 PRO A CG    1 
ATOM   4336  C  CD    . PRO A 1 1996 ? 129.572 162.226 136.048 1.00 75.22  ? 1996 PRO A CD    1 
ATOM   4337  N  N     . ILE A 1 1997 ? 134.128 161.103 136.417 1.00 62.27  ? 1997 ILE A N     1 
ATOM   4338  C  CA    . ILE A 1 1997 ? 135.100 160.462 137.295 1.00 54.35  ? 1997 ILE A CA    1 
ATOM   4339  C  C     . ILE A 1 1997 ? 135.152 161.212 138.619 1.00 51.74  ? 1997 ILE A C     1 
ATOM   4340  O  O     . ILE A 1 1997 ? 135.355 162.431 138.654 1.00 49.12  ? 1997 ILE A O     1 
ATOM   4341  C  CB    . ILE A 1 1997 ? 136.483 160.407 136.635 1.00 49.45  ? 1997 ILE A CB    1 
ATOM   4342  C  CG1   . ILE A 1 1997 ? 136.355 160.005 135.163 1.00 57.01  ? 1997 ILE A CG1   1 
ATOM   4343  C  CG2   . ILE A 1 1997 ? 137.397 159.461 137.399 1.00 43.47  ? 1997 ILE A CG2   1 
ATOM   4344  C  CD1   . ILE A 1 1997 ? 136.316 158.509 134.934 1.00 58.24  ? 1997 ILE A CD1   1 
ATOM   4345  N  N     . THR A 1 1998 ? 134.971 160.481 139.716 1.00 43.77  ? 1998 THR A N     1 
ATOM   4346  C  CA    . THR A 1 1998 ? 135.019 161.045 141.054 1.00 40.13  ? 1998 THR A CA    1 
ATOM   4347  C  C     . THR A 1 1998 ? 135.976 160.226 141.908 1.00 40.44  ? 1998 THR A C     1 
ATOM   4348  O  O     . THR A 1 1998 ? 136.212 159.042 141.655 1.00 42.51  ? 1998 THR A O     1 
ATOM   4349  C  CB    . THR A 1 1998 ? 133.630 161.075 141.710 1.00 38.92  ? 1998 THR A CB    1 
ATOM   4350  O  OG1   . THR A 1 1998 ? 132.927 159.866 141.402 1.00 50.59  ? 1998 THR A OG1   1 
ATOM   4351  C  CG2   . THR A 1 1998 ? 132.828 162.262 141.202 1.00 39.78  ? 1998 THR A CG2   1 
ATOM   4352  N  N     . CYS A 1 1999 ? 136.528 160.875 142.929 1.00 34.85  ? 1999 CYS A N     1 
ATOM   4353  C  CA    . CYS A 1 1999 ? 137.449 160.232 143.852 1.00 31.04  ? 1999 CYS A CA    1 
ATOM   4354  C  C     . CYS A 1 1999 ? 137.069 160.591 145.281 1.00 34.03  ? 1999 CYS A C     1 
ATOM   4355  O  O     . CYS A 1 1999 ? 136.294 161.519 145.528 1.00 35.04  ? 1999 CYS A O     1 
ATOM   4356  C  CB    . CYS A 1 1999 ? 138.904 160.628 143.565 1.00 31.33  ? 1999 CYS A CB    1 
ATOM   4357  S  SG    . CYS A 1 1999 ? 139.518 162.008 144.546 1.00 49.16  ? 1999 CYS A SG    1 
ATOM   4358  N  N     . GLU A 1 2000 ? 137.627 159.837 146.224 1.00 38.49  ? 2000 GLU A N     1 
ATOM   4359  C  CA    . GLU A 1 2000 ? 137.277 159.953 147.637 1.00 34.79  ? 2000 GLU A CA    1 
ATOM   4360  C  C     . GLU A 1 2000 ? 138.250 160.922 148.299 1.00 34.72  ? 2000 GLU A C     1 
ATOM   4361  O  O     . GLU A 1 2000 ? 139.391 160.565 148.603 1.00 37.38  ? 2000 GLU A O     1 
ATOM   4362  C  CB    . GLU A 1 2000 ? 137.314 158.580 148.300 1.00 39.86  ? 2000 GLU A CB    1 
ATOM   4363  C  CG    . GLU A 1 2000 ? 137.046 158.582 149.791 1.00 46.57  ? 2000 GLU A CG    1 
ATOM   4364  C  CD    . GLU A 1 2000 ? 135.567 158.631 150.108 1.00 49.16  ? 2000 GLU A CD    1 
ATOM   4365  O  OE1   . GLU A 1 2000 ? 134.761 158.197 149.258 1.00 40.47  ? 2000 GLU A OE1   1 
ATOM   4366  O  OE2   . GLU A 1 2000 ? 135.209 159.091 151.210 1.00 51.63  ? 2000 GLU A OE2   1 
ATOM   4367  N  N     . LEU A 1 2001 ? 137.801 162.155 148.527 1.00 28.93  ? 2001 LEU A N     1 
ATOM   4368  C  CA    . LEU A 1 2001 ? 138.613 163.188 149.162 1.00 28.25  ? 2001 LEU A CA    1 
ATOM   4369  C  C     . LEU A 1 2001 ? 137.852 163.765 150.345 1.00 32.53  ? 2001 LEU A C     1 
ATOM   4370  O  O     . LEU A 1 2001 ? 136.740 164.279 150.178 1.00 38.77  ? 2001 LEU A O     1 
ATOM   4371  C  CB    . LEU A 1 2001 ? 138.974 164.297 148.171 1.00 29.69  ? 2001 LEU A CB    1 
ATOM   4372  C  CG    . LEU A 1 2001 ? 140.228 164.086 147.322 1.00 26.41  ? 2001 LEU A CG    1 
ATOM   4373  C  CD1   . LEU A 1 2001 ? 140.349 165.177 146.270 1.00 18.82  ? 2001 LEU A CD1   1 
ATOM   4374  C  CD2   . LEU A 1 2001 ? 141.468 164.040 148.196 1.00 21.38  ? 2001 LEU A CD2   1 
ATOM   4375  N  N     . LEU A 1 2002 ? 138.461 163.695 151.530 1.00 34.59  ? 2002 LEU A N     1 
ATOM   4376  C  CA    . LEU A 1 2002 ? 137.876 164.236 152.758 1.00 31.97  ? 2002 LEU A CA    1 
ATOM   4377  C  C     . LEU A 1 2002 ? 136.467 163.695 152.988 1.00 36.09  ? 2002 LEU A C     1 
ATOM   4378  O  O     . LEU A 1 2002 ? 135.545 164.432 153.343 1.00 38.46  ? 2002 LEU A O     1 
ATOM   4379  C  CB    . LEU A 1 2002 ? 137.879 165.765 152.742 1.00 30.34  ? 2002 LEU A CB    1 
ATOM   4380  C  CG    . LEU A 1 2002 ? 139.253 166.432 152.821 1.00 23.42  ? 2002 LEU A CG    1 
ATOM   4381  C  CD1   . LEU A 1 2002 ? 139.111 167.925 153.070 1.00 18.64  ? 2002 LEU A CD1   1 
ATOM   4382  C  CD2   . LEU A 1 2002 ? 140.101 165.784 153.904 1.00 21.21  ? 2002 LEU A CD2   1 
ATOM   4383  N  N     . ASN A 1 2003 ? 136.303 162.389 152.766 1.00 39.25  ? 2003 ASN A N     1 
ATOM   4384  C  CA    . ASN A 1 2003 ? 135.030 161.694 152.963 1.00 40.85  ? 2003 ASN A CA    1 
ATOM   4385  C  C     . ASN A 1 2003 ? 133.926 162.262 152.075 1.00 39.53  ? 2003 ASN A C     1 
ATOM   4386  O  O     . ASN A 1 2003 ? 132.743 162.201 152.420 1.00 44.87  ? 2003 ASN A O     1 
ATOM   4387  C  CB    . ASN A 1 2003 ? 134.605 161.718 154.435 1.00 43.79  ? 2003 ASN A CB    1 
ATOM   4388  C  CG    . ASN A 1 2003 ? 135.623 161.058 155.344 1.00 43.15  ? 2003 ASN A CG    1 
ATOM   4389  O  OD1   . ASN A 1 2003 ? 136.214 161.706 156.207 1.00 48.11  ? 2003 ASN A OD1   1 
ATOM   4390  N  ND2   . ASN A 1 2003 ? 135.837 159.761 155.150 1.00 38.27  ? 2003 ASN A ND2   1 
ATOM   4391  N  N     . LYS A 1 2004 ? 134.303 162.815 150.924 1.00 37.03  ? 2004 LYS A N     1 
ATOM   4392  C  CA    . LYS A 1 2004 ? 133.355 163.348 149.958 1.00 35.01  ? 2004 LYS A CA    1 
ATOM   4393  C  C     . LYS A 1 2004 ? 133.720 162.856 148.565 1.00 35.91  ? 2004 LYS A C     1 
ATOM   4394  O  O     . LYS A 1 2004 ? 134.891 162.608 148.263 1.00 41.33  ? 2004 LYS A O     1 
ATOM   4395  C  CB    . LYS A 1 2004 ? 133.332 164.884 149.971 1.00 36.23  ? 2004 LYS A CB    1 
ATOM   4396  C  CG    . LYS A 1 2004 ? 132.946 165.500 151.306 1.00 41.11  ? 2004 LYS A CG    1 
ATOM   4397  C  CD    . LYS A 1 2004 ? 131.513 165.167 151.682 1.00 43.67  ? 2004 LYS A CD    1 
ATOM   4398  C  CE    . LYS A 1 2004 ? 131.144 165.776 153.026 1.00 44.92  ? 2004 LYS A CE    1 
ATOM   4399  N  NZ    . LYS A 1 2004 ? 129.840 165.264 153.530 1.00 45.67  ? 2004 LYS A NZ    1 
ATOM   4400  N  N     . GLN A 1 2005 ? 132.705 162.716 147.717 1.00 37.40  ? 2005 GLN A N     1 
ATOM   4401  C  CA    . GLN A 1 2005 ? 132.905 162.357 146.317 1.00 36.09  ? 2005 GLN A CA    1 
ATOM   4402  C  C     . GLN A 1 2005 ? 133.125 163.643 145.529 1.00 33.47  ? 2005 GLN A C     1 
ATOM   4403  O  O     . GLN A 1 2005 ? 132.209 164.461 145.393 1.00 34.43  ? 2005 GLN A O     1 
ATOM   4404  C  CB    . GLN A 1 2005 ? 131.713 161.571 145.780 1.00 36.80  ? 2005 GLN A CB    1 
ATOM   4405  C  CG    . GLN A 1 2005 ? 131.707 160.104 146.178 1.00 41.12  ? 2005 GLN A CG    1 
ATOM   4406  C  CD    . GLN A 1 2005 ? 132.898 159.343 145.630 1.00 38.17  ? 2005 GLN A CD    1 
ATOM   4407  O  OE1   . GLN A 1 2005 ? 133.125 159.311 144.422 1.00 38.69  ? 2005 GLN A OE1   1 
ATOM   4408  N  NE2   . GLN A 1 2005 ? 133.665 158.724 146.520 1.00 40.42  ? 2005 GLN A NE2   1 
ATOM   4409  N  N     . VAL A 1 2006 ? 134.337 163.821 145.011 1.00 31.65  ? 2006 VAL A N     1 
ATOM   4410  C  CA    . VAL A 1 2006 ? 134.748 165.054 144.351 1.00 33.06  ? 2006 VAL A CA    1 
ATOM   4411  C  C     . VAL A 1 2006 ? 135.074 164.741 142.898 1.00 31.60  ? 2006 VAL A C     1 
ATOM   4412  O  O     . VAL A 1 2006 ? 135.835 163.809 142.612 1.00 33.92  ? 2006 VAL A O     1 
ATOM   4413  C  CB    . VAL A 1 2006 ? 135.951 165.696 145.065 1.00 34.64  ? 2006 VAL A CB    1 
ATOM   4414  C  CG1   . VAL A 1 2006 ? 136.733 166.588 144.114 1.00 28.90  ? 2006 VAL A CG1   1 
ATOM   4415  C  CG2   . VAL A 1 2006 ? 135.486 166.480 146.280 1.00 31.26  ? 2006 VAL A CG2   1 
ATOM   4416  N  N     . LYS A 1 2007 ? 134.492 165.515 141.985 1.00 32.46  ? 2007 LYS A N     1 
ATOM   4417  C  CA    . LYS A 1 2007 ? 134.751 165.331 140.564 1.00 36.66  ? 2007 LYS A CA    1 
ATOM   4418  C  C     . LYS A 1 2007 ? 136.203 165.659 140.239 1.00 35.56  ? 2007 LYS A C     1 
ATOM   4419  O  O     . LYS A 1 2007 ? 136.779 166.607 140.778 1.00 34.22  ? 2007 LYS A O     1 
ATOM   4420  C  CB    . LYS A 1 2007 ? 133.814 166.211 139.740 1.00 36.67  ? 2007 LYS A CB    1 
ATOM   4421  C  CG    . LYS A 1 2007 ? 133.229 165.526 138.517 1.00 41.19  ? 2007 LYS A CG    1 
ATOM   4422  C  CD    . LYS A 1 2007 ? 131.888 166.132 138.123 1.00 55.40  ? 2007 LYS A CD    1 
ATOM   4423  C  CE    . LYS A 1 2007 ? 131.845 167.631 138.378 1.00 57.19  ? 2007 LYS A CE    1 
ATOM   4424  N  NZ    . LYS A 1 2007 ? 130.581 168.240 137.879 1.00 54.05  ? 2007 LYS A NZ    1 
ATOM   4425  N  N     . VAL A 1 2008 ? 136.794 164.866 139.349 1.00 33.07  ? 2008 VAL A N     1 
ATOM   4426  C  CA    . VAL A 1 2008 ? 138.193 165.010 138.964 1.00 25.24  ? 2008 VAL A CA    1 
ATOM   4427  C  C     . VAL A 1 2008 ? 138.255 165.367 137.487 1.00 28.01  ? 2008 VAL A C     1 
ATOM   4428  O  O     . VAL A 1 2008 ? 137.742 164.627 136.639 1.00 39.91  ? 2008 VAL A O     1 
ATOM   4429  C  CB    . VAL A 1 2008 ? 138.992 163.728 139.253 1.00 25.41  ? 2008 VAL A CB    1 
ATOM   4430  C  CG1   . VAL A 1 2008 ? 140.409 163.857 138.723 1.00 28.16  ? 2008 VAL A CG1   1 
ATOM   4431  C  CG2   . VAL A 1 2008 ? 139.000 163.433 140.743 1.00 32.21  ? 2008 VAL A CG2   1 
ATOM   4432  N  N     . SER A 1 2009 ? 138.882 166.499 137.181 1.00 23.18  ? 2009 SER A N     1 
ATOM   4433  C  CA    . SER A 1 2009 ? 139.092 166.959 135.815 1.00 23.66  ? 2009 SER A CA    1 
ATOM   4434  C  C     . SER A 1 2009 ? 140.396 166.391 135.261 1.00 26.43  ? 2009 SER A C     1 
ATOM   4435  O  O     . SER A 1 2009 ? 141.390 166.296 135.988 1.00 28.55  ? 2009 SER A O     1 
ATOM   4436  C  CB    . SER A 1 2009 ? 139.131 168.482 135.759 1.00 21.39  ? 2009 SER A CB    1 
ATOM   4437  O  OG    . SER A 1 2009 ? 139.392 168.943 134.445 1.00 25.60  ? 2009 SER A OG    1 
ATOM   4438  N  N     . PRO A 1 2010 ? 140.414 166.005 133.981 1.00 23.47  ? 2010 PRO A N     1 
ATOM   4439  C  CA    . PRO A 1 2010 ? 141.637 165.420 133.408 1.00 27.26  ? 2010 PRO A CA    1 
ATOM   4440  C  C     . PRO A 1 2010 ? 142.815 166.378 133.356 1.00 27.51  ? 2010 PRO A C     1 
ATOM   4441  O  O     . PRO A 1 2010 ? 143.954 165.918 133.215 1.00 31.79  ? 2010 PRO A O     1 
ATOM   4442  C  CB    . PRO A 1 2010 ? 141.199 164.999 131.999 1.00 30.07  ? 2010 PRO A CB    1 
ATOM   4443  C  CG    . PRO A 1 2010 ? 140.027 165.871 131.692 1.00 27.97  ? 2010 PRO A CG    1 
ATOM   4444  C  CD    . PRO A 1 2010 ? 139.322 166.083 132.998 1.00 25.28  ? 2010 PRO A CD    1 
ATOM   4445  N  N     . ASP A 1 2011 ? 142.586 167.685 133.464 1.00 19.16  ? 2011 ASP A N     1 
ATOM   4446  C  CA    . ASP A 1 2011 ? 143.672 168.657 133.432 1.00 16.38  ? 2011 ASP A CA    1 
ATOM   4447  C  C     . ASP A 1 2011 ? 144.382 168.796 134.772 1.00 17.24  ? 2011 ASP A C     1 
ATOM   4448  O  O     . ASP A 1 2011 ? 145.352 169.557 134.863 1.00 16.10  ? 2011 ASP A O     1 
ATOM   4449  C  CB    . ASP A 1 2011 ? 143.142 170.021 132.985 1.00 16.70  ? 2011 ASP A CB    1 
ATOM   4450  C  CG    . ASP A 1 2011 ? 142.781 170.050 131.514 1.00 29.14  ? 2011 ASP A CG    1 
ATOM   4451  O  OD1   . ASP A 1 2011 ? 142.633 168.963 130.917 1.00 34.65  ? 2011 ASP A OD1   1 
ATOM   4452  O  OD2   . ASP A 1 2011 ? 142.650 171.158 130.954 1.00 24.24  ? 2011 ASP A OD2   1 
ATOM   4453  N  N     . MET A 1 2012 ? 143.929 168.089 135.802 1.00 13.15  ? 2012 MET A N     1 
ATOM   4454  C  CA    . MET A 1 2012 ? 144.563 168.146 137.108 1.00 9.76   ? 2012 MET A CA    1 
ATOM   4455  C  C     . MET A 1 2012 ? 145.930 167.473 137.085 1.00 10.94  ? 2012 MET A C     1 
ATOM   4456  O  O     . MET A 1 2012 ? 146.141 166.461 136.411 1.00 13.07  ? 2012 MET A O     1 
ATOM   4457  C  CB    . MET A 1 2012 ? 143.680 167.477 138.162 1.00 16.81  ? 2012 MET A CB    1 
ATOM   4458  C  CG    . MET A 1 2012 ? 143.899 167.997 139.570 1.00 15.98  ? 2012 MET A CG    1 
ATOM   4459  S  SD    . MET A 1 2012 ? 145.050 166.958 140.486 1.00 20.64  ? 2012 MET A SD    1 
ATOM   4460  C  CE    . MET A 1 2012 ? 144.968 167.704 142.110 1.00 15.43  ? 2012 MET A CE    1 
ATOM   4461  N  N     . ALA A 1 2013 ? 146.863 168.052 137.837 1.00 7.75   ? 2013 ALA A N     1 
ATOM   4462  C  CA    . ALA A 1 2013 ? 148.188 167.477 137.993 1.00 4.82   ? 2013 ALA A CA    1 
ATOM   4463  C  C     . ALA A 1 2013 ? 148.781 167.961 139.306 1.00 4.82   ? 2013 ALA A C     1 
ATOM   4464  O  O     . ALA A 1 2013 ? 148.448 169.041 139.799 1.00 7.37   ? 2013 ALA A O     1 
ATOM   4465  C  CB    . ALA A 1 2013 ? 149.107 167.840 136.822 1.00 4.89   ? 2013 ALA A CB    1 
ATOM   4466  N  N     . ILE A 1 2014 ? 149.670 167.146 139.867 1.00 3.12   ? 2014 ILE A N     1 
ATOM   4467  C  CA    . ILE A 1 2014 ? 150.335 167.450 141.128 1.00 2.68   ? 2014 ILE A CA    1 
ATOM   4468  C  C     . ILE A 1 2014 ? 151.838 167.434 140.895 1.00 2.40   ? 2014 ILE A C     1 
ATOM   4469  O  O     . ILE A 1 2014 ? 152.371 166.480 140.320 1.00 1.90   ? 2014 ILE A O     1 
ATOM   4470  C  CB    . ILE A 1 2014 ? 149.952 166.452 142.237 1.00 3.31   ? 2014 ILE A CB    1 
ATOM   4471  C  CG1   . ILE A 1 2014 ? 148.435 166.388 142.402 1.00 5.46   ? 2014 ILE A CG1   1 
ATOM   4472  C  CG2   . ILE A 1 2014 ? 150.610 166.839 143.548 1.00 3.41   ? 2014 ILE A CG2   1 
ATOM   4473  C  CD1   . ILE A 1 2014 ? 147.981 165.404 143.454 1.00 8.39   ? 2014 ILE A CD1   1 
ATOM   4474  N  N     . PHE A 1 2015 ? 152.513 168.490 141.333 1.00 2.66   ? 2015 PHE A N     1 
ATOM   4475  C  CA    . PHE A 1 2015 ? 153.963 168.587 141.265 1.00 2.33   ? 2015 PHE A CA    1 
ATOM   4476  C  C     . PHE A 1 2015 ? 154.490 169.065 142.608 1.00 4.65   ? 2015 PHE A C     1 
ATOM   4477  O  O     . PHE A 1 2015 ? 153.941 169.995 143.204 1.00 5.02   ? 2015 PHE A O     1 
ATOM   4478  C  CB    . PHE A 1 2015 ? 154.415 169.539 140.151 1.00 2.43   ? 2015 PHE A CB    1 
ATOM   4479  C  CG    . PHE A 1 2015 ? 154.054 169.072 138.772 1.00 2.38   ? 2015 PHE A CG    1 
ATOM   4480  C  CD1   . PHE A 1 2015 ? 152.815 169.361 138.227 1.00 1.92   ? 2015 PHE A CD1   1 
ATOM   4481  C  CD2   . PHE A 1 2015 ? 154.958 168.347 138.018 1.00 1.90   ? 2015 PHE A CD2   1 
ATOM   4482  C  CE1   . PHE A 1 2015 ? 152.485 168.930 136.960 1.00 1.67   ? 2015 PHE A CE1   1 
ATOM   4483  C  CE2   . PHE A 1 2015 ? 154.634 167.915 136.750 1.00 1.97   ? 2015 PHE A CE2   1 
ATOM   4484  C  CZ    . PHE A 1 2015 ? 153.397 168.207 136.220 1.00 2.37   ? 2015 PHE A CZ    1 
ATOM   4485  N  N     . ILE A 1 2016 ? 155.550 168.418 143.081 1.00 4.93   ? 2016 ILE A N     1 
ATOM   4486  C  CA    . ILE A 1 2016 ? 156.181 168.753 144.350 1.00 6.14   ? 2016 ILE A CA    1 
ATOM   4487  C  C     . ILE A 1 2016 ? 157.618 169.164 144.071 1.00 6.00   ? 2016 ILE A C     1 
ATOM   4488  O  O     . ILE A 1 2016 ? 158.257 168.630 143.158 1.00 5.28   ? 2016 ILE A O     1 
ATOM   4489  C  CB    . ILE A 1 2016 ? 156.119 167.579 145.346 1.00 5.78   ? 2016 ILE A CB    1 
ATOM   4490  C  CG1   . ILE A 1 2016 ? 156.817 166.345 144.772 1.00 5.29   ? 2016 ILE A CG1   1 
ATOM   4491  C  CG2   . ILE A 1 2016 ? 154.677 167.256 145.697 1.00 6.37   ? 2016 ILE A CG2   1 
ATOM   4492  C  CD1   . ILE A 1 2016 ? 156.846 165.169 145.716 1.00 5.08   ? 2016 ILE A CD1   1 
ATOM   4493  N  N     . THR A 1 2017 ? 158.111 170.132 144.836 1.00 9.50   ? 2017 THR A N     1 
ATOM   4494  C  CA    . THR A 1 2017 ? 159.473 170.628 144.706 1.00 8.46   ? 2017 THR A CA    1 
ATOM   4495  C  C     . THR A 1 2017 ? 160.137 170.620 146.074 1.00 13.70  ? 2017 THR A C     1 
ATOM   4496  O  O     . THR A 1 2017 ? 159.533 171.052 147.061 1.00 17.86  ? 2017 THR A O     1 
ATOM   4497  C  CB    . THR A 1 2017 ? 159.493 172.039 144.116 1.00 17.46  ? 2017 THR A CB    1 
ATOM   4498  O  OG1   . THR A 1 2017 ? 158.426 172.178 143.170 1.00 20.47  ? 2017 THR A OG1   1 
ATOM   4499  C  CG2   . THR A 1 2017 ? 160.811 172.299 143.423 1.00 15.54  ? 2017 THR A CG2   1 
ATOM   4500  N  N     . MET A 1 2018 ? 161.375 170.135 146.131 1.00 13.09  ? 2018 MET A N     1 
ATOM   4501  C  CA    . MET A 1 2018 ? 162.086 170.051 147.396 1.00 12.55  ? 2018 MET A CA    1 
ATOM   4502  C  C     . MET A 1 2018 ? 163.569 170.291 147.170 1.00 10.24  ? 2018 MET A C     1 
ATOM   4503  O  O     . MET A 1 2018 ? 164.071 170.186 146.048 1.00 9.46   ? 2018 MET A O     1 
ATOM   4504  C  CB    . MET A 1 2018 ? 161.906 168.689 148.076 1.00 13.94  ? 2018 MET A CB    1 
ATOM   4505  C  CG    . MET A 1 2018 ? 161.591 167.551 147.130 1.00 16.43  ? 2018 MET A CG    1 
ATOM   4506  S  SD    . MET A 1 2018 ? 160.657 166.246 147.940 1.00 11.78  ? 2018 MET A SD    1 
ATOM   4507  C  CE    . MET A 1 2018 ? 159.034 166.988 147.993 1.00 12.66  ? 2018 MET A CE    1 
ATOM   4508  N  N     . ASN A 1 2019 ? 164.256 170.621 148.256 1.00 19.04  ? 2019 ASN A N     1 
ATOM   4509  C  CA    . ASN A 1 2019 ? 165.708 170.581 148.306 1.00 17.98  ? 2019 ASN A CA    1 
ATOM   4510  C  C     . ASN A 1 2019 ? 166.091 169.485 149.291 1.00 20.23  ? 2019 ASN A C     1 
ATOM   4511  O  O     . ASN A 1 2019 ? 166.101 169.718 150.507 1.00 26.45  ? 2019 ASN A O     1 
ATOM   4512  C  CB    . ASN A 1 2019 ? 166.289 171.931 148.727 1.00 20.13  ? 2019 ASN A CB    1 
ATOM   4513  C  CG    . ASN A 1 2019 ? 167.805 171.956 148.678 1.00 24.03  ? 2019 ASN A CG    1 
ATOM   4514  O  OD1   . ASN A 1 2019 ? 168.446 170.973 148.306 1.00 20.85  ? 2019 ASN A OD1   1 
ATOM   4515  N  ND2   . ASN A 1 2019 ? 168.388 173.086 149.056 1.00 28.40  ? 2019 ASN A ND2   1 
ATOM   4516  N  N     . PRO A 1 2020 ? 166.404 168.277 148.813 1.00 20.94  ? 2020 PRO A N     1 
ATOM   4517  C  CA    . PRO A 1 2020 ? 166.700 167.170 149.732 1.00 22.47  ? 2020 PRO A CA    1 
ATOM   4518  C  C     . PRO A 1 2020 ? 168.012 167.322 150.483 1.00 27.65  ? 2020 PRO A C     1 
ATOM   4519  O  O     . PRO A 1 2020 ? 168.293 166.507 151.370 1.00 29.43  ? 2020 PRO A O     1 
ATOM   4520  C  CB    . PRO A 1 2020 ? 166.733 165.951 148.801 1.00 23.16  ? 2020 PRO A CB    1 
ATOM   4521  C  CG    . PRO A 1 2020 ? 167.155 166.510 147.486 1.00 19.77  ? 2020 PRO A CG    1 
ATOM   4522  C  CD    . PRO A 1 2020 ? 166.511 167.869 147.401 1.00 16.72  ? 2020 PRO A CD    1 
ATOM   4523  N  N     . GLY A 1 2021 ? 168.819 168.329 150.161 1.00 25.12  ? 2021 GLY A N     1 
ATOM   4524  C  CA    . GLY A 1 2021 ? 170.063 168.587 150.849 1.00 26.82  ? 2021 GLY A CA    1 
ATOM   4525  C  C     . GLY A 1 2021 ? 169.964 169.490 152.055 1.00 31.08  ? 2021 GLY A C     1 
ATOM   4526  O  O     . GLY A 1 2021 ? 170.987 169.762 152.691 1.00 39.24  ? 2021 GLY A O     1 
ATOM   4527  N  N     . TYR A 1 2022 ? 168.768 169.967 152.396 1.00 30.20  ? 2022 TYR A N     1 
ATOM   4528  C  CA    . TYR A 1 2022 ? 168.583 170.804 153.576 1.00 34.55  ? 2022 TYR A CA    1 
ATOM   4529  C  C     . TYR A 1 2022 ? 168.460 169.908 154.802 1.00 38.00  ? 2022 TYR A C     1 
ATOM   4530  O  O     . TYR A 1 2022 ? 167.546 169.081 154.887 1.00 38.50  ? 2022 TYR A O     1 
ATOM   4531  C  CB    . TYR A 1 2022 ? 167.351 171.692 153.426 1.00 35.07  ? 2022 TYR A CB    1 
ATOM   4532  C  CG    . TYR A 1 2022 ? 167.612 173.004 152.722 1.00 38.24  ? 2022 TYR A CG    1 
ATOM   4533  C  CD1   . TYR A 1 2022 ? 168.861 173.607 152.775 1.00 41.08  ? 2022 TYR A CD1   1 
ATOM   4534  C  CD2   . TYR A 1 2022 ? 166.603 173.648 152.018 1.00 39.49  ? 2022 TYR A CD2   1 
ATOM   4535  C  CE1   . TYR A 1 2022 ? 169.103 174.808 152.137 1.00 36.48  ? 2022 TYR A CE1   1 
ATOM   4536  C  CE2   . TYR A 1 2022 ? 166.835 174.851 151.378 1.00 44.54  ? 2022 TYR A CE2   1 
ATOM   4537  C  CZ    . TYR A 1 2022 ? 168.086 175.426 151.440 1.00 45.13  ? 2022 TYR A CZ    1 
ATOM   4538  O  OH    . TYR A 1 2022 ? 168.322 176.623 150.805 1.00 46.82  ? 2022 TYR A OH    1 
ATOM   4539  N  N     . ALA A 1 2023 ? 169.383 170.064 155.748 1.00 44.45  ? 2023 ALA A N     1 
ATOM   4540  C  CA    . ALA A 1 2023 ? 169.296 169.326 156.998 1.00 42.54  ? 2023 ALA A CA    1 
ATOM   4541  C  C     . ALA A 1 2023 ? 168.090 169.794 157.802 1.00 44.03  ? 2023 ALA A C     1 
ATOM   4542  O  O     . ALA A 1 2023 ? 167.774 170.986 157.844 1.00 44.56  ? 2023 ALA A O     1 
ATOM   4543  C  CB    . ALA A 1 2023 ? 170.578 169.503 157.812 1.00 35.40  ? 2023 ALA A CB    1 
ATOM   4544  N  N     . GLY A 1 2024 ? 167.414 168.846 158.443 1.00 37.44  ? 2024 GLY A N     1 
ATOM   4545  C  CA    . GLY A 1 2024 ? 166.225 169.158 159.207 1.00 38.22  ? 2024 GLY A CA    1 
ATOM   4546  C  C     . GLY A 1 2024 ? 164.935 169.138 158.424 1.00 39.06  ? 2024 GLY A C     1 
ATOM   4547  O  O     . GLY A 1 2024 ? 163.936 169.696 158.891 1.00 37.91  ? 2024 GLY A O     1 
ATOM   4548  N  N     . ARG A 1 2025 ? 164.921 168.520 157.248 1.00 37.14  ? 2025 ARG A N     1 
ATOM   4549  C  CA    . ARG A 1 2025 ? 163.724 168.406 156.430 1.00 26.47  ? 2025 ARG A CA    1 
ATOM   4550  C  C     . ARG A 1 2025 ? 163.194 166.980 156.490 1.00 24.43  ? 2025 ARG A C     1 
ATOM   4551  O  O     . ARG A 1 2025 ? 163.954 166.023 156.657 1.00 29.78  ? 2025 ARG A O     1 
ATOM   4552  C  CB    . ARG A 1 2025 ? 164.005 168.800 154.978 1.00 27.88  ? 2025 ARG A CB    1 
ATOM   4553  C  CG    . ARG A 1 2025 ? 164.271 170.281 154.785 1.00 28.19  ? 2025 ARG A CG    1 
ATOM   4554  C  CD    . ARG A 1 2025 ? 162.979 171.054 154.604 1.00 25.91  ? 2025 ARG A CD    1 
ATOM   4555  N  NE    . ARG A 1 2025 ? 163.184 172.489 154.746 1.00 29.82  ? 2025 ARG A NE    1 
ATOM   4556  C  CZ    . ARG A 1 2025 ? 163.264 173.340 153.732 1.00 31.31  ? 2025 ARG A CZ    1 
ATOM   4557  N  NH1   . ARG A 1 2025 ? 163.160 172.933 152.478 1.00 31.85  ? 2025 ARG A NH1   1 
ATOM   4558  N  NH2   . ARG A 1 2025 ? 163.454 174.632 153.983 1.00 32.50  ? 2025 ARG A NH2   1 
ATOM   4559  N  N     . SER A 1 2026 ? 161.878 166.851 156.355 1.00 19.11  ? 2026 SER A N     1 
ATOM   4560  C  CA    . SER A 1 2026 ? 161.239 165.549 156.459 1.00 21.36  ? 2026 SER A CA    1 
ATOM   4561  C  C     . SER A 1 2026 ? 161.630 164.652 155.291 1.00 21.80  ? 2026 SER A C     1 
ATOM   4562  O  O     . SER A 1 2026 ? 161.876 165.115 154.173 1.00 19.48  ? 2026 SER A O     1 
ATOM   4563  C  CB    . SER A 1 2026 ? 159.721 165.704 156.507 1.00 22.35  ? 2026 SER A CB    1 
ATOM   4564  O  OG    . SER A 1 2026 ? 159.329 166.569 157.557 1.00 22.89  ? 2026 SER A OG    1 
ATOM   4565  N  N     . ASN A 1 2027 ? 161.685 163.353 155.564 1.00 25.03  ? 2027 ASN A N     1 
ATOM   4566  C  CA    . ASN A 1 2027 ? 161.969 162.345 154.553 1.00 23.90  ? 2027 ASN A CA    1 
ATOM   4567  C  C     . ASN A 1 2027 ? 160.649 161.770 154.060 1.00 22.42  ? 2027 ASN A C     1 
ATOM   4568  O  O     . ASN A 1 2027 ? 159.833 161.302 154.862 1.00 23.73  ? 2027 ASN A O     1 
ATOM   4569  C  CB    . ASN A 1 2027 ? 162.864 161.242 155.117 1.00 23.88  ? 2027 ASN A CB    1 
ATOM   4570  C  CG    . ASN A 1 2027 ? 164.320 161.422 154.738 1.00 37.24  ? 2027 ASN A CG    1 
ATOM   4571  O  OD1   . ASN A 1 2027 ? 165.189 161.543 155.601 1.00 49.59  ? 2027 ASN A OD1   1 
ATOM   4572  N  ND2   . ASN A 1 2027 ? 164.593 161.442 153.439 1.00 38.85  ? 2027 ASN A ND2   1 
ATOM   4573  N  N     . LEU A 1 2028 ? 160.439 161.814 152.752 1.00 14.49  ? 2028 LEU A N     1 
ATOM   4574  C  CA    . LEU A 1 2028 ? 159.194 161.315 152.182 1.00 15.02  ? 2028 LEU A CA    1 
ATOM   4575  C  C     . LEU A 1 2028 ? 159.101 159.806 152.373 1.00 14.40  ? 2028 LEU A C     1 
ATOM   4576  O  O     . LEU A 1 2028 ? 160.084 159.095 152.134 1.00 15.56  ? 2028 LEU A O     1 
ATOM   4577  C  CB    . LEU A 1 2028 ? 159.101 161.653 150.695 1.00 14.88  ? 2028 LEU A CB    1 
ATOM   4578  C  CG    . LEU A 1 2028 ? 158.529 162.996 150.230 1.00 14.41  ? 2028 LEU A CG    1 
ATOM   4579  C  CD1   . LEU A 1 2028 ? 158.961 164.150 151.121 1.00 10.29  ? 2028 LEU A CD1   1 
ATOM   4580  C  CD2   . LEU A 1 2028 ? 158.914 163.254 148.783 1.00 24.00  ? 2028 LEU A CD2   1 
ATOM   4581  N  N     . PRO A 1 2029 ? 157.956 159.281 152.806 1.00 13.81  ? 2029 PRO A N     1 
ATOM   4582  C  CA    . PRO A 1 2029 ? 157.783 157.826 152.828 1.00 13.71  ? 2029 PRO A CA    1 
ATOM   4583  C  C     . PRO A 1 2029 ? 157.857 157.256 151.420 1.00 14.48  ? 2029 PRO A C     1 
ATOM   4584  O  O     . PRO A 1 2029 ? 157.506 157.915 150.439 1.00 16.77  ? 2029 PRO A O     1 
ATOM   4585  C  CB    . PRO A 1 2029 ? 156.391 157.636 153.444 1.00 12.83  ? 2029 PRO A CB    1 
ATOM   4586  C  CG    . PRO A 1 2029 ? 155.715 158.959 153.307 1.00 10.82  ? 2029 PRO A CG    1 
ATOM   4587  C  CD    . PRO A 1 2029 ? 156.795 159.988 153.371 1.00 13.19  ? 2029 PRO A CD    1 
ATOM   4588  N  N     . ASP A 1 2030 ? 158.335 156.012 151.330 1.00 15.54  ? 2030 ASP A N     1 
ATOM   4589  C  CA    . ASP A 1 2030 ? 158.566 155.398 150.026 1.00 16.94  ? 2030 ASP A CA    1 
ATOM   4590  C  C     . ASP A 1 2030 ? 157.274 155.240 149.236 1.00 17.07  ? 2030 ASP A C     1 
ATOM   4591  O  O     . ASP A 1 2030 ? 157.276 155.398 148.009 1.00 16.98  ? 2030 ASP A O     1 
ATOM   4592  C  CB    . ASP A 1 2030 ? 159.257 154.046 150.196 1.00 25.95  ? 2030 ASP A CB    1 
ATOM   4593  C  CG    . ASP A 1 2030 ? 160.626 154.169 150.838 1.00 36.66  ? 2030 ASP A CG    1 
ATOM   4594  O  OD1   . ASP A 1 2030 ? 161.268 155.227 150.675 1.00 32.77  ? 2030 ASP A OD1   1 
ATOM   4595  O  OD2   . ASP A 1 2030 ? 161.060 153.208 151.507 1.00 41.32  ? 2030 ASP A OD2   1 
ATOM   4596  N  N     . ASN A 1 2031 ? 156.165 154.927 149.909 1.00 17.09  ? 2031 ASN A N     1 
ATOM   4597  C  CA    . ASN A 1 2031 ? 154.889 154.809 149.213 1.00 16.27  ? 2031 ASN A CA    1 
ATOM   4598  C  C     . ASN A 1 2031 ? 154.409 156.144 148.658 1.00 12.80  ? 2031 ASN A C     1 
ATOM   4599  O  O     . ASN A 1 2031 ? 153.539 156.160 147.782 1.00 10.84  ? 2031 ASN A O     1 
ATOM   4600  C  CB    . ASN A 1 2031 ? 153.832 154.211 150.142 1.00 12.24  ? 2031 ASN A CB    1 
ATOM   4601  C  CG    . ASN A 1 2031 ? 153.386 155.179 151.215 1.00 11.42  ? 2031 ASN A CG    1 
ATOM   4602  O  OD1   . ASN A 1 2031 ? 154.209 155.780 151.904 1.00 15.40  ? 2031 ASN A OD1   1 
ATOM   4603  N  ND2   . ASN A 1 2031 ? 152.077 155.331 151.368 1.00 11.93  ? 2031 ASN A ND2   1 
ATOM   4604  N  N     . LEU A 1 2032 ? 154.949 157.259 149.149 1.00 10.53  ? 2032 LEU A N     1 
ATOM   4605  C  CA    . LEU A 1 2032 ? 154.660 158.568 148.581 1.00 10.18  ? 2032 LEU A CA    1 
ATOM   4606  C  C     . LEU A 1 2032 ? 155.607 158.915 147.440 1.00 11.18  ? 2032 LEU A C     1 
ATOM   4607  O  O     . LEU A 1 2032 ? 155.187 159.520 146.448 1.00 8.74   ? 2032 LEU A O     1 
ATOM   4608  C  CB    . LEU A 1 2032 ? 154.736 159.643 149.668 1.00 11.74  ? 2032 LEU A CB    1 
ATOM   4609  C  CG    . LEU A 1 2032 ? 154.559 161.098 149.231 1.00 8.82   ? 2032 LEU A CG    1 
ATOM   4610  C  CD1   . LEU A 1 2032 ? 153.154 161.331 148.708 1.00 8.38   ? 2032 LEU A CD1   1 
ATOM   4611  C  CD2   . LEU A 1 2032 ? 154.869 162.043 150.378 1.00 11.92  ? 2032 LEU A CD2   1 
ATOM   4612  N  N     . LYS A 1 2033 ? 156.882 158.538 147.564 1.00 13.09  ? 2033 LYS A N     1 
ATOM   4613  C  CA    . LYS A 1 2033 ? 157.851 158.825 146.513 1.00 10.68  ? 2033 LYS A CA    1 
ATOM   4614  C  C     . LYS A 1 2033 ? 157.546 158.052 145.238 1.00 8.17   ? 2033 LYS A C     1 
ATOM   4615  O  O     . LYS A 1 2033 ? 157.796 158.553 144.136 1.00 10.27  ? 2033 LYS A O     1 
ATOM   4616  C  CB    . LYS A 1 2033 ? 159.263 158.509 147.003 1.00 9.91   ? 2033 LYS A CB    1 
ATOM   4617  C  CG    . LYS A 1 2033 ? 159.887 159.621 147.827 1.00 9.49   ? 2033 LYS A CG    1 
ATOM   4618  C  CD    . LYS A 1 2033 ? 161.361 159.366 148.081 1.00 16.16  ? 2033 LYS A CD    1 
ATOM   4619  C  CE    . LYS A 1 2033 ? 161.565 158.214 149.051 1.00 16.84  ? 2033 LYS A CE    1 
ATOM   4620  N  NZ    . LYS A 1 2033 ? 162.987 158.095 149.472 1.00 18.72  ? 2033 LYS A NZ    1 
ATOM   4621  N  N     . LYS A 1 2034 ? 157.011 156.836 145.363 1.00 9.28   ? 2034 LYS A N     1 
ATOM   4622  C  CA    . LYS A 1 2034 ? 156.633 156.051 144.194 1.00 9.93   ? 2034 LYS A CA    1 
ATOM   4623  C  C     . LYS A 1 2034 ? 155.454 156.651 143.442 1.00 9.08   ? 2034 LYS A C     1 
ATOM   4624  O  O     . LYS A 1 2034 ? 155.166 156.214 142.323 1.00 14.92  ? 2034 LYS A O     1 
ATOM   4625  C  CB    . LYS A 1 2034 ? 156.304 154.617 144.609 1.00 12.52  ? 2034 LYS A CB    1 
ATOM   4626  C  CG    . LYS A 1 2034 ? 155.093 154.502 145.518 1.00 14.16  ? 2034 LYS A CG    1 
ATOM   4627  C  CD    . LYS A 1 2034 ? 154.499 153.104 145.475 1.00 20.04  ? 2034 LYS A CD    1 
ATOM   4628  C  CE    . LYS A 1 2034 ? 153.315 153.034 144.530 1.00 23.96  ? 2034 LYS A CE    1 
ATOM   4629  N  NZ    . LYS A 1 2034 ? 153.133 151.665 143.974 1.00 30.44  ? 2034 LYS A NZ    1 
ATOM   4630  N  N     . LEU A 1 2035 ? 154.769 157.630 144.024 1.00 6.93   ? 2035 LEU A N     1 
ATOM   4631  C  CA    . LEU A 1 2035 ? 153.655 158.308 143.380 1.00 6.80   ? 2035 LEU A CA    1 
ATOM   4632  C  C     . LEU A 1 2035 ? 154.103 159.469 142.502 1.00 5.45   ? 2035 LEU A C     1 
ATOM   4633  O  O     . LEU A 1 2035 ? 153.258 160.129 141.890 1.00 5.72   ? 2035 LEU A O     1 
ATOM   4634  C  CB    . LEU A 1 2035 ? 152.673 158.815 144.440 1.00 7.66   ? 2035 LEU A CB    1 
ATOM   4635  C  CG    . LEU A 1 2035 ? 151.375 158.034 144.643 1.00 7.71   ? 2035 LEU A CG    1 
ATOM   4636  C  CD1   . LEU A 1 2035 ? 151.642 156.540 144.693 1.00 12.04  ? 2035 LEU A CD1   1 
ATOM   4637  C  CD2   . LEU A 1 2035 ? 150.692 158.504 145.913 1.00 13.09  ? 2035 LEU A CD2   1 
ATOM   4638  N  N     . PHE A 1 2036 ? 155.405 159.730 142.432 1.00 5.35   ? 2036 PHE A N     1 
ATOM   4639  C  CA    . PHE A 1 2036 ? 155.954 160.861 141.701 1.00 3.71   ? 2036 PHE A CA    1 
ATOM   4640  C  C     . PHE A 1 2036 ? 157.140 160.406 140.866 1.00 5.51   ? 2036 PHE A C     1 
ATOM   4641  O  O     . PHE A 1 2036 ? 157.778 159.396 141.176 1.00 8.46   ? 2036 PHE A O     1 
ATOM   4642  C  CB    . PHE A 1 2036 ? 156.405 161.973 142.653 1.00 3.47   ? 2036 PHE A CB    1 
ATOM   4643  C  CG    . PHE A 1 2036 ? 155.287 162.620 143.415 1.00 3.92   ? 2036 PHE A CG    1 
ATOM   4644  C  CD1   . PHE A 1 2036 ? 154.853 162.091 144.618 1.00 4.26   ? 2036 PHE A CD1   1 
ATOM   4645  C  CD2   . PHE A 1 2036 ? 154.688 163.775 142.944 1.00 3.69   ? 2036 PHE A CD2   1 
ATOM   4646  C  CE1   . PHE A 1 2036 ? 153.830 162.689 145.324 1.00 4.51   ? 2036 PHE A CE1   1 
ATOM   4647  C  CE2   . PHE A 1 2036 ? 153.665 164.379 143.644 1.00 4.60   ? 2036 PHE A CE2   1 
ATOM   4648  C  CZ    . PHE A 1 2036 ? 153.236 163.835 144.838 1.00 6.05   ? 2036 PHE A CZ    1 
ATOM   4649  N  N     . ARG A 1 2037 ? 157.432 161.158 139.810 1.00 4.93   ? 2037 ARG A N     1 
ATOM   4650  C  CA    . ARG A 1 2037 ? 158.639 160.957 139.019 1.00 4.23   ? 2037 ARG A CA    1 
ATOM   4651  C  C     . ARG A 1 2037 ? 159.610 162.091 139.317 1.00 4.18   ? 2037 ARG A C     1 
ATOM   4652  O  O     . ARG A 1 2037 ? 159.315 163.258 139.037 1.00 4.58   ? 2037 ARG A O     1 
ATOM   4653  C  CB    . ARG A 1 2037 ? 158.313 160.902 137.528 1.00 4.14   ? 2037 ARG A CB    1 
ATOM   4654  C  CG    . ARG A 1 2037 ? 157.693 159.594 137.078 1.00 7.28   ? 2037 ARG A CG    1 
ATOM   4655  C  CD    . ARG A 1 2037 ? 158.659 158.434 137.270 1.00 10.08  ? 2037 ARG A CD    1 
ATOM   4656  N  NE    . ARG A 1 2037 ? 159.661 158.348 136.211 1.00 16.30  ? 2037 ARG A NE    1 
ATOM   4657  C  CZ    . ARG A 1 2037 ? 159.400 158.169 134.922 1.00 15.80  ? 2037 ARG A CZ    1 
ATOM   4658  N  NH1   . ARG A 1 2037 ? 158.165 157.995 134.479 1.00 12.80  ? 2037 ARG A NH1   1 
ATOM   4659  N  NH2   . ARG A 1 2037 ? 160.408 158.147 134.055 1.00 10.02  ? 2037 ARG A NH2   1 
ATOM   4660  N  N     . SER A 1 2038 ? 160.761 161.750 139.882 1.00 4.67   ? 2038 SER A N     1 
ATOM   4661  C  CA    . SER A 1 2038 ? 161.736 162.737 140.318 1.00 4.38   ? 2038 SER A CA    1 
ATOM   4662  C  C     . SER A 1 2038 ? 162.771 162.993 139.231 1.00 6.33   ? 2038 SER A C     1 
ATOM   4663  O  O     . SER A 1 2038 ? 163.151 162.091 138.480 1.00 10.72  ? 2038 SER A O     1 
ATOM   4664  C  CB    . SER A 1 2038 ? 162.435 162.279 141.600 1.00 8.25   ? 2038 SER A CB    1 
ATOM   4665  O  OG    . SER A 1 2038 ? 163.307 161.191 141.346 1.00 11.93  ? 2038 SER A OG    1 
ATOM   4666  N  N     . LEU A 1 2039 ? 163.223 164.242 139.156 1.00 5.49   ? 2039 LEU A N     1 
ATOM   4667  C  CA    . LEU A 1 2039 ? 164.301 164.628 138.257 1.00 5.67   ? 2039 LEU A CA    1 
ATOM   4668  C  C     . LEU A 1 2039 ? 165.226 165.587 138.986 1.00 5.29   ? 2039 LEU A C     1 
ATOM   4669  O  O     . LEU A 1 2039 ? 164.760 166.519 139.647 1.00 7.24   ? 2039 LEU A O     1 
ATOM   4670  C  CB    . LEU A 1 2039 ? 163.766 165.286 136.982 1.00 8.42   ? 2039 LEU A CB    1 
ATOM   4671  C  CG    . LEU A 1 2039 ? 164.806 166.154 136.273 1.00 6.89   ? 2039 LEU A CG    1 
ATOM   4672  C  CD1   . LEU A 1 2039 ? 165.792 165.297 135.491 1.00 7.12   ? 2039 LEU A CD1   1 
ATOM   4673  C  CD2   . LEU A 1 2039 ? 164.145 167.168 135.384 1.00 6.50   ? 2039 LEU A CD2   1 
ATOM   4674  N  N     . ALA A 1 2040 ? 166.530 165.358 138.864 1.00 7.46   ? 2040 ALA A N     1 
ATOM   4675  C  CA    . ALA A 1 2040 ? 167.533 166.224 139.471 1.00 6.08   ? 2040 ALA A CA    1 
ATOM   4676  C  C     . ALA A 1 2040 ? 167.790 167.409 138.548 1.00 6.31   ? 2040 ALA A C     1 
ATOM   4677  O  O     . ALA A 1 2040 ? 168.183 167.231 137.391 1.00 9.41   ? 2040 ALA A O     1 
ATOM   4678  C  CB    . ALA A 1 2040 ? 168.820 165.449 139.738 1.00 9.36   ? 2040 ALA A CB    1 
ATOM   4679  N  N     . MET A 1 2041 ? 167.562 168.614 139.055 1.00 6.64   ? 2041 MET A N     1 
ATOM   4680  C  CA    . MET A 1 2041 ? 167.923 169.851 138.368 1.00 10.27  ? 2041 MET A CA    1 
ATOM   4681  C  C     . MET A 1 2041 ? 168.906 170.581 139.275 1.00 12.11  ? 2041 MET A C     1 
ATOM   4682  O  O     . MET A 1 2041 ? 168.503 171.251 140.229 1.00 12.43  ? 2041 MET A O     1 
ATOM   4683  C  CB    . MET A 1 2041 ? 166.693 170.702 138.066 1.00 12.61  ? 2041 MET A CB    1 
ATOM   4684  C  CG    . MET A 1 2041 ? 165.523 169.928 137.483 1.00 8.35   ? 2041 MET A CG    1 
ATOM   4685  S  SD    . MET A 1 2041 ? 164.090 170.963 137.127 1.00 19.94  ? 2041 MET A SD    1 
ATOM   4686  C  CE    . MET A 1 2041 ? 164.836 172.588 137.121 1.00 10.06  ? 2041 MET A CE    1 
ATOM   4687  N  N     . THR A 1 2042 ? 170.193 170.444 138.980 1.00 11.59  ? 2042 THR A N     1 
ATOM   4688  C  CA    . THR A 1 2042 ? 171.240 170.963 139.850 1.00 11.84  ? 2042 THR A CA    1 
ATOM   4689  C  C     . THR A 1 2042 ? 172.084 172.048 139.206 1.00 15.78  ? 2042 THR A C     1 
ATOM   4690  O  O     . THR A 1 2042 ? 172.534 172.964 139.900 1.00 18.99  ? 2042 THR A O     1 
ATOM   4691  C  CB    . THR A 1 2042 ? 172.158 169.820 140.311 1.00 12.77  ? 2042 THR A CB    1 
ATOM   4692  O  OG1   . THR A 1 2042 ? 172.768 169.204 139.170 1.00 15.67  ? 2042 THR A OG1   1 
ATOM   4693  C  CG2   . THR A 1 2042 ? 171.361 168.777 141.076 1.00 14.15  ? 2042 THR A CG2   1 
ATOM   4694  N  N     . LYS A 1 2043 ? 172.315 171.975 137.895 1.00 15.06  ? 2043 LYS A N     1 
ATOM   4695  C  CA    . LYS A 1 2043 ? 173.204 172.899 137.192 1.00 15.07  ? 2043 LYS A CA    1 
ATOM   4696  C  C     . LYS A 1 2043 ? 172.443 173.543 136.042 1.00 17.99  ? 2043 LYS A C     1 
ATOM   4697  O  O     . LYS A 1 2043 ? 172.461 173.033 134.911 1.00 17.21  ? 2043 LYS A O     1 
ATOM   4698  C  CB    . LYS A 1 2043 ? 174.451 172.177 136.688 1.00 15.78  ? 2043 LYS A CB    1 
ATOM   4699  C  CG    . LYS A 1 2043 ? 175.570 172.076 137.712 1.00 21.22  ? 2043 LYS A CG    1 
ATOM   4700  C  CD    . LYS A 1 2043 ? 175.608 173.295 138.618 1.00 30.99  ? 2043 LYS A CD    1 
ATOM   4701  C  CE    . LYS A 1 2043 ? 176.423 173.028 139.872 1.00 32.79  ? 2043 LYS A CE    1 
ATOM   4702  N  NZ    . LYS A 1 2043 ? 176.812 174.292 140.555 1.00 45.75  ? 2043 LYS A NZ    1 
ATOM   4703  N  N     . PRO A 1 2044 ? 171.750 174.653 136.285 1.00 19.93  ? 2044 PRO A N     1 
ATOM   4704  C  CA    . PRO A 1 2044 ? 171.088 175.360 135.186 1.00 17.32  ? 2044 PRO A CA    1 
ATOM   4705  C  C     . PRO A 1 2044 ? 172.097 175.899 134.186 1.00 17.42  ? 2044 PRO A C     1 
ATOM   4706  O  O     . PRO A 1 2044 ? 173.220 176.271 134.536 1.00 22.00  ? 2044 PRO A O     1 
ATOM   4707  C  CB    . PRO A 1 2044 ? 170.341 176.498 135.891 1.00 17.46  ? 2044 PRO A CB    1 
ATOM   4708  C  CG    . PRO A 1 2044 ? 171.051 176.674 137.191 1.00 15.20  ? 2044 PRO A CG    1 
ATOM   4709  C  CD    . PRO A 1 2044 ? 171.527 175.310 137.584 1.00 17.69  ? 2044 PRO A CD    1 
ATOM   4710  N  N     . ASP A 1 2045 ? 171.680 175.935 132.920 1.00 14.91  ? 2045 ASP A N     1 
ATOM   4711  C  CA    . ASP A 1 2045 ? 172.528 176.436 131.839 1.00 13.99  ? 2045 ASP A CA    1 
ATOM   4712  C  C     . ASP A 1 2045 ? 172.441 177.959 131.829 1.00 14.10  ? 2045 ASP A C     1 
ATOM   4713  O  O     . ASP A 1 2045 ? 171.707 178.572 131.052 1.00 13.57  ? 2045 ASP A O     1 
ATOM   4714  C  CB    . ASP A 1 2045 ? 172.112 175.830 130.505 1.00 16.23  ? 2045 ASP A CB    1 
ATOM   4715  C  CG    . ASP A 1 2045 ? 171.943 174.324 130.575 1.00 20.83  ? 2045 ASP A CG    1 
ATOM   4716  O  OD1   . ASP A 1 2045 ? 170.788 173.853 130.626 1.00 14.70  ? 2045 ASP A OD1   1 
ATOM   4717  O  OD2   . ASP A 1 2045 ? 172.967 173.610 130.578 1.00 21.08  ? 2045 ASP A OD2   1 
ATOM   4718  N  N     . ARG A 1 2046 ? 173.219 178.575 132.724 1.00 13.31  ? 2046 ARG A N     1 
ATOM   4719  C  CA    . ARG A 1 2046 ? 173.179 180.027 132.872 1.00 12.21  ? 2046 ARG A CA    1 
ATOM   4720  C  C     . ARG A 1 2046 ? 173.664 180.740 131.618 1.00 10.57  ? 2046 ARG A C     1 
ATOM   4721  O  O     . ARG A 1 2046 ? 173.136 181.801 131.267 1.00 9.97   ? 2046 ARG A O     1 
ATOM   4722  C  CB    . ARG A 1 2046 ? 174.019 180.460 134.073 1.00 15.01  ? 2046 ARG A CB    1 
ATOM   4723  C  CG    . ARG A 1 2046 ? 173.738 179.692 135.349 1.00 15.01  ? 2046 ARG A CG    1 
ATOM   4724  C  CD    . ARG A 1 2046 ? 174.959 179.683 136.250 1.00 18.43  ? 2046 ARG A CD    1 
ATOM   4725  N  NE    . ARG A 1 2046 ? 174.650 179.194 137.588 1.00 24.17  ? 2046 ARG A NE    1 
ATOM   4726  C  CZ    . ARG A 1 2046 ? 175.032 179.792 138.709 1.00 22.55  ? 2046 ARG A CZ    1 
ATOM   4727  N  NH1   . ARG A 1 2046 ? 175.738 180.910 138.690 1.00 23.11  ? 2046 ARG A NH1   1 
ATOM   4728  N  NH2   . ARG A 1 2046 ? 174.698 179.253 139.878 1.00 17.63  ? 2046 ARG A NH2   1 
ATOM   4729  N  N     . GLN A 1 2047 ? 174.672 180.183 130.942 1.00 13.33  ? 2047 GLN A N     1 
ATOM   4730  C  CA    . GLN A 1 2047 ? 175.227 180.833 129.759 1.00 12.41  ? 2047 GLN A CA    1 
ATOM   4731  C  C     . GLN A 1 2047 ? 174.174 180.983 128.669 1.00 13.13  ? 2047 GLN A C     1 
ATOM   4732  O  O     . GLN A 1 2047 ? 174.061 182.041 128.039 1.00 14.49  ? 2047 GLN A O     1 
ATOM   4733  C  CB    . GLN A 1 2047 ? 176.429 180.038 129.247 1.00 13.97  ? 2047 GLN A CB    1 
ATOM   4734  C  CG    . GLN A 1 2047 ? 176.732 180.245 127.774 1.00 21.58  ? 2047 GLN A CG    1 
ATOM   4735  C  CD    . GLN A 1 2047 ? 177.901 181.180 127.548 1.00 36.23  ? 2047 GLN A CD    1 
ATOM   4736  O  OE1   . GLN A 1 2047 ? 178.597 181.562 128.488 1.00 35.77  ? 2047 GLN A OE1   1 
ATOM   4737  N  NE2   . GLN A 1 2047 ? 178.122 181.557 126.295 1.00 38.17  ? 2047 GLN A NE2   1 
ATOM   4738  N  N     . LEU A 1 2048 ? 173.386 179.931 128.435 1.00 10.89  ? 2048 LEU A N     1 
ATOM   4739  C  CA    . LEU A 1 2048 ? 172.329 180.015 127.434 1.00 7.78   ? 2048 LEU A CA    1 
ATOM   4740  C  C     . LEU A 1 2048 ? 171.224 180.965 127.878 1.00 8.69   ? 2048 LEU A C     1 
ATOM   4741  O  O     . LEU A 1 2048 ? 170.638 181.673 127.051 1.00 10.16  ? 2048 LEU A O     1 
ATOM   4742  C  CB    . LEU A 1 2048 ? 171.767 178.623 127.147 1.00 10.18  ? 2048 LEU A CB    1 
ATOM   4743  C  CG    . LEU A 1 2048 ? 170.651 178.536 126.106 1.00 9.22   ? 2048 LEU A CG    1 
ATOM   4744  C  CD1   . LEU A 1 2048 ? 171.178 178.903 124.730 1.00 6.99   ? 2048 LEU A CD1   1 
ATOM   4745  C  CD2   . LEU A 1 2048 ? 170.044 177.146 126.093 1.00 10.01  ? 2048 LEU A CD2   1 
ATOM   4746  N  N     . ILE A 1 2049 ? 170.924 180.995 129.179 1.00 8.48   ? 2049 ILE A N     1 
ATOM   4747  C  CA    . ILE A 1 2049 ? 169.920 181.925 129.692 1.00 6.47   ? 2049 ILE A CA    1 
ATOM   4748  C  C     . ILE A 1 2049 ? 170.375 183.363 129.480 1.00 8.49   ? 2049 ILE A C     1 
ATOM   4749  O  O     . ILE A 1 2049 ? 169.607 184.216 129.019 1.00 12.96  ? 2049 ILE A O     1 
ATOM   4750  C  CB    . ILE A 1 2049 ? 169.633 181.640 131.177 1.00 6.48   ? 2049 ILE A CB    1 
ATOM   4751  C  CG1   . ILE A 1 2049 ? 169.025 180.249 131.348 1.00 5.47   ? 2049 ILE A CG1   1 
ATOM   4752  C  CG2   . ILE A 1 2049 ? 168.702 182.692 131.751 1.00 6.46   ? 2049 ILE A CG2   1 
ATOM   4753  C  CD1   . ILE A 1 2049 ? 168.871 179.832 132.789 1.00 5.42   ? 2049 ILE A CD1   1 
ATOM   4754  N  N     . ALA A 1 2050 ? 171.634 183.652 129.814 1.00 8.46   ? 2050 ALA A N     1 
ATOM   4755  C  CA    . ALA A 1 2050 ? 172.148 185.010 129.676 1.00 8.91   ? 2050 ALA A CA    1 
ATOM   4756  C  C     . ALA A 1 2050 ? 172.193 185.441 128.216 1.00 13.65  ? 2050 ALA A C     1 
ATOM   4757  O  O     . ALA A 1 2050 ? 171.886 186.594 127.892 1.00 17.52  ? 2050 ALA A O     1 
ATOM   4758  C  CB    . ALA A 1 2050 ? 173.534 185.113 130.309 1.00 13.61  ? 2050 ALA A CB    1 
ATOM   4759  N  N     . GLN A 1 2051 ? 172.580 184.530 127.322 1.00 13.01  ? 2051 GLN A N     1 
ATOM   4760  C  CA    . GLN A 1 2051 ? 172.692 184.874 125.909 1.00 12.82  ? 2051 GLN A CA    1 
ATOM   4761  C  C     . GLN A 1 2051 ? 171.326 185.177 125.303 1.00 14.71  ? 2051 GLN A C     1 
ATOM   4762  O  O     . GLN A 1 2051 ? 171.164 186.159 124.571 1.00 20.48  ? 2051 GLN A O     1 
ATOM   4763  C  CB    . GLN A 1 2051 ? 173.382 183.739 125.151 1.00 15.79  ? 2051 GLN A CB    1 
ATOM   4764  C  CG    . GLN A 1 2051 ? 173.157 183.761 123.650 1.00 19.33  ? 2051 GLN A CG    1 
ATOM   4765  C  CD    . GLN A 1 2051 ? 173.519 182.446 122.992 1.00 32.14  ? 2051 GLN A CD    1 
ATOM   4766  O  OE1   . GLN A 1 2051 ? 174.491 181.795 123.373 1.00 32.27  ? 2051 GLN A OE1   1 
ATOM   4767  N  NE2   . GLN A 1 2051 ? 172.732 182.045 122.000 1.00 31.75  ? 2051 GLN A NE2   1 
ATOM   4768  N  N     . VAL A 1 2052 ? 170.328 184.342 125.602 1.00 12.44  ? 2052 VAL A N     1 
ATOM   4769  C  CA    . VAL A 1 2052 ? 169.006 184.532 125.014 1.00 9.79   ? 2052 VAL A CA    1 
ATOM   4770  C  C     . VAL A 1 2052 ? 168.330 185.771 125.590 1.00 11.54  ? 2052 VAL A C     1 
ATOM   4771  O  O     . VAL A 1 2052 ? 167.688 186.537 124.861 1.00 16.06  ? 2052 VAL A O     1 
ATOM   4772  C  CB    . VAL A 1 2052 ? 168.146 183.270 125.210 1.00 8.39   ? 2052 VAL A CB    1 
ATOM   4773  C  CG1   . VAL A 1 2052 ? 166.736 183.504 124.700 1.00 9.40   ? 2052 VAL A CG1   1 
ATOM   4774  C  CG2   . VAL A 1 2052 ? 168.775 182.091 124.489 1.00 9.74   ? 2052 VAL A CG2   1 
ATOM   4775  N  N     . MET A 1 2053 ? 168.458 185.988 126.901 1.00 10.79  ? 2053 MET A N     1 
ATOM   4776  C  CA    . MET A 1 2053 ? 167.827 187.149 127.521 1.00 12.14  ? 2053 MET A CA    1 
ATOM   4777  C  C     . MET A 1 2053 ? 168.384 188.452 126.964 1.00 15.01  ? 2053 MET A C     1 
ATOM   4778  O  O     . MET A 1 2053 ? 167.625 189.375 126.645 1.00 19.05  ? 2053 MET A O     1 
ATOM   4779  C  CB    . MET A 1 2053 ? 168.011 187.105 129.037 1.00 17.18  ? 2053 MET A CB    1 
ATOM   4780  C  CG    . MET A 1 2053 ? 166.912 186.380 129.783 1.00 14.85  ? 2053 MET A CG    1 
ATOM   4781  S  SD    . MET A 1 2053 ? 167.237 186.373 131.552 1.00 42.05  ? 2053 MET A SD    1 
ATOM   4782  C  CE    . MET A 1 2053 ? 166.420 187.894 132.024 1.00 23.03  ? 2053 MET A CE    1 
ATOM   4783  N  N     . LEU A 1 2054 ? 169.709 188.548 126.842 1.00 14.44  ? 2054 LEU A N     1 
ATOM   4784  C  CA    . LEU A 1 2054 ? 170.314 189.751 126.284 1.00 16.90  ? 2054 LEU A CA    1 
ATOM   4785  C  C     . LEU A 1 2054 ? 169.987 189.907 124.806 1.00 18.99  ? 2054 LEU A C     1 
ATOM   4786  O  O     . LEU A 1 2054 ? 169.830 191.034 124.323 1.00 24.37  ? 2054 LEU A O     1 
ATOM   4787  C  CB    . LEU A 1 2054 ? 171.825 189.724 126.498 1.00 19.85  ? 2054 LEU A CB    1 
ATOM   4788  C  CG    . LEU A 1 2054 ? 172.287 189.883 127.946 1.00 15.70  ? 2054 LEU A CG    1 
ATOM   4789  C  CD1   . LEU A 1 2054 ? 173.794 189.754 128.043 1.00 18.35  ? 2054 LEU A CD1   1 
ATOM   4790  C  CD2   . LEU A 1 2054 ? 171.827 191.218 128.503 1.00 19.02  ? 2054 LEU A CD2   1 
ATOM   4791  N  N     . TYR A 1 2055 ? 169.890 188.795 124.076 1.00 16.73  ? 2055 TYR A N     1 
ATOM   4792  C  CA    . TYR A 1 2055 ? 169.530 188.858 122.664 1.00 13.26  ? 2055 TYR A CA    1 
ATOM   4793  C  C     . TYR A 1 2055 ? 168.115 189.392 122.479 1.00 17.58  ? 2055 TYR A C     1 
ATOM   4794  O  O     . TYR A 1 2055 ? 167.856 190.174 121.557 1.00 26.74  ? 2055 TYR A O     1 
ATOM   4795  C  CB    . TYR A 1 2055 ? 169.678 187.474 122.034 1.00 13.88  ? 2055 TYR A CB    1 
ATOM   4796  C  CG    . TYR A 1 2055 ? 169.463 187.435 120.540 1.00 15.73  ? 2055 TYR A CG    1 
ATOM   4797  C  CD1   . TYR A 1 2055 ? 170.129 188.314 119.700 1.00 16.69  ? 2055 TYR A CD1   1 
ATOM   4798  C  CD2   . TYR A 1 2055 ? 168.609 186.503 119.969 1.00 18.26  ? 2055 TYR A CD2   1 
ATOM   4799  C  CE1   . TYR A 1 2055 ? 169.939 188.275 118.333 1.00 19.05  ? 2055 TYR A CE1   1 
ATOM   4800  C  CE2   . TYR A 1 2055 ? 168.414 186.456 118.605 1.00 20.57  ? 2055 TYR A CE2   1 
ATOM   4801  C  CZ    . TYR A 1 2055 ? 169.081 187.343 117.792 1.00 23.09  ? 2055 TYR A CZ    1 
ATOM   4802  O  OH    . TYR A 1 2055 ? 168.888 187.298 116.432 1.00 27.52  ? 2055 TYR A OH    1 
ATOM   4803  N  N     . SER A 1 2056 ? 167.188 188.984 123.346 1.00 13.23  ? 2056 SER A N     1 
ATOM   4804  C  CA    . SER A 1 2056 ? 165.808 189.441 123.249 1.00 12.26  ? 2056 SER A CA    1 
ATOM   4805  C  C     . SER A 1 2056 ? 165.612 190.856 123.775 1.00 19.15  ? 2056 SER A C     1 
ATOM   4806  O  O     . SER A 1 2056 ? 164.608 191.493 123.436 1.00 26.29  ? 2056 SER A O     1 
ATOM   4807  C  CB    . SER A 1 2056 ? 164.883 188.486 124.006 1.00 14.90  ? 2056 SER A CB    1 
ATOM   4808  O  OG    . SER A 1 2056 ? 165.207 188.452 125.385 1.00 19.79  ? 2056 SER A OG    1 
ATOM   4809  N  N     . GLN A 1 2057 ? 166.533 191.361 124.593 1.00 19.04  ? 2057 GLN A N     1 
ATOM   4810  C  CA    . GLN A 1 2057 ? 166.398 192.697 125.158 1.00 19.52  ? 2057 GLN A CA    1 
ATOM   4811  C  C     . GLN A 1 2057 ? 166.974 193.790 124.267 1.00 24.08  ? 2057 GLN A C     1 
ATOM   4812  O  O     . GLN A 1 2057 ? 166.759 194.973 124.552 1.00 29.32  ? 2057 GLN A O     1 
ATOM   4813  C  CB    . GLN A 1 2057 ? 167.063 192.759 126.537 1.00 20.62  ? 2057 GLN A CB    1 
ATOM   4814  C  CG    . GLN A 1 2057 ? 166.171 192.283 127.672 1.00 19.96  ? 2057 GLN A CG    1 
ATOM   4815  C  CD    . GLN A 1 2057 ? 166.942 192.017 128.951 1.00 28.36  ? 2057 GLN A CD    1 
ATOM   4816  O  OE1   . GLN A 1 2057 ? 168.144 192.267 129.028 1.00 32.23  ? 2057 GLN A OE1   1 
ATOM   4817  N  NE2   . GLN A 1 2057 ? 166.250 191.507 129.963 1.00 28.31  ? 2057 GLN A NE2   1 
ATOM   4818  N  N     . GLY A 1 2058 ? 167.689 193.433 123.204 1.00 23.02  ? 2058 GLY A N     1 
ATOM   4819  C  CA    . GLY A 1 2058 ? 168.215 194.406 122.270 1.00 23.32  ? 2058 GLY A CA    1 
ATOM   4820  C  C     . GLY A 1 2058 ? 169.710 194.635 122.315 1.00 27.35  ? 2058 GLY A C     1 
ATOM   4821  O  O     . GLY A 1 2058 ? 170.163 195.707 121.895 1.00 33.63  ? 2058 GLY A O     1 
ATOM   4822  N  N     . PHE A 1 2059 ? 170.491 193.680 122.810 1.00 27.81  ? 2059 PHE A N     1 
ATOM   4823  C  CA    . PHE A 1 2059 ? 171.938 193.834 122.847 1.00 25.89  ? 2059 PHE A CA    1 
ATOM   4824  C  C     . PHE A 1 2059 ? 172.560 193.212 121.602 1.00 31.31  ? 2059 PHE A C     1 
ATOM   4825  O  O     . PHE A 1 2059 ? 172.333 192.034 121.306 1.00 31.39  ? 2059 PHE A O     1 
ATOM   4826  C  CB    . PHE A 1 2059 ? 172.514 193.192 124.109 1.00 26.06  ? 2059 PHE A CB    1 
ATOM   4827  C  CG    . PHE A 1 2059 ? 172.168 193.926 125.376 1.00 23.42  ? 2059 PHE A CG    1 
ATOM   4828  C  CD1   . PHE A 1 2059 ? 170.925 193.774 125.965 1.00 23.52  ? 2059 PHE A CD1   1 
ATOM   4829  C  CD2   . PHE A 1 2059 ? 173.086 194.773 125.973 1.00 27.75  ? 2059 PHE A CD2   1 
ATOM   4830  C  CE1   . PHE A 1 2059 ? 170.606 194.448 127.128 1.00 23.25  ? 2059 PHE A CE1   1 
ATOM   4831  C  CE2   . PHE A 1 2059 ? 172.773 195.450 127.137 1.00 27.78  ? 2059 PHE A CE2   1 
ATOM   4832  C  CZ    . PHE A 1 2059 ? 171.531 195.287 127.714 1.00 21.33  ? 2059 PHE A CZ    1 
ATOM   4833  N  N     . ARG A 1 2060 ? 173.340 194.010 120.868 1.00 33.18  ? 2060 ARG A N     1 
ATOM   4834  C  CA    . ARG A 1 2060 ? 173.999 193.501 119.669 1.00 30.93  ? 2060 ARG A CA    1 
ATOM   4835  C  C     . ARG A 1 2060 ? 175.111 192.519 120.007 1.00 34.22  ? 2060 ARG A C     1 
ATOM   4836  O  O     . ARG A 1 2060 ? 175.357 191.577 119.245 1.00 40.30  ? 2060 ARG A O     1 
ATOM   4837  C  CB    . ARG A 1 2060 ? 174.557 194.657 118.841 1.00 34.28  ? 2060 ARG A CB    1 
ATOM   4838  C  CG    . ARG A 1 2060 ? 173.720 195.917 118.890 1.00 40.90  ? 2060 ARG A CG    1 
ATOM   4839  C  CD    . ARG A 1 2060 ? 172.514 195.799 117.963 1.00 49.66  ? 2060 ARG A CD    1 
ATOM   4840  N  NE    . ARG A 1 2060 ? 172.801 196.031 116.548 1.00 57.06  ? 2060 ARG A NE    1 
ATOM   4841  C  CZ    . ARG A 1 2060 ? 173.467 197.066 116.048 1.00 63.20  ? 2060 ARG A CZ    1 
ATOM   4842  N  NH1   . ARG A 1 2060 ? 173.882 198.064 116.811 1.00 65.32  ? 2060 ARG A NH1   1 
ATOM   4843  N  NH2   . ARG A 1 2060 ? 173.701 197.113 114.740 1.00 56.10  ? 2060 ARG A NH2   1 
ATOM   4844  N  N     . THR A 1 2061 ? 175.788 192.717 121.135 1.00 30.37  ? 2061 THR A N     1 
ATOM   4845  C  CA    . THR A 1 2061 ? 176.913 191.883 121.551 1.00 32.46  ? 2061 THR A CA    1 
ATOM   4846  C  C     . THR A 1 2061 ? 176.510 190.893 122.634 1.00 34.30  ? 2061 THR A C     1 
ATOM   4847  O  O     . THR A 1 2061 ? 177.265 190.650 123.579 1.00 36.48  ? 2061 THR A O     1 
ATOM   4848  C  CB    . THR A 1 2061 ? 178.070 192.757 122.027 1.00 34.06  ? 2061 THR A CB    1 
ATOM   4849  O  OG1   . THR A 1 2061 ? 177.613 193.633 123.065 1.00 35.59  ? 2061 THR A OG1   1 
ATOM   4850  C  CG2   . THR A 1 2061 ? 178.614 193.589 120.875 1.00 37.82  ? 2061 THR A CG2   1 
ATOM   4851  N  N     . ALA A 1 2062 ? 175.313 190.312 122.513 1.00 31.46  ? 2062 ALA A N     1 
ATOM   4852  C  CA    . ALA A 1 2062 ? 174.784 189.452 123.568 1.00 27.02  ? 2062 ALA A CA    1 
ATOM   4853  C  C     . ALA A 1 2062 ? 175.674 188.239 123.807 1.00 30.44  ? 2062 ALA A C     1 
ATOM   4854  O  O     . ALA A 1 2062 ? 175.912 187.854 124.958 1.00 34.73  ? 2062 ALA A O     1 
ATOM   4855  C  CB    . ALA A 1 2062 ? 173.362 189.014 123.221 1.00 23.56  ? 2062 ALA A CB    1 
ATOM   4856  N  N     . GLU A 1 2063 ? 176.171 187.618 122.734 1.00 29.76  ? 2063 GLU A N     1 
ATOM   4857  C  CA    . GLU A 1 2063 ? 177.016 186.437 122.891 1.00 34.01  ? 2063 GLU A CA    1 
ATOM   4858  C  C     . GLU A 1 2063 ? 178.313 186.779 123.616 1.00 34.86  ? 2063 GLU A C     1 
ATOM   4859  O  O     . GLU A 1 2063 ? 178.761 186.035 124.496 1.00 35.28  ? 2063 GLU A O     1 
ATOM   4860  C  CB    . GLU A 1 2063 ? 177.310 185.813 121.528 1.00 42.94  ? 2063 GLU A CB    1 
ATOM   4861  C  CG    . GLU A 1 2063 ? 177.207 184.296 121.514 1.00 46.42  ? 2063 GLU A CG    1 
ATOM   4862  C  CD    . GLU A 1 2063 ? 178.043 183.665 120.420 1.00 55.96  ? 2063 GLU A CD    1 
ATOM   4863  O  OE1   . GLU A 1 2063 ? 178.973 182.899 120.747 1.00 52.29  ? 2063 GLU A OE1   1 
ATOM   4864  O  OE2   . GLU A 1 2063 ? 177.770 183.936 119.231 1.00 56.98  ? 2063 GLU A OE2   1 
ATOM   4865  N  N     . VAL A 1 2064 ? 178.934 187.903 123.254 1.00 34.85  ? 2064 VAL A N     1 
ATOM   4866  C  CA    . VAL A 1 2064 ? 180.143 188.338 123.948 1.00 33.91  ? 2064 VAL A CA    1 
ATOM   4867  C  C     . VAL A 1 2064 ? 179.823 188.700 125.393 1.00 30.37  ? 2064 VAL A C     1 
ATOM   4868  O  O     . VAL A 1 2064 ? 180.573 188.359 126.316 1.00 33.02  ? 2064 VAL A O     1 
ATOM   4869  C  CB    . VAL A 1 2064 ? 180.798 189.512 123.197 1.00 28.47  ? 2064 VAL A CB    1 
ATOM   4870  C  CG1   . VAL A 1 2064 ? 181.957 190.078 123.999 1.00 26.85  ? 2064 VAL A CG1   1 
ATOM   4871  C  CG2   . VAL A 1 2064 ? 181.269 189.061 121.826 1.00 29.64  ? 2064 VAL A CG2   1 
ATOM   4872  N  N     . LEU A 1 2065 ? 178.706 189.398 125.610 1.00 27.76  ? 2065 LEU A N     1 
ATOM   4873  C  CA    . LEU A 1 2065 ? 178.315 189.777 126.964 1.00 24.78  ? 2065 LEU A CA    1 
ATOM   4874  C  C     . LEU A 1 2065 ? 178.032 188.551 127.825 1.00 29.84  ? 2065 LEU A C     1 
ATOM   4875  O  O     . LEU A 1 2065 ? 178.440 188.496 128.991 1.00 29.48  ? 2065 LEU A O     1 
ATOM   4876  C  CB    . LEU A 1 2065 ? 177.088 190.686 126.916 1.00 22.05  ? 2065 LEU A CB    1 
ATOM   4877  C  CG    . LEU A 1 2065 ? 177.284 192.125 126.442 1.00 21.22  ? 2065 LEU A CG    1 
ATOM   4878  C  CD1   . LEU A 1 2065 ? 175.939 192.796 126.252 1.00 26.93  ? 2065 LEU A CD1   1 
ATOM   4879  C  CD2   . LEU A 1 2065 ? 178.128 192.906 127.427 1.00 28.05  ? 2065 LEU A CD2   1 
ATOM   4880  N  N     . ALA A 1 2066 ? 177.329 187.562 127.269 1.00 29.00  ? 2066 ALA A N     1 
ATOM   4881  C  CA    . ALA A 1 2066 ? 176.993 186.365 128.033 1.00 29.47  ? 2066 ALA A CA    1 
ATOM   4882  C  C     . ALA A 1 2066 ? 178.244 185.581 128.406 1.00 31.04  ? 2066 ALA A C     1 
ATOM   4883  O  O     . ALA A 1 2066 ? 178.359 185.070 129.527 1.00 33.83  ? 2066 ALA A O     1 
ATOM   4884  C  CB    . ALA A 1 2066 ? 176.025 185.489 127.238 1.00 32.29  ? 2066 ALA A CB    1 
ATOM   4885  N  N     . ASN A 1 2067 ? 179.196 185.473 127.477 1.00 35.87  ? 2067 ASN A N     1 
ATOM   4886  C  CA    . ASN A 1 2067 ? 180.440 184.771 127.764 1.00 33.65  ? 2067 ASN A CA    1 
ATOM   4887  C  C     . ASN A 1 2067 ? 181.314 185.533 128.750 1.00 32.53  ? 2067 ASN A C     1 
ATOM   4888  O  O     . ASN A 1 2067 ? 182.294 184.975 129.253 1.00 34.76  ? 2067 ASN A O     1 
ATOM   4889  C  CB    . ASN A 1 2067 ? 181.208 184.518 126.466 1.00 33.45  ? 2067 ASN A CB    1 
ATOM   4890  C  CG    . ASN A 1 2067 ? 180.522 183.504 125.573 1.00 38.51  ? 2067 ASN A CG    1 
ATOM   4891  O  OD1   . ASN A 1 2067 ? 180.411 182.328 125.920 1.00 45.35  ? 2067 ASN A OD1   1 
ATOM   4892  N  ND2   . ASN A 1 2067 ? 180.054 183.955 124.416 1.00 42.95  ? 2067 ASN A ND2   1 
ATOM   4893  N  N     . LYS A 1 2068 ? 180.984 186.793 129.033 1.00 29.29  ? 2068 LYS A N     1 
ATOM   4894  C  CA    . LYS A 1 2068 ? 181.739 187.592 129.988 1.00 26.96  ? 2068 LYS A CA    1 
ATOM   4895  C  C     . LYS A 1 2068 ? 181.063 187.686 131.348 1.00 29.86  ? 2068 LYS A C     1 
ATOM   4896  O  O     . LYS A 1 2068 ? 181.751 187.849 132.362 1.00 32.14  ? 2068 LYS A O     1 
ATOM   4897  C  CB    . LYS A 1 2068 ? 181.953 189.005 129.439 1.00 25.65  ? 2068 LYS A CB    1 
ATOM   4898  C  CG    . LYS A 1 2068 ? 183.068 189.126 128.417 1.00 26.49  ? 2068 LYS A CG    1 
ATOM   4899  C  CD    . LYS A 1 2068 ? 183.149 190.541 127.869 1.00 28.00  ? 2068 LYS A CD    1 
ATOM   4900  C  CE    . LYS A 1 2068 ? 184.485 190.802 127.195 1.00 32.56  ? 2068 LYS A CE    1 
ATOM   4901  N  NZ    . LYS A 1 2068 ? 185.626 190.597 128.129 1.00 31.74  ? 2068 LYS A NZ    1 
ATOM   4902  N  N     . ILE A 1 2069 ? 179.737 187.581 131.399 1.00 28.21  ? 2069 ILE A N     1 
ATOM   4903  C  CA    . ILE A 1 2069 ? 179.000 187.874 132.624 1.00 24.82  ? 2069 ILE A CA    1 
ATOM   4904  C  C     . ILE A 1 2069 ? 178.788 186.612 133.452 1.00 24.57  ? 2069 ILE A C     1 
ATOM   4905  O  O     . ILE A 1 2069 ? 178.675 186.680 134.680 1.00 31.78  ? 2069 ILE A O     1 
ATOM   4906  C  CB    . ILE A 1 2069 ? 177.660 188.567 132.307 1.00 24.08  ? 2069 ILE A CB    1 
ATOM   4907  C  CG1   . ILE A 1 2069 ? 177.152 189.318 133.538 1.00 24.75  ? 2069 ILE A CG1   1 
ATOM   4908  C  CG2   . ILE A 1 2069 ? 176.622 187.570 131.811 1.00 23.51  ? 2069 ILE A CG2   1 
ATOM   4909  C  CD1   . ILE A 1 2069 ? 178.160 190.286 134.111 1.00 25.00  ? 2069 ILE A CD1   1 
ATOM   4910  N  N     . VAL A 1 2070 ? 178.740 185.456 132.799 1.00 21.45  ? 2070 VAL A N     1 
ATOM   4911  C  CA    . VAL A 1 2070 ? 178.524 184.198 133.512 1.00 25.62  ? 2070 VAL A CA    1 
ATOM   4912  C  C     . VAL A 1 2070 ? 179.810 183.770 134.217 1.00 30.82  ? 2070 VAL A C     1 
ATOM   4913  O  O     . VAL A 1 2070 ? 179.757 183.428 135.407 1.00 29.09  ? 2070 VAL A O     1 
ATOM   4914  C  CB    . VAL A 1 2070 ? 177.989 183.103 132.574 1.00 24.74  ? 2070 VAL A CB    1 
ATOM   4915  C  CG1   . VAL A 1 2070 ? 177.828 181.793 133.325 1.00 21.33  ? 2070 VAL A CG1   1 
ATOM   4916  C  CG2   . VAL A 1 2070 ? 176.665 183.535 131.963 1.00 21.58  ? 2070 VAL A CG2   1 
ATOM   4917  N  N     . PRO A 1 2071 ? 180.977 183.757 133.555 1.00 29.71  ? 2071 PRO A N     1 
ATOM   4918  C  CA    . PRO A 1 2071 ? 182.214 183.485 134.306 1.00 26.81  ? 2071 PRO A CA    1 
ATOM   4919  C  C     . PRO A 1 2071 ? 182.495 184.505 135.393 1.00 29.32  ? 2071 PRO A C     1 
ATOM   4920  O  O     . PRO A 1 2071 ? 183.112 184.161 136.409 1.00 29.93  ? 2071 PRO A O     1 
ATOM   4921  C  CB    . PRO A 1 2071 ? 183.295 183.507 133.216 1.00 30.52  ? 2071 PRO A CB    1 
ATOM   4922  C  CG    . PRO A 1 2071 ? 182.571 183.150 131.976 1.00 31.72  ? 2071 PRO A CG    1 
ATOM   4923  C  CD    . PRO A 1 2071 ? 181.248 183.837 132.107 1.00 28.21  ? 2071 PRO A CD    1 
ATOM   4924  N  N     . PHE A 1 2072 ? 182.069 185.757 135.203 1.00 27.67  ? 2072 PHE A N     1 
ATOM   4925  C  CA    . PHE A 1 2072 ? 182.283 186.780 136.221 1.00 24.08  ? 2072 PHE A CA    1 
ATOM   4926  C  C     . PHE A 1 2072 ? 181.568 186.425 137.519 1.00 29.36  ? 2072 PHE A C     1 
ATOM   4927  O  O     . PHE A 1 2072 ? 182.125 186.596 138.610 1.00 33.10  ? 2072 PHE A O     1 
ATOM   4928  C  CB    . PHE A 1 2072 ? 181.815 188.139 135.703 1.00 21.63  ? 2072 PHE A CB    1 
ATOM   4929  C  CG    . PHE A 1 2072 ? 181.724 189.194 136.766 1.00 25.70  ? 2072 PHE A CG    1 
ATOM   4930  C  CD1   . PHE A 1 2072 ? 182.866 189.813 137.245 1.00 31.13  ? 2072 PHE A CD1   1 
ATOM   4931  C  CD2   . PHE A 1 2072 ? 180.496 189.568 137.287 1.00 25.35  ? 2072 PHE A CD2   1 
ATOM   4932  C  CE1   . PHE A 1 2072 ? 182.785 190.784 138.224 1.00 30.00  ? 2072 PHE A CE1   1 
ATOM   4933  C  CE2   . PHE A 1 2072 ? 180.410 190.536 138.266 1.00 22.61  ? 2072 PHE A CE2   1 
ATOM   4934  C  CZ    . PHE A 1 2072 ? 181.556 191.147 138.734 1.00 25.39  ? 2072 PHE A CZ    1 
ATOM   4935  N  N     . PHE A 1 2073 ? 180.331 185.935 137.421 1.00 29.23  ? 2073 PHE A N     1 
ATOM   4936  C  CA    . PHE A 1 2073 ? 179.614 185.500 138.616 1.00 26.47  ? 2073 PHE A CA    1 
ATOM   4937  C  C     . PHE A 1 2073 ? 180.315 184.319 139.274 1.00 30.59  ? 2073 PHE A C     1 
ATOM   4938  O  O     . PHE A 1 2073 ? 180.366 184.225 140.506 1.00 33.27  ? 2073 PHE A O     1 
ATOM   4939  C  CB    . PHE A 1 2073 ? 178.169 185.149 138.263 1.00 26.60  ? 2073 PHE A CB    1 
ATOM   4940  C  CG    . PHE A 1 2073 ? 177.218 186.305 138.389 1.00 26.23  ? 2073 PHE A CG    1 
ATOM   4941  C  CD1   . PHE A 1 2073 ? 177.174 187.291 137.419 1.00 22.46  ? 2073 PHE A CD1   1 
ATOM   4942  C  CD2   . PHE A 1 2073 ? 176.370 186.406 139.479 1.00 24.53  ? 2073 PHE A CD2   1 
ATOM   4943  C  CE1   . PHE A 1 2073 ? 176.302 188.356 137.532 1.00 21.79  ? 2073 PHE A CE1   1 
ATOM   4944  C  CE2   . PHE A 1 2073 ? 175.495 187.468 139.598 1.00 23.59  ? 2073 PHE A CE2   1 
ATOM   4945  C  CZ    . PHE A 1 2073 ? 175.462 188.445 138.623 1.00 20.03  ? 2073 PHE A CZ    1 
ATOM   4946  N  N     . LYS A 1 2074 ? 180.855 183.402 138.467 1.00 28.57  ? 2074 LYS A N     1 
ATOM   4947  C  CA    . LYS A 1 2074 ? 181.666 182.322 139.017 1.00 25.76  ? 2074 LYS A CA    1 
ATOM   4948  C  C     . LYS A 1 2074 ? 182.921 182.867 139.687 1.00 29.74  ? 2074 LYS A C     1 
ATOM   4949  O  O     . LYS A 1 2074 ? 183.324 182.386 140.753 1.00 36.23  ? 2074 LYS A O     1 
ATOM   4950  C  CB    . LYS A 1 2074 ? 182.034 181.328 137.917 1.00 29.84  ? 2074 LYS A CB    1 
ATOM   4951  C  CG    . LYS A 1 2074 ? 181.859 179.873 138.313 1.00 32.16  ? 2074 LYS A CG    1 
ATOM   4952  C  CD    . LYS A 1 2074 ? 182.478 178.942 137.285 1.00 36.08  ? 2074 LYS A CD    1 
ATOM   4953  C  CE    . LYS A 1 2074 ? 183.984 179.132 137.210 1.00 47.96  ? 2074 LYS A CE    1 
ATOM   4954  N  NZ    . LYS A 1 2074 ? 184.634 178.116 136.337 1.00 58.23  ? 2074 LYS A NZ    1 
ATOM   4955  N  N     . LEU A 1 2075 ? 183.554 183.871 139.075 1.00 28.37  ? 2075 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 2075 ? 184.753 184.462 139.662 1.00 29.41  ? 2075 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 2075 ? 184.451 185.108 141.008 1.00 32.70  ? 2075 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 2075 ? 185.225 184.964 141.961 1.00 39.91  ? 2075 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 2075 ? 185.353 185.490 138.702 1.00 34.20  ? 2075 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 2075 ? 186.223 184.956 137.564 1.00 33.92  ? 2075 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 2075 ? 186.516 186.060 136.562 1.00 34.14  ? 2075 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 2075 ? 187.514 184.367 138.107 1.00 39.07  ? 2075 LEU A CD2   1 
ATOM   4963  N  N     . CYS A 1 2076 ? 183.329 185.825 141.105 1.00 35.28  ? 2076 CYS A N     1 
ATOM   4964  C  CA    . CYS A 1 2076 ? 182.978 186.483 142.360 1.00 30.01  ? 2076 CYS A CA    1 
ATOM   4965  C  C     . CYS A 1 2076 ? 182.676 185.466 143.453 1.00 30.54  ? 2076 CYS A C     1 
ATOM   4966  O  O     . CYS A 1 2076 ? 182.901 185.733 144.639 1.00 34.03  ? 2076 CYS A O     1 
ATOM   4967  C  CB    . CYS A 1 2076 ? 181.784 187.412 142.147 1.00 22.96  ? 2076 CYS A CB    1 
ATOM   4968  S  SG    . CYS A 1 2076 ? 182.200 188.973 141.350 1.00 40.98  ? 2076 CYS A SG    1 
ATOM   4969  N  N     . ASP A 1 2077 ? 182.160 184.297 143.075 1.00 26.31  ? 2077 ASP A N     1 
ATOM   4970  C  CA    . ASP A 1 2077 ? 181.833 183.282 144.070 1.00 26.12  ? 2077 ASP A CA    1 
ATOM   4971  C  C     . ASP A 1 2077 ? 183.092 182.672 144.677 1.00 34.38  ? 2077 ASP A C     1 
ATOM   4972  O  O     . ASP A 1 2077 ? 183.095 182.278 145.849 1.00 42.93  ? 2077 ASP A O     1 
ATOM   4973  C  CB    . ASP A 1 2077 ? 180.958 182.198 143.442 1.00 33.59  ? 2077 ASP A CB    1 
ATOM   4974  C  CG    . ASP A 1 2077 ? 180.590 181.103 144.423 1.00 47.34  ? 2077 ASP A CG    1 
ATOM   4975  O  OD1   . ASP A 1 2077 ? 179.855 181.394 145.391 1.00 44.35  ? 2077 ASP A OD1   1 
ATOM   4976  O  OD2   . ASP A 1 2077 ? 181.033 179.953 144.228 1.00 55.54  ? 2077 ASP A OD2   1 
ATOM   4977  N  N     . GLU A 1 2078 ? 184.171 182.589 143.900 1.00 38.75  ? 2078 GLU A N     1 
ATOM   4978  C  CA    . GLU A 1 2078 ? 185.379 181.890 144.318 1.00 39.27  ? 2078 GLU A CA    1 
ATOM   4979  C  C     . GLU A 1 2078 ? 186.538 182.816 144.666 1.00 39.44  ? 2078 GLU A C     1 
ATOM   4980  O  O     . GLU A 1 2078 ? 187.541 182.343 145.210 1.00 43.50  ? 2078 GLU A O     1 
ATOM   4981  C  CB    . GLU A 1 2078 ? 185.823 180.911 143.226 1.00 37.33  ? 2078 GLU A CB    1 
ATOM   4982  C  CG    . GLU A 1 2078 ? 184.682 180.207 142.516 1.00 45.29  ? 2078 GLU A CG    1 
ATOM   4983  C  CD    . GLU A 1 2078 ? 185.125 178.944 141.805 1.00 58.40  ? 2078 GLU A CD    1 
ATOM   4984  O  OE1   . GLU A 1 2078 ? 186.338 178.799 141.549 1.00 59.24  ? 2078 GLU A OE1   1 
ATOM   4985  O  OE2   . GLU A 1 2078 ? 184.260 178.098 141.500 1.00 63.25  ? 2078 GLU A OE2   1 
ATOM   4986  N  N     . GLN A 1 2079 ? 186.438 184.113 144.376 1.00 36.00  ? 2079 GLN A N     1 
ATOM   4987  C  CA    . GLN A 1 2079 ? 187.566 185.002 144.632 1.00 39.25  ? 2079 GLN A CA    1 
ATOM   4988  C  C     . GLN A 1 2079 ? 187.234 186.039 145.698 1.00 41.06  ? 2079 GLN A C     1 
ATOM   4989  O  O     . GLN A 1 2079 ? 188.137 186.580 146.343 1.00 44.79  ? 2079 GLN A O     1 
ATOM   4990  C  CB    . GLN A 1 2079 ? 188.012 185.691 143.341 1.00 36.79  ? 2079 GLN A CB    1 
ATOM   4991  C  CG    . GLN A 1 2079 ? 188.684 184.753 142.354 1.00 36.73  ? 2079 GLN A CG    1 
ATOM   4992  C  CD    . GLN A 1 2079 ? 189.937 185.346 141.746 1.00 51.08  ? 2079 GLN A CD    1 
ATOM   4993  O  OE1   . GLN A 1 2079 ? 190.052 186.560 141.594 1.00 55.35  ? 2079 GLN A OE1   1 
ATOM   4994  N  NE2   . GLN A 1 2079 ? 190.887 184.488 141.395 1.00 57.61  ? 2079 GLN A NE2   1 
ATOM   4995  N  N     . LEU A 1 2080 ? 185.951 186.326 145.888 1.00 38.58  ? 2080 LEU A N     1 
ATOM   4996  C  CA    . LEU A 1 2080 ? 185.543 187.202 146.973 1.00 32.89  ? 2080 LEU A CA    1 
ATOM   4997  C  C     . LEU A 1 2080 ? 185.517 186.434 148.291 1.00 33.54  ? 2080 LEU A C     1 
ATOM   4998  O  O     . LEU A 1 2080 ? 185.437 185.203 148.322 1.00 39.96  ? 2080 LEU A O     1 
ATOM   4999  C  CB    . LEU A 1 2080 ? 184.170 187.814 146.690 1.00 32.28  ? 2080 LEU A CB    1 
ATOM   5000  C  CG    . LEU A 1 2080 ? 184.042 188.661 145.423 1.00 29.07  ? 2080 LEU A CG    1 
ATOM   5001  C  CD1   . LEU A 1 2080 ? 182.691 189.353 145.376 1.00 28.53  ? 2080 LEU A CD1   1 
ATOM   5002  C  CD2   . LEU A 1 2080 ? 185.166 189.679 145.343 1.00 31.11  ? 2080 LEU A CD2   1 
ATOM   5003  N  N     . SER A 1 2081 ? 185.593 187.181 149.389 1.00 30.80  ? 2081 SER A N     1 
ATOM   5004  C  CA    . SER A 1 2081 ? 185.573 186.569 150.711 1.00 32.13  ? 2081 SER A CA    1 
ATOM   5005  C  C     . SER A 1 2081 ? 184.233 185.890 150.965 1.00 27.07  ? 2081 SER A C     1 
ATOM   5006  O  O     . SER A 1 2081 ? 183.179 186.385 150.557 1.00 30.36  ? 2081 SER A O     1 
ATOM   5007  C  CB    . SER A 1 2081 ? 185.844 187.623 151.784 1.00 31.24  ? 2081 SER A CB    1 
ATOM   5008  O  OG    . SER A 1 2081 ? 184.705 188.439 151.995 1.00 28.21  ? 2081 SER A OG    1 
ATOM   5009  N  N     . SER A 1 2082 ? 184.279 184.748 151.645 1.00 22.34  ? 2082 SER A N     1 
ATOM   5010  C  CA    . SER A 1 2082 ? 183.069 183.976 151.903 1.00 23.13  ? 2082 SER A CA    1 
ATOM   5011  C  C     . SER A 1 2082 ? 182.248 184.640 153.001 1.00 22.54  ? 2082 SER A C     1 
ATOM   5012  O  O     . SER A 1 2082 ? 182.684 184.718 154.154 1.00 23.38  ? 2082 SER A O     1 
ATOM   5013  C  CB    . SER A 1 2082 ? 183.429 182.545 152.292 1.00 26.19  ? 2082 SER A CB    1 
ATOM   5014  O  OG    . SER A 1 2082 ? 182.275 181.815 152.672 1.00 25.81  ? 2082 SER A OG    1 
ATOM   5015  N  N     . GLN A 1 2083 ? 181.058 185.118 152.642 1.00 22.58  ? 2083 GLN A N     1 
ATOM   5016  C  CA    . GLN A 1 2083 ? 180.136 185.733 153.584 1.00 16.52  ? 2083 GLN A CA    1 
ATOM   5017  C  C     . GLN A 1 2083 ? 178.779 185.054 153.474 1.00 14.31  ? 2083 GLN A C     1 
ATOM   5018  O  O     . GLN A 1 2083 ? 178.343 184.676 152.384 1.00 17.53  ? 2083 GLN A O     1 
ATOM   5019  C  CB    . GLN A 1 2083 ? 179.992 187.241 153.333 1.00 15.26  ? 2083 GLN A CB    1 
ATOM   5020  C  CG    . GLN A 1 2083 ? 181.314 187.975 153.178 1.00 17.05  ? 2083 GLN A CG    1 
ATOM   5021  C  CD    . GLN A 1 2083 ? 181.988 188.249 154.507 1.00 19.60  ? 2083 GLN A CD    1 
ATOM   5022  O  OE1   . GLN A 1 2083 ? 181.355 188.188 155.561 1.00 20.96  ? 2083 GLN A OE1   1 
ATOM   5023  N  NE2   . GLN A 1 2083 ? 183.280 188.551 154.465 1.00 20.51  ? 2083 GLN A NE2   1 
ATOM   5024  N  N     . SER A 1 2084 ? 178.113 184.902 154.622 1.00 15.63  ? 2084 SER A N     1 
ATOM   5025  C  CA    . SER A 1 2084 ? 176.829 184.211 154.657 1.00 18.83  ? 2084 SER A CA    1 
ATOM   5026  C  C     . SER A 1 2084 ? 175.743 184.951 153.888 1.00 20.16  ? 2084 SER A C     1 
ATOM   5027  O  O     . SER A 1 2084 ? 174.774 184.321 153.451 1.00 17.86  ? 2084 SER A O     1 
ATOM   5028  C  CB    . SER A 1 2084 ? 176.384 184.000 156.105 1.00 16.80  ? 2084 SER A CB    1 
ATOM   5029  O  OG    . SER A 1 2084 ? 176.406 185.219 156.826 1.00 21.73  ? 2084 SER A OG    1 
ATOM   5030  N  N     . HIS A 1 2085 ? 175.879 186.263 153.710 1.00 16.98  ? 2085 HIS A N     1 
ATOM   5031  C  CA    . HIS A 1 2085 ? 174.907 187.056 152.973 1.00 13.89  ? 2085 HIS A CA    1 
ATOM   5032  C  C     . HIS A 1 2085 ? 175.301 187.257 151.516 1.00 17.11  ? 2085 HIS A C     1 
ATOM   5033  O  O     . HIS A 1 2085 ? 174.763 188.151 150.856 1.00 21.36  ? 2085 HIS A O     1 
ATOM   5034  C  CB    . HIS A 1 2085 ? 174.701 188.410 153.655 1.00 12.34  ? 2085 HIS A CB    1 
ATOM   5035  C  CG    . HIS A 1 2085 ? 175.920 189.278 153.660 1.00 13.82  ? 2085 HIS A CG    1 
ATOM   5036  N  ND1   . HIS A 1 2085 ? 176.998 189.044 154.485 1.00 16.82  ? 2085 HIS A ND1   1 
ATOM   5037  C  CD2   . HIS A 1 2085 ? 176.226 190.387 152.947 1.00 13.14  ? 2085 HIS A CD2   1 
ATOM   5038  C  CE1   . HIS A 1 2085 ? 177.919 189.967 154.275 1.00 14.58  ? 2085 HIS A CE1   1 
ATOM   5039  N  NE2   . HIS A 1 2085 ? 177.476 190.795 153.347 1.00 12.54  ? 2085 HIS A NE2   1 
ATOM   5040  N  N     . TYR A 1 2086 ? 176.226 186.449 151.003 1.00 14.35  ? 2086 TYR A N     1 
ATOM   5041  C  CA    . TYR A 1 2086 ? 176.642 186.525 149.610 1.00 15.56  ? 2086 TYR A CA    1 
ATOM   5042  C  C     . TYR A 1 2086 ? 175.883 185.490 148.791 1.00 18.30  ? 2086 TYR A C     1 
ATOM   5043  O  O     . TYR A 1 2086 ? 175.778 184.326 149.192 1.00 21.23  ? 2086 TYR A O     1 
ATOM   5044  C  CB    . TYR A 1 2086 ? 178.146 186.291 149.475 1.00 18.13  ? 2086 TYR A CB    1 
ATOM   5045  C  CG    . TYR A 1 2086 ? 179.000 187.512 149.723 1.00 15.41  ? 2086 TYR A CG    1 
ATOM   5046  C  CD1   . TYR A 1 2086 ? 178.446 188.688 150.207 1.00 15.64  ? 2086 TYR A CD1   1 
ATOM   5047  C  CD2   . TYR A 1 2086 ? 180.362 187.486 149.471 1.00 18.31  ? 2086 TYR A CD2   1 
ATOM   5048  C  CE1   . TYR A 1 2086 ? 179.230 189.802 150.436 1.00 14.45  ? 2086 TYR A CE1   1 
ATOM   5049  C  CE2   . TYR A 1 2086 ? 181.150 188.594 149.693 1.00 22.49  ? 2086 TYR A CE2   1 
ATOM   5050  C  CZ    . TYR A 1 2086 ? 180.581 189.748 150.176 1.00 18.60  ? 2086 TYR A CZ    1 
ATOM   5051  O  OH    . TYR A 1 2086 ? 181.373 190.849 150.398 1.00 18.83  ? 2086 TYR A OH    1 
ATOM   5052  N  N     . ASP A 1 2087 ? 175.358 185.916 147.645 1.00 17.55  ? 2087 ASP A N     1 
ATOM   5053  C  CA    . ASP A 1 2087 ? 174.680 185.020 146.716 1.00 18.16  ? 2087 ASP A CA    1 
ATOM   5054  C  C     . ASP A 1 2087 ? 175.068 185.415 145.301 1.00 17.52  ? 2087 ASP A C     1 
ATOM   5055  O  O     . ASP A 1 2087 ? 174.849 186.559 144.893 1.00 15.57  ? 2087 ASP A O     1 
ATOM   5056  C  CB    . ASP A 1 2087 ? 173.159 185.075 146.892 1.00 22.70  ? 2087 ASP A CB    1 
ATOM   5057  C  CG    . ASP A 1 2087 ? 172.421 184.297 145.820 1.00 28.20  ? 2087 ASP A CG    1 
ATOM   5058  O  OD1   . ASP A 1 2087 ? 172.620 183.067 145.735 1.00 23.39  ? 2087 ASP A OD1   1 
ATOM   5059  O  OD2   . ASP A 1 2087 ? 171.647 184.915 145.058 1.00 22.70  ? 2087 ASP A OD2   1 
ATOM   5060  N  N     . PHE A 1 2088 ? 175.641 184.472 144.560 1.00 19.47  ? 2088 PHE A N     1 
ATOM   5061  C  CA    . PHE A 1 2088 ? 176.066 184.686 143.183 1.00 19.18  ? 2088 PHE A CA    1 
ATOM   5062  C  C     . PHE A 1 2088 ? 175.502 183.601 142.281 1.00 16.93  ? 2088 PHE A C     1 
ATOM   5063  O  O     . PHE A 1 2088 ? 176.153 183.146 141.336 1.00 20.45  ? 2088 PHE A O     1 
ATOM   5064  C  CB    . PHE A 1 2088 ? 177.588 184.738 143.082 1.00 22.92  ? 2088 PHE A CB    1 
ATOM   5065  C  CG    . PHE A 1 2088 ? 178.213 185.801 143.936 1.00 21.87  ? 2088 PHE A CG    1 
ATOM   5066  C  CD1   . PHE A 1 2088 ? 178.063 187.140 143.619 1.00 20.72  ? 2088 PHE A CD1   1 
ATOM   5067  C  CD2   . PHE A 1 2088 ? 178.948 185.462 145.059 1.00 21.60  ? 2088 PHE A CD2   1 
ATOM   5068  C  CE1   . PHE A 1 2088 ? 178.638 188.121 144.403 1.00 22.97  ? 2088 PHE A CE1   1 
ATOM   5069  C  CE2   . PHE A 1 2088 ? 179.525 186.439 145.848 1.00 20.93  ? 2088 PHE A CE2   1 
ATOM   5070  C  CZ    . PHE A 1 2088 ? 179.369 187.770 145.520 1.00 21.59  ? 2088 PHE A CZ    1 
ATOM   5071  N  N     . GLY A 1 2089 ? 174.278 183.171 142.563 1.00 16.19  ? 2089 GLY A N     1 
ATOM   5072  C  CA    . GLY A 1 2089 ? 173.626 182.123 141.808 1.00 15.71  ? 2089 GLY A CA    1 
ATOM   5073  C  C     . GLY A 1 2089 ? 172.860 182.654 140.617 1.00 15.30  ? 2089 GLY A C     1 
ATOM   5074  O  O     . GLY A 1 2089 ? 173.036 183.795 140.183 1.00 19.47  ? 2089 GLY A O     1 
ATOM   5075  N  N     . LEU A 1 2090 ? 171.991 181.797 140.079 1.00 14.64  ? 2090 LEU A N     1 
ATOM   5076  C  CA    . LEU A 1 2090 ? 171.220 182.162 138.896 1.00 11.72  ? 2090 LEU A CA    1 
ATOM   5077  C  C     . LEU A 1 2090 ? 170.213 183.267 139.192 1.00 9.51   ? 2090 LEU A C     1 
ATOM   5078  O  O     . LEU A 1 2090 ? 169.960 184.117 138.330 1.00 11.75  ? 2090 LEU A O     1 
ATOM   5079  C  CB    . LEU A 1 2090 ? 170.518 180.925 138.338 1.00 11.17  ? 2090 LEU A CB    1 
ATOM   5080  C  CG    . LEU A 1 2090 ? 169.448 181.130 137.269 1.00 8.33   ? 2090 LEU A CG    1 
ATOM   5081  C  CD1   . LEU A 1 2090 ? 170.089 181.440 135.932 1.00 13.32  ? 2090 LEU A CD1   1 
ATOM   5082  C  CD2   . LEU A 1 2090 ? 168.584 179.891 137.172 1.00 8.20   ? 2090 LEU A CD2   1 
ATOM   5083  N  N     . ARG A 1 2091 ? 169.633 183.275 140.395 1.00 12.69  ? 2091 ARG A N     1 
ATOM   5084  C  CA    . ARG A 1 2091 ? 168.683 184.324 140.750 1.00 9.32   ? 2091 ARG A CA    1 
ATOM   5085  C  C     . ARG A 1 2091 ? 169.349 185.695 140.764 1.00 12.00  ? 2091 ARG A C     1 
ATOM   5086  O  O     . ARG A 1 2091 ? 168.754 186.684 140.321 1.00 12.49  ? 2091 ARG A O     1 
ATOM   5087  C  CB    . ARG A 1 2091 ? 168.050 184.022 142.107 1.00 10.29  ? 2091 ARG A CB    1 
ATOM   5088  C  CG    . ARG A 1 2091 ? 166.616 184.502 142.238 1.00 13.26  ? 2091 ARG A CG    1 
ATOM   5089  C  CD    . ARG A 1 2091 ? 166.086 184.283 143.643 1.00 11.95  ? 2091 ARG A CD    1 
ATOM   5090  N  NE    . ARG A 1 2091 ? 165.972 182.869 143.977 1.00 12.81  ? 2091 ARG A NE    1 
ATOM   5091  C  CZ    . ARG A 1 2091 ? 164.959 182.095 143.613 1.00 15.70  ? 2091 ARG A CZ    1 
ATOM   5092  N  NH1   . ARG A 1 2091 ? 163.944 182.571 142.911 1.00 16.80  ? 2091 ARG A NH1   1 
ATOM   5093  N  NH2   . ARG A 1 2091 ? 164.962 180.813 143.967 1.00 7.62   ? 2091 ARG A NH2   1 
ATOM   5094  N  N     . ALA A 1 2092 ? 170.577 185.776 141.280 1.00 14.82  ? 2092 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2092 ? 171.322 187.028 141.212 1.00 12.62  ? 2092 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2092 ? 171.638 187.399 139.769 1.00 15.62  ? 2092 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2092 ? 171.546 188.571 139.385 1.00 19.85  ? 2092 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2092 ? 172.605 186.923 142.035 1.00 17.54  ? 2092 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2093 ? 172.016 186.410 138.955 1.00 13.78  ? 2093 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2093 ? 172.269 186.668 137.541 1.00 11.64  ? 2093 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2093 ? 170.988 187.063 136.816 1.00 13.01  ? 2093 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2093 ? 171.017 187.882 135.891 1.00 16.21  ? 2093 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2093 ? 172.904 185.439 136.889 1.00 15.56  ? 2093 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2093 ? 173.101 185.499 135.373 1.00 14.52  ? 2093 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2093 ? 174.193 186.490 135.014 1.00 11.59  ? 2093 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2093 ? 173.421 184.121 134.822 1.00 13.17  ? 2093 LEU A CD2   1 
ATOM   5107  N  N     . LYS A 1 2094 ? 169.855 186.481 137.210 1.00 13.99  ? 2094 LYS A N     1 
ATOM   5108  C  CA    . LYS A 1 2094 ? 168.588 186.847 136.585 1.00 12.83  ? 2094 LYS A CA    1 
ATOM   5109  C  C     . LYS A 1 2094 ? 168.238 188.304 136.861 1.00 16.78  ? 2094 LYS A C     1 
ATOM   5110  O  O     . LYS A 1 2094 ? 167.727 189.005 135.980 1.00 23.69  ? 2094 LYS A O     1 
ATOM   5111  C  CB    . LYS A 1 2094 ? 167.474 185.923 137.077 1.00 11.10  ? 2094 LYS A CB    1 
ATOM   5112  C  CG    . LYS A 1 2094 ? 166.130 186.158 136.407 1.00 14.56  ? 2094 LYS A CG    1 
ATOM   5113  C  CD    . LYS A 1 2094 ? 166.112 185.605 134.993 1.00 11.49  ? 2094 LYS A CD    1 
ATOM   5114  C  CE    . LYS A 1 2094 ? 164.757 185.810 134.339 1.00 12.43  ? 2094 LYS A CE    1 
ATOM   5115  N  NZ    . LYS A 1 2094 ? 163.673 185.072 135.031 1.00 12.95  ? 2094 LYS A NZ    1 
ATOM   5116  N  N     . SER A 1 2095 ? 168.508 188.778 138.079 1.00 14.94  ? 2095 SER A N     1 
ATOM   5117  C  CA    . SER A 1 2095 ? 168.167 190.153 138.432 1.00 16.25  ? 2095 SER A CA    1 
ATOM   5118  C  C     . SER A 1 2095 ? 168.979 191.159 137.625 1.00 18.65  ? 2095 SER A C     1 
ATOM   5119  O  O     . SER A 1 2095 ? 168.434 192.156 137.137 1.00 20.59  ? 2095 SER A O     1 
ATOM   5120  C  CB    . SER A 1 2095 ? 168.377 190.377 139.929 1.00 18.46  ? 2095 SER A CB    1 
ATOM   5121  O  OG    . SER A 1 2095 ? 169.754 190.359 140.263 1.00 21.24  ? 2095 SER A OG    1 
ATOM   5122  N  N     . VAL A 1 2096 ? 170.284 190.920 137.477 1.00 19.81  ? 2096 VAL A N     1 
ATOM   5123  C  CA    . VAL A 1 2096 ? 171.139 191.883 136.786 1.00 16.48  ? 2096 VAL A CA    1 
ATOM   5124  C  C     . VAL A 1 2096 ? 170.788 191.947 135.303 1.00 18.12  ? 2096 VAL A C     1 
ATOM   5125  O  O     . VAL A 1 2096 ? 170.797 193.025 134.696 1.00 22.60  ? 2096 VAL A O     1 
ATOM   5126  C  CB    . VAL A 1 2096 ? 172.626 191.549 137.019 1.00 14.67  ? 2096 VAL A CB    1 
ATOM   5127  C  CG1   . VAL A 1 2096 ? 172.945 190.129 136.601 1.00 21.40  ? 2096 VAL A CG1   1 
ATOM   5128  C  CG2   . VAL A 1 2096 ? 173.512 192.522 136.272 1.00 21.84  ? 2096 VAL A CG2   1 
ATOM   5129  N  N     . LEU A 1 2097 ? 170.465 190.800 134.698 1.00 16.20  ? 2097 LEU A N     1 
ATOM   5130  C  CA    . LEU A 1 2097 ? 170.079 190.794 133.291 1.00 13.73  ? 2097 LEU A CA    1 
ATOM   5131  C  C     . LEU A 1 2097 ? 168.782 191.561 133.066 1.00 18.12  ? 2097 LEU A C     1 
ATOM   5132  O  O     . LEU A 1 2097 ? 168.655 192.299 132.082 1.00 23.66  ? 2097 LEU A O     1 
ATOM   5133  C  CB    . LEU A 1 2097 ? 169.950 189.358 132.783 1.00 16.14  ? 2097 LEU A CB    1 
ATOM   5134  C  CG    . LEU A 1 2097 ? 171.225 188.513 132.784 1.00 13.31  ? 2097 LEU A CG    1 
ATOM   5135  C  CD1   . LEU A 1 2097 ? 170.900 187.057 132.497 1.00 11.88  ? 2097 LEU A CD1   1 
ATOM   5136  C  CD2   . LEU A 1 2097 ? 172.227 189.049 131.774 1.00 11.66  ? 2097 LEU A CD2   1 
ATOM   5137  N  N     . VAL A 1 2098 ? 167.804 191.392 133.960 1.00 20.23  ? 2098 VAL A N     1 
ATOM   5138  C  CA    . VAL A 1 2098 ? 166.563 192.155 133.855 1.00 20.92  ? 2098 VAL A CA    1 
ATOM   5139  C  C     . VAL A 1 2098 ? 166.838 193.641 134.041 1.00 21.05  ? 2098 VAL A C     1 
ATOM   5140  O  O     . VAL A 1 2098 ? 166.322 194.482 133.295 1.00 27.15  ? 2098 VAL A O     1 
ATOM   5141  C  CB    . VAL A 1 2098 ? 165.527 191.639 134.871 1.00 21.07  ? 2098 VAL A CB    1 
ATOM   5142  C  CG1   . VAL A 1 2098 ? 164.310 192.549 134.898 1.00 19.84  ? 2098 VAL A CG1   1 
ATOM   5143  C  CG2   . VAL A 1 2098 ? 165.119 190.215 134.535 1.00 20.31  ? 2098 VAL A CG2   1 
ATOM   5144  N  N     . SER A 1 2099 ? 167.658 193.987 135.036 1.00 20.41  ? 2099 SER A N     1 
ATOM   5145  C  CA    . SER A 1 2099 ? 167.984 195.389 135.273 1.00 20.21  ? 2099 SER A CA    1 
ATOM   5146  C  C     . SER A 1 2099 ? 168.817 195.961 134.134 1.00 22.25  ? 2099 SER A C     1 
ATOM   5147  O  O     . SER A 1 2099 ? 168.743 197.161 133.844 1.00 27.40  ? 2099 SER A O     1 
ATOM   5148  C  CB    . SER A 1 2099 ? 168.715 195.537 136.607 1.00 23.49  ? 2099 SER A CB    1 
ATOM   5149  O  OG    . SER A 1 2099 ? 168.225 194.611 137.561 1.00 28.27  ? 2099 SER A OG    1 
ATOM   5150  N  N     . ALA A 1 2100 ? 169.620 195.120 133.477 1.00 24.26  ? 2100 ALA A N     1 
ATOM   5151  C  CA    . ALA A 1 2100 ? 170.386 195.581 132.324 1.00 23.39  ? 2100 ALA A CA    1 
ATOM   5152  C  C     . ALA A 1 2100 ? 169.465 196.030 131.198 1.00 26.19  ? 2100 ALA A C     1 
ATOM   5153  O  O     . ALA A 1 2100 ? 169.722 197.047 130.543 1.00 31.00  ? 2100 ALA A O     1 
ATOM   5154  C  CB    . ALA A 1 2100 ? 171.329 194.478 131.842 1.00 22.89  ? 2100 ALA A CB    1 
ATOM   5155  N  N     . GLY A 1 2101 ? 168.390 195.279 130.953 1.00 23.42  ? 2101 GLY A N     1 
ATOM   5156  C  CA    . GLY A 1 2101 ? 167.405 195.718 129.978 1.00 26.39  ? 2101 GLY A CA    1 
ATOM   5157  C  C     . GLY A 1 2101 ? 166.715 197.001 130.397 1.00 29.66  ? 2101 GLY A C     1 
ATOM   5158  O  O     . GLY A 1 2101 ? 166.455 197.881 129.573 1.00 31.05  ? 2101 GLY A O     1 
ATOM   5159  N  N     . ASN A 1 2102 ? 166.400 197.118 131.689 1.00 25.87  ? 2102 ASN A N     1 
ATOM   5160  C  CA    . ASN A 1 2102 ? 165.778 198.339 132.193 1.00 24.52  ? 2102 ASN A CA    1 
ATOM   5161  C  C     . ASN A 1 2102 ? 166.716 199.532 132.059 1.00 30.43  ? 2102 ASN A C     1 
ATOM   5162  O  O     . ASN A 1 2102 ? 166.289 200.625 131.668 1.00 35.79  ? 2102 ASN A O     1 
ATOM   5163  C  CB    . ASN A 1 2102 ? 165.359 198.148 133.650 1.00 30.60  ? 2102 ASN A CB    1 
ATOM   5164  C  CG    . ASN A 1 2102 ? 164.197 197.188 133.802 1.00 32.14  ? 2102 ASN A CG    1 
ATOM   5165  O  OD1   . ASN A 1 2102 ? 163.491 196.892 132.839 1.00 32.12  ? 2102 ASN A OD1   1 
ATOM   5166  N  ND2   . ASN A 1 2102 ? 163.993 196.694 135.018 1.00 21.51  ? 2102 ASN A ND2   1 
ATOM   5167  N  N     . VAL A 1 2103 ? 167.996 199.344 132.384 1.00 31.75  ? 2103 VAL A N     1 
ATOM   5168  C  CA    . VAL A 1 2103 ? 168.962 200.433 132.273 1.00 31.97  ? 2103 VAL A CA    1 
ATOM   5169  C  C     . VAL A 1 2103 ? 169.142 200.843 130.816 1.00 33.44  ? 2103 VAL A C     1 
ATOM   5170  O  O     . VAL A 1 2103 ? 169.197 202.036 130.496 1.00 38.86  ? 2103 VAL A O     1 
ATOM   5171  C  CB    . VAL A 1 2103 ? 170.299 200.028 132.921 1.00 28.57  ? 2103 VAL A CB    1 
ATOM   5172  C  CG1   . VAL A 1 2103 ? 171.409 200.976 132.496 1.00 29.36  ? 2103 VAL A CG1   1 
ATOM   5173  C  CG2   . VAL A 1 2103 ? 170.169 200.011 134.435 1.00 30.29  ? 2103 VAL A CG2   1 
ATOM   5174  N  N     . LYS A 1 2104 ? 169.233 199.865 129.911 1.00 28.79  ? 2104 LYS A N     1 
ATOM   5175  C  CA    . LYS A 1 2104 ? 169.401 200.181 128.497 1.00 30.61  ? 2104 LYS A CA    1 
ATOM   5176  C  C     . LYS A 1 2104 ? 168.200 200.947 127.957 1.00 33.00  ? 2104 LYS A C     1 
ATOM   5177  O  O     . LYS A 1 2104 ? 168.359 201.891 127.174 1.00 39.52  ? 2104 LYS A O     1 
ATOM   5178  C  CB    . LYS A 1 2104 ? 169.631 198.901 127.694 1.00 28.72  ? 2104 LYS A CB    1 
ATOM   5179  C  CG    . LYS A 1 2104 ? 170.028 199.147 126.249 1.00 24.77  ? 2104 LYS A CG    1 
ATOM   5180  C  CD    . LYS A 1 2104 ? 170.309 197.847 125.516 1.00 23.03  ? 2104 LYS A CD    1 
ATOM   5181  C  CE    . LYS A 1 2104 ? 169.028 197.198 125.031 1.00 21.08  ? 2104 LYS A CE    1 
ATOM   5182  N  NZ    . LYS A 1 2104 ? 168.362 198.009 123.976 1.00 19.85  ? 2104 LYS A NZ    1 
ATOM   5183  N  N     . ARG A 1 2105 ? 166.989 200.553 128.360 1.00 32.90  ? 2105 ARG A N     1 
ATOM   5184  C  CA    . ARG A 1 2105 ? 165.803 201.310 127.975 1.00 31.72  ? 2105 ARG A CA    1 
ATOM   5185  C  C     . ARG A 1 2105 ? 165.851 202.725 128.538 1.00 38.84  ? 2105 ARG A C     1 
ATOM   5186  O  O     . ARG A 1 2105 ? 165.515 203.690 127.842 1.00 43.53  ? 2105 ARG A O     1 
ATOM   5187  C  CB    . ARG A 1 2105 ? 164.540 200.594 128.453 1.00 29.92  ? 2105 ARG A CB    1 
ATOM   5188  C  CG    . ARG A 1 2105 ? 163.901 199.687 127.418 1.00 33.88  ? 2105 ARG A CG    1 
ATOM   5189  C  CD    . ARG A 1 2105 ? 162.671 198.993 127.988 1.00 26.32  ? 2105 ARG A CD    1 
ATOM   5190  N  NE    . ARG A 1 2105 ? 163.014 197.917 128.911 1.00 24.37  ? 2105 ARG A NE    1 
ATOM   5191  C  CZ    . ARG A 1 2105 ? 163.544 196.755 128.553 1.00 33.55  ? 2105 ARG A CZ    1 
ATOM   5192  N  NH1   . ARG A 1 2105 ? 163.804 196.473 127.287 1.00 33.96  ? 2105 ARG A NH1   1 
ATOM   5193  N  NH2   . ARG A 1 2105 ? 163.817 195.852 129.489 1.00 34.83  ? 2105 ARG A NH2   1 
ATOM   5194  N  N     . GLU A 1 2106 ? 166.264 202.864 129.800 1.00 41.42  ? 2106 GLU A N     1 
ATOM   5195  C  CA    . GLU A 1 2106 ? 166.364 204.186 130.408 1.00 40.81  ? 2106 GLU A CA    1 
ATOM   5196  C  C     . GLU A 1 2106 ? 167.420 205.037 129.715 1.00 48.31  ? 2106 GLU A C     1 
ATOM   5197  O  O     . GLU A 1 2106 ? 167.214 206.236 129.492 1.00 57.89  ? 2106 GLU A O     1 
ATOM   5198  C  CB    . GLU A 1 2106 ? 166.673 204.054 131.899 1.00 41.76  ? 2106 GLU A CB    1 
ATOM   5199  C  CG    . GLU A 1 2106 ? 166.213 205.234 132.735 1.00 53.36  ? 2106 GLU A CG    1 
ATOM   5200  C  CD    . GLU A 1 2106 ? 167.154 205.533 133.885 1.00 69.03  ? 2106 GLU A CD    1 
ATOM   5201  O  OE1   . GLU A 1 2106 ? 167.186 206.695 134.342 1.00 69.59  ? 2106 GLU A OE1   1 
ATOM   5202  O  OE2   . GLU A 1 2106 ? 167.862 204.606 134.331 1.00 66.42  ? 2106 GLU A OE2   1 
ATOM   5203  N  N     . ARG A 1 2107 ? 168.564 204.437 129.377 1.00 45.19  ? 2107 ARG A N     1 
ATOM   5204  C  CA    . ARG A 1 2107 ? 169.602 205.178 128.668 1.00 45.76  ? 2107 ARG A CA    1 
ATOM   5205  C  C     . ARG A 1 2107 ? 169.134 205.599 127.282 1.00 52.35  ? 2107 ARG A C     1 
ATOM   5206  O  O     . ARG A 1 2107 ? 169.377 206.735 126.860 1.00 59.20  ? 2107 ARG A O     1 
ATOM   5207  C  CB    . ARG A 1 2107 ? 170.878 204.343 128.574 1.00 45.85  ? 2107 ARG A CB    1 
ATOM   5208  C  CG    . ARG A 1 2107 ? 171.642 204.234 129.882 1.00 46.90  ? 2107 ARG A CG    1 
ATOM   5209  C  CD    . ARG A 1 2107 ? 173.132 204.081 129.635 1.00 42.07  ? 2107 ARG A CD    1 
ATOM   5210  N  NE    . ARG A 1 2107 ? 173.864 203.807 130.865 1.00 42.50  ? 2107 ARG A NE    1 
ATOM   5211  C  CZ    . ARG A 1 2107 ? 175.186 203.754 130.954 1.00 46.92  ? 2107 ARG A CZ    1 
ATOM   5212  N  NH1   . ARG A 1 2107 ? 175.958 203.952 129.897 1.00 50.19  ? 2107 ARG A NH1   1 
ATOM   5213  N  NH2   . ARG A 1 2107 ? 175.748 203.496 132.131 1.00 41.06  ? 2107 ARG A NH2   1 
ATOM   5214  N  N     . ILE A 1 2108 ? 168.455 204.702 126.562 1.00 53.47  ? 2108 ILE A N     1 
ATOM   5215  C  CA    . ILE A 1 2108 ? 167.958 205.038 125.230 1.00 48.84  ? 2108 ILE A CA    1 
ATOM   5216  C  C     . ILE A 1 2108 ? 166.964 206.189 125.311 1.00 56.15  ? 2108 ILE A C     1 
ATOM   5217  O  O     . ILE A 1 2108 ? 167.000 207.119 124.495 1.00 63.51  ? 2108 ILE A O     1 
ATOM   5218  C  CB    . ILE A 1 2108 ? 167.343 203.795 124.560 1.00 46.39  ? 2108 ILE A CB    1 
ATOM   5219  C  CG1   . ILE A 1 2108 ? 168.445 202.910 123.974 1.00 46.39  ? 2108 ILE A CG1   1 
ATOM   5220  C  CG2   . ILE A 1 2108 ? 166.354 204.196 123.476 1.00 53.58  ? 2108 ILE A CG2   1 
ATOM   5221  C  CD1   . ILE A 1 2108 ? 168.095 201.440 123.937 1.00 34.83  ? 2108 ILE A CD1   1 
ATOM   5222  N  N     . GLN A 1 2109 ? 166.069 206.153 126.301 1.00 56.12  ? 2109 GLN A N     1 
ATOM   5223  C  CA    . GLN A 1 2109 ? 165.158 207.272 126.519 1.00 57.18  ? 2109 GLN A CA    1 
ATOM   5224  C  C     . GLN A 1 2109 ? 165.924 208.553 126.823 1.00 63.68  ? 2109 GLN A C     1 
ATOM   5225  O  O     . GLN A 1 2109 ? 165.512 209.645 126.414 1.00 69.48  ? 2109 GLN A O     1 
ATOM   5226  C  CB    . GLN A 1 2109 ? 164.189 206.949 127.657 1.00 53.66  ? 2109 GLN A CB    1 
ATOM   5227  C  CG    . GLN A 1 2109 ? 163.141 205.906 127.312 1.00 52.73  ? 2109 GLN A CG    1 
ATOM   5228  C  CD    . GLN A 1 2109 ? 162.183 206.381 126.240 1.00 65.01  ? 2109 GLN A CD    1 
ATOM   5229  O  OE1   . GLN A 1 2109 ? 162.194 205.882 125.116 1.00 69.93  ? 2109 GLN A OE1   1 
ATOM   5230  N  NE2   . GLN A 1 2109 ? 161.347 207.354 126.583 1.00 67.10  ? 2109 GLN A NE2   1 
ATOM   5231  N  N     . LYS A 1 2110 ? 167.040 208.439 127.547 1.00 65.02  ? 2110 LYS A N     1 
ATOM   5232  C  CA    . LYS A 1 2110 ? 167.827 209.619 127.890 1.00 69.55  ? 2110 LYS A CA    1 
ATOM   5233  C  C     . LYS A 1 2110 ? 168.480 210.233 126.656 1.00 71.35  ? 2110 LYS A C     1 
ATOM   5234  O  O     . LYS A 1 2110 ? 168.438 211.454 126.467 1.00 75.98  ? 2110 LYS A O     1 
ATOM   5235  C  CB    . LYS A 1 2110 ? 168.880 209.253 128.935 1.00 68.89  ? 2110 LYS A CB    1 
ATOM   5236  C  CG    . LYS A 1 2110 ? 169.929 210.324 129.164 1.00 76.22  ? 2110 LYS A CG    1 
ATOM   5237  C  CD    . LYS A 1 2110 ? 170.918 209.908 130.240 1.00 72.71  ? 2110 LYS A CD    1 
ATOM   5238  C  CE    . LYS A 1 2110 ? 171.784 208.750 129.774 1.00 68.14  ? 2110 LYS A CE    1 
ATOM   5239  N  NZ    . LYS A 1 2110 ? 172.681 209.141 128.652 1.00 69.64  ? 2110 LYS A NZ    1 
ATOM   5240  N  N     . ILE A 1 2111 ? 169.090 209.403 125.803 1.00 66.45  ? 2111 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 2111 ? 169.764 209.921 124.614 1.00 68.56  ? 2111 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 2111 ? 168.762 210.563 123.663 1.00 76.56  ? 2111 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 2111 ? 169.038 211.609 123.062 1.00 81.75  ? 2111 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 2111 ? 170.569 208.807 123.918 1.00 65.12  ? 2111 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 2111 ? 171.423 208.046 124.936 1.00 69.62  ? 2111 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 2111 ? 171.426 209.388 122.802 1.00 65.23  ? 2111 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 2111 ? 172.637 207.361 124.341 1.00 68.26  ? 2111 ILE A CD1   1 
ATOM   5248  N  N     . LYS A 1 2112 ? 167.588 209.946 123.505 1.00 74.66  ? 2112 LYS A N     1 
ATOM   5249  C  CA    . LYS A 1 2112 ? 166.565 210.521 122.637 1.00 74.26  ? 2112 LYS A CA    1 
ATOM   5250  C  C     . LYS A 1 2112 ? 166.115 211.884 123.148 1.00 78.79  ? 2112 LYS A C     1 
ATOM   5251  O  O     . LYS A 1 2112 ? 165.887 212.807 122.357 1.00 84.76  ? 2112 LYS A O     1 
ATOM   5252  C  CB    . LYS A 1 2112 ? 165.375 209.568 122.524 1.00 70.97  ? 2112 LYS A CB    1 
ATOM   5253  C  CG    . LYS A 1 2112 ? 165.694 208.255 121.828 1.00 76.20  ? 2112 LYS A CG    1 
ATOM   5254  C  CD    . LYS A 1 2112 ? 164.458 207.380 121.701 1.00 79.23  ? 2112 LYS A CD    1 
ATOM   5255  C  CE    . LYS A 1 2112 ? 163.861 207.463 120.307 1.00 82.79  ? 2112 LYS A CE    1 
ATOM   5256  N  NZ    . LYS A 1 2112 ? 164.762 206.860 119.286 1.00 82.95  ? 2112 LYS A NZ    1 
ATOM   5257  N  N     . ARG A 1 2113 ? 165.973 212.027 124.468 1.00 78.60  ? 2113 ARG A N     1 
ATOM   5258  C  CA    . ARG A 1 2113 ? 165.598 213.318 125.035 1.00 81.75  ? 2113 ARG A CA    1 
ATOM   5259  C  C     . ARG A 1 2113 ? 166.683 214.363 124.800 1.00 87.04  ? 2113 ARG A C     1 
ATOM   5260  O  O     . ARG A 1 2113 ? 166.381 215.517 124.475 1.00 90.53  ? 2113 ARG A O     1 
ATOM   5261  C  CB    . ARG A 1 2113 ? 165.298 213.166 126.528 1.00 76.15  ? 2113 ARG A CB    1 
ATOM   5262  C  CG    . ARG A 1 2113 ? 165.727 214.345 127.384 1.00 76.89  ? 2113 ARG A CG    1 
ATOM   5263  C  CD    . ARG A 1 2113 ? 165.186 214.219 128.801 1.00 82.10  ? 2113 ARG A CD    1 
ATOM   5264  N  NE    . ARG A 1 2113 ? 165.833 213.151 129.554 1.00 88.58  ? 2113 ARG A NE    1 
ATOM   5265  C  CZ    . ARG A 1 2113 ? 167.083 213.188 129.995 1.00 86.33  ? 2113 ARG A CZ    1 
ATOM   5266  N  NH1   . ARG A 1 2113 ? 167.860 214.239 129.789 1.00 84.27  ? 2113 ARG A NH1   1 
ATOM   5267  N  NH2   . ARG A 1 2113 ? 167.565 212.145 130.667 1.00 81.20  ? 2113 ARG A NH2   1 
ATOM   5268  N  N     . GLU A 1 2114 ? 167.954 213.979 124.956 1.00 83.76  ? 2114 GLU A N     1 
ATOM   5269  C  CA    . GLU A 1 2114 ? 169.043 214.914 124.688 1.00 85.56  ? 2114 GLU A CA    1 
ATOM   5270  C  C     . GLU A 1 2114 ? 169.053 215.342 123.226 1.00 89.66  ? 2114 GLU A C     1 
ATOM   5271  O  O     . GLU A 1 2114 ? 169.274 216.518 122.916 1.00 94.72  ? 2114 GLU A O     1 
ATOM   5272  C  CB    . GLU A 1 2114 ? 170.388 214.294 125.066 1.00 85.03  ? 2114 GLU A CB    1 
ATOM   5273  C  CG    . GLU A 1 2114 ? 170.524 213.904 126.526 1.00 87.51  ? 2114 GLU A CG    1 
ATOM   5274  C  CD    . GLU A 1 2114 ? 171.769 213.078 126.786 1.00 91.35  ? 2114 GLU A CD    1 
ATOM   5275  O  OE1   . GLU A 1 2114 ? 172.660 213.052 125.911 1.00 87.56  ? 2114 GLU A OE1   1 
ATOM   5276  O  OE2   . GLU A 1 2114 ? 171.863 212.463 127.868 1.00 88.29  ? 2114 GLU A OE2   1 
ATOM   5277  N  N     . LYS A 1 2115 ? 168.824 214.396 122.313 1.00 88.85  ? 2115 LYS A N     1 
ATOM   5278  C  CA    . LYS A 1 2115 ? 168.736 214.739 120.898 1.00 89.62  ? 2115 LYS A CA    1 
ATOM   5279  C  C     . LYS A 1 2115 ? 167.551 215.658 120.629 1.00 92.46  ? 2115 LYS A C     1 
ATOM   5280  O  O     . LYS A 1 2115 ? 167.649 216.591 119.823 1.00 97.69  ? 2115 LYS A O     1 
ATOM   5281  C  CB    . LYS A 1 2115 ? 168.634 213.465 120.060 1.00 87.07  ? 2115 LYS A CB    1 
ATOM   5282  C  CG    . LYS A 1 2115 ? 169.958 212.742 119.867 1.00 87.51  ? 2115 LYS A CG    1 
ATOM   5283  C  CD    . LYS A 1 2115 ? 169.765 211.414 119.153 1.00 88.75  ? 2115 LYS A CD    1 
ATOM   5284  C  CE    . LYS A 1 2115 ? 171.075 210.898 118.581 1.00 84.91  ? 2115 LYS A CE    1 
ATOM   5285  N  NZ    . LYS A 1 2115 ? 172.134 210.800 119.622 1.00 83.16  ? 2115 LYS A NZ    1 
ATOM   5286  N  N     . GLU A 1 2116 ? 166.421 215.406 121.294 1.00 92.86  ? 2116 GLU A N     1 
ATOM   5287  C  CA    . GLU A 1 2116 ? 165.232 216.226 121.081 1.00 96.01  ? 2116 GLU A CA    1 
ATOM   5288  C  C     . GLU A 1 2116 ? 165.451 217.663 121.542 1.00 98.55  ? 2116 GLU A C     1 
ATOM   5289  O  O     . GLU A 1 2116 ? 165.045 218.608 120.856 1.00 98.31  ? 2116 GLU A O     1 
ATOM   5290  C  CB    . GLU A 1 2116 ? 164.035 215.606 121.803 1.00 92.48  ? 2116 GLU A CB    1 
ATOM   5291  C  CG    . GLU A 1 2116 ? 162.690 216.192 121.400 1.00 96.03  ? 2116 GLU A CG    1 
ATOM   5292  C  CD    . GLU A 1 2116 ? 162.255 217.330 122.303 1.00 95.91  ? 2116 GLU A CD    1 
ATOM   5293  O  OE1   . GLU A 1 2116 ? 162.633 217.323 123.493 1.00 96.86  ? 2116 GLU A OE1   1 
ATOM   5294  O  OE2   . GLU A 1 2116 ? 161.533 218.229 121.823 1.00 91.44  ? 2116 GLU A OE2   1 
ATOM   5295  N  N     . GLU A 1 2117 ? 166.089 217.852 122.698 1.00 99.21  ? 2117 GLU A N     1 
ATOM   5296  C  CA    . GLU A 1 2117 ? 166.306 219.194 123.225 1.00 98.74  ? 2117 GLU A CA    1 
ATOM   5297  C  C     . GLU A 1 2117 ? 167.550 219.864 122.657 1.00 98.05  ? 2117 GLU A C     1 
ATOM   5298  O  O     . GLU A 1 2117 ? 167.781 221.044 122.942 1.00 95.94  ? 2117 GLU A O     1 
ATOM   5299  C  CB    . GLU A 1 2117 ? 166.388 219.153 124.755 1.00 100.74 ? 2117 GLU A CB    1 
ATOM   5300  C  CG    . GLU A 1 2117 ? 167.567 218.369 125.312 1.00 103.29 ? 2117 GLU A CG    1 
ATOM   5301  C  CD    . GLU A 1 2117 ? 168.758 219.251 125.634 1.00 106.88 ? 2117 GLU A CD    1 
ATOM   5302  O  OE1   . GLU A 1 2117 ? 168.582 220.486 125.707 1.00 105.42 ? 2117 GLU A OE1   1 
ATOM   5303  O  OE2   . GLU A 1 2117 ? 169.867 218.709 125.820 1.00 103.93 ? 2117 GLU A OE2   1 
ATOM   5304  N  N     . ARG A 1 2118 ? 168.351 219.149 121.867 1.00 101.70 ? 2118 ARG A N     1 
ATOM   5305  C  CA    . ARG A 1 2118 ? 169.524 219.706 121.192 1.00 100.45 ? 2118 ARG A CA    1 
ATOM   5306  C  C     . ARG A 1 2118 ? 169.370 219.398 119.705 1.00 99.78  ? 2118 ARG A C     1 
ATOM   5307  O  O     . ARG A 1 2118 ? 169.861 218.376 119.219 1.00 98.67  ? 2118 ARG A O     1 
ATOM   5308  C  CB    . ARG A 1 2118 ? 170.818 219.131 121.761 1.00 96.91  ? 2118 ARG A CB    1 
ATOM   5309  C  CG    . ARG A 1 2118 ? 171.252 219.756 123.077 1.00 100.42 ? 2118 ARG A CG    1 
ATOM   5310  C  CD    . ARG A 1 2118 ? 171.522 221.244 122.927 1.00 103.01 ? 2118 ARG A CD    1 
ATOM   5311  N  NE    . ARG A 1 2118 ? 172.554 221.514 121.932 1.00 108.16 ? 2118 ARG A NE    1 
ATOM   5312  C  CZ    . ARG A 1 2118 ? 172.352 222.186 120.806 1.00 105.48 ? 2118 ARG A CZ    1 
ATOM   5313  N  NH1   . ARG A 1 2118 ? 171.162 222.675 120.497 1.00 103.67 ? 2118 ARG A NH1   1 
ATOM   5314  N  NH2   . ARG A 1 2118 ? 173.370 222.371 119.970 1.00 100.83 ? 2118 ARG A NH2   1 
ATOM   5315  N  N     . GLY A 1 2119 ? 168.691 220.286 118.985 1.00 98.60  ? 2119 GLY A N     1 
ATOM   5316  C  CA    . GLY A 1 2119 ? 168.394 220.047 117.591 1.00 102.51 ? 2119 GLY A CA    1 
ATOM   5317  C  C     . GLY A 1 2119 ? 167.255 219.059 117.416 1.00 104.98 ? 2119 GLY A C     1 
ATOM   5318  O  O     . GLY A 1 2119 ? 166.501 218.750 118.344 1.00 100.31 ? 2119 GLY A O     1 
ATOM   5319  N  N     . GLU A 1 2120 ? 167.131 218.558 116.186 1.00 106.62 ? 2120 GLU A N     1 
ATOM   5320  C  CA    . GLU A 1 2120 ? 166.109 217.564 115.841 1.00 107.68 ? 2120 GLU A CA    1 
ATOM   5321  C  C     . GLU A 1 2120 ? 166.761 216.517 114.939 1.00 104.57 ? 2120 GLU A C     1 
ATOM   5322  O  O     . GLU A 1 2120 ? 166.767 216.654 113.713 1.00 104.60 ? 2120 GLU A O     1 
ATOM   5323  C  CB    . GLU A 1 2120 ? 164.903 218.214 115.174 1.00 107.98 ? 2120 GLU A CB    1 
ATOM   5324  C  CG    . GLU A 1 2120 ? 164.014 218.996 116.128 1.00 109.02 ? 2120 GLU A CG    1 
ATOM   5325  C  CD    . GLU A 1 2120 ? 162.967 219.821 115.406 1.00 107.84 ? 2120 GLU A CD    1 
ATOM   5326  O  OE1   . GLU A 1 2120 ? 162.184 219.238 114.626 1.00 108.78 ? 2120 GLU A OE1   1 
ATOM   5327  O  OE2   . GLU A 1 2120 ? 162.926 221.051 115.619 1.00 103.26 ? 2120 GLU A OE2   1 
ATOM   5328  N  N     . ALA A 1 2121 ? 167.308 215.472 115.558 1.00 101.63 ? 2121 ALA A N     1 
ATOM   5329  C  CA    . ALA A 1 2121 ? 167.918 214.374 114.810 1.00 100.33 ? 2121 ALA A CA    1 
ATOM   5330  C  C     . ALA A 1 2121 ? 167.866 213.130 115.686 1.00 99.57  ? 2121 ALA A C     1 
ATOM   5331  O  O     . ALA A 1 2121 ? 168.681 212.989 116.603 1.00 97.65  ? 2121 ALA A O     1 
ATOM   5332  C  CB    . ALA A 1 2121 ? 169.349 214.713 114.413 1.00 94.00  ? 2121 ALA A CB    1 
ATOM   5333  N  N     . VAL A 1 2122 ? 166.920 212.237 115.406 1.00 95.55  ? 2122 VAL A N     1 
ATOM   5334  C  CA    . VAL A 1 2122 ? 166.729 211.018 116.181 1.00 90.72  ? 2122 VAL A CA    1 
ATOM   5335  C  C     . VAL A 1 2122 ? 166.710 209.835 115.224 1.00 90.28  ? 2122 VAL A C     1 
ATOM   5336  O  O     . VAL A 1 2122 ? 165.922 209.814 114.271 1.00 89.08  ? 2122 VAL A O     1 
ATOM   5337  C  CB    . VAL A 1 2122 ? 165.431 211.065 117.010 1.00 90.50  ? 2122 VAL A CB    1 
ATOM   5338  C  CG1   . VAL A 1 2122 ? 165.020 209.664 117.441 1.00 89.78  ? 2122 VAL A CG1   1 
ATOM   5339  C  CG2   . VAL A 1 2122 ? 165.606 211.972 118.219 1.00 88.78  ? 2122 VAL A CG2   1 
ATOM   5340  N  N     . ASP A 1 2123 ? 167.576 208.855 115.475 1.00 91.75  ? 2123 ASP A N     1 
ATOM   5341  C  CA    . ASP A 1 2123 ? 167.643 207.644 114.665 1.00 90.19  ? 2123 ASP A CA    1 
ATOM   5342  C  C     . ASP A 1 2123 ? 167.856 206.456 115.589 1.00 87.81  ? 2123 ASP A C     1 
ATOM   5343  O  O     . ASP A 1 2123 ? 168.827 206.429 116.351 1.00 87.28  ? 2123 ASP A O     1 
ATOM   5344  C  CB    . ASP A 1 2123 ? 168.768 207.729 113.629 1.00 89.02  ? 2123 ASP A CB    1 
ATOM   5345  C  CG    . ASP A 1 2123 ? 168.850 206.491 112.758 1.00 86.74  ? 2123 ASP A CG    1 
ATOM   5346  O  OD1   . ASP A 1 2123 ? 167.803 206.068 112.225 1.00 83.76  ? 2123 ASP A OD1   1 
ATOM   5347  O  OD2   . ASP A 1 2123 ? 169.961 205.941 112.606 1.00 86.09  ? 2123 ASP A OD2   1 
ATOM   5348  N  N     . GLU A 1 2124 ? 166.949 205.478 115.521 1.00 85.14  ? 2124 GLU A N     1 
ATOM   5349  C  CA    . GLU A 1 2124 ? 167.075 204.294 116.366 1.00 80.73  ? 2124 GLU A CA    1 
ATOM   5350  C  C     . GLU A 1 2124 ? 168.327 203.497 116.021 1.00 80.07  ? 2124 GLU A C     1 
ATOM   5351  O  O     . GLU A 1 2124 ? 169.016 202.992 116.915 1.00 77.11  ? 2124 GLU A O     1 
ATOM   5352  C  CB    . GLU A 1 2124 ? 165.827 203.420 116.236 1.00 68.71  ? 2124 GLU A CB    1 
ATOM   5353  C  CG    . GLU A 1 2124 ? 164.630 203.928 117.025 1.00 73.62  ? 2124 GLU A CG    1 
ATOM   5354  C  CD    . GLU A 1 2124 ? 164.741 203.638 118.510 1.00 80.58  ? 2124 GLU A CD    1 
ATOM   5355  O  OE1   . GLU A 1 2124 ? 165.630 202.853 118.901 1.00 80.08  ? 2124 GLU A OE1   1 
ATOM   5356  O  OE2   . GLU A 1 2124 ? 163.941 204.200 119.287 1.00 77.95  ? 2124 GLU A OE2   1 
ATOM   5357  N  N     . GLY A 1 2125 ? 168.633 203.368 114.728 1.00 76.07  ? 2125 GLY A N     1 
ATOM   5358  C  CA    . GLY A 1 2125 ? 169.803 202.602 114.328 1.00 76.93  ? 2125 GLY A CA    1 
ATOM   5359  C  C     . GLY A 1 2125 ? 171.103 203.206 114.822 1.00 82.24  ? 2125 GLY A C     1 
ATOM   5360  O  O     . GLY A 1 2125 ? 172.006 202.488 115.259 1.00 76.63  ? 2125 GLY A O     1 
ATOM   5361  N  N     . GLU A 1 2126 ? 171.221 204.534 114.751 1.00 87.28  ? 2126 GLU A N     1 
ATOM   5362  C  CA    . GLU A 1 2126 ? 172.438 205.195 115.215 1.00 83.60  ? 2126 GLU A CA    1 
ATOM   5363  C  C     . GLU A 1 2126 ? 172.625 205.023 116.717 1.00 76.92  ? 2126 GLU A C     1 
ATOM   5364  O  O     . GLU A 1 2126 ? 173.744 204.786 117.188 1.00 77.27  ? 2126 GLU A O     1 
ATOM   5365  C  CB    . GLU A 1 2126 ? 172.404 206.677 114.843 1.00 86.30  ? 2126 GLU A CB    1 
ATOM   5366  C  CG    . GLU A 1 2126 ? 173.734 207.390 115.013 1.00 87.61  ? 2126 GLU A CG    1 
ATOM   5367  C  CD    . GLU A 1 2126 ? 173.642 208.873 114.714 1.00 94.81  ? 2126 GLU A CD    1 
ATOM   5368  O  OE1   . GLU A 1 2126 ? 172.513 209.375 114.532 1.00 96.60  ? 2126 GLU A OE1   1 
ATOM   5369  O  OE2   . GLU A 1 2126 ? 174.698 209.537 114.659 1.00 94.32  ? 2126 GLU A OE2   1 
ATOM   5370  N  N     . ILE A 1 2127 ? 171.542 205.148 117.488 1.00 73.01  ? 2127 ILE A N     1 
ATOM   5371  C  CA    . ILE A 1 2127 ? 171.636 204.983 118.935 1.00 74.29  ? 2127 ILE A CA    1 
ATOM   5372  C  C     . ILE A 1 2127 ? 172.008 203.549 119.289 1.00 70.90  ? 2127 ILE A C     1 
ATOM   5373  O  O     . ILE A 1 2127 ? 172.846 203.310 120.166 1.00 64.64  ? 2127 ILE A O     1 
ATOM   5374  C  CB    . ILE A 1 2127 ? 170.320 205.411 119.608 1.00 71.32  ? 2127 ILE A CB    1 
ATOM   5375  C  CG1   . ILE A 1 2127 ? 170.028 206.884 119.316 1.00 75.03  ? 2127 ILE A CG1   1 
ATOM   5376  C  CG2   . ILE A 1 2127 ? 170.380 205.164 121.108 1.00 63.87  ? 2127 ILE A CG2   1 
ATOM   5377  C  CD1   . ILE A 1 2127 ? 168.664 207.338 119.778 1.00 76.73  ? 2127 ILE A CD1   1 
ATOM   5378  N  N     . ALA A 1 2128 ? 171.395 202.573 118.614 1.00 71.28  ? 2128 ALA A N     1 
ATOM   5379  C  CA    . ALA A 1 2128 ? 171.671 201.173 118.918 1.00 69.89  ? 2128 ALA A CA    1 
ATOM   5380  C  C     . ALA A 1 2128 ? 173.125 200.818 118.635 1.00 68.59  ? 2128 ALA A C     1 
ATOM   5381  O  O     . ALA A 1 2128 ? 173.744 200.057 119.389 1.00 62.68  ? 2128 ALA A O     1 
ATOM   5382  C  CB    . ALA A 1 2128 ? 170.732 200.268 118.121 1.00 64.52  ? 2128 ALA A CB    1 
ATOM   5383  N  N     . GLU A 1 2129 ? 173.688 201.354 117.550 1.00 71.47  ? 2129 GLU A N     1 
ATOM   5384  C  CA    . GLU A 1 2129 ? 175.078 201.055 117.218 1.00 66.92  ? 2129 GLU A CA    1 
ATOM   5385  C  C     . GLU A 1 2129 ? 176.040 201.732 118.186 1.00 62.49  ? 2129 GLU A C     1 
ATOM   5386  O  O     . GLU A 1 2129 ? 176.982 201.099 118.677 1.00 57.18  ? 2129 GLU A O     1 
ATOM   5387  C  CB    . GLU A 1 2129 ? 175.377 201.480 115.781 1.00 68.67  ? 2129 GLU A CB    1 
ATOM   5388  C  CG    . GLU A 1 2129 ? 175.092 200.406 114.743 1.00 73.18  ? 2129 GLU A CG    1 
ATOM   5389  C  CD    . GLU A 1 2129 ? 174.799 200.983 113.372 1.00 78.88  ? 2129 GLU A CD    1 
ATOM   5390  O  OE1   . GLU A 1 2129 ? 175.519 201.913 112.951 1.00 85.58  ? 2129 GLU A OE1   1 
ATOM   5391  O  OE2   . GLU A 1 2129 ? 173.851 200.506 112.715 1.00 73.29  ? 2129 GLU A OE2   1 
ATOM   5392  N  N     . ASN A 1 2130 ? 175.821 203.012 118.473 1.00 67.71  ? 2130 ASN A N     1 
ATOM   5393  C  CA    . ASN A 1 2130 ? 176.708 203.774 119.350 1.00 64.03  ? 2130 ASN A CA    1 
ATOM   5394  C  C     . ASN A 1 2130 ? 176.139 203.795 120.768 1.00 59.90  ? 2130 ASN A C     1 
ATOM   5395  O  O     . ASN A 1 2130 ? 175.764 204.832 121.316 1.00 62.35  ? 2130 ASN A O     1 
ATOM   5396  C  CB    . ASN A 1 2130 ? 176.909 205.183 118.801 1.00 60.68  ? 2130 ASN A CB    1 
ATOM   5397  C  CG    . ASN A 1 2130 ? 177.353 205.184 117.352 1.00 66.38  ? 2130 ASN A CG    1 
ATOM   5398  O  OD1   . ASN A 1 2130 ? 178.284 204.471 116.975 1.00 66.56  ? 2130 ASN A OD1   1 
ATOM   5399  N  ND2   . ASN A 1 2130 ? 176.684 205.983 116.530 1.00 70.04  ? 2130 ASN A ND2   1 
ATOM   5400  N  N     . LEU A 1 2131 ? 176.084 202.602 121.364 1.00 59.15  ? 2131 LEU A N     1 
ATOM   5401  C  CA    . LEU A 1 2131 ? 175.553 202.434 122.706 1.00 53.25  ? 2131 LEU A CA    1 
ATOM   5402  C  C     . LEU A 1 2131 ? 176.496 201.536 123.499 1.00 49.30  ? 2131 LEU A C     1 
ATOM   5403  O  O     . LEU A 1 2131 ? 176.736 200.382 123.096 1.00 47.25  ? 2131 LEU A O     1 
ATOM   5404  C  CB    . LEU A 1 2131 ? 174.144 201.838 122.678 1.00 53.06  ? 2131 LEU A CB    1 
ATOM   5405  C  CG    . LEU A 1 2131 ? 173.361 201.887 123.988 1.00 47.96  ? 2131 LEU A CG    1 
ATOM   5406  C  CD1   . LEU A 1 2131 ? 172.720 203.252 124.177 1.00 51.52  ? 2131 LEU A CD1   1 
ATOM   5407  C  CD2   . LEU A 1 2131 ? 172.312 200.793 124.006 1.00 43.85  ? 2131 LEU A CD2   1 
ATOM   5408  N  N     . PRO A 1 2132 ? 177.038 202.018 124.618 1.00 49.95  ? 2132 PRO A N     1 
ATOM   5409  C  CA    . PRO A 1 2132 ? 178.001 201.227 125.415 1.00 48.68  ? 2132 PRO A CA    1 
ATOM   5410  C  C     . PRO A 1 2132 ? 177.330 200.115 126.218 1.00 41.71  ? 2132 PRO A C     1 
ATOM   5411  O  O     . PRO A 1 2132 ? 176.988 200.244 127.393 1.00 39.65  ? 2132 PRO A O     1 
ATOM   5412  C  CB    . PRO A 1 2132 ? 178.636 202.287 126.317 1.00 48.15  ? 2132 PRO A CB    1 
ATOM   5413  C  CG    . PRO A 1 2132 ? 177.570 203.312 126.491 1.00 45.48  ? 2132 PRO A CG    1 
ATOM   5414  C  CD    . PRO A 1 2132 ? 176.791 203.348 125.203 1.00 45.58  ? 2132 PRO A CD    1 
ATOM   5415  N  N     . GLU A 1 2133 ? 177.125 198.979 125.547 1.00 33.52  ? 2133 GLU A N     1 
ATOM   5416  C  CA    . GLU A 1 2133 ? 176.473 197.843 126.189 1.00 31.96  ? 2133 GLU A CA    1 
ATOM   5417  C  C     . GLU A 1 2133 ? 177.316 197.291 127.332 1.00 34.49  ? 2133 GLU A C     1 
ATOM   5418  O  O     . GLU A 1 2133 ? 176.779 196.734 128.297 1.00 39.28  ? 2133 GLU A O     1 
ATOM   5419  C  CB    . GLU A 1 2133 ? 176.184 196.758 125.152 1.00 33.70  ? 2133 GLU A CB    1 
ATOM   5420  C  CG    . GLU A 1 2133 ? 175.151 197.168 124.116 1.00 36.30  ? 2133 GLU A CG    1 
ATOM   5421  C  CD    . GLU A 1 2133 ? 174.899 196.092 123.080 1.00 39.23  ? 2133 GLU A CD    1 
ATOM   5422  O  OE1   . GLU A 1 2133 ? 175.615 195.069 123.093 1.00 41.52  ? 2133 GLU A OE1   1 
ATOM   5423  O  OE2   . GLU A 1 2133 ? 173.985 196.274 122.248 1.00 38.75  ? 2133 GLU A OE2   1 
ATOM   5424  N  N     . GLN A 1 2134 ? 178.640 197.429 127.238 1.00 35.42  ? 2134 GLN A N     1 
ATOM   5425  C  CA    . GLN A 1 2134 ? 179.515 196.988 128.319 1.00 32.11  ? 2134 GLN A CA    1 
ATOM   5426  C  C     . GLN A 1 2134 ? 179.255 197.775 129.599 1.00 32.65  ? 2134 GLN A C     1 
ATOM   5427  O  O     . GLN A 1 2134 ? 179.187 197.202 130.692 1.00 32.67  ? 2134 GLN A O     1 
ATOM   5428  C  CB    . GLN A 1 2134 ? 180.978 197.122 127.890 1.00 28.93  ? 2134 GLN A CB    1 
ATOM   5429  C  CG    . GLN A 1 2134 ? 181.410 196.147 126.807 1.00 30.14  ? 2134 GLN A CG    1 
ATOM   5430  C  CD    . GLN A 1 2134 ? 181.957 194.852 127.372 1.00 35.16  ? 2134 GLN A CD    1 
ATOM   5431  O  OE1   . GLN A 1 2134 ? 181.220 194.054 127.951 1.00 38.74  ? 2134 GLN A OE1   1 
ATOM   5432  N  NE2   . GLN A 1 2134 ? 183.251 194.630 127.196 1.00 28.83  ? 2134 GLN A NE2   1 
ATOM   5433  N  N     . GLU A 1 2135 ? 179.101 199.097 129.481 1.00 31.70  ? 2135 GLU A N     1 
ATOM   5434  C  CA    . GLU A 1 2135 ? 178.860 199.915 130.666 1.00 33.99  ? 2135 GLU A CA    1 
ATOM   5435  C  C     . GLU A 1 2135 ? 177.473 199.662 131.245 1.00 32.10  ? 2135 GLU A C     1 
ATOM   5436  O  O     . GLU A 1 2135 ? 177.283 199.733 132.465 1.00 28.82  ? 2135 GLU A O     1 
ATOM   5437  C  CB    . GLU A 1 2135 ? 179.044 201.398 130.339 1.00 38.49  ? 2135 GLU A CB    1 
ATOM   5438  C  CG    . GLU A 1 2135 ? 180.485 201.874 130.450 1.00 43.92  ? 2135 GLU A CG    1 
ATOM   5439  C  CD    . GLU A 1 2135 ? 180.860 202.887 129.387 1.00 58.92  ? 2135 GLU A CD    1 
ATOM   5440  O  OE1   . GLU A 1 2135 ? 182.067 203.025 129.095 1.00 61.23  ? 2135 GLU A OE1   1 
ATOM   5441  O  OE2   . GLU A 1 2135 ? 179.953 203.561 128.858 1.00 60.20  ? 2135 GLU A OE2   1 
ATOM   5442  N  N     . ILE A 1 2136 ? 176.492 199.374 130.387 1.00 31.70  ? 2136 ILE A N     1 
ATOM   5443  C  CA    . ILE A 1 2136 ? 175.140 199.093 130.865 1.00 28.52  ? 2136 ILE A CA    1 
ATOM   5444  C  C     . ILE A 1 2136 ? 175.137 197.848 131.743 1.00 25.24  ? 2136 ILE A C     1 
ATOM   5445  O  O     . ILE A 1 2136 ? 174.543 197.830 132.828 1.00 22.87  ? 2136 ILE A O     1 
ATOM   5446  C  CB    . ILE A 1 2136 ? 174.171 198.950 129.677 1.00 28.86  ? 2136 ILE A CB    1 
ATOM   5447  C  CG1   . ILE A 1 2136 ? 174.019 200.287 128.950 1.00 33.80  ? 2136 ILE A CG1   1 
ATOM   5448  C  CG2   . ILE A 1 2136 ? 172.818 198.441 130.145 1.00 29.37  ? 2136 ILE A CG2   1 
ATOM   5449  C  CD1   . ILE A 1 2136 ? 173.382 200.168 127.584 1.00 33.26  ? 2136 ILE A CD1   1 
ATOM   5450  N  N     . LEU A 1 2137 ? 175.807 196.788 131.287 1.00 23.53  ? 2137 LEU A N     1 
ATOM   5451  C  CA    . LEU A 1 2137 ? 175.875 195.560 132.072 1.00 20.69  ? 2137 LEU A CA    1 
ATOM   5452  C  C     . LEU A 1 2137 ? 176.666 195.768 133.358 1.00 24.74  ? 2137 LEU A C     1 
ATOM   5453  O  O     . LEU A 1 2137 ? 176.303 195.233 134.413 1.00 28.16  ? 2137 LEU A O     1 
ATOM   5454  C  CB    . LEU A 1 2137 ? 176.490 194.440 131.233 1.00 25.86  ? 2137 LEU A CB    1 
ATOM   5455  C  CG    . LEU A 1 2137 ? 176.320 193.007 131.736 1.00 26.01  ? 2137 LEU A CG    1 
ATOM   5456  C  CD1   . LEU A 1 2137 ? 174.891 192.538 131.541 1.00 29.98  ? 2137 LEU A CD1   1 
ATOM   5457  C  CD2   . LEU A 1 2137 ? 177.286 192.083 131.016 1.00 26.53  ? 2137 LEU A CD2   1 
ATOM   5458  N  N     . ILE A 1 2138 ? 177.753 196.538 133.288 1.00 26.24  ? 2138 ILE A N     1 
ATOM   5459  C  CA    . ILE A 1 2138 ? 178.565 196.793 134.474 1.00 21.48  ? 2138 ILE A CA    1 
ATOM   5460  C  C     . ILE A 1 2138 ? 177.775 197.596 135.500 1.00 23.43  ? 2138 ILE A C     1 
ATOM   5461  O  O     . ILE A 1 2138 ? 177.817 197.305 136.702 1.00 31.30  ? 2138 ILE A O     1 
ATOM   5462  C  CB    . ILE A 1 2138 ? 179.874 197.500 134.079 1.00 26.92  ? 2138 ILE A CB    1 
ATOM   5463  C  CG1   . ILE A 1 2138 ? 180.846 196.503 133.447 1.00 32.02  ? 2138 ILE A CG1   1 
ATOM   5464  C  CG2   . ILE A 1 2138 ? 180.516 198.165 135.286 1.00 27.74  ? 2138 ILE A CG2   1 
ATOM   5465  C  CD1   . ILE A 1 2138 ? 180.785 195.122 134.053 1.00 31.86  ? 2138 ILE A CD1   1 
ATOM   5466  N  N     . GLN A 1 2139 ? 177.043 198.614 135.044 1.00 22.68  ? 2139 GLN A N     1 
ATOM   5467  C  CA    . GLN A 1 2139 ? 176.212 199.399 135.951 1.00 21.98  ? 2139 GLN A CA    1 
ATOM   5468  C  C     . GLN A 1 2139 ? 175.151 198.531 136.612 1.00 23.26  ? 2139 GLN A C     1 
ATOM   5469  O  O     . GLN A 1 2139 ? 174.872 198.677 137.808 1.00 27.23  ? 2139 GLN A O     1 
ATOM   5470  C  CB    . GLN A 1 2139 ? 175.560 200.555 135.194 1.00 24.65  ? 2139 GLN A CB    1 
ATOM   5471  C  CG    . GLN A 1 2139 ? 174.717 201.472 136.060 1.00 26.74  ? 2139 GLN A CG    1 
ATOM   5472  C  CD    . GLN A 1 2139 ? 173.672 202.222 135.261 1.00 28.60  ? 2139 GLN A CD    1 
ATOM   5473  O  OE1   . GLN A 1 2139 ? 173.967 202.786 134.208 1.00 34.23  ? 2139 GLN A OE1   1 
ATOM   5474  N  NE2   . GLN A 1 2139 ? 172.441 202.231 135.757 1.00 31.44  ? 2139 GLN A NE2   1 
ATOM   5475  N  N     . SER A 1 2140 ? 174.545 197.623 135.844 1.00 22.89  ? 2140 SER A N     1 
ATOM   5476  C  CA    . SER A 1 2140 ? 173.567 196.701 136.410 1.00 17.53  ? 2140 SER A CA    1 
ATOM   5477  C  C     . SER A 1 2140 ? 174.205 195.780 137.442 1.00 21.37  ? 2140 SER A C     1 
ATOM   5478  O  O     . SER A 1 2140 ? 173.603 195.490 138.483 1.00 24.12  ? 2140 SER A O     1 
ATOM   5479  C  CB    . SER A 1 2140 ? 172.915 195.889 135.292 1.00 20.98  ? 2140 SER A CB    1 
ATOM   5480  O  OG    . SER A 1 2140 ? 171.710 195.289 135.728 1.00 25.91  ? 2140 SER A OG    1 
ATOM   5481  N  N     . VAL A 1 2141 ? 175.422 195.303 137.168 1.00 22.74  ? 2141 VAL A N     1 
ATOM   5482  C  CA    . VAL A 1 2141 ? 176.103 194.407 138.100 1.00 22.32  ? 2141 VAL A CA    1 
ATOM   5483  C  C     . VAL A 1 2141 ? 176.397 195.126 139.410 1.00 26.14  ? 2141 VAL A C     1 
ATOM   5484  O  O     . VAL A 1 2141 ? 176.110 194.615 140.500 1.00 30.26  ? 2141 VAL A O     1 
ATOM   5485  C  CB    . VAL A 1 2141 ? 177.391 193.853 137.465 1.00 19.97  ? 2141 VAL A CB    1 
ATOM   5486  C  CG1   . VAL A 1 2141 ? 178.348 193.363 138.539 1.00 23.67  ? 2141 VAL A CG1   1 
ATOM   5487  C  CG2   . VAL A 1 2141 ? 177.068 192.736 136.497 1.00 23.27  ? 2141 VAL A CG2   1 
ATOM   5488  N  N     . CYS A 1 2142 ? 176.973 196.325 139.322 1.00 23.55  ? 2142 CYS A N     1 
ATOM   5489  C  CA    . CYS A 1 2142 ? 177.384 197.040 140.525 1.00 23.27  ? 2142 CYS A CA    1 
ATOM   5490  C  C     . CYS A 1 2142 ? 176.178 197.468 141.353 1.00 22.76  ? 2142 CYS A C     1 
ATOM   5491  O  O     . CYS A 1 2142 ? 176.203 197.401 142.587 1.00 27.21  ? 2142 CYS A O     1 
ATOM   5492  C  CB    . CYS A 1 2142 ? 178.238 198.247 140.146 1.00 29.61  ? 2142 CYS A CB    1 
ATOM   5493  S  SG    . CYS A 1 2142 ? 179.870 197.832 139.491 1.00 42.30  ? 2142 CYS A SG    1 
ATOM   5494  N  N     . GLU A 1 2143 ? 175.106 197.906 140.689 1.00 24.53  ? 2143 GLU A N     1 
ATOM   5495  C  CA    . GLU A 1 2143 ? 173.926 198.364 141.415 1.00 22.83  ? 2143 GLU A CA    1 
ATOM   5496  C  C     . GLU A 1 2143 ? 173.294 197.246 142.235 1.00 27.18  ? 2143 GLU A C     1 
ATOM   5497  O  O     . GLU A 1 2143 ? 172.568 197.518 143.197 1.00 33.56  ? 2143 GLU A O     1 
ATOM   5498  C  CB    . GLU A 1 2143 ? 172.904 198.948 140.440 1.00 25.18  ? 2143 GLU A CB    1 
ATOM   5499  C  CG    . GLU A 1 2143 ? 172.797 200.463 140.490 1.00 36.93  ? 2143 GLU A CG    1 
ATOM   5500  C  CD    . GLU A 1 2143 ? 172.163 201.048 139.244 1.00 40.50  ? 2143 GLU A CD    1 
ATOM   5501  O  OE1   . GLU A 1 2143 ? 171.573 200.278 138.457 1.00 46.28  ? 2143 GLU A OE1   1 
ATOM   5502  O  OE2   . GLU A 1 2143 ? 172.254 202.279 139.052 1.00 44.02  ? 2143 GLU A OE2   1 
ATOM   5503  N  N     . THR A 1 2144 ? 173.557 195.990 141.877 1.00 25.25  ? 2144 THR A N     1 
ATOM   5504  C  CA    . THR A 1 2144 ? 172.971 194.857 142.581 1.00 18.31  ? 2144 THR A CA    1 
ATOM   5505  C  C     . THR A 1 2144 ? 173.956 194.157 143.508 1.00 25.04  ? 2144 THR A C     1 
ATOM   5506  O  O     . THR A 1 2144 ? 173.541 193.593 144.527 1.00 33.50  ? 2144 THR A O     1 
ATOM   5507  C  CB    . THR A 1 2144 ? 172.410 193.849 141.571 1.00 24.87  ? 2144 THR A CB    1 
ATOM   5508  O  OG1   . THR A 1 2144 ? 171.635 194.542 140.586 1.00 26.57  ? 2144 THR A OG1   1 
ATOM   5509  C  CG2   . THR A 1 2144 ? 171.524 192.826 142.265 1.00 26.66  ? 2144 THR A CG2   1 
ATOM   5510  N  N     . MET A 1 2145 ? 175.252 194.190 143.196 1.00 22.73  ? 2145 MET A N     1 
ATOM   5511  C  CA    . MET A 1 2145 ? 176.240 193.432 143.953 1.00 19.77  ? 2145 MET A CA    1 
ATOM   5512  C  C     . MET A 1 2145 ? 177.119 194.278 144.862 1.00 15.46  ? 2145 MET A C     1 
ATOM   5513  O  O     . MET A 1 2145 ? 177.674 193.743 145.822 1.00 15.65  ? 2145 MET A O     1 
ATOM   5514  C  CB    . MET A 1 2145 ? 177.142 192.634 143.002 1.00 27.03  ? 2145 MET A CB    1 
ATOM   5515  C  CG    . MET A 1 2145 ? 176.389 191.797 141.978 1.00 30.14  ? 2145 MET A CG    1 
ATOM   5516  S  SD    . MET A 1 2145 ? 176.012 190.129 142.548 1.00 45.21  ? 2145 MET A SD    1 
ATOM   5517  C  CE    . MET A 1 2145 ? 174.381 190.364 143.251 1.00 27.44  ? 2145 MET A CE    1 
ATOM   5518  N  N     . VAL A 1 2146 ? 177.281 195.573 144.583 1.00 16.40  ? 2146 VAL A N     1 
ATOM   5519  C  CA    . VAL A 1 2146 ? 178.117 196.416 145.447 1.00 15.89  ? 2146 VAL A CA    1 
ATOM   5520  C  C     . VAL A 1 2146 ? 177.548 196.556 146.853 1.00 15.49  ? 2146 VAL A C     1 
ATOM   5521  O  O     . VAL A 1 2146 ? 178.312 196.405 147.819 1.00 16.52  ? 2146 VAL A O     1 
ATOM   5522  C  CB    . VAL A 1 2146 ? 178.389 197.765 144.768 1.00 14.03  ? 2146 VAL A CB    1 
ATOM   5523  C  CG1   . VAL A 1 2146 ? 178.922 198.772 145.774 1.00 13.80  ? 2146 VAL A CG1   1 
ATOM   5524  C  CG2   . VAL A 1 2146 ? 179.370 197.590 143.619 1.00 14.73  ? 2146 VAL A CG2   1 
ATOM   5525  N  N     . PRO A 1 2147 ? 176.254 196.843 147.060 1.00 13.57  ? 2147 PRO A N     1 
ATOM   5526  C  CA    . PRO A 1 2147 ? 175.777 197.079 148.436 1.00 10.67  ? 2147 PRO A CA    1 
ATOM   5527  C  C     . PRO A 1 2147 ? 175.997 195.916 149.386 1.00 10.13  ? 2147 PRO A C     1 
ATOM   5528  O  O     . PRO A 1 2147 ? 176.205 196.142 150.585 1.00 10.46  ? 2147 PRO A O     1 
ATOM   5529  C  CB    . PRO A 1 2147 ? 174.282 197.359 148.237 1.00 11.21  ? 2147 PRO A CB    1 
ATOM   5530  C  CG    . PRO A 1 2147 ? 174.199 197.933 146.883 1.00 12.21  ? 2147 PRO A CG    1 
ATOM   5531  C  CD    . PRO A 1 2147 ? 175.213 197.186 146.072 1.00 14.46  ? 2147 PRO A CD    1 
ATOM   5532  N  N     . LYS A 1 2148 ? 175.956 194.679 148.897 1.00 9.75   ? 2148 LYS A N     1 
ATOM   5533  C  CA    . LYS A 1 2148 ? 176.153 193.516 149.751 1.00 9.27   ? 2148 LYS A CA    1 
ATOM   5534  C  C     . LYS A 1 2148 ? 177.615 193.271 150.100 1.00 12.45  ? 2148 LYS A C     1 
ATOM   5535  O  O     . LYS A 1 2148 ? 177.890 192.554 151.068 1.00 14.78  ? 2148 LYS A O     1 
ATOM   5536  C  CB    . LYS A 1 2148 ? 175.572 192.273 149.073 1.00 10.73  ? 2148 LYS A CB    1 
ATOM   5537  C  CG    . LYS A 1 2148 ? 176.336 191.858 147.833 1.00 12.66  ? 2148 LYS A CG    1 
ATOM   5538  C  CD    . LYS A 1 2148 ? 175.603 190.808 147.022 1.00 14.08  ? 2148 LYS A CD    1 
ATOM   5539  C  CE    . LYS A 1 2148 ? 176.121 189.418 147.312 1.00 19.72  ? 2148 LYS A CE    1 
ATOM   5540  N  NZ    . LYS A 1 2148 ? 175.628 188.456 146.292 1.00 25.34  ? 2148 LYS A NZ    1 
ATOM   5541  N  N     . LEU A 1 2149 ? 178.551 193.849 149.352 1.00 12.03  ? 2149 LEU A N     1 
ATOM   5542  C  CA    . LEU A 1 2149 ? 179.966 193.570 149.550 1.00 13.19  ? 2149 LEU A CA    1 
ATOM   5543  C  C     . LEU A 1 2149 ? 180.494 194.223 150.819 1.00 13.86  ? 2149 LEU A C     1 
ATOM   5544  O  O     . LEU A 1 2149 ? 180.057 195.310 151.208 1.00 19.23  ? 2149 LEU A O     1 
ATOM   5545  C  CB    . LEU A 1 2149 ? 180.779 194.053 148.350 1.00 16.67  ? 2149 LEU A CB    1 
ATOM   5546  C  CG    . LEU A 1 2149 ? 180.594 193.289 147.042 1.00 11.89  ? 2149 LEU A CG    1 
ATOM   5547  C  CD1   . LEU A 1 2149 ? 181.640 193.724 146.038 1.00 15.18  ? 2149 LEU A CD1   1 
ATOM   5548  C  CD2   . LEU A 1 2149 ? 180.666 191.792 147.280 1.00 13.33  ? 2149 LEU A CD2   1 
ATOM   5549  N  N     . VAL A 1 2150 ? 181.442 193.547 151.464 1.00 14.45  ? 2150 VAL A N     1 
ATOM   5550  C  CA    . VAL A 1 2150 ? 182.164 194.105 152.601 1.00 17.93  ? 2150 VAL A CA    1 
ATOM   5551  C  C     . VAL A 1 2150 ? 183.235 195.047 152.069 1.00 24.36  ? 2150 VAL A C     1 
ATOM   5552  O  O     . VAL A 1 2150 ? 183.510 195.068 150.864 1.00 25.23  ? 2150 VAL A O     1 
ATOM   5553  C  CB    . VAL A 1 2150 ? 182.776 192.999 153.479 1.00 20.39  ? 2150 VAL A CB    1 
ATOM   5554  C  CG1   . VAL A 1 2150 ? 181.683 192.109 154.047 1.00 13.09  ? 2150 VAL A CG1   1 
ATOM   5555  C  CG2   . VAL A 1 2150 ? 183.773 192.180 152.679 1.00 21.93  ? 2150 VAL A CG2   1 
ATOM   5556  N  N     . ALA A 1 2151 ? 183.848 195.828 152.962 1.00 27.80  ? 2151 ALA A N     1 
ATOM   5557  C  CA    . ALA A 1 2151 ? 184.811 196.837 152.530 1.00 26.91  ? 2151 ALA A CA    1 
ATOM   5558  C  C     . ALA A 1 2151 ? 186.003 196.207 151.820 1.00 29.34  ? 2151 ALA A C     1 
ATOM   5559  O  O     . ALA A 1 2151 ? 186.516 196.762 150.842 1.00 27.60  ? 2151 ALA A O     1 
ATOM   5560  C  CB    . ALA A 1 2151 ? 185.275 197.666 153.727 1.00 21.98  ? 2151 ALA A CB    1 
ATOM   5561  N  N     . GLU A 1 2152 ? 186.460 195.049 152.298 1.00 30.86  ? 2152 GLU A N     1 
ATOM   5562  C  CA    . GLU A 1 2152 ? 187.610 194.389 151.693 1.00 31.17  ? 2152 GLU A CA    1 
ATOM   5563  C  C     . GLU A 1 2152 ? 187.304 193.815 150.317 1.00 35.12  ? 2152 GLU A C     1 
ATOM   5564  O  O     . GLU A 1 2152 ? 188.231 193.618 149.524 1.00 38.82  ? 2152 GLU A O     1 
ATOM   5565  C  CB    . GLU A 1 2152 ? 188.136 193.268 152.600 1.00 32.66  ? 2152 GLU A CB    1 
ATOM   5566  C  CG    . GLU A 1 2152 ? 188.241 193.598 154.093 1.00 37.73  ? 2152 GLU A CG    1 
ATOM   5567  C  CD    . GLU A 1 2152 ? 186.897 193.646 154.801 1.00 38.01  ? 2152 GLU A CD    1 
ATOM   5568  O  OE1   . GLU A 1 2152 ? 186.361 192.569 155.137 1.00 31.03  ? 2152 GLU A OE1   1 
ATOM   5569  O  OE2   . GLU A 1 2152 ? 186.378 194.760 155.023 1.00 35.55  ? 2152 GLU A OE2   1 
ATOM   5570  N  N     . ASP A 1 2153 ? 186.034 193.542 150.014 1.00 34.84  ? 2153 ASP A N     1 
ATOM   5571  C  CA    . ASP A 1 2153 ? 185.680 192.937 148.736 1.00 23.98  ? 2153 ASP A CA    1 
ATOM   5572  C  C     . ASP A 1 2153 ? 185.356 193.962 147.657 1.00 25.22  ? 2153 ASP A C     1 
ATOM   5573  O  O     . ASP A 1 2153 ? 185.276 193.591 146.482 1.00 27.35  ? 2153 ASP A O     1 
ATOM   5574  C  CB    . ASP A 1 2153 ? 184.492 191.991 148.915 1.00 20.14  ? 2153 ASP A CB    1 
ATOM   5575  C  CG    . ASP A 1 2153 ? 184.884 190.681 149.569 1.00 33.09  ? 2153 ASP A CG    1 
ATOM   5576  O  OD1   . ASP A 1 2153 ? 186.094 190.378 149.621 1.00 39.24  ? 2153 ASP A OD1   1 
ATOM   5577  O  OD2   . ASP A 1 2153 ? 183.982 189.953 150.034 1.00 32.52  ? 2153 ASP A OD2   1 
ATOM   5578  N  N     . ILE A 1 2154 ? 185.156 195.232 148.021 1.00 28.05  ? 2154 ILE A N     1 
ATOM   5579  C  CA    . ILE A 1 2154 ? 184.854 196.249 147.010 1.00 27.01  ? 2154 ILE A CA    1 
ATOM   5580  C  C     . ILE A 1 2154 ? 186.009 196.444 146.034 1.00 30.21  ? 2154 ILE A C     1 
ATOM   5581  O  O     . ILE A 1 2154 ? 185.767 196.426 144.816 1.00 33.57  ? 2154 ILE A O     1 
ATOM   5582  C  CB    . ILE A 1 2154 ? 184.415 197.559 147.689 1.00 28.47  ? 2154 ILE A CB    1 
ATOM   5583  C  CG1   . ILE A 1 2154 ? 183.253 197.301 148.648 1.00 23.50  ? 2154 ILE A CG1   1 
ATOM   5584  C  CG2   . ILE A 1 2154 ? 184.027 198.595 146.647 1.00 28.89  ? 2154 ILE A CG2   1 
ATOM   5585  C  CD1   . ILE A 1 2154 ? 182.877 198.500 149.486 1.00 24.34  ? 2154 ILE A CD1   1 
ATOM   5586  N  N     . PRO A 1 2155 ? 187.262 196.638 146.472 1.00 28.90  ? 2155 PRO A N     1 
ATOM   5587  C  CA    . PRO A 1 2155 ? 188.360 196.642 145.491 1.00 24.59  ? 2155 PRO A CA    1 
ATOM   5588  C  C     . PRO A 1 2155 ? 188.516 195.310 144.783 1.00 27.97  ? 2155 PRO A C     1 
ATOM   5589  O  O     . PRO A 1 2155 ? 188.939 195.272 143.620 1.00 29.86  ? 2155 PRO A O     1 
ATOM   5590  C  CB    . PRO A 1 2155 ? 189.592 196.982 146.343 1.00 29.63  ? 2155 PRO A CB    1 
ATOM   5591  C  CG    . PRO A 1 2155 ? 189.051 197.630 147.562 1.00 30.40  ? 2155 PRO A CG    1 
ATOM   5592  C  CD    . PRO A 1 2155 ? 187.757 196.938 147.828 1.00 27.44  ? 2155 PRO A CD    1 
ATOM   5593  N  N     . LEU A 1 2156 ? 188.189 194.210 145.465 1.00 29.81  ? 2156 LEU A N     1 
ATOM   5594  C  CA    . LEU A 1 2156 ? 188.332 192.887 144.867 1.00 29.97  ? 2156 LEU A CA    1 
ATOM   5595  C  C     . LEU A 1 2156 ? 187.419 192.722 143.658 1.00 31.30  ? 2156 LEU A C     1 
ATOM   5596  O  O     . LEU A 1 2156 ? 187.845 192.215 142.614 1.00 35.44  ? 2156 LEU A O     1 
ATOM   5597  C  CB    . LEU A 1 2156 ? 188.034 191.814 145.915 1.00 31.11  ? 2156 LEU A CB    1 
ATOM   5598  C  CG    . LEU A 1 2156 ? 189.221 191.101 146.564 1.00 37.93  ? 2156 LEU A CG    1 
ATOM   5599  C  CD1   . LEU A 1 2156 ? 189.772 190.028 145.646 1.00 41.89  ? 2156 LEU A CD1   1 
ATOM   5600  C  CD2   . LEU A 1 2156 ? 190.307 192.098 146.939 1.00 46.29  ? 2156 LEU A CD2   1 
ATOM   5601  N  N     . LEU A 1 2157 ? 186.160 193.149 143.778 1.00 32.51  ? 2157 LEU A N     1 
ATOM   5602  C  CA    . LEU A 1 2157 ? 185.227 193.016 142.664 1.00 33.27  ? 2157 LEU A CA    1 
ATOM   5603  C  C     . LEU A 1 2157 ? 185.536 194.017 141.559 1.00 26.57  ? 2157 LEU A C     1 
ATOM   5604  O  O     . LEU A 1 2157 ? 185.480 193.675 140.372 1.00 27.99  ? 2157 LEU A O     1 
ATOM   5605  C  CB    . LEU A 1 2157 ? 183.790 193.182 143.159 1.00 34.04  ? 2157 LEU A CB    1 
ATOM   5606  C  CG    . LEU A 1 2157 ? 182.667 192.982 142.138 1.00 27.60  ? 2157 LEU A CG    1 
ATOM   5607  C  CD1   . LEU A 1 2157 ? 181.518 192.207 142.754 1.00 22.39  ? 2157 LEU A CD1   1 
ATOM   5608  C  CD2   . LEU A 1 2157 ? 182.172 194.320 141.613 1.00 28.08  ? 2157 LEU A CD2   1 
ATOM   5609  N  N     . PHE A 1 2158 ? 185.860 195.260 141.925 1.00 28.40  ? 2158 PHE A N     1 
ATOM   5610  C  CA    . PHE A 1 2158 ? 186.205 196.254 140.915 1.00 32.67  ? 2158 PHE A CA    1 
ATOM   5611  C  C     . PHE A 1 2158 ? 187.491 195.890 140.188 1.00 30.18  ? 2158 PHE A C     1 
ATOM   5612  O  O     . PHE A 1 2158 ? 187.678 196.279 139.030 1.00 30.75  ? 2158 PHE A O     1 
ATOM   5613  C  CB    . PHE A 1 2158 ? 186.318 197.639 141.552 1.00 29.13  ? 2158 PHE A CB    1 
ATOM   5614  C  CG    . PHE A 1 2158 ? 185.010 198.371 141.639 1.00 31.59  ? 2158 PHE A CG    1 
ATOM   5615  C  CD1   . PHE A 1 2158 ? 184.279 198.376 142.814 1.00 32.32  ? 2158 PHE A CD1   1 
ATOM   5616  C  CD2   . PHE A 1 2158 ? 184.509 199.050 140.541 1.00 30.40  ? 2158 PHE A CD2   1 
ATOM   5617  C  CE1   . PHE A 1 2158 ? 183.074 199.046 142.895 1.00 30.78  ? 2158 PHE A CE1   1 
ATOM   5618  C  CE2   . PHE A 1 2158 ? 183.305 199.724 140.616 1.00 29.17  ? 2158 PHE A CE2   1 
ATOM   5619  C  CZ    . PHE A 1 2158 ? 182.586 199.720 141.794 1.00 30.66  ? 2158 PHE A CZ    1 
ATOM   5620  N  N     . SER A 1 2159 ? 188.388 195.153 140.846 1.00 33.77  ? 2159 SER A N     1 
ATOM   5621  C  CA    . SER A 1 2159 ? 189.543 194.613 140.139 1.00 31.33  ? 2159 SER A CA    1 
ATOM   5622  C  C     . SER A 1 2159 ? 189.119 193.542 139.144 1.00 32.59  ? 2159 SER A C     1 
ATOM   5623  O  O     . SER A 1 2159 ? 189.532 193.575 137.980 1.00 35.41  ? 2159 SER A O     1 
ATOM   5624  C  CB    . SER A 1 2159 ? 190.558 194.052 141.133 1.00 36.17  ? 2159 SER A CB    1 
ATOM   5625  O  OG    . SER A 1 2159 ? 189.999 193.001 141.899 1.00 44.76  ? 2159 SER A OG    1 
ATOM   5626  N  N     . LEU A 1 2160 ? 188.280 192.597 139.579 1.00 32.25  ? 2160 LEU A N     1 
ATOM   5627  C  CA    . LEU A 1 2160 ? 187.785 191.560 138.678 1.00 30.15  ? 2160 LEU A CA    1 
ATOM   5628  C  C     . LEU A 1 2160 ? 187.024 192.161 137.504 1.00 33.16  ? 2160 LEU A C     1 
ATOM   5629  O  O     . LEU A 1 2160 ? 187.003 191.588 136.408 1.00 40.78  ? 2160 LEU A O     1 
ATOM   5630  C  CB    . LEU A 1 2160 ? 186.895 190.580 139.441 1.00 29.25  ? 2160 LEU A CB    1 
ATOM   5631  C  CG    . LEU A 1 2160 ? 187.573 189.695 140.485 1.00 36.70  ? 2160 LEU A CG    1 
ATOM   5632  C  CD1   . LEU A 1 2160 ? 186.546 189.116 141.443 1.00 34.95  ? 2160 LEU A CD1   1 
ATOM   5633  C  CD2   . LEU A 1 2160 ? 188.344 188.585 139.796 1.00 41.15  ? 2160 LEU A CD2   1 
ATOM   5634  N  N     . LEU A 1 2161 ? 186.384 193.312 137.717 1.00 31.41  ? 2161 LEU A N     1 
ATOM   5635  C  CA    . LEU A 1 2161 ? 185.703 193.991 136.621 1.00 29.15  ? 2161 LEU A CA    1 
ATOM   5636  C  C     . LEU A 1 2161 ? 186.697 194.458 135.566 1.00 32.24  ? 2161 LEU A C     1 
ATOM   5637  O  O     . LEU A 1 2161 ? 186.344 194.609 134.391 1.00 38.63  ? 2161 LEU A O     1 
ATOM   5638  C  CB    . LEU A 1 2161 ? 184.898 195.173 137.160 1.00 30.74  ? 2161 LEU A CB    1 
ATOM   5639  C  CG    . LEU A 1 2161 ? 183.599 194.837 137.892 1.00 30.37  ? 2161 LEU A CG    1 
ATOM   5640  C  CD1   . LEU A 1 2161 ? 182.985 196.092 138.492 1.00 31.22  ? 2161 LEU A CD1   1 
ATOM   5641  C  CD2   . LEU A 1 2161 ? 182.617 194.139 136.969 1.00 34.11  ? 2161 LEU A CD2   1 
ATOM   5642  N  N     . SER A 1 2162 ? 187.948 194.694 135.970 1.00 33.13  ? 2162 SER A N     1 
ATOM   5643  C  CA    . SER A 1 2162 ? 188.951 195.180 135.029 1.00 36.66  ? 2162 SER A CA    1 
ATOM   5644  C  C     . SER A 1 2162 ? 189.467 194.073 134.116 1.00 38.36  ? 2162 SER A C     1 
ATOM   5645  O  O     . SER A 1 2162 ? 189.746 194.331 132.940 1.00 40.96  ? 2162 SER A O     1 
ATOM   5646  C  CB    . SER A 1 2162 ? 190.108 195.830 135.789 1.00 39.54  ? 2162 SER A CB    1 
ATOM   5647  O  OG    . SER A 1 2162 ? 191.027 194.857 136.253 1.00 38.91  ? 2162 SER A OG    1 
ATOM   5648  N  N     . ASP A 1 2163 ? 189.608 192.845 134.624 1.00 37.10  ? 2163 ASP A N     1 
ATOM   5649  C  CA    . ASP A 1 2163 ? 190.074 191.760 133.764 1.00 39.80  ? 2163 ASP A CA    1 
ATOM   5650  C  C     . ASP A 1 2163 ? 188.986 191.310 132.797 1.00 39.52  ? 2163 ASP A C     1 
ATOM   5651  O  O     . ASP A 1 2163 ? 189.259 191.079 131.613 1.00 43.71  ? 2163 ASP A O     1 
ATOM   5652  C  CB    . ASP A 1 2163 ? 190.562 190.571 134.595 1.00 43.38  ? 2163 ASP A CB    1 
ATOM   5653  C  CG    . ASP A 1 2163 ? 191.330 190.990 135.829 1.00 54.68  ? 2163 ASP A CG    1 
ATOM   5654  O  OD1   . ASP A 1 2163 ? 190.742 191.658 136.696 1.00 51.32  ? 2163 ASP A OD1   1 
ATOM   5655  O  OD2   . ASP A 1 2163 ? 192.527 190.646 135.931 1.00 57.51  ? 2163 ASP A OD2   1 
ATOM   5656  N  N     . VAL A 1 2164 ? 187.752 191.181 133.276 1.00 34.49  ? 2164 VAL A N     1 
ATOM   5657  C  CA    . VAL A 1 2164 ? 186.681 190.668 132.432 1.00 32.72  ? 2164 VAL A CA    1 
ATOM   5658  C  C     . VAL A 1 2164 ? 186.100 191.751 131.525 1.00 34.79  ? 2164 VAL A C     1 
ATOM   5659  O  O     . VAL A 1 2164 ? 185.731 191.464 130.381 1.00 33.40  ? 2164 VAL A O     1 
ATOM   5660  C  CB    . VAL A 1 2164 ? 185.584 190.027 133.297 1.00 31.32  ? 2164 VAL A CB    1 
ATOM   5661  C  CG1   . VAL A 1 2164 ? 184.620 189.242 132.428 1.00 28.74  ? 2164 VAL A CG1   1 
ATOM   5662  C  CG2   . VAL A 1 2164 ? 186.201 189.131 134.357 1.00 35.59  ? 2164 VAL A CG2   1 
ATOM   5663  N  N     . PHE A 1 2165 ? 186.014 192.990 132.004 1.00 36.57  ? 2165 PHE A N     1 
ATOM   5664  C  CA    . PHE A 1 2165 ? 185.488 194.112 131.226 1.00 32.23  ? 2165 PHE A CA    1 
ATOM   5665  C  C     . PHE A 1 2165 ? 186.495 195.254 131.273 1.00 36.79  ? 2165 PHE A C     1 
ATOM   5666  O  O     . PHE A 1 2165 ? 186.283 196.255 131.970 1.00 41.13  ? 2165 PHE A O     1 
ATOM   5667  C  CB    . PHE A 1 2165 ? 184.123 194.566 131.748 1.00 31.14  ? 2165 PHE A CB    1 
ATOM   5668  C  CG    . PHE A 1 2165 ? 183.130 193.451 131.917 1.00 29.21  ? 2165 PHE A CG    1 
ATOM   5669  C  CD1   . PHE A 1 2165 ? 183.100 192.698 133.079 1.00 37.47  ? 2165 PHE A CD1   1 
ATOM   5670  C  CD2   . PHE A 1 2165 ? 182.218 193.165 130.915 1.00 28.07  ? 2165 PHE A CD2   1 
ATOM   5671  C  CE1   . PHE A 1 2165 ? 182.183 191.677 133.235 1.00 37.77  ? 2165 PHE A CE1   1 
ATOM   5672  C  CE2   . PHE A 1 2165 ? 181.299 192.145 131.066 1.00 30.20  ? 2165 PHE A CE2   1 
ATOM   5673  C  CZ    . PHE A 1 2165 ? 181.282 191.400 132.227 1.00 30.58  ? 2165 PHE A CZ    1 
ATOM   5674  N  N     . PRO A 1 2166 ? 187.608 195.135 130.549 1.00 41.47  ? 2166 PRO A N     1 
ATOM   5675  C  CA    . PRO A 1 2166 ? 188.602 196.214 130.557 1.00 41.60  ? 2166 PRO A CA    1 
ATOM   5676  C  C     . PRO A 1 2166 ? 188.138 197.410 129.740 1.00 43.35  ? 2166 PRO A C     1 
ATOM   5677  O  O     . PRO A 1 2166 ? 187.593 197.265 128.644 1.00 40.99  ? 2166 PRO A O     1 
ATOM   5678  C  CB    . PRO A 1 2166 ? 189.839 195.559 129.934 1.00 38.20  ? 2166 PRO A CB    1 
ATOM   5679  C  CG    . PRO A 1 2166 ? 189.287 194.495 129.053 1.00 36.64  ? 2166 PRO A CG    1 
ATOM   5680  C  CD    . PRO A 1 2166 ? 188.035 193.993 129.720 1.00 38.01  ? 2166 PRO A CD    1 
ATOM   5681  N  N     . GLY A 1 2167 ? 188.364 198.603 130.289 1.00 43.66  ? 2167 GLY A N     1 
ATOM   5682  C  CA    . GLY A 1 2167 ? 188.101 199.841 129.588 1.00 40.67  ? 2167 GLY A CA    1 
ATOM   5683  C  C     . GLY A 1 2167 ? 186.797 200.524 129.941 1.00 44.57  ? 2167 GLY A C     1 
ATOM   5684  O  O     . GLY A 1 2167 ? 186.600 201.680 129.545 1.00 51.45  ? 2167 GLY A O     1 
ATOM   5685  N  N     . VAL A 1 2168 ? 185.903 199.857 130.666 1.00 48.27  ? 2168 VAL A N     1 
ATOM   5686  C  CA    . VAL A 1 2168 ? 184.605 200.412 131.030 1.00 47.58  ? 2168 VAL A CA    1 
ATOM   5687  C  C     . VAL A 1 2168 ? 184.586 200.652 132.532 1.00 47.04  ? 2168 VAL A C     1 
ATOM   5688  O  O     . VAL A 1 2168 ? 184.979 199.777 133.315 1.00 40.00  ? 2168 VAL A O     1 
ATOM   5689  C  CB    . VAL A 1 2168 ? 183.452 199.490 130.598 1.00 42.55  ? 2168 VAL A CB    1 
ATOM   5690  C  CG1   . VAL A 1 2168 ? 183.126 199.719 129.134 1.00 41.42  ? 2168 VAL A CG1   1 
ATOM   5691  C  CG2   . VAL A 1 2168 ? 183.815 198.037 130.838 1.00 35.48  ? 2168 VAL A CG2   1 
ATOM   5692  N  N     . GLN A 1 2169 ? 184.133 201.837 132.932 1.00 49.57  ? 2169 GLN A N     1 
ATOM   5693  C  CA    . GLN A 1 2169 ? 184.132 202.255 134.324 1.00 50.30  ? 2169 GLN A CA    1 
ATOM   5694  C  C     . GLN A 1 2169 ? 182.704 202.484 134.800 1.00 53.03  ? 2169 GLN A C     1 
ATOM   5695  O  O     . GLN A 1 2169 ? 181.813 202.813 134.011 1.00 55.07  ? 2169 GLN A O     1 
ATOM   5696  C  CB    . GLN A 1 2169 ? 184.950 203.540 134.523 1.00 52.38  ? 2169 GLN A CB    1 
ATOM   5697  C  CG    . GLN A 1 2169 ? 185.918 203.868 133.392 1.00 52.06  ? 2169 GLN A CG    1 
ATOM   5698  C  CD    . GLN A 1 2169 ? 187.029 202.843 133.230 1.00 57.23  ? 2169 GLN A CD    1 
ATOM   5699  O  OE1   . GLN A 1 2169 ? 187.240 201.990 134.092 1.00 56.63  ? 2169 GLN A OE1   1 
ATOM   5700  N  NE2   . GLN A 1 2169 ? 187.744 202.925 132.114 1.00 52.89  ? 2169 GLN A NE2   1 
ATOM   5701  N  N     . TYR A 1 2170 ? 182.497 202.307 136.102 1.00 54.42  ? 2170 TYR A N     1 
ATOM   5702  C  CA    . TYR A 1 2170 ? 181.205 202.546 136.735 1.00 50.96  ? 2170 TYR A CA    1 
ATOM   5703  C  C     . TYR A 1 2170 ? 181.224 203.935 137.360 1.00 58.03  ? 2170 TYR A C     1 
ATOM   5704  O  O     . TYR A 1 2170 ? 181.997 204.196 138.288 1.00 61.48  ? 2170 TYR A O     1 
ATOM   5705  C  CB    . TYR A 1 2170 ? 180.904 201.487 137.792 1.00 45.51  ? 2170 TYR A CB    1 
ATOM   5706  C  CG    . TYR A 1 2170 ? 179.600 201.721 138.522 1.00 48.28  ? 2170 TYR A CG    1 
ATOM   5707  C  CD1   . TYR A 1 2170 ? 179.479 201.433 139.874 1.00 48.26  ? 2170 TYR A CD1   1 
ATOM   5708  C  CD2   . TYR A 1 2170 ? 178.484 202.213 137.855 1.00 46.95  ? 2170 TYR A CD2   1 
ATOM   5709  C  CE1   . TYR A 1 2170 ? 178.290 201.645 140.547 1.00 49.53  ? 2170 TYR A CE1   1 
ATOM   5710  C  CE2   . TYR A 1 2170 ? 177.291 202.424 138.519 1.00 47.00  ? 2170 TYR A CE2   1 
ATOM   5711  C  CZ    . TYR A 1 2170 ? 177.199 202.137 139.864 1.00 54.84  ? 2170 TYR A CZ    1 
ATOM   5712  O  OH    . TYR A 1 2170 ? 176.013 202.345 140.530 1.00 52.20  ? 2170 TYR A OH    1 
ATOM   5713  N  N     . HIS A 1 2171 ? 180.376 204.823 136.853 1.00 61.60  ? 2171 HIS A N     1 
ATOM   5714  C  CA    . HIS A 1 2171 ? 180.180 206.145 137.434 1.00 61.23  ? 2171 HIS A CA    1 
ATOM   5715  C  C     . HIS A 1 2171 ? 178.745 206.229 137.941 1.00 55.32  ? 2171 HIS A C     1 
ATOM   5716  O  O     . HIS A 1 2171 ? 177.814 206.435 137.156 1.00 56.68  ? 2171 HIS A O     1 
ATOM   5717  C  CB    . HIS A 1 2171 ? 180.479 207.242 136.415 1.00 67.22  ? 2171 HIS A CB    1 
ATOM   5718  C  CG    . HIS A 1 2171 ? 181.929 207.604 136.328 1.00 76.85  ? 2171 HIS A CG    1 
ATOM   5719  N  ND1   . HIS A 1 2171 ? 182.536 207.971 135.147 1.00 78.98  ? 2171 HIS A ND1   1 
ATOM   5720  C  CD2   . HIS A 1 2171 ? 182.893 207.652 137.278 1.00 73.33  ? 2171 HIS A CD2   1 
ATOM   5721  C  CE1   . HIS A 1 2171 ? 183.811 208.232 135.372 1.00 76.91  ? 2171 HIS A CE1   1 
ATOM   5722  N  NE2   . HIS A 1 2171 ? 184.054 208.046 136.657 1.00 75.63  ? 2171 HIS A NE2   1 
ATOM   5723  N  N     . ARG A 1 2172 ? 178.571 206.059 139.249 1.00 47.57  ? 2172 ARG A N     1 
ATOM   5724  C  CA    . ARG A 1 2172 ? 177.242 206.089 139.839 1.00 48.14  ? 2172 ARG A CA    1 
ATOM   5725  C  C     . ARG A 1 2172 ? 176.632 207.481 139.716 1.00 51.54  ? 2172 ARG A C     1 
ATOM   5726  O  O     . ARG A 1 2172 ? 177.331 208.499 139.740 1.00 50.26  ? 2172 ARG A O     1 
ATOM   5727  C  CB    . ARG A 1 2172 ? 177.301 205.654 141.306 1.00 47.12  ? 2172 ARG A CB    1 
ATOM   5728  C  CG    . ARG A 1 2172 ? 177.242 206.791 142.315 1.00 48.84  ? 2172 ARG A CG    1 
ATOM   5729  C  CD    . ARG A 1 2172 ? 176.850 206.295 143.697 1.00 43.07  ? 2172 ARG A CD    1 
ATOM   5730  N  NE    . ARG A 1 2172 ? 175.526 205.684 143.709 1.00 47.76  ? 2172 ARG A NE    1 
ATOM   5731  C  CZ    . ARG A 1 2172 ? 175.019 205.017 144.737 1.00 38.97  ? 2172 ARG A CZ    1 
ATOM   5732  N  NH1   . ARG A 1 2172 ? 175.700 204.855 145.860 1.00 26.40  ? 2172 ARG A NH1   1 
ATOM   5733  N  NH2   . ARG A 1 2172 ? 173.799 204.499 144.636 1.00 29.14  ? 2172 ARG A NH2   1 
ATOM   5734  N  N     . GLY A 1 2173 ? 175.312 207.516 139.553 1.00 46.78  ? 2173 GLY A N     1 
ATOM   5735  C  CA    . GLY A 1 2173 ? 174.627 208.785 139.417 1.00 44.93  ? 2173 GLY A CA    1 
ATOM   5736  C  C     . GLY A 1 2173 ? 174.634 209.578 140.709 1.00 46.51  ? 2173 GLY A C     1 
ATOM   5737  O  O     . GLY A 1 2173 ? 174.647 209.028 141.810 1.00 45.64  ? 2173 GLY A O     1 
ATOM   5738  N  N     . GLU A 1 2174 ? 174.628 210.900 140.565 1.00 48.04  ? 2174 GLU A N     1 
ATOM   5739  C  CA    . GLU A 1 2174 ? 174.596 211.816 141.703 1.00 46.96  ? 2174 GLU A CA    1 
ATOM   5740  C  C     . GLU A 1 2174 ? 173.141 212.221 141.909 1.00 51.00  ? 2174 GLU A C     1 
ATOM   5741  O  O     . GLU A 1 2174 ? 172.628 213.129 141.254 1.00 53.30  ? 2174 GLU A O     1 
ATOM   5742  C  CB    . GLU A 1 2174 ? 175.502 213.018 141.463 1.00 46.08  ? 2174 GLU A CB    1 
ATOM   5743  C  CG    . GLU A 1 2174 ? 176.100 213.611 142.730 1.00 56.98  ? 2174 GLU A CG    1 
ATOM   5744  C  CD    . GLU A 1 2174 ? 175.279 214.757 143.285 1.00 63.90  ? 2174 GLU A CD    1 
ATOM   5745  O  OE1   . GLU A 1 2174 ? 174.615 215.453 142.489 1.00 60.79  ? 2174 GLU A OE1   1 
ATOM   5746  O  OE2   . GLU A 1 2174 ? 175.298 214.964 144.517 1.00 58.97  ? 2174 GLU A OE2   1 
ATOM   5747  N  N     . MET A 1 2175 ? 172.471 211.534 142.835 1.00 42.09  ? 2175 MET A N     1 
ATOM   5748  C  CA    . MET A 1 2175 ? 171.048 211.747 143.094 1.00 39.66  ? 2175 MET A CA    1 
ATOM   5749  C  C     . MET A 1 2175 ? 170.893 213.020 143.919 1.00 37.06  ? 2175 MET A C     1 
ATOM   5750  O  O     . MET A 1 2175 ? 170.642 212.997 145.126 1.00 37.30  ? 2175 MET A O     1 
ATOM   5751  C  CB    . MET A 1 2175 ? 170.448 210.538 143.801 1.00 43.58  ? 2175 MET A CB    1 
ATOM   5752  C  CG    . MET A 1 2175 ? 170.962 209.203 143.287 1.00 42.74  ? 2175 MET A CG    1 
ATOM   5753  S  SD    . MET A 1 2175 ? 169.658 207.972 143.109 1.00 66.48  ? 2175 MET A SD    1 
ATOM   5754  C  CE    . MET A 1 2175 ? 168.579 208.789 141.937 1.00 31.39  ? 2175 MET A CE    1 
ATOM   5755  N  N     . THR A 1 2176 ? 171.034 214.159 143.235 1.00 39.56  ? 2176 THR A N     1 
ATOM   5756  C  CA    . THR A 1 2176 ? 171.045 215.447 143.922 1.00 40.54  ? 2176 THR A CA    1 
ATOM   5757  C  C     . THR A 1 2176 ? 169.724 215.709 144.636 1.00 34.97  ? 2176 THR A C     1 
ATOM   5758  O  O     . THR A 1 2176 ? 169.706 216.175 145.780 1.00 31.49  ? 2176 THR A O     1 
ATOM   5759  C  CB    . THR A 1 2176 ? 171.346 216.569 142.927 1.00 44.49  ? 2176 THR A CB    1 
ATOM   5760  O  OG1   . THR A 1 2176 ? 172.612 216.326 142.301 1.00 44.58  ? 2176 THR A OG1   1 
ATOM   5761  C  CG2   . THR A 1 2176 ? 171.391 217.914 143.636 1.00 45.93  ? 2176 THR A CG2   1 
ATOM   5762  N  N     . ALA A 1 2177 ? 168.604 215.408 143.974 1.00 33.63  ? 2177 ALA A N     1 
ATOM   5763  C  CA    . ALA A 1 2177 ? 167.298 215.676 144.570 1.00 30.22  ? 2177 ALA A CA    1 
ATOM   5764  C  C     . ALA A 1 2177 ? 167.089 214.863 145.841 1.00 30.47  ? 2177 ALA A C     1 
ATOM   5765  O  O     . ALA A 1 2177 ? 166.551 215.371 146.832 1.00 29.11  ? 2177 ALA A O     1 
ATOM   5766  C  CB    . ALA A 1 2177 ? 166.189 215.387 143.559 1.00 27.64  ? 2177 ALA A CB    1 
ATOM   5767  N  N     . LEU A 1 2178 ? 167.506 213.595 145.833 1.00 29.75  ? 2178 LEU A N     1 
ATOM   5768  C  CA    . LEU A 1 2178 ? 167.324 212.753 147.011 1.00 25.23  ? 2178 LEU A CA    1 
ATOM   5769  C  C     . LEU A 1 2178 ? 168.289 213.136 148.126 1.00 25.50  ? 2178 LEU A C     1 
ATOM   5770  O  O     . LEU A 1 2178 ? 167.930 213.083 149.307 1.00 28.72  ? 2178 LEU A O     1 
ATOM   5771  C  CB    . LEU A 1 2178 ? 167.490 211.282 146.633 1.00 23.35  ? 2178 LEU A CB    1 
ATOM   5772  C  CG    . LEU A 1 2178 ? 167.171 210.264 147.728 1.00 22.81  ? 2178 LEU A CG    1 
ATOM   5773  C  CD1   . LEU A 1 2178 ? 165.690 210.282 148.058 1.00 26.08  ? 2178 LEU A CD1   1 
ATOM   5774  C  CD2   . LEU A 1 2178 ? 167.602 208.877 147.296 1.00 22.87  ? 2178 LEU A CD2   1 
ATOM   5775  N  N     . ARG A 1 2179 ? 169.517 213.526 147.773 1.00 23.21  ? 2179 ARG A N     1 
ATOM   5776  C  CA    . ARG A 1 2179 ? 170.497 213.892 148.793 1.00 22.04  ? 2179 ARG A CA    1 
ATOM   5777  C  C     . ARG A 1 2179 ? 170.056 215.127 149.570 1.00 26.72  ? 2179 ARG A C     1 
ATOM   5778  O  O     . ARG A 1 2179 ? 170.263 215.206 150.787 1.00 30.46  ? 2179 ARG A O     1 
ATOM   5779  C  CB    . ARG A 1 2179 ? 171.866 214.119 148.153 1.00 26.76  ? 2179 ARG A CB    1 
ATOM   5780  C  CG    . ARG A 1 2179 ? 172.502 212.863 147.580 1.00 28.38  ? 2179 ARG A CG    1 
ATOM   5781  C  CD    . ARG A 1 2179 ? 173.875 213.155 146.999 1.00 30.56  ? 2179 ARG A CD    1 
ATOM   5782  N  NE    . ARG A 1 2179 ? 174.912 213.191 148.023 1.00 36.46  ? 2179 ARG A NE    1 
ATOM   5783  C  CZ    . ARG A 1 2179 ? 175.739 212.186 148.275 1.00 40.92  ? 2179 ARG A CZ    1 
ATOM   5784  N  NH1   . ARG A 1 2179 ? 175.707 211.072 147.565 1.00 34.87  ? 2179 ARG A NH1   1 
ATOM   5785  N  NH2   . ARG A 1 2179 ? 176.623 212.304 149.261 1.00 41.59  ? 2179 ARG A NH2   1 
ATOM   5786  N  N     . GLU A 1 2180 ? 169.457 216.107 148.886 1.00 28.27  ? 2180 GLU A N     1 
ATOM   5787  C  CA    . GLU A 1 2180 ? 168.949 217.286 149.583 1.00 28.11  ? 2180 GLU A CA    1 
ATOM   5788  C  C     . GLU A 1 2180 ? 167.839 216.913 150.556 1.00 27.64  ? 2180 GLU A C     1 
ATOM   5789  O  O     . GLU A 1 2180 ? 167.780 217.438 151.675 1.00 29.87  ? 2180 GLU A O     1 
ATOM   5790  C  CB    . GLU A 1 2180 ? 168.453 218.326 148.577 1.00 31.91  ? 2180 GLU A CB    1 
ATOM   5791  C  CG    . GLU A 1 2180 ? 169.491 218.755 147.553 1.00 42.94  ? 2180 GLU A CG    1 
ATOM   5792  C  CD    . GLU A 1 2180 ? 170.334 219.922 148.030 1.00 51.93  ? 2180 GLU A CD    1 
ATOM   5793  O  OE1   . GLU A 1 2180 ? 169.762 221.002 148.290 1.00 49.44  ? 2180 GLU A OE1   1 
ATOM   5794  O  OE2   . GLU A 1 2180 ? 171.567 219.761 148.144 1.00 55.21  ? 2180 GLU A OE2   1 
ATOM   5795  N  N     . GLU A 1 2181 ? 166.947 216.010 150.145 1.00 25.70  ? 2181 GLU A N     1 
ATOM   5796  C  CA    . GLU A 1 2181 ? 165.906 215.532 151.049 1.00 25.10  ? 2181 GLU A CA    1 
ATOM   5797  C  C     . GLU A 1 2181 ? 166.508 214.795 152.239 1.00 24.88  ? 2181 GLU A C     1 
ATOM   5798  O  O     . GLU A 1 2181 ? 166.051 214.955 153.377 1.00 27.50  ? 2181 GLU A O     1 
ATOM   5799  C  CB    . GLU A 1 2181 ? 164.930 214.630 150.291 1.00 24.97  ? 2181 GLU A CB    1 
ATOM   5800  C  CG    . GLU A 1 2181 ? 163.922 215.357 149.392 1.00 25.25  ? 2181 GLU A CG    1 
ATOM   5801  C  CD    . GLU A 1 2181 ? 163.073 216.405 150.107 1.00 37.84  ? 2181 GLU A CD    1 
ATOM   5802  O  OE1   . GLU A 1 2181 ? 162.337 217.131 149.406 1.00 46.61  ? 2181 GLU A OE1   1 
ATOM   5803  O  OE2   . GLU A 1 2181 ? 163.096 216.488 151.354 1.00 39.24  ? 2181 GLU A OE2   1 
ATOM   5804  N  N     . LEU A 1 2182 ? 167.537 213.979 151.993 1.00 19.49  ? 2182 LEU A N     1 
ATOM   5805  C  CA    . LEU A 1 2182 ? 168.201 213.268 153.080 1.00 17.95  ? 2182 LEU A CA    1 
ATOM   5806  C  C     . LEU A 1 2182 ? 168.844 214.239 154.061 1.00 22.03  ? 2182 LEU A C     1 
ATOM   5807  O  O     . LEU A 1 2182 ? 168.780 214.035 155.279 1.00 23.92  ? 2182 LEU A O     1 
ATOM   5808  C  CB    . LEU A 1 2182 ? 169.252 212.312 152.517 1.00 17.66  ? 2182 LEU A CB    1 
ATOM   5809  C  CG    . LEU A 1 2182 ? 168.762 211.116 151.701 1.00 18.81  ? 2182 LEU A CG    1 
ATOM   5810  C  CD1   . LEU A 1 2182 ? 169.939 210.372 151.095 1.00 16.68  ? 2182 LEU A CD1   1 
ATOM   5811  C  CD2   . LEU A 1 2182 ? 167.920 210.181 152.549 1.00 14.05  ? 2182 LEU A CD2   1 
ATOM   5812  N  N     . LYS A 1 2183 ? 169.476 215.298 153.548 1.00 25.38  ? 2183 LYS A N     1 
ATOM   5813  C  CA    . LYS A 1 2183 ? 170.130 216.267 154.421 1.00 22.85  ? 2183 LYS A CA    1 
ATOM   5814  C  C     . LYS A 1 2183 ? 169.124 216.965 155.327 1.00 23.24  ? 2183 LYS A C     1 
ATOM   5815  O  O     . LYS A 1 2183 ? 169.379 217.151 156.523 1.00 24.89  ? 2183 LYS A O     1 
ATOM   5816  C  CB    . LYS A 1 2183 ? 170.897 217.290 153.582 1.00 24.56  ? 2183 LYS A CB    1 
ATOM   5817  C  CG    . LYS A 1 2183 ? 172.146 217.836 154.251 1.00 36.04  ? 2183 LYS A CG    1 
ATOM   5818  C  CD    . LYS A 1 2183 ? 172.384 219.290 153.882 1.00 40.78  ? 2183 LYS A CD    1 
ATOM   5819  C  CE    . LYS A 1 2183 ? 173.517 219.885 154.701 1.00 46.56  ? 2183 LYS A CE    1 
ATOM   5820  N  NZ    . LYS A 1 2183 ? 174.825 219.766 154.000 1.00 47.71  ? 2183 LYS A NZ    1 
ATOM   5821  N  N     . LYS A 1 2184 ? 167.974 217.360 154.776 1.00 24.57  ? 2184 LYS A N     1 
ATOM   5822  C  CA    . LYS A 1 2184 ? 166.953 218.017 155.586 1.00 22.96  ? 2184 LYS A CA    1 
ATOM   5823  C  C     . LYS A 1 2184 ? 166.388 217.073 156.639 1.00 23.98  ? 2184 LYS A C     1 
ATOM   5824  O  O     . LYS A 1 2184 ? 166.175 217.471 157.790 1.00 27.10  ? 2184 LYS A O     1 
ATOM   5825  C  CB    . LYS A 1 2184 ? 165.837 218.552 154.690 1.00 29.59  ? 2184 LYS A CB    1 
ATOM   5826  C  CG    . LYS A 1 2184 ? 166.107 219.935 154.123 1.00 33.62  ? 2184 LYS A CG    1 
ATOM   5827  C  CD    . LYS A 1 2184 ? 164.868 220.513 153.460 1.00 35.15  ? 2184 LYS A CD    1 
ATOM   5828  C  CE    . LYS A 1 2184 ? 164.796 220.122 151.995 1.00 41.74  ? 2184 LYS A CE    1 
ATOM   5829  N  NZ    . LYS A 1 2184 ? 164.000 218.882 151.798 1.00 42.36  ? 2184 LYS A NZ    1 
ATOM   5830  N  N     . VAL A 1 2185 ? 166.131 215.818 156.263 1.00 21.74  ? 2185 VAL A N     1 
ATOM   5831  C  CA    . VAL A 1 2185 ? 165.591 214.850 157.214 1.00 19.84  ? 2185 VAL A CA    1 
ATOM   5832  C  C     . VAL A 1 2185 ? 166.601 214.567 158.318 1.00 21.59  ? 2185 VAL A C     1 
ATOM   5833  O  O     . VAL A 1 2185 ? 166.249 214.507 159.503 1.00 21.68  ? 2185 VAL A O     1 
ATOM   5834  C  CB    . VAL A 1 2185 ? 165.168 213.562 156.483 1.00 23.12  ? 2185 VAL A CB    1 
ATOM   5835  C  CG1   . VAL A 1 2185 ? 164.958 212.427 157.473 1.00 22.87  ? 2185 VAL A CG1   1 
ATOM   5836  C  CG2   . VAL A 1 2185 ? 163.907 213.804 155.668 1.00 25.07  ? 2185 VAL A CG2   1 
ATOM   5837  N  N     . CYS A 1 2186 ? 167.873 214.394 157.951 1.00 21.94  ? 2186 CYS A N     1 
ATOM   5838  C  CA    . CYS A 1 2186 ? 168.903 214.121 158.948 1.00 16.88  ? 2186 CYS A CA    1 
ATOM   5839  C  C     . CYS A 1 2186 ? 169.067 215.291 159.909 1.00 17.05  ? 2186 CYS A C     1 
ATOM   5840  O  O     . CYS A 1 2186 ? 169.309 215.092 161.105 1.00 18.06  ? 2186 CYS A O     1 
ATOM   5841  C  CB    . CYS A 1 2186 ? 170.231 213.802 158.262 1.00 15.95  ? 2186 CYS A CB    1 
ATOM   5842  S  SG    . CYS A 1 2186 ? 170.303 212.168 157.498 1.00 18.89  ? 2186 CYS A SG    1 
ATOM   5843  N  N     . GLN A 1 2187 ? 168.951 216.521 159.403 1.00 19.65  ? 2187 GLN A N     1 
ATOM   5844  C  CA    . GLN A 1 2187 ? 169.061 217.690 160.271 1.00 21.07  ? 2187 GLN A CA    1 
ATOM   5845  C  C     . GLN A 1 2187 ? 167.937 217.719 161.299 1.00 22.94  ? 2187 GLN A C     1 
ATOM   5846  O  O     . GLN A 1 2187 ? 168.172 218.008 162.479 1.00 27.40  ? 2187 GLN A O     1 
ATOM   5847  C  CB    . GLN A 1 2187 ? 169.059 218.968 159.431 1.00 22.18  ? 2187 GLN A CB    1 
ATOM   5848  C  CG    . GLN A 1 2187 ? 168.732 220.229 160.214 1.00 27.47  ? 2187 GLN A CG    1 
ATOM   5849  C  CD    . GLN A 1 2187 ? 169.852 220.644 161.148 1.00 36.39  ? 2187 GLN A CD    1 
ATOM   5850  O  OE1   . GLN A 1 2187 ? 171.024 220.369 160.892 1.00 34.74  ? 2187 GLN A OE1   1 
ATOM   5851  N  NE2   . GLN A 1 2187 ? 169.495 221.310 162.241 1.00 34.67  ? 2187 GLN A NE2   1 
ATOM   5852  N  N     . GLU A 1 2188 ? 166.710 217.413 160.875 1.00 21.83  ? 2188 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2188 ? 165.583 217.382 161.798 1.00 22.57  ? 2188 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2188 ? 165.596 216.154 162.700 1.00 21.48  ? 2188 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2188 ? 164.935 216.162 163.743 1.00 23.65  ? 2188 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2188 ? 164.265 217.443 161.021 1.00 22.79  ? 2188 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2188 ? 163.613 216.091 160.781 1.00 27.30  ? 2188 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2188 ? 162.559 216.136 159.693 1.00 38.97  ? 2188 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2188 ? 161.814 215.144 159.543 1.00 42.87  ? 2188 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2188 ? 162.474 217.164 158.988 1.00 38.41  ? 2188 GLU A OE2   1 
ATOM   5861  N  N     . MET A 1 2189 ? 166.333 215.110 162.327 1.00 21.30  ? 2189 MET A N     1 
ATOM   5862  C  CA    . MET A 1 2189 ? 166.417 213.887 163.111 1.00 16.89  ? 2189 MET A CA    1 
ATOM   5863  C  C     . MET A 1 2189 ? 167.722 213.782 163.890 1.00 16.11  ? 2189 MET A C     1 
ATOM   5864  O  O     . MET A 1 2189 ? 168.034 212.708 164.413 1.00 16.63  ? 2189 MET A O     1 
ATOM   5865  C  CB    . MET A 1 2189 ? 166.246 212.667 162.203 1.00 19.20  ? 2189 MET A CB    1 
ATOM   5866  C  CG    . MET A 1 2189 ? 164.846 212.073 162.226 1.00 21.98  ? 2189 MET A CG    1 
ATOM   5867  S  SD    . MET A 1 2189 ? 164.734 210.493 161.366 1.00 43.94  ? 2189 MET A SD    1 
ATOM   5868  C  CE    . MET A 1 2189 ? 164.737 209.354 162.747 1.00 34.12  ? 2189 MET A CE    1 
ATOM   5869  N  N     . TYR A 1 2190 ? 168.491 214.871 163.966 1.00 14.28  ? 2190 TYR A N     1 
ATOM   5870  C  CA    . TYR A 1 2190 ? 169.734 214.930 164.736 1.00 11.92  ? 2190 TYR A CA    1 
ATOM   5871  C  C     . TYR A 1 2190 ? 170.758 213.909 164.248 1.00 15.45  ? 2190 TYR A C     1 
ATOM   5872  O  O     . TYR A 1 2190 ? 171.523 213.353 165.040 1.00 12.89  ? 2190 TYR A O     1 
ATOM   5873  C  CB    . TYR A 1 2190 ? 169.468 214.746 166.233 1.00 16.84  ? 2190 TYR A CB    1 
ATOM   5874  C  CG    . TYR A 1 2190 ? 168.373 215.639 166.769 1.00 19.04  ? 2190 TYR A CG    1 
ATOM   5875  C  CD1   . TYR A 1 2190 ? 168.484 217.020 166.706 1.00 20.57  ? 2190 TYR A CD1   1 
ATOM   5876  C  CD2   . TYR A 1 2190 ? 167.225 215.099 167.332 1.00 18.06  ? 2190 TYR A CD2   1 
ATOM   5877  C  CE1   . TYR A 1 2190 ? 167.485 217.838 167.191 1.00 23.12  ? 2190 TYR A CE1   1 
ATOM   5878  C  CE2   . TYR A 1 2190 ? 166.221 215.911 167.820 1.00 23.63  ? 2190 TYR A CE2   1 
ATOM   5879  C  CZ    . TYR A 1 2190 ? 166.356 217.279 167.747 1.00 25.34  ? 2190 TYR A CZ    1 
ATOM   5880  O  OH    . TYR A 1 2190 ? 165.358 218.091 168.233 1.00 27.14  ? 2190 TYR A OH    1 
ATOM   5881  N  N     . LEU A 1 2191 ? 170.784 213.656 162.943 1.00 19.01  ? 2191 LEU A N     1 
ATOM   5882  C  CA    . LEU A 1 2191 ? 171.704 212.700 162.348 1.00 11.55  ? 2191 LEU A CA    1 
ATOM   5883  C  C     . LEU A 1 2191 ? 172.730 213.415 161.479 1.00 11.43  ? 2191 LEU A C     1 
ATOM   5884  O  O     . LEU A 1 2191 ? 172.426 214.406 160.811 1.00 14.79  ? 2191 LEU A O     1 
ATOM   5885  C  CB    . LEU A 1 2191 ? 170.949 211.661 161.516 1.00 12.06  ? 2191 LEU A CB    1 
ATOM   5886  C  CG    . LEU A 1 2191 ? 169.976 210.749 162.266 1.00 11.12  ? 2191 LEU A CG    1 
ATOM   5887  C  CD1   . LEU A 1 2191 ? 169.702 209.494 161.460 1.00 11.47  ? 2191 LEU A CD1   1 
ATOM   5888  C  CD2   . LEU A 1 2191 ? 170.519 210.391 163.641 1.00 10.21  ? 2191 LEU A CD2   1 
ATOM   5889  N  N     . THR A 1 2192 ? 173.955 212.897 161.497 1.00 15.45  ? 2192 THR A N     1 
ATOM   5890  C  CA    . THR A 1 2192 ? 175.051 213.502 160.755 1.00 13.55  ? 2192 THR A CA    1 
ATOM   5891  C  C     . THR A 1 2192 ? 174.977 213.100 159.288 1.00 16.74  ? 2192 THR A C     1 
ATOM   5892  O  O     . THR A 1 2192 ? 174.780 211.924 158.965 1.00 17.81  ? 2192 THR A O     1 
ATOM   5893  C  CB    . THR A 1 2192 ? 176.395 213.082 161.352 1.00 15.04  ? 2192 THR A CB    1 
ATOM   5894  O  OG1   . THR A 1 2192 ? 176.461 213.500 162.721 1.00 21.83  ? 2192 THR A OG1   1 
ATOM   5895  C  CG2   . THR A 1 2192 ? 177.543 213.717 160.584 1.00 13.15  ? 2192 THR A CG2   1 
ATOM   5896  N  N     . TYR A 1 2193 ? 175.134 214.079 158.403 1.00 16.75  ? 2193 TYR A N     1 
ATOM   5897  C  CA    . TYR A 1 2193 ? 175.106 213.863 156.965 1.00 16.72  ? 2193 TYR A CA    1 
ATOM   5898  C  C     . TYR A 1 2193 ? 176.437 214.293 156.364 1.00 22.96  ? 2193 TYR A C     1 
ATOM   5899  O  O     . TYR A 1 2193 ? 176.998 215.324 156.747 1.00 25.18  ? 2193 TYR A O     1 
ATOM   5900  C  CB    . TYR A 1 2193 ? 173.940 214.633 156.327 1.00 21.60  ? 2193 TYR A CB    1 
ATOM   5901  C  CG    . TYR A 1 2193 ? 173.916 214.652 154.810 1.00 26.72  ? 2193 TYR A CG    1 
ATOM   5902  C  CD1   . TYR A 1 2193 ? 174.750 215.495 154.084 1.00 29.16  ? 2193 TYR A CD1   1 
ATOM   5903  C  CD2   . TYR A 1 2193 ? 173.057 213.821 154.105 1.00 28.99  ? 2193 TYR A CD2   1 
ATOM   5904  C  CE1   . TYR A 1 2193 ? 174.727 215.510 152.708 1.00 28.88  ? 2193 TYR A CE1   1 
ATOM   5905  C  CE2   . TYR A 1 2193 ? 173.030 213.829 152.725 1.00 29.92  ? 2193 TYR A CE2   1 
ATOM   5906  C  CZ    . TYR A 1 2193 ? 173.867 214.675 152.033 1.00 31.98  ? 2193 TYR A CZ    1 
ATOM   5907  O  OH    . TYR A 1 2193 ? 173.843 214.687 150.658 1.00 43.01  ? 2193 TYR A OH    1 
ATOM   5908  N  N     . GLY A 1 2194 ? 176.935 213.499 155.427 1.00 23.44  ? 2194 GLY A N     1 
ATOM   5909  C  CA    . GLY A 1 2194 ? 178.179 213.818 154.747 1.00 24.57  ? 2194 GLY A CA    1 
ATOM   5910  C  C     . GLY A 1 2194 ? 178.128 213.371 153.305 1.00 30.42  ? 2194 GLY A C     1 
ATOM   5911  O  O     . GLY A 1 2194 ? 177.336 212.499 152.933 1.00 30.02  ? 2194 GLY A O     1 
ATOM   5912  N  N     . ASP A 1 2195 ? 178.984 213.974 152.485 1.00 35.38  ? 2195 ASP A N     1 
ATOM   5913  C  CA    . ASP A 1 2195 ? 179.066 213.672 151.061 1.00 30.94  ? 2195 ASP A CA    1 
ATOM   5914  C  C     . ASP A 1 2195 ? 180.445 213.110 150.744 1.00 33.64  ? 2195 ASP A C     1 
ATOM   5915  O  O     . ASP A 1 2195 ? 181.437 213.846 150.758 1.00 37.81  ? 2195 ASP A O     1 
ATOM   5916  C  CB    . ASP A 1 2195 ? 178.787 214.917 150.220 1.00 31.38  ? 2195 ASP A CB    1 
ATOM   5917  C  CG    . ASP A 1 2195 ? 177.309 215.228 150.113 1.00 41.39  ? 2195 ASP A CG    1 
ATOM   5918  O  OD1   . ASP A 1 2195 ? 176.492 214.347 150.451 1.00 41.63  ? 2195 ASP A OD1   1 
ATOM   5919  O  OD2   . ASP A 1 2195 ? 176.962 216.351 149.689 1.00 47.87  ? 2195 ASP A OD2   1 
ATOM   5920  N  N     . GLY A 1 2196 ? 180.502 211.816 150.446 1.00 30.16  ? 2196 GLY A N     1 
ATOM   5921  C  CA    . GLY A 1 2196 ? 181.753 211.183 150.082 1.00 30.39  ? 2196 GLY A CA    1 
ATOM   5922  C  C     . GLY A 1 2196 ? 182.632 210.837 151.266 1.00 33.08  ? 2196 GLY A C     1 
ATOM   5923  O  O     . GLY A 1 2196 ? 182.321 209.921 152.032 1.00 34.63  ? 2196 GLY A O     1 
ATOM   5924  N  N     . GLU A 1 2197 ? 183.736 211.563 151.425 1.00 36.75  ? 2197 GLU A N     1 
ATOM   5925  C  CA    . GLU A 1 2197 ? 184.704 211.286 152.477 1.00 35.32  ? 2197 GLU A CA    1 
ATOM   5926  C  C     . GLU A 1 2197 ? 184.456 212.083 153.751 1.00 31.70  ? 2197 GLU A C     1 
ATOM   5927  O  O     . GLU A 1 2197 ? 185.221 211.937 154.710 1.00 32.53  ? 2197 GLU A O     1 
ATOM   5928  C  CB    . GLU A 1 2197 ? 186.124 211.557 151.971 1.00 41.05  ? 2197 GLU A CB    1 
ATOM   5929  C  CG    . GLU A 1 2197 ? 186.780 210.353 151.320 1.00 45.30  ? 2197 GLU A CG    1 
ATOM   5930  C  CD    . GLU A 1 2197 ? 186.563 209.078 152.111 1.00 47.63  ? 2197 GLU A CD    1 
ATOM   5931  O  OE1   . GLU A 1 2197 ? 187.174 208.935 153.191 1.00 45.25  ? 2197 GLU A OE1   1 
ATOM   5932  O  OE2   . GLU A 1 2197 ? 185.780 208.219 151.654 1.00 47.10  ? 2197 GLU A OE2   1 
ATOM   5933  N  N     . GLU A 1 2198 ? 183.420 212.916 153.790 1.00 32.14  ? 2198 GLU A N     1 
ATOM   5934  C  CA    . GLU A 1 2198 ? 183.095 213.619 155.019 1.00 30.18  ? 2198 GLU A CA    1 
ATOM   5935  C  C     . GLU A 1 2198 ? 182.488 212.655 156.035 1.00 27.10  ? 2198 GLU A C     1 
ATOM   5936  O  O     . GLU A 1 2198 ? 182.114 211.522 155.718 1.00 29.28  ? 2198 GLU A O     1 
ATOM   5937  C  CB    . GLU A 1 2198 ? 182.134 214.776 154.748 1.00 29.15  ? 2198 GLU A CB    1 
ATOM   5938  C  CG    . GLU A 1 2198 ? 182.254 215.383 153.366 1.00 34.36  ? 2198 GLU A CG    1 
ATOM   5939  C  CD    . GLU A 1 2198 ? 181.255 216.499 153.139 1.00 39.18  ? 2198 GLU A CD    1 
ATOM   5940  O  OE1   . GLU A 1 2198 ? 180.316 216.630 153.952 1.00 32.40  ? 2198 GLU A OE1   1 
ATOM   5941  O  OE2   . GLU A 1 2198 ? 181.406 217.245 152.149 1.00 43.84  ? 2198 GLU A OE2   1 
ATOM   5942  N  N     . VAL A 1 2199 ? 182.398 213.122 157.277 1.00 23.11  ? 2199 VAL A N     1 
ATOM   5943  C  CA    . VAL A 1 2199 ? 181.867 212.316 158.369 1.00 21.10  ? 2199 VAL A CA    1 
ATOM   5944  C  C     . VAL A 1 2199 ? 180.402 212.009 158.088 1.00 21.27  ? 2199 VAL A C     1 
ATOM   5945  O  O     . VAL A 1 2199 ? 179.555 212.909 158.081 1.00 25.75  ? 2199 VAL A O     1 
ATOM   5946  C  CB    . VAL A 1 2199 ? 182.042 213.034 159.720 1.00 15.56  ? 2199 VAL A CB    1 
ATOM   5947  C  CG1   . VAL A 1 2199 ? 181.626 212.128 160.861 1.00 15.35  ? 2199 VAL A CG1   1 
ATOM   5948  C  CG2   . VAL A 1 2199 ? 183.482 213.492 159.892 1.00 18.89  ? 2199 VAL A CG2   1 
ATOM   5949  N  N     . GLY A 1 2200 ? 180.096 210.734 157.851 1.00 15.90  ? 2200 GLY A N     1 
ATOM   5950  C  CA    . GLY A 1 2200 ? 178.761 210.313 157.487 1.00 16.14  ? 2200 GLY A CA    1 
ATOM   5951  C  C     . GLY A 1 2200 ? 178.553 210.022 156.017 1.00 21.69  ? 2200 GLY A C     1 
ATOM   5952  O  O     . GLY A 1 2200 ? 177.437 209.655 155.630 1.00 18.54  ? 2200 GLY A O     1 
ATOM   5953  N  N     . GLY A 1 2201 ? 179.587 210.173 155.187 1.00 22.79  ? 2201 GLY A N     1 
ATOM   5954  C  CA    . GLY A 1 2201 ? 179.428 209.905 153.767 1.00 16.32  ? 2201 GLY A CA    1 
ATOM   5955  C  C     . GLY A 1 2201 ? 179.154 208.443 153.471 1.00 15.45  ? 2201 GLY A C     1 
ATOM   5956  O  O     . GLY A 1 2201 ? 178.360 208.119 152.583 1.00 17.59  ? 2201 GLY A O     1 
ATOM   5957  N  N     . MET A 1 2202 ? 179.814 207.541 154.201 1.00 14.97  ? 2202 MET A N     1 
ATOM   5958  C  CA    . MET A 1 2202 ? 179.575 206.114 154.007 1.00 11.05  ? 2202 MET A CA    1 
ATOM   5959  C  C     . MET A 1 2202 ? 178.142 205.740 154.364 1.00 10.40  ? 2202 MET A C     1 
ATOM   5960  O  O     . MET A 1 2202 ? 177.518 204.922 153.678 1.00 12.77  ? 2202 MET A O     1 
ATOM   5961  C  CB    . MET A 1 2202 ? 180.567 205.299 154.837 1.00 11.81  ? 2202 MET A CB    1 
ATOM   5962  C  CG    . MET A 1 2202 ? 182.003 205.786 154.737 1.00 15.99  ? 2202 MET A CG    1 
ATOM   5963  S  SD    . MET A 1 2202 ? 183.185 204.694 155.550 1.00 57.29  ? 2202 MET A SD    1 
ATOM   5964  C  CE    . MET A 1 2202 ? 182.269 203.155 155.587 1.00 17.75  ? 2202 MET A CE    1 
ATOM   5965  N  N     . TRP A 1 2203 ? 177.608 206.319 155.442 1.00 10.34  ? 2203 TRP A N     1 
ATOM   5966  C  CA    . TRP A 1 2203 ? 176.224 206.051 155.817 1.00 7.04   ? 2203 TRP A CA    1 
ATOM   5967  C  C     . TRP A 1 2203 ? 175.256 206.567 154.761 1.00 9.00   ? 2203 TRP A C     1 
ATOM   5968  O  O     . TRP A 1 2203 ? 174.269 205.899 154.433 1.00 9.46   ? 2203 TRP A O     1 
ATOM   5969  C  CB    . TRP A 1 2203 ? 175.914 206.677 157.175 1.00 8.30   ? 2203 TRP A CB    1 
ATOM   5970  C  CG    . TRP A 1 2203 ? 174.547 206.341 157.672 1.00 6.73   ? 2203 TRP A CG    1 
ATOM   5971  C  CD1   . TRP A 1 2203 ? 174.132 205.149 158.187 1.00 3.78   ? 2203 TRP A CD1   1 
ATOM   5972  C  CD2   . TRP A 1 2203 ? 173.404 207.200 157.675 1.00 5.00   ? 2203 TRP A CD2   1 
ATOM   5973  N  NE1   . TRP A 1 2203 ? 172.803 205.217 158.526 1.00 3.33   ? 2203 TRP A NE1   1 
ATOM   5974  C  CE2   . TRP A 1 2203 ? 172.333 206.466 158.219 1.00 3.42   ? 2203 TRP A CE2   1 
ATOM   5975  C  CE3   . TRP A 1 2203 ? 173.184 208.521 157.276 1.00 5.50   ? 2203 TRP A CE3   1 
ATOM   5976  C  CZ2   . TRP A 1 2203 ? 171.062 207.009 158.375 1.00 5.34   ? 2203 TRP A CZ2   1 
ATOM   5977  C  CZ3   . TRP A 1 2203 ? 171.923 209.057 157.431 1.00 8.66   ? 2203 TRP A CZ3   1 
ATOM   5978  C  CH2   . TRP A 1 2203 ? 170.877 208.302 157.975 1.00 7.78   ? 2203 TRP A CH2   1 
ATOM   5979  N  N     . VAL A 1 2204 ? 175.520 207.760 154.225 1.00 10.16  ? 2204 VAL A N     1 
ATOM   5980  C  CA    . VAL A 1 2204 ? 174.671 208.307 153.172 1.00 8.84   ? 2204 VAL A CA    1 
ATOM   5981  C  C     . VAL A 1 2204 ? 174.730 207.424 151.933 1.00 8.60   ? 2204 VAL A C     1 
ATOM   5982  O  O     . VAL A 1 2204 ? 173.709 207.180 151.279 1.00 11.46  ? 2204 VAL A O     1 
ATOM   5983  C  CB    . VAL A 1 2204 ? 175.076 209.759 152.863 1.00 13.88  ? 2204 VAL A CB    1 
ATOM   5984  C  CG1   . VAL A 1 2204 ? 174.394 210.249 151.595 1.00 20.74  ? 2204 VAL A CG1   1 
ATOM   5985  C  CG2   . VAL A 1 2204 ? 174.735 210.661 154.034 1.00 14.72  ? 2204 VAL A CG2   1 
ATOM   5986  N  N     . GLU A 1 2205 ? 175.920 206.922 151.598 1.00 8.49   ? 2205 GLU A N     1 
ATOM   5987  C  CA    . GLU A 1 2205 ? 176.049 206.018 150.460 1.00 9.51   ? 2205 GLU A CA    1 
ATOM   5988  C  C     . GLU A 1 2205 ? 175.251 204.740 150.681 1.00 7.94   ? 2205 GLU A C     1 
ATOM   5989  O  O     . GLU A 1 2205 ? 174.628 204.220 149.749 1.00 11.57  ? 2205 GLU A O     1 
ATOM   5990  C  CB    . GLU A 1 2205 ? 177.523 205.696 150.211 1.00 11.32  ? 2205 GLU A CB    1 
ATOM   5991  C  CG    . GLU A 1 2205 ? 178.286 206.781 149.466 1.00 16.79  ? 2205 GLU A CG    1 
ATOM   5992  C  CD    . GLU A 1 2205 ? 177.981 206.800 147.981 1.00 29.97  ? 2205 GLU A CD    1 
ATOM   5993  O  OE1   . GLU A 1 2205 ? 178.823 206.315 147.196 1.00 34.80  ? 2205 GLU A OE1   1 
ATOM   5994  O  OE2   . GLU A 1 2205 ? 176.904 207.304 147.596 1.00 23.44  ? 2205 GLU A OE2   1 
ATOM   5995  N  N     . LYS A 1 2206 ? 175.257 204.219 151.911 1.00 7.40   ? 2206 LYS A N     1 
ATOM   5996  C  CA    . LYS A 1 2206 ? 174.476 203.023 152.214 1.00 6.01   ? 2206 LYS A CA    1 
ATOM   5997  C  C     . LYS A 1 2206 ? 172.985 203.283 152.041 1.00 6.51   ? 2206 LYS A C     1 
ATOM   5998  O  O     . LYS A 1 2206 ? 172.248 202.416 151.557 1.00 6.20   ? 2206 LYS A O     1 
ATOM   5999  C  CB    . LYS A 1 2206 ? 174.776 202.547 153.635 1.00 4.45   ? 2206 LYS A CB    1 
ATOM   6000  C  CG    . LYS A 1 2206 ? 176.025 201.690 153.756 1.00 4.40   ? 2206 LYS A CG    1 
ATOM   6001  C  CD    . LYS A 1 2206 ? 175.905 200.404 152.963 1.00 3.65   ? 2206 LYS A CD    1 
ATOM   6002  C  CE    . LYS A 1 2206 ? 177.247 199.999 152.376 1.00 4.37   ? 2206 LYS A CE    1 
ATOM   6003  N  NZ    . LYS A 1 2206 ? 177.224 198.602 151.861 1.00 5.60   ? 2206 LYS A NZ    1 
ATOM   6004  N  N     . VAL A 1 2207 ? 172.521 204.469 152.442 1.00 9.20   ? 2207 VAL A N     1 
ATOM   6005  C  CA    . VAL A 1 2207 ? 171.117 204.825 152.260 1.00 6.65   ? 2207 VAL A CA    1 
ATOM   6006  C  C     . VAL A 1 2207 ? 170.771 204.879 150.778 1.00 6.95   ? 2207 VAL A C     1 
ATOM   6007  O  O     . VAL A 1 2207 ? 169.724 204.379 150.349 1.00 10.30  ? 2207 VAL A O     1 
ATOM   6008  C  CB    . VAL A 1 2207 ? 170.809 206.161 152.962 1.00 7.39   ? 2207 VAL A CB    1 
ATOM   6009  C  CG1   . VAL A 1 2207 ? 169.398 206.623 152.639 1.00 9.13   ? 2207 VAL A CG1   1 
ATOM   6010  C  CG2   . VAL A 1 2207 ? 171.004 206.033 154.463 1.00 4.75   ? 2207 VAL A CG2   1 
ATOM   6011  N  N     . LEU A 1 2208 ? 171.648 205.484 149.972 1.00 7.68   ? 2208 LEU A N     1 
ATOM   6012  C  CA    . LEU A 1 2208 ? 171.416 205.542 148.532 1.00 6.62   ? 2208 LEU A CA    1 
ATOM   6013  C  C     . LEU A 1 2208 ? 171.426 204.150 147.915 1.00 7.13   ? 2208 LEU A C     1 
ATOM   6014  O  O     . LEU A 1 2208 ? 170.648 203.863 146.998 1.00 10.44  ? 2208 LEU A O     1 
ATOM   6015  C  CB    . LEU A 1 2208 ? 172.467 206.430 147.868 1.00 6.74   ? 2208 LEU A CB    1 
ATOM   6016  C  CG    . LEU A 1 2208 ? 172.488 207.893 148.303 1.00 9.70   ? 2208 LEU A CG    1 
ATOM   6017  C  CD1   . LEU A 1 2208 ? 173.573 208.643 147.560 1.00 15.85  ? 2208 LEU A CD1   1 
ATOM   6018  C  CD2   . LEU A 1 2208 ? 171.138 208.538 148.070 1.00 13.57  ? 2208 LEU A CD2   1 
ATOM   6019  N  N     . GLN A 1 2209 ? 172.313 203.277 148.396 1.00 6.42   ? 2209 GLN A N     1 
ATOM   6020  C  CA    . GLN A 1 2209 ? 172.306 201.889 147.946 1.00 6.82   ? 2209 GLN A CA    1 
ATOM   6021  C  C     . GLN A 1 2209 ? 171.005 201.198 148.327 1.00 7.79   ? 2209 GLN A C     1 
ATOM   6022  O  O     . GLN A 1 2209 ? 170.472 200.391 147.557 1.00 13.25  ? 2209 GLN A O     1 
ATOM   6023  C  CB    . GLN A 1 2209 ? 173.503 201.144 148.533 1.00 5.10   ? 2209 GLN A CB    1 
ATOM   6024  C  CG    . GLN A 1 2209 ? 174.839 201.592 147.977 1.00 7.07   ? 2209 GLN A CG    1 
ATOM   6025  C  CD    . GLN A 1 2209 ? 176.003 200.923 148.670 1.00 5.82   ? 2209 GLN A CD    1 
ATOM   6026  O  OE1   . GLN A 1 2209 ? 175.815 200.068 149.532 1.00 6.74   ? 2209 GLN A OE1   1 
ATOM   6027  N  NE2   . GLN A 1 2209 ? 177.217 201.310 148.298 1.00 8.02   ? 2209 GLN A NE2   1 
ATOM   6028  N  N     . LEU A 1 2210 ? 170.484 201.497 149.518 1.00 6.57   ? 2210 LEU A N     1 
ATOM   6029  C  CA    . LEU A 1 2210 ? 169.206 200.930 149.933 1.00 7.20   ? 2210 LEU A CA    1 
ATOM   6030  C  C     . LEU A 1 2210 ? 168.074 201.409 149.034 1.00 9.67   ? 2210 LEU A C     1 
ATOM   6031  O  O     . LEU A 1 2210 ? 167.176 200.633 148.687 1.00 13.55  ? 2210 LEU A O     1 
ATOM   6032  C  CB    . LEU A 1 2210 ? 168.930 201.285 151.393 1.00 7.37   ? 2210 LEU A CB    1 
ATOM   6033  C  CG    . LEU A 1 2210 ? 167.687 200.665 152.027 1.00 8.07   ? 2210 LEU A CG    1 
ATOM   6034  C  CD1   . LEU A 1 2210 ? 167.915 199.193 152.299 1.00 7.71   ? 2210 LEU A CD1   1 
ATOM   6035  C  CD2   . LEU A 1 2210 ? 167.328 201.395 153.306 1.00 5.83   ? 2210 LEU A CD2   1 
ATOM   6036  N  N     . TYR A 1 2211 ? 168.100 202.687 148.645 1.00 8.51   ? 2211 TYR A N     1 
ATOM   6037  C  CA    . TYR A 1 2211 ? 167.073 203.211 147.750 1.00 9.60   ? 2211 TYR A CA    1 
ATOM   6038  C  C     . TYR A 1 2211 ? 167.111 202.518 146.396 1.00 13.31  ? 2211 TYR A C     1 
ATOM   6039  O  O     . TYR A 1 2211 ? 166.062 202.214 145.816 1.00 21.49  ? 2211 TYR A O     1 
ATOM   6040  C  CB    . TYR A 1 2211 ? 167.239 204.720 147.578 1.00 14.63  ? 2211 TYR A CB    1 
ATOM   6041  C  CG    . TYR A 1 2211 ? 166.336 205.308 146.517 1.00 21.42  ? 2211 TYR A CG    1 
ATOM   6042  C  CD1   . TYR A 1 2211 ? 164.955 205.213 146.623 1.00 18.33  ? 2211 TYR A CD1   1 
ATOM   6043  C  CD2   . TYR A 1 2211 ? 166.864 205.958 145.409 1.00 20.34  ? 2211 TYR A CD2   1 
ATOM   6044  C  CE1   . TYR A 1 2211 ? 164.127 205.746 145.655 1.00 20.02  ? 2211 TYR A CE1   1 
ATOM   6045  C  CE2   . TYR A 1 2211 ? 166.042 206.497 144.439 1.00 21.20  ? 2211 TYR A CE2   1 
ATOM   6046  C  CZ    . TYR A 1 2211 ? 164.675 206.388 144.567 1.00 21.30  ? 2211 TYR A CZ    1 
ATOM   6047  O  OH    . TYR A 1 2211 ? 163.853 206.922 143.602 1.00 30.91  ? 2211 TYR A OH    1 
ATOM   6048  N  N     . GLN A 1 2212 ? 168.311 202.271 145.869 1.00 11.28  ? 2212 GLN A N     1 
ATOM   6049  C  CA    . GLN A 1 2212 ? 168.425 201.593 144.583 1.00 13.82  ? 2212 GLN A CA    1 
ATOM   6050  C  C     . GLN A 1 2212 ? 167.892 200.169 144.662 1.00 12.82  ? 2212 GLN A C     1 
ATOM   6051  O  O     . GLN A 1 2212 ? 167.236 199.691 143.729 1.00 19.64  ? 2212 GLN A O     1 
ATOM   6052  C  CB    . GLN A 1 2212 ? 169.879 201.601 144.118 1.00 18.86  ? 2212 GLN A CB    1 
ATOM   6053  C  CG    . GLN A 1 2212 ? 170.132 202.479 142.909 1.00 26.06  ? 2212 GLN A CG    1 
ATOM   6054  C  CD    . GLN A 1 2212 ? 171.570 202.941 142.820 1.00 30.72  ? 2212 GLN A CD    1 
ATOM   6055  O  OE1   . GLN A 1 2212 ? 172.493 202.205 143.168 1.00 34.04  ? 2212 GLN A OE1   1 
ATOM   6056  N  NE2   . GLN A 1 2212 ? 171.769 204.167 142.351 1.00 41.24  ? 2212 GLN A NE2   1 
ATOM   6057  N  N     . ILE A 1 2213 ? 168.165 199.474 145.768 1.00 9.69   ? 2213 ILE A N     1 
ATOM   6058  C  CA    . ILE A 1 2213 ? 167.712 198.095 145.908 1.00 11.10  ? 2213 ILE A CA    1 
ATOM   6059  C  C     . ILE A 1 2213 ? 166.191 198.035 146.019 1.00 14.36  ? 2213 ILE A C     1 
ATOM   6060  O  O     . ILE A 1 2213 ? 165.564 197.089 145.526 1.00 20.26  ? 2213 ILE A O     1 
ATOM   6061  C  CB    . ILE A 1 2213 ? 168.414 197.432 147.108 1.00 13.42  ? 2213 ILE A CB    1 
ATOM   6062  C  CG1   . ILE A 1 2213 ? 169.888 197.194 146.786 1.00 13.62  ? 2213 ILE A CG1   1 
ATOM   6063  C  CG2   . ILE A 1 2213 ? 167.784 196.095 147.433 1.00 12.31  ? 2213 ILE A CG2   1 
ATOM   6064  C  CD1   . ILE A 1 2213 ? 170.114 196.381 145.532 1.00 13.43  ? 2213 ILE A CD1   1 
ATOM   6065  N  N     . THR A 1 2214 ? 165.571 199.038 146.653 1.00 13.53  ? 2214 THR A N     1 
ATOM   6066  C  CA    . THR A 1 2214 ? 164.113 199.077 146.744 1.00 11.17  ? 2214 THR A CA    1 
ATOM   6067  C  C     . THR A 1 2214 ? 163.471 199.054 145.362 1.00 14.04  ? 2214 THR A C     1 
ATOM   6068  O  O     . THR A 1 2214 ? 162.410 198.448 145.171 1.00 14.58  ? 2214 THR A O     1 
ATOM   6069  C  CB    . THR A 1 2214 ? 163.652 200.324 147.503 1.00 9.68   ? 2214 THR A CB    1 
ATOM   6070  O  OG1   . THR A 1 2214 ? 164.316 201.481 146.980 1.00 14.18  ? 2214 THR A OG1   1 
ATOM   6071  C  CG2   . THR A 1 2214 ? 163.944 200.206 148.988 1.00 9.79   ? 2214 THR A CG2   1 
ATOM   6072  N  N     . GLN A 1 2215 ? 164.099 199.713 144.387 1.00 15.50  ? 2215 GLN A N     1 
ATOM   6073  C  CA    . GLN A 1 2215 ? 163.529 199.800 143.049 1.00 16.04  ? 2215 GLN A CA    1 
ATOM   6074  C  C     . GLN A 1 2215 ? 163.681 198.506 142.261 1.00 18.03  ? 2215 GLN A C     1 
ATOM   6075  O  O     . GLN A 1 2215 ? 162.831 198.209 141.415 1.00 24.67  ? 2215 GLN A O     1 
ATOM   6076  C  CB    . GLN A 1 2215 ? 164.177 200.957 142.290 1.00 16.07  ? 2215 GLN A CB    1 
ATOM   6077  C  CG    . GLN A 1 2215 ? 164.105 202.284 143.028 1.00 16.51  ? 2215 GLN A CG    1 
ATOM   6078  C  CD    . GLN A 1 2215 ? 164.696 203.429 142.233 1.00 28.61  ? 2215 GLN A CD    1 
ATOM   6079  O  OE1   . GLN A 1 2215 ? 165.907 203.650 142.251 1.00 31.11  ? 2215 GLN A OE1   1 
ATOM   6080  N  NE2   . GLN A 1 2215 ? 163.844 204.165 141.530 1.00 30.60  ? 2215 GLN A NE2   1 
ATOM   6081  N  N     . ILE A 1 2216 ? 164.736 197.735 142.512 1.00 14.28  ? 2216 ILE A N     1 
ATOM   6082  C  CA    . ILE A 1 2216 ? 164.944 196.484 141.789 1.00 16.72  ? 2216 ILE A CA    1 
ATOM   6083  C  C     . ILE A 1 2216 ? 164.234 195.321 142.469 1.00 17.92  ? 2216 ILE A C     1 
ATOM   6084  O  O     . ILE A 1 2216 ? 163.558 194.528 141.809 1.00 24.21  ? 2216 ILE A O     1 
ATOM   6085  C  CB    . ILE A 1 2216 ? 166.452 196.203 141.636 1.00 21.11  ? 2216 ILE A CB    1 
ATOM   6086  C  CG1   . ILE A 1 2216 ? 167.218 197.498 141.369 1.00 19.61  ? 2216 ILE A CG1   1 
ATOM   6087  C  CG2   . ILE A 1 2216 ? 166.697 195.195 140.524 1.00 20.29  ? 2216 ILE A CG2   1 
ATOM   6088  C  CD1   . ILE A 1 2216 ? 168.665 197.444 141.805 1.00 16.07  ? 2216 ILE A CD1   1 
ATOM   6089  N  N     . ASN A 1 2217 ? 164.373 195.197 143.785 1.00 15.36  ? 2217 ASN A N     1 
ATOM   6090  C  CA    . ASN A 1 2217 ? 163.832 194.072 144.532 1.00 14.98  ? 2217 ASN A CA    1 
ATOM   6091  C  C     . ASN A 1 2217 ? 162.650 194.520 145.378 1.00 11.76  ? 2217 ASN A C     1 
ATOM   6092  O  O     . ASN A 1 2217 ? 162.632 195.642 145.892 1.00 11.83  ? 2217 ASN A O     1 
ATOM   6093  C  CB    . ASN A 1 2217 ? 164.900 193.452 145.438 1.00 14.76  ? 2217 ASN A CB    1 
ATOM   6094  C  CG    . ASN A 1 2217 ? 166.052 192.855 144.660 1.00 16.90  ? 2217 ASN A CG    1 
ATOM   6095  O  OD1   . ASN A 1 2217 ? 167.137 193.433 144.597 1.00 19.60  ? 2217 ASN A OD1   1 
ATOM   6096  N  ND2   . ASN A 1 2217 ? 165.826 191.690 144.065 1.00 20.64  ? 2217 ASN A ND2   1 
ATOM   6097  N  N     . HIS A 1 2218 ? 161.663 193.639 145.516 1.00 10.33  ? 2218 HIS A N     1 
ATOM   6098  C  CA    . HIS A 1 2218 ? 160.606 193.820 146.500 1.00 8.87   ? 2218 HIS A CA    1 
ATOM   6099  C  C     . HIS A 1 2218 ? 160.952 193.182 147.838 1.00 8.38   ? 2218 HIS A C     1 
ATOM   6100  O  O     . HIS A 1 2218 ? 160.202 193.350 148.805 1.00 8.54   ? 2218 HIS A O     1 
ATOM   6101  C  CB    . HIS A 1 2218 ? 159.282 193.254 145.975 1.00 6.56   ? 2218 HIS A CB    1 
ATOM   6102  C  CG    . HIS A 1 2218 ? 159.337 191.800 145.629 1.00 6.32   ? 2218 HIS A CG    1 
ATOM   6103  N  ND1   . HIS A 1 2218 ? 159.842 191.338 144.434 1.00 8.17   ? 2218 HIS A ND1   1 
ATOM   6104  C  CD2   . HIS A 1 2218 ? 158.944 190.703 146.319 1.00 8.55   ? 2218 HIS A CD2   1 
ATOM   6105  C  CE1   . HIS A 1 2218 ? 159.762 190.020 144.403 1.00 8.86   ? 2218 HIS A CE1   1 
ATOM   6106  N  NE2   . HIS A 1 2218 ? 159.220 189.610 145.536 1.00 9.62   ? 2218 HIS A NE2   1 
ATOM   6107  N  N     . GLY A 1 2219 ? 162.068 192.462 147.910 1.00 6.93   ? 2219 GLY A N     1 
ATOM   6108  C  CA    . GLY A 1 2219 ? 162.559 191.909 149.156 1.00 6.84   ? 2219 GLY A CA    1 
ATOM   6109  C  C     . GLY A 1 2219 ? 163.969 192.377 149.449 1.00 7.78   ? 2219 GLY A C     1 
ATOM   6110  O  O     . GLY A 1 2219 ? 164.858 192.263 148.600 1.00 11.66  ? 2219 GLY A O     1 
ATOM   6111  N  N     . LEU A 1 2220 ? 164.188 192.906 150.649 1.00 6.31   ? 2220 LEU A N     1 
ATOM   6112  C  CA    . LEU A 1 2220 ? 165.455 193.516 151.018 1.00 4.94   ? 2220 LEU A CA    1 
ATOM   6113  C  C     . LEU A 1 2220 ? 165.906 192.998 152.374 1.00 7.12   ? 2220 LEU A C     1 
ATOM   6114  O  O     . LEU A 1 2220 ? 165.096 192.594 153.211 1.00 7.97   ? 2220 LEU A O     1 
ATOM   6115  C  CB    . LEU A 1 2220 ? 165.350 195.043 151.071 1.00 6.20   ? 2220 LEU A CB    1 
ATOM   6116  C  CG    . LEU A 1 2220 ? 164.556 195.721 149.960 1.00 8.99   ? 2220 LEU A CG    1 
ATOM   6117  C  CD1   . LEU A 1 2220 ? 163.117 195.946 150.383 1.00 8.79   ? 2220 LEU A CD1   1 
ATOM   6118  C  CD2   . LEU A 1 2220 ? 165.215 197.031 149.625 1.00 10.17  ? 2220 LEU A CD2   1 
ATOM   6119  N  N     . MET A 1 2221 ? 167.219 193.024 152.584 1.00 7.43   ? 2221 MET A N     1 
ATOM   6120  C  CA    . MET A 1 2221 ? 167.804 192.667 153.870 1.00 5.57   ? 2221 MET A CA    1 
ATOM   6121  C  C     . MET A 1 2221 ? 168.885 193.677 154.213 1.00 4.95   ? 2221 MET A C     1 
ATOM   6122  O  O     . MET A 1 2221 ? 169.870 193.805 153.480 1.00 6.59   ? 2221 MET A O     1 
ATOM   6123  C  CB    . MET A 1 2221 ? 168.383 191.250 153.849 1.00 7.63   ? 2221 MET A CB    1 
ATOM   6124  C  CG    . MET A 1 2221 ? 167.338 190.152 153.897 1.00 8.88   ? 2221 MET A CG    1 
ATOM   6125  S  SD    . MET A 1 2221 ? 167.920 188.675 154.746 1.00 13.90  ? 2221 MET A SD    1 
ATOM   6126  C  CE    . MET A 1 2221 ? 166.455 187.652 154.677 1.00 11.49  ? 2221 MET A CE    1 
ATOM   6127  N  N     . MET A 1 2222 ? 168.696 194.398 155.315 1.00 6.85   ? 2222 MET A N     1 
ATOM   6128  C  CA    . MET A 1 2222 ? 169.745 195.242 155.878 1.00 4.66   ? 2222 MET A CA    1 
ATOM   6129  C  C     . MET A 1 2222 ? 170.526 194.379 156.858 1.00 4.89   ? 2222 MET A C     1 
ATOM   6130  O  O     . MET A 1 2222 ? 170.016 194.001 157.915 1.00 4.54   ? 2222 MET A O     1 
ATOM   6131  C  CB    . MET A 1 2222 ? 169.157 196.475 156.556 1.00 4.81   ? 2222 MET A CB    1 
ATOM   6132  C  CG    . MET A 1 2222 ? 168.815 197.606 155.603 1.00 4.26   ? 2222 MET A CG    1 
ATOM   6133  S  SD    . MET A 1 2222 ? 167.138 198.217 155.836 1.00 19.11  ? 2222 MET A SD    1 
ATOM   6134  C  CE    . MET A 1 2222 ? 166.195 196.717 155.587 1.00 8.28   ? 2222 MET A CE    1 
ATOM   6135  N  N     . VAL A 1 2223 ? 171.766 194.060 156.504 1.00 7.20   ? 2223 VAL A N     1 
ATOM   6136  C  CA    . VAL A 1 2223 ? 172.595 193.143 157.274 1.00 4.47   ? 2223 VAL A CA    1 
ATOM   6137  C  C     . VAL A 1 2223 ? 173.779 193.913 157.837 1.00 5.25   ? 2223 VAL A C     1 
ATOM   6138  O  O     . VAL A 1 2223 ? 174.481 194.618 157.101 1.00 9.12   ? 2223 VAL A O     1 
ATOM   6139  C  CB    . VAL A 1 2223 ? 173.068 191.962 156.410 1.00 4.99   ? 2223 VAL A CB    1 
ATOM   6140  C  CG1   . VAL A 1 2223 ? 173.753 190.913 157.270 1.00 8.65   ? 2223 VAL A CG1   1 
ATOM   6141  C  CG2   . VAL A 1 2223 ? 171.898 191.361 155.648 1.00 6.96   ? 2223 VAL A CG2   1 
ATOM   6142  N  N     . GLY A 1 2224 ? 174.000 193.784 159.141 1.00 4.64   ? 2224 GLY A N     1 
ATOM   6143  C  CA    . GLY A 1 2224 ? 175.127 194.415 159.779 1.00 4.64   ? 2224 GLY A CA    1 
ATOM   6144  C  C     . GLY A 1 2224 ? 175.092 194.291 161.285 1.00 5.41   ? 2224 GLY A C     1 
ATOM   6145  O  O     . GLY A 1 2224 ? 174.042 194.047 161.885 1.00 8.32   ? 2224 GLY A O     1 
ATOM   6146  N  N     . PRO A 1 2225 ? 176.244 194.476 161.928 1.00 6.29   ? 2225 PRO A N     1 
ATOM   6147  C  CA    . PRO A 1 2225 ? 176.307 194.351 163.387 1.00 4.69   ? 2225 PRO A CA    1 
ATOM   6148  C  C     . PRO A 1 2225 ? 175.381 195.342 164.073 1.00 4.70   ? 2225 PRO A C     1 
ATOM   6149  O  O     . PRO A 1 2225 ? 174.963 196.349 163.497 1.00 8.09   ? 2225 PRO A O     1 
ATOM   6150  C  CB    . PRO A 1 2225 ? 177.777 194.648 163.708 1.00 6.28   ? 2225 PRO A CB    1 
ATOM   6151  C  CG    . PRO A 1 2225 ? 178.504 194.360 162.437 1.00 5.33   ? 2225 PRO A CG    1 
ATOM   6152  C  CD    . PRO A 1 2225 ? 177.565 194.753 161.341 1.00 6.45   ? 2225 PRO A CD    1 
ATOM   6153  N  N     . SER A 1 2226 ? 175.045 195.027 165.322 1.00 4.34   ? 2226 SER A N     1 
ATOM   6154  C  CA    . SER A 1 2226 ? 174.164 195.889 166.095 1.00 5.15   ? 2226 SER A CA    1 
ATOM   6155  C  C     . SER A 1 2226 ? 174.745 197.293 166.180 1.00 3.22   ? 2226 SER A C     1 
ATOM   6156  O  O     . SER A 1 2226 ? 175.943 197.476 166.410 1.00 5.86   ? 2226 SER A O     1 
ATOM   6157  C  CB    . SER A 1 2226 ? 173.955 195.314 167.497 1.00 4.04   ? 2226 SER A CB    1 
ATOM   6158  O  OG    . SER A 1 2226 ? 173.125 196.158 168.276 1.00 4.55   ? 2226 SER A OG    1 
ATOM   6159  N  N     . GLY A 1 2227 ? 173.888 198.288 165.989 1.00 2.40   ? 2227 GLY A N     1 
ATOM   6160  C  CA    . GLY A 1 2227 ? 174.353 199.661 165.953 1.00 2.59   ? 2227 GLY A CA    1 
ATOM   6161  C  C     . GLY A 1 2227 ? 175.230 199.991 164.765 1.00 3.89   ? 2227 GLY A C     1 
ATOM   6162  O  O     . GLY A 1 2227 ? 176.285 200.614 164.932 1.00 10.20  ? 2227 GLY A O     1 
ATOM   6163  N  N     . SER A 1 2228 ? 174.835 199.562 163.567 1.00 3.37   ? 2228 SER A N     1 
ATOM   6164  C  CA    . SER A 1 2228 ? 175.520 199.944 162.341 1.00 3.59   ? 2228 SER A CA    1 
ATOM   6165  C  C     . SER A 1 2228 ? 174.731 200.952 161.520 1.00 3.28   ? 2228 SER A C     1 
ATOM   6166  O  O     . SER A 1 2228 ? 175.102 201.223 160.373 1.00 6.55   ? 2228 SER A O     1 
ATOM   6167  C  CB    . SER A 1 2228 ? 175.823 198.705 161.490 1.00 3.67   ? 2228 SER A CB    1 
ATOM   6168  O  OG    . SER A 1 2228 ? 174.665 197.909 161.317 1.00 3.12   ? 2228 SER A OG    1 
ATOM   6169  N  N     . GLY A 1 2229 ? 173.661 201.515 162.072 1.00 2.00   ? 2229 GLY A N     1 
ATOM   6170  C  CA    . GLY A 1 2229 ? 172.859 202.485 161.355 1.00 2.04   ? 2229 GLY A CA    1 
ATOM   6171  C  C     . GLY A 1 2229 ? 171.849 201.913 160.388 1.00 0.82   ? 2229 GLY A C     1 
ATOM   6172  O  O     . GLY A 1 2229 ? 171.350 202.654 159.535 1.00 1.52   ? 2229 GLY A O     1 
ATOM   6173  N  N     . LYS A 1 2230 ? 171.534 200.619 160.486 1.00 1.70   ? 2230 LYS A N     1 
ATOM   6174  C  CA    . LYS A 1 2230 ? 170.589 200.015 159.552 1.00 0.87   ? 2230 LYS A CA    1 
ATOM   6175  C  C     . LYS A 1 2230 ? 169.199 200.623 159.697 1.00 1.50   ? 2230 LYS A C     1 
ATOM   6176  O  O     . LYS A 1 2230 ? 168.584 201.030 158.705 1.00 3.24   ? 2230 LYS A O     1 
ATOM   6177  C  CB    . LYS A 1 2230 ? 170.527 198.502 159.759 1.00 1.24   ? 2230 LYS A CB    1 
ATOM   6178  C  CG    . LYS A 1 2230 ? 171.824 197.770 159.485 1.00 1.97   ? 2230 LYS A CG    1 
ATOM   6179  C  CD    . LYS A 1 2230 ? 171.789 196.371 160.076 1.00 3.32   ? 2230 LYS A CD    1 
ATOM   6180  C  CE    . LYS A 1 2230 ? 171.615 196.408 161.582 1.00 3.05   ? 2230 LYS A CE    1 
ATOM   6181  N  NZ    . LYS A 1 2230 ? 171.012 195.154 162.105 1.00 4.30   ? 2230 LYS A NZ    1 
ATOM   6182  N  N     . SER A 1 2231 ? 168.684 200.685 160.926 1.00 1.66   ? 2231 SER A N     1 
ATOM   6183  C  CA    . SER A 1 2231 ? 167.336 201.202 161.137 1.00 2.00   ? 2231 SER A CA    1 
ATOM   6184  C  C     . SER A 1 2231 ? 167.254 202.684 160.802 1.00 2.28   ? 2231 SER A C     1 
ATOM   6185  O  O     . SER A 1 2231 ? 166.292 203.137 160.173 1.00 3.00   ? 2231 SER A O     1 
ATOM   6186  C  CB    . SER A 1 2231 ? 166.890 200.946 162.576 1.00 2.55   ? 2231 SER A CB    1 
ATOM   6187  O  OG    . SER A 1 2231 ? 167.983 201.022 163.468 1.00 8.11   ? 2231 SER A OG    1 
ATOM   6188  N  N     . MET A 1 2232 ? 168.264 203.457 161.205 1.00 2.19   ? 2232 MET A N     1 
ATOM   6189  C  CA    . MET A 1 2232 ? 168.252 204.888 160.919 1.00 2.74   ? 2232 MET A CA    1 
ATOM   6190  C  C     . MET A 1 2232 ? 168.320 205.149 159.419 1.00 3.92   ? 2232 MET A C     1 
ATOM   6191  O  O     . MET A 1 2232 ? 167.849 206.185 158.940 1.00 5.77   ? 2232 MET A O     1 
ATOM   6192  C  CB    . MET A 1 2232 ? 169.414 205.575 161.635 1.00 3.77   ? 2232 MET A CB    1 
ATOM   6193  C  CG    . MET A 1 2232 ? 169.070 206.190 162.987 1.00 6.07   ? 2232 MET A CG    1 
ATOM   6194  S  SD    . MET A 1 2232 ? 167.450 206.977 163.088 1.00 28.95  ? 2232 MET A SD    1 
ATOM   6195  C  CE    . MET A 1 2232 ? 166.500 205.703 163.915 1.00 7.92   ? 2232 MET A CE    1 
ATOM   6196  N  N     . ALA A 1 2233 ? 168.909 204.219 158.665 1.00 3.49   ? 2233 ALA A N     1 
ATOM   6197  C  CA    . ALA A 1 2233 ? 169.017 204.391 157.221 1.00 2.39   ? 2233 ALA A CA    1 
ATOM   6198  C  C     . ALA A 1 2233 ? 167.648 204.343 156.554 1.00 5.03   ? 2233 ALA A C     1 
ATOM   6199  O  O     . ALA A 1 2233 ? 167.297 205.230 155.766 1.00 9.37   ? 2233 ALA A O     1 
ATOM   6200  C  CB    . ALA A 1 2233 ? 169.937 203.321 156.637 1.00 2.05   ? 2233 ALA A CB    1 
ATOM   6201  N  N     . TRP A 1 2234 ? 166.857 203.311 156.858 1.00 3.07   ? 2234 TRP A N     1 
ATOM   6202  C  CA    . TRP A 1 2234 ? 165.575 203.152 156.179 1.00 2.47   ? 2234 TRP A CA    1 
ATOM   6203  C  C     . TRP A 1 2234 ? 164.512 204.094 156.732 1.00 3.67   ? 2234 TRP A C     1 
ATOM   6204  O  O     . TRP A 1 2234 ? 163.572 204.445 156.011 1.00 6.19   ? 2234 TRP A O     1 
ATOM   6205  C  CB    . TRP A 1 2234 ? 165.125 201.686 156.236 1.00 2.55   ? 2234 TRP A CB    1 
ATOM   6206  C  CG    . TRP A 1 2234 ? 164.692 201.169 157.576 1.00 2.76   ? 2234 TRP A CG    1 
ATOM   6207  C  CD1   . TRP A 1 2234 ? 165.404 200.343 158.394 1.00 1.64   ? 2234 TRP A CD1   1 
ATOM   6208  C  CD2   . TRP A 1 2234 ? 163.435 201.392 158.229 1.00 2.67   ? 2234 TRP A CD2   1 
ATOM   6209  N  NE1   . TRP A 1 2234 ? 164.684 200.060 159.526 1.00 1.66   ? 2234 TRP A NE1   1 
ATOM   6210  C  CE2   . TRP A 1 2234 ? 163.471 200.691 159.450 1.00 2.04   ? 2234 TRP A CE2   1 
ATOM   6211  C  CE3   . TRP A 1 2234 ? 162.289 202.126 157.906 1.00 3.09   ? 2234 TRP A CE3   1 
ATOM   6212  C  CZ2   . TRP A 1 2234 ? 162.409 200.702 160.348 1.00 4.06   ? 2234 TRP A CZ2   1 
ATOM   6213  C  CZ3   . TRP A 1 2234 ? 161.239 202.138 158.799 1.00 3.78   ? 2234 TRP A CZ3   1 
ATOM   6214  C  CH2   . TRP A 1 2234 ? 161.304 201.429 160.005 1.00 4.47   ? 2234 TRP A CH2   1 
ATOM   6215  N  N     . ARG A 1 2235 ? 164.633 204.514 157.994 1.00 3.12   ? 2235 ARG A N     1 
ATOM   6216  C  CA    . ARG A 1 2235 ? 163.725 205.534 158.513 1.00 3.59   ? 2235 ARG A CA    1 
ATOM   6217  C  C     . ARG A 1 2235 ? 163.924 206.860 157.790 1.00 6.96   ? 2235 ARG A C     1 
ATOM   6218  O  O     . ARG A 1 2235 ? 162.955 207.529 157.413 1.00 7.46   ? 2235 ARG A O     1 
ATOM   6219  C  CB    . ARG A 1 2235 ? 163.924 205.718 160.017 1.00 5.60   ? 2235 ARG A CB    1 
ATOM   6220  C  CG    . ARG A 1 2235 ? 163.620 204.502 160.870 1.00 4.24   ? 2235 ARG A CG    1 
ATOM   6221  C  CD    . ARG A 1 2235 ? 163.350 204.932 162.302 1.00 8.40   ? 2235 ARG A CD    1 
ATOM   6222  N  NE    . ARG A 1 2235 ? 162.885 203.839 163.146 1.00 15.61  ? 2235 ARG A NE    1 
ATOM   6223  C  CZ    . ARG A 1 2235 ? 161.612 203.505 163.309 1.00 14.79  ? 2235 ARG A CZ    1 
ATOM   6224  N  NH1   . ARG A 1 2235 ? 160.643 204.140 162.671 1.00 10.65  ? 2235 ARG A NH1   1 
ATOM   6225  N  NH2   . ARG A 1 2235 ? 161.305 202.510 164.135 1.00 15.68  ? 2235 ARG A NH2   1 
ATOM   6226  N  N     . VAL A 1 2236 ? 165.182 207.262 157.599 1.00 6.91   ? 2236 VAL A N     1 
ATOM   6227  C  CA    . VAL A 1 2236 ? 165.470 208.518 156.915 1.00 6.49   ? 2236 VAL A CA    1 
ATOM   6228  C  C     . VAL A 1 2236 ? 165.067 208.431 155.448 1.00 7.92   ? 2236 VAL A C     1 
ATOM   6229  O  O     . VAL A 1 2236 ? 164.504 209.379 154.888 1.00 12.19  ? 2236 VAL A O     1 
ATOM   6230  C  CB    . VAL A 1 2236 ? 166.957 208.880 157.084 1.00 7.36   ? 2236 VAL A CB    1 
ATOM   6231  C  CG1   . VAL A 1 2236 ? 167.372 209.937 156.081 1.00 11.19  ? 2236 VAL A CG1   1 
ATOM   6232  C  CG2   . VAL A 1 2236 ? 167.225 209.361 158.499 1.00 11.22  ? 2236 VAL A CG2   1 
ATOM   6233  N  N     . LEU A 1 2237 ? 165.340 207.293 154.806 1.00 5.97   ? 2237 LEU A N     1 
ATOM   6234  C  CA    . LEU A 1 2237 ? 164.952 207.117 153.410 1.00 5.80   ? 2237 LEU A CA    1 
ATOM   6235  C  C     . LEU A 1 2237 ? 163.440 207.168 153.244 1.00 7.90   ? 2237 LEU A C     1 
ATOM   6236  O  O     . LEU A 1 2237 ? 162.932 207.764 152.287 1.00 13.86  ? 2237 LEU A O     1 
ATOM   6237  C  CB    . LEU A 1 2237 ? 165.507 205.798 152.873 1.00 6.64   ? 2237 LEU A CB    1 
ATOM   6238  C  CG    . LEU A 1 2237 ? 165.141 205.451 151.430 1.00 7.59   ? 2237 LEU A CG    1 
ATOM   6239  C  CD1   . LEU A 1 2237 ? 165.688 206.497 150.473 1.00 10.87  ? 2237 LEU A CD1   1 
ATOM   6240  C  CD2   . LEU A 1 2237 ? 165.649 204.066 151.070 1.00 7.06   ? 2237 LEU A CD2   1 
ATOM   6241  N  N     . LEU A 1 2238 ? 162.703 206.545 154.166 1.00 6.17   ? 2238 LEU A N     1 
ATOM   6242  C  CA    . LEU A 1 2238 ? 161.246 206.546 154.079 1.00 5.79   ? 2238 LEU A CA    1 
ATOM   6243  C  C     . LEU A 1 2238 ? 160.692 207.964 154.156 1.00 7.42   ? 2238 LEU A C     1 
ATOM   6244  O  O     . LEU A 1 2238 ? 159.784 208.331 153.401 1.00 10.34  ? 2238 LEU A O     1 
ATOM   6245  C  CB    . LEU A 1 2238 ? 160.659 205.673 155.187 1.00 5.76   ? 2238 LEU A CB    1 
ATOM   6246  C  CG    . LEU A 1 2238 ? 159.177 205.318 155.077 1.00 5.56   ? 2238 LEU A CG    1 
ATOM   6247  C  CD1   . LEU A 1 2238 ? 158.884 204.656 153.743 1.00 7.71   ? 2238 LEU A CD1   1 
ATOM   6248  C  CD2   . LEU A 1 2238 ? 158.765 204.418 156.223 1.00 5.82   ? 2238 LEU A CD2   1 
ATOM   6249  N  N     . LYS A 1 2239 ? 161.227 208.777 155.069 1.00 8.05   ? 2239 LYS A N     1 
ATOM   6250  C  CA    . LYS A 1 2239 ? 160.786 210.164 155.168 1.00 9.56   ? 2239 LYS A CA    1 
ATOM   6251  C  C     . LYS A 1 2239 ? 161.228 210.976 153.958 1.00 11.34  ? 2239 LYS A C     1 
ATOM   6252  O  O     . LYS A 1 2239 ? 160.464 211.803 153.446 1.00 15.86  ? 2239 LYS A O     1 
ATOM   6253  C  CB    . LYS A 1 2239 ? 161.313 210.794 156.457 1.00 12.51  ? 2239 LYS A CB    1 
ATOM   6254  C  CG    . LYS A 1 2239 ? 160.704 210.222 157.724 1.00 18.02  ? 2239 LYS A CG    1 
ATOM   6255  C  CD    . LYS A 1 2239 ? 161.256 210.919 158.955 1.00 26.57  ? 2239 LYS A CD    1 
ATOM   6256  C  CE    . LYS A 1 2239 ? 160.666 210.342 160.229 1.00 31.28  ? 2239 LYS A CE    1 
ATOM   6257  N  NZ    . LYS A 1 2239 ? 161.206 211.014 161.442 1.00 31.88  ? 2239 LYS A NZ    1 
ATOM   6258  N  N     . ALA A 1 2240 ? 162.460 210.760 153.490 1.00 11.38  ? 2240 ALA A N     1 
ATOM   6259  C  CA    . ALA A 1 2240 ? 162.964 211.522 152.351 1.00 13.58  ? 2240 ALA A CA    1 
ATOM   6260  C  C     . ALA A 1 2240 ? 162.169 211.224 151.086 1.00 13.47  ? 2240 ALA A C     1 
ATOM   6261  O  O     . ALA A 1 2240 ? 161.855 212.137 150.315 1.00 20.28  ? 2240 ALA A O     1 
ATOM   6262  C  CB    . ALA A 1 2240 ? 164.448 211.224 152.136 1.00 15.83  ? 2240 ALA A CB    1 
ATOM   6263  N  N     . LEU A 1 2241 ? 161.838 209.952 150.855 1.00 12.42  ? 2241 LEU A N     1 
ATOM   6264  C  CA    . LEU A 1 2241 ? 160.998 209.605 149.714 1.00 13.85  ? 2241 LEU A CA    1 
ATOM   6265  C  C     . LEU A 1 2241 ? 159.609 210.211 149.854 1.00 15.39  ? 2241 LEU A C     1 
ATOM   6266  O  O     . LEU A 1 2241 ? 158.983 210.591 148.857 1.00 19.56  ? 2241 LEU A O     1 
ATOM   6267  C  CB    . LEU A 1 2241 ? 160.914 208.087 149.568 1.00 11.61  ? 2241 LEU A CB    1 
ATOM   6268  C  CG    . LEU A 1 2241 ? 162.165 207.417 149.002 1.00 13.70  ? 2241 LEU A CG    1 
ATOM   6269  C  CD1   . LEU A 1 2241 ? 161.919 205.940 148.754 1.00 19.47  ? 2241 LEU A CD1   1 
ATOM   6270  C  CD2   . LEU A 1 2241 ? 162.603 208.115 147.727 1.00 15.99  ? 2241 LEU A CD2   1 
ATOM   6271  N  N     . GLU A 1 2242 ? 159.106 210.298 151.087 1.00 15.44  ? 2242 GLU A N     1 
ATOM   6272  C  CA    . GLU A 1 2242 ? 157.826 210.955 151.325 1.00 18.14  ? 2242 GLU A CA    1 
ATOM   6273  C  C     . GLU A 1 2242 ? 157.886 212.431 150.957 1.00 19.32  ? 2242 GLU A C     1 
ATOM   6274  O  O     . GLU A 1 2242 ? 156.945 212.971 150.365 1.00 22.59  ? 2242 GLU A O     1 
ATOM   6275  C  CB    . GLU A 1 2242 ? 157.421 210.782 152.788 1.00 19.70  ? 2242 GLU A CB    1 
ATOM   6276  C  CG    . GLU A 1 2242 ? 155.939 210.941 153.048 1.00 25.11  ? 2242 GLU A CG    1 
ATOM   6277  C  CD    . GLU A 1 2242 ? 155.650 211.572 154.394 1.00 39.56  ? 2242 GLU A CD    1 
ATOM   6278  O  OE1   . GLU A 1 2242 ? 154.777 211.049 155.119 1.00 45.60  ? 2242 GLU A OE1   1 
ATOM   6279  O  OE2   . GLU A 1 2242 ? 156.295 212.587 154.727 1.00 43.51  ? 2242 GLU A OE2   1 
ATOM   6280  N  N     . ARG A 1 2243 ? 158.987 213.100 151.302 1.00 23.36  ? 2243 ARG A N     1 
ATOM   6281  C  CA    . ARG A 1 2243 ? 159.103 214.527 151.027 1.00 23.78  ? 2243 ARG A CA    1 
ATOM   6282  C  C     . ARG A 1 2243 ? 159.483 214.798 149.578 1.00 26.00  ? 2243 ARG A C     1 
ATOM   6283  O  O     . ARG A 1 2243 ? 159.318 215.925 149.097 1.00 35.95  ? 2243 ARG A O     1 
ATOM   6284  C  CB    . ARG A 1 2243 ? 160.127 215.153 151.973 1.00 24.88  ? 2243 ARG A CB    1 
ATOM   6285  C  CG    . ARG A 1 2243 ? 159.563 215.510 153.338 1.00 31.40  ? 2243 ARG A CG    1 
ATOM   6286  C  CD    . ARG A 1 2243 ? 160.661 215.601 154.383 1.00 37.71  ? 2243 ARG A CD    1 
ATOM   6287  N  NE    . ARG A 1 2243 ? 161.390 216.861 154.309 1.00 44.59  ? 2243 ARG A NE    1 
ATOM   6288  C  CZ    . ARG A 1 2243 ? 161.675 217.621 155.358 1.00 43.68  ? 2243 ARG A CZ    1 
ATOM   6289  N  NH1   . ARG A 1 2243 ? 161.313 217.273 156.582 1.00 41.82  ? 2243 ARG A NH1   1 
ATOM   6290  N  NH2   . ARG A 1 2243 ? 162.339 218.758 155.174 1.00 45.26  ? 2243 ARG A NH2   1 
ATOM   6291  N  N     . LEU A 1 2244 ? 159.989 213.791 148.867 1.00 24.35  ? 2244 LEU A N     1 
ATOM   6292  C  CA    . LEU A 1 2244 ? 160.431 213.980 147.488 1.00 22.13  ? 2244 LEU A CA    1 
ATOM   6293  C  C     . LEU A 1 2244 ? 159.368 213.533 146.488 1.00 25.77  ? 2244 LEU A C     1 
ATOM   6294  O  O     . LEU A 1 2244 ? 158.932 214.321 145.643 1.00 32.59  ? 2244 LEU A O     1 
ATOM   6295  C  CB    . LEU A 1 2244 ? 161.747 213.229 147.255 1.00 21.47  ? 2244 LEU A CB    1 
ATOM   6296  C  CG    . LEU A 1 2244 ? 162.248 213.157 145.812 1.00 21.44  ? 2244 LEU A CG    1 
ATOM   6297  C  CD1   . LEU A 1 2244 ? 162.996 214.428 145.448 1.00 28.66  ? 2244 LEU A CD1   1 
ATOM   6298  C  CD2   . LEU A 1 2244 ? 163.132 211.938 145.609 1.00 20.95  ? 2244 LEU A CD2   1 
ATOM   6299  N  N     . GLU A 1 2245 ? 158.943 212.271 146.570 1.00 23.79  ? 2245 GLU A N     1 
ATOM   6300  C  CA    . GLU A 1 2245 ? 157.925 211.756 145.663 1.00 25.34  ? 2245 GLU A CA    1 
ATOM   6301  C  C     . GLU A 1 2245 ? 156.515 212.193 146.037 1.00 29.76  ? 2245 GLU A C     1 
ATOM   6302  O  O     . GLU A 1 2245 ? 155.616 212.109 145.193 1.00 30.50  ? 2245 GLU A O     1 
ATOM   6303  C  CB    . GLU A 1 2245 ? 157.978 210.227 145.615 1.00 26.18  ? 2245 GLU A CB    1 
ATOM   6304  C  CG    . GLU A 1 2245 ? 159.336 209.652 145.258 1.00 26.56  ? 2245 GLU A CG    1 
ATOM   6305  C  CD    . GLU A 1 2245 ? 159.372 208.142 145.383 1.00 32.65  ? 2245 GLU A CD    1 
ATOM   6306  O  OE1   . GLU A 1 2245 ? 158.420 207.571 145.954 1.00 31.96  ? 2245 GLU A OE1   1 
ATOM   6307  O  OE2   . GLU A 1 2245 ? 160.349 207.525 144.910 1.00 32.40  ? 2245 GLU A OE2   1 
ATOM   6308  N  N     . GLY A 1 2246 ? 156.298 212.653 147.266 1.00 24.78  ? 2246 GLY A N     1 
ATOM   6309  C  CA    . GLY A 1 2246 ? 154.970 213.020 147.707 1.00 25.23  ? 2246 GLY A CA    1 
ATOM   6310  C  C     . GLY A 1 2246 ? 154.085 211.863 148.107 1.00 30.95  ? 2246 GLY A C     1 
ATOM   6311  O  O     . GLY A 1 2246 ? 152.891 212.071 148.349 1.00 35.53  ? 2246 GLY A O     1 
ATOM   6312  N  N     . VAL A 1 2247 ? 154.628 210.652 148.187 1.00 29.83  ? 2247 VAL A N     1 
ATOM   6313  C  CA    . VAL A 1 2247 ? 153.869 209.464 148.560 1.00 29.99  ? 2247 VAL A CA    1 
ATOM   6314  C  C     . VAL A 1 2247 ? 154.121 209.189 150.036 1.00 28.01  ? 2247 VAL A C     1 
ATOM   6315  O  O     . VAL A 1 2247 ? 155.274 209.055 150.462 1.00 25.39  ? 2247 VAL A O     1 
ATOM   6316  C  CB    . VAL A 1 2247 ? 154.260 208.254 147.698 1.00 26.87  ? 2247 VAL A CB    1 
ATOM   6317  C  CG1   . VAL A 1 2247 ? 153.438 207.036 148.090 1.00 24.04  ? 2247 VAL A CG1   1 
ATOM   6318  C  CG2   . VAL A 1 2247 ? 154.083 208.575 146.223 1.00 23.47  ? 2247 VAL A CG2   1 
ATOM   6319  N  N     . GLU A 1 2248 ? 153.045 209.100 150.815 1.00 27.90  ? 2248 GLU A N     1 
ATOM   6320  C  CA    . GLU A 1 2248 ? 153.181 208.886 152.249 1.00 27.36  ? 2248 GLU A CA    1 
ATOM   6321  C  C     . GLU A 1 2248 ? 153.709 207.486 152.534 1.00 24.27  ? 2248 GLU A C     1 
ATOM   6322  O  O     . GLU A 1 2248 ? 153.210 206.496 151.993 1.00 25.01  ? 2248 GLU A O     1 
ATOM   6323  C  CB    . GLU A 1 2248 ? 151.839 209.108 152.945 1.00 32.99  ? 2248 GLU A CB    1 
ATOM   6324  C  CG    . GLU A 1 2248 ? 151.914 209.042 154.461 1.00 39.04  ? 2248 GLU A CG    1 
ATOM   6325  C  CD    . GLU A 1 2248 ? 150.601 208.626 155.089 1.00 44.70  ? 2248 GLU A CD    1 
ATOM   6326  O  OE1   . GLU A 1 2248 ? 150.579 208.367 156.311 1.00 49.15  ? 2248 GLU A OE1   1 
ATOM   6327  O  OE2   . GLU A 1 2248 ? 149.586 208.577 154.365 1.00 39.07  ? 2248 GLU A OE2   1 
ATOM   6328  N  N     . GLY A 1 2249 ? 154.728 207.410 153.390 1.00 23.94  ? 2249 GLY A N     1 
ATOM   6329  C  CA    . GLY A 1 2249 ? 155.379 206.161 153.705 1.00 15.90  ? 2249 GLY A CA    1 
ATOM   6330  C  C     . GLY A 1 2249 ? 154.942 205.625 155.051 1.00 14.80  ? 2249 GLY A C     1 
ATOM   6331  O  O     . GLY A 1 2249 ? 154.977 206.337 156.057 1.00 18.58  ? 2249 GLY A O     1 
ATOM   6332  N  N     . VAL A 1 2250 ? 154.528 204.361 155.064 1.00 12.54  ? 2250 VAL A N     1 
ATOM   6333  C  CA    . VAL A 1 2250 ? 154.078 203.679 156.271 1.00 10.65  ? 2250 VAL A CA    1 
ATOM   6334  C  C     . VAL A 1 2250 ? 154.976 202.472 156.496 1.00 9.49   ? 2250 VAL A C     1 
ATOM   6335  O  O     . VAL A 1 2250 ? 155.185 201.670 155.579 1.00 10.23  ? 2250 VAL A O     1 
ATOM   6336  C  CB    . VAL A 1 2250 ? 152.602 203.252 156.167 1.00 13.20  ? 2250 VAL A CB    1 
ATOM   6337  C  CG1   . VAL A 1 2250 ? 152.163 202.547 157.440 1.00 11.45  ? 2250 VAL A CG1   1 
ATOM   6338  C  CG2   . VAL A 1 2250 ? 151.720 204.457 155.886 1.00 15.99  ? 2250 VAL A CG2   1 
ATOM   6339  N  N     . ALA A 1 2251 ? 155.505 202.347 157.709 1.00 7.93   ? 2251 ALA A N     1 
ATOM   6340  C  CA    . ALA A 1 2251 ? 156.407 201.262 158.067 1.00 3.76   ? 2251 ALA A CA    1 
ATOM   6341  C  C     . ALA A 1 2251 ? 155.755 200.380 159.119 1.00 4.04   ? 2251 ALA A C     1 
ATOM   6342  O  O     . ALA A 1 2251 ? 155.310 200.873 160.161 1.00 7.20   ? 2251 ALA A O     1 
ATOM   6343  C  CB    . ALA A 1 2251 ? 157.741 201.803 158.584 1.00 3.71   ? 2251 ALA A CB    1 
ATOM   6344  N  N     . HIS A 1 2252 ? 155.702 199.080 158.845 1.00 3.34   ? 2252 HIS A N     1 
ATOM   6345  C  CA    . HIS A 1 2252 ? 155.212 198.083 159.792 1.00 3.16   ? 2252 HIS A CA    1 
ATOM   6346  C  C     . HIS A 1 2252 ? 156.395 197.227 160.220 1.00 4.44   ? 2252 HIS A C     1 
ATOM   6347  O  O     . HIS A 1 2252 ? 156.906 196.425 159.432 1.00 5.31   ? 2252 HIS A O     1 
ATOM   6348  C  CB    . HIS A 1 2252 ? 154.106 197.229 159.176 1.00 3.83   ? 2252 HIS A CB    1 
ATOM   6349  C  CG    . HIS A 1 2252 ? 153.087 198.018 158.415 1.00 4.02   ? 2252 HIS A CG    1 
ATOM   6350  N  ND1   . HIS A 1 2252 ? 151.875 198.386 158.958 1.00 4.08   ? 2252 HIS A ND1   1 
ATOM   6351  C  CD2   . HIS A 1 2252 ? 153.098 198.508 157.153 1.00 6.09   ? 2252 HIS A CD2   1 
ATOM   6352  C  CE1   . HIS A 1 2252 ? 151.184 199.071 158.065 1.00 7.11   ? 2252 HIS A CE1   1 
ATOM   6353  N  NE2   . HIS A 1 2252 ? 151.904 199.159 156.961 1.00 10.41  ? 2252 HIS A NE2   1 
ATOM   6354  N  N     . ILE A 1 2253 ? 156.826 197.393 161.465 1.00 4.60   ? 2253 ILE A N     1 
ATOM   6355  C  CA    . ILE A 1 2253 ? 157.976 196.676 162.000 1.00 3.52   ? 2253 ILE A CA    1 
ATOM   6356  C  C     . ILE A 1 2253 ? 157.466 195.492 162.806 1.00 5.45   ? 2253 ILE A C     1 
ATOM   6357  O  O     . ILE A 1 2253 ? 156.671 195.659 163.738 1.00 8.84   ? 2253 ILE A O     1 
ATOM   6358  C  CB    . ILE A 1 2253 ? 158.859 197.593 162.858 1.00 3.90   ? 2253 ILE A CB    1 
ATOM   6359  C  CG1   . ILE A 1 2253 ? 159.007 198.957 162.188 1.00 4.61   ? 2253 ILE A CG1   1 
ATOM   6360  C  CG2   . ILE A 1 2253 ? 160.223 196.960 163.079 1.00 6.86   ? 2253 ILE A CG2   1 
ATOM   6361  C  CD1   . ILE A 1 2253 ? 159.719 199.970 163.039 1.00 9.08   ? 2253 ILE A CD1   1 
ATOM   6362  N  N     . ILE A 1 2254 ? 157.922 194.296 162.447 1.00 4.27   ? 2254 ILE A N     1 
ATOM   6363  C  CA    . ILE A 1 2254 ? 157.518 193.060 163.102 1.00 5.15   ? 2254 ILE A CA    1 
ATOM   6364  C  C     . ILE A 1 2254 ? 158.764 192.360 163.622 1.00 9.68   ? 2254 ILE A C     1 
ATOM   6365  O  O     . ILE A 1 2254 ? 159.741 192.195 162.883 1.00 9.43   ? 2254 ILE A O     1 
ATOM   6366  C  CB    . ILE A 1 2254 ? 156.740 192.138 162.145 1.00 5.91   ? 2254 ILE A CB    1 
ATOM   6367  C  CG1   . ILE A 1 2254 ? 155.462 192.822 161.656 1.00 8.50   ? 2254 ILE A CG1   1 
ATOM   6368  C  CG2   . ILE A 1 2254 ? 156.418 190.814 162.820 1.00 8.93   ? 2254 ILE A CG2   1 
ATOM   6369  C  CD1   . ILE A 1 2254 ? 154.759 192.073 160.549 1.00 4.95   ? 2254 ILE A CD1   1 
ATOM   6370  N  N     . ASP A 1 2255 ? 158.734 191.964 164.892 1.00 13.59  ? 2255 ASP A N     1 
ATOM   6371  C  CA    . ASP A 1 2255 ? 159.750 191.068 165.425 1.00 8.96   ? 2255 ASP A CA    1 
ATOM   6372  C  C     . ASP A 1 2255 ? 159.255 189.638 165.263 1.00 10.10  ? 2255 ASP A C     1 
ATOM   6373  O  O     . ASP A 1 2255 ? 158.451 189.162 166.074 1.00 11.31  ? 2255 ASP A O     1 
ATOM   6374  C  CB    . ASP A 1 2255 ? 160.049 191.381 166.890 1.00 10.35  ? 2255 ASP A CB    1 
ATOM   6375  C  CG    . ASP A 1 2255 ? 161.443 190.953 167.307 1.00 18.36  ? 2255 ASP A CG    1 
ATOM   6376  O  OD1   . ASP A 1 2255 ? 161.859 189.833 166.943 1.00 15.05  ? 2255 ASP A OD1   1 
ATOM   6377  O  OD2   . ASP A 1 2255 ? 162.122 191.734 168.006 1.00 30.84  ? 2255 ASP A OD2   1 
ATOM   6378  N  N     . PRO A 1 2256 ? 159.700 188.929 164.222 1.00 9.60   ? 2256 PRO A N     1 
ATOM   6379  C  CA    . PRO A 1 2256 ? 159.154 187.589 163.957 1.00 7.56   ? 2256 PRO A CA    1 
ATOM   6380  C  C     . PRO A 1 2256 ? 159.415 186.587 165.064 1.00 9.13   ? 2256 PRO A C     1 
ATOM   6381  O  O     . PRO A 1 2256 ? 158.581 185.700 165.278 1.00 11.80  ? 2256 PRO A O     1 
ATOM   6382  C  CB    . PRO A 1 2256 ? 159.857 187.180 162.658 1.00 5.83   ? 2256 PRO A CB    1 
ATOM   6383  C  CG    . PRO A 1 2256 ? 161.142 187.930 162.693 1.00 6.37   ? 2256 PRO A CG    1 
ATOM   6384  C  CD    . PRO A 1 2256 ? 160.828 189.251 163.332 1.00 8.22   ? 2256 PRO A CD    1 
ATOM   6385  N  N     . LYS A 1 2257 ? 160.537 186.695 165.773 1.00 7.67   ? 2257 LYS A N     1 
ATOM   6386  C  CA    . LYS A 1 2257 ? 160.882 185.736 166.809 1.00 7.07   ? 2257 LYS A CA    1 
ATOM   6387  C  C     . LYS A 1 2257 ? 160.462 186.178 168.203 1.00 11.04  ? 2257 LYS A C     1 
ATOM   6388  O  O     . LYS A 1 2257 ? 160.681 185.431 169.161 1.00 11.76  ? 2257 LYS A O     1 
ATOM   6389  C  CB    . LYS A 1 2257 ? 162.388 185.456 166.788 1.00 11.61  ? 2257 LYS A CB    1 
ATOM   6390  C  CG    . LYS A 1 2257 ? 162.881 184.977 165.438 1.00 8.42   ? 2257 LYS A CG    1 
ATOM   6391  C  CD    . LYS A 1 2257 ? 162.895 183.465 165.373 1.00 6.98   ? 2257 LYS A CD    1 
ATOM   6392  C  CE    . LYS A 1 2257 ? 164.211 182.902 165.865 1.00 9.25   ? 2257 LYS A CE    1 
ATOM   6393  N  NZ    . LYS A 1 2257 ? 164.265 181.423 165.723 1.00 11.75  ? 2257 LYS A NZ    1 
ATOM   6394  N  N     . ALA A 1 2258 ? 159.872 187.365 168.341 1.00 10.39  ? 2258 ALA A N     1 
ATOM   6395  C  CA    . ALA A 1 2258 ? 159.281 187.773 169.607 1.00 7.79   ? 2258 ALA A CA    1 
ATOM   6396  C  C     . ALA A 1 2258 ? 157.912 187.150 169.836 1.00 8.29   ? 2258 ALA A C     1 
ATOM   6397  O  O     . ALA A 1 2258 ? 157.387 187.237 170.951 1.00 14.17  ? 2258 ALA A O     1 
ATOM   6398  C  CB    . ALA A 1 2258 ? 159.169 189.296 169.676 1.00 6.87   ? 2258 ALA A CB    1 
ATOM   6399  N  N     . ILE A 1 2259 ? 157.329 186.531 168.811 1.00 9.79   ? 2259 ILE A N     1 
ATOM   6400  C  CA    . ILE A 1 2259 ? 156.051 185.844 168.914 1.00 10.20  ? 2259 ILE A CA    1 
ATOM   6401  C  C     . ILE A 1 2259 ? 156.209 184.456 168.310 1.00 11.12  ? 2259 ILE A C     1 
ATOM   6402  O  O     . ILE A 1 2259 ? 157.236 184.125 167.714 1.00 11.49  ? 2259 ILE A O     1 
ATOM   6403  C  CB    . ILE A 1 2259 ? 154.913 186.608 168.206 1.00 9.21   ? 2259 ILE A CB    1 
ATOM   6404  C  CG1   . ILE A 1 2259 ? 155.277 186.866 166.743 1.00 8.80   ? 2259 ILE A CG1   1 
ATOM   6405  C  CG2   . ILE A 1 2259 ? 154.623 187.916 168.923 1.00 8.14   ? 2259 ILE A CG2   1 
ATOM   6406  C  CD1   . ILE A 1 2259 ? 154.301 187.760 166.019 1.00 8.35   ? 2259 ILE A CD1   1 
ATOM   6407  N  N     . SER A 1 2260 ? 155.173 183.640 168.475 1.00 10.67  ? 2260 SER A N     1 
ATOM   6408  C  CA    . SER A 1 2260 ? 155.180 182.315 167.880 1.00 10.36  ? 2260 SER A CA    1 
ATOM   6409  C  C     . SER A 1 2260 ? 154.903 182.403 166.382 1.00 10.52  ? 2260 SER A C     1 
ATOM   6410  O  O     . SER A 1 2260 ? 154.376 183.398 165.875 1.00 12.09  ? 2260 SER A O     1 
ATOM   6411  C  CB    . SER A 1 2260 ? 154.143 181.415 168.554 1.00 14.71  ? 2260 SER A CB    1 
ATOM   6412  O  OG    . SER A 1 2260 ? 152.826 181.866 168.290 1.00 21.55  ? 2260 SER A OG    1 
ATOM   6413  N  N     . LYS A 1 2261 ? 155.276 181.339 165.668 1.00 11.39  ? 2261 LYS A N     1 
ATOM   6414  C  CA    . LYS A 1 2261 ? 155.028 181.297 164.231 1.00 9.09   ? 2261 LYS A CA    1 
ATOM   6415  C  C     . LYS A 1 2261 ? 153.537 181.258 163.926 1.00 10.65  ? 2261 LYS A C     1 
ATOM   6416  O  O     . LYS A 1 2261 ? 153.101 181.768 162.887 1.00 10.45  ? 2261 LYS A O     1 
ATOM   6417  C  CB    . LYS A 1 2261 ? 155.735 180.091 163.612 1.00 9.48   ? 2261 LYS A CB    1 
ATOM   6418  C  CG    . LYS A 1 2261 ? 155.742 180.090 162.094 1.00 11.27  ? 2261 LYS A CG    1 
ATOM   6419  C  CD    . LYS A 1 2261 ? 156.507 178.901 161.544 1.00 12.32  ? 2261 LYS A CD    1 
ATOM   6420  C  CE    . LYS A 1 2261 ? 156.090 178.594 160.117 1.00 15.61  ? 2261 LYS A CE    1 
ATOM   6421  N  NZ    . LYS A 1 2261 ? 156.703 177.334 159.620 1.00 19.77  ? 2261 LYS A NZ    1 
ATOM   6422  N  N     . ASP A 1 2262 ? 152.743 180.655 164.815 1.00 14.10  ? 2262 ASP A N     1 
ATOM   6423  C  CA    . ASP A 1 2262 ? 151.293 180.681 164.652 1.00 11.37  ? 2262 ASP A CA    1 
ATOM   6424  C  C     . ASP A 1 2262 ? 150.754 182.103 164.736 1.00 12.46  ? 2262 ASP A C     1 
ATOM   6425  O  O     . ASP A 1 2262 ? 149.865 182.486 163.967 1.00 12.35  ? 2262 ASP A O     1 
ATOM   6426  C  CB    . ASP A 1 2262 ? 150.631 179.793 165.705 1.00 12.24  ? 2262 ASP A CB    1 
ATOM   6427  C  CG    . ASP A 1 2262 ? 150.600 178.332 165.301 1.00 28.37  ? 2262 ASP A CG    1 
ATOM   6428  O  OD1   . ASP A 1 2262 ? 150.565 177.467 166.200 1.00 32.16  ? 2262 ASP A OD1   1 
ATOM   6429  O  OD2   . ASP A 1 2262 ? 150.605 178.049 164.085 1.00 27.70  ? 2262 ASP A OD2   1 
ATOM   6430  N  N     . HIS A 1 2263 ? 151.278 182.901 165.667 1.00 11.48  ? 2263 HIS A N     1 
ATOM   6431  C  CA    . HIS A 1 2263 ? 150.851 184.286 165.811 1.00 9.93   ? 2263 HIS A CA    1 
ATOM   6432  C  C     . HIS A 1 2263 ? 151.411 185.197 164.728 1.00 8.56   ? 2263 HIS A C     1 
ATOM   6433  O  O     . HIS A 1 2263 ? 150.910 186.314 164.563 1.00 8.63   ? 2263 HIS A O     1 
ATOM   6434  C  CB    . HIS A 1 2263 ? 151.260 184.824 167.185 1.00 12.35  ? 2263 HIS A CB    1 
ATOM   6435  C  CG    . HIS A 1 2263 ? 150.456 184.265 168.317 1.00 17.67  ? 2263 HIS A CG    1 
ATOM   6436  N  ND1   . HIS A 1 2263 ? 149.110 183.992 168.211 1.00 18.00  ? 2263 HIS A ND1   1 
ATOM   6437  C  CD2   . HIS A 1 2263 ? 150.810 183.930 169.580 1.00 19.69  ? 2263 HIS A CD2   1 
ATOM   6438  C  CE1   . HIS A 1 2263 ? 148.669 183.512 169.360 1.00 20.01  ? 2263 HIS A CE1   1 
ATOM   6439  N  NE2   . HIS A 1 2263 ? 149.680 183.464 170.208 1.00 20.27  ? 2263 HIS A NE2   1 
ATOM   6440  N  N     . LEU A 1 2264 ? 152.430 184.753 163.994 1.00 8.72   ? 2264 LEU A N     1 
ATOM   6441  C  CA    . LEU A 1 2264 ? 153.036 185.567 162.947 1.00 6.88   ? 2264 LEU A CA    1 
ATOM   6442  C  C     . LEU A 1 2264 ? 152.321 185.419 161.611 1.00 5.65   ? 2264 LEU A C     1 
ATOM   6443  O  O     . LEU A 1 2264 ? 152.187 186.398 160.868 1.00 6.85   ? 2264 LEU A O     1 
ATOM   6444  C  CB    . LEU A 1 2264 ? 154.514 185.199 162.790 1.00 6.44   ? 2264 LEU A CB    1 
ATOM   6445  C  CG    . LEU A 1 2264 ? 155.274 185.847 161.633 1.00 5.16   ? 2264 LEU A CG    1 
ATOM   6446  C  CD1   . LEU A 1 2264 ? 155.418 187.340 161.863 1.00 5.35   ? 2264 LEU A CD1   1 
ATOM   6447  C  CD2   . LEU A 1 2264 ? 156.633 185.197 161.453 1.00 3.87   ? 2264 LEU A CD2   1 
ATOM   6448  N  N     . TYR A 1 2265 ? 151.851 184.215 161.291 1.00 5.54   ? 2265 TYR A N     1 
ATOM   6449  C  CA    . TYR A 1 2265 ? 151.231 183.940 160.003 1.00 5.75   ? 2265 TYR A CA    1 
ATOM   6450  C  C     . TYR A 1 2265 ? 149.754 183.598 160.094 1.00 6.75   ? 2265 TYR A C     1 
ATOM   6451  O  O     . TYR A 1 2265 ? 149.010 183.885 159.155 1.00 6.81   ? 2265 TYR A O     1 
ATOM   6452  C  CB    . TYR A 1 2265 ? 151.958 182.786 159.302 1.00 5.04   ? 2265 TYR A CB    1 
ATOM   6453  C  CG    . TYR A 1 2265 ? 153.341 183.145 158.817 1.00 5.39   ? 2265 TYR A CG    1 
ATOM   6454  C  CD1   . TYR A 1 2265 ? 153.527 184.120 157.849 1.00 4.83   ? 2265 TYR A CD1   1 
ATOM   6455  C  CD2   . TYR A 1 2265 ? 154.461 182.511 159.330 1.00 6.24   ? 2265 TYR A CD2   1 
ATOM   6456  C  CE1   . TYR A 1 2265 ? 154.789 184.451 157.405 1.00 5.34   ? 2265 TYR A CE1   1 
ATOM   6457  C  CE2   . TYR A 1 2265 ? 155.726 182.835 158.892 1.00 5.89   ? 2265 TYR A CE2   1 
ATOM   6458  C  CZ    . TYR A 1 2265 ? 155.885 183.805 157.930 1.00 5.70   ? 2265 TYR A CZ    1 
ATOM   6459  O  OH    . TYR A 1 2265 ? 157.147 184.128 157.492 1.00 9.39   ? 2265 TYR A OH    1 
ATOM   6460  N  N     . GLY A 1 2266 ? 149.315 182.998 161.192 1.00 6.79   ? 2266 GLY A N     1 
ATOM   6461  C  CA    . GLY A 1 2266 ? 147.941 182.569 161.348 1.00 5.91   ? 2266 GLY A CA    1 
ATOM   6462  C  C     . GLY A 1 2266 ? 147.851 181.104 161.724 1.00 10.13  ? 2266 GLY A C     1 
ATOM   6463  O  O     . GLY A 1 2266 ? 148.803 180.335 161.604 1.00 11.53  ? 2266 GLY A O     1 
ATOM   6464  N  N     . THR A 1 2267 ? 146.661 180.731 162.187 1.00 13.82  ? 2267 THR A N     1 
ATOM   6465  C  CA    . THR A 1 2267 ? 146.402 179.385 162.677 1.00 16.05  ? 2267 THR A CA    1 
ATOM   6466  C  C     . THR A 1 2267 ? 145.117 178.861 162.056 1.00 15.78  ? 2267 THR A C     1 
ATOM   6467  O  O     . THR A 1 2267 ? 144.122 179.588 161.970 1.00 13.68  ? 2267 THR A O     1 
ATOM   6468  C  CB    . THR A 1 2267 ? 146.296 179.369 164.208 1.00 15.07  ? 2267 THR A CB    1 
ATOM   6469  O  OG1   . THR A 1 2267 ? 147.557 179.734 164.779 1.00 11.79  ? 2267 THR A OG1   1 
ATOM   6470  C  CG2   . THR A 1 2267 ? 145.907 177.988 164.712 1.00 20.52  ? 2267 THR A CG2   1 
ATOM   6471  N  N     . LEU A 1 2268 ? 145.143 177.605 161.621 1.00 17.57  ? 2268 LEU A N     1 
ATOM   6472  C  CA    . LEU A 1 2268 ? 143.953 176.909 161.151 1.00 18.52  ? 2268 LEU A CA    1 
ATOM   6473  C  C     . LEU A 1 2268 ? 143.437 176.033 162.284 1.00 26.54  ? 2268 LEU A C     1 
ATOM   6474  O  O     . LEU A 1 2268 ? 144.153 175.146 162.763 1.00 31.34  ? 2268 LEU A O     1 
ATOM   6475  C  CB    . LEU A 1 2268 ? 144.262 176.071 159.911 1.00 22.44  ? 2268 LEU A CB    1 
ATOM   6476  C  CG    . LEU A 1 2268 ? 143.107 175.786 158.948 1.00 26.08  ? 2268 LEU A CG    1 
ATOM   6477  C  CD1   . LEU A 1 2268 ? 142.278 177.036 158.710 1.00 23.96  ? 2268 LEU A CD1   1 
ATOM   6478  C  CD2   . LEU A 1 2268 ? 143.636 175.238 157.634 1.00 22.04  ? 2268 LEU A CD2   1 
ATOM   6479  N  N     . ASP A 1 2269 ? 142.209 176.286 162.713 1.00 34.46  ? 2269 ASP A N     1 
ATOM   6480  C  CA    . ASP A 1 2269 ? 141.627 175.531 163.816 1.00 39.61  ? 2269 ASP A CA    1 
ATOM   6481  C  C     . ASP A 1 2269 ? 141.404 174.088 163.382 1.00 45.46  ? 2269 ASP A C     1 
ATOM   6482  O  O     . ASP A 1 2269 ? 140.683 173.851 162.405 1.00 46.56  ? 2269 ASP A O     1 
ATOM   6483  C  CB    . ASP A 1 2269 ? 140.312 176.170 164.251 1.00 39.34  ? 2269 ASP A CB    1 
ATOM   6484  C  CG    . ASP A 1 2269 ? 139.999 175.931 165.716 1.00 53.26  ? 2269 ASP A CG    1 
ATOM   6485  O  OD1   . ASP A 1 2269 ? 140.639 175.055 166.333 1.00 49.73  ? 2269 ASP A OD1   1 
ATOM   6486  O  OD2   . ASP A 1 2269 ? 139.111 176.625 166.253 1.00 59.28  ? 2269 ASP A OD2   1 
ATOM   6487  N  N     . PRO A 1 2270 ? 142.000 173.103 164.057 1.00 45.12  ? 2270 PRO A N     1 
ATOM   6488  C  CA    . PRO A 1 2270 ? 141.816 171.706 163.628 1.00 47.23  ? 2270 PRO A CA    1 
ATOM   6489  C  C     . PRO A 1 2270 ? 140.381 171.219 163.715 1.00 49.59  ? 2270 PRO A C     1 
ATOM   6490  O  O     . PRO A 1 2270 ? 140.026 170.265 163.012 1.00 49.03  ? 2270 PRO A O     1 
ATOM   6491  C  CB    . PRO A 1 2270 ? 142.734 170.923 164.579 1.00 50.09  ? 2270 PRO A CB    1 
ATOM   6492  C  CG    . PRO A 1 2270 ? 142.947 171.830 165.748 1.00 43.98  ? 2270 PRO A CG    1 
ATOM   6493  C  CD    . PRO A 1 2270 ? 142.929 173.218 165.192 1.00 42.70  ? 2270 PRO A CD    1 
ATOM   6494  N  N     . ASN A 1 2271 ? 139.543 171.839 164.545 1.00 51.83  ? 2271 ASN A N     1 
ATOM   6495  C  CA    . ASN A 1 2271 ? 138.170 171.381 164.730 1.00 46.81  ? 2271 ASN A CA    1 
ATOM   6496  C  C     . ASN A 1 2271 ? 137.212 172.013 163.722 1.00 47.78  ? 2271 ASN A C     1 
ATOM   6497  O  O     . ASN A 1 2271 ? 136.567 171.306 162.941 1.00 48.39  ? 2271 ASN A O     1 
ATOM   6498  C  CB    . ASN A 1 2271 ? 137.713 171.673 166.163 1.00 49.16  ? 2271 ASN A CB    1 
ATOM   6499  C  CG    . ASN A 1 2271 ? 138.739 171.255 167.198 1.00 55.46  ? 2271 ASN A CG    1 
ATOM   6500  O  OD1   . ASN A 1 2271 ? 139.209 170.118 167.196 1.00 57.19  ? 2271 ASN A OD1   1 
ATOM   6501  N  ND2   . ASN A 1 2271 ? 139.091 172.175 168.088 1.00 51.03  ? 2271 ASN A ND2   1 
ATOM   6502  N  N     . THR A 1 2272 ? 137.108 173.340 163.729 1.00 45.56  ? 2272 THR A N     1 
ATOM   6503  C  CA    . THR A 1 2272 ? 136.153 174.044 162.883 1.00 45.54  ? 2272 THR A CA    1 
ATOM   6504  C  C     . THR A 1 2272 ? 136.739 174.479 161.546 1.00 45.95  ? 2272 THR A C     1 
ATOM   6505  O  O     . THR A 1 2272 ? 135.999 175.007 160.709 1.00 41.93  ? 2272 THR A O     1 
ATOM   6506  C  CB    . THR A 1 2272 ? 135.596 175.267 163.621 1.00 47.09  ? 2272 THR A CB    1 
ATOM   6507  O  OG1   . THR A 1 2272 ? 134.586 175.893 162.819 1.00 56.66  ? 2272 THR A OG1   1 
ATOM   6508  C  CG2   . THR A 1 2272 ? 136.701 176.266 163.910 1.00 42.80  ? 2272 THR A CG2   1 
ATOM   6509  N  N     . ARG A 1 2273 ? 138.039 174.268 161.326 1.00 45.56  ? 2273 ARG A N     1 
ATOM   6510  C  CA    . ARG A 1 2273 ? 138.701 174.606 160.063 1.00 38.43  ? 2273 ARG A CA    1 
ATOM   6511  C  C     . ARG A 1 2273 ? 138.530 176.084 159.718 1.00 35.63  ? 2273 ARG A C     1 
ATOM   6512  O  O     . ARG A 1 2273 ? 138.369 176.455 158.554 1.00 33.07  ? 2273 ARG A O     1 
ATOM   6513  C  CB    . ARG A 1 2273 ? 138.199 173.719 158.921 1.00 39.49  ? 2273 ARG A CB    1 
ATOM   6514  C  CG    . ARG A 1 2273 ? 138.251 172.228 159.221 1.00 38.80  ? 2273 ARG A CG    1 
ATOM   6515  C  CD    . ARG A 1 2273 ? 139.614 171.805 159.746 1.00 38.05  ? 2273 ARG A CD    1 
ATOM   6516  N  NE    . ARG A 1 2273 ? 140.662 171.979 158.749 1.00 34.01  ? 2273 ARG A NE    1 
ATOM   6517  C  CZ    . ARG A 1 2273 ? 141.955 171.797 158.981 1.00 30.71  ? 2273 ARG A CZ    1 
ATOM   6518  N  NH1   . ARG A 1 2273 ? 142.398 171.431 160.172 1.00 34.26  ? 2273 ARG A NH1   1 
ATOM   6519  N  NH2   . ARG A 1 2273 ? 142.824 171.982 157.992 1.00 27.09  ? 2273 ARG A NH2   1 
ATOM   6520  N  N     . GLU A 1 2274 ? 138.565 176.935 160.739 1.00 40.22  ? 2274 GLU A N     1 
ATOM   6521  C  CA    . GLU A 1 2274 ? 138.449 178.375 160.566 1.00 35.41  ? 2274 GLU A CA    1 
ATOM   6522  C  C     . GLU A 1 2274 ? 139.830 179.013 160.630 1.00 28.14  ? 2274 GLU A C     1 
ATOM   6523  O  O     . GLU A 1 2274 ? 140.674 178.614 161.437 1.00 28.30  ? 2274 GLU A O     1 
ATOM   6524  C  CB    . GLU A 1 2274 ? 137.537 178.984 161.633 1.00 37.75  ? 2274 GLU A CB    1 
ATOM   6525  C  CG    . GLU A 1 2274 ? 137.227 180.457 161.421 1.00 41.63  ? 2274 GLU A CG    1 
ATOM   6526  C  CD    . GLU A 1 2274 ? 135.826 180.826 161.866 1.00 59.46  ? 2274 GLU A CD    1 
ATOM   6527  O  OE1   . GLU A 1 2274 ? 135.467 180.519 163.021 1.00 66.95  ? 2274 GLU A OE1   1 
ATOM   6528  O  OE2   . GLU A 1 2274 ? 135.084 181.423 161.058 1.00 58.73  ? 2274 GLU A OE2   1 
ATOM   6529  N  N     . TRP A 1 2275 ? 140.055 180.004 159.772 1.00 22.71  ? 2275 TRP A N     1 
ATOM   6530  C  CA    . TRP A 1 2275 ? 141.349 180.661 159.668 1.00 18.38  ? 2275 TRP A CA    1 
ATOM   6531  C  C     . TRP A 1 2275 ? 141.344 181.977 160.435 1.00 17.81  ? 2275 TRP A C     1 
ATOM   6532  O  O     . TRP A 1 2275 ? 140.476 182.828 160.218 1.00 23.12  ? 2275 TRP A O     1 
ATOM   6533  C  CB    . TRP A 1 2275 ? 141.708 180.914 158.203 1.00 16.64  ? 2275 TRP A CB    1 
ATOM   6534  C  CG    . TRP A 1 2275 ? 142.942 181.741 158.029 1.00 12.99  ? 2275 TRP A CG    1 
ATOM   6535  C  CD1   . TRP A 1 2275 ? 143.002 183.076 157.757 1.00 12.61  ? 2275 TRP A CD1   1 
ATOM   6536  C  CD2   . TRP A 1 2275 ? 144.298 181.289 158.118 1.00 11.99  ? 2275 TRP A CD2   1 
ATOM   6537  N  NE1   . TRP A 1 2275 ? 144.309 183.485 157.671 1.00 13.40  ? 2275 TRP A NE1   1 
ATOM   6538  C  CE2   . TRP A 1 2275 ? 145.125 182.406 157.888 1.00 9.88   ? 2275 TRP A CE2   1 
ATOM   6539  C  CE3   . TRP A 1 2275 ? 144.892 180.050 158.369 1.00 11.66  ? 2275 TRP A CE3   1 
ATOM   6540  C  CZ2   . TRP A 1 2275 ? 146.514 182.321 157.902 1.00 7.31   ? 2275 TRP A CZ2   1 
ATOM   6541  C  CZ3   . TRP A 1 2275 ? 146.271 179.967 158.382 1.00 12.55  ? 2275 TRP A CZ3   1 
ATOM   6542  C  CH2   . TRP A 1 2275 ? 147.067 181.095 158.150 1.00 11.33  ? 2275 TRP A CH2   1 
ATOM   6543  N  N     . THR A 1 2276 ? 142.314 182.136 161.331 1.00 13.18  ? 2276 THR A N     1 
ATOM   6544  C  CA    . THR A 1 2276 ? 142.569 183.400 162.009 1.00 11.18  ? 2276 THR A CA    1 
ATOM   6545  C  C     . THR A 1 2276 ? 143.883 183.962 161.482 1.00 10.75  ? 2276 THR A C     1 
ATOM   6546  O  O     . THR A 1 2276 ? 144.849 183.216 161.290 1.00 9.89   ? 2276 THR A O     1 
ATOM   6547  C  CB    . THR A 1 2276 ? 142.609 183.226 163.529 1.00 13.66  ? 2276 THR A CB    1 
ATOM   6548  O  OG1   . THR A 1 2276 ? 142.935 184.477 164.148 1.00 14.43  ? 2276 THR A OG1   1 
ATOM   6549  C  CG2   . THR A 1 2276 ? 143.628 182.172 163.940 1.00 13.91  ? 2276 THR A CG2   1 
ATOM   6550  N  N     . ASP A 1 2277 ? 143.908 185.265 161.223 1.00 11.87  ? 2277 ASP A N     1 
ATOM   6551  C  CA    . ASP A 1 2277 ? 145.080 185.884 160.623 1.00 8.20   ? 2277 ASP A CA    1 
ATOM   6552  C  C     . ASP A 1 2277 ? 146.194 186.051 161.647 1.00 8.51   ? 2277 ASP A C     1 
ATOM   6553  O  O     . ASP A 1 2277 ? 145.944 186.254 162.838 1.00 14.96  ? 2277 ASP A O     1 
ATOM   6554  C  CB    . ASP A 1 2277 ? 144.717 187.242 160.025 1.00 9.77   ? 2277 ASP A CB    1 
ATOM   6555  C  CG    . ASP A 1 2277 ? 144.431 187.166 158.543 1.00 13.22  ? 2277 ASP A CG    1 
ATOM   6556  O  OD1   . ASP A 1 2277 ? 144.528 186.059 157.975 1.00 17.22  ? 2277 ASP A OD1   1 
ATOM   6557  O  OD2   . ASP A 1 2277 ? 144.109 188.213 157.945 1.00 14.52  ? 2277 ASP A OD2   1 
ATOM   6558  N  N     . GLY A 1 2278 ? 147.433 185.965 161.172 1.00 7.08   ? 2278 GLY A N     1 
ATOM   6559  C  CA    . GLY A 1 2278 ? 148.592 186.255 161.987 1.00 5.27   ? 2278 GLY A CA    1 
ATOM   6560  C  C     . GLY A 1 2278 ? 148.952 187.724 161.917 1.00 5.78   ? 2278 GLY A C     1 
ATOM   6561  O  O     . GLY A 1 2278 ? 148.188 188.558 161.425 1.00 7.58   ? 2278 GLY A O     1 
ATOM   6562  N  N     . LEU A 1 2279 ? 150.145 188.043 162.417 1.00 6.93   ? 2279 LEU A N     1 
ATOM   6563  C  CA    . LEU A 1 2279 ? 150.588 189.433 162.433 1.00 5.74   ? 2279 LEU A CA    1 
ATOM   6564  C  C     . LEU A 1 2279 ? 150.934 189.915 161.029 1.00 5.88   ? 2279 LEU A C     1 
ATOM   6565  O  O     . LEU A 1 2279 ? 150.421 190.940 160.566 1.00 6.25   ? 2279 LEU A O     1 
ATOM   6566  C  CB    . LEU A 1 2279 ? 151.783 189.592 163.373 1.00 4.58   ? 2279 LEU A CB    1 
ATOM   6567  C  CG    . LEU A 1 2279 ? 152.288 191.021 163.566 1.00 4.84   ? 2279 LEU A CG    1 
ATOM   6568  C  CD1   . LEU A 1 2279 ? 151.128 191.967 163.825 1.00 6.96   ? 2279 LEU A CD1   1 
ATOM   6569  C  CD2   . LEU A 1 2279 ? 153.286 191.074 164.703 1.00 6.96   ? 2279 LEU A CD2   1 
ATOM   6570  N  N     . PHE A 1 2280 ? 151.812 189.187 160.336 1.00 5.01   ? 2280 PHE A N     1 
ATOM   6571  C  CA    . PHE A 1 2280 ? 152.177 189.568 158.976 1.00 4.62   ? 2280 PHE A CA    1 
ATOM   6572  C  C     . PHE A 1 2280 ? 150.990 189.434 158.031 1.00 5.57   ? 2280 PHE A C     1 
ATOM   6573  O  O     . PHE A 1 2280 ? 150.804 190.261 157.130 1.00 6.20   ? 2280 PHE A O     1 
ATOM   6574  C  CB    . PHE A 1 2280 ? 153.349 188.716 158.492 1.00 4.60   ? 2280 PHE A CB    1 
ATOM   6575  C  CG    . PHE A 1 2280 ? 153.677 188.909 157.042 1.00 4.32   ? 2280 PHE A CG    1 
ATOM   6576  C  CD1   . PHE A 1 2280 ? 154.226 190.098 156.596 1.00 4.64   ? 2280 PHE A CD1   1 
ATOM   6577  C  CD2   . PHE A 1 2280 ? 153.425 187.906 156.123 1.00 4.72   ? 2280 PHE A CD2   1 
ATOM   6578  C  CE1   . PHE A 1 2280 ? 154.527 190.280 155.263 1.00 4.99   ? 2280 PHE A CE1   1 
ATOM   6579  C  CE2   . PHE A 1 2280 ? 153.721 188.083 154.789 1.00 5.92   ? 2280 PHE A CE2   1 
ATOM   6580  C  CZ    . PHE A 1 2280 ? 154.272 189.271 154.357 1.00 6.61   ? 2280 PHE A CZ    1 
ATOM   6581  N  N     . THR A 1 2281 ? 150.180 188.389 158.216 1.00 4.53   ? 2281 THR A N     1 
ATOM   6582  C  CA    . THR A 1 2281 ? 149.027 188.174 157.348 1.00 3.85   ? 2281 THR A CA    1 
ATOM   6583  C  C     . THR A 1 2281 ? 148.011 189.302 157.482 1.00 5.69   ? 2281 THR A C     1 
ATOM   6584  O  O     . THR A 1 2281 ? 147.440 189.754 156.483 1.00 7.23   ? 2281 THR A O     1 
ATOM   6585  C  CB    . THR A 1 2281 ? 148.376 186.829 157.668 1.00 4.81   ? 2281 THR A CB    1 
ATOM   6586  O  OG1   . THR A 1 2281 ? 149.393 185.835 157.835 1.00 6.07   ? 2281 THR A OG1   1 
ATOM   6587  C  CG2   . THR A 1 2281 ? 147.446 186.406 156.540 1.00 6.84   ? 2281 THR A CG2   1 
ATOM   6588  N  N     . HIS A 1 2282 ? 147.766 189.765 158.711 1.00 5.64   ? 2282 HIS A N     1 
ATOM   6589  C  CA    . HIS A 1 2282 ? 146.780 190.821 158.920 1.00 6.39   ? 2282 HIS A CA    1 
ATOM   6590  C  C     . HIS A 1 2282 ? 147.230 192.133 158.291 1.00 7.03   ? 2282 HIS A C     1 
ATOM   6591  O  O     . HIS A 1 2282 ? 146.424 192.847 157.684 1.00 9.61   ? 2282 HIS A O     1 
ATOM   6592  C  CB    . HIS A 1 2282 ? 146.519 191.005 160.415 1.00 8.64   ? 2282 HIS A CB    1 
ATOM   6593  C  CG    . HIS A 1 2282 ? 145.853 192.300 160.759 1.00 13.79  ? 2282 HIS A CG    1 
ATOM   6594  N  ND1   . HIS A 1 2282 ? 144.500 192.508 160.594 1.00 15.89  ? 2282 HIS A ND1   1 
ATOM   6595  C  CD2   . HIS A 1 2282 ? 146.351 193.455 161.261 1.00 12.84  ? 2282 HIS A CD2   1 
ATOM   6596  C  CE1   . HIS A 1 2282 ? 144.195 193.734 160.978 1.00 14.70  ? 2282 HIS A CE1   1 
ATOM   6597  N  NE2   . HIS A 1 2282 ? 145.300 194.330 161.387 1.00 14.43  ? 2282 HIS A NE2   1 
ATOM   6598  N  N     . VAL A 1 2283 ? 148.513 192.471 158.434 1.00 6.23   ? 2283 VAL A N     1 
ATOM   6599  C  CA    . VAL A 1 2283 ? 149.030 193.702 157.842 1.00 4.89   ? 2283 VAL A CA    1 
ATOM   6600  C  C     . VAL A 1 2283 ? 148.947 193.635 156.322 1.00 6.26   ? 2283 VAL A C     1 
ATOM   6601  O  O     . VAL A 1 2283 ? 148.500 194.580 155.663 1.00 11.06  ? 2283 VAL A O     1 
ATOM   6602  C  CB    . VAL A 1 2283 ? 150.470 193.963 158.319 1.00 4.87   ? 2283 VAL A CB    1 
ATOM   6603  C  CG1   . VAL A 1 2283 ? 151.117 195.062 157.490 1.00 4.14   ? 2283 VAL A CG1   1 
ATOM   6604  C  CG2   . VAL A 1 2283 ? 150.483 194.326 159.796 1.00 4.98   ? 2283 VAL A CG2   1 
ATOM   6605  N  N     . LEU A 1 2284 ? 149.375 192.510 155.744 1.00 5.06   ? 2284 LEU A N     1 
ATOM   6606  C  CA    . LEU A 1 2284 ? 149.361 192.372 154.292 1.00 5.31   ? 2284 LEU A CA    1 
ATOM   6607  C  C     . LEU A 1 2284 ? 147.941 192.393 153.742 1.00 7.97   ? 2284 LEU A C     1 
ATOM   6608  O  O     . LEU A 1 2284 ? 147.675 193.041 152.723 1.00 10.42  ? 2284 LEU A O     1 
ATOM   6609  C  CB    . LEU A 1 2284 ? 150.078 191.087 153.880 1.00 5.77   ? 2284 LEU A CB    1 
ATOM   6610  C  CG    . LEU A 1 2284 ? 150.309 190.910 152.380 1.00 6.63   ? 2284 LEU A CG    1 
ATOM   6611  C  CD1   . LEU A 1 2284 ? 151.176 192.033 151.847 1.00 7.71   ? 2284 LEU A CD1   1 
ATOM   6612  C  CD2   . LEU A 1 2284 ? 150.940 189.561 152.092 1.00 8.36   ? 2284 LEU A CD2   1 
ATOM   6613  N  N     . ARG A 1 2285 ? 147.017 191.688 154.398 1.00 7.98   ? 2285 ARG A N     1 
ATOM   6614  C  CA    . ARG A 1 2285 ? 145.637 191.658 153.926 1.00 7.85   ? 2285 ARG A CA    1 
ATOM   6615  C  C     . ARG A 1 2285 ? 144.988 193.033 154.021 1.00 10.13  ? 2285 ARG A C     1 
ATOM   6616  O  O     . ARG A 1 2285 ? 144.226 193.428 153.132 1.00 16.73  ? 2285 ARG A O     1 
ATOM   6617  C  CB    . ARG A 1 2285 ? 144.834 190.628 154.716 1.00 10.29  ? 2285 ARG A CB    1 
ATOM   6618  C  CG    . ARG A 1 2285 ? 143.447 190.368 154.159 1.00 11.11  ? 2285 ARG A CG    1 
ATOM   6619  C  CD    . ARG A 1 2285 ? 142.612 189.554 155.127 1.00 10.59  ? 2285 ARG A CD    1 
ATOM   6620  N  NE    . ARG A 1 2285 ? 143.270 188.304 155.485 1.00 8.35   ? 2285 ARG A NE    1 
ATOM   6621  C  CZ    . ARG A 1 2285 ? 143.274 187.217 154.726 1.00 10.63  ? 2285 ARG A CZ    1 
ATOM   6622  N  NH1   . ARG A 1 2285 ? 142.665 187.190 153.553 1.00 15.52  ? 2285 ARG A NH1   1 
ATOM   6623  N  NH2   . ARG A 1 2285 ? 143.906 186.128 155.156 1.00 14.17  ? 2285 ARG A NH2   1 
ATOM   6624  N  N     . LYS A 1 2286 ? 145.277 193.773 155.093 1.00 10.27  ? 2286 LYS A N     1 
ATOM   6625  C  CA    . LYS A 1 2286 ? 144.721 195.115 155.238 1.00 10.80  ? 2286 LYS A CA    1 
ATOM   6626  C  C     . LYS A 1 2286 ? 145.206 196.033 154.124 1.00 12.80  ? 2286 LYS A C     1 
ATOM   6627  O  O     . LYS A 1 2286 ? 144.434 196.840 153.593 1.00 19.74  ? 2286 LYS A O     1 
ATOM   6628  C  CB    . LYS A 1 2286 ? 145.087 195.684 156.610 1.00 13.36  ? 2286 LYS A CB    1 
ATOM   6629  C  CG    . LYS A 1 2286 ? 144.896 197.184 156.745 1.00 20.38  ? 2286 LYS A CG    1 
ATOM   6630  C  CD    . LYS A 1 2286 ? 145.252 197.656 158.145 1.00 21.14  ? 2286 LYS A CD    1 
ATOM   6631  C  CE    . LYS A 1 2286 ? 144.096 197.454 159.110 1.00 22.29  ? 2286 LYS A CE    1 
ATOM   6632  N  NZ    . LYS A 1 2286 ? 142.955 198.362 158.813 1.00 29.69  ? 2286 LYS A NZ    1 
ATOM   6633  N  N     . ILE A 1 2287 ? 146.485 195.924 153.757 1.00 12.86  ? 2287 ILE A N     1 
ATOM   6634  C  CA    . ILE A 1 2287 ? 147.019 196.716 152.652 1.00 10.85  ? 2287 ILE A CA    1 
ATOM   6635  C  C     . ILE A 1 2287 ? 146.345 196.328 151.342 1.00 14.13  ? 2287 ILE A C     1 
ATOM   6636  O  O     . ILE A 1 2287 ? 145.974 197.192 150.538 1.00 19.67  ? 2287 ILE A O     1 
ATOM   6637  C  CB    . ILE A 1 2287 ? 148.548 196.550 152.573 1.00 9.56   ? 2287 ILE A CB    1 
ATOM   6638  C  CG1   . ILE A 1 2287 ? 149.213 197.155 153.809 1.00 11.18  ? 2287 ILE A CG1   1 
ATOM   6639  C  CG2   . ILE A 1 2287 ? 149.093 197.196 151.310 1.00 13.99  ? 2287 ILE A CG2   1 
ATOM   6640  C  CD1   . ILE A 1 2287 ? 150.665 196.772 153.967 1.00 10.12  ? 2287 ILE A CD1   1 
ATOM   6641  N  N     . ILE A 1 2288 ? 146.176 195.024 151.107 1.00 13.00  ? 2288 ILE A N     1 
ATOM   6642  C  CA    . ILE A 1 2288 ? 145.565 194.556 149.865 1.00 12.62  ? 2288 ILE A CA    1 
ATOM   6643  C  C     . ILE A 1 2288 ? 144.126 195.043 149.757 1.00 17.54  ? 2288 ILE A C     1 
ATOM   6644  O  O     . ILE A 1 2288 ? 143.685 195.493 148.692 1.00 23.41  ? 2288 ILE A O     1 
ATOM   6645  C  CB    . ILE A 1 2288 ? 145.652 193.021 149.774 1.00 12.98  ? 2288 ILE A CB    1 
ATOM   6646  C  CG1   . ILE A 1 2288 ? 147.098 192.579 149.551 1.00 11.61  ? 2288 ILE A CG1   1 
ATOM   6647  C  CG2   . ILE A 1 2288 ? 144.759 192.497 148.661 1.00 11.28  ? 2288 ILE A CG2   1 
ATOM   6648  C  CD1   . ILE A 1 2288 ? 147.345 191.126 149.883 1.00 7.26   ? 2288 ILE A CD1   1 
ATOM   6649  N  N     . ASP A 1 2289 ? 143.371 194.958 150.855 1.00 16.36  ? 2289 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2289 ? 141.993 195.438 150.843 1.00 18.26  ? 2289 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2289 ? 141.934 196.937 150.575 1.00 22.36  ? 2289 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2289 ? 141.064 197.408 149.833 1.00 24.93  ? 2289 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2289 ? 141.306 195.098 152.165 1.00 19.94  ? 2289 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2289 ? 141.288 193.607 152.445 1.00 28.65  ? 2289 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2289 ? 141.313 192.818 151.478 1.00 28.40  ? 2289 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2289 ? 141.252 193.223 153.632 1.00 25.89  ? 2289 ASP A OD2   1 
ATOM   6657  N  N     . SER A 1 2290 ? 142.856 197.698 151.170 1.00 21.29  ? 2290 SER A N     1 
ATOM   6658  C  CA    . SER A 1 2290 ? 142.973 199.140 150.945 1.00 22.09  ? 2290 SER A CA    1 
ATOM   6659  C  C     . SER A 1 2290 ? 141.659 199.860 151.243 1.00 23.37  ? 2290 SER A C     1 
ATOM   6660  O  O     . SER A 1 2290 ? 141.213 200.729 150.492 1.00 27.05  ? 2290 SER A O     1 
ATOM   6661  C  CB    . SER A 1 2290 ? 143.449 199.436 149.521 1.00 22.71  ? 2290 SER A CB    1 
ATOM   6662  O  OG    . SER A 1 2290 ? 143.727 200.815 149.352 1.00 25.40  ? 2290 SER A OG    1 
ATOM   6663  N  N     . VAL A 1 2291 ? 141.033 199.479 152.358 1.00 26.45  ? 2291 VAL A N     1 
ATOM   6664  C  CA    . VAL A 1 2291 ? 139.800 200.134 152.779 1.00 26.68  ? 2291 VAL A CA    1 
ATOM   6665  C  C     . VAL A 1 2291 ? 140.057 201.604 153.085 1.00 28.22  ? 2291 VAL A C     1 
ATOM   6666  O  O     . VAL A 1 2291 ? 139.227 202.471 152.785 1.00 30.71  ? 2291 VAL A O     1 
ATOM   6667  C  CB    . VAL A 1 2291 ? 139.195 199.394 153.986 1.00 27.48  ? 2291 VAL A CB    1 
ATOM   6668  C  CG1   . VAL A 1 2291 ? 137.945 200.102 154.480 1.00 33.23  ? 2291 VAL A CG1   1 
ATOM   6669  C  CG2   . VAL A 1 2291 ? 138.884 197.952 153.620 1.00 28.13  ? 2291 VAL A CG2   1 
ATOM   6670  N  N     . ARG A 1 2292 ? 141.211 201.911 153.672 1.00 28.29  ? 2292 ARG A N     1 
ATOM   6671  C  CA    . ARG A 1 2292 ? 141.583 203.272 154.039 1.00 27.76  ? 2292 ARG A CA    1 
ATOM   6672  C  C     . ARG A 1 2292 ? 142.722 203.797 153.168 1.00 29.21  ? 2292 ARG A C     1 
ATOM   6673  O  O     . ARG A 1 2292 ? 143.600 204.524 153.636 1.00 30.46  ? 2292 ARG A O     1 
ATOM   6674  C  CB    . ARG A 1 2292 ? 141.956 203.344 155.517 1.00 30.05  ? 2292 ARG A CB    1 
ATOM   6675  C  CG    . ARG A 1 2292 ? 140.818 202.957 156.448 1.00 31.45  ? 2292 ARG A CG    1 
ATOM   6676  C  CD    . ARG A 1 2292 ? 141.327 202.543 157.818 1.00 35.72  ? 2292 ARG A CD    1 
ATOM   6677  N  NE    . ARG A 1 2292 ? 140.242 202.100 158.685 1.00 41.27  ? 2292 ARG A NE    1 
ATOM   6678  C  CZ    . ARG A 1 2292 ? 139.687 200.896 158.636 1.00 40.38  ? 2292 ARG A CZ    1 
ATOM   6679  N  NH1   . ARG A 1 2292 ? 140.092 199.983 157.768 1.00 36.36  ? 2292 ARG A NH1   1 
ATOM   6680  N  NH2   . ARG A 1 2292 ? 138.700 200.602 159.477 1.00 41.90  ? 2292 ARG A NH2   1 
ATOM   6681  N  N     . GLY A 1 2293 ? 142.714 203.433 151.890 1.00 28.59  ? 2293 GLY A N     1 
ATOM   6682  C  CA    . GLY A 1 2293 ? 143.695 203.940 150.944 1.00 26.49  ? 2293 GLY A CA    1 
ATOM   6683  C  C     . GLY A 1 2293 ? 145.122 203.503 151.195 1.00 28.18  ? 2293 GLY A C     1 
ATOM   6684  O  O     . GLY A 1 2293 ? 146.042 204.326 151.101 1.00 28.39  ? 2293 GLY A O     1 
ATOM   6685  N  N     . GLU A 1 2294 ? 145.334 202.225 151.512 1.00 27.87  ? 2294 GLU A N     1 
ATOM   6686  C  CA    . GLU A 1 2294 ? 146.680 201.729 151.767 1.00 23.51  ? 2294 GLU A CA    1 
ATOM   6687  C  C     . GLU A 1 2294 ? 147.472 201.470 150.493 1.00 21.98  ? 2294 GLU A C     1 
ATOM   6688  O  O     . GLU A 1 2294 ? 148.704 201.397 150.553 1.00 25.79  ? 2294 GLU A O     1 
ATOM   6689  C  CB    . GLU A 1 2294 ? 146.621 200.446 152.600 1.00 20.49  ? 2294 GLU A CB    1 
ATOM   6690  C  CG    . GLU A 1 2294 ? 146.550 200.683 154.098 1.00 27.49  ? 2294 GLU A CG    1 
ATOM   6691  C  CD    . GLU A 1 2294 ? 145.128 200.828 154.600 1.00 38.89  ? 2294 GLU A CD    1 
ATOM   6692  O  OE1   . GLU A 1 2294 ? 144.195 200.438 153.867 1.00 36.82  ? 2294 GLU A OE1   1 
ATOM   6693  O  OE2   . GLU A 1 2294 ? 144.942 201.332 155.727 1.00 43.40  ? 2294 GLU A OE2   1 
ATOM   6694  N  N     . LEU A 1 2295 ? 146.804 201.331 149.347 1.00 21.52  ? 2295 LEU A N     1 
ATOM   6695  C  CA    . LEU A 1 2295 ? 147.502 201.060 148.097 1.00 17.55  ? 2295 LEU A CA    1 
ATOM   6696  C  C     . LEU A 1 2295 ? 148.101 202.307 147.463 1.00 22.17  ? 2295 LEU A C     1 
ATOM   6697  O  O     . LEU A 1 2295 ? 148.948 202.180 146.572 1.00 23.63  ? 2295 LEU A O     1 
ATOM   6698  C  CB    . LEU A 1 2295 ? 146.558 200.384 147.100 1.00 14.73  ? 2295 LEU A CB    1 
ATOM   6699  C  CG    . LEU A 1 2295 ? 146.252 198.910 147.366 1.00 16.09  ? 2295 LEU A CG    1 
ATOM   6700  C  CD1   . LEU A 1 2295 ? 145.212 198.387 146.388 1.00 20.87  ? 2295 LEU A CD1   1 
ATOM   6701  C  CD2   . LEU A 1 2295 ? 147.521 198.079 147.303 1.00 16.77  ? 2295 LEU A CD2   1 
ATOM   6702  N  N     . GLN A 1 2296 ? 147.693 203.498 147.894 1.00 23.35  ? 2296 GLN A N     1 
ATOM   6703  C  CA    . GLN A 1 2296 ? 148.265 204.741 147.397 1.00 20.89  ? 2296 GLN A CA    1 
ATOM   6704  C  C     . GLN A 1 2296 ? 149.435 205.220 148.242 1.00 25.53  ? 2296 GLN A C     1 
ATOM   6705  O  O     . GLN A 1 2296 ? 149.995 206.284 147.958 1.00 32.36  ? 2296 GLN A O     1 
ATOM   6706  C  CB    . GLN A 1 2296 ? 147.190 205.831 147.333 1.00 19.98  ? 2296 GLN A CB    1 
ATOM   6707  C  CG    . GLN A 1 2296 ? 145.802 205.318 146.984 1.00 24.28  ? 2296 GLN A CG    1 
ATOM   6708  C  CD    . GLN A 1 2296 ? 145.773 204.539 145.684 1.00 27.43  ? 2296 GLN A CD    1 
ATOM   6709  O  OE1   . GLN A 1 2296 ? 145.176 203.466 145.604 1.00 26.19  ? 2296 GLN A OE1   1 
ATOM   6710  N  NE2   . GLN A 1 2296 ? 146.420 205.077 144.656 1.00 30.22  ? 2296 GLN A NE2   1 
ATOM   6711  N  N     . LYS A 1 2297 ? 149.811 204.464 149.266 1.00 22.60  ? 2297 LYS A N     1 
ATOM   6712  C  CA    . LYS A 1 2297 ? 150.927 204.786 150.137 1.00 18.79  ? 2297 LYS A CA    1 
ATOM   6713  C  C     . LYS A 1 2297 ? 152.059 203.794 149.909 1.00 18.67  ? 2297 LYS A C     1 
ATOM   6714  O  O     . LYS A 1 2297 ? 151.854 202.690 149.398 1.00 19.89  ? 2297 LYS A O     1 
ATOM   6715  C  CB    . LYS A 1 2297 ? 150.500 204.754 151.608 1.00 21.29  ? 2297 LYS A CB    1 
ATOM   6716  C  CG    . LYS A 1 2297 ? 149.397 205.730 151.965 1.00 24.51  ? 2297 LYS A CG    1 
ATOM   6717  C  CD    . LYS A 1 2297 ? 149.050 205.635 153.441 1.00 25.74  ? 2297 LYS A CD    1 
ATOM   6718  C  CE    . LYS A 1 2297 ? 148.215 204.402 153.739 1.00 29.73  ? 2297 LYS A CE    1 
ATOM   6719  N  NZ    . LYS A 1 2297 ? 147.781 204.352 155.161 1.00 31.80  ? 2297 LYS A NZ    1 
ATOM   6720  N  N     . ARG A 1 2298 ? 153.265 204.199 150.295 1.00 19.21  ? 2298 ARG A N     1 
ATOM   6721  C  CA    . ARG A 1 2298 ? 154.423 203.314 150.257 1.00 11.06  ? 2298 ARG A CA    1 
ATOM   6722  C  C     . ARG A 1 2298 ? 154.440 202.510 151.551 1.00 12.37  ? 2298 ARG A C     1 
ATOM   6723  O  O     . ARG A 1 2298 ? 154.715 203.053 152.626 1.00 16.81  ? 2298 ARG A O     1 
ATOM   6724  C  CB    . ARG A 1 2298 ? 155.713 204.109 150.074 1.00 12.68  ? 2298 ARG A CB    1 
ATOM   6725  C  CG    . ARG A 1 2298 ? 156.975 203.330 150.405 1.00 11.18  ? 2298 ARG A CG    1 
ATOM   6726  C  CD    . ARG A 1 2298 ? 158.222 204.164 150.173 1.00 12.14  ? 2298 ARG A CD    1 
ATOM   6727  N  NE    . ARG A 1 2298 ? 158.613 204.182 148.769 1.00 12.42  ? 2298 ARG A NE    1 
ATOM   6728  C  CZ    . ARG A 1 2298 ? 158.462 205.223 147.963 1.00 15.09  ? 2298 ARG A CZ    1 
ATOM   6729  N  NH1   . ARG A 1 2298 ? 157.926 206.355 148.388 1.00 15.80  ? 2298 ARG A NH1   1 
ATOM   6730  N  NH2   . ARG A 1 2298 ? 158.858 205.126 146.697 1.00 18.78  ? 2298 ARG A NH2   1 
ATOM   6731  N  N     . GLN A 1 2299 ? 154.132 201.220 151.452 1.00 11.03  ? 2299 GLN A N     1 
ATOM   6732  C  CA    . GLN A 1 2299 ? 154.036 200.344 152.612 1.00 7.49   ? 2299 GLN A CA    1 
ATOM   6733  C  C     . GLN A 1 2299 ? 155.310 199.517 152.723 1.00 6.95   ? 2299 GLN A C     1 
ATOM   6734  O  O     . GLN A 1 2299 ? 155.630 198.738 151.819 1.00 11.43  ? 2299 GLN A O     1 
ATOM   6735  C  CB    . GLN A 1 2299 ? 152.814 199.432 152.508 1.00 9.58   ? 2299 GLN A CB    1 
ATOM   6736  C  CG    . GLN A 1 2299 ? 151.539 200.137 152.081 1.00 13.14  ? 2299 GLN A CG    1 
ATOM   6737  C  CD    . GLN A 1 2299 ? 150.826 200.801 153.238 1.00 14.56  ? 2299 GLN A CD    1 
ATOM   6738  O  OE1   . GLN A 1 2299 ? 150.374 201.939 153.133 1.00 19.97  ? 2299 GLN A OE1   1 
ATOM   6739  N  NE2   . GLN A 1 2299 ? 150.724 200.092 154.353 1.00 12.55  ? 2299 GLN A NE2   1 
ATOM   6740  N  N     . TRP A 1 2300 ? 156.033 199.690 153.825 1.00 6.98   ? 2300 TRP A N     1 
ATOM   6741  C  CA    . TRP A 1 2300 ? 157.244 198.929 154.103 1.00 6.16   ? 2300 TRP A CA    1 
ATOM   6742  C  C     . TRP A 1 2300 ? 156.989 198.043 155.312 1.00 3.92   ? 2300 TRP A C     1 
ATOM   6743  O  O     . TRP A 1 2300 ? 156.561 198.531 156.364 1.00 4.00   ? 2300 TRP A O     1 
ATOM   6744  C  CB    . TRP A 1 2300 ? 158.434 199.858 154.354 1.00 8.30   ? 2300 TRP A CB    1 
ATOM   6745  C  CG    . TRP A 1 2300 ? 159.010 200.443 153.103 1.00 7.43   ? 2300 TRP A CG    1 
ATOM   6746  C  CD1   . TRP A 1 2300 ? 158.537 200.289 151.833 1.00 7.00   ? 2300 TRP A CD1   1 
ATOM   6747  C  CD2   . TRP A 1 2300 ? 160.165 201.281 153.002 1.00 6.90   ? 2300 TRP A CD2   1 
ATOM   6748  N  NE1   . TRP A 1 2300 ? 159.329 200.976 150.946 1.00 6.96   ? 2300 TRP A NE1   1 
ATOM   6749  C  CE2   . TRP A 1 2300 ? 160.336 201.594 151.639 1.00 7.44   ? 2300 TRP A CE2   1 
ATOM   6750  C  CE3   . TRP A 1 2300 ? 161.076 201.792 153.931 1.00 7.55   ? 2300 TRP A CE3   1 
ATOM   6751  C  CZ2   . TRP A 1 2300 ? 161.378 202.398 151.182 1.00 7.38   ? 2300 TRP A CZ2   1 
ATOM   6752  C  CZ3   . TRP A 1 2300 ? 162.108 202.589 153.477 1.00 6.16   ? 2300 TRP A CZ3   1 
ATOM   6753  C  CH2   . TRP A 1 2300 ? 162.251 202.885 152.115 1.00 6.52   ? 2300 TRP A CH2   1 
ATOM   6754  N  N     . ILE A 1 2301 ? 157.241 196.750 155.161 1.00 4.07   ? 2301 ILE A N     1 
ATOM   6755  C  CA    . ILE A 1 2301 ? 157.128 195.794 156.255 1.00 3.10   ? 2301 ILE A CA    1 
ATOM   6756  C  C     . ILE A 1 2301 ? 158.537 195.338 156.601 1.00 4.36   ? 2301 ILE A C     1 
ATOM   6757  O  O     . ILE A 1 2301 ? 159.144 194.550 155.868 1.00 5.82   ? 2301 ILE A O     1 
ATOM   6758  C  CB    . ILE A 1 2301 ? 156.224 194.611 155.887 1.00 2.59   ? 2301 ILE A CB    1 
ATOM   6759  C  CG1   . ILE A 1 2301 ? 154.859 195.113 155.414 1.00 2.61   ? 2301 ILE A CG1   1 
ATOM   6760  C  CG2   . ILE A 1 2301 ? 156.065 193.678 157.074 1.00 4.85   ? 2301 ILE A CG2   1 
ATOM   6761  C  CD1   . ILE A 1 2301 ? 153.923 194.015 154.978 1.00 4.54   ? 2301 ILE A CD1   1 
ATOM   6762  N  N     . VAL A 1 2302 ? 159.060 195.833 157.717 1.00 3.30   ? 2302 VAL A N     1 
ATOM   6763  C  CA    . VAL A 1 2302 ? 160.421 195.545 158.148 1.00 3.13   ? 2302 VAL A CA    1 
ATOM   6764  C  C     . VAL A 1 2302 ? 160.377 194.402 159.152 1.00 3.46   ? 2302 VAL A C     1 
ATOM   6765  O  O     . VAL A 1 2302 ? 159.657 194.472 160.155 1.00 4.56   ? 2302 VAL A O     1 
ATOM   6766  C  CB    . VAL A 1 2302 ? 161.092 196.787 158.754 1.00 3.52   ? 2302 VAL A CB    1 
ATOM   6767  C  CG1   . VAL A 1 2302 ? 162.570 196.530 158.983 1.00 3.63   ? 2302 VAL A CG1   1 
ATOM   6768  C  CG2   . VAL A 1 2302 ? 160.891 197.988 157.845 1.00 2.97   ? 2302 VAL A CG2   1 
ATOM   6769  N  N     . PHE A 1 2303 ? 161.143 193.347 158.879 1.00 4.15   ? 2303 PHE A N     1 
ATOM   6770  C  CA    . PHE A 1 2303 ? 161.279 192.224 159.806 1.00 3.93   ? 2303 PHE A CA    1 
ATOM   6771  C  C     . PHE A 1 2303 ? 162.560 192.405 160.620 1.00 6.34   ? 2303 PHE A C     1 
ATOM   6772  O  O     . PHE A 1 2303 ? 163.609 191.818 160.348 1.00 9.68   ? 2303 PHE A O     1 
ATOM   6773  C  CB    . PHE A 1 2303 ? 161.271 190.903 159.049 1.00 4.67   ? 2303 PHE A CB    1 
ATOM   6774  C  CG    . PHE A 1 2303 ? 159.896 190.403 158.715 1.00 5.10   ? 2303 PHE A CG    1 
ATOM   6775  C  CD1   . PHE A 1 2303 ? 159.045 189.958 159.712 1.00 5.16   ? 2303 PHE A CD1   1 
ATOM   6776  C  CD2   . PHE A 1 2303 ? 159.456 190.372 157.402 1.00 4.83   ? 2303 PHE A CD2   1 
ATOM   6777  C  CE1   . PHE A 1 2303 ? 157.781 189.496 159.407 1.00 5.83   ? 2303 PHE A CE1   1 
ATOM   6778  C  CE2   . PHE A 1 2303 ? 158.192 189.909 157.091 1.00 5.22   ? 2303 PHE A CE2   1 
ATOM   6779  C  CZ    . PHE A 1 2303 ? 157.354 189.470 158.095 1.00 5.47   ? 2303 PHE A CZ    1 
ATOM   6780  N  N     . ASP A 1 2304 ? 162.453 193.250 161.642 1.00 6.51   ? 2304 ASP A N     1 
ATOM   6781  C  CA    . ASP A 1 2304 ? 163.582 193.557 162.512 1.00 4.96   ? 2304 ASP A CA    1 
ATOM   6782  C  C     . ASP A 1 2304 ? 163.677 192.471 163.576 1.00 7.63   ? 2304 ASP A C     1 
ATOM   6783  O  O     . ASP A 1 2304 ? 162.866 192.428 164.506 1.00 12.51  ? 2304 ASP A O     1 
ATOM   6784  C  CB    . ASP A 1 2304 ? 163.409 194.939 163.135 1.00 6.70   ? 2304 ASP A CB    1 
ATOM   6785  C  CG    . ASP A 1 2304 ? 164.670 195.442 163.814 1.00 9.89   ? 2304 ASP A CG    1 
ATOM   6786  O  OD1   . ASP A 1 2304 ? 165.616 194.649 163.999 1.00 10.22  ? 2304 ASP A OD1   1 
ATOM   6787  O  OD2   . ASP A 1 2304 ? 164.713 196.639 164.167 1.00 12.62  ? 2304 ASP A OD2   1 
ATOM   6788  N  N     . GLY A 1 2305 ? 164.659 191.593 163.440 1.00 6.41   ? 2305 GLY A N     1 
ATOM   6789  C  CA    . GLY A 1 2305 ? 164.815 190.495 164.368 1.00 7.84   ? 2305 GLY A CA    1 
ATOM   6790  C  C     . GLY A 1 2305 ? 165.750 189.448 163.796 1.00 9.07   ? 2305 GLY A C     1 
ATOM   6791  O  O     . GLY A 1 2305 ? 166.513 189.708 162.867 1.00 11.86  ? 2305 GLY A O     1 
ATOM   6792  N  N     . ASP A 1 2306 ? 165.671 188.258 164.380 1.00 8.16   ? 2306 ASP A N     1 
ATOM   6793  C  CA    . ASP A 1 2306 ? 166.487 187.143 163.931 1.00 7.27   ? 2306 ASP A CA    1 
ATOM   6794  C  C     . ASP A 1 2306 ? 165.773 186.372 162.827 1.00 11.43  ? 2306 ASP A C     1 
ATOM   6795  O  O     . ASP A 1 2306 ? 164.551 186.202 162.848 1.00 19.28  ? 2306 ASP A O     1 
ATOM   6796  C  CB    . ASP A 1 2306 ? 166.810 186.210 165.099 1.00 14.66  ? 2306 ASP A CB    1 
ATOM   6797  C  CG    . ASP A 1 2306 ? 167.635 186.888 166.177 1.00 16.73  ? 2306 ASP A CG    1 
ATOM   6798  O  OD1   . ASP A 1 2306 ? 167.831 186.279 167.249 1.00 13.33  ? 2306 ASP A OD1   1 
ATOM   6799  O  OD2   . ASP A 1 2306 ? 168.085 188.031 165.954 1.00 18.27  ? 2306 ASP A OD2   1 
ATOM   6800  N  N     . VAL A 1 2307 ? 166.552 185.903 161.857 1.00 10.51  ? 2307 VAL A N     1 
ATOM   6801  C  CA    . VAL A 1 2307 ? 166.034 185.171 160.706 1.00 9.47   ? 2307 VAL A CA    1 
ATOM   6802  C  C     . VAL A 1 2307 ? 166.482 183.722 160.828 1.00 12.00  ? 2307 VAL A C     1 
ATOM   6803  O  O     . VAL A 1 2307 ? 167.683 183.445 160.939 1.00 18.13  ? 2307 VAL A O     1 
ATOM   6804  C  CB    . VAL A 1 2307 ? 166.508 185.783 159.378 1.00 9.80   ? 2307 VAL A CB    1 
ATOM   6805  C  CG1   . VAL A 1 2307 ? 166.408 184.766 158.254 1.00 9.83   ? 2307 VAL A CG1   1 
ATOM   6806  C  CG2   . VAL A 1 2307 ? 165.686 187.014 159.045 1.00 11.23  ? 2307 VAL A CG2   1 
ATOM   6807  N  N     . ASP A 1 2308 ? 165.524 182.807 160.818 1.00 9.46   ? 2308 ASP A N     1 
ATOM   6808  C  CA    . ASP A 1 2308 ? 165.779 181.377 160.843 1.00 12.99  ? 2308 ASP A CA    1 
ATOM   6809  C  C     . ASP A 1 2308 ? 164.851 180.689 159.856 1.00 13.01  ? 2308 ASP A C     1 
ATOM   6810  O  O     . ASP A 1 2308 ? 163.763 181.195 159.559 1.00 10.06  ? 2308 ASP A O     1 
ATOM   6811  C  CB    . ASP A 1 2308 ? 165.586 180.801 162.254 1.00 13.12  ? 2308 ASP A CB    1 
ATOM   6812  C  CG    . ASP A 1 2308 ? 164.139 180.525 162.584 1.00 13.99  ? 2308 ASP A CG    1 
ATOM   6813  O  OD1   . ASP A 1 2308 ? 163.447 181.444 163.059 1.00 15.70  ? 2308 ASP A OD1   1 
ATOM   6814  O  OD2   . ASP A 1 2308 ? 163.697 179.380 162.380 1.00 16.57  ? 2308 ASP A OD2   1 
ATOM   6815  N  N     . PRO A 1 2309 ? 165.252 179.529 159.326 1.00 13.08  ? 2309 PRO A N     1 
ATOM   6816  C  CA    . PRO A 1 2309 ? 164.477 178.917 158.231 1.00 12.21  ? 2309 PRO A CA    1 
ATOM   6817  C  C     . PRO A 1 2309 ? 163.053 178.534 158.598 1.00 14.87  ? 2309 PRO A C     1 
ATOM   6818  O  O     . PRO A 1 2309 ? 162.223 178.379 157.694 1.00 14.26  ? 2309 PRO A O     1 
ATOM   6819  C  CB    . PRO A 1 2309 ? 165.308 177.677 157.863 1.00 14.63  ? 2309 PRO A CB    1 
ATOM   6820  C  CG    . PRO A 1 2309 ? 166.243 177.468 159.009 1.00 15.64  ? 2309 PRO A CG    1 
ATOM   6821  C  CD    . PRO A 1 2309 ? 166.520 178.822 159.559 1.00 14.10  ? 2309 PRO A CD    1 
ATOM   6822  N  N     . GLU A 1 2310 ? 162.737 178.362 159.883 1.00 17.94  ? 2310 GLU A N     1 
ATOM   6823  C  CA    . GLU A 1 2310 ? 161.393 177.921 160.245 1.00 12.62  ? 2310 GLU A CA    1 
ATOM   6824  C  C     . GLU A 1 2310 ? 160.341 178.960 159.874 1.00 14.71  ? 2310 GLU A C     1 
ATOM   6825  O  O     . GLU A 1 2310 ? 159.264 178.609 159.378 1.00 23.34  ? 2310 GLU A O     1 
ATOM   6826  C  CB    . GLU A 1 2310 ? 161.324 177.600 161.738 1.00 15.77  ? 2310 GLU A CB    1 
ATOM   6827  C  CG    . GLU A 1 2310 ? 162.072 176.339 162.138 1.00 21.53  ? 2310 GLU A CG    1 
ATOM   6828  C  CD    . GLU A 1 2310 ? 161.611 175.789 163.473 1.00 35.33  ? 2310 GLU A CD    1 
ATOM   6829  O  OE1   . GLU A 1 2310 ? 162.136 174.739 163.898 1.00 31.11  ? 2310 GLU A OE1   1 
ATOM   6830  O  OE2   . GLU A 1 2310 ? 160.723 176.407 164.096 1.00 33.30  ? 2310 GLU A OE2   1 
ATOM   6831  N  N     . TRP A 1 2311 ? 160.631 180.241 160.101 1.00 10.81  ? 2311 TRP A N     1 
ATOM   6832  C  CA    . TRP A 1 2311 ? 159.628 181.277 159.884 1.00 6.69   ? 2311 TRP A CA    1 
ATOM   6833  C  C     . TRP A 1 2311 ? 159.783 181.990 158.549 1.00 7.13   ? 2311 TRP A C     1 
ATOM   6834  O  O     . TRP A 1 2311 ? 158.775 182.350 157.932 1.00 8.27   ? 2311 TRP A O     1 
ATOM   6835  C  CB    . TRP A 1 2311 ? 159.668 182.299 161.031 1.00 6.16   ? 2311 TRP A CB    1 
ATOM   6836  C  CG    . TRP A 1 2311 ? 160.697 183.388 160.887 1.00 7.45   ? 2311 TRP A CG    1 
ATOM   6837  C  CD1   . TRP A 1 2311 ? 161.919 183.441 161.488 1.00 7.18   ? 2311 TRP A CD1   1 
ATOM   6838  C  CD2   . TRP A 1 2311 ? 160.570 184.603 160.134 1.00 5.75   ? 2311 TRP A CD2   1 
ATOM   6839  N  NE1   . TRP A 1 2311 ? 162.574 184.594 161.134 1.00 6.57   ? 2311 TRP A NE1   1 
ATOM   6840  C  CE2   . TRP A 1 2311 ? 161.766 185.326 160.305 1.00 6.19   ? 2311 TRP A CE2   1 
ATOM   6841  C  CE3   . TRP A 1 2311 ? 159.568 185.140 159.320 1.00 5.57   ? 2311 TRP A CE3   1 
ATOM   6842  C  CZ2   . TRP A 1 2311 ? 161.988 186.557 159.694 1.00 7.23   ? 2311 TRP A CZ2   1 
ATOM   6843  C  CZ3   . TRP A 1 2311 ? 159.789 186.361 158.715 1.00 5.40   ? 2311 TRP A CZ3   1 
ATOM   6844  C  CH2   . TRP A 1 2311 ? 160.988 187.058 158.908 1.00 4.69   ? 2311 TRP A CH2   1 
ATOM   6845  N  N     . VAL A 1 2312 ? 161.014 182.201 158.079 1.00 9.61   ? 2312 VAL A N     1 
ATOM   6846  C  CA    . VAL A 1 2312 ? 161.216 183.009 156.882 1.00 5.96   ? 2312 VAL A CA    1 
ATOM   6847  C  C     . VAL A 1 2312 ? 161.034 182.204 155.599 1.00 8.39   ? 2312 VAL A C     1 
ATOM   6848  O  O     . VAL A 1 2312 ? 160.769 182.793 154.541 1.00 9.11   ? 2312 VAL A O     1 
ATOM   6849  C  CB    . VAL A 1 2312 ? 162.607 183.673 156.910 1.00 4.88   ? 2312 VAL A CB    1 
ATOM   6850  C  CG1   . VAL A 1 2312 ? 163.708 182.635 156.740 1.00 7.28   ? 2312 VAL A CG1   1 
ATOM   6851  C  CG2   . VAL A 1 2312 ? 162.709 184.783 155.873 1.00 7.17   ? 2312 VAL A CG2   1 
ATOM   6852  N  N     . GLU A 1 2313 ? 161.144 180.874 155.662 1.00 8.86   ? 2313 GLU A N     1 
ATOM   6853  C  CA    . GLU A 1 2313 ? 160.894 180.050 154.485 1.00 7.54   ? 2313 GLU A CA    1 
ATOM   6854  C  C     . GLU A 1 2313 ? 159.436 180.107 154.049 1.00 10.49  ? 2313 GLU A C     1 
ATOM   6855  O  O     . GLU A 1 2313 ? 159.133 179.777 152.897 1.00 15.73  ? 2313 GLU A O     1 
ATOM   6856  C  CB    . GLU A 1 2313 ? 161.299 178.602 154.759 1.00 14.94  ? 2313 GLU A CB    1 
ATOM   6857  C  CG    . GLU A 1 2313 ? 161.669 177.805 153.523 1.00 19.87  ? 2313 GLU A CG    1 
ATOM   6858  C  CD    . GLU A 1 2313 ? 163.169 177.682 153.343 1.00 28.93  ? 2313 GLU A CD    1 
ATOM   6859  O  OE1   . GLU A 1 2313 ? 163.914 178.089 154.260 1.00 25.57  ? 2313 GLU A OE1   1 
ATOM   6860  O  OE2   . GLU A 1 2313 ? 163.603 177.177 152.287 1.00 38.94  ? 2313 GLU A OE2   1 
ATOM   6861  N  N     . ASN A 1 2314 ? 158.532 180.511 154.943 1.00 10.78  ? 2314 ASN A N     1 
ATOM   6862  C  CA    . ASN A 1 2314 ? 157.151 180.778 154.564 1.00 8.88   ? 2314 ASN A CA    1 
ATOM   6863  C  C     . ASN A 1 2314 ? 157.033 181.955 153.609 1.00 11.71  ? 2314 ASN A C     1 
ATOM   6864  O  O     . ASN A 1 2314 ? 156.014 182.076 152.921 1.00 17.29  ? 2314 ASN A O     1 
ATOM   6865  C  CB    . ASN A 1 2314 ? 156.306 181.048 155.810 1.00 7.64   ? 2314 ASN A CB    1 
ATOM   6866  C  CG    . ASN A 1 2314 ? 155.730 179.785 156.408 1.00 13.31  ? 2314 ASN A CG    1 
ATOM   6867  O  OD1   . ASN A 1 2314 ? 156.193 178.683 156.121 1.00 28.18  ? 2314 ASN A OD1   1 
ATOM   6868  N  ND2   . ASN A 1 2314 ? 154.713 179.938 157.247 1.00 11.50  ? 2314 ASN A ND2   1 
ATOM   6869  N  N     . LEU A 1 2315 ? 158.046 182.817 153.552 1.00 10.12  ? 2315 LEU A N     1 
ATOM   6870  C  CA    . LEU A 1 2315 ? 158.052 183.988 152.690 1.00 7.80   ? 2315 LEU A CA    1 
ATOM   6871  C  C     . LEU A 1 2315 ? 158.725 183.727 151.350 1.00 8.77   ? 2315 LEU A C     1 
ATOM   6872  O  O     . LEU A 1 2315 ? 158.913 184.668 150.573 1.00 9.14   ? 2315 LEU A O     1 
ATOM   6873  C  CB    . LEU A 1 2315 ? 158.744 185.155 153.396 1.00 8.47   ? 2315 LEU A CB    1 
ATOM   6874  C  CG    . LEU A 1 2315 ? 158.067 185.709 154.649 1.00 7.09   ? 2315 LEU A CG    1 
ATOM   6875  C  CD1   . LEU A 1 2315 ? 158.894 186.833 155.250 1.00 8.02   ? 2315 LEU A CD1   1 
ATOM   6876  C  CD2   . LEU A 1 2315 ? 156.663 186.185 154.330 1.00 8.28   ? 2315 LEU A CD2   1 
ATOM   6877  N  N     . ASN A 1 2316 ? 159.098 182.476 151.065 1.00 10.71  ? 2316 ASN A N     1 
ATOM   6878  C  CA    . ASN A 1 2316 ? 159.822 182.182 149.832 1.00 8.45   ? 2316 ASN A CA    1 
ATOM   6879  C  C     . ASN A 1 2316 ? 159.016 182.583 148.604 1.00 7.77   ? 2316 ASN A C     1 
ATOM   6880  O  O     . ASN A 1 2316 ? 159.514 183.313 147.739 1.00 10.70  ? 2316 ASN A O     1 
ATOM   6881  C  CB    . ASN A 1 2316 ? 160.178 180.697 149.771 1.00 10.79  ? 2316 ASN A CB    1 
ATOM   6882  C  CG    . ASN A 1 2316 ? 161.452 180.372 150.522 1.00 13.58  ? 2316 ASN A CG    1 
ATOM   6883  O  OD1   . ASN A 1 2316 ? 162.100 181.256 151.081 1.00 15.51  ? 2316 ASN A OD1   1 
ATOM   6884  N  ND2   . ASN A 1 2316 ? 161.826 179.099 150.526 1.00 12.94  ? 2316 ASN A ND2   1 
ATOM   6885  N  N     . SER A 1 2317 ? 157.762 182.132 148.517 1.00 7.67   ? 2317 SER A N     1 
ATOM   6886  C  CA    . SER A 1 2317 ? 156.926 182.491 147.377 1.00 6.94   ? 2317 SER A CA    1 
ATOM   6887  C  C     . SER A 1 2317 ? 156.611 183.981 147.360 1.00 7.37   ? 2317 SER A C     1 
ATOM   6888  O  O     . SER A 1 2317 ? 156.357 184.546 146.290 1.00 10.12  ? 2317 SER A O     1 
ATOM   6889  C  CB    . SER A 1 2317 ? 155.639 181.669 147.391 1.00 11.73  ? 2317 SER A CB    1 
ATOM   6890  O  OG    . SER A 1 2317 ? 154.596 182.359 148.055 1.00 23.07  ? 2317 SER A OG    1 
ATOM   6891  N  N     . VAL A 1 2318 ? 156.620 184.628 148.526 1.00 8.53   ? 2318 VAL A N     1 
ATOM   6892  C  CA    . VAL A 1 2318 ? 156.450 186.076 148.571 1.00 6.06   ? 2318 VAL A CA    1 
ATOM   6893  C  C     . VAL A 1 2318 ? 157.653 186.771 147.947 1.00 7.30   ? 2318 VAL A C     1 
ATOM   6894  O  O     . VAL A 1 2318 ? 157.506 187.721 147.169 1.00 9.78   ? 2318 VAL A O     1 
ATOM   6895  C  CB    . VAL A 1 2318 ? 156.218 186.542 150.020 1.00 7.67   ? 2318 VAL A CB    1 
ATOM   6896  C  CG1   . VAL A 1 2318 ? 155.955 188.038 150.061 1.00 8.06   ? 2318 VAL A CG1   1 
ATOM   6897  C  CG2   . VAL A 1 2318 ? 155.071 185.772 150.650 1.00 9.59   ? 2318 VAL A CG2   1 
ATOM   6898  N  N     . LEU A 1 2319 ? 158.860 186.309 148.275 1.00 8.11   ? 2319 LEU A N     1 
ATOM   6899  C  CA    . LEU A 1 2319 ? 160.081 186.930 147.780 1.00 7.65   ? 2319 LEU A CA    1 
ATOM   6900  C  C     . LEU A 1 2319 ? 160.521 186.390 146.425 1.00 11.11  ? 2319 LEU A C     1 
ATOM   6901  O  O     . LEU A 1 2319 ? 161.525 186.867 145.886 1.00 11.90  ? 2319 LEU A O     1 
ATOM   6902  C  CB    . LEU A 1 2319 ? 161.209 186.753 148.800 1.00 9.25   ? 2319 LEU A CB    1 
ATOM   6903  C  CG    . LEU A 1 2319 ? 160.895 187.223 150.223 1.00 6.08   ? 2319 LEU A CG    1 
ATOM   6904  C  CD1   . LEU A 1 2319 ? 161.590 186.346 151.253 1.00 7.26   ? 2319 LEU A CD1   1 
ATOM   6905  C  CD2   . LEU A 1 2319 ? 161.275 188.680 150.409 1.00 6.24   ? 2319 LEU A CD2   1 
ATOM   6906  N  N     . ASP A 1 2320 ? 159.806 185.417 145.867 1.00 12.16  ? 2320 ASP A N     1 
ATOM   6907  C  CA    . ASP A 1 2320 ? 160.050 184.971 144.502 1.00 10.10  ? 2320 ASP A CA    1 
ATOM   6908  C  C     . ASP A 1 2320 ? 159.381 185.940 143.530 1.00 16.03  ? 2320 ASP A C     1 
ATOM   6909  O  O     . ASP A 1 2320 ? 158.901 187.012 143.909 1.00 16.22  ? 2320 ASP A O     1 
ATOM   6910  C  CB    . ASP A 1 2320 ? 159.542 183.546 144.297 1.00 10.76  ? 2320 ASP A CB    1 
ATOM   6911  C  CG    . ASP A 1 2320 ? 160.428 182.507 144.947 1.00 20.61  ? 2320 ASP A CG    1 
ATOM   6912  O  OD1   . ASP A 1 2320 ? 161.662 182.583 144.774 1.00 23.35  ? 2320 ASP A OD1   1 
ATOM   6913  O  OD2   . ASP A 1 2320 ? 159.888 181.599 145.615 1.00 18.07  ? 2320 ASP A OD2   1 
ATOM   6914  N  N     . ASP A 1 2321 ? 159.342 185.566 142.252 1.00 20.60  ? 2321 ASP A N     1 
ATOM   6915  C  CA    . ASP A 1 2321 ? 158.574 186.328 141.278 1.00 19.81  ? 2321 ASP A CA    1 
ATOM   6916  C  C     . ASP A 1 2321 ? 157.082 186.046 141.375 1.00 21.76  ? 2321 ASP A C     1 
ATOM   6917  O  O     . ASP A 1 2321 ? 156.286 186.782 140.782 1.00 24.10  ? 2321 ASP A O     1 
ATOM   6918  C  CB    . ASP A 1 2321 ? 159.069 186.027 139.862 1.00 30.76  ? 2321 ASP A CB    1 
ATOM   6919  C  CG    . ASP A 1 2321 ? 160.567 186.202 139.719 1.00 35.58  ? 2321 ASP A CG    1 
ATOM   6920  O  OD1   . ASP A 1 2321 ? 161.062 187.321 139.970 1.00 34.77  ? 2321 ASP A OD1   1 
ATOM   6921  O  OD2   . ASP A 1 2321 ? 161.250 185.223 139.355 1.00 38.79  ? 2321 ASP A OD2   1 
ATOM   6922  N  N     . ASN A 1 2322 ? 156.690 184.997 142.103 1.00 16.34  ? 2322 ASN A N     1 
ATOM   6923  C  CA    . ASN A 1 2322 ? 155.271 184.717 142.301 1.00 13.50  ? 2322 ASN A CA    1 
ATOM   6924  C  C     . ASN A 1 2322 ? 154.599 185.819 143.109 1.00 12.64  ? 2322 ASN A C     1 
ATOM   6925  O  O     . ASN A 1 2322 ? 153.471 186.223 142.801 1.00 18.49  ? 2322 ASN A O     1 
ATOM   6926  C  CB    . ASN A 1 2322 ? 155.094 183.364 142.991 1.00 12.63  ? 2322 ASN A CB    1 
ATOM   6927  C  CG    . ASN A 1 2322 ? 155.806 182.240 142.266 1.00 18.92  ? 2322 ASN A CG    1 
ATOM   6928  O  OD1   . ASN A 1 2322 ? 155.521 181.958 141.102 1.00 20.93  ? 2322 ASN A OD1   1 
ATOM   6929  N  ND2   . ASN A 1 2322 ? 156.737 181.588 142.952 1.00 16.27  ? 2322 ASN A ND2   1 
ATOM   6930  N  N     . LYS A 1 2323 ? 155.279 186.316 144.146 1.00 9.25   ? 2323 LYS A N     1 
ATOM   6931  C  CA    . LYS A 1 2323 ? 154.761 187.377 145.012 1.00 8.61   ? 2323 LYS A CA    1 
ATOM   6932  C  C     . LYS A 1 2323 ? 153.403 187.001 145.603 1.00 9.33   ? 2323 LYS A C     1 
ATOM   6933  O  O     . LYS A 1 2323 ? 152.446 187.777 145.573 1.00 12.57  ? 2323 LYS A O     1 
ATOM   6934  C  CB    . LYS A 1 2323 ? 154.686 188.711 144.265 1.00 10.00  ? 2323 LYS A CB    1 
ATOM   6935  C  CG    . LYS A 1 2323 ? 155.911 189.018 143.423 1.00 11.30  ? 2323 LYS A CG    1 
ATOM   6936  C  CD    . LYS A 1 2323 ? 155.594 190.027 142.335 1.00 11.32  ? 2323 LYS A CD    1 
ATOM   6937  C  CE    . LYS A 1 2323 ? 156.684 191.080 142.232 1.00 14.34  ? 2323 LYS A CE    1 
ATOM   6938  N  NZ    . LYS A 1 2323 ? 156.444 192.217 143.164 1.00 17.04  ? 2323 LYS A NZ    1 
ATOM   6939  N  N     . LEU A 1 2324 ? 153.326 185.790 146.148 1.00 7.65   ? 2324 LEU A N     1 
ATOM   6940  C  CA    . LEU A 1 2324 ? 152.106 185.263 146.740 1.00 7.45   ? 2324 LEU A CA    1 
ATOM   6941  C  C     . LEU A 1 2324 ? 152.387 184.792 148.157 1.00 9.40   ? 2324 LEU A C     1 
ATOM   6942  O  O     . LEU A 1 2324 ? 153.416 184.158 148.411 1.00 13.30  ? 2324 LEU A O     1 
ATOM   6943  C  CB    . LEU A 1 2324 ? 151.544 184.106 145.910 1.00 9.48   ? 2324 LEU A CB    1 
ATOM   6944  C  CG    . LEU A 1 2324 ? 150.938 184.452 144.552 1.00 11.50  ? 2324 LEU A CG    1 
ATOM   6945  C  CD1   . LEU A 1 2324 ? 150.406 183.201 143.879 1.00 13.99  ? 2324 LEU A CD1   1 
ATOM   6946  C  CD2   . LEU A 1 2324 ? 149.833 185.477 144.718 1.00 9.25   ? 2324 LEU A CD2   1 
ATOM   6947  N  N     . LEU A 1 2325 ? 151.474 185.102 149.075 1.00 7.51   ? 2325 LEU A N     1 
ATOM   6948  C  CA    . LEU A 1 2325 ? 151.522 184.565 150.432 1.00 9.00   ? 2325 LEU A CA    1 
ATOM   6949  C  C     . LEU A 1 2325 ? 150.517 183.423 150.506 1.00 12.00  ? 2325 LEU A C     1 
ATOM   6950  O  O     . LEU A 1 2325 ? 149.310 183.648 150.617 1.00 17.39  ? 2325 LEU A O     1 
ATOM   6951  C  CB    . LEU A 1 2325 ? 151.220 185.646 151.464 1.00 8.58   ? 2325 LEU A CB    1 
ATOM   6952  C  CG    . LEU A 1 2325 ? 151.200 185.166 152.917 1.00 7.62   ? 2325 LEU A CG    1 
ATOM   6953  C  CD1   . LEU A 1 2325 ? 152.552 184.593 153.311 1.00 8.71   ? 2325 LEU A CD1   1 
ATOM   6954  C  CD2   . LEU A 1 2325 ? 150.794 186.287 153.856 1.00 7.70   ? 2325 LEU A CD2   1 
ATOM   6955  N  N     . THR A 1 2326 ? 151.016 182.194 150.440 1.00 13.40  ? 2326 THR A N     1 
ATOM   6956  C  CA    . THR A 1 2326 ? 150.149 181.026 150.450 1.00 13.39  ? 2326 THR A CA    1 
ATOM   6957  C  C     . THR A 1 2326 ? 149.861 180.596 151.881 1.00 14.16  ? 2326 THR A C     1 
ATOM   6958  O  O     . THR A 1 2326 ? 150.782 180.422 152.686 1.00 16.21  ? 2326 THR A O     1 
ATOM   6959  C  CB    . THR A 1 2326 ? 150.788 179.878 149.673 1.00 15.22  ? 2326 THR A CB    1 
ATOM   6960  O  OG1   . THR A 1 2326 ? 152.202 179.887 149.892 1.00 20.52  ? 2326 THR A OG1   1 
ATOM   6961  C  CG2   . THR A 1 2326 ? 150.515 180.032 148.190 1.00 13.07  ? 2326 THR A CG2   1 
ATOM   6962  N  N     . LEU A 1 2327 ? 148.585 180.430 152.193 1.00 13.91  ? 2327 LEU A N     1 
ATOM   6963  C  CA    . LEU A 1 2327 ? 148.142 179.991 153.500 1.00 13.36  ? 2327 LEU A CA    1 
ATOM   6964  C  C     . LEU A 1 2327 ? 147.569 178.580 153.414 1.00 16.27  ? 2327 LEU A C     1 
ATOM   6965  O  O     . LEU A 1 2327 ? 147.083 178.168 152.356 1.00 19.67  ? 2327 LEU A O     1 
ATOM   6966  C  CB    . LEU A 1 2327 ? 147.086 180.948 154.066 1.00 15.19  ? 2327 LEU A CB    1 
ATOM   6967  C  CG    . LEU A 1 2327 ? 147.441 182.436 154.039 1.00 11.80  ? 2327 LEU A CG    1 
ATOM   6968  C  CD1   . LEU A 1 2327 ? 146.252 183.282 154.464 1.00 13.68  ? 2327 LEU A CD1   1 
ATOM   6969  C  CD2   . LEU A 1 2327 ? 148.647 182.719 154.919 1.00 8.24   ? 2327 LEU A CD2   1 
ATOM   6970  N  N     . PRO A 1 2328 ? 147.622 177.808 154.504 1.00 13.23  ? 2328 PRO A N     1 
ATOM   6971  C  CA    . PRO A 1 2328 ? 147.178 176.405 154.430 1.00 13.27  ? 2328 PRO A CA    1 
ATOM   6972  C  C     . PRO A 1 2328 ? 145.711 176.233 154.074 1.00 18.99  ? 2328 PRO A C     1 
ATOM   6973  O  O     . PRO A 1 2328 ? 145.331 175.152 153.607 1.00 27.93  ? 2328 PRO A O     1 
ATOM   6974  C  CB    . PRO A 1 2328 ? 147.478 175.863 155.836 1.00 18.65  ? 2328 PRO A CB    1 
ATOM   6975  C  CG    . PRO A 1 2328 ? 147.677 177.064 156.697 1.00 17.76  ? 2328 PRO A CG    1 
ATOM   6976  C  CD    . PRO A 1 2328 ? 148.223 178.130 155.808 1.00 12.47  ? 2328 PRO A CD    1 
ATOM   6977  N  N     . ASN A 1 2329 ? 144.875 177.252 154.267 1.00 17.42  ? 2329 ASN A N     1 
ATOM   6978  C  CA    . ASN A 1 2329 ? 143.461 177.159 153.928 1.00 16.13  ? 2329 ASN A CA    1 
ATOM   6979  C  C     . ASN A 1 2329 ? 143.187 177.385 152.445 1.00 18.82  ? 2329 ASN A C     1 
ATOM   6980  O  O     . ASN A 1 2329 ? 142.027 177.588 152.069 1.00 24.92  ? 2329 ASN A O     1 
ATOM   6981  C  CB    . ASN A 1 2329 ? 142.649 178.152 154.765 1.00 18.79  ? 2329 ASN A CB    1 
ATOM   6982  C  CG    . ASN A 1 2329 ? 143.055 179.590 154.522 1.00 19.26  ? 2329 ASN A CG    1 
ATOM   6983  O  OD1   . ASN A 1 2329 ? 144.206 179.964 154.731 1.00 19.91  ? 2329 ASN A OD1   1 
ATOM   6984  N  ND2   . ASN A 1 2329 ? 142.108 180.405 154.078 1.00 20.24  ? 2329 ASN A ND2   1 
ATOM   6985  N  N     . GLY A 1 2330 ? 144.214 177.352 151.598 1.00 16.40  ? 2330 GLY A N     1 
ATOM   6986  C  CA    . GLY A 1 2330 ? 144.040 177.549 150.176 1.00 17.25  ? 2330 GLY A CA    1 
ATOM   6987  C  C     . GLY A 1 2330 ? 144.003 178.990 149.722 1.00 23.08  ? 2330 GLY A C     1 
ATOM   6988  O  O     . GLY A 1 2330 ? 143.821 179.238 148.523 1.00 25.42  ? 2330 GLY A O     1 
ATOM   6989  N  N     . GLU A 1 2331 ? 144.168 179.946 150.631 1.00 22.86  ? 2331 GLU A N     1 
ATOM   6990  C  CA    . GLU A 1 2331 ? 144.131 181.354 150.268 1.00 19.35  ? 2331 GLU A CA    1 
ATOM   6991  C  C     . GLU A 1 2331 ? 145.509 181.830 149.831 1.00 16.28  ? 2331 GLU A C     1 
ATOM   6992  O  O     . GLU A 1 2331 ? 146.528 181.463 150.423 1.00 16.50  ? 2331 GLU A O     1 
ATOM   6993  C  CB    . GLU A 1 2331 ? 143.636 182.191 151.447 1.00 19.55  ? 2331 GLU A CB    1 
ATOM   6994  C  CG    . GLU A 1 2331 ? 142.844 183.420 151.047 1.00 21.89  ? 2331 GLU A CG    1 
ATOM   6995  C  CD    . GLU A 1 2331 ? 142.455 184.271 152.239 1.00 26.36  ? 2331 GLU A CD    1 
ATOM   6996  O  OE1   . GLU A 1 2331 ? 142.352 183.721 153.355 1.00 28.27  ? 2331 GLU A OE1   1 
ATOM   6997  O  OE2   . GLU A 1 2331 ? 142.249 185.489 152.058 1.00 30.73  ? 2331 GLU A OE2   1 
ATOM   6998  N  N     . ARG A 1 2332 ? 145.534 182.652 148.784 1.00 21.44  ? 2332 ARG A N     1 
ATOM   6999  C  CA    . ARG A 1 2332 ? 146.769 183.213 148.250 1.00 16.67  ? 2332 ARG A CA    1 
ATOM   7000  C  C     . ARG A 1 2332 ? 146.622 184.724 148.181 1.00 14.89  ? 2332 ARG A C     1 
ATOM   7001  O  O     . ARG A 1 2332 ? 145.665 185.230 147.585 1.00 17.99  ? 2332 ARG A O     1 
ATOM   7002  C  CB    . ARG A 1 2332 ? 147.085 182.630 146.869 1.00 17.91  ? 2332 ARG A CB    1 
ATOM   7003  C  CG    . ARG A 1 2332 ? 147.189 181.111 146.863 1.00 20.90  ? 2332 ARG A CG    1 
ATOM   7004  C  CD    . ARG A 1 2332 ? 146.769 180.518 145.529 1.00 17.12  ? 2332 ARG A CD    1 
ATOM   7005  N  NE    . ARG A 1 2332 ? 147.902 180.299 144.639 1.00 14.66  ? 2332 ARG A NE    1 
ATOM   7006  C  CZ    . ARG A 1 2332 ? 147.934 180.663 143.365 1.00 20.80  ? 2332 ARG A CZ    1 
ATOM   7007  N  NH1   . ARG A 1 2332 ? 146.907 181.273 142.795 1.00 26.49  ? 2332 ARG A NH1   1 
ATOM   7008  N  NH2   . ARG A 1 2332 ? 149.020 180.406 142.643 1.00 12.99  ? 2332 ARG A NH2   1 
ATOM   7009  N  N     . LEU A 1 2333 ? 147.565 185.441 148.787 1.00 12.14  ? 2333 LEU A N     1 
ATOM   7010  C  CA    . LEU A 1 2333 ? 147.535 186.896 148.861 1.00 8.89   ? 2333 LEU A CA    1 
ATOM   7011  C  C     . LEU A 1 2333 ? 148.653 187.461 147.996 1.00 8.20   ? 2333 LEU A C     1 
ATOM   7012  O  O     . LEU A 1 2333 ? 149.828 187.145 148.211 1.00 13.95  ? 2333 LEU A O     1 
ATOM   7013  C  CB    . LEU A 1 2333 ? 147.677 187.375 150.306 1.00 10.72  ? 2333 LEU A CB    1 
ATOM   7014  C  CG    . LEU A 1 2333 ? 146.443 187.278 151.209 1.00 11.83  ? 2333 LEU A CG    1 
ATOM   7015  C  CD1   . LEU A 1 2333 ? 146.246 185.867 151.737 1.00 13.29  ? 2333 LEU A CD1   1 
ATOM   7016  C  CD2   . LEU A 1 2333 ? 146.546 188.266 152.357 1.00 9.41   ? 2333 LEU A CD2   1 
ATOM   7017  N  N     . SER A 1 2334 ? 148.287 188.299 147.029 1.00 9.48   ? 2334 SER A N     1 
ATOM   7018  C  CA    . SER A 1 2334 ? 149.253 188.859 146.094 1.00 8.42   ? 2334 SER A CA    1 
ATOM   7019  C  C     . SER A 1 2334 ? 149.933 190.082 146.695 1.00 9.70   ? 2334 SER A C     1 
ATOM   7020  O  O     . SER A 1 2334 ? 149.282 190.917 147.330 1.00 13.01  ? 2334 SER A O     1 
ATOM   7021  C  CB    . SER A 1 2334 ? 148.569 189.229 144.779 1.00 12.33  ? 2334 SER A CB    1 
ATOM   7022  O  OG    . SER A 1 2334 ? 147.997 188.089 144.163 1.00 19.29  ? 2334 SER A OG    1 
ATOM   7023  N  N     . LEU A 1 2335 ? 151.237 190.187 146.489 1.00 7.98   ? 2335 LEU A N     1 
ATOM   7024  C  CA    . LEU A 1 2335 ? 151.995 191.325 146.993 1.00 7.15   ? 2335 LEU A CA    1 
ATOM   7025  C  C     . LEU A 1 2335 ? 151.773 192.536 146.098 1.00 10.07  ? 2335 LEU A C     1 
ATOM   7026  O  O     . LEU A 1 2335 ? 152.101 192.481 144.906 1.00 14.32  ? 2335 LEU A O     1 
ATOM   7027  C  CB    . LEU A 1 2335 ? 153.479 190.980 147.060 1.00 9.09   ? 2335 LEU A CB    1 
ATOM   7028  C  CG    . LEU A 1 2335 ? 154.358 191.864 147.945 1.00 10.08  ? 2335 LEU A CG    1 
ATOM   7029  C  CD1   . LEU A 1 2335 ? 153.816 191.915 149.357 1.00 8.41   ? 2335 LEU A CD1   1 
ATOM   7030  C  CD2   . LEU A 1 2335 ? 155.792 191.360 147.939 1.00 13.11  ? 2335 LEU A CD2   1 
ATOM   7031  N  N     . PRO A 1 2336 ? 151.222 193.637 146.614 1.00 7.39   ? 2336 PRO A N     1 
ATOM   7032  C  CA    . PRO A 1 2336 ? 151.028 194.814 145.774 1.00 6.98   ? 2336 PRO A CA    1 
ATOM   7033  C  C     . PRO A 1 2336 ? 152.360 195.432 145.394 1.00 10.89  ? 2336 PRO A C     1 
ATOM   7034  O  O     . PRO A 1 2336 ? 153.359 195.284 146.119 1.00 13.32  ? 2336 PRO A O     1 
ATOM   7035  C  CB    . PRO A 1 2336 ? 150.205 195.757 146.670 1.00 10.68  ? 2336 PRO A CB    1 
ATOM   7036  C  CG    . PRO A 1 2336 ? 149.604 194.876 147.715 1.00 10.99  ? 2336 PRO A CG    1 
ATOM   7037  C  CD    . PRO A 1 2336 ? 150.608 193.795 147.942 1.00 9.75   ? 2336 PRO A CD    1 
ATOM   7038  N  N     . PRO A 1 2337 ? 152.427 196.133 144.259 1.00 9.43   ? 2337 PRO A N     1 
ATOM   7039  C  CA    . PRO A 1 2337 ? 153.709 196.714 143.828 1.00 10.99  ? 2337 PRO A CA    1 
ATOM   7040  C  C     . PRO A 1 2337 ? 154.247 197.792 144.754 1.00 11.42  ? 2337 PRO A C     1 
ATOM   7041  O  O     . PRO A 1 2337 ? 155.440 198.111 144.673 1.00 12.98  ? 2337 PRO A O     1 
ATOM   7042  C  CB    . PRO A 1 2337 ? 153.386 197.283 142.439 1.00 10.65  ? 2337 PRO A CB    1 
ATOM   7043  C  CG    . PRO A 1 2337 ? 151.909 197.487 142.445 1.00 9.55   ? 2337 PRO A CG    1 
ATOM   7044  C  CD    . PRO A 1 2337 ? 151.348 196.386 143.290 1.00 8.16   ? 2337 PRO A CD    1 
ATOM   7045  N  N     . ASN A 1 2338 ? 153.420 198.363 145.625 1.00 9.07   ? 2338 ASN A N     1 
ATOM   7046  C  CA    . ASN A 1 2338 ? 153.855 199.425 146.522 1.00 8.25   ? 2338 ASN A CA    1 
ATOM   7047  C  C     . ASN A 1 2338 ? 154.367 198.905 147.858 1.00 10.26  ? 2338 ASN A C     1 
ATOM   7048  O  O     . ASN A 1 2338 ? 154.686 199.711 148.739 1.00 13.38  ? 2338 ASN A O     1 
ATOM   7049  C  CB    . ASN A 1 2338 ? 152.710 200.415 146.763 1.00 9.72   ? 2338 ASN A CB    1 
ATOM   7050  C  CG    . ASN A 1 2338 ? 151.577 199.811 147.569 1.00 14.00  ? 2338 ASN A CG    1 
ATOM   7051  O  OD1   . ASN A 1 2338 ? 150.971 198.820 147.165 1.00 15.89  ? 2338 ASN A OD1   1 
ATOM   7052  N  ND2   . ASN A 1 2338 ? 151.286 200.409 148.718 1.00 14.42  ? 2338 ASN A ND2   1 
ATOM   7053  N  N     . VAL A 1 2339 ? 154.457 197.589 148.032 1.00 9.98   ? 2339 VAL A N     1 
ATOM   7054  C  CA    . VAL A 1 2339 ? 154.853 196.983 149.298 1.00 6.98   ? 2339 VAL A CA    1 
ATOM   7055  C  C     . VAL A 1 2339 ? 156.270 196.441 149.169 1.00 8.40   ? 2339 VAL A C     1 
ATOM   7056  O  O     . VAL A 1 2339 ? 156.607 195.789 148.173 1.00 12.85  ? 2339 VAL A O     1 
ATOM   7057  C  CB    . VAL A 1 2339 ? 153.874 195.871 149.711 1.00 6.00   ? 2339 VAL A CB    1 
ATOM   7058  C  CG1   . VAL A 1 2339 ? 154.303 195.241 151.027 1.00 8.11   ? 2339 VAL A CG1   1 
ATOM   7059  C  CG2   . VAL A 1 2339 ? 152.462 196.421 149.816 1.00 7.79   ? 2339 VAL A CG2   1 
ATOM   7060  N  N     . ARG A 1 2340 ? 157.099 196.715 150.172 1.00 5.51   ? 2340 ARG A N     1 
ATOM   7061  C  CA    . ARG A 1 2340 ? 158.449 196.175 150.265 1.00 5.97   ? 2340 ARG A CA    1 
ATOM   7062  C  C     . ARG A 1 2340 ? 158.572 195.337 151.529 1.00 6.55   ? 2340 ARG A C     1 
ATOM   7063  O  O     . ARG A 1 2340 ? 158.098 195.742 152.595 1.00 6.66   ? 2340 ARG A O     1 
ATOM   7064  C  CB    . ARG A 1 2340 ? 159.496 197.291 150.276 1.00 7.06   ? 2340 ARG A CB    1 
ATOM   7065  C  CG    . ARG A 1 2340 ? 159.576 198.101 148.997 1.00 7.78   ? 2340 ARG A CG    1 
ATOM   7066  C  CD    . ARG A 1 2340 ? 160.093 197.258 147.845 1.00 6.61   ? 2340 ARG A CD    1 
ATOM   7067  N  NE    . ARG A 1 2340 ? 160.230 198.037 146.621 1.00 9.17   ? 2340 ARG A NE    1 
ATOM   7068  C  CZ    . ARG A 1 2340 ? 159.222 198.375 145.829 1.00 9.68   ? 2340 ARG A CZ    1 
ATOM   7069  N  NH1   . ARG A 1 2340 ? 157.979 198.013 146.099 1.00 7.43   ? 2340 ARG A NH1   1 
ATOM   7070  N  NH2   . ARG A 1 2340 ? 159.468 199.094 144.738 1.00 13.07  ? 2340 ARG A NH2   1 
ATOM   7071  N  N     . ILE A 1 2341 ? 159.205 194.175 151.408 1.00 6.85   ? 2341 ILE A N     1 
ATOM   7072  C  CA    . ILE A 1 2341 ? 159.488 193.309 152.546 1.00 5.06   ? 2341 ILE A CA    1 
ATOM   7073  C  C     . ILE A 1 2341 ? 160.955 193.480 152.911 1.00 5.35   ? 2341 ILE A C     1 
ATOM   7074  O  O     . ILE A 1 2341 ? 161.844 193.141 152.121 1.00 5.60   ? 2341 ILE A O     1 
ATOM   7075  C  CB    . ILE A 1 2341 ? 159.158 191.841 152.235 1.00 4.98   ? 2341 ILE A CB    1 
ATOM   7076  C  CG1   . ILE A 1 2341 ? 157.710 191.710 151.763 1.00 6.05   ? 2341 ILE A CG1   1 
ATOM   7077  C  CG2   . ILE A 1 2341 ? 159.412 190.969 153.454 1.00 5.91   ? 2341 ILE A CG2   1 
ATOM   7078  C  CD1   . ILE A 1 2341 ? 156.694 192.149 152.794 1.00 5.38   ? 2341 ILE A CD1   1 
ATOM   7079  N  N     . MET A 1 2342 ? 161.210 194.005 154.106 1.00 5.94   ? 2342 MET A N     1 
ATOM   7080  C  CA    . MET A 1 2342 ? 162.558 194.286 154.574 1.00 5.58   ? 2342 MET A CA    1 
ATOM   7081  C  C     . MET A 1 2342 ? 162.892 193.419 155.777 1.00 4.64   ? 2342 MET A C     1 
ATOM   7082  O  O     . MET A 1 2342 ? 162.022 193.115 156.599 1.00 4.29   ? 2342 MET A O     1 
ATOM   7083  C  CB    . MET A 1 2342 ? 162.724 195.763 154.943 1.00 4.98   ? 2342 MET A CB    1 
ATOM   7084  C  CG    . MET A 1 2342 ? 162.095 196.735 153.965 1.00 7.53   ? 2342 MET A CG    1 
ATOM   7085  S  SD    . MET A 1 2342 ? 163.143 198.182 153.730 1.00 28.78  ? 2342 MET A SD    1 
ATOM   7086  C  CE    . MET A 1 2342 ? 162.435 198.888 152.249 1.00 9.74   ? 2342 MET A CE    1 
ATOM   7087  N  N     . PHE A 1 2343 ? 164.159 193.023 155.871 1.00 5.25   ? 2343 PHE A N     1 
ATOM   7088  C  CA    . PHE A 1 2343 ? 164.679 192.276 157.011 1.00 4.54   ? 2343 PHE A CA    1 
ATOM   7089  C  C     . PHE A 1 2343 ? 165.869 193.046 157.566 1.00 4.89   ? 2343 PHE A C     1 
ATOM   7090  O  O     . PHE A 1 2343 ? 166.920 193.118 156.922 1.00 7.17   ? 2343 PHE A O     1 
ATOM   7091  C  CB    . PHE A 1 2343 ? 165.093 190.859 156.612 1.00 4.85   ? 2343 PHE A CB    1 
ATOM   7092  C  CG    . PHE A 1 2343 ? 164.006 190.068 155.944 1.00 4.95   ? 2343 PHE A CG    1 
ATOM   7093  C  CD1   . PHE A 1 2343 ? 163.764 190.201 154.588 1.00 4.62   ? 2343 PHE A CD1   1 
ATOM   7094  C  CD2   . PHE A 1 2343 ? 163.233 189.182 156.671 1.00 5.05   ? 2343 PHE A CD2   1 
ATOM   7095  C  CE1   . PHE A 1 2343 ? 162.769 189.473 153.972 1.00 4.80   ? 2343 PHE A CE1   1 
ATOM   7096  C  CE2   . PHE A 1 2343 ? 162.236 188.450 156.061 1.00 5.15   ? 2343 PHE A CE2   1 
ATOM   7097  C  CZ    . PHE A 1 2343 ? 162.004 188.596 154.710 1.00 4.42   ? 2343 PHE A CZ    1 
ATOM   7098  N  N     . GLU A 1 2344 ? 165.707 193.620 158.754 1.00 3.58   ? 2344 GLU A N     1 
ATOM   7099  C  CA    . GLU A 1 2344 ? 166.798 194.293 159.451 1.00 3.26   ? 2344 GLU A CA    1 
ATOM   7100  C  C     . GLU A 1 2344 ? 167.394 193.299 160.441 1.00 3.91   ? 2344 GLU A C     1 
ATOM   7101  O  O     . GLU A 1 2344 ? 166.794 193.014 161.482 1.00 5.50   ? 2344 GLU A O     1 
ATOM   7102  C  CB    . GLU A 1 2344 ? 166.307 195.551 160.158 1.00 4.57   ? 2344 GLU A CB    1 
ATOM   7103  C  CG    . GLU A 1 2344 ? 167.415 196.353 160.810 1.00 2.44   ? 2344 GLU A CG    1 
ATOM   7104  C  CD    . GLU A 1 2344 ? 166.884 197.509 161.622 1.00 3.44   ? 2344 GLU A CD    1 
ATOM   7105  O  OE1   . GLU A 1 2344 ? 166.031 198.254 161.098 1.00 5.95   ? 2344 GLU A OE1   1 
ATOM   7106  O  OE2   . GLU A 1 2344 ? 167.324 197.677 162.778 1.00 3.62   ? 2344 GLU A OE2   1 
ATOM   7107  N  N     . VAL A 1 2345 ? 168.575 192.775 160.116 1.00 4.24   ? 2345 VAL A N     1 
ATOM   7108  C  CA    . VAL A 1 2345 ? 169.178 191.689 160.873 1.00 4.28   ? 2345 VAL A CA    1 
ATOM   7109  C  C     . VAL A 1 2345 ? 170.606 192.062 161.242 1.00 5.45   ? 2345 VAL A C     1 
ATOM   7110  O  O     . VAL A 1 2345 ? 171.212 192.962 160.658 1.00 5.15   ? 2345 VAL A O     1 
ATOM   7111  C  CB    . VAL A 1 2345 ? 169.164 190.360 160.090 1.00 5.52   ? 2345 VAL A CB    1 
ATOM   7112  C  CG1   . VAL A 1 2345 ? 167.740 189.895 159.863 1.00 6.65   ? 2345 VAL A CG1   1 
ATOM   7113  C  CG2   . VAL A 1 2345 ? 169.897 190.516 158.769 1.00 6.24   ? 2345 VAL A CG2   1 
ATOM   7114  N  N     . GLN A 1 2346 ? 171.138 191.350 162.235 1.00 8.57   ? 2346 GLN A N     1 
ATOM   7115  C  CA    . GLN A 1 2346 ? 172.530 191.504 162.630 1.00 7.27   ? 2346 GLN A CA    1 
ATOM   7116  C  C     . GLN A 1 2346 ? 173.427 190.386 162.117 1.00 10.61  ? 2346 GLN A C     1 
ATOM   7117  O  O     . GLN A 1 2346 ? 174.649 190.563 162.080 1.00 17.68  ? 2346 GLN A O     1 
ATOM   7118  C  CB    . GLN A 1 2346 ? 172.649 191.592 164.157 1.00 7.44   ? 2346 GLN A CB    1 
ATOM   7119  C  CG    . GLN A 1 2346 ? 172.200 190.346 164.891 1.00 11.17  ? 2346 GLN A CG    1 
ATOM   7120  C  CD    . GLN A 1 2346 ? 172.618 190.345 166.347 1.00 12.46  ? 2346 GLN A CD    1 
ATOM   7121  O  OE1   . GLN A 1 2346 ? 173.499 191.103 166.753 1.00 10.77  ? 2346 GLN A OE1   1 
ATOM   7122  N  NE2   . GLN A 1 2346 ? 171.986 189.491 167.143 1.00 10.52  ? 2346 GLN A NE2   1 
ATOM   7123  N  N     . ASP A 1 2347 ? 172.855 189.252 161.720 1.00 10.40  ? 2347 ASP A N     1 
ATOM   7124  C  CA    . ASP A 1 2347 ? 173.628 188.153 161.163 1.00 10.27  ? 2347 ASP A CA    1 
ATOM   7125  C  C     . ASP A 1 2347 ? 172.702 187.281 160.330 1.00 12.46  ? 2347 ASP A C     1 
ATOM   7126  O  O     . ASP A 1 2347 ? 171.477 187.396 160.406 1.00 14.81  ? 2347 ASP A O     1 
ATOM   7127  C  CB    . ASP A 1 2347 ? 174.307 187.322 162.257 1.00 13.55  ? 2347 ASP A CB    1 
ATOM   7128  C  CG    . ASP A 1 2347 ? 173.312 186.692 163.211 1.00 20.60  ? 2347 ASP A CG    1 
ATOM   7129  O  OD1   . ASP A 1 2347 ? 173.059 185.477 163.091 1.00 26.72  ? 2347 ASP A OD1   1 
ATOM   7130  O  OD2   . ASP A 1 2347 ? 172.786 187.405 164.087 1.00 18.43  ? 2347 ASP A OD2   1 
ATOM   7131  N  N     . LEU A 1 2348 ? 173.309 186.406 159.527 1.00 13.08  ? 2348 LEU A N     1 
ATOM   7132  C  CA    . LEU A 1 2348 ? 172.572 185.453 158.705 1.00 12.97  ? 2348 LEU A CA    1 
ATOM   7133  C  C     . LEU A 1 2348 ? 173.176 184.059 158.808 1.00 16.03  ? 2348 LEU A C     1 
ATOM   7134  O  O     . LEU A 1 2348 ? 173.103 183.273 157.859 1.00 24.41  ? 2348 LEU A O     1 
ATOM   7135  C  CB    . LEU A 1 2348 ? 172.524 185.907 157.246 1.00 12.61  ? 2348 LEU A CB    1 
ATOM   7136  C  CG    . LEU A 1 2348 ? 171.519 187.008 156.900 1.00 11.19  ? 2348 LEU A CG    1 
ATOM   7137  C  CD1   . LEU A 1 2348 ? 171.644 187.409 155.440 1.00 12.81  ? 2348 LEU A CD1   1 
ATOM   7138  C  CD2   . LEU A 1 2348 ? 170.102 186.559 157.215 1.00 10.23  ? 2348 LEU A CD2   1 
ATOM   7139  N  N     . LYS A 1 2349 ? 173.774 183.734 159.956 1.00 15.05  ? 2349 LYS A N     1 
ATOM   7140  C  CA    . LYS A 1 2349 ? 174.445 182.450 160.123 1.00 18.95  ? 2349 LYS A CA    1 
ATOM   7141  C  C     . LYS A 1 2349 ? 173.482 181.272 160.136 1.00 16.75  ? 2349 LYS A C     1 
ATOM   7142  O  O     . LYS A 1 2349 ? 173.932 180.128 160.010 1.00 18.75  ? 2349 LYS A O     1 
ATOM   7143  C  CB    . LYS A 1 2349 ? 175.269 182.451 161.412 1.00 18.30  ? 2349 LYS A CB    1 
ATOM   7144  C  CG    . LYS A 1 2349 ? 174.458 182.736 162.661 1.00 15.86  ? 2349 LYS A CG    1 
ATOM   7145  C  CD    . LYS A 1 2349 ? 175.353 182.958 163.867 1.00 16.87  ? 2349 LYS A CD    1 
ATOM   7146  C  CE    . LYS A 1 2349 ? 176.026 181.670 164.304 1.00 22.55  ? 2349 LYS A CE    1 
ATOM   7147  N  NZ    . LYS A 1 2349 ? 176.800 181.854 165.562 1.00 26.73  ? 2349 LYS A NZ    1 
ATOM   7148  N  N     . TYR A 1 2350 ? 172.180 181.515 160.285 1.00 12.72  ? 2350 TYR A N     1 
ATOM   7149  C  CA    . TYR A 1 2350 ? 171.190 180.450 160.288 1.00 13.74  ? 2350 TYR A CA    1 
ATOM   7150  C  C     . TYR A 1 2350 ? 170.293 180.456 159.060 1.00 18.39  ? 2350 TYR A C     1 
ATOM   7151  O  O     . TYR A 1 2350 ? 169.572 179.477 158.839 1.00 20.03  ? 2350 TYR A O     1 
ATOM   7152  C  CB    . TYR A 1 2350 ? 170.327 180.536 161.555 1.00 16.94  ? 2350 TYR A CB    1 
ATOM   7153  C  CG    . TYR A 1 2350 ? 171.101 180.241 162.819 1.00 14.17  ? 2350 TYR A CG    1 
ATOM   7154  C  CD1   . TYR A 1 2350 ? 171.559 178.961 163.090 1.00 13.98  ? 2350 TYR A CD1   1 
ATOM   7155  C  CD2   . TYR A 1 2350 ? 171.392 181.247 163.729 1.00 12.54  ? 2350 TYR A CD2   1 
ATOM   7156  C  CE1   . TYR A 1 2350 ? 172.272 178.686 164.238 1.00 16.11  ? 2350 TYR A CE1   1 
ATOM   7157  C  CE2   . TYR A 1 2350 ? 172.107 180.982 164.879 1.00 16.83  ? 2350 TYR A CE2   1 
ATOM   7158  C  CZ    . TYR A 1 2350 ? 172.543 179.700 165.130 1.00 18.65  ? 2350 TYR A CZ    1 
ATOM   7159  O  OH    . TYR A 1 2350 ? 173.254 179.432 166.276 1.00 22.08  ? 2350 TYR A OH    1 
ATOM   7160  N  N     . ALA A 1 2351 ? 170.318 181.518 158.260 1.00 24.39  ? 2351 ALA A N     1 
ATOM   7161  C  CA    . ALA A 1 2351 ? 169.542 181.550 157.031 1.00 17.56  ? 2351 ALA A CA    1 
ATOM   7162  C  C     . ALA A 1 2351 ? 170.124 180.586 156.004 1.00 18.44  ? 2351 ALA A C     1 
ATOM   7163  O  O     . ALA A 1 2351 ? 171.328 180.315 155.983 1.00 19.50  ? 2351 ALA A O     1 
ATOM   7164  C  CB    . ALA A 1 2351 ? 169.504 182.966 156.458 1.00 15.05  ? 2351 ALA A CB    1 
ATOM   7165  N  N     . THR A 1 2352 ? 169.252 180.064 155.147 1.00 20.47  ? 2352 THR A N     1 
ATOM   7166  C  CA    . THR A 1 2352 ? 169.662 179.126 154.117 1.00 21.07  ? 2352 THR A CA    1 
ATOM   7167  C  C     . THR A 1 2352 ? 169.871 179.856 152.792 1.00 21.03  ? 2352 THR A C     1 
ATOM   7168  O  O     . THR A 1 2352 ? 169.634 181.060 152.668 1.00 21.03  ? 2352 THR A O     1 
ATOM   7169  C  CB    . THR A 1 2352 ? 168.630 178.009 153.970 1.00 24.94  ? 2352 THR A CB    1 
ATOM   7170  O  OG1   . THR A 1 2352 ? 167.365 178.571 153.599 1.00 27.72  ? 2352 THR A OG1   1 
ATOM   7171  C  CG2   . THR A 1 2352 ? 168.479 177.250 155.278 1.00 22.61  ? 2352 THR A CG2   1 
ATOM   7172  N  N     . LEU A 1 2353 ? 170.329 179.112 151.783 1.00 27.11  ? 2353 LEU A N     1 
ATOM   7173  C  CA    . LEU A 1 2353 ? 170.588 179.709 150.477 1.00 22.55  ? 2353 LEU A CA    1 
ATOM   7174  C  C     . LEU A 1 2353 ? 169.304 180.167 149.799 1.00 18.27  ? 2353 LEU A C     1 
ATOM   7175  O  O     . LEU A 1 2353 ? 169.333 181.108 148.997 1.00 18.84  ? 2353 LEU A O     1 
ATOM   7176  C  CB    . LEU A 1 2353 ? 171.333 178.718 149.584 1.00 26.91  ? 2353 LEU A CB    1 
ATOM   7177  C  CG    . LEU A 1 2353 ? 172.148 179.326 148.442 1.00 31.36  ? 2353 LEU A CG    1 
ATOM   7178  C  CD1   . LEU A 1 2353 ? 173.540 179.704 148.922 1.00 30.42  ? 2353 LEU A CD1   1 
ATOM   7179  C  CD2   . LEU A 1 2353 ? 172.223 178.366 147.265 1.00 30.03  ? 2353 LEU A CD2   1 
ATOM   7180  N  N     . ALA A 1 2354 ? 168.177 179.516 150.098 1.00 17.73  ? 2354 ALA A N     1 
ATOM   7181  C  CA    . ALA A 1 2354 ? 166.915 179.900 149.474 1.00 18.15  ? 2354 ALA A CA    1 
ATOM   7182  C  C     . ALA A 1 2354 ? 166.514 181.318 149.857 1.00 14.50  ? 2354 ALA A C     1 
ATOM   7183  O  O     . ALA A 1 2354 ? 166.083 182.101 149.004 1.00 14.46  ? 2354 ALA A O     1 
ATOM   7184  C  CB    . ALA A 1 2354 ? 165.818 178.908 149.860 1.00 19.21  ? 2354 ALA A CB    1 
ATOM   7185  N  N     . THR A 1 2355 ? 166.654 181.670 151.136 1.00 15.72  ? 2355 THR A N     1 
ATOM   7186  C  CA    . THR A 1 2355 ? 166.258 183.002 151.583 1.00 14.01  ? 2355 THR A CA    1 
ATOM   7187  C  C     . THR A 1 2355 ? 167.218 184.071 151.076 1.00 13.95  ? 2355 THR A C     1 
ATOM   7188  O  O     . THR A 1 2355 ? 166.786 185.141 150.634 1.00 16.93  ? 2355 THR A O     1 
ATOM   7189  C  CB    . THR A 1 2355 ? 166.175 183.042 153.108 1.00 15.67  ? 2355 THR A CB    1 
ATOM   7190  O  OG1   . THR A 1 2355 ? 165.460 181.892 153.579 1.00 20.56  ? 2355 THR A OG1   1 
ATOM   7191  C  CG2   . THR A 1 2355 ? 165.460 184.298 153.565 1.00 12.33  ? 2355 THR A CG2   1 
ATOM   7192  N  N     . VAL A 1 2356 ? 168.523 183.800 151.135 1.00 15.03  ? 2356 VAL A N     1 
ATOM   7193  C  CA    . VAL A 1 2356 ? 169.514 184.802 150.753 1.00 12.95  ? 2356 VAL A CA    1 
ATOM   7194  C  C     . VAL A 1 2356 ? 169.410 185.123 149.267 1.00 15.33  ? 2356 VAL A C     1 
ATOM   7195  O  O     . VAL A 1 2356 ? 169.587 186.274 148.851 1.00 22.39  ? 2356 VAL A O     1 
ATOM   7196  C  CB    . VAL A 1 2356 ? 170.925 184.319 151.136 1.00 18.08  ? 2356 VAL A CB    1 
ATOM   7197  C  CG1   . VAL A 1 2356 ? 171.983 185.302 150.656 1.00 16.97  ? 2356 VAL A CG1   1 
ATOM   7198  C  CG2   . VAL A 1 2356 ? 171.023 184.109 152.639 1.00 13.39  ? 2356 VAL A CG2   1 
ATOM   7199  N  N     . SER A 1 2357 ? 169.110 184.115 148.445 1.00 13.78  ? 2357 SER A N     1 
ATOM   7200  C  CA    . SER A 1 2357 ? 169.048 184.324 147.002 1.00 10.56  ? 2357 SER A CA    1 
ATOM   7201  C  C     . SER A 1 2357 ? 167.881 185.217 146.597 1.00 14.76  ? 2357 SER A C     1 
ATOM   7202  O  O     . SER A 1 2357 ? 167.998 185.985 145.636 1.00 15.84  ? 2357 SER A O     1 
ATOM   7203  C  CB    . SER A 1 2357 ? 168.954 182.978 146.285 1.00 10.85  ? 2357 SER A CB    1 
ATOM   7204  O  OG    . SER A 1 2357 ? 167.780 182.282 146.665 1.00 14.98  ? 2357 SER A OG    1 
ATOM   7205  N  N     . ARG A 1 2358 ? 166.759 185.140 147.311 1.00 11.82  ? 2358 ARG A N     1 
ATOM   7206  C  CA    . ARG A 1 2358 ? 165.528 185.813 146.917 1.00 11.55  ? 2358 ARG A CA    1 
ATOM   7207  C  C     . ARG A 1 2358 ? 165.480 187.280 147.328 1.00 17.98  ? 2358 ARG A C     1 
ATOM   7208  O  O     . ARG A 1 2358 ? 164.523 187.974 146.973 1.00 23.02  ? 2358 ARG A O     1 
ATOM   7209  C  CB    . ARG A 1 2358 ? 164.317 185.092 147.513 1.00 15.50  ? 2358 ARG A CB    1 
ATOM   7210  C  CG    . ARG A 1 2358 ? 164.128 183.659 147.059 1.00 11.92  ? 2358 ARG A CG    1 
ATOM   7211  C  CD    . ARG A 1 2358 ? 163.077 182.973 147.919 1.00 10.67  ? 2358 ARG A CD    1 
ATOM   7212  N  NE    . ARG A 1 2358 ? 162.419 181.865 147.239 1.00 9.89   ? 2358 ARG A NE    1 
ATOM   7213  C  CZ    . ARG A 1 2358 ? 162.991 180.700 146.967 1.00 13.54  ? 2358 ARG A CZ    1 
ATOM   7214  N  NH1   . ARG A 1 2358 ? 164.242 180.445 147.314 1.00 21.45  ? 2358 ARG A NH1   1 
ATOM   7215  N  NH2   . ARG A 1 2358 ? 162.289 179.765 146.334 1.00 16.01  ? 2358 ARG A NH2   1 
ATOM   7216  N  N     . CYS A 1 2359 ? 166.476 187.768 148.061 1.00 15.04  ? 2359 CYS A N     1 
ATOM   7217  C  CA    . CYS A 1 2359 ? 166.409 189.105 148.632 1.00 12.99  ? 2359 CYS A CA    1 
ATOM   7218  C  C     . CYS A 1 2359 ? 167.590 189.939 148.165 1.00 14.68  ? 2359 CYS A C     1 
ATOM   7219  O  O     . CYS A 1 2359 ? 168.691 189.417 147.966 1.00 24.04  ? 2359 CYS A O     1 
ATOM   7220  C  CB    . CYS A 1 2359 ? 166.392 189.053 150.166 1.00 15.63  ? 2359 CYS A CB    1 
ATOM   7221  S  SG    . CYS A 1 2359 ? 164.820 188.534 150.887 1.00 27.65  ? 2359 CYS A SG    1 
ATOM   7222  N  N     . GLY A 1 2360 ? 167.350 191.235 147.983 1.00 12.32  ? 2360 GLY A N     1 
ATOM   7223  C  CA    . GLY A 1 2360 ? 168.445 192.164 147.800 1.00 8.27   ? 2360 GLY A CA    1 
ATOM   7224  C  C     . GLY A 1 2360 ? 169.105 192.497 149.123 1.00 6.50   ? 2360 GLY A C     1 
ATOM   7225  O  O     . GLY A 1 2360 ? 168.456 192.586 150.165 1.00 9.89   ? 2360 GLY A O     1 
ATOM   7226  N  N     . MET A 1 2361 ? 170.419 192.684 149.083 1.00 6.93   ? 2361 MET A N     1 
ATOM   7227  C  CA    . MET A 1 2361 ? 171.220 192.792 150.293 1.00 4.71   ? 2361 MET A CA    1 
ATOM   7228  C  C     . MET A 1 2361 ? 171.997 194.099 150.302 1.00 4.70   ? 2361 MET A C     1 
ATOM   7229  O  O     . MET A 1 2361 ? 172.659 194.442 149.318 1.00 8.92   ? 2361 MET A O     1 
ATOM   7230  C  CB    . MET A 1 2361 ? 172.184 191.610 150.413 1.00 6.40   ? 2361 MET A CB    1 
ATOM   7231  C  CG    . MET A 1 2361 ? 171.490 190.270 150.558 1.00 9.64   ? 2361 MET A CG    1 
ATOM   7232  S  SD    . MET A 1 2361 ? 171.399 189.707 152.263 1.00 27.92  ? 2361 MET A SD    1 
ATOM   7233  C  CE    . MET A 1 2361 ? 170.305 188.302 152.081 1.00 21.33  ? 2361 MET A CE    1 
ATOM   7234  N  N     . VAL A 1 2362 ? 171.908 194.821 151.415 1.00 4.45   ? 2362 VAL A N     1 
ATOM   7235  C  CA    . VAL A 1 2362 ? 172.764 195.965 151.698 1.00 5.46   ? 2362 VAL A CA    1 
ATOM   7236  C  C     . VAL A 1 2362 ? 173.521 195.648 152.978 1.00 5.93   ? 2362 VAL A C     1 
ATOM   7237  O  O     . VAL A 1 2362 ? 172.906 195.402 154.023 1.00 4.97   ? 2362 VAL A O     1 
ATOM   7238  C  CB    . VAL A 1 2362 ? 171.962 197.267 151.841 1.00 5.15   ? 2362 VAL A CB    1 
ATOM   7239  C  CG1   . VAL A 1 2362 ? 172.900 198.461 151.908 1.00 4.74   ? 2362 VAL A CG1   1 
ATOM   7240  C  CG2   . VAL A 1 2362 ? 170.984 197.417 150.688 1.00 6.95   ? 2362 VAL A CG2   1 
ATOM   7241  N  N     . TRP A 1 2363 ? 174.848 195.652 152.901 1.00 6.13   ? 2363 TRP A N     1 
ATOM   7242  C  CA    . TRP A 1 2363 ? 175.695 195.294 154.030 1.00 5.35   ? 2363 TRP A CA    1 
ATOM   7243  C  C     . TRP A 1 2363 ? 176.112 196.555 154.774 1.00 6.17   ? 2363 TRP A C     1 
ATOM   7244  O  O     . TRP A 1 2363 ? 176.701 197.465 154.182 1.00 9.06   ? 2363 TRP A O     1 
ATOM   7245  C  CB    . TRP A 1 2363 ? 176.928 194.517 153.571 1.00 8.83   ? 2363 TRP A CB    1 
ATOM   7246  C  CG    . TRP A 1 2363 ? 177.981 194.412 154.633 1.00 10.12  ? 2363 TRP A CG    1 
ATOM   7247  C  CD1   . TRP A 1 2363 ? 179.143 195.122 154.708 1.00 9.94   ? 2363 TRP A CD1   1 
ATOM   7248  C  CD2   . TRP A 1 2363 ? 177.956 193.561 155.784 1.00 8.43   ? 2363 TRP A CD2   1 
ATOM   7249  N  NE1   . TRP A 1 2363 ? 179.849 194.758 155.829 1.00 7.58   ? 2363 TRP A NE1   1 
ATOM   7250  C  CE2   . TRP A 1 2363 ? 179.140 193.802 156.507 1.00 7.59   ? 2363 TRP A CE2   1 
ATOM   7251  C  CE3   . TRP A 1 2363 ? 177.048 192.615 156.271 1.00 8.50   ? 2363 TRP A CE3   1 
ATOM   7252  C  CZ2   . TRP A 1 2363 ? 179.442 193.132 157.690 1.00 7.56   ? 2363 TRP A CZ2   1 
ATOM   7253  C  CZ3   . TRP A 1 2363 ? 177.349 191.951 157.444 1.00 9.38   ? 2363 TRP A CZ3   1 
ATOM   7254  C  CH2   . TRP A 1 2363 ? 178.536 192.213 158.141 1.00 7.08   ? 2363 TRP A CH2   1 
ATOM   7255  N  N     . PHE A 1 2364 ? 175.809 196.596 156.073 1.00 5.41   ? 2364 PHE A N     1 
ATOM   7256  C  CA    . PHE A 1 2364 ? 176.223 197.747 156.918 1.00 5.46   ? 2364 PHE A CA    1 
ATOM   7257  C  C     . PHE A 1 2364 ? 177.342 197.278 157.839 1.00 6.95   ? 2364 PHE A C     1 
ATOM   7258  O  O     . PHE A 1 2364 ? 177.278 196.135 158.337 1.00 8.58   ? 2364 PHE A O     1 
ATOM   7259  C  CB    . PHE A 1 2364 ? 175.026 198.261 157.722 1.00 4.99   ? 2364 PHE A CB    1 
ATOM   7260  C  CG    . PHE A 1 2364 ? 173.936 198.936 156.901 1.00 2.21   ? 2364 PHE A CG    1 
ATOM   7261  C  CD1   . PHE A 1 2364 ? 172.953 198.185 156.267 1.00 2.32   ? 2364 PHE A CD1   1 
ATOM   7262  C  CD2   . PHE A 1 2364 ? 173.883 200.320 156.789 1.00 1.56   ? 2364 PHE A CD2   1 
ATOM   7263  C  CE1   . PHE A 1 2364 ? 171.959 198.803 155.526 1.00 1.60   ? 2364 PHE A CE1   1 
ATOM   7264  C  CE2   . PHE A 1 2364 ? 172.884 200.932 156.050 1.00 1.15   ? 2364 PHE A CE2   1 
ATOM   7265  C  CZ    . PHE A 1 2364 ? 171.926 200.173 155.421 1.00 1.26   ? 2364 PHE A CZ    1 
ATOM   7266  N  N     . SER A 1 2365 ? 178.345 198.131 158.056 1.00 8.14   ? 2365 SER A N     1 
ATOM   7267  C  CA    . SER A 1 2365 ? 179.478 197.777 158.947 1.00 8.53   ? 2365 SER A CA    1 
ATOM   7268  C  C     . SER A 1 2365 ? 179.536 198.771 160.113 1.00 13.75  ? 2365 SER A C     1 
ATOM   7269  O  O     . SER A 1 2365 ? 178.956 199.871 159.980 1.00 13.94  ? 2365 SER A O     1 
ATOM   7270  C  CB    . SER A 1 2365 ? 180.778 197.758 158.191 1.00 13.38  ? 2365 SER A CB    1 
ATOM   7271  O  OG    . SER A 1 2365 ? 181.133 199.066 157.765 1.00 17.43  ? 2365 SER A OG    1 
ATOM   7272  N  N     . GLU A 1 2366 ? 180.206 198.400 161.206 1.00 15.70  ? 2366 GLU A N     1 
ATOM   7273  C  CA    . GLU A 1 2366 ? 180.369 199.344 162.342 1.00 17.51  ? 2366 GLU A CA    1 
ATOM   7274  C  C     . GLU A 1 2366 ? 181.103 200.590 161.825 1.00 16.64  ? 2366 GLU A C     1 
ATOM   7275  O  O     . GLU A 1 2366 ? 180.872 201.687 162.377 1.00 21.04  ? 2366 GLU A O     1 
ATOM   7276  C  CB    . GLU A 1 2366 ? 181.119 198.677 163.494 1.00 25.57  ? 2366 GLU A CB    1 
ATOM   7277  C  CG    . GLU A 1 2366 ? 181.309 199.597 164.696 1.00 25.65  ? 2366 GLU A CG    1 
ATOM   7278  C  CD    . GLU A 1 2366 ? 182.015 198.966 165.881 1.00 31.71  ? 2366 GLU A CD    1 
ATOM   7279  O  OE1   . GLU A 1 2366 ? 182.195 199.665 166.901 1.00 30.93  ? 2366 GLU A OE1   1 
ATOM   7280  O  OE2   . GLU A 1 2366 ? 182.386 197.777 165.786 1.00 41.25  ? 2366 GLU A OE2   1 
ATOM   7281  N  N     . ASP A 1 2367 ? 181.938 200.422 160.796 1.00 16.52  ? 2367 ASP A N     1 
ATOM   7282  C  CA    . ASP A 1 2367 ? 182.683 201.568 160.204 1.00 16.22  ? 2367 ASP A CA    1 
ATOM   7283  C  C     . ASP A 1 2367 ? 181.688 202.585 159.637 1.00 18.54  ? 2367 ASP A C     1 
ATOM   7284  O  O     . ASP A 1 2367 ? 181.965 203.800 159.733 1.00 22.18  ? 2367 ASP A O     1 
ATOM   7285  C  CB    . ASP A 1 2367 ? 183.675 201.094 159.154 1.00 17.26  ? 2367 ASP A CB    1 
ATOM   7286  C  CG    . ASP A 1 2367 ? 184.648 200.019 159.614 1.00 25.65  ? 2367 ASP A CG    1 
ATOM   7287  O  OD1   . ASP A 1 2367 ? 184.554 199.608 160.789 1.00 29.50  ? 2367 ASP A OD1   1 
ATOM   7288  O  OD2   . ASP A 1 2367 ? 185.493 199.604 158.793 1.00 21.37  ? 2367 ASP A OD2   1 
ATOM   7289  N  N     . VAL A 1 2368 ? 180.577 202.106 159.069 1.00 15.30  ? 2368 VAL A N     1 
ATOM   7290  C  CA    . VAL A 1 2368 ? 179.562 203.018 158.461 1.00 12.02  ? 2368 VAL A CA    1 
ATOM   7291  C  C     . VAL A 1 2368 ? 179.111 204.026 159.528 1.00 16.07  ? 2368 VAL A C     1 
ATOM   7292  O  O     . VAL A 1 2368 ? 179.044 205.232 159.208 1.00 16.75  ? 2368 VAL A O     1 
ATOM   7293  C  CB    . VAL A 1 2368 ? 178.369 202.224 157.895 1.00 12.27  ? 2368 VAL A CB    1 
ATOM   7294  C  CG1   . VAL A 1 2368 ? 177.263 203.141 157.388 1.00 9.99   ? 2368 VAL A CG1   1 
ATOM   7295  C  CG2   . VAL A 1 2368 ? 178.801 201.247 156.810 1.00 18.39  ? 2368 VAL A CG2   1 
ATOM   7296  N  N     . LEU A 1 2369 ? 178.821 203.550 160.743 1.00 16.77  ? 2369 LEU A N     1 
ATOM   7297  C  CA    . LEU A 1 2369 ? 178.430 204.459 161.852 1.00 11.95  ? 2369 LEU A CA    1 
ATOM   7298  C  C     . LEU A 1 2369 ? 179.693 204.831 162.643 1.00 12.53  ? 2369 LEU A C     1 
ATOM   7299  O  O     . LEU A 1 2369 ? 180.062 204.071 163.561 1.00 18.57  ? 2369 LEU A O     1 
ATOM   7300  C  CB    . LEU A 1 2369 ? 177.382 203.782 162.733 1.00 10.13  ? 2369 LEU A CB    1 
ATOM   7301  C  CG    . LEU A 1 2369 ? 176.878 204.590 163.933 1.00 12.91  ? 2369 LEU A CG    1 
ATOM   7302  C  CD1   . LEU A 1 2369 ? 176.222 205.886 163.493 1.00 12.17  ? 2369 LEU A CD1   1 
ATOM   7303  C  CD2   . LEU A 1 2369 ? 175.915 203.764 164.765 1.00 7.87   ? 2369 LEU A CD2   1 
ATOM   7304  N  N     . SER A 1 2370 ? 180.328 205.952 162.291 1.00 12.78  ? 2370 SER A N     1 
ATOM   7305  C  CA    . SER A 1 2370 ? 181.580 206.373 162.971 1.00 14.97  ? 2370 SER A CA    1 
ATOM   7306  C  C     . SER A 1 2370 ? 181.264 206.870 164.387 1.00 17.55  ? 2370 SER A C     1 
ATOM   7307  O  O     . SER A 1 2370 ? 180.202 207.505 164.567 1.00 15.21  ? 2370 SER A O     1 
ATOM   7308  C  CB    . SER A 1 2370 ? 182.300 207.432 162.179 1.00 17.68  ? 2370 SER A CB    1 
ATOM   7309  O  OG    . SER A 1 2370 ? 181.609 208.671 162.245 1.00 19.02  ? 2370 SER A OG    1 
ATOM   7310  N  N     . THR A 1 2371 ? 182.151 206.593 165.347 1.00 23.71  ? 2371 THR A N     1 
ATOM   7311  C  CA    . THR A 1 2371 ? 181.946 207.074 166.709 1.00 18.44  ? 2371 THR A CA    1 
ATOM   7312  C  C     . THR A 1 2371 ? 181.732 208.584 166.740 1.00 15.73  ? 2371 THR A C     1 
ATOM   7313  O  O     . THR A 1 2371 ? 181.048 209.096 167.634 1.00 18.06  ? 2371 THR A O     1 
ATOM   7314  C  CB    . THR A 1 2371 ? 183.139 206.669 167.579 1.00 27.06  ? 2371 THR A CB    1 
ATOM   7315  O  OG1   . THR A 1 2371 ? 183.245 205.240 167.603 1.00 22.58  ? 2371 THR A OG1   1 
ATOM   7316  C  CG2   . THR A 1 2371 ? 182.971 207.163 169.006 1.00 24.95  ? 2371 THR A CG2   1 
ATOM   7317  N  N     . ASP A 1 2372 ? 182.285 209.304 165.760 1.00 19.40  ? 2372 ASP A N     1 
ATOM   7318  C  CA    . ASP A 1 2372 ? 182.099 210.751 165.702 1.00 20.04  ? 2372 ASP A CA    1 
ATOM   7319  C  C     . ASP A 1 2372 ? 180.630 211.115 165.531 1.00 20.80  ? 2372 ASP A C     1 
ATOM   7320  O  O     . ASP A 1 2372 ? 180.146 212.078 166.138 1.00 23.04  ? 2372 ASP A O     1 
ATOM   7321  C  CB    . ASP A 1 2372 ? 182.924 211.339 164.558 1.00 22.64  ? 2372 ASP A CB    1 
ATOM   7322  C  CG    . ASP A 1 2372 ? 184.376 210.916 164.608 1.00 38.24  ? 2372 ASP A CG    1 
ATOM   7323  O  OD1   . ASP A 1 2372 ? 185.222 211.750 164.989 1.00 45.44  ? 2372 ASP A OD1   1 
ATOM   7324  O  OD2   . ASP A 1 2372 ? 184.672 209.752 164.265 1.00 35.36  ? 2372 ASP A OD2   1 
ATOM   7325  N  N     . MET A 1 2373 ? 179.906 210.361 164.702 1.00 17.99  ? 2373 MET A N     1 
ATOM   7326  C  CA    . MET A 1 2373 ? 178.511 210.692 164.435 1.00 12.06  ? 2373 MET A CA    1 
ATOM   7327  C  C     . MET A 1 2373 ? 177.628 210.379 165.636 1.00 13.61  ? 2373 MET A C     1 
ATOM   7328  O  O     . MET A 1 2373 ? 176.622 211.058 165.869 1.00 19.93  ? 2373 MET A O     1 
ATOM   7329  C  CB    . MET A 1 2373 ? 178.029 209.950 163.189 1.00 14.73  ? 2373 MET A CB    1 
ATOM   7330  C  CG    . MET A 1 2373 ? 178.950 210.147 161.998 1.00 17.30  ? 2373 MET A CG    1 
ATOM   7331  S  SD    . MET A 1 2373 ? 178.823 208.910 160.695 1.00 21.44  ? 2373 MET A SD    1 
ATOM   7332  C  CE    . MET A 1 2373 ? 177.333 208.052 161.166 1.00 12.91  ? 2373 MET A CE    1 
ATOM   7333  N  N     . ILE A 1 2374 ? 177.983 209.349 166.406 1.00 16.17  ? 2374 ILE A N     1 
ATOM   7334  C  CA    . ILE A 1 2374 ? 177.250 209.062 167.634 1.00 11.62  ? 2374 ILE A CA    1 
ATOM   7335  C  C     . ILE A 1 2374 ? 177.431 210.198 168.633 1.00 15.58  ? 2374 ILE A C     1 
ATOM   7336  O  O     . ILE A 1 2374 ? 176.475 210.617 169.299 1.00 17.41  ? 2374 ILE A O     1 
ATOM   7337  C  CB    . ILE A 1 2374 ? 177.694 207.711 168.221 1.00 8.71   ? 2374 ILE A CB    1 
ATOM   7338  C  CG1   . ILE A 1 2374 ? 177.189 206.559 167.354 1.00 12.43  ? 2374 ILE A CG1   1 
ATOM   7339  C  CG2   . ILE A 1 2374 ? 177.163 207.549 169.631 1.00 12.15  ? 2374 ILE A CG2   1 
ATOM   7340  C  CD1   . ILE A 1 2374 ? 178.190 205.440 167.192 1.00 14.32  ? 2374 ILE A CD1   1 
ATOM   7341  N  N     . PHE A 1 2375 ? 178.656 210.716 168.751 1.00 14.31  ? 2375 PHE A N     1 
ATOM   7342  C  CA    . PHE A 1 2375 ? 178.898 211.867 169.615 1.00 12.81  ? 2375 PHE A CA    1 
ATOM   7343  C  C     . PHE A 1 2375 ? 178.111 213.082 169.144 1.00 19.54  ? 2375 PHE A C     1 
ATOM   7344  O  O     . PHE A 1 2375 ? 177.535 213.812 169.958 1.00 25.10  ? 2375 PHE A O     1 
ATOM   7345  C  CB    . PHE A 1 2375 ? 180.391 212.192 169.655 1.00 16.87  ? 2375 PHE A CB    1 
ATOM   7346  C  CG    . PHE A 1 2375 ? 181.217 211.183 170.396 1.00 20.03  ? 2375 PHE A CG    1 
ATOM   7347  C  CD1   . PHE A 1 2375 ? 180.618 210.169 171.123 1.00 17.78  ? 2375 PHE A CD1   1 
ATOM   7348  C  CD2   . PHE A 1 2375 ? 182.599 211.249 170.362 1.00 21.10  ? 2375 PHE A CD2   1 
ATOM   7349  C  CE1   . PHE A 1 2375 ? 181.382 209.246 171.803 1.00 19.92  ? 2375 PHE A CE1   1 
ATOM   7350  C  CE2   . PHE A 1 2375 ? 183.366 210.326 171.038 1.00 21.16  ? 2375 PHE A CE2   1 
ATOM   7351  C  CZ    . PHE A 1 2375 ? 182.757 209.324 171.759 1.00 19.28  ? 2375 PHE A CZ    1 
ATOM   7352  N  N     . ASN A 1 2376 ? 178.083 213.317 167.829 1.00 17.62  ? 2376 ASN A N     1 
ATOM   7353  C  CA    . ASN A 1 2376 ? 177.333 214.446 167.291 1.00 14.36  ? 2376 ASN A CA    1 
ATOM   7354  C  C     . ASN A 1 2376 ? 175.843 214.302 167.567 1.00 15.82  ? 2376 ASN A C     1 
ATOM   7355  O  O     . ASN A 1 2376 ? 175.169 215.283 167.903 1.00 20.62  ? 2376 ASN A O     1 
ATOM   7356  C  CB    . ASN A 1 2376 ? 177.590 214.577 165.790 1.00 16.43  ? 2376 ASN A CB    1 
ATOM   7357  C  CG    . ASN A 1 2376 ? 179.013 214.988 165.477 1.00 19.91  ? 2376 ASN A CG    1 
ATOM   7358  O  OD1   . ASN A 1 2376 ? 179.769 215.375 166.367 1.00 25.19  ? 2376 ASN A OD1   1 
ATOM   7359  N  ND2   . ASN A 1 2376 ? 179.387 214.903 164.206 1.00 19.85  ? 2376 ASN A ND2   1 
ATOM   7360  N  N     . ASN A 1 2377 ? 175.309 213.087 167.425 1.00 14.27  ? 2377 ASN A N     1 
ATOM   7361  C  CA    . ASN A 1 2377 ? 173.892 212.864 167.690 1.00 13.00  ? 2377 ASN A CA    1 
ATOM   7362  C  C     . ASN A 1 2377 ? 173.558 213.135 169.152 1.00 19.70  ? 2377 ASN A C     1 
ATOM   7363  O  O     . ASN A 1 2377 ? 172.528 213.743 169.464 1.00 19.85  ? 2377 ASN A O     1 
ATOM   7364  C  CB    . ASN A 1 2377 ? 173.505 211.436 167.302 1.00 11.59  ? 2377 ASN A CB    1 
ATOM   7365  C  CG    . ASN A 1 2377 ? 172.053 211.124 167.601 1.00 14.17  ? 2377 ASN A CG    1 
ATOM   7366  O  OD1   . ASN A 1 2377 ? 171.746 210.213 168.370 1.00 18.38  ? 2377 ASN A OD1   1 
ATOM   7367  N  ND2   . ASN A 1 2377 ? 171.149 211.882 166.993 1.00 15.68  ? 2377 ASN A ND2   1 
ATOM   7368  N  N     . PHE A 1 2378 ? 174.423 212.688 170.065 1.00 22.08  ? 2378 PHE A N     1 
ATOM   7369  C  CA    . PHE A 1 2378 ? 174.191 212.921 171.487 1.00 16.39  ? 2378 PHE A CA    1 
ATOM   7370  C  C     . PHE A 1 2378 ? 174.233 214.409 171.814 1.00 19.67  ? 2378 PHE A C     1 
ATOM   7371  O  O     . PHE A 1 2378 ? 173.403 214.914 172.579 1.00 22.02  ? 2378 PHE A O     1 
ATOM   7372  C  CB    . PHE A 1 2378 ? 175.226 212.158 172.316 1.00 16.04  ? 2378 PHE A CB    1 
ATOM   7373  C  CG    . PHE A 1 2378 ? 175.332 212.630 173.738 1.00 20.33  ? 2378 PHE A CG    1 
ATOM   7374  C  CD1   . PHE A 1 2378 ? 174.244 212.554 174.592 1.00 17.76  ? 2378 PHE A CD1   1 
ATOM   7375  C  CD2   . PHE A 1 2378 ? 176.518 213.158 174.218 1.00 19.79  ? 2378 PHE A CD2   1 
ATOM   7376  C  CE1   . PHE A 1 2378 ? 174.340 212.991 175.898 1.00 17.32  ? 2378 PHE A CE1   1 
ATOM   7377  C  CE2   . PHE A 1 2378 ? 176.618 213.598 175.522 1.00 20.26  ? 2378 PHE A CE2   1 
ATOM   7378  C  CZ    . PHE A 1 2378 ? 175.528 213.514 176.363 1.00 18.08  ? 2378 PHE A CZ    1 
ATOM   7379  N  N     . LEU A 1 2379 ? 175.201 215.129 171.243 1.00 18.87  ? 2379 LEU A N     1 
ATOM   7380  C  CA    . LEU A 1 2379 ? 175.335 216.552 171.538 1.00 18.32  ? 2379 LEU A CA    1 
ATOM   7381  C  C     . LEU A 1 2379 ? 174.212 217.362 170.902 1.00 21.83  ? 2379 LEU A C     1 
ATOM   7382  O  O     . LEU A 1 2379 ? 173.715 218.320 171.505 1.00 27.82  ? 2379 LEU A O     1 
ATOM   7383  C  CB    . LEU A 1 2379 ? 176.699 217.056 171.070 1.00 19.44  ? 2379 LEU A CB    1 
ATOM   7384  C  CG    . LEU A 1 2379 ? 177.892 216.578 171.899 1.00 19.75  ? 2379 LEU A CG    1 
ATOM   7385  C  CD1   . LEU A 1 2379 ? 179.194 217.092 171.316 1.00 23.99  ? 2379 LEU A CD1   1 
ATOM   7386  C  CD2   . LEU A 1 2379 ? 177.745 217.013 173.345 1.00 22.23  ? 2379 LEU A CD2   1 
ATOM   7387  N  N     . ALA A 1 2380 ? 173.806 217.001 169.681 1.00 19.17  ? 2380 ALA A N     1 
ATOM   7388  C  CA    . ALA A 1 2380 ? 172.715 217.716 169.025 1.00 19.63  ? 2380 ALA A CA    1 
ATOM   7389  C  C     . ALA A 1 2380 ? 171.405 217.544 169.783 1.00 23.82  ? 2380 ALA A C     1 
ATOM   7390  O  O     . ALA A 1 2380 ? 170.639 218.501 169.939 1.00 25.00  ? 2380 ALA A O     1 
ATOM   7391  C  CB    . ALA A 1 2380 ? 172.568 217.240 167.580 1.00 15.84  ? 2380 ALA A CB    1 
ATOM   7392  N  N     . ARG A 1 2381 ? 171.128 216.326 170.256 1.00 24.09  ? 2381 ARG A N     1 
ATOM   7393  C  CA    . ARG A 1 2381 ? 169.938 216.099 171.070 1.00 20.13  ? 2381 ARG A CA    1 
ATOM   7394  C  C     . ARG A 1 2381 ? 170.013 216.868 172.382 1.00 25.93  ? 2381 ARG A C     1 
ATOM   7395  O  O     . ARG A 1 2381 ? 169.006 217.410 172.853 1.00 32.84  ? 2381 ARG A O     1 
ATOM   7396  C  CB    . ARG A 1 2381 ? 169.762 214.604 171.337 1.00 16.77  ? 2381 ARG A CB    1 
ATOM   7397  C  CG    . ARG A 1 2381 ? 169.413 213.785 170.107 1.00 18.12  ? 2381 ARG A CG    1 
ATOM   7398  C  CD    . ARG A 1 2381 ? 169.283 212.311 170.452 1.00 15.89  ? 2381 ARG A CD    1 
ATOM   7399  N  NE    . ARG A 1 2381 ? 168.267 212.070 171.470 1.00 15.10  ? 2381 ARG A NE    1 
ATOM   7400  C  CZ    . ARG A 1 2381 ? 166.967 211.981 171.224 1.00 19.31  ? 2381 ARG A CZ    1 
ATOM   7401  N  NH1   . ARG A 1 2381 ? 166.486 212.104 169.998 1.00 25.74  ? 2381 ARG A NH1   1 
ATOM   7402  N  NH2   . ARG A 1 2381 ? 166.130 211.765 172.234 1.00 21.26  ? 2381 ARG A NH2   1 
ATOM   7403  N  N     . LEU A 1 2382 ? 171.201 216.922 172.990 1.00 19.90  ? 2382 LEU A N     1 
ATOM   7404  C  CA    . LEU A 1 2382 ? 171.355 217.626 174.258 1.00 22.00  ? 2382 LEU A CA    1 
ATOM   7405  C  C     . LEU A 1 2382 ? 171.097 219.119 174.098 1.00 27.37  ? 2382 LEU A C     1 
ATOM   7406  O  O     . LEU A 1 2382 ? 170.491 219.749 174.971 1.00 30.63  ? 2382 LEU A O     1 
ATOM   7407  C  CB    . LEU A 1 2382 ? 172.753 217.377 174.825 1.00 24.51  ? 2382 LEU A CB    1 
ATOM   7408  C  CG    . LEU A 1 2382 ? 172.993 217.782 176.279 1.00 21.85  ? 2382 LEU A CG    1 
ATOM   7409  C  CD1   . LEU A 1 2382 ? 172.082 216.996 177.204 1.00 23.64  ? 2382 LEU A CD1   1 
ATOM   7410  C  CD2   . LEU A 1 2382 ? 174.448 217.573 176.656 1.00 25.62  ? 2382 LEU A CD2   1 
ATOM   7411  N  N     . ARG A 1 2383 ? 171.547 219.703 172.985 1.00 27.96  ? 2383 ARG A N     1 
ATOM   7412  C  CA    . ARG A 1 2383 ? 171.364 221.132 172.768 1.00 24.01  ? 2383 ARG A CA    1 
ATOM   7413  C  C     . ARG A 1 2383 ? 169.958 221.478 172.294 1.00 27.08  ? 2383 ARG A C     1 
ATOM   7414  O  O     . ARG A 1 2383 ? 169.599 222.660 172.275 1.00 33.22  ? 2383 ARG A O     1 
ATOM   7415  C  CB    . ARG A 1 2383 ? 172.387 221.642 171.754 1.00 21.13  ? 2383 ARG A CB    1 
ATOM   7416  C  CG    . ARG A 1 2383 ? 173.808 221.717 172.284 1.00 26.75  ? 2383 ARG A CG    1 
ATOM   7417  C  CD    . ARG A 1 2383 ? 174.786 222.065 171.176 1.00 29.52  ? 2383 ARG A CD    1 
ATOM   7418  N  NE    . ARG A 1 2383 ? 176.100 222.421 171.696 1.00 32.57  ? 2383 ARG A NE    1 
ATOM   7419  C  CZ    . ARG A 1 2383 ? 177.225 221.797 171.375 1.00 33.39  ? 2383 ARG A CZ    1 
ATOM   7420  N  NH1   . ARG A 1 2383 ? 177.233 220.772 170.538 1.00 28.62  ? 2383 ARG A NH1   1 
ATOM   7421  N  NH2   . ARG A 1 2383 ? 178.372 222.210 171.908 1.00 36.45  ? 2383 ARG A NH2   1 
ATOM   7422  N  N     . SER A 1 2384 ? 169.158 220.484 171.913 1.00 25.92  ? 2384 SER A N     1 
ATOM   7423  C  CA    . SER A 1 2384 ? 167.839 220.725 171.340 1.00 27.14  ? 2384 SER A CA    1 
ATOM   7424  C  C     . SER A 1 2384 ? 166.701 220.256 172.239 1.00 35.02  ? 2384 SER A C     1 
ATOM   7425  O  O     . SER A 1 2384 ? 165.783 221.028 172.528 1.00 39.21  ? 2384 SER A O     1 
ATOM   7426  C  CB    . SER A 1 2384 ? 167.732 220.042 169.971 1.00 29.30  ? 2384 SER A CB    1 
ATOM   7427  O  OG    . SER A 1 2384 ? 168.704 220.544 169.072 1.00 38.29  ? 2384 SER A OG    1 
ATOM   7428  N  N     . ILE A 1 2385 ? 166.740 219.005 172.686 1.00 31.53  ? 2385 ILE A N     1 
ATOM   7429  C  CA    . ILE A 1 2385 ? 165.631 218.396 173.413 1.00 33.39  ? 2385 ILE A CA    1 
ATOM   7430  C  C     . ILE A 1 2385 ? 165.820 218.681 174.900 1.00 36.32  ? 2385 ILE A C     1 
ATOM   7431  O  O     . ILE A 1 2385 ? 166.824 218.236 175.479 1.00 35.74  ? 2385 ILE A O     1 
ATOM   7432  C  CB    . ILE A 1 2385 ? 165.555 216.887 173.153 1.00 29.90  ? 2385 ILE A CB    1 
ATOM   7433  C  CG1   . ILE A 1 2385 ? 165.495 216.611 171.650 1.00 29.25  ? 2385 ILE A CG1   1 
ATOM   7434  C  CG2   . ILE A 1 2385 ? 164.349 216.284 173.857 1.00 30.00  ? 2385 ILE A CG2   1 
ATOM   7435  C  CD1   . ILE A 1 2385 ? 165.501 215.143 171.298 1.00 24.81  ? 2385 ILE A CD1   1 
ATOM   7436  N  N     . PRO A 1 2386 ? 164.906 219.404 175.544 1.00 38.13  ? 2386 PRO A N     1 
ATOM   7437  C  CA    . PRO A 1 2386 ? 164.998 219.583 176.996 1.00 41.71  ? 2386 PRO A CA    1 
ATOM   7438  C  C     . PRO A 1 2386 ? 164.775 218.268 177.726 1.00 43.08  ? 2386 PRO A C     1 
ATOM   7439  O  O     . PRO A 1 2386 ? 164.042 217.390 177.267 1.00 49.88  ? 2386 PRO A O     1 
ATOM   7440  C  CB    . PRO A 1 2386 ? 163.882 220.590 177.308 1.00 39.12  ? 2386 PRO A CB    1 
ATOM   7441  C  CG    . PRO A 1 2386 ? 163.467 221.160 175.977 1.00 37.15  ? 2386 PRO A CG    1 
ATOM   7442  C  CD    . PRO A 1 2386 ? 163.737 220.091 174.974 1.00 37.38  ? 2386 PRO A CD    1 
ATOM   7443  N  N     . LEU A 1 2387 ? 165.426 218.139 178.884 1.00 34.99  ? 2387 LEU A N     1 
ATOM   7444  C  CA    . LEU A 1 2387 ? 165.334 216.896 179.641 1.00 40.12  ? 2387 LEU A CA    1 
ATOM   7445  C  C     . LEU A 1 2387 ? 164.053 216.807 180.462 1.00 49.31  ? 2387 LEU A C     1 
ATOM   7446  O  O     . LEU A 1 2387 ? 163.605 215.698 180.777 1.00 48.54  ? 2387 LEU A O     1 
ATOM   7447  C  CB    . LEU A 1 2387 ? 166.558 216.739 180.545 1.00 37.69  ? 2387 LEU A CB    1 
ATOM   7448  C  CG    . LEU A 1 2387 ? 167.823 216.243 179.840 1.00 31.69  ? 2387 LEU A CG    1 
ATOM   7449  C  CD1   . LEU A 1 2387 ? 168.972 216.091 180.822 1.00 33.48  ? 2387 LEU A CD1   1 
ATOM   7450  C  CD2   . LEU A 1 2387 ? 167.552 214.930 179.123 1.00 28.71  ? 2387 LEU A CD2   1 
ATOM   7451  N  N     . ASP A 1 2388 ? 163.454 217.945 180.824 1.00 54.88  ? 2388 ASP A N     1 
ATOM   7452  C  CA    . ASP A 1 2388 ? 162.172 217.910 181.524 1.00 51.68  ? 2388 ASP A CA    1 
ATOM   7453  C  C     . ASP A 1 2388 ? 161.068 217.359 180.631 1.00 55.10  ? 2388 ASP A C     1 
ATOM   7454  O  O     . ASP A 1 2388 ? 160.260 216.532 181.070 1.00 60.69  ? 2388 ASP A O     1 
ATOM   7455  C  CB    . ASP A 1 2388 ? 161.801 219.306 182.022 1.00 57.46  ? 2388 ASP A CB    1 
ATOM   7456  C  CG    . ASP A 1 2388 ? 162.998 220.083 182.526 1.00 62.30  ? 2388 ASP A CG    1 
ATOM   7457  O  OD1   . ASP A 1 2388 ? 163.591 219.665 183.541 1.00 64.25  ? 2388 ASP A OD1   1 
ATOM   7458  O  OD2   . ASP A 1 2388 ? 163.350 221.107 181.905 1.00 58.34  ? 2388 ASP A OD2   1 
ATOM   7459  N  N     . GLU A 1 2389 ? 161.017 217.804 179.380 1.00 51.78  ? 2389 GLU A N     1 
ATOM   7460  C  CA    . GLU A 1 2389 ? 159.977 217.377 178.456 1.00 57.07  ? 2389 GLU A CA    1 
ATOM   7461  C  C     . GLU A 1 2389 ? 160.437 217.549 177.013 1.00 51.18  ? 2389 GLU A C     1 
ATOM   7462  O  O     . GLU A 1 2389 ? 161.180 218.477 176.696 0.00 49.66  ? 2389 GLU A O     1 
ATOM   7463  C  CB    . GLU A 1 2389 ? 158.688 218.166 178.699 1.00 65.48  ? 2389 GLU A CB    1 
ATOM   7464  C  CG    . GLU A 1 2389 ? 157.501 217.698 177.874 1.00 70.43  ? 2389 GLU A CG    1 
ATOM   7465  C  CD    . GLU A 1 2389 ? 156.924 216.388 178.373 1.00 75.21  ? 2389 GLU A CD    1 
ATOM   7466  O  OE1   . GLU A 1 2389 ? 157.500 215.324 178.060 1.00 79.73  ? 2389 GLU A OE1   1 
ATOM   7467  O  OE2   . GLU A 1 2389 ? 155.893 216.423 179.076 1.00 75.05  ? 2389 GLU A OE2   1 
ATOM   7468  N  N     . SER A 1 2410 ? 164.328 226.449 177.525 1.00 49.00  ? 2410 SER A N     1 
ATOM   7469  C  CA    . SER A 1 2410 ? 164.161 225.779 178.841 1.00 51.87  ? 2410 SER A CA    1 
ATOM   7470  C  C     . SER A 1 2410 ? 165.389 226.047 179.722 1.00 49.76  ? 2410 SER A C     1 
ATOM   7471  O  O     . SER A 1 2410 ? 166.519 226.019 179.188 1.00 43.67  ? 2410 SER A O     1 
ATOM   7472  C  CB    . SER A 1 2410 ? 163.928 224.301 178.675 1.00 42.97  ? 2410 SER A CB    1 
ATOM   7473  O  OG    . SER A 1 2410 ? 163.944 223.640 179.933 1.00 37.94  ? 2410 SER A OG    1 
ATOM   7474  N  N     . PRO A 1 2411 ? 165.222 226.298 181.039 1.00 50.55  ? 2411 PRO A N     1 
ATOM   7475  C  CA    . PRO A 1 2411 ? 166.365 226.485 181.921 1.00 48.66  ? 2411 PRO A CA    1 
ATOM   7476  C  C     . PRO A 1 2411 ? 167.201 225.218 181.905 1.00 46.57  ? 2411 PRO A C     1 
ATOM   7477  O  O     . PRO A 1 2411 ? 168.444 225.309 181.867 1.00 46.58  ? 2411 PRO A O     1 
ATOM   7478  C  CB    . PRO A 1 2411 ? 165.721 226.754 183.287 1.00 41.50  ? 2411 PRO A CB    1 
ATOM   7479  C  CG    . PRO A 1 2411 ? 164.333 226.165 183.165 1.00 40.14  ? 2411 PRO A CG    1 
ATOM   7480  C  CD    . PRO A 1 2411 ? 163.942 226.397 181.717 1.00 43.94  ? 2411 PRO A CD    1 
ATOM   7481  N  N     . MET A 1 2412 ? 166.538 224.058 181.925 1.00 43.12  ? 2412 MET A N     1 
ATOM   7482  C  CA    . MET A 1 2412 ? 167.261 222.763 181.856 1.00 44.31  ? 2412 MET A CA    1 
ATOM   7483  C  C     . MET A 1 2412 ? 168.004 222.683 180.515 1.00 44.70  ? 2412 MET A C     1 
ATOM   7484  O  O     . MET A 1 2412 ? 169.181 222.262 180.511 1.00 44.55  ? 2412 MET A O     1 
ATOM   7485  C  CB    . MET A 1 2412 ? 166.285 221.587 181.969 1.00 47.04  ? 2412 MET A CB    1 
ATOM   7486  C  CG    . MET A 1 2412 ? 166.898 220.240 181.638 1.00 51.25  ? 2412 MET A CG    1 
ATOM   7487  S  SD    . MET A 1 2412 ? 168.039 219.633 182.897 1.00 50.62  ? 2412 MET A SD    1 
ATOM   7488  C  CE    . MET A 1 2412 ? 166.865 218.994 184.099 1.00 43.02  ? 2412 MET A CE    1 
ATOM   7489  N  N     . LEU A 1 2413 ? 167.339 223.081 179.426 1.00 46.94  ? 2413 LEU A N     1 
ATOM   7490  C  CA    . LEU A 1 2413 ? 167.977 223.051 178.084 1.00 42.97  ? 2413 LEU A CA    1 
ATOM   7491  C  C     . LEU A 1 2413 ? 169.186 223.999 178.095 1.00 41.68  ? 2413 LEU A C     1 
ATOM   7492  O  O     . LEU A 1 2413 ? 170.227 223.638 177.506 1.00 44.83  ? 2413 LEU A O     1 
ATOM   7493  C  CB    . LEU A 1 2413 ? 166.974 223.431 176.997 1.00 44.01  ? 2413 LEU A CB    1 
ATOM   7494  C  CG    . LEU A 1 2413 ? 167.445 223.217 175.555 1.00 39.76  ? 2413 LEU A CG    1 
ATOM   7495  C  CD1   . LEU A 1 2413 ? 167.834 221.766 175.332 1.00 37.25  ? 2413 LEU A CD1   1 
ATOM   7496  C  CD2   . LEU A 1 2413 ? 166.371 223.638 174.569 1.00 39.64  ? 2413 LEU A CD2   1 
ATOM   7497  N  N     . GLN A 1 2414 ? 169.050 225.157 178.746 1.00 43.58  ? 2414 GLN A N     1 
ATOM   7498  C  CA    . GLN A 1 2414 ? 170.188 226.107 178.851 1.00 42.63  ? 2414 GLN A CA    1 
ATOM   7499  C  C     . GLN A 1 2414 ? 171.346 225.398 179.567 1.00 43.40  ? 2414 GLN A C     1 
ATOM   7500  O  O     . GLN A 1 2414 ? 172.486 225.464 179.059 1.00 43.76  ? 2414 GLN A O     1 
ATOM   7501  C  CB    . GLN A 1 2414 ? 169.771 227.368 179.607 1.00 39.37  ? 2414 GLN A CB    1 
ATOM   7502  C  CG    . GLN A 1 2414 ? 170.865 228.426 179.685 1.00 45.21  ? 2414 GLN A CG    1 
ATOM   7503  C  CD    . GLN A 1 2414 ? 171.397 228.826 178.326 1.00 53.80  ? 2414 GLN A CD    1 
ATOM   7504  O  OE1   . GLN A 1 2414 ? 170.658 229.312 177.462 1.00 60.63  ? 2414 GLN A OE1   1 
ATOM   7505  N  NE2   . GLN A 1 2414 ? 172.689 228.622 178.123 1.00 50.39  ? 2414 GLN A NE2   1 
ATOM   7506  N  N     . ILE A 1 2415 ? 171.056 224.738 180.692 1.00 41.01  ? 2415 ILE A N     1 
ATOM   7507  C  CA    . ILE A 1 2415 ? 172.108 223.958 181.409 1.00 41.80  ? 2415 ILE A CA    1 
ATOM   7508  C  C     . ILE A 1 2415 ? 172.684 222.935 180.422 1.00 40.74  ? 2415 ILE A C     1 
ATOM   7509  O  O     . ILE A 1 2415 ? 173.924 222.794 180.369 1.00 39.71  ? 2415 ILE A O     1 
ATOM   7510  C  CB    . ILE A 1 2415 ? 171.525 223.271 182.657 1.00 37.93  ? 2415 ILE A CB    1 
ATOM   7511  C  CG1   . ILE A 1 2415 ? 170.886 224.280 183.611 1.00 40.98  ? 2415 ILE A CG1   1 
ATOM   7512  C  CG2   . ILE A 1 2415 ? 172.584 222.421 183.359 1.00 37.00  ? 2415 ILE A CG2   1 
ATOM   7513  C  CD1   . ILE A 1 2415 ? 170.260 223.654 184.843 1.00 42.32  ? 2415 ILE A CD1   1 
ATOM   7514  N  N     . GLN A 1 2416 ? 171.811 222.263 179.665 1.00 37.77  ? 2416 GLN A N     1 
ATOM   7515  C  CA    . GLN A 1 2416 ? 172.265 221.260 178.709 1.00 30.46  ? 2416 GLN A CA    1 
ATOM   7516  C  C     . GLN A 1 2416 ? 173.212 221.865 177.680 1.00 36.27  ? 2416 GLN A C     1 
ATOM   7517  O  O     . GLN A 1 2416 ? 174.216 221.246 177.309 1.00 37.25  ? 2416 GLN A O     1 
ATOM   7518  C  CB    . GLN A 1 2416 ? 171.064 220.617 178.017 1.00 31.95  ? 2416 GLN A CB    1 
ATOM   7519  C  CG    . GLN A 1 2416 ? 170.263 219.679 178.902 1.00 30.67  ? 2416 GLN A CG    1 
ATOM   7520  C  CD    . GLN A 1 2416 ? 168.919 219.323 178.299 1.00 34.39  ? 2416 GLN A CD    1 
ATOM   7521  O  OE1   . GLN A 1 2416 ? 167.885 219.423 178.958 1.00 40.66  ? 2416 GLN A OE1   1 
ATOM   7522  N  NE2   . GLN A 1 2416 ? 168.929 218.904 177.040 1.00 32.18  ? 2416 GLN A NE2   1 
ATOM   7523  N  N     . ARG A 1 2417 ? 172.905 223.075 177.204 1.00 39.73  ? 2417 ARG A N     1 
ATOM   7524  C  CA    . ARG A 1 2417 ? 173.748 223.713 176.197 1.00 35.98  ? 2417 ARG A CA    1 
ATOM   7525  C  C     . ARG A 1 2417 ? 175.120 224.065 176.760 1.00 36.53  ? 2417 ARG A C     1 
ATOM   7526  O  O     . ARG A 1 2417 ? 176.144 223.828 176.109 1.00 39.30  ? 2417 ARG A O     1 
ATOM   7527  C  CB    . ARG A 1 2417 ? 173.053 224.958 175.649 1.00 36.05  ? 2417 ARG A CB    1 
ATOM   7528  C  CG    . ARG A 1 2417 ? 171.781 224.654 174.878 1.00 34.77  ? 2417 ARG A CG    1 
ATOM   7529  C  CD    . ARG A 1 2417 ? 171.441 225.754 173.892 1.00 37.15  ? 2417 ARG A CD    1 
ATOM   7530  N  NE    . ARG A 1 2417 ? 170.324 225.376 173.034 1.00 46.02  ? 2417 ARG A NE    1 
ATOM   7531  C  CZ    . ARG A 1 2417 ? 169.143 225.978 173.032 1.00 40.96  ? 2417 ARG A CZ    1 
ATOM   7532  N  NH1   . ARG A 1 2417 ? 168.888 227.002 173.830 1.00 39.68  ? 2417 ARG A NH1   1 
ATOM   7533  N  NH2   . ARG A 1 2417 ? 168.194 225.540 172.209 1.00 37.27  ? 2417 ARG A NH2   1 
ATOM   7534  N  N     . ASP A 1 2418 ? 175.163 224.637 177.966 1.00 37.09  ? 2418 ASP A N     1 
ATOM   7535  C  CA    . ASP A 1 2418 ? 176.447 224.914 178.602 1.00 37.52  ? 2418 ASP A CA    1 
ATOM   7536  C  C     . ASP A 1 2418 ? 177.199 223.626 178.909 1.00 36.07  ? 2418 ASP A C     1 
ATOM   7537  O  O     . ASP A 1 2418 ? 178.426 223.567 178.768 1.00 33.01  ? 2418 ASP A O     1 
ATOM   7538  C  CB    . ASP A 1 2418 ? 176.243 225.738 179.873 1.00 39.14  ? 2418 ASP A CB    1 
ATOM   7539  C  CG    . ASP A 1 2418 ? 175.535 227.053 179.609 1.00 53.38  ? 2418 ASP A CG    1 
ATOM   7540  O  OD1   . ASP A 1 2418 ? 174.743 227.123 178.648 1.00 52.90  ? 2418 ASP A OD1   1 
ATOM   7541  O  OD2   . ASP A 1 2418 ? 175.770 228.016 180.368 1.00 55.74  ? 2418 ASP A OD2   1 
ATOM   7542  N  N     . ALA A 1 2419 ? 176.482 222.584 179.336 1.00 37.66  ? 2419 ALA A N     1 
ATOM   7543  C  CA    . ALA A 1 2419 ? 177.124 221.297 179.575 1.00 32.97  ? 2419 ALA A CA    1 
ATOM   7544  C  C     . ALA A 1 2419 ? 177.678 220.707 178.283 1.00 34.41  ? 2419 ALA A C     1 
ATOM   7545  O  O     . ALA A 1 2419 ? 178.795 220.180 178.264 1.00 33.65  ? 2419 ALA A O     1 
ATOM   7546  C  CB    . ALA A 1 2419 ? 176.138 220.329 180.229 1.00 29.28  ? 2419 ALA A CB    1 
ATOM   7547  N  N     . ALA A 1 2420 ? 176.914 220.798 177.190 1.00 37.07  ? 2420 ALA A N     1 
ATOM   7548  C  CA    . ALA A 1 2420 ? 177.363 220.237 175.919 1.00 33.90  ? 2420 ALA A CA    1 
ATOM   7549  C  C     . ALA A 1 2420 ? 178.632 220.922 175.426 1.00 34.31  ? 2420 ALA A C     1 
ATOM   7550  O  O     . ALA A 1 2420 ? 179.480 220.286 174.790 1.00 37.58  ? 2420 ALA A O     1 
ATOM   7551  C  CB    . ALA A 1 2420 ? 176.254 220.348 174.873 1.00 32.18  ? 2420 ALA A CB    1 
ATOM   7552  N  N     . THR A 1 2421 ? 178.774 222.219 175.702 1.00 34.69  ? 2421 THR A N     1 
ATOM   7553  C  CA    . THR A 1 2421 ? 180.000 222.924 175.340 1.00 34.86  ? 2421 THR A CA    1 
ATOM   7554  C  C     . THR A 1 2421 ? 181.195 222.374 176.112 1.00 34.55  ? 2421 THR A C     1 
ATOM   7555  O  O     . THR A 1 2421 ? 182.295 222.242 175.561 1.00 33.01  ? 2421 THR A O     1 
ATOM   7556  C  CB    . THR A 1 2421 ? 179.829 224.424 175.593 1.00 34.78  ? 2421 THR A CB    1 
ATOM   7557  O  OG1   . THR A 1 2421 ? 178.967 224.983 174.596 1.00 40.52  ? 2421 THR A OG1   1 
ATOM   7558  C  CG2   . THR A 1 2421 ? 181.170 225.142 175.547 1.00 35.02  ? 2421 THR A CG2   1 
ATOM   7559  N  N     . ILE A 1 2422 ? 180.992 222.033 177.385 1.00 30.67  ? 2422 ILE A N     1 
ATOM   7560  C  CA    . ILE A 1 2422 ? 182.100 221.595 178.229 1.00 31.44  ? 2422 ILE A CA    1 
ATOM   7561  C  C     . ILE A 1 2422 ? 182.612 220.227 177.790 1.00 34.17  ? 2422 ILE A C     1 
ATOM   7562  O  O     . ILE A 1 2422 ? 183.825 219.986 177.760 1.00 34.13  ? 2422 ILE A O     1 
ATOM   7563  C  CB    . ILE A 1 2422 ? 181.668 221.598 179.706 1.00 32.00  ? 2422 ILE A CB    1 
ATOM   7564  C  CG1   . ILE A 1 2422 ? 181.327 223.020 180.150 1.00 32.92  ? 2422 ILE A CG1   1 
ATOM   7565  C  CG2   . ILE A 1 2422 ? 182.769 221.030 180.586 1.00 33.15  ? 2422 ILE A CG2   1 
ATOM   7566  C  CD1   . ILE A 1 2422 ? 180.451 223.081 181.378 1.00 35.64  ? 2422 ILE A CD1   1 
ATOM   7567  N  N     . MET A 1 2423 ? 181.706 219.311 177.442 1.00 32.18  ? 2423 MET A N     1 
ATOM   7568  C  CA    . MET A 1 2423 ? 182.124 217.991 176.984 1.00 32.72  ? 2423 MET A CA    1 
ATOM   7569  C  C     . MET A 1 2423 ? 182.546 217.972 175.521 1.00 36.10  ? 2423 MET A C     1 
ATOM   7570  O  O     . MET A 1 2423 ? 183.000 216.927 175.043 1.00 37.95  ? 2423 MET A O     1 
ATOM   7571  C  CB    . MET A 1 2423 ? 181.011 216.959 177.191 1.00 38.63  ? 2423 MET A CB    1 
ATOM   7572  C  CG    . MET A 1 2423 ? 179.974 217.314 178.234 1.00 36.12  ? 2423 MET A CG    1 
ATOM   7573  S  SD    . MET A 1 2423 ? 178.594 216.154 178.209 1.00 41.13  ? 2423 MET A SD    1 
ATOM   7574  C  CE    . MET A 1 2423 ? 177.348 217.082 179.095 1.00 32.83  ? 2423 MET A CE    1 
ATOM   7575  N  N     . GLN A 1 2424 ? 182.395 219.085 174.803 1.00 34.65  ? 2424 GLN A N     1 
ATOM   7576  C  CA    . GLN A 1 2424 ? 182.776 219.119 173.392 1.00 32.28  ? 2424 GLN A CA    1 
ATOM   7577  C  C     . GLN A 1 2424 ? 184.236 218.752 173.153 1.00 33.50  ? 2424 GLN A C     1 
ATOM   7578  O  O     . GLN A 1 2424 ? 184.500 217.951 172.240 1.00 39.85  ? 2424 GLN A O     1 
ATOM   7579  C  CB    . GLN A 1 2424 ? 182.443 220.494 172.802 1.00 33.53  ? 2424 GLN A CB    1 
ATOM   7580  C  CG    . GLN A 1 2424 ? 182.551 220.560 171.287 1.00 31.79  ? 2424 GLN A CG    1 
ATOM   7581  C  CD    . GLN A 1 2424 ? 181.460 219.777 170.587 1.00 29.73  ? 2424 GLN A CD    1 
ATOM   7582  O  OE1   . GLN A 1 2424 ? 180.276 220.083 170.721 1.00 31.46  ? 2424 GLN A OE1   1 
ATOM   7583  N  NE2   . GLN A 1 2424 ? 181.855 218.758 169.833 1.00 33.41  ? 2424 GLN A NE2   1 
ATOM   7584  N  N     . PRO A 1 2425 ? 185.220 219.280 173.896 1.00 27.56  ? 2425 PRO A N     1 
ATOM   7585  C  CA    . PRO A 1 2425 ? 186.614 218.880 173.625 1.00 28.26  ? 2425 PRO A CA    1 
ATOM   7586  C  C     . PRO A 1 2425 ? 186.873 217.392 173.793 1.00 30.82  ? 2425 PRO A C     1 
ATOM   7587  O  O     . PRO A 1 2425 ? 187.802 216.859 173.173 1.00 37.10  ? 2425 PRO A O     1 
ATOM   7588  C  CB    . PRO A 1 2425 ? 187.416 219.711 174.637 1.00 29.17  ? 2425 PRO A CB    1 
ATOM   7589  C  CG    . PRO A 1 2425 ? 186.567 220.884 174.912 1.00 29.28  ? 2425 PRO A CG    1 
ATOM   7590  C  CD    . PRO A 1 2425 ? 185.162 220.375 174.883 1.00 31.52  ? 2425 PRO A CD    1 
ATOM   7591  N  N     . TYR A 1 2426 ? 186.088 216.704 174.622 1.00 32.25  ? 2426 TYR A N     1 
ATOM   7592  C  CA    . TYR A 1 2426 ? 186.311 215.283 174.858 1.00 31.99  ? 2426 TYR A CA    1 
ATOM   7593  C  C     . TYR A 1 2426 ? 185.548 214.389 173.888 1.00 32.84  ? 2426 TYR A C     1 
ATOM   7594  O  O     . TYR A 1 2426 ? 185.949 213.238 173.686 1.00 34.90  ? 2426 TYR A O     1 
ATOM   7595  C  CB    . TYR A 1 2426 ? 185.940 214.932 176.300 1.00 31.25  ? 2426 TYR A CB    1 
ATOM   7596  C  CG    . TYR A 1 2426 ? 186.498 215.907 177.312 1.00 26.44  ? 2426 TYR A CG    1 
ATOM   7597  C  CD1   . TYR A 1 2426 ? 187.831 215.849 177.692 1.00 24.48  ? 2426 TYR A CD1   1 
ATOM   7598  C  CD2   . TYR A 1 2426 ? 185.699 216.893 177.875 1.00 26.40  ? 2426 TYR A CD2   1 
ATOM   7599  C  CE1   . TYR A 1 2426 ? 188.351 216.737 178.610 1.00 26.51  ? 2426 TYR A CE1   1 
ATOM   7600  C  CE2   . TYR A 1 2426 ? 186.212 217.788 178.794 1.00 28.39  ? 2426 TYR A CE2   1 
ATOM   7601  C  CZ    . TYR A 1 2426 ? 187.539 217.704 179.157 1.00 31.45  ? 2426 TYR A CZ    1 
ATOM   7602  O  OH    . TYR A 1 2426 ? 188.061 218.587 180.071 1.00 35.32  ? 2426 TYR A OH    1 
ATOM   7603  N  N     . PHE A 1 2427 ? 184.442 214.892 173.335 1.00 31.47  ? 2427 PHE A N     1 
ATOM   7604  C  CA    . PHE A 1 2427 ? 183.677 214.108 172.326 1.00 29.88  ? 2427 PHE A CA    1 
ATOM   7605  C  C     . PHE A 1 2427 ? 184.221 214.462 170.946 1.00 36.17  ? 2427 PHE A C     1 
ATOM   7606  O  O     . PHE A 1 2427 ? 183.488 215.073 170.138 1.00 40.87  ? 2427 PHE A O     1 
ATOM   7607  C  CB    . PHE A 1 2427 ? 182.174 214.364 172.469 1.00 30.91  ? 2427 PHE A CB    1 
ATOM   7608  C  CG    . PHE A 1 2427 ? 181.537 213.661 173.660 1.00 24.11  ? 2427 PHE A CG    1 
ATOM   7609  C  CD1   . PHE A 1 2427 ? 181.035 212.371 173.540 1.00 22.88  ? 2427 PHE A CD1   1 
ATOM   7610  C  CD2   . PHE A 1 2427 ? 181.447 214.288 174.897 1.00 25.23  ? 2427 PHE A CD2   1 
ATOM   7611  C  CE1   . PHE A 1 2427 ? 180.458 211.730 174.624 1.00 24.17  ? 2427 PHE A CE1   1 
ATOM   7612  C  CE2   . PHE A 1 2427 ? 180.869 213.643 175.978 1.00 28.86  ? 2427 PHE A CE2   1 
ATOM   7613  C  CZ    . PHE A 1 2427 ? 180.376 212.367 175.840 1.00 29.32  ? 2427 PHE A CZ    1 
ATOM   7614  N  N     . THR A 1 2428 ? 185.478 214.096 170.685 1.00 36.09  ? 2428 THR A N     1 
ATOM   7615  C  CA    . THR A 1 2428 ? 186.120 214.431 169.396 1.00 35.01  ? 2428 THR A CA    1 
ATOM   7616  C  C     . THR A 1 2428 ? 186.813 213.202 168.855 1.00 40.31  ? 2428 THR A C     1 
ATOM   7617  O  O     . THR A 1 2428 ? 186.934 212.211 169.609 1.00 45.21  ? 2428 THR A O     1 
ATOM   7618  C  CB    . THR A 1 2428 ? 187.109 215.575 169.609 1.00 37.29  ? 2428 THR A CB    1 
ATOM   7619  O  OG1   . THR A 1 2428 ? 188.040 215.084 170.568 1.00 36.00  ? 2428 THR A OG1   1 
ATOM   7620  C  CG2   . THR A 1 2428 ? 186.442 216.834 170.132 1.00 36.35  ? 2428 THR A CG2   1 
ATOM   7621  N  N     . SER A 1 2429 ? 187.261 213.254 167.597 1.00 45.04  ? 2429 SER A N     1 
ATOM   7622  C  CA    . SER A 1 2429 ? 188.016 212.118 167.010 1.00 44.29  ? 2429 SER A CA    1 
ATOM   7623  C  C     . SER A 1 2429 ? 189.209 211.793 167.918 1.00 46.74  ? 2429 SER A C     1 
ATOM   7624  O  O     . SER A 1 2429 ? 189.865 212.748 168.388 1.00 48.35  ? 2429 SER A O     1 
ATOM   7625  C  CB    . SER A 1 2429 ? 188.471 212.435 165.611 1.00 42.60  ? 2429 SER A CB    1 
ATOM   7626  O  OG    . SER A 1 2429 ? 187.396 212.928 164.824 1.00 47.65  ? 2429 SER A OG    1 
ATOM   7627  N  N     . ASN A 1 2430 ? 189.454 210.506 168.177 1.00 43.75  ? 2430 ASN A N     1 
ATOM   7628  C  CA    . ASN A 1 2430 ? 190.591 210.085 169.045 1.00 47.65  ? 2430 ASN A CA    1 
ATOM   7629  C  C     . ASN A 1 2430 ? 190.600 210.952 170.310 1.00 51.91  ? 2430 ASN A C     1 
ATOM   7630  O  O     . ASN A 1 2430 ? 191.704 211.265 170.807 1.00 51.78  ? 2430 ASN A O     1 
ATOM   7631  C  CB    . ASN A 1 2430 ? 191.914 210.081 168.283 1.00 55.28  ? 2430 ASN A CB    1 
ATOM   7632  C  CG    . ASN A 1 2430 ? 192.286 211.438 167.734 1.00 57.56  ? 2430 ASN A CG    1 
ATOM   7633  O  OD1   . ASN A 1 2430 ? 192.552 212.371 168.499 1.00 61.24  ? 2430 ASN A OD1   1 
ATOM   7634  N  ND2   . ASN A 1 2430 ? 192.330 211.564 166.416 1.00 49.12  ? 2430 ASN A ND2   1 
ATOM   7635  N  N     . GLY A 1 2431 ? 189.416 211.308 170.818 1.00 49.53  ? 2431 GLY A N     1 
ATOM   7636  C  CA    . GLY A 1 2431 ? 189.318 212.128 172.041 1.00 40.50  ? 2431 GLY A CA    1 
ATOM   7637  C  C     . GLY A 1 2431 ? 189.389 211.262 173.283 1.00 38.04  ? 2431 GLY A C     1 
ATOM   7638  O  O     . GLY A 1 2431 ? 189.575 210.036 173.137 1.00 41.68  ? 2431 GLY A O     1 
ATOM   7639  N  N     . LEU A 1 2432 ? 189.241 211.869 174.464 1.00 35.31  ? 2432 LEU A N     1 
ATOM   7640  C  CA    . LEU A 1 2432 ? 189.327 211.109 175.738 1.00 26.40  ? 2432 LEU A CA    1 
ATOM   7641  C  C     . LEU A 1 2432 ? 188.348 209.928 175.685 1.00 27.06  ? 2432 LEU A C     1 
ATOM   7642  O  O     . LEU A 1 2432 ? 188.785 208.786 175.936 1.00 32.47  ? 2432 LEU A O     1 
ATOM   7643  C  CB    . LEU A 1 2432 ? 189.013 212.040 176.907 1.00 28.01  ? 2432 LEU A CB    1 
ATOM   7644  C  CG    . LEU A 1 2432 ? 188.914 211.376 178.284 1.00 35.98  ? 2432 LEU A CG    1 
ATOM   7645  C  CD1   . LEU A 1 2432 ? 190.234 210.735 178.676 1.00 30.25  ? 2432 LEU A CD1   1 
ATOM   7646  C  CD2   . LEU A 1 2432 ? 188.469 212.374 179.339 1.00 29.12  ? 2432 LEU A CD2   1 
ATOM   7647  N  N     . VAL A 1 2433 ? 187.083 210.197 175.351 1.00 29.07  ? 2433 VAL A N     1 
ATOM   7648  C  CA    . VAL A 1 2433 ? 186.049 209.120 175.312 1.00 22.93  ? 2433 VAL A CA    1 
ATOM   7649  C  C     . VAL A 1 2433 ? 186.486 208.064 174.287 1.00 26.99  ? 2433 VAL A C     1 
ATOM   7650  O  O     . VAL A 1 2433 ? 186.436 206.860 174.621 1.00 30.68  ? 2433 VAL A O     1 
ATOM   7651  C  CB    . VAL A 1 2433 ? 184.665 209.695 174.961 1.00 18.20  ? 2433 VAL A CB    1 
ATOM   7652  C  CG1   . VAL A 1 2433 ? 183.575 208.633 175.040 1.00 20.17  ? 2433 VAL A CG1   1 
ATOM   7653  C  CG2   . VAL A 1 2433 ? 184.311 210.896 175.830 1.00 22.02  ? 2433 VAL A CG2   1 
ATOM   7654  N  N     . THR A 1 2434 ? 186.915 208.502 173.100 1.00 29.33  ? 2434 THR A N     1 
ATOM   7655  C  CA    . THR A 1 2434 ? 187.309 207.556 172.034 1.00 30.49  ? 2434 THR A CA    1 
ATOM   7656  C  C     . THR A 1 2434 ? 188.467 206.711 172.519 1.00 31.58  ? 2434 THR A C     1 
ATOM   7657  O  O     . THR A 1 2434 ? 188.384 205.469 172.394 1.00 30.15  ? 2434 THR A O     1 
ATOM   7658  C  CB    . THR A 1 2434 ? 187.671 208.339 170.774 1.00 30.89  ? 2434 THR A CB    1 
ATOM   7659  O  OG1   . THR A 1 2434 ? 186.500 209.077 170.442 1.00 34.07  ? 2434 THR A OG1   1 
ATOM   7660  C  CG2   . THR A 1 2434 ? 188.061 207.434 169.619 1.00 30.83  ? 2434 THR A CG2   1 
ATOM   7661  N  N     . LYS A 1 2435 ? 189.507 207.350 173.062 1.00 29.91  ? 2435 LYS A N     1 
ATOM   7662  C  CA    . LYS A 1 2435 ? 190.711 206.607 173.518 1.00 28.68  ? 2435 LYS A CA    1 
ATOM   7663  C  C     . LYS A 1 2435 ? 190.303 205.641 174.638 1.00 29.31  ? 2435 LYS A C     1 
ATOM   7664  O  O     . LYS A 1 2435 ? 190.725 204.465 174.591 1.00 29.72  ? 2435 LYS A O     1 
ATOM   7665  C  CB    . LYS A 1 2435 ? 191.791 207.582 174.000 1.00 33.75  ? 2435 LYS A CB    1 
ATOM   7666  C  CG    . LYS A 1 2435 ? 192.315 208.544 172.944 1.00 34.98  ? 2435 LYS A CG    1 
ATOM   7667  C  CD    . LYS A 1 2435 ? 193.522 209.341 173.423 1.00 38.94  ? 2435 LYS A CD    1 
ATOM   7668  C  CE    . LYS A 1 2435 ? 193.220 210.167 174.632 1.00 43.24  ? 2435 LYS A CE    1 
ATOM   7669  N  NZ    . LYS A 1 2435 ? 192.262 211.233 174.330 1.00 43.84  ? 2435 LYS A NZ    1 
ATOM   7670  N  N     . ALA A 1 2436 ? 189.506 206.122 175.596 1.00 29.17  ? 2436 ALA A N     1 
ATOM   7671  C  CA    . ALA A 1 2436 ? 189.035 205.259 176.704 1.00 22.62  ? 2436 ALA A CA    1 
ATOM   7672  C  C     . ALA A 1 2436 ? 188.256 204.080 176.122 1.00 22.13  ? 2436 ALA A C     1 
ATOM   7673  O  O     . ALA A 1 2436 ? 188.513 202.926 176.525 1.00 27.55  ? 2436 ALA A O     1 
ATOM   7674  C  CB    . ALA A 1 2436 ? 188.186 206.066 177.657 1.00 21.28  ? 2436 ALA A CB    1 
ATOM   7675  N  N     . LEU A 1 2437 ? 187.337 204.364 175.196 1.00 22.07  ? 2437 LEU A N     1 
ATOM   7676  C  CA    . LEU A 1 2437 ? 186.538 203.302 174.594 1.00 19.09  ? 2437 LEU A CA    1 
ATOM   7677  C  C     . LEU A 1 2437 ? 187.420 202.280 173.888 1.00 22.37  ? 2437 LEU A C     1 
ATOM   7678  O  O     . LEU A 1 2437 ? 187.177 201.072 173.983 1.00 23.95  ? 2437 LEU A O     1 
ATOM   7679  C  CB    . LEU A 1 2437 ? 185.522 203.898 173.622 1.00 18.17  ? 2437 LEU A CB    1 
ATOM   7680  C  CG    . LEU A 1 2437 ? 184.488 202.939 173.031 1.00 15.97  ? 2437 LEU A CG    1 
ATOM   7681  C  CD1   . LEU A 1 2437 ? 183.445 202.569 174.069 1.00 17.16  ? 2437 LEU A CD1   1 
ATOM   7682  C  CD2   . LEU A 1 2437 ? 183.833 203.558 171.808 1.00 19.26  ? 2437 LEU A CD2   1 
ATOM   7683  N  N     . GLU A 1 2438 ? 188.445 202.746 173.171 1.00 27.07  ? 2438 GLU A N     1 
ATOM   7684  C  CA    . GLU A 1 2438 ? 189.359 201.826 172.501 1.00 27.93  ? 2438 GLU A CA    1 
ATOM   7685  C  C     . GLU A 1 2438 ? 190.106 200.959 173.507 1.00 29.15  ? 2438 GLU A C     1 
ATOM   7686  O  O     . GLU A 1 2438 ? 190.273 199.753 173.296 1.00 30.54  ? 2438 GLU A O     1 
ATOM   7687  C  CB    . GLU A 1 2438 ? 190.340 202.611 171.630 1.00 25.54  ? 2438 GLU A CB    1 
ATOM   7688  C  CG    . GLU A 1 2438 ? 190.965 201.802 170.507 1.00 29.42  ? 2438 GLU A CG    1 
ATOM   7689  C  CD    . GLU A 1 2438 ? 192.393 201.397 170.811 1.00 51.25  ? 2438 GLU A CD    1 
ATOM   7690  O  OE1   . GLU A 1 2438 ? 193.124 202.207 171.419 1.00 51.60  ? 2438 GLU A OE1   1 
ATOM   7691  O  OE2   . GLU A 1 2438 ? 192.786 200.271 170.440 1.00 48.84  ? 2438 GLU A OE2   1 
ATOM   7692  N  N     . HIS A 1 2439 ? 190.563 201.559 174.609 1.00 26.28  ? 2439 HIS A N     1 
ATOM   7693  C  CA    . HIS A 1 2439 ? 191.268 200.795 175.632 1.00 28.68  ? 2439 HIS A CA    1 
ATOM   7694  C  C     . HIS A 1 2439 ? 190.331 199.831 176.349 1.00 30.07  ? 2439 HIS A C     1 
ATOM   7695  O  O     . HIS A 1 2439 ? 190.755 198.758 176.793 1.00 31.50  ? 2439 HIS A O     1 
ATOM   7696  C  CB    . HIS A 1 2439 ? 191.927 201.746 176.631 1.00 30.44  ? 2439 HIS A CB    1 
ATOM   7697  C  CG    . HIS A 1 2439 ? 192.699 201.053 177.709 1.00 35.22  ? 2439 HIS A CG    1 
ATOM   7698  N  ND1   . HIS A 1 2439 ? 193.949 200.513 177.499 1.00 33.58  ? 2439 HIS A ND1   1 
ATOM   7699  C  CD2   . HIS A 1 2439 ? 192.399 200.812 179.008 1.00 35.08  ? 2439 HIS A CD2   1 
ATOM   7700  C  CE1   . HIS A 1 2439 ? 194.387 199.970 178.620 1.00 36.95  ? 2439 HIS A CE1   1 
ATOM   7701  N  NE2   . HIS A 1 2439 ? 193.465 200.137 179.551 1.00 37.42  ? 2439 HIS A NE2   1 
ATOM   7702  N  N     . ALA A 1 2440 ? 189.054 200.202 176.478 1.00 27.77  ? 2440 ALA A N     1 
ATOM   7703  C  CA    . ALA A 1 2440 ? 188.097 199.356 177.183 1.00 20.52  ? 2440 ALA A CA    1 
ATOM   7704  C  C     . ALA A 1 2440 ? 187.867 198.033 176.465 1.00 19.71  ? 2440 ALA A C     1 
ATOM   7705  O  O     . ALA A 1 2440 ? 187.669 197.003 177.119 1.00 22.24  ? 2440 ALA A O     1 
ATOM   7706  C  CB    . ALA A 1 2440 ? 186.774 200.097 177.362 1.00 22.39  ? 2440 ALA A CB    1 
ATOM   7707  N  N     . PHE A 1 2441 ? 187.884 198.037 175.130 1.00 25.81  ? 2441 PHE A N     1 
ATOM   7708  C  CA    . PHE A 1 2441 ? 187.644 196.810 174.378 1.00 23.88  ? 2441 PHE A CA    1 
ATOM   7709  C  C     . PHE A 1 2441 ? 188.752 195.783 174.572 1.00 29.45  ? 2441 PHE A C     1 
ATOM   7710  O  O     . PHE A 1 2441 ? 188.556 194.608 174.242 1.00 27.32  ? 2441 PHE A O     1 
ATOM   7711  C  CB    . PHE A 1 2441 ? 187.484 197.127 172.891 1.00 22.29  ? 2441 PHE A CB    1 
ATOM   7712  C  CG    . PHE A 1 2441 ? 186.091 197.532 172.504 1.00 27.64  ? 2441 PHE A CG    1 
ATOM   7713  C  CD1   . PHE A 1 2441 ? 185.739 198.868 172.431 1.00 26.12  ? 2441 PHE A CD1   1 
ATOM   7714  C  CD2   . PHE A 1 2441 ? 185.133 196.575 172.214 1.00 26.58  ? 2441 PHE A CD2   1 
ATOM   7715  C  CE1   . PHE A 1 2441 ? 184.458 199.244 172.076 1.00 23.74  ? 2441 PHE A CE1   1 
ATOM   7716  C  CE2   . PHE A 1 2441 ? 183.850 196.945 171.859 1.00 26.35  ? 2441 PHE A CE2   1 
ATOM   7717  C  CZ    . PHE A 1 2441 ? 183.513 198.281 171.790 1.00 24.53  ? 2441 PHE A CZ    1 
ATOM   7718  N  N     . GLN A 1 2442 ? 189.906 196.194 175.095 1.00 32.20  ? 2442 GLN A N     1 
ATOM   7719  C  CA    . GLN A 1 2442 ? 191.006 195.276 175.352 1.00 27.84  ? 2442 GLN A CA    1 
ATOM   7720  C  C     . GLN A 1 2442 ? 190.924 194.613 176.720 1.00 27.12  ? 2442 GLN A C     1 
ATOM   7721  O  O     . GLN A 1 2442 ? 191.713 193.703 176.998 1.00 36.36  ? 2442 GLN A O     1 
ATOM   7722  C  CB    . GLN A 1 2442 ? 192.346 196.008 175.221 1.00 35.63  ? 2442 GLN A CB    1 
ATOM   7723  C  CG    . GLN A 1 2442 ? 192.756 196.294 173.785 1.00 39.81  ? 2442 GLN A CG    1 
ATOM   7724  C  CD    . GLN A 1 2442 ? 193.266 197.708 173.594 1.00 46.48  ? 2442 GLN A CD    1 
ATOM   7725  O  OE1   . GLN A 1 2442 ? 193.082 198.309 172.536 1.00 47.10  ? 2442 GLN A OE1   1 
ATOM   7726  N  NE2   . GLN A 1 2442 ? 193.913 198.248 174.620 1.00 46.35  ? 2442 GLN A NE2   1 
ATOM   7727  N  N     . LEU A 1 2443 ? 189.998 195.039 177.575 1.00 28.21  ? 2443 LEU A N     1 
ATOM   7728  C  CA    . LEU A 1 2443 ? 189.836 194.432 178.886 1.00 26.71  ? 2443 LEU A CA    1 
ATOM   7729  C  C     . LEU A 1 2443 ? 188.817 193.296 178.819 1.00 26.71  ? 2443 LEU A C     1 
ATOM   7730  O  O     . LEU A 1 2443 ? 188.225 193.012 177.774 1.00 28.03  ? 2443 LEU A O     1 
ATOM   7731  C  CB    . LEU A 1 2443 ? 189.418 195.483 179.912 1.00 24.18  ? 2443 LEU A CB    1 
ATOM   7732  C  CG    . LEU A 1 2443 ? 190.080 196.857 179.803 1.00 25.77  ? 2443 LEU A CG    1 
ATOM   7733  C  CD1   . LEU A 1 2443 ? 189.182 197.929 180.398 1.00 28.35  ? 2443 LEU A CD1   1 
ATOM   7734  C  CD2   . LEU A 1 2443 ? 191.436 196.852 180.483 1.00 31.99  ? 2443 LEU A CD2   1 
ATOM   7735  N  N     . GLU A 1 2444 ? 188.608 192.638 179.954 1.00 21.37  ? 2444 GLU A N     1 
ATOM   7736  C  CA    . GLU A 1 2444 ? 187.672 191.528 180.061 1.00 24.76  ? 2444 GLU A CA    1 
ATOM   7737  C  C     . GLU A 1 2444 ? 186.453 191.975 180.852 1.00 23.34  ? 2444 GLU A C     1 
ATOM   7738  O  O     . GLU A 1 2444 ? 186.586 192.540 181.942 1.00 23.14  ? 2444 GLU A O     1 
ATOM   7739  C  CB    . GLU A 1 2444 ? 188.327 190.317 180.731 1.00 29.89  ? 2444 GLU A CB    1 
ATOM   7740  C  CG    . GLU A 1 2444 ? 187.741 188.980 180.310 1.00 32.23  ? 2444 GLU A CG    1 
ATOM   7741  C  CD    . GLU A 1 2444 ? 186.877 188.358 181.388 1.00 41.95  ? 2444 GLU A CD    1 
ATOM   7742  O  OE1   . GLU A 1 2444 ? 187.361 188.215 182.531 1.00 43.01  ? 2444 GLU A OE1   1 
ATOM   7743  O  OE2   . GLU A 1 2444 ? 185.714 188.011 181.094 1.00 38.08  ? 2444 GLU A OE2   1 
ATOM   7744  N  N     . HIS A 1 2445 ? 185.271 191.723 180.297 1.00 23.13  ? 2445 HIS A N     1 
ATOM   7745  C  CA    . HIS A 1 2445 ? 184.012 192.113 180.908 1.00 19.76  ? 2445 HIS A CA    1 
ATOM   7746  C  C     . HIS A 1 2445 ? 183.145 190.882 181.124 1.00 17.95  ? 2445 HIS A C     1 
ATOM   7747  O  O     . HIS A 1 2445 ? 183.279 189.877 180.419 1.00 16.80  ? 2445 HIS A O     1 
ATOM   7748  C  CB    . HIS A 1 2445 ? 183.269 193.135 180.041 1.00 16.88  ? 2445 HIS A CB    1 
ATOM   7749  C  CG    . HIS A 1 2445 ? 184.136 194.254 179.556 1.00 16.04  ? 2445 HIS A CG    1 
ATOM   7750  N  ND1   . HIS A 1 2445 ? 184.225 195.464 180.209 1.00 19.93  ? 2445 HIS A ND1   1 
ATOM   7751  C  CD2   . HIS A 1 2445 ? 184.963 194.342 178.488 1.00 15.56  ? 2445 HIS A CD2   1 
ATOM   7752  C  CE1   . HIS A 1 2445 ? 185.065 196.251 179.561 1.00 19.44  ? 2445 HIS A CE1   1 
ATOM   7753  N  NE2   . HIS A 1 2445 ? 185.527 195.594 178.513 1.00 16.69  ? 2445 HIS A NE2   1 
ATOM   7754  N  N     . ILE A 1 2446 ? 182.255 190.968 182.115 1.00 16.28  ? 2446 ILE A N     1 
ATOM   7755  C  CA    . ILE A 1 2446 ? 181.371 189.850 182.416 1.00 14.84  ? 2446 ILE A CA    1 
ATOM   7756  C  C     . ILE A 1 2446 ? 180.403 189.579 181.273 1.00 17.23  ? 2446 ILE A C     1 
ATOM   7757  O  O     . ILE A 1 2446 ? 179.858 188.474 181.173 1.00 21.37  ? 2446 ILE A O     1 
ATOM   7758  C  CB    . ILE A 1 2446 ? 180.620 190.108 183.737 1.00 16.11  ? 2446 ILE A CB    1 
ATOM   7759  C  CG1   . ILE A 1 2446 ? 180.209 188.783 184.381 1.00 17.70  ? 2446 ILE A CG1   1 
ATOM   7760  C  CG2   . ILE A 1 2446 ? 179.417 191.014 183.512 1.00 12.44  ? 2446 ILE A CG2   1 
ATOM   7761  C  CD1   . ILE A 1 2446 ? 181.377 187.867 184.672 1.00 14.48  ? 2446 ILE A CD1   1 
ATOM   7762  N  N     . MET A 1 2447 ? 180.179 190.559 180.401 1.00 18.98  ? 2447 MET A N     1 
ATOM   7763  C  CA    . MET A 1 2447 ? 179.363 190.394 179.210 1.00 11.61  ? 2447 MET A CA    1 
ATOM   7764  C  C     . MET A 1 2447 ? 180.130 190.925 178.009 1.00 13.86  ? 2447 MET A C     1 
ATOM   7765  O  O     . MET A 1 2447 ? 181.084 191.695 178.149 1.00 18.61  ? 2447 MET A O     1 
ATOM   7766  C  CB    . MET A 1 2447 ? 178.018 191.119 179.335 1.00 16.37  ? 2447 MET A CB    1 
ATOM   7767  C  CG    . MET A 1 2447 ? 177.080 190.517 180.360 1.00 13.41  ? 2447 MET A CG    1 
ATOM   7768  S  SD    . MET A 1 2447 ? 175.369 190.560 179.804 1.00 27.64  ? 2447 MET A SD    1 
ATOM   7769  C  CE    . MET A 1 2447 ? 174.568 189.664 181.126 1.00 23.29  ? 2447 MET A CE    1 
ATOM   7770  N  N     . ASP A 1 2448 ? 179.711 190.494 176.822 1.00 16.30  ? 2448 ASP A N     1 
ATOM   7771  C  CA    . ASP A 1 2448 ? 180.341 190.968 175.598 1.00 13.84  ? 2448 ASP A CA    1 
ATOM   7772  C  C     . ASP A 1 2448 ? 180.186 192.477 175.479 1.00 16.16  ? 2448 ASP A C     1 
ATOM   7773  O  O     . ASP A 1 2448 ? 179.087 193.016 175.642 1.00 20.80  ? 2448 ASP A O     1 
ATOM   7774  C  CB    . ASP A 1 2448 ? 179.726 190.272 174.384 1.00 15.50  ? 2448 ASP A CB    1 
ATOM   7775  C  CG    . ASP A 1 2448 ? 180.420 188.969 174.047 1.00 24.41  ? 2448 ASP A CG    1 
ATOM   7776  O  OD1   . ASP A 1 2448 ? 181.667 188.956 173.992 1.00 30.84  ? 2448 ASP A OD1   1 
ATOM   7777  O  OD2   . ASP A 1 2448 ? 179.718 187.957 173.836 1.00 21.48  ? 2448 ASP A OD2   1 
ATOM   7778  N  N     . LEU A 1 2449 ? 181.291 193.160 175.197 1.00 16.75  ? 2449 LEU A N     1 
ATOM   7779  C  CA    . LEU A 1 2449 ? 181.300 194.614 175.131 1.00 16.36  ? 2449 LEU A CA    1 
ATOM   7780  C  C     . LEU A 1 2449 ? 180.989 195.081 173.716 1.00 17.89  ? 2449 LEU A C     1 
ATOM   7781  O  O     . LEU A 1 2449 ? 181.652 194.671 172.758 1.00 19.49  ? 2449 LEU A O     1 
ATOM   7782  C  CB    . LEU A 1 2449 ? 182.650 195.174 175.582 1.00 17.77  ? 2449 LEU A CB    1 
ATOM   7783  C  CG    . LEU A 1 2449 ? 182.608 196.629 176.055 1.00 16.62  ? 2449 LEU A CG    1 
ATOM   7784  C  CD1   . LEU A 1 2449 ? 181.928 196.733 177.411 1.00 18.10  ? 2449 LEU A CD1   1 
ATOM   7785  C  CD2   . LEU A 1 2449 ? 184.001 197.234 176.094 1.00 17.04  ? 2449 LEU A CD2   1 
ATOM   7786  N  N     . THR A 1 2450 ? 179.983 195.940 173.595 1.00 16.23  ? 2450 THR A N     1 
ATOM   7787  C  CA    . THR A 1 2450 ? 179.634 196.580 172.338 1.00 17.69  ? 2450 THR A CA    1 
ATOM   7788  C  C     . THR A 1 2450 ? 179.727 198.089 172.505 1.00 17.39  ? 2450 THR A C     1 
ATOM   7789  O  O     . THR A 1 2450 ? 179.592 198.616 173.614 1.00 16.26  ? 2450 THR A O     1 
ATOM   7790  C  CB    . THR A 1 2450 ? 178.226 196.186 171.874 1.00 16.18  ? 2450 THR A CB    1 
ATOM   7791  O  OG1   . THR A 1 2450 ? 177.301 196.344 172.957 1.00 25.77  ? 2450 THR A OG1   1 
ATOM   7792  C  CG2   . THR A 1 2450 ? 178.206 194.740 171.399 1.00 9.73   ? 2450 THR A CG2   1 
ATOM   7793  N  N     . ARG A 1 2451 ? 179.972 198.780 171.390 1.00 14.09  ? 2451 ARG A N     1 
ATOM   7794  C  CA    . ARG A 1 2451 ? 180.206 200.220 171.447 1.00 14.44  ? 2451 ARG A CA    1 
ATOM   7795  C  C     . ARG A 1 2451 ? 178.979 200.970 171.952 1.00 12.75  ? 2451 ARG A C     1 
ATOM   7796  O  O     . ARG A 1 2451 ? 179.099 201.880 172.781 1.00 15.54  ? 2451 ARG A O     1 
ATOM   7797  C  CB    . ARG A 1 2451 ? 180.619 200.735 170.068 1.00 18.16  ? 2451 ARG A CB    1 
ATOM   7798  C  CG    . ARG A 1 2451 ? 180.683 202.248 169.964 1.00 16.33  ? 2451 ARG A CG    1 
ATOM   7799  C  CD    . ARG A 1 2451 ? 181.065 202.691 168.564 1.00 23.61  ? 2451 ARG A CD    1 
ATOM   7800  N  NE    . ARG A 1 2451 ? 180.140 202.181 167.559 1.00 22.42  ? 2451 ARG A NE    1 
ATOM   7801  C  CZ    . ARG A 1 2451 ? 180.227 202.439 166.262 1.00 18.56  ? 2451 ARG A CZ    1 
ATOM   7802  N  NH1   . ARG A 1 2451 ? 181.187 203.207 165.773 1.00 13.17  ? 2451 ARG A NH1   1 
ATOM   7803  N  NH2   . ARG A 1 2451 ? 179.328 201.916 165.434 1.00 19.12  ? 2451 ARG A NH2   1 
ATOM   7804  N  N     . LEU A 1 2452 ? 177.791 200.603 171.472 1.00 14.15  ? 2452 LEU A N     1 
ATOM   7805  C  CA    . LEU A 1 2452 ? 176.600 201.379 171.798 1.00 11.94  ? 2452 LEU A CA    1 
ATOM   7806  C  C     . LEU A 1 2452 ? 176.084 201.111 173.206 1.00 12.44  ? 2452 LEU A C     1 
ATOM   7807  O  O     . LEU A 1 2452 ? 175.451 201.992 173.799 1.00 14.56  ? 2452 LEU A O     1 
ATOM   7808  C  CB    . LEU A 1 2452 ? 175.501 201.119 170.770 1.00 8.44   ? 2452 LEU A CB    1 
ATOM   7809  C  CG    . LEU A 1 2452 ? 175.605 202.039 169.552 1.00 6.16   ? 2452 LEU A CG    1 
ATOM   7810  C  CD1   . LEU A 1 2452 ? 174.388 201.907 168.666 1.00 9.16   ? 2452 LEU A CD1   1 
ATOM   7811  C  CD2   . LEU A 1 2452 ? 175.798 203.483 169.985 1.00 9.78   ? 2452 LEU A CD2   1 
ATOM   7812  N  N     . ARG A 1 2453 ? 176.320 199.918 173.756 1.00 12.27  ? 2453 ARG A N     1 
ATOM   7813  C  CA    . ARG A 1 2453 ? 175.980 199.687 175.158 1.00 10.07  ? 2453 ARG A CA    1 
ATOM   7814  C  C     . ARG A 1 2453 ? 176.761 200.628 176.063 1.00 15.53  ? 2453 ARG A C     1 
ATOM   7815  O  O     . ARG A 1 2453 ? 176.196 201.265 176.960 1.00 20.96  ? 2453 ARG A O     1 
ATOM   7816  C  CB    . ARG A 1 2453 ? 176.263 198.240 175.554 1.00 11.24  ? 2453 ARG A CB    1 
ATOM   7817  C  CG    . ARG A 1 2453 ? 175.985 197.983 177.028 1.00 10.84  ? 2453 ARG A CG    1 
ATOM   7818  C  CD    . ARG A 1 2453 ? 175.953 196.511 177.378 1.00 11.39  ? 2453 ARG A CD    1 
ATOM   7819  N  NE    . ARG A 1 2453 ? 177.218 195.859 177.069 1.00 17.70  ? 2453 ARG A NE    1 
ATOM   7820  C  CZ    . ARG A 1 2453 ? 178.005 195.299 177.976 1.00 18.14  ? 2453 ARG A CZ    1 
ATOM   7821  N  NH1   . ARG A 1 2453 ? 177.702 195.321 179.263 1.00 20.88  ? 2453 ARG A NH1   1 
ATOM   7822  N  NH2   . ARG A 1 2453 ? 179.131 194.709 177.584 1.00 21.00  ? 2453 ARG A NH2   1 
ATOM   7823  N  N     . CYS A 1 2454 ? 178.073 200.718 175.841 1.00 13.16  ? 2454 CYS A N     1 
ATOM   7824  C  CA    . CYS A 1 2454 ? 178.916 201.584 176.655 1.00 10.24  ? 2454 CYS A CA    1 
ATOM   7825  C  C     . CYS A 1 2454 ? 178.530 203.046 176.482 1.00 10.36  ? 2454 CYS A C     1 
ATOM   7826  O  O     . CYS A 1 2454 ? 178.467 203.802 177.460 1.00 11.98  ? 2454 CYS A O     1 
ATOM   7827  C  CB    . CYS A 1 2454 ? 180.382 201.369 176.282 1.00 14.34  ? 2454 CYS A CB    1 
ATOM   7828  S  SG    . CYS A 1 2454 ? 181.282 200.278 177.395 1.00 34.82  ? 2454 CYS A SG    1 
ATOM   7829  N  N     . LEU A 1 2455 ? 178.264 203.461 175.243 1.00 15.47  ? 2455 LEU A N     1 
ATOM   7830  C  CA    . LEU A 1 2455 ? 177.972 204.865 174.976 1.00 13.93  ? 2455 LEU A CA    1 
ATOM   7831  C  C     . LEU A 1 2455 ? 176.571 205.240 175.444 1.00 11.73  ? 2455 LEU A C     1 
ATOM   7832  O  O     . LEU A 1 2455 ? 176.362 206.337 175.974 1.00 15.73  ? 2455 LEU A O     1 
ATOM   7833  C  CB    . LEU A 1 2455 ? 178.149 205.151 173.487 1.00 14.11  ? 2455 LEU A CB    1 
ATOM   7834  C  CG    . LEU A 1 2455 ? 179.594 205.420 173.057 1.00 12.93  ? 2455 LEU A CG    1 
ATOM   7835  C  CD1   . LEU A 1 2455 ? 179.638 206.268 171.808 1.00 19.51  ? 2455 LEU A CD1   1 
ATOM   7836  C  CD2   . LEU A 1 2455 ? 180.384 206.082 174.178 1.00 11.90  ? 2455 LEU A CD2   1 
ATOM   7837  N  N     . GLY A 1 2456 ? 175.598 204.347 175.253 1.00 9.99   ? 2456 GLY A N     1 
ATOM   7838  C  CA    . GLY A 1 2456 ? 174.272 204.591 175.797 1.00 11.31  ? 2456 GLY A CA    1 
ATOM   7839  C  C     . GLY A 1 2456 ? 174.284 204.688 177.310 1.00 17.27  ? 2456 GLY A C     1 
ATOM   7840  O  O     . GLY A 1 2456 ? 173.532 205.467 177.900 1.00 16.87  ? 2456 GLY A O     1 
ATOM   7841  N  N     . SER A 1 2457 ? 175.136 203.891 177.956 1.00 17.97  ? 2457 SER A N     1 
ATOM   7842  C  CA    . SER A 1 2457 ? 175.357 204.038 179.390 1.00 10.54  ? 2457 SER A CA    1 
ATOM   7843  C  C     . SER A 1 2457 ? 175.962 205.398 179.712 1.00 12.00  ? 2457 SER A C     1 
ATOM   7844  O  O     . SER A 1 2457 ? 175.567 206.054 180.683 1.00 14.62  ? 2457 SER A O     1 
ATOM   7845  C  CB    . SER A 1 2457 ? 176.264 202.914 179.891 1.00 10.14  ? 2457 SER A CB    1 
ATOM   7846  O  OG    . SER A 1 2457 ? 176.255 202.845 181.303 1.00 15.46  ? 2457 SER A OG    1 
ATOM   7847  N  N     . LEU A 1 2458 ? 176.931 205.835 178.905 1.00 10.72  ? 2458 LEU A N     1 
ATOM   7848  C  CA    . LEU A 1 2458 ? 177.585 207.116 179.151 1.00 10.32  ? 2458 LEU A CA    1 
ATOM   7849  C  C     . LEU A 1 2458 ? 176.621 208.279 178.958 1.00 13.96  ? 2458 LEU A C     1 
ATOM   7850  O  O     . LEU A 1 2458 ? 176.595 209.213 179.768 1.00 17.74  ? 2458 LEU A O     1 
ATOM   7851  C  CB    . LEU A 1 2458 ? 178.797 207.263 178.230 1.00 11.84  ? 2458 LEU A CB    1 
ATOM   7852  C  CG    . LEU A 1 2458 ? 179.551 208.593 178.248 1.00 15.01  ? 2458 LEU A CG    1 
ATOM   7853  C  CD1   . LEU A 1 2458 ? 180.301 208.761 179.552 1.00 11.89  ? 2458 LEU A CD1   1 
ATOM   7854  C  CD2   . LEU A 1 2458 ? 180.502 208.686 177.067 1.00 19.68  ? 2458 LEU A CD2   1 
ATOM   7855  N  N     . PHE A 1 2459 ? 175.818 208.239 177.892 1.00 14.81  ? 2459 PHE A N     1 
ATOM   7856  C  CA    . PHE A 1 2459 ? 174.921 209.351 177.592 1.00 13.97  ? 2459 PHE A CA    1 
ATOM   7857  C  C     . PHE A 1 2459 ? 173.853 209.516 178.665 1.00 16.15  ? 2459 PHE A C     1 
ATOM   7858  O  O     . PHE A 1 2459 ? 173.519 210.644 179.046 1.00 16.78  ? 2459 PHE A O     1 
ATOM   7859  C  CB    . PHE A 1 2459 ? 174.277 209.152 176.219 1.00 14.84  ? 2459 PHE A CB    1 
ATOM   7860  C  CG    . PHE A 1 2459 ? 175.263 209.088 175.088 1.00 14.97  ? 2459 PHE A CG    1 
ATOM   7861  C  CD1   . PHE A 1 2459 ? 176.523 209.650 175.214 1.00 12.56  ? 2459 PHE A CD1   1 
ATOM   7862  C  CD2   . PHE A 1 2459 ? 174.930 208.463 173.900 1.00 14.99  ? 2459 PHE A CD2   1 
ATOM   7863  C  CE1   . PHE A 1 2459 ? 177.430 209.590 174.175 1.00 14.94  ? 2459 PHE A CE1   1 
ATOM   7864  C  CE2   . PHE A 1 2459 ? 175.833 208.400 172.858 1.00 12.34  ? 2459 PHE A CE2   1 
ATOM   7865  C  CZ    . PHE A 1 2459 ? 177.083 208.964 172.996 1.00 12.47  ? 2459 PHE A CZ    1 
ATOM   7866  N  N     . SER A 1 2460 ? 173.299 208.405 179.157 1.00 15.45  ? 2460 SER A N     1 
ATOM   7867  C  CA    . SER A 1 2460 ? 172.281 208.487 180.200 1.00 13.56  ? 2460 SER A CA    1 
ATOM   7868  C  C     . SER A 1 2460 ? 172.847 209.098 181.475 1.00 16.46  ? 2460 SER A C     1 
ATOM   7869  O  O     . SER A 1 2460 ? 172.176 209.892 182.144 1.00 22.59  ? 2460 SER A O     1 
ATOM   7870  C  CB    . SER A 1 2460 ? 171.702 207.100 180.479 1.00 16.44  ? 2460 SER A CB    1 
ATOM   7871  O  OG    . SER A 1 2460 ? 171.158 206.530 179.302 1.00 25.92  ? 2460 SER A OG    1 
ATOM   7872  N  N     . MET A 1 2461 ? 174.080 208.732 181.831 1.00 14.15  ? 2461 MET A N     1 
ATOM   7873  C  CA    . MET A 1 2461 ? 174.710 209.305 183.015 1.00 11.71  ? 2461 MET A CA    1 
ATOM   7874  C  C     . MET A 1 2461 ? 174.952 210.800 182.843 1.00 16.36  ? 2461 MET A C     1 
ATOM   7875  O  O     . MET A 1 2461 ? 174.776 211.576 183.790 1.00 22.49  ? 2461 MET A O     1 
ATOM   7876  C  CB    . MET A 1 2461 ? 176.018 208.573 183.314 1.00 14.91  ? 2461 MET A CB    1 
ATOM   7877  C  CG    . MET A 1 2461 ? 175.815 207.171 183.867 1.00 14.83  ? 2461 MET A CG    1 
ATOM   7878  S  SD    . MET A 1 2461 ? 177.355 206.278 184.146 1.00 12.76  ? 2461 MET A SD    1 
ATOM   7879  C  CE    . MET A 1 2461 ? 177.948 207.086 185.628 1.00 14.73  ? 2461 MET A CE    1 
ATOM   7880  N  N     . LEU A 1 2462 ? 175.353 211.223 181.642 1.00 16.09  ? 2462 LEU A N     1 
ATOM   7881  C  CA    . LEU A 1 2462 ? 175.560 212.646 181.391 1.00 13.26  ? 2462 LEU A CA    1 
ATOM   7882  C  C     . LEU A 1 2462 ? 174.247 213.417 181.457 1.00 16.09  ? 2462 LEU A C     1 
ATOM   7883  O  O     . LEU A 1 2462 ? 174.234 214.597 181.828 1.00 17.72  ? 2462 LEU A O     1 
ATOM   7884  C  CB    . LEU A 1 2462 ? 176.241 212.847 180.040 1.00 13.28  ? 2462 LEU A CB    1 
ATOM   7885  C  CG    . LEU A 1 2462 ? 177.652 212.269 179.937 1.00 14.42  ? 2462 LEU A CG    1 
ATOM   7886  C  CD1   . LEU A 1 2462 ? 178.120 212.232 178.494 1.00 20.13  ? 2462 LEU A CD1   1 
ATOM   7887  C  CD2   . LEU A 1 2462 ? 178.612 213.076 180.793 1.00 11.73  ? 2462 LEU A CD2   1 
ATOM   7888  N  N     . HIS A 1 2463 ? 173.135 212.775 181.094 1.00 16.84  ? 2463 HIS A N     1 
ATOM   7889  C  CA    . HIS A 1 2463 ? 171.830 213.394 181.300 1.00 18.88  ? 2463 HIS A CA    1 
ATOM   7890  C  C     . HIS A 1 2463 ? 171.558 213.610 182.783 1.00 22.51  ? 2463 HIS A C     1 
ATOM   7891  O  O     . HIS A 1 2463 ? 170.978 214.629 183.176 1.00 25.77  ? 2463 HIS A O     1 
ATOM   7892  C  CB    . HIS A 1 2463 ? 170.729 212.538 180.673 1.00 19.83  ? 2463 HIS A CB    1 
ATOM   7893  C  CG    . HIS A 1 2463 ? 170.723 212.562 179.176 1.00 24.77  ? 2463 HIS A CG    1 
ATOM   7894  N  ND1   . HIS A 1 2463 ? 169.983 211.677 178.421 1.00 21.09  ? 2463 HIS A ND1   1 
ATOM   7895  C  CD2   . HIS A 1 2463 ? 171.360 213.367 178.294 1.00 23.98  ? 2463 HIS A CD2   1 
ATOM   7896  C  CE1   . HIS A 1 2463 ? 170.169 211.934 177.139 1.00 21.81  ? 2463 HIS A CE1   1 
ATOM   7897  N  NE2   . HIS A 1 2463 ? 171.000 212.955 177.035 1.00 23.87  ? 2463 HIS A NE2   1 
ATOM   7898  N  N     . GLN A 1 2464 ? 171.968 212.655 183.622 1.00 23.27  ? 2464 GLN A N     1 
ATOM   7899  C  CA    . GLN A 1 2464 ? 171.781 212.799 185.062 1.00 26.68  ? 2464 GLN A CA    1 
ATOM   7900  C  C     . GLN A 1 2464 ? 172.566 213.985 185.605 1.00 28.84  ? 2464 GLN A C     1 
ATOM   7901  O  O     . GLN A 1 2464 ? 172.088 214.702 186.492 1.00 36.89  ? 2464 GLN A O     1 
ATOM   7902  C  CB    . GLN A 1 2464 ? 172.192 211.512 185.775 1.00 21.94  ? 2464 GLN A CB    1 
ATOM   7903  C  CG    . GLN A 1 2464 ? 171.764 211.440 187.230 1.00 22.89  ? 2464 GLN A CG    1 
ATOM   7904  C  CD    . GLN A 1 2464 ? 170.288 211.721 187.416 1.00 32.63  ? 2464 GLN A CD    1 
ATOM   7905  O  OE1   . GLN A 1 2464 ? 169.442 211.130 186.745 1.00 30.61  ? 2464 GLN A OE1   1 
ATOM   7906  N  NE2   . GLN A 1 2464 ? 169.969 212.628 188.331 1.00 33.36  ? 2464 GLN A NE2   1 
ATOM   7907  N  N     . ALA A 1 2465 ? 173.779 214.204 185.088 1.00 21.64  ? 2465 ALA A N     1 
ATOM   7908  C  CA    . ALA A 1 2465 ? 174.584 215.334 185.540 1.00 23.28  ? 2465 ALA A CA    1 
ATOM   7909  C  C     . ALA A 1 2465 ? 173.890 216.657 185.247 1.00 29.75  ? 2465 ALA A C     1 
ATOM   7910  O  O     . ALA A 1 2465 ? 173.907 217.573 186.078 1.00 34.95  ? 2465 ALA A O     1 
ATOM   7911  C  CB    . ALA A 1 2465 ? 175.962 215.294 184.881 1.00 20.13  ? 2465 ALA A CB    1 
ATOM   7912  N  N     . CYS A 1 2466 ? 173.280 216.780 184.066 1.00 29.62  ? 2466 CYS A N     1 
ATOM   7913  C  CA    . CYS A 1 2466 ? 172.508 217.978 183.756 1.00 31.82  ? 2466 CYS A CA    1 
ATOM   7914  C  C     . CYS A 1 2466 ? 171.312 218.115 184.690 1.00 32.28  ? 2466 CYS A C     1 
ATOM   7915  O  O     . CYS A 1 2466 ? 170.995 219.219 185.147 1.00 34.53  ? 2466 CYS A O     1 
ATOM   7916  C  CB    . CYS A 1 2466 ? 172.053 217.947 182.297 1.00 25.42  ? 2466 CYS A CB    1 
ATOM   7917  S  SG    . CYS A 1 2466 ? 173.397 218.033 181.094 1.00 39.15  ? 2466 CYS A SG    1 
ATOM   7918  N  N     . ARG A 1 2467 ? 170.633 217.002 184.979 1.00 30.40  ? 2467 ARG A N     1 
ATOM   7919  C  CA    . ARG A 1 2467 ? 169.522 217.037 185.924 1.00 32.15  ? 2467 ARG A CA    1 
ATOM   7920  C  C     . ARG A 1 2467 ? 170.006 217.365 187.331 1.00 34.40  ? 2467 ARG A C     1 
ATOM   7921  O  O     . ARG A 1 2467 ? 169.298 218.023 188.102 1.00 37.89  ? 2467 ARG A O     1 
ATOM   7922  C  CB    . ARG A 1 2467 ? 168.778 215.702 185.910 1.00 32.21  ? 2467 ARG A CB    1 
ATOM   7923  C  CG    . ARG A 1 2467 ? 167.996 215.440 184.636 1.00 36.46  ? 2467 ARG A CG    1 
ATOM   7924  C  CD    . ARG A 1 2467 ? 167.319 214.081 184.678 1.00 36.70  ? 2467 ARG A CD    1 
ATOM   7925  N  NE    . ARG A 1 2467 ? 166.292 213.944 183.652 1.00 41.08  ? 2467 ARG A NE    1 
ATOM   7926  C  CZ    . ARG A 1 2467 ? 165.093 214.509 183.707 1.00 46.59  ? 2467 ARG A CZ    1 
ATOM   7927  N  NH1   . ARG A 1 2467 ? 164.727 215.257 184.735 1.00 39.23  ? 2467 ARG A NH1   1 
ATOM   7928  N  NH2   . ARG A 1 2467 ? 164.239 214.317 182.706 1.00 45.78  ? 2467 ARG A NH2   1 
ATOM   7929  N  N     . ASN A 1 2468 ? 171.224 216.924 187.660 1.00 31.23  ? 2468 ASN A N     1 
ATOM   7930  C  CA    . ASN A 1 2468 ? 171.809 217.223 188.996 1.00 30.30  ? 2468 ASN A CA    1 
ATOM   7931  C  C     . ASN A 1 2468 ? 172.014 218.735 189.129 1.00 33.90  ? 2468 ASN A C     1 
ATOM   7932  O  O     . ASN A 1 2468 ? 171.652 219.293 190.189 1.00 35.89  ? 2468 ASN A O     1 
ATOM   7933  C  CB    . ASN A 1 2468 ? 173.111 216.462 189.219 1.00 27.55  ? 2468 ASN A CB    1 
ATOM   7934  C  CG    . ASN A 1 2468 ? 172.898 214.969 189.281 1.00 27.23  ? 2468 ASN A CG    1 
ATOM   7935  O  OD1   . ASN A 1 2468 ? 171.757 214.500 189.212 1.00 32.41  ? 2468 ASN A OD1   1 
ATOM   7936  N  ND2   . ASN A 1 2468 ? 173.975 214.209 189.417 1.00 27.81  ? 2468 ASN A ND2   1 
ATOM   7937  N  N     . VAL A 1 2469 ? 172.572 219.369 188.094 1.00 33.30  ? 2469 VAL A N     1 
ATOM   7938  C  CA    . VAL A 1 2469 ? 172.840 220.839 188.136 1.00 37.14  ? 2469 VAL A CA    1 
ATOM   7939  C  C     . VAL A 1 2469 ? 171.505 221.577 188.324 1.00 39.76  ? 2469 VAL A C     1 
ATOM   7940  O  O     . VAL A 1 2469 ? 171.467 222.540 189.120 1.00 43.54  ? 2469 VAL A O     1 
ATOM   7941  C  CB    . VAL A 1 2469 ? 173.566 221.311 186.862 1.00 38.47  ? 2469 VAL A CB    1 
ATOM   7942  C  CG1   . VAL A 1 2469 ? 173.725 222.826 186.827 1.00 38.58  ? 2469 VAL A CG1   1 
ATOM   7943  C  CG2   . VAL A 1 2469 ? 174.912 220.619 186.691 1.00 34.91  ? 2469 VAL A CG2   1 
ATOM   7944  N  N     . ALA A 1 2470 ? 170.459 221.131 187.625 1.00 36.74  ? 2470 ALA A N     1 
ATOM   7945  C  CA    . ALA A 1 2470 ? 169.126 221.765 187.756 1.00 36.68  ? 2470 ALA A CA    1 
ATOM   7946  C  C     . ALA A 1 2470 ? 168.670 221.684 189.214 1.00 43.87  ? 2470 ALA A C     1 
ATOM   7947  O  O     . ALA A 1 2470 ? 168.155 222.691 189.745 1.00 52.36  ? 2470 ALA A O     1 
ATOM   7948  C  CB    . ALA A 1 2470 ? 168.143 221.085 186.832 1.00 34.95  ? 2470 ALA A CB    1 
ATOM   7949  N  N     . GLN A 1 2471 ? 168.867 220.523 189.844 1.00 44.12  ? 2471 GLN A N     1 
ATOM   7950  C  CA    . GLN A 1 2471 ? 168.452 220.336 191.258 1.00 46.93  ? 2471 GLN A CA    1 
ATOM   7951  C  C     . GLN A 1 2471 ? 169.187 221.357 192.141 1.00 49.01  ? 2471 GLN A C     1 
ATOM   7952  O  O     . GLN A 1 2471 ? 168.524 221.995 192.987 1.00 57.35  ? 2471 GLN A O     1 
ATOM   7953  C  CB    . GLN A 1 2471 ? 168.753 218.905 191.701 1.00 43.62  ? 2471 GLN A CB    1 
ATOM   7954  C  CG    . GLN A 1 2471 ? 168.384 218.614 193.151 1.00 54.37  ? 2471 GLN A CG    1 
ATOM   7955  C  CD    . GLN A 1 2471 ? 168.765 217.219 193.594 1.00 64.12  ? 2471 GLN A CD    1 
ATOM   7956  O  OE1   . GLN A 1 2471 ? 168.308 216.217 193.033 1.00 66.43  ? 2471 GLN A OE1   1 
ATOM   7957  N  NE2   . GLN A 1 2471 ? 169.613 217.142 194.609 1.00 56.04  ? 2471 GLN A NE2   1 
ATOM   7958  N  N     . TYR A 1 2472 ? 170.499 221.510 191.940 1.00 45.71  ? 2472 TYR A N     1 
ATOM   7959  C  CA    . TYR A 1 2472 ? 171.294 222.474 192.748 1.00 45.22  ? 2472 TYR A CA    1 
ATOM   7960  C  C     . TYR A 1 2472 ? 170.716 223.873 192.562 1.00 47.02  ? 2472 TYR A C     1 
ATOM   7961  O  O     . TYR A 1 2472 ? 170.522 224.592 193.565 1.00 48.61  ? 2472 TYR A O     1 
ATOM   7962  C  CB    . TYR A 1 2472 ? 172.767 222.442 192.333 1.00 40.32  ? 2472 TYR A CB    1 
ATOM   7963  C  CG    . TYR A 1 2472 ? 173.592 223.594 192.892 1.00 43.32  ? 2472 TYR A CG    1 
ATOM   7964  C  CD1   . TYR A 1 2472 ? 174.220 223.494 194.127 1.00 46.17  ? 2472 TYR A CD1   1 
ATOM   7965  C  CD2   . TYR A 1 2472 ? 173.738 224.781 192.185 1.00 48.44  ? 2472 TYR A CD2   1 
ATOM   7966  C  CE1   . TYR A 1 2472 ? 174.969 224.539 194.641 1.00 48.18  ? 2472 TYR A CE1   1 
ATOM   7967  C  CE2   . TYR A 1 2472 ? 174.484 225.833 192.689 1.00 47.18  ? 2472 TYR A CE2   1 
ATOM   7968  C  CZ    . TYR A 1 2472 ? 175.102 225.711 193.920 1.00 51.07  ? 2472 TYR A CZ    1 
ATOM   7969  O  OH    . TYR A 1 2472 ? 175.839 226.745 194.420 1.00 57.75  ? 2472 TYR A OH    1 
ATOM   7970  N  N     . ASN A 1 2473 ? 170.444 224.250 191.310 1.00 52.47  ? 2473 ASN A N     1 
ATOM   7971  C  CA    . ASN A 1 2473 ? 169.912 225.610 191.017 1.00 52.29  ? 2473 ASN A CA    1 
ATOM   7972  C  C     . ASN A 1 2473 ? 168.556 225.775 191.709 1.00 54.37  ? 2473 ASN A C     1 
ATOM   7973  O  O     . ASN A 1 2473 ? 168.315 226.856 192.287 1.00 54.71  ? 2473 ASN A O     1 
ATOM   7974  C  CB    . ASN A 1 2473 ? 169.843 225.863 189.515 1.00 47.14  ? 2473 ASN A CB    1 
ATOM   7975  C  CG    . ASN A 1 2473 ? 171.199 225.751 188.860 1.00 54.52  ? 2473 ASN A CG    1 
ATOM   7976  O  OD1   . ASN A 1 2473 ? 172.197 225.481 189.538 1.00 52.18  ? 2473 ASN A OD1   1 
ATOM   7977  N  ND2   . ASN A 1 2473 ? 171.258 225.953 187.552 1.00 55.48  ? 2473 ASN A ND2   1 
ATOM   7978  N  N     . ALA A 1 2474 ? 167.708 224.744 191.654 1.00 53.73  ? 2474 ALA A N     1 
ATOM   7979  C  CA    . ALA A 1 2474 ? 166.391 224.798 192.333 1.00 51.20  ? 2474 ALA A CA    1 
ATOM   7980  C  C     . ALA A 1 2474 ? 166.607 224.925 193.841 1.00 51.05  ? 2474 ALA A C     1 
ATOM   7981  O  O     . ALA A 1 2474 ? 165.956 225.784 194.473 1.00 51.74  ? 2474 ALA A O     1 
ATOM   7982  C  CB    . ALA A 1 2474 ? 165.584 223.566 191.991 1.00 49.34  ? 2474 ALA A CB    1 
ATOM   7983  N  N     . ASN A 1 2475 ? 167.494 224.098 194.399 1.00 51.85  ? 2475 ASN A N     1 
ATOM   7984  C  CA    . ASN A 1 2475 ? 167.787 224.159 195.826 1.00 54.71  ? 2475 ASN A CA    1 
ATOM   7985  C  C     . ASN A 1 2475 ? 168.488 225.452 196.219 1.00 53.34  ? 2475 ASN A C     1 
ATOM   7986  O  O     . ASN A 1 2475 ? 168.492 225.804 197.404 1.00 50.74  ? 2475 ASN A O     1 
ATOM   7987  C  CB    . ASN A 1 2475 ? 168.641 222.961 196.242 1.00 51.88  ? 2475 ASN A CB    1 
ATOM   7988  C  CG    . ASN A 1 2475 ? 167.909 221.643 196.091 1.00 55.54  ? 2475 ASN A CG    1 
ATOM   7989  O  OD1   . ASN A 1 2475 ? 166.725 221.538 196.411 1.00 53.63  ? 2475 ASN A OD1   1 
ATOM   7990  N  ND2   . ASN A 1 2475 ? 168.612 220.627 195.604 1.00 52.37  ? 2475 ASN A ND2   1 
ATOM   7991  N  N     . HIS A 1 2476 ? 169.079 226.163 195.261 1.00 53.20  ? 2476 HIS A N     1 
ATOM   7992  C  CA    . HIS A 1 2476 ? 169.769 227.428 195.513 1.00 55.27  ? 2476 HIS A CA    1 
ATOM   7993  C  C     . HIS A 1 2476 ? 169.242 228.476 194.541 1.00 63.23  ? 2476 HIS A C     1 
ATOM   7994  O  O     . HIS A 1 2476 ? 169.946 228.889 193.611 1.00 67.71  ? 2476 HIS A O     1 
ATOM   7995  C  CB    . HIS A 1 2476 ? 171.284 227.270 195.373 1.00 56.90  ? 2476 HIS A CB    1 
ATOM   7996  C  CG    . HIS A 1 2476 ? 171.885 226.272 196.314 1.00 56.02  ? 2476 HIS A CG    1 
ATOM   7997  N  ND1   . HIS A 1 2476 ? 171.534 224.939 196.316 1.00 49.04  ? 2476 HIS A ND1   1 
ATOM   7998  C  CD2   . HIS A 1 2476 ? 172.823 226.413 197.281 1.00 56.77  ? 2476 HIS A CD2   1 
ATOM   7999  C  CE1   . HIS A 1 2476 ? 172.225 224.304 197.245 1.00 52.22  ? 2476 HIS A CE1   1 
ATOM   8000  N  NE2   . HIS A 1 2476 ? 173.015 225.175 197.845 1.00 58.83  ? 2476 HIS A NE2   1 
ATOM   8001  N  N     . PRO A 1 2477 ? 167.992 228.919 194.719 1.00 63.90  ? 2477 PRO A N     1 
ATOM   8002  C  CA    . PRO A 1 2477 ? 167.433 229.904 193.775 1.00 65.27  ? 2477 PRO A CA    1 
ATOM   8003  C  C     . PRO A 1 2477 ? 168.204 231.212 193.735 1.00 69.49  ? 2477 PRO A C     1 
ATOM   8004  O  O     . PRO A 1 2477 ? 168.323 231.824 192.666 1.00 66.29  ? 2477 PRO A O     1 
ATOM   8005  C  CB    . PRO A 1 2477 ? 165.999 230.106 194.290 1.00 59.23  ? 2477 PRO A CB    1 
ATOM   8006  C  CG    . PRO A 1 2477 ? 165.723 228.923 195.166 1.00 56.19  ? 2477 PRO A CG    1 
ATOM   8007  C  CD    . PRO A 1 2477 ? 167.037 228.575 195.783 1.00 57.69  ? 2477 PRO A CD    1 
ATOM   8008  N  N     . ASP A 1 2478 ? 168.743 231.622 194.886 1.00 71.42  ? 2478 ASP A N     1 
ATOM   8009  C  CA    . ASP A 1 2478 ? 169.551 232.871 194.950 1.00 77.54  ? 2478 ASP A CA    1 
ATOM   8010  C  C     . ASP A 1 2478 ? 170.865 232.666 194.190 1.00 77.25  ? 2478 ASP A C     1 
ATOM   8011  O  O     . ASP A 1 2478 ? 171.222 233.547 193.378 1.00 76.48  ? 2478 ASP A O     1 
ATOM   8012  C  CB    . ASP A 1 2478 ? 169.782 233.309 196.387 1.00 79.89  ? 2478 ASP A CB    1 
ATOM   8013  C  CG    . ASP A 1 2478 ? 170.955 234.254 196.600 1.00 86.72  ? 2478 ASP A CG    1 
ATOM   8014  O  OD1   . ASP A 1 2478 ? 170.953 235.340 195.983 1.00 87.58  ? 2478 ASP A OD1   1 
ATOM   8015  O  OD2   . ASP A 1 2478 ? 171.857 233.898 197.385 1.00 86.35  ? 2478 ASP A OD2   1 
ATOM   8016  N  N     . PHE A 1 2479 ? 171.555 231.550 194.442 1.00 73.76  ? 2479 PHE A N     1 
ATOM   8017  C  CA    . PHE A 1 2479 ? 172.873 231.307 193.793 1.00 76.03  ? 2479 PHE A CA    1 
ATOM   8018  C  C     . PHE A 1 2479 ? 172.815 230.028 192.961 1.00 74.07  ? 2479 PHE A C     1 
ATOM   8019  O  O     . PHE A 1 2479 ? 173.010 228.926 193.516 1.00 72.86  ? 2479 PHE A O     1 
ATOM   8020  C  CB    . PHE A 1 2479 ? 173.968 231.242 194.862 1.00 77.80  ? 2479 PHE A CB    1 
ATOM   8021  C  CG    . PHE A 1 2479 ? 174.240 232.567 195.561 1.00 83.83  ? 2479 PHE A CG    1 
ATOM   8022  C  CD1   . PHE A 1 2479 ? 174.039 233.774 194.901 1.00 81.26  ? 2479 PHE A CD1   1 
ATOM   8023  C  CD2   . PHE A 1 2479 ? 174.698 232.602 196.872 1.00 84.83  ? 2479 PHE A CD2   1 
ATOM   8024  C  CE1   . PHE A 1 2479 ? 174.287 234.979 195.538 1.00 81.81  ? 2479 PHE A CE1   1 
ATOM   8025  C  CE2   . PHE A 1 2479 ? 174.946 233.810 197.504 1.00 84.60  ? 2479 PHE A CE2   1 
ATOM   8026  C  CZ    . PHE A 1 2479 ? 174.740 234.995 196.837 1.00 86.27  ? 2479 PHE A CZ    1 
ATOM   8027  N  N     . PRO A 1 2480 ? 172.566 230.117 191.635 1.00 69.84  ? 2480 PRO A N     1 
ATOM   8028  C  CA    . PRO A 1 2480 ? 172.582 228.939 190.781 1.00 61.82  ? 2480 PRO A CA    1 
ATOM   8029  C  C     . PRO A 1 2480 ? 174.016 228.559 190.447 1.00 60.28  ? 2480 PRO A C     1 
ATOM   8030  O  O     . PRO A 1 2480 ? 174.932 229.370 190.693 1.00 60.62  ? 2480 PRO A O     1 
ATOM   8031  C  CB    . PRO A 1 2480 ? 171.802 229.418 189.555 1.00 56.28  ? 2480 PRO A CB    1 
ATOM   8032  C  CG    . PRO A 1 2480 ? 172.132 230.891 189.476 1.00 58.16  ? 2480 PRO A CG    1 
ATOM   8033  C  CD    . PRO A 1 2480 ? 172.256 231.346 190.922 1.00 65.14  ? 2480 PRO A CD    1 
ATOM   8034  N  N     . MET A 1 2481 ? 174.216 227.357 189.900 1.00 53.32  ? 2481 MET A N     1 
ATOM   8035  C  CA    . MET A 1 2481 ? 175.591 226.883 189.591 1.00 56.30  ? 2481 MET A CA    1 
ATOM   8036  C  C     . MET A 1 2481 ? 176.261 227.866 188.617 1.00 56.07  ? 2481 MET A C     1 
ATOM   8037  O  O     . MET A 1 2481 ? 175.586 228.306 187.661 1.00 51.63  ? 2481 MET A O     1 
ATOM   8038  C  CB    . MET A 1 2481 ? 175.569 225.481 188.973 1.00 56.46  ? 2481 MET A CB    1 
ATOM   8039  C  CG    . MET A 1 2481 ? 176.935 224.978 188.552 1.00 52.14  ? 2481 MET A CG    1 
ATOM   8040  S  SD    . MET A 1 2481 ? 176.942 223.222 188.139 1.00 69.73  ? 2481 MET A SD    1 
ATOM   8041  C  CE    . MET A 1 2481 ? 176.357 222.530 189.692 1.00 49.62  ? 2481 MET A CE    1 
ATOM   8042  N  N     . GLN A 1 2482 ? 177.533 228.197 188.859 1.00 55.89  ? 2482 GLN A N     1 
ATOM   8043  C  CA    . GLN A 1 2482 ? 178.276 229.121 187.961 1.00 58.40  ? 2482 GLN A CA    1 
ATOM   8044  C  C     . GLN A 1 2482 ? 178.894 228.320 186.803 1.00 58.02  ? 2482 GLN A C     1 
ATOM   8045  O  O     . GLN A 1 2482 ? 178.943 227.075 186.902 1.00 59.77  ? 2482 GLN A O     1 
ATOM   8046  C  CB    . GLN A 1 2482 ? 179.350 229.875 188.742 1.00 55.98  ? 2482 GLN A CB    1 
ATOM   8047  C  CG    . GLN A 1 2482 ? 178.793 230.727 189.876 1.00 55.28  ? 2482 GLN A CG    1 
ATOM   8048  C  CD    . GLN A 1 2482 ? 177.661 231.628 189.435 1.00 56.01  ? 2482 GLN A CD    1 
ATOM   8049  O  OE1   . GLN A 1 2482 ? 177.818 232.475 188.549 1.00 59.65  ? 2482 GLN A OE1   1 
ATOM   8050  N  NE2   . GLN A 1 2482 ? 176.500 231.448 190.047 1.00 54.92  ? 2482 GLN A NE2   1 
ATOM   8051  N  N     . ILE A 1 2483 ? 179.353 229.011 185.756 1.00 56.12  ? 2483 ILE A N     1 
ATOM   8052  C  CA    . ILE A 1 2483 ? 179.955 228.321 184.575 1.00 56.51  ? 2483 ILE A CA    1 
ATOM   8053  C  C     . ILE A 1 2483 ? 181.206 227.553 185.031 1.00 56.71  ? 2483 ILE A C     1 
ATOM   8054  O  O     . ILE A 1 2483 ? 181.362 226.383 184.622 1.00 57.78  ? 2483 ILE A O     1 
ATOM   8055  C  CB    . ILE A 1 2483 ? 180.279 229.326 183.454 1.00 61.01  ? 2483 ILE A CB    1 
ATOM   8056  C  CG1   . ILE A 1 2483 ? 179.042 230.123 183.045 1.00 61.05  ? 2483 ILE A CG1   1 
ATOM   8057  C  CG2   . ILE A 1 2483 ? 180.920 228.622 182.258 1.00 56.55  ? 2483 ILE A CG2   1 
ATOM   8058  C  CD1   . ILE A 1 2483 ? 177.876 229.262 182.595 1.00 60.56  ? 2483 ILE A CD1   1 
ATOM   8059  N  N     . GLU A 1 2484 ? 182.053 228.187 185.848 1.00 55.81  ? 2484 GLU A N     1 
ATOM   8060  C  CA    . GLU A 1 2484 ? 183.282 227.517 186.350 1.00 56.62  ? 2484 GLU A CA    1 
ATOM   8061  C  C     . GLU A 1 2484 ? 182.877 226.261 187.138 1.00 55.51  ? 2484 GLU A C     1 
ATOM   8062  O  O     . GLU A 1 2484 ? 183.487 225.193 186.906 1.00 53.39  ? 2484 GLU A O     1 
ATOM   8063  C  CB    . GLU A 1 2484 ? 184.108 228.463 187.223 1.00 54.12  ? 2484 GLU A CB    1 
ATOM   8064  C  CG    . GLU A 1 2484 ? 183.344 228.998 188.430 1.00 60.00  ? 2484 GLU A CG    1 
ATOM   8065  C  CD    . GLU A 1 2484 ? 184.201 229.798 189.394 1.00 72.53  ? 2484 GLU A CD    1 
ATOM   8066  O  OE1   . GLU A 1 2484 ? 184.764 230.829 188.968 1.00 75.47  ? 2484 GLU A OE1   1 
ATOM   8067  O  OE2   . GLU A 1 2484 ? 184.307 229.388 190.568 1.00 71.90  ? 2484 GLU A OE2   1 
ATOM   8068  N  N     . GLN A 1 2485 ? 181.879 226.386 188.017 1.00 54.85  ? 2485 GLN A N     1 
ATOM   8069  C  CA    . GLN A 1 2485 ? 181.411 225.226 188.817 1.00 53.09  ? 2485 GLN A CA    1 
ATOM   8070  C  C     . GLN A 1 2485 ? 180.896 224.145 187.856 1.00 50.66  ? 2485 GLN A C     1 
ATOM   8071  O  O     . GLN A 1 2485 ? 181.282 222.967 188.022 1.00 52.51  ? 2485 GLN A O     1 
ATOM   8072  C  CB    . GLN A 1 2485 ? 180.315 225.655 189.792 1.00 53.60  ? 2485 GLN A CB    1 
ATOM   8073  C  CG    . GLN A 1 2485 ? 179.834 224.539 190.713 1.00 52.42  ? 2485 GLN A CG    1 
ATOM   8074  C  CD    . GLN A 1 2485 ? 178.801 225.000 191.718 1.00 56.19  ? 2485 GLN A CD    1 
ATOM   8075  O  OE1   . GLN A 1 2485 ? 177.675 224.492 191.769 1.00 53.36  ? 2485 GLN A OE1   1 
ATOM   8076  N  NE2   . GLN A 1 2485 ? 179.178 225.973 192.534 1.00 56.99  ? 2485 GLN A NE2   1 
ATOM   8077  N  N     . LEU A 1 2486 ? 180.079 224.544 186.878 1.00 46.60  ? 2486 LEU A N     1 
ATOM   8078  C  CA    . LEU A 1 2486 ? 179.510 223.567 185.915 1.00 41.64  ? 2486 LEU A CA    1 
ATOM   8079  C  C     . LEU A 1 2486 ? 180.663 222.862 185.189 1.00 44.26  ? 2486 LEU A C     1 
ATOM   8080  O  O     . LEU A 1 2486 ? 180.627 221.618 185.090 1.00 41.95  ? 2486 LEU A O     1 
ATOM   8081  C  CB    . LEU A 1 2486 ? 178.583 224.284 184.936 1.00 41.65  ? 2486 LEU A CB    1 
ATOM   8082  C  CG    . LEU A 1 2486 ? 177.928 223.400 183.870 1.00 39.57  ? 2486 LEU A CG    1 
ATOM   8083  C  CD1   . LEU A 1 2486 ? 177.138 222.279 184.520 1.00 44.89  ? 2486 LEU A CD1   1 
ATOM   8084  C  CD2   . LEU A 1 2486 ? 177.035 224.222 182.957 1.00 35.44  ? 2486 LEU A CD2   1 
ATOM   8085  N  N     . GLU A 1 2487 ? 181.655 223.629 184.730 1.00 44.78  ? 2487 GLU A N     1 
ATOM   8086  C  CA    . GLU A 1 2487 ? 182.782 223.037 183.966 1.00 42.77  ? 2487 GLU A CA    1 
ATOM   8087  C  C     . GLU A 1 2487 ? 183.479 221.976 184.829 1.00 40.83  ? 2487 GLU A C     1 
ATOM   8088  O  O     . GLU A 1 2487 ? 183.663 220.842 184.339 1.00 37.85  ? 2487 GLU A O     1 
ATOM   8089  C  CB    . GLU A 1 2487 ? 183.772 224.128 183.562 1.00 46.52  ? 2487 GLU A CB    1 
ATOM   8090  C  CG    . GLU A 1 2487 ? 184.935 223.599 182.729 1.00 48.34  ? 2487 GLU A CG    1 
ATOM   8091  C  CD    . GLU A 1 2487 ? 186.042 224.613 182.508 1.00 54.65  ? 2487 GLU A CD    1 
ATOM   8092  O  OE1   . GLU A 1 2487 ? 186.624 225.075 183.511 1.00 61.01  ? 2487 GLU A OE1   1 
ATOM   8093  O  OE2   . GLU A 1 2487 ? 186.323 224.939 181.336 1.00 53.02  ? 2487 GLU A OE2   1 
ATOM   8094  N  N     . ARG A 1 2488 ? 183.827 222.328 186.070 1.00 45.41  ? 2488 ARG A N     1 
ATOM   8095  C  CA    . ARG A 1 2488 ? 184.552 221.384 186.960 1.00 40.48  ? 2488 ARG A CA    1 
ATOM   8096  C  C     . ARG A 1 2488 ? 183.692 220.130 187.174 1.00 34.19  ? 2488 ARG A C     1 
ATOM   8097  O  O     . ARG A 1 2488 ? 184.229 219.008 187.034 1.00 32.39  ? 2488 ARG A O     1 
ATOM   8098  C  CB    . ARG A 1 2488 ? 184.862 222.063 188.297 1.00 43.15  ? 2488 ARG A CB    1 
ATOM   8099  C  CG    . ARG A 1 2488 ? 185.732 223.304 188.160 1.00 43.70  ? 2488 ARG A CG    1 
ATOM   8100  C  CD    . ARG A 1 2488 ? 185.856 224.059 189.473 1.00 45.55  ? 2488 ARG A CD    1 
ATOM   8101  N  NE    . ARG A 1 2488 ? 184.570 224.592 189.935 1.00 46.72  ? 2488 ARG A NE    1 
ATOM   8102  C  CZ    . ARG A 1 2488 ? 184.408 225.290 191.052 1.00 53.11  ? 2488 ARG A CZ    1 
ATOM   8103  N  NH1   . ARG A 1 2488 ? 185.430 225.474 191.869 1.00 57.19  ? 2488 ARG A NH1   1 
ATOM   8104  N  NH2   . ARG A 1 2488 ? 183.228 225.802 191.351 1.00 52.83  ? 2488 ARG A NH2   1 
ATOM   8105  N  N     . TYR A 1 2489 ? 182.407 220.320 187.481 1.00 34.22  ? 2489 TYR A N     1 
ATOM   8106  C  CA    . TYR A 1 2489 ? 181.511 219.165 187.752 1.00 26.95  ? 2489 TYR A CA    1 
ATOM   8107  C  C     . TYR A 1 2489 ? 181.437 218.288 186.506 1.00 31.79  ? 2489 TYR A C     1 
ATOM   8108  O  O     . TYR A 1 2489 ? 181.621 217.060 186.624 1.00 28.67  ? 2489 TYR A O     1 
ATOM   8109  C  CB    . TYR A 1 2489 ? 180.121 219.650 188.174 1.00 25.04  ? 2489 TYR A CB    1 
ATOM   8110  C  CG    . TYR A 1 2489 ? 179.115 218.526 188.378 1.00 28.66  ? 2489 TYR A CG    1 
ATOM   8111  C  CD1   . TYR A 1 2489 ? 178.992 217.887 189.606 1.00 29.46  ? 2489 TYR A CD1   1 
ATOM   8112  C  CD2   . TYR A 1 2489 ? 178.295 218.101 187.340 1.00 29.36  ? 2489 TYR A CD2   1 
ATOM   8113  C  CE1   . TYR A 1 2489 ? 178.082 216.861 189.796 1.00 27.22  ? 2489 TYR A CE1   1 
ATOM   8114  C  CE2   . TYR A 1 2489 ? 177.381 217.076 187.518 1.00 29.33  ? 2489 TYR A CE2   1 
ATOM   8115  C  CZ    . TYR A 1 2489 ? 177.274 216.455 188.749 1.00 29.57  ? 2489 TYR A CZ    1 
ATOM   8116  O  OH    . TYR A 1 2489 ? 176.374 215.445 188.927 1.00 33.97  ? 2489 TYR A OH    1 
ATOM   8117  N  N     . ILE A 1 2490 ? 181.194 218.897 185.342 1.00 29.71  ? 2490 ILE A N     1 
ATOM   8118  C  CA    . ILE A 1 2490 ? 181.033 218.105 184.086 1.00 23.82  ? 2490 ILE A CA    1 
ATOM   8119  C  C     . ILE A 1 2490 ? 182.338 217.344 183.809 1.00 26.63  ? 2490 ILE A C     1 
ATOM   8120  O  O     . ILE A 1 2490 ? 182.261 216.134 183.505 1.00 29.84  ? 2490 ILE A O     1 
ATOM   8121  C  CB    . ILE A 1 2490 ? 180.642 219.017 182.909 1.00 30.31  ? 2490 ILE A CB    1 
ATOM   8122  C  CG1   . ILE A 1 2490 ? 179.307 219.715 183.159 1.00 31.79  ? 2490 ILE A CG1   1 
ATOM   8123  C  CG2   . ILE A 1 2490 ? 180.632 218.237 181.594 1.00 29.71  ? 2490 ILE A CG2   1 
ATOM   8124  C  CD1   . ILE A 1 2490 ? 178.163 218.767 183.469 1.00 27.77  ? 2490 ILE A CD1   1 
ATOM   8125  N  N     . GLN A 1 2491 ? 183.483 218.021 183.927 1.00 25.47  ? 2491 GLN A N     1 
ATOM   8126  C  CA    . GLN A 1 2491 ? 184.781 217.371 183.613 1.00 24.64  ? 2491 GLN A CA    1 
ATOM   8127  C  C     . GLN A 1 2491 ? 184.978 216.159 184.534 1.00 26.61  ? 2491 GLN A C     1 
ATOM   8128  O  O     . GLN A 1 2491 ? 185.249 215.055 184.013 1.00 28.78  ? 2491 GLN A O     1 
ATOM   8129  C  CB    . GLN A 1 2491 ? 185.933 218.359 183.785 1.00 30.92  ? 2491 GLN A CB    1 
ATOM   8130  C  CG    . GLN A 1 2491 ? 185.986 219.446 182.718 1.00 38.25  ? 2491 GLN A CG    1 
ATOM   8131  C  CD    . GLN A 1 2491 ? 187.236 220.292 182.804 1.00 40.74  ? 2491 GLN A CD    1 
ATOM   8132  O  OE1   . GLN A 1 2491 ? 187.179 221.513 182.987 1.00 41.86  ? 2491 GLN A OE1   1 
ATOM   8133  N  NE2   . GLN A 1 2491 ? 188.385 219.645 182.676 1.00 39.62  ? 2491 GLN A NE2   1 
ATOM   8134  N  N     . ARG A 1 2492 ? 184.837 216.361 185.847 1.00 28.56  ? 2492 ARG A N     1 
ATOM   8135  C  CA    . ARG A 1 2492 ? 185.033 215.251 186.814 1.00 24.74  ? 2492 ARG A CA    1 
ATOM   8136  C  C     . ARG A 1 2492 ? 183.946 214.194 186.578 1.00 20.58  ? 2492 ARG A C     1 
ATOM   8137  O  O     . ARG A 1 2492 ? 184.279 212.989 186.578 1.00 23.11  ? 2492 ARG A O     1 
ATOM   8138  C  CB    . ARG A 1 2492 ? 184.986 215.766 188.256 1.00 29.28  ? 2492 ARG A CB    1 
ATOM   8139  C  CG    . ARG A 1 2492 ? 186.184 216.608 188.667 1.00 32.05  ? 2492 ARG A CG    1 
ATOM   8140  C  CD    . ARG A 1 2492 ? 186.042 217.107 190.096 1.00 36.50  ? 2492 ARG A CD    1 
ATOM   8141  N  NE    . ARG A 1 2492 ? 187.258 217.776 190.571 1.00 36.94  ? 2492 ARG A NE    1 
ATOM   8142  C  CZ    . ARG A 1 2492 ? 187.799 218.850 190.012 1.00 42.82  ? 2492 ARG A CZ    1 
ATOM   8143  N  NH1   . ARG A 1 2492 ? 187.115 219.556 189.129 1.00 44.54  ? 2492 ARG A NH1   1 
ATOM   8144  N  NH2   . ARG A 1 2492 ? 189.023 219.220 190.344 1.00 47.28  ? 2492 ARG A NH2   1 
ATOM   8145  N  N     . TYR A 1 2493 ? 182.703 214.637 186.378 1.00 19.83  ? 2493 TYR A N     1 
ATOM   8146  C  CA    . TYR A 1 2493 ? 181.580 213.682 186.184 1.00 17.69  ? 2493 TYR A CA    1 
ATOM   8147  C  C     . TYR A 1 2493 ? 181.855 212.855 184.935 1.00 17.57  ? 2493 TYR A C     1 
ATOM   8148  O  O     . TYR A 1 2493 ? 181.587 211.637 184.946 1.00 19.92  ? 2493 TYR A O     1 
ATOM   8149  C  CB    . TYR A 1 2493 ? 180.226 214.388 186.072 1.00 17.70  ? 2493 TYR A CB    1 
ATOM   8150  C  CG    . TYR A 1 2493 ? 179.043 213.430 186.075 1.00 15.74  ? 2493 TYR A CG    1 
ATOM   8151  C  CD1   . TYR A 1 2493 ? 178.567 212.875 184.893 1.00 16.59  ? 2493 TYR A CD1   1 
ATOM   8152  C  CD2   . TYR A 1 2493 ? 178.412 213.074 187.259 1.00 14.19  ? 2493 TYR A CD2   1 
ATOM   8153  C  CE1   . TYR A 1 2493 ? 177.496 211.998 184.890 1.00 17.79  ? 2493 TYR A CE1   1 
ATOM   8154  C  CE2   . TYR A 1 2493 ? 177.338 212.199 187.269 1.00 15.90  ? 2493 TYR A CE2   1 
ATOM   8155  C  CZ    . TYR A 1 2493 ? 176.879 211.660 186.081 1.00 18.84  ? 2493 TYR A CZ    1 
ATOM   8156  O  OH    . TYR A 1 2493 ? 175.821 210.797 186.086 1.00 22.16  ? 2493 TYR A OH    1 
ATOM   8157  N  N     . LEU A 1 2494 ? 182.372 213.496 183.882 1.00 21.07  ? 2494 LEU A N     1 
ATOM   8158  C  CA    . LEU A 1 2494 ? 182.607 212.774 182.636 1.00 19.33  ? 2494 LEU A CA    1 
ATOM   8159  C  C     . LEU A 1 2494 ? 183.608 211.643 182.835 1.00 18.87  ? 2494 LEU A C     1 
ATOM   8160  O  O     . LEU A 1 2494 ? 183.380 210.520 182.373 1.00 19.90  ? 2494 LEU A O     1 
ATOM   8161  C  CB    . LEU A 1 2494 ? 183.093 213.737 181.554 1.00 21.25  ? 2494 LEU A CB    1 
ATOM   8162  C  CG    . LEU A 1 2494 ? 183.338 213.123 180.175 1.00 21.38  ? 2494 LEU A CG    1 
ATOM   8163  C  CD1   . LEU A 1 2494 ? 182.080 213.193 179.327 1.00 16.94  ? 2494 LEU A CD1   1 
ATOM   8164  C  CD2   . LEU A 1 2494 ? 184.498 213.816 179.483 1.00 24.69  ? 2494 LEU A CD2   1 
ATOM   8165  N  N     . VAL A 1 2495 ? 184.714 211.916 183.530 1.00 20.80  ? 2495 VAL A N     1 
ATOM   8166  C  CA    . VAL A 1 2495 ? 185.666 210.858 183.859 1.00 18.17  ? 2495 VAL A CA    1 
ATOM   8167  C  C     . VAL A 1 2495 ? 185.002 209.809 184.740 1.00 15.69  ? 2495 VAL A C     1 
ATOM   8168  O  O     . VAL A 1 2495 ? 185.200 208.602 184.557 1.00 16.67  ? 2495 VAL A O     1 
ATOM   8169  C  CB    . VAL A 1 2495 ? 186.918 211.454 184.530 1.00 20.39  ? 2495 VAL A CB    1 
ATOM   8170  C  CG1   . VAL A 1 2495 ? 187.870 210.351 184.960 1.00 19.07  ? 2495 VAL A CG1   1 
ATOM   8171  C  CG2   . VAL A 1 2495 ? 187.610 212.427 183.589 1.00 23.92  ? 2495 VAL A CG2   1 
ATOM   8172  N  N     . TYR A 1 2496 ? 184.202 210.257 185.710 1.00 15.47  ? 2496 TYR A N     1 
ATOM   8173  C  CA    . TYR A 1 2496 ? 183.441 209.332 186.543 1.00 16.19  ? 2496 TYR A CA    1 
ATOM   8174  C  C     . TYR A 1 2496 ? 182.464 208.516 185.706 1.00 15.07  ? 2496 TYR A C     1 
ATOM   8175  O  O     . TYR A 1 2496 ? 182.309 207.308 185.920 1.00 17.32  ? 2496 TYR A O     1 
ATOM   8176  C  CB    . TYR A 1 2496 ? 182.714 210.113 187.640 1.00 14.80  ? 2496 TYR A CB    1 
ATOM   8177  C  CG    . TYR A 1 2496 ? 181.530 209.412 188.271 1.00 15.22  ? 2496 TYR A CG    1 
ATOM   8178  C  CD1   . TYR A 1 2496 ? 180.244 209.599 187.780 1.00 17.55  ? 2496 TYR A CD1   1 
ATOM   8179  C  CD2   . TYR A 1 2496 ? 181.695 208.577 189.366 1.00 16.02  ? 2496 TYR A CD2   1 
ATOM   8180  C  CE1   . TYR A 1 2496 ? 179.160 208.966 188.357 1.00 16.56  ? 2496 TYR A CE1   1 
ATOM   8181  C  CE2   . TYR A 1 2496 ? 180.617 207.940 189.949 1.00 15.76  ? 2496 TYR A CE2   1 
ATOM   8182  C  CZ    . TYR A 1 2496 ? 179.353 208.138 189.440 1.00 17.98  ? 2496 TYR A CZ    1 
ATOM   8183  O  OH    . TYR A 1 2496 ? 178.277 207.505 190.019 1.00 18.98  ? 2496 TYR A OH    1 
ATOM   8184  N  N     . ALA A 1 2497 ? 181.793 209.160 184.748 1.00 16.51  ? 2497 ALA A N     1 
ATOM   8185  C  CA    . ALA A 1 2497 ? 180.851 208.442 183.897 1.00 15.63  ? 2497 ALA A CA    1 
ATOM   8186  C  C     . ALA A 1 2497 ? 181.564 207.467 182.967 1.00 13.50  ? 2497 ALA A C     1 
ATOM   8187  O  O     . ALA A 1 2497 ? 181.071 206.359 182.731 1.00 14.04  ? 2497 ALA A O     1 
ATOM   8188  C  CB    . ALA A 1 2497 ? 180.006 209.432 183.097 1.00 18.95  ? 2497 ALA A CB    1 
ATOM   8189  N  N     . ILE A 1 2498 ? 182.723 207.858 182.428 1.00 14.08  ? 2498 ILE A N     1 
ATOM   8190  C  CA    . ILE A 1 2498 ? 183.450 206.980 181.512 1.00 11.79  ? 2498 ILE A CA    1 
ATOM   8191  C  C     . ILE A 1 2498 ? 183.865 205.693 182.212 1.00 14.11  ? 2498 ILE A C     1 
ATOM   8192  O  O     . ILE A 1 2498 ? 183.725 204.597 181.656 1.00 16.29  ? 2498 ILE A O     1 
ATOM   8193  C  CB    . ILE A 1 2498 ? 184.663 207.712 180.905 1.00 13.71  ? 2498 ILE A CB    1 
ATOM   8194  C  CG1   . ILE A 1 2498 ? 184.203 208.824 179.960 1.00 16.03  ? 2498 ILE A CG1   1 
ATOM   8195  C  CG2   . ILE A 1 2498 ? 185.576 206.730 180.187 1.00 19.70  ? 2498 ILE A CG2   1 
ATOM   8196  C  CD1   . ILE A 1 2498 ? 185.228 209.203 178.913 1.00 24.84  ? 2498 ILE A CD1   1 
ATOM   8197  N  N     . LEU A 1 2499 ? 184.382 205.802 183.437 1.00 15.12  ? 2499 LEU A N     1 
ATOM   8198  C  CA    . LEU A 1 2499 ? 184.805 204.614 184.173 1.00 13.40  ? 2499 LEU A CA    1 
ATOM   8199  C  C     . LEU A 1 2499 ? 183.647 203.651 184.393 1.00 12.91  ? 2499 LEU A C     1 
ATOM   8200  O  O     . LEU A 1 2499 ? 183.757 202.453 184.108 1.00 17.30  ? 2499 LEU A O     1 
ATOM   8201  C  CB    . LEU A 1 2499 ? 185.417 205.013 185.514 1.00 15.40  ? 2499 LEU A CB    1 
ATOM   8202  C  CG    . LEU A 1 2499 ? 186.831 205.578 185.488 1.00 22.35  ? 2499 LEU A CG    1 
ATOM   8203  C  CD1   . LEU A 1 2499 ? 187.194 206.096 186.855 1.00 23.09  ? 2499 LEU A CD1   1 
ATOM   8204  C  CD2   . LEU A 1 2499 ? 187.790 204.487 185.068 1.00 23.94  ? 2499 LEU A CD2   1 
ATOM   8205  N  N     . TRP A 1 2500 ? 182.526 204.154 184.904 1.00 11.37  ? 2500 TRP A N     1 
ATOM   8206  C  CA    . TRP A 1 2500 ? 181.441 203.262 185.280 1.00 10.29  ? 2500 TRP A CA    1 
ATOM   8207  C  C     . TRP A 1 2500 ? 180.670 202.741 184.076 1.00 11.24  ? 2500 TRP A C     1 
ATOM   8208  O  O     . TRP A 1 2500 ? 180.136 201.630 184.137 1.00 14.32  ? 2500 TRP A O     1 
ATOM   8209  C  CB    . TRP A 1 2500 ? 180.477 203.967 186.233 1.00 11.28  ? 2500 TRP A CB    1 
ATOM   8210  C  CG    . TRP A 1 2500 ? 180.870 203.860 187.677 1.00 11.09  ? 2500 TRP A CG    1 
ATOM   8211  C  CD1   . TRP A 1 2500 ? 181.190 204.891 188.510 1.00 11.87  ? 2500 TRP A CD1   1 
ATOM   8212  C  CD2   . TRP A 1 2500 ? 181.059 202.660 188.439 1.00 12.75  ? 2500 TRP A CD2   1 
ATOM   8213  N  NE1   . TRP A 1 2500 ? 181.520 204.415 189.753 1.00 17.60  ? 2500 TRP A NE1   1 
ATOM   8214  C  CE2   . TRP A 1 2500 ? 181.453 203.047 189.735 1.00 19.01  ? 2500 TRP A CE2   1 
ATOM   8215  C  CE3   . TRP A 1 2500 ? 180.919 201.297 188.155 1.00 12.91  ? 2500 TRP A CE3   1 
ATOM   8216  C  CZ2   . TRP A 1 2500 ? 181.705 202.122 190.745 1.00 21.00  ? 2500 TRP A CZ2   1 
ATOM   8217  C  CZ3   . TRP A 1 2500 ? 181.164 200.383 189.161 1.00 18.34  ? 2500 TRP A CZ3   1 
ATOM   8218  C  CH2   . TRP A 1 2500 ? 181.556 200.799 190.439 1.00 22.97  ? 2500 TRP A CH2   1 
ATOM   8219  N  N     . SER A 1 2501 ? 180.599 203.512 182.993 1.00 12.16  ? 2501 SER A N     1 
ATOM   8220  C  CA    . SER A 1 2501 ? 179.940 203.074 181.771 1.00 8.84   ? 2501 SER A CA    1 
ATOM   8221  C  C     . SER A 1 2501 ? 180.783 202.115 180.947 1.00 12.04  ? 2501 SER A C     1 
ATOM   8222  O  O     . SER A 1 2501 ? 180.224 201.289 180.219 1.00 14.39  ? 2501 SER A O     1 
ATOM   8223  C  CB    . SER A 1 2501 ? 179.569 204.282 180.905 1.00 10.63  ? 2501 SER A CB    1 
ATOM   8224  O  OG    . SER A 1 2501 ? 178.778 205.205 181.633 1.00 13.28  ? 2501 SER A OG    1 
ATOM   8225  N  N     . LEU A 1 2502 ? 182.110 202.199 181.046 1.00 11.75  ? 2502 LEU A N     1 
ATOM   8226  C  CA    . LEU A 1 2502 ? 182.996 201.349 180.264 1.00 11.21  ? 2502 LEU A CA    1 
ATOM   8227  C  C     . LEU A 1 2502 ? 183.602 200.211 181.072 1.00 17.73  ? 2502 LEU A C     1 
ATOM   8228  O  O     . LEU A 1 2502 ? 184.120 199.259 180.478 1.00 29.34  ? 2502 LEU A O     1 
ATOM   8229  C  CB    . LEU A 1 2502 ? 184.127 202.180 179.642 1.00 16.78  ? 2502 LEU A CB    1 
ATOM   8230  C  CG    . LEU A 1 2502 ? 183.909 202.856 178.282 1.00 13.80  ? 2502 LEU A CG    1 
ATOM   8231  C  CD1   . LEU A 1 2502 ? 182.563 203.563 178.197 1.00 9.84   ? 2502 LEU A CD1   1 
ATOM   8232  C  CD2   . LEU A 1 2502 ? 185.040 203.825 177.978 1.00 12.74  ? 2502 LEU A CD2   1 
ATOM   8233  N  N     . SER A 1 2503 ? 183.551 200.280 182.406 1.00 18.32  ? 2503 SER A N     1 
ATOM   8234  C  CA    . SER A 1 2503 ? 184.113 199.216 183.229 1.00 13.48  ? 2503 SER A CA    1 
ATOM   8235  C  C     . SER A 1 2503 ? 183.146 198.750 184.312 1.00 16.81  ? 2503 SER A C     1 
ATOM   8236  O  O     . SER A 1 2503 ? 183.561 198.039 185.234 1.00 25.73  ? 2503 SER A O     1 
ATOM   8237  C  CB    . SER A 1 2503 ? 185.430 199.662 183.872 1.00 15.33  ? 2503 SER A CB    1 
ATOM   8238  O  OG    . SER A 1 2503 ? 185.233 200.785 184.711 1.00 21.92  ? 2503 SER A OG    1 
ATOM   8239  N  N     . GLY A 1 2504 ? 181.869 199.126 184.224 1.00 13.41  ? 2504 GLY A N     1 
ATOM   8240  C  CA    . GLY A 1 2504 ? 180.910 198.680 185.218 1.00 14.52  ? 2504 GLY A CA    1 
ATOM   8241  C  C     . GLY A 1 2504 ? 180.631 197.193 185.148 1.00 15.86  ? 2504 GLY A C     1 
ATOM   8242  O  O     . GLY A 1 2504 ? 180.257 196.580 186.152 1.00 16.94  ? 2504 GLY A O     1 
ATOM   8243  N  N     . ASP A 1 2505 ? 180.817 196.589 183.974 1.00 15.91  ? 2505 ASP A N     1 
ATOM   8244  C  CA    . ASP A 1 2505 ? 180.619 195.158 183.783 1.00 13.12  ? 2505 ASP A CA    1 
ATOM   8245  C  C     . ASP A 1 2505 ? 181.921 194.375 183.908 1.00 19.38  ? 2505 ASP A C     1 
ATOM   8246  O  O     . ASP A 1 2505 ? 182.064 193.304 183.310 1.00 25.02  ? 2505 ASP A O     1 
ATOM   8247  C  CB    . ASP A 1 2505 ? 179.962 194.888 182.428 1.00 13.96  ? 2505 ASP A CB    1 
ATOM   8248  C  CG    . ASP A 1 2505 ? 180.715 195.524 181.271 1.00 26.60  ? 2505 ASP A CG    1 
ATOM   8249  O  OD1   . ASP A 1 2505 ? 181.856 195.992 181.471 1.00 25.62  ? 2505 ASP A OD1   1 
ATOM   8250  O  OD2   . ASP A 1 2505 ? 180.163 195.551 180.151 1.00 34.61  ? 2505 ASP A OD2   1 
ATOM   8251  N  N     . SER A 1 2506 ? 182.873 194.891 184.680 1.00 16.62  ? 2506 SER A N     1 
ATOM   8252  C  CA    . SER A 1 2506 ? 184.180 194.276 184.843 1.00 19.67  ? 2506 SER A CA    1 
ATOM   8253  C  C     . SER A 1 2506 ? 184.494 194.146 186.326 1.00 23.22  ? 2506 SER A C     1 
ATOM   8254  O  O     . SER A 1 2506 ? 183.881 194.800 187.174 1.00 28.98  ? 2506 SER A O     1 
ATOM   8255  C  CB    . SER A 1 2506 ? 185.271 195.091 184.135 1.00 23.98  ? 2506 SER A CB    1 
ATOM   8256  O  OG    . SER A 1 2506 ? 184.779 195.673 182.942 1.00 21.28  ? 2506 SER A OG    1 
ATOM   8257  N  N     . ARG A 1 2507 ? 185.460 193.285 186.637 1.00 23.82  ? 2507 ARG A N     1 
ATOM   8258  C  CA    . ARG A 1 2507 ? 185.869 193.094 188.019 1.00 21.09  ? 2507 ARG A CA    1 
ATOM   8259  C  C     . ARG A 1 2507 ? 186.668 194.303 188.505 1.00 26.50  ? 2507 ARG A C     1 
ATOM   8260  O  O     . ARG A 1 2507 ? 186.893 195.275 187.778 1.00 26.78  ? 2507 ARG A O     1 
ATOM   8261  C  CB    . ARG A 1 2507 ? 186.671 191.803 188.166 1.00 20.84  ? 2507 ARG A CB    1 
ATOM   8262  C  CG    . ARG A 1 2507 ? 186.223 190.687 187.239 1.00 31.49  ? 2507 ARG A CG    1 
ATOM   8263  C  CD    . ARG A 1 2507 ? 187.097 189.453 187.385 1.00 41.40  ? 2507 ARG A CD    1 
ATOM   8264  N  NE    . ARG A 1 2507 ? 188.142 189.384 186.371 1.00 51.11  ? 2507 ARG A NE    1 
ATOM   8265  C  CZ    . ARG A 1 2507 ? 189.359 189.889 186.511 1.00 44.95  ? 2507 ARG A CZ    1 
ATOM   8266  N  NH1   . ARG A 1 2507 ? 189.724 190.519 187.616 1.00 38.60  ? 2507 ARG A NH1   1 
ATOM   8267  N  NH2   . ARG A 1 2507 ? 190.236 189.753 185.521 1.00 42.11  ? 2507 ARG A NH2   1 
ATOM   8268  N  N     . LEU A 1 2508 ? 187.099 194.234 189.766 1.00 27.66  ? 2508 LEU A N     1 
ATOM   8269  C  CA    . LEU A 1 2508 ? 187.777 195.369 190.386 1.00 26.85  ? 2508 LEU A CA    1 
ATOM   8270  C  C     . LEU A 1 2508 ? 189.111 195.662 189.710 1.00 27.42  ? 2508 LEU A C     1 
ATOM   8271  O  O     . LEU A 1 2508 ? 189.510 196.826 189.595 1.00 31.28  ? 2508 LEU A O     1 
ATOM   8272  C  CB    . LEU A 1 2508 ? 187.973 195.100 191.879 1.00 30.19  ? 2508 LEU A CB    1 
ATOM   8273  C  CG    . LEU A 1 2508 ? 188.873 196.038 192.688 1.00 33.43  ? 2508 LEU A CG    1 
ATOM   8274  C  CD1   . LEU A 1 2508 ? 188.435 197.488 192.533 1.00 35.70  ? 2508 LEU A CD1   1 
ATOM   8275  C  CD2   . LEU A 1 2508 ? 188.885 195.632 194.152 1.00 26.64  ? 2508 LEU A CD2   1 
ATOM   8276  N  N     . LYS A 1 2509 ? 189.816 194.622 189.258 1.00 27.19  ? 2509 LYS A N     1 
ATOM   8277  C  CA    . LYS A 1 2509 ? 191.138 194.829 188.674 1.00 30.61  ? 2509 LYS A CA    1 
ATOM   8278  C  C     . LYS A 1 2509 ? 191.063 195.656 187.397 1.00 34.57  ? 2509 LYS A C     1 
ATOM   8279  O  O     . LYS A 1 2509 ? 191.872 196.569 187.193 1.00 37.79  ? 2509 LYS A O     1 
ATOM   8280  C  CB    . LYS A 1 2509 ? 191.811 193.484 188.402 1.00 35.14  ? 2509 LYS A CB    1 
ATOM   8281  C  CG    . LYS A 1 2509 ? 193.316 193.586 188.200 1.00 41.68  ? 2509 LYS A CG    1 
ATOM   8282  C  CD    . LYS A 1 2509 ? 193.888 192.360 187.505 1.00 43.53  ? 2509 LYS A CD    1 
ATOM   8283  C  CE    . LYS A 1 2509 ? 192.991 191.883 186.376 1.00 43.66  ? 2509 LYS A CE    1 
ATOM   8284  N  NZ    . LYS A 1 2509 ? 193.101 190.412 186.175 1.00 40.75  ? 2509 LYS A NZ    1 
ATOM   8285  N  N     . MET A 1 2510 ? 190.097 195.359 186.524 1.00 32.81  ? 2510 MET A N     1 
ATOM   8286  C  CA    . MET A 1 2510 ? 189.986 196.109 185.277 1.00 26.14  ? 2510 MET A CA    1 
ATOM   8287  C  C     . MET A 1 2510 ? 189.364 197.484 185.485 1.00 27.26  ? 2510 MET A C     1 
ATOM   8288  O  O     . MET A 1 2510 ? 189.600 198.391 184.679 1.00 34.17  ? 2510 MET A O     1 
ATOM   8289  C  CB    . MET A 1 2510 ? 189.207 195.302 184.240 1.00 24.05  ? 2510 MET A CB    1 
ATOM   8290  C  CG    . MET A 1 2510 ? 189.564 193.828 184.246 1.00 29.95  ? 2510 MET A CG    1 
ATOM   8291  S  SD    . MET A 1 2510 ? 190.683 193.441 182.886 1.00 44.76  ? 2510 MET A SD    1 
ATOM   8292  C  CE    . MET A 1 2510 ? 190.731 191.656 182.968 1.00 36.17  ? 2510 MET A CE    1 
ATOM   8293  N  N     . ARG A 1 2511 ? 188.571 197.666 186.543 1.00 24.87  ? 2511 ARG A N     1 
ATOM   8294  C  CA    . ARG A 1 2511 ? 188.171 199.020 186.913 1.00 23.11  ? 2511 ARG A CA    1 
ATOM   8295  C  C     . ARG A 1 2511 ? 189.382 199.841 187.333 1.00 31.76  ? 2511 ARG A C     1 
ATOM   8296  O  O     . ARG A 1 2511 ? 189.470 201.036 187.027 1.00 36.54  ? 2511 ARG A O     1 
ATOM   8297  C  CB    . ARG A 1 2511 ? 187.126 198.993 188.028 1.00 23.07  ? 2511 ARG A CB    1 
ATOM   8298  C  CG    . ARG A 1 2511 ? 185.814 198.339 187.639 1.00 21.78  ? 2511 ARG A CG    1 
ATOM   8299  C  CD    . ARG A 1 2511 ? 184.877 198.237 188.829 1.00 23.97  ? 2511 ARG A CD    1 
ATOM   8300  N  NE    . ARG A 1 2511 ? 183.600 197.639 188.462 1.00 20.37  ? 2511 ARG A NE    1 
ATOM   8301  C  CZ    . ARG A 1 2511 ? 182.656 197.296 189.327 1.00 23.74  ? 2511 ARG A CZ    1 
ATOM   8302  N  NH1   . ARG A 1 2511 ? 182.810 197.481 190.628 1.00 22.47  ? 2511 ARG A NH1   1 
ATOM   8303  N  NH2   . ARG A 1 2511 ? 181.527 196.756 188.875 1.00 19.45  ? 2511 ARG A NH2   1 
ATOM   8304  N  N     . ALA A 1 2512 ? 190.323 199.216 188.043 1.00 32.61  ? 2512 ALA A N     1 
ATOM   8305  C  CA    . ALA A 1 2512 ? 191.592 199.875 188.328 1.00 31.29  ? 2512 ALA A CA    1 
ATOM   8306  C  C     . ALA A 1 2512 ? 192.386 200.108 187.048 1.00 30.15  ? 2512 ALA A C     1 
ATOM   8307  O  O     . ALA A 1 2512 ? 193.012 201.162 186.882 1.00 32.94  ? 2512 ALA A O     1 
ATOM   8308  C  CB    . ALA A 1 2512 ? 192.403 199.046 189.323 1.00 29.57  ? 2512 ALA A CB    1 
ATOM   8309  N  N     . GLU A 1 2513 ? 192.373 199.134 186.133 1.00 30.47  ? 2513 GLU A N     1 
ATOM   8310  C  CA    . GLU A 1 2513 ? 193.125 199.267 184.889 1.00 32.72  ? 2513 GLU A CA    1 
ATOM   8311  C  C     . GLU A 1 2513 ? 192.630 200.450 184.065 1.00 33.45  ? 2513 GLU A C     1 
ATOM   8312  O  O     . GLU A 1 2513 ? 193.430 201.234 183.542 1.00 35.62  ? 2513 GLU A O     1 
ATOM   8313  C  CB    . GLU A 1 2513 ? 193.030 197.975 184.075 1.00 29.87  ? 2513 GLU A CB    1 
ATOM   8314  C  CG    . GLU A 1 2513 ? 193.843 196.817 184.625 1.00 38.25  ? 2513 GLU A CG    1 
ATOM   8315  C  CD    . GLU A 1 2513 ? 193.920 195.654 183.655 1.00 49.34  ? 2513 GLU A CD    1 
ATOM   8316  O  OE1   . GLU A 1 2513 ? 193.910 195.900 182.431 1.00 51.07  ? 2513 GLU A OE1   1 
ATOM   8317  O  OE2   . GLU A 1 2513 ? 193.987 194.496 184.116 1.00 43.72  ? 2513 GLU A OE2   1 
ATOM   8318  N  N     . LEU A 1 2514 ? 191.309 200.589 183.932 1.00 29.73  ? 2514 LEU A N     1 
ATOM   8319  C  CA    . LEU A 1 2514 ? 190.761 201.699 183.160 1.00 30.03  ? 2514 LEU A CA    1 
ATOM   8320  C  C     . LEU A 1 2514 ? 191.071 203.036 183.819 1.00 31.28  ? 2514 LEU A C     1 
ATOM   8321  O  O     . LEU A 1 2514 ? 191.386 204.016 183.135 1.00 32.93  ? 2514 LEU A O     1 
ATOM   8322  C  CB    . LEU A 1 2514 ? 189.253 201.524 182.979 1.00 30.47  ? 2514 LEU A CB    1 
ATOM   8323  C  CG    . LEU A 1 2514 ? 188.581 202.519 182.030 1.00 27.44  ? 2514 LEU A CG    1 
ATOM   8324  C  CD1   . LEU A 1 2514 ? 189.159 202.399 180.631 1.00 28.27  ? 2514 LEU A CD1   1 
ATOM   8325  C  CD2   . LEU A 1 2514 ? 187.076 202.319 182.010 1.00 22.19  ? 2514 LEU A CD2   1 
ATOM   8326  N  N     . GLY A 1 2515 ? 190.987 203.097 185.150 1.00 31.09  ? 2515 GLY A N     1 
ATOM   8327  C  CA    . GLY A 1 2515 ? 191.320 204.329 185.845 1.00 33.06  ? 2515 GLY A CA    1 
ATOM   8328  C  C     . GLY A 1 2515 ? 192.774 204.723 185.673 1.00 34.15  ? 2515 GLY A C     1 
ATOM   8329  O  O     . GLY A 1 2515 ? 193.094 205.904 185.524 1.00 32.90  ? 2515 GLY A O     1 
ATOM   8330  N  N     . GLU A 1 2516 ? 193.674 203.738 185.699 1.00 35.73  ? 2516 GLU A N     1 
ATOM   8331  C  CA    . GLU A 1 2516 ? 195.088 204.021 185.479 1.00 33.14  ? 2516 GLU A CA    1 
ATOM   8332  C  C     . GLU A 1 2516 ? 195.333 204.553 184.072 1.00 36.35  ? 2516 GLU A C     1 
ATOM   8333  O  O     . GLU A 1 2516 ? 196.108 205.499 183.884 1.00 38.96  ? 2516 GLU A O     1 
ATOM   8334  C  CB    . GLU A 1 2516 ? 195.917 202.762 185.731 1.00 33.46  ? 2516 GLU A CB    1 
ATOM   8335  C  CG    . GLU A 1 2516 ? 195.981 202.345 187.191 1.00 37.77  ? 2516 GLU A CG    1 
ATOM   8336  C  CD    . GLU A 1 2516 ? 196.129 200.846 187.364 1.00 43.69  ? 2516 GLU A CD    1 
ATOM   8337  O  OE1   . GLU A 1 2516 ? 196.367 200.150 186.355 1.00 41.82  ? 2516 GLU A OE1   1 
ATOM   8338  O  OE2   . GLU A 1 2516 ? 196.004 200.364 188.509 1.00 36.11  ? 2516 GLU A OE2   1 
ATOM   8339  N  N     . TYR A 1 2517 ? 194.681 203.958 183.069 1.00 37.50  ? 2517 TYR A N     1 
ATOM   8340  C  CA    . TYR A 1 2517 ? 194.889 204.398 181.693 1.00 32.67  ? 2517 TYR A CA    1 
ATOM   8341  C  C     . TYR A 1 2517 ? 194.294 205.781 181.456 1.00 32.83  ? 2517 TYR A C     1 
ATOM   8342  O  O     . TYR A 1 2517 ? 194.880 206.601 180.740 1.00 41.00  ? 2517 TYR A O     1 
ATOM   8343  C  CB    . TYR A 1 2517 ? 194.296 203.382 180.717 1.00 31.49  ? 2517 TYR A CB    1 
ATOM   8344  C  CG    . TYR A 1 2517 ? 194.510 203.741 179.264 1.00 36.31  ? 2517 TYR A CG    1 
ATOM   8345  C  CD1   . TYR A 1 2517 ? 195.714 203.463 178.632 1.00 39.60  ? 2517 TYR A CD1   1 
ATOM   8346  C  CD2   . TYR A 1 2517 ? 193.510 204.356 178.524 1.00 37.75  ? 2517 TYR A CD2   1 
ATOM   8347  C  CE1   . TYR A 1 2517 ? 195.916 203.791 177.304 1.00 43.67  ? 2517 TYR A CE1   1 
ATOM   8348  C  CE2   . TYR A 1 2517 ? 193.704 204.685 177.196 1.00 34.66  ? 2517 TYR A CE2   1 
ATOM   8349  C  CZ    . TYR A 1 2517 ? 194.907 204.402 176.592 1.00 41.05  ? 2517 TYR A CZ    1 
ATOM   8350  O  OH    . TYR A 1 2517 ? 195.101 204.729 175.270 1.00 43.57  ? 2517 TYR A OH    1 
ATOM   8351  N  N     . ILE A 1 2518 ? 193.125 206.058 182.041 1.00 29.70  ? 2518 ILE A N     1 
ATOM   8352  C  CA    . ILE A 1 2518 ? 192.524 207.382 181.898 1.00 29.94  ? 2518 ILE A CA    1 
ATOM   8353  C  C     . ILE A 1 2518 ? 193.408 208.439 182.545 1.00 34.04  ? 2518 ILE A C     1 
ATOM   8354  O  O     . ILE A 1 2518 ? 193.581 209.538 182.005 1.00 41.70  ? 2518 ILE A O     1 
ATOM   8355  C  CB    . ILE A 1 2518 ? 191.096 207.395 182.476 1.00 31.02  ? 2518 ILE A CB    1 
ATOM   8356  C  CG1   . ILE A 1 2518 ? 190.168 206.542 181.610 1.00 33.74  ? 2518 ILE A CG1   1 
ATOM   8357  C  CG2   . ILE A 1 2518 ? 190.565 208.815 182.579 1.00 30.66  ? 2518 ILE A CG2   1 
ATOM   8358  C  CD1   . ILE A 1 2518 ? 188.792 206.354 182.195 1.00 30.24  ? 2518 ILE A CD1   1 
ATOM   8359  N  N     . ARG A 1 2519 ? 193.993 208.121 183.703 1.00 35.74  ? 2519 ARG A N     1 
ATOM   8360  C  CA    . ARG A 1 2519 ? 194.933 209.041 184.337 1.00 36.98  ? 2519 ARG A CA    1 
ATOM   8361  C  C     . ARG A 1 2519 ? 196.118 209.334 183.426 1.00 36.61  ? 2519 ARG A C     1 
ATOM   8362  O  O     . ARG A 1 2519 ? 196.732 210.404 183.514 1.00 37.96  ? 2519 ARG A O     1 
ATOM   8363  C  CB    . ARG A 1 2519 ? 195.414 208.460 185.667 1.00 37.16  ? 2519 ARG A CB    1 
ATOM   8364  C  CG    . ARG A 1 2519 ? 196.025 209.479 186.613 1.00 37.79  ? 2519 ARG A CG    1 
ATOM   8365  C  CD    . ARG A 1 2519 ? 196.585 208.805 187.856 1.00 36.34  ? 2519 ARG A CD    1 
ATOM   8366  N  NE    . ARG A 1 2519 ? 195.605 208.732 188.932 1.00 42.89  ? 2519 ARG A NE    1 
ATOM   8367  C  CZ    . ARG A 1 2519 ? 195.277 209.748 189.719 1.00 44.72  ? 2519 ARG A CZ    1 
ATOM   8368  N  NH1   . ARG A 1 2519 ? 195.839 210.937 189.583 1.00 42.97  ? 2519 ARG A NH1   1 
ATOM   8369  N  NH2   . ARG A 1 2519 ? 194.365 209.564 190.669 1.00 44.19  ? 2519 ARG A NH2   1 
ATOM   8370  N  N     . ARG A 1 2520 ? 196.454 208.394 182.542 1.00 37.93  ? 2520 ARG A N     1 
ATOM   8371  C  CA    . ARG A 1 2520 ? 197.596 208.582 181.655 1.00 40.34  ? 2520 ARG A CA    1 
ATOM   8372  C  C     . ARG A 1 2520 ? 197.270 209.533 180.509 1.00 40.78  ? 2520 ARG A C     1 
ATOM   8373  O  O     . ARG A 1 2520 ? 198.165 210.201 179.978 1.00 41.51  ? 2520 ARG A O     1 
ATOM   8374  C  CB    . ARG A 1 2520 ? 198.058 207.230 181.112 1.00 37.94  ? 2520 ARG A CB    1 
ATOM   8375  C  CG    . ARG A 1 2520 ? 199.523 206.926 181.358 1.00 44.74  ? 2520 ARG A CG    1 
ATOM   8376  C  CD    . ARG A 1 2520 ? 199.929 205.624 180.690 1.00 49.28  ? 2520 ARG A CD    1 
ATOM   8377  N  NE    . ARG A 1 2520 ? 198.934 204.577 180.888 1.00 47.08  ? 2520 ARG A NE    1 
ATOM   8378  C  CZ    . ARG A 1 2520 ? 198.926 203.738 181.915 1.00 48.22  ? 2520 ARG A CZ    1 
ATOM   8379  N  NH1   . ARG A 1 2520 ? 199.844 203.801 182.865 1.00 50.95  ? 2520 ARG A NH1   1 
ATOM   8380  N  NH2   . ARG A 1 2520 ? 197.973 202.813 181.990 1.00 42.67  ? 2520 ARG A NH2   1 
ATOM   8381  N  N     . ILE A 1 2521 ? 195.998 209.610 180.108 1.00 39.65  ? 2521 ILE A N     1 
ATOM   8382  C  CA    . ILE A 1 2521 ? 195.625 210.324 178.892 1.00 40.25  ? 2521 ILE A CA    1 
ATOM   8383  C  C     . ILE A 1 2521 ? 194.922 211.645 179.167 1.00 39.19  ? 2521 ILE A C     1 
ATOM   8384  O  O     . ILE A 1 2521 ? 195.003 212.560 178.337 1.00 42.11  ? 2521 ILE A O     1 
ATOM   8385  C  CB    . ILE A 1 2521 ? 194.731 209.452 177.988 1.00 37.63  ? 2521 ILE A CB    1 
ATOM   8386  C  CG1   . ILE A 1 2521 ? 193.460 209.045 178.739 1.00 39.76  ? 2521 ILE A CG1   1 
ATOM   8387  C  CG2   . ILE A 1 2521 ? 195.499 208.232 177.498 1.00 39.21  ? 2521 ILE A CG2   1 
ATOM   8388  C  CD1   . ILE A 1 2521 ? 192.761 207.836 178.176 1.00 39.95  ? 2521 ILE A CD1   1 
ATOM   8389  N  N     . THR A 1 2522 ? 194.237 211.778 180.296 1.00 37.35  ? 2522 THR A N     1 
ATOM   8390  C  CA    . THR A 1 2522 ? 193.332 212.896 180.507 1.00 40.63  ? 2522 THR A CA    1 
ATOM   8391  C  C     . THR A 1 2522 ? 194.066 214.112 181.059 1.00 41.48  ? 2522 THR A C     1 
ATOM   8392  O  O     . THR A 1 2522 ? 195.128 214.008 181.679 1.00 42.12  ? 2522 THR A O     1 
ATOM   8393  C  CB    . THR A 1 2522 ? 192.191 212.508 181.454 1.00 40.37  ? 2522 THR A CB    1 
ATOM   8394  O  OG1   . THR A 1 2522 ? 191.153 213.492 181.376 1.00 38.55  ? 2522 THR A OG1   1 
ATOM   8395  C  CG2   . THR A 1 2522 ? 192.686 212.431 182.891 1.00 42.82  ? 2522 THR A CG2   1 
ATOM   8396  N  N     . THR A 1 2523 ? 193.484 215.282 180.802 1.00 40.22  ? 2523 THR A N     1 
ATOM   8397  C  CA    . THR A 1 2523 ? 193.931 216.537 181.385 1.00 45.23  ? 2523 THR A CA    1 
ATOM   8398  C  C     . THR A 1 2523 ? 193.027 217.004 182.516 1.00 44.95  ? 2523 THR A C     1 
ATOM   8399  O  O     . THR A 1 2523 ? 193.349 217.992 183.185 1.00 46.95  ? 2523 THR A O     1 
ATOM   8400  C  CB    . THR A 1 2523 ? 194.020 217.623 180.304 1.00 52.41  ? 2523 THR A CB    1 
ATOM   8401  O  OG1   . THR A 1 2523 ? 194.981 218.613 180.692 1.00 50.50  ? 2523 THR A OG1   1 
ATOM   8402  C  CG2   . THR A 1 2523 ? 192.663 218.284 180.085 1.00 42.87  ? 2523 THR A CG2   1 
ATOM   8403  N  N     . VAL A 1 2524 ? 191.913 216.320 182.747 1.00 42.33  ? 2524 VAL A N     1 
ATOM   8404  C  CA    . VAL A 1 2524 ? 191.003 216.676 183.842 1.00 44.56  ? 2524 VAL A CA    1 
ATOM   8405  C  C     . VAL A 1 2524 ? 191.700 216.430 185.173 1.00 44.62  ? 2524 VAL A C     1 
ATOM   8406  O  O     . VAL A 1 2524 ? 192.405 215.414 185.318 1.00 44.37  ? 2524 VAL A O     1 
ATOM   8407  C  CB    . VAL A 1 2524 ? 189.709 215.865 183.737 1.00 38.92  ? 2524 VAL A CB    1 
ATOM   8408  C  CG1   . VAL A 1 2524 ? 188.671 216.379 184.720 1.00 36.96  ? 2524 VAL A CG1   1 
ATOM   8409  C  CG2   . VAL A 1 2524 ? 189.168 215.914 182.317 1.00 34.43  ? 2524 VAL A CG2   1 
ATOM   8410  N  N     . PRO A 1 2525 ? 191.562 217.321 186.155 1.00 44.04  ? 2525 PRO A N     1 
ATOM   8411  C  CA    . PRO A 1 2525 ? 192.131 217.046 187.479 1.00 43.00  ? 2525 PRO A CA    1 
ATOM   8412  C  C     . PRO A 1 2525 ? 191.547 215.773 188.073 1.00 44.89  ? 2525 PRO A C     1 
ATOM   8413  O  O     . PRO A 1 2525 ? 190.356 215.488 187.934 1.00 47.35  ? 2525 PRO A O     1 
ATOM   8414  C  CB    . PRO A 1 2525 ? 191.742 218.282 188.296 1.00 45.83  ? 2525 PRO A CB    1 
ATOM   8415  C  CG    . PRO A 1 2525 ? 191.563 219.360 187.284 1.00 43.95  ? 2525 PRO A CG    1 
ATOM   8416  C  CD    . PRO A 1 2525 ? 191.023 218.688 186.055 1.00 43.48  ? 2525 PRO A CD    1 
ATOM   8417  N  N     . LEU A 1 2526 ? 192.399 215.011 188.741 1.00 42.88  ? 2526 LEU A N     1 
ATOM   8418  C  CA    . LEU A 1 2526 ? 192.066 213.699 189.269 1.00 39.65  ? 2526 LEU A CA    1 
ATOM   8419  C  C     . LEU A 1 2526 ? 192.482 213.619 190.727 1.00 44.27  ? 2526 LEU A C     1 
ATOM   8420  O  O     . LEU A 1 2526 ? 193.356 214.370 191.173 1.00 44.95  ? 2526 LEU A O     1 
ATOM   8421  C  CB    . LEU A 1 2526 ? 192.763 212.597 188.457 1.00 35.41  ? 2526 LEU A CB    1 
ATOM   8422  C  CG    . LEU A 1 2526 ? 192.160 212.330 187.076 1.00 37.65  ? 2526 LEU A CG    1 
ATOM   8423  C  CD1   . LEU A 1 2526 ? 192.732 211.064 186.471 1.00 37.09  ? 2526 LEU A CD1   1 
ATOM   8424  C  CD2   . LEU A 1 2526 ? 190.643 212.246 187.155 1.00 38.75  ? 2526 LEU A CD2   1 
ATOM   8425  N  N     . PRO A 1 2527 ? 191.858 212.733 191.506 1.00 46.81  ? 2527 PRO A N     1 
ATOM   8426  C  CA    . PRO A 1 2527 ? 192.267 212.573 192.906 1.00 47.58  ? 2527 PRO A CA    1 
ATOM   8427  C  C     . PRO A 1 2527 ? 193.736 212.188 193.012 1.00 55.53  ? 2527 PRO A C     1 
ATOM   8428  O  O     . PRO A 1 2527 ? 194.247 211.383 192.231 1.00 53.18  ? 2527 PRO A O     1 
ATOM   8429  C  CB    . PRO A 1 2527 ? 191.351 211.456 193.419 1.00 43.04  ? 2527 PRO A CB    1 
ATOM   8430  C  CG    . PRO A 1 2527 ? 190.156 211.516 192.529 1.00 36.87  ? 2527 PRO A CG    1 
ATOM   8431  C  CD    . PRO A 1 2527 ? 190.676 211.915 191.180 1.00 41.05  ? 2527 PRO A CD    1 
ATOM   8432  N  N     . THR A 1 2528 ? 194.412 212.774 194.000 1.00 57.94  ? 2528 THR A N     1 
ATOM   8433  C  CA    . THR A 1 2528 ? 195.851 212.631 194.166 1.00 55.77  ? 2528 THR A CA    1 
ATOM   8434  C  C     . THR A 1 2528 ? 196.221 211.545 195.171 1.00 62.47  ? 2528 THR A C     1 
ATOM   8435  O  O     . THR A 1 2528 ? 197.336 211.558 195.703 1.00 63.90  ? 2528 THR A O     1 
ATOM   8436  C  CB    . THR A 1 2528 ? 196.466 213.966 194.585 1.00 60.58  ? 2528 THR A CB    1 
ATOM   8437  O  OG1   . THR A 1 2528 ? 195.846 214.420 195.795 1.00 65.28  ? 2528 THR A OG1   1 
ATOM   8438  C  CG2   . THR A 1 2528 ? 196.261 215.009 193.497 1.00 52.34  ? 2528 THR A CG2   1 
ATOM   8439  N  N     . ALA A 1 2529 ? 195.312 210.618 195.445 1.00 68.19  ? 2529 ALA A N     1 
ATOM   8440  C  CA    . ALA A 1 2529 ? 195.616 209.523 196.354 1.00 66.43  ? 2529 ALA A CA    1 
ATOM   8441  C  C     . ALA A 1 2529 ? 196.704 208.639 195.751 1.00 73.31  ? 2529 ALA A C     1 
ATOM   8442  O  O     . ALA A 1 2529 ? 196.630 208.298 194.562 1.00 74.05  ? 2529 ALA A O     1 
ATOM   8443  C  CB    . ALA A 1 2529 ? 194.362 208.700 196.640 1.00 62.05  ? 2529 ALA A CB    1 
ATOM   8444  N  N     . PRO A 1 2530 ? 197.728 208.261 196.522 1.00 77.02  ? 2530 PRO A N     1 
ATOM   8445  C  CA    . PRO A 1 2530 ? 198.820 207.458 195.946 1.00 77.45  ? 2530 PRO A CA    1 
ATOM   8446  C  C     . PRO A 1 2530 ? 198.382 206.106 195.409 1.00 78.20  ? 2530 PRO A C     1 
ATOM   8447  O  O     . PRO A 1 2530 ? 198.931 205.649 194.398 1.00 79.16  ? 2530 PRO A O     1 
ATOM   8448  C  CB    . PRO A 1 2530 ? 199.798 207.308 197.120 1.00 78.10  ? 2530 PRO A CB    1 
ATOM   8449  C  CG    . PRO A 1 2530 ? 198.969 207.530 198.343 1.00 77.79  ? 2530 PRO A CG    1 
ATOM   8450  C  CD    . PRO A 1 2530 ? 197.935 208.540 197.952 1.00 74.51  ? 2530 PRO A CD    1 
ATOM   8451  N  N     . ASN A 1 2531 ? 197.412 205.449 196.046 1.00 71.42  ? 2531 ASN A N     1 
ATOM   8452  C  CA    . ASN A 1 2531 ? 197.031 204.093 195.666 1.00 69.27  ? 2531 ASN A CA    1 
ATOM   8453  C  C     . ASN A 1 2531 ? 195.535 203.872 195.508 1.00 67.77  ? 2531 ASN A C     1 
ATOM   8454  O  O     . ASN A 1 2531 ? 195.149 202.872 194.891 1.00 65.07  ? 2531 ASN A O     1 
ATOM   8455  C  CB    . ASN A 1 2531 ? 197.568 203.080 196.689 1.00 70.58  ? 2531 ASN A CB    1 
ATOM   8456  C  CG    . ASN A 1 2531 ? 198.987 202.642 196.385 1.00 80.09  ? 2531 ASN A CG    1 
ATOM   8457  O  OD1   . ASN A 1 2531 ? 199.543 202.980 195.340 1.00 80.17  ? 2531 ASN A OD1   1 
ATOM   8458  N  ND2   . ASN A 1 2531 ? 199.581 201.885 197.300 1.00 77.76  ? 2531 ASN A ND2   1 
ATOM   8459  N  N     . ILE A 1 2532 ? 194.688 204.744 196.036 1.00 66.97  ? 2532 ILE A N     1 
ATOM   8460  C  CA    . ILE A 1 2532 ? 193.239 204.536 195.923 1.00 53.60  ? 2532 ILE A CA    1 
ATOM   8461  C  C     . ILE A 1 2532 ? 192.812 204.758 194.476 1.00 47.36  ? 2532 ILE A C     1 
ATOM   8462  O  O     . ILE A 1 2532 ? 193.105 205.823 193.903 1.00 50.30  ? 2532 ILE A O     1 
ATOM   8463  C  CB    . ILE A 1 2532 ? 192.486 205.472 196.872 1.00 53.09  ? 2532 ILE A CB    1 
ATOM   8464  C  CG1   . ILE A 1 2532 ? 192.783 205.123 198.334 1.00 51.09  ? 2532 ILE A CG1   1 
ATOM   8465  C  CG2   . ILE A 1 2532 ? 190.991 205.403 196.609 1.00 49.21  ? 2532 ILE A CG2   1 
ATOM   8466  C  CD1   . ILE A 1 2532 ? 193.947 205.884 198.938 1.00 55.55  ? 2532 ILE A CD1   1 
ATOM   8467  N  N     . PRO A 1 2533 ? 192.134 203.802 193.846 1.00 43.22  ? 2533 PRO A N     1 
ATOM   8468  C  CA    . PRO A 1 2533 ? 191.706 203.992 192.457 1.00 43.45  ? 2533 PRO A CA    1 
ATOM   8469  C  C     . PRO A 1 2533 ? 190.631 205.061 192.341 1.00 40.22  ? 2533 PRO A C     1 
ATOM   8470  O  O     . PRO A 1 2533 ? 189.925 205.388 193.297 1.00 38.62  ? 2533 PRO A O     1 
ATOM   8471  C  CB    . PRO A 1 2533 ? 191.167 202.615 192.057 1.00 38.02  ? 2533 PRO A CB    1 
ATOM   8472  C  CG    . PRO A 1 2533 ? 190.769 201.981 193.343 1.00 39.23  ? 2533 PRO A CG    1 
ATOM   8473  C  CD    . PRO A 1 2533 ? 191.734 202.488 194.377 1.00 42.76  ? 2533 PRO A CD    1 
ATOM   8474  N  N     . ILE A 1 2534 ? 190.524 205.615 191.131 1.00 34.15  ? 2534 ILE A N     1 
ATOM   8475  C  CA    . ILE A 1 2534 ? 189.574 206.694 190.881 1.00 31.91  ? 2534 ILE A CA    1 
ATOM   8476  C  C     . ILE A 1 2534 ? 188.142 206.197 191.050 1.00 27.84  ? 2534 ILE A C     1 
ATOM   8477  O  O     . ILE A 1 2534 ? 187.251 206.965 191.434 1.00 28.11  ? 2534 ILE A O     1 
ATOM   8478  C  CB    . ILE A 1 2534 ? 189.817 207.285 189.480 1.00 31.04  ? 2534 ILE A CB    1 
ATOM   8479  C  CG1   . ILE A 1 2534 ? 191.161 208.007 189.442 1.00 34.10  ? 2534 ILE A CG1   1 
ATOM   8480  C  CG2   . ILE A 1 2534 ? 188.735 208.286 189.117 1.00 30.66  ? 2534 ILE A CG2   1 
ATOM   8481  C  CD1   . ILE A 1 2534 ? 191.814 207.992 188.082 1.00 35.33  ? 2534 ILE A CD1   1 
ATOM   8482  N  N     . ILE A 1 2535 ? 187.901 204.908 190.796 1.00 25.51  ? 2535 ILE A N     1 
ATOM   8483  C  CA    . ILE A 1 2535 ? 186.561 204.347 190.924 1.00 25.02  ? 2535 ILE A CA    1 
ATOM   8484  C  C     . ILE A 1 2535 ? 186.038 204.428 192.353 1.00 27.75  ? 2535 ILE A C     1 
ATOM   8485  O  O     . ILE A 1 2535 ? 184.832 204.269 192.577 1.00 27.89  ? 2535 ILE A O     1 
ATOM   8486  C  CB    . ILE A 1 2535 ? 186.545 202.891 190.419 1.00 25.49  ? 2535 ILE A CB    1 
ATOM   8487  C  CG1   . ILE A 1 2535 ? 185.146 202.503 189.935 1.00 25.96  ? 2535 ILE A CG1   1 
ATOM   8488  C  CG2   . ILE A 1 2535 ? 187.023 201.937 191.504 1.00 27.03  ? 2535 ILE A CG2   1 
ATOM   8489  C  CD1   . ILE A 1 2535 ? 184.748 203.155 188.632 1.00 20.58  ? 2535 ILE A CD1   1 
ATOM   8490  N  N     . ASP A 1 2536 ? 186.908 204.681 193.328 1.00 28.95  ? 2536 ASP A N     1 
ATOM   8491  C  CA    . ASP A 1 2536 ? 186.506 204.831 194.718 1.00 27.91  ? 2536 ASP A CA    1 
ATOM   8492  C  C     . ASP A 1 2536 ? 186.129 206.265 195.067 1.00 27.58  ? 2536 ASP A C     1 
ATOM   8493  O  O     . ASP A 1 2536 ? 185.900 206.565 196.242 1.00 34.91  ? 2536 ASP A O     1 
ATOM   8494  C  CB    . ASP A 1 2536 ? 187.623 204.350 195.646 1.00 32.98  ? 2536 ASP A CB    1 
ATOM   8495  C  CG    . ASP A 1 2536 ? 187.824 202.849 195.587 1.00 39.59  ? 2536 ASP A CG    1 
ATOM   8496  O  OD1   . ASP A 1 2536 ? 188.888 202.373 196.036 1.00 42.63  ? 2536 ASP A OD1   1 
ATOM   8497  O  OD2   . ASP A 1 2536 ? 186.922 202.145 195.087 1.00 39.82  ? 2536 ASP A OD2   1 
ATOM   8498  N  N     . TYR A 1 2537 ? 186.067 207.153 194.078 1.00 22.17  ? 2537 TYR A N     1 
ATOM   8499  C  CA    . TYR A 1 2537 ? 185.711 208.549 194.281 1.00 23.71  ? 2537 TYR A CA    1 
ATOM   8500  C  C     . TYR A 1 2537 ? 184.443 208.877 193.508 1.00 25.79  ? 2537 TYR A C     1 
ATOM   8501  O  O     . TYR A 1 2537 ? 184.213 208.345 192.418 1.00 31.45  ? 2537 TYR A O     1 
ATOM   8502  C  CB    . TYR A 1 2537 ? 186.835 209.485 193.825 1.00 28.82  ? 2537 TYR A CB    1 
ATOM   8503  C  CG    . TYR A 1 2537 ? 188.020 209.550 194.756 1.00 29.70  ? 2537 TYR A CG    1 
ATOM   8504  C  CD1   . TYR A 1 2537 ? 189.025 208.597 194.698 1.00 29.86  ? 2537 TYR A CD1   1 
ATOM   8505  C  CD2   . TYR A 1 2537 ? 188.140 210.572 195.686 1.00 30.85  ? 2537 TYR A CD2   1 
ATOM   8506  C  CE1   . TYR A 1 2537 ? 190.113 208.656 195.545 1.00 36.57  ? 2537 TYR A CE1   1 
ATOM   8507  C  CE2   . TYR A 1 2537 ? 189.223 210.639 196.538 1.00 32.35  ? 2537 TYR A CE2   1 
ATOM   8508  C  CZ    . TYR A 1 2537 ? 190.207 209.678 196.463 1.00 40.28  ? 2537 TYR A CZ    1 
ATOM   8509  O  OH    . TYR A 1 2537 ? 191.289 209.741 197.309 1.00 54.54  ? 2537 TYR A OH    1 
ATOM   8510  N  N     . GLU A 1 2538 ? 183.625 209.753 194.078 1.00 25.51  ? 2538 GLU A N     1 
ATOM   8511  C  CA    . GLU A 1 2538 ? 182.474 210.318 193.394 1.00 20.10  ? 2538 GLU A CA    1 
ATOM   8512  C  C     . GLU A 1 2538 ? 182.723 211.791 193.104 1.00 26.35  ? 2538 GLU A C     1 
ATOM   8513  O  O     . GLU A 1 2538 ? 183.693 212.390 193.576 1.00 31.21  ? 2538 GLU A O     1 
ATOM   8514  C  CB    . GLU A 1 2538 ? 181.198 210.149 194.225 1.00 25.23  ? 2538 GLU A CB    1 
ATOM   8515  C  CG    . GLU A 1 2538 ? 181.116 211.066 195.429 1.00 26.77  ? 2538 GLU A CG    1 
ATOM   8516  C  CD    . GLU A 1 2538 ? 179.701 211.532 195.709 1.00 33.41  ? 2538 GLU A CD    1 
ATOM   8517  O  OE1   . GLU A 1 2538 ? 178.752 210.819 195.323 1.00 32.66  ? 2538 GLU A OE1   1 
ATOM   8518  O  OE2   . GLU A 1 2538 ? 179.539 212.614 196.311 1.00 38.51  ? 2538 GLU A OE2   1 
ATOM   8519  N  N     . VAL A 1 2539 ? 181.830 212.376 192.315 1.00 26.16  ? 2539 VAL A N     1 
ATOM   8520  C  CA    . VAL A 1 2539 ? 181.897 213.787 191.960 1.00 21.52  ? 2539 VAL A CA    1 
ATOM   8521  C  C     . VAL A 1 2539 ? 180.796 214.505 192.725 1.00 23.22  ? 2539 VAL A C     1 
ATOM   8522  O  O     . VAL A 1 2539 ? 179.605 214.297 192.462 1.00 29.57  ? 2539 VAL A O     1 
ATOM   8523  C  CB    . VAL A 1 2539 ? 181.760 214.006 190.449 1.00 23.04  ? 2539 VAL A CB    1 
ATOM   8524  C  CG1   . VAL A 1 2539 ? 182.035 215.457 190.099 1.00 24.42  ? 2539 VAL A CG1   1 
ATOM   8525  C  CG2   . VAL A 1 2539 ? 182.709 213.090 189.701 1.00 23.00  ? 2539 VAL A CG2   1 
ATOM   8526  N  N     . SER A 1 2540 ? 181.198 215.391 193.640 1.00 26.97  ? 2540 SER A N     1 
ATOM   8527  C  CA    . SER A 1 2540 ? 180.202 216.213 194.372 1.00 28.62  ? 2540 SER A CA    1 
ATOM   8528  C  C     . SER A 1 2540 ? 179.754 217.368 193.465 1.00 32.56  ? 2540 SER A C     1 
ATOM   8529  O  O     . SER A 1 2540 ? 180.539 217.754 192.571 1.00 35.09  ? 2540 SER A O     1 
ATOM   8530  C  CB    . SER A 1 2540 ? 180.777 216.727 195.662 1.00 30.73  ? 2540 SER A CB    1 
ATOM   8531  O  OG    . SER A 1 2540 ? 181.943 217.502 195.420 1.00 31.60  ? 2540 SER A OG    1 
ATOM   8532  N  N     . ILE A 1 2541 ? 178.539 217.882 193.680 1.00 34.39  ? 2541 ILE A N     1 
ATOM   8533  C  CA    . ILE A 1 2541 ? 178.003 218.999 192.845 1.00 33.67  ? 2541 ILE A CA    1 
ATOM   8534  C  C     . ILE A 1 2541 ? 178.922 220.218 193.018 1.00 38.95  ? 2541 ILE A C     1 
ATOM   8535  O  O     . ILE A 1 2541 ? 178.789 221.178 192.227 1.00 39.52  ? 2541 ILE A O     1 
ATOM   8536  C  CB    . ILE A 1 2541 ? 176.548 219.322 193.233 1.00 31.34  ? 2541 ILE A CB    1 
ATOM   8537  C  CG1   . ILE A 1 2541 ? 175.806 220.044 192.107 1.00 34.77  ? 2541 ILE A CG1   1 
ATOM   8538  C  CG2   . ILE A 1 2541 ? 176.493 220.106 194.544 1.00 37.13  ? 2541 ILE A CG2   1 
ATOM   8539  C  CD1   . ILE A 1 2541 ? 175.654 219.221 190.840 1.00 32.95  ? 2541 ILE A CD1   1 
ATOM   8540  N  N     . SER A 1 2542 ? 179.817 220.173 194.010 1.00 36.52  ? 2542 SER A N     1 
ATOM   8541  C  CA    . SER A 1 2542 ? 180.751 221.301 194.262 1.00 36.77  ? 2542 SER A CA    1 
ATOM   8542  C  C     . SER A 1 2542 ? 181.788 221.373 193.133 1.00 40.91  ? 2542 SER A C     1 
ATOM   8543  O  O     . SER A 1 2542 ? 182.517 222.387 193.066 1.00 44.04  ? 2542 SER A O     1 
ATOM   8544  C  CB    . SER A 1 2542 ? 181.421 221.159 195.602 1.00 39.07  ? 2542 SER A CB    1 
ATOM   8545  O  OG    . SER A 1 2542 ? 182.295 220.039 195.612 1.00 44.76  ? 2542 SER A OG    1 
ATOM   8546  N  N     . GLY A 1 2543 ? 181.850 220.341 192.288 1.00 36.44  ? 2543 GLY A N     1 
ATOM   8547  C  CA    . GLY A 1 2543 ? 182.844 220.306 191.199 1.00 35.14  ? 2543 GLY A CA    1 
ATOM   8548  C  C     . GLY A 1 2543 ? 184.186 219.830 191.714 1.00 38.91  ? 2543 GLY A C     1 
ATOM   8549  O  O     . GLY A 1 2543 ? 185.208 220.124 191.060 1.00 40.67  ? 2543 GLY A O     1 
ATOM   8550  N  N     . GLU A 1 2544 ? 184.188 219.125 192.850 1.00 36.24  ? 2544 GLU A N     1 
ATOM   8551  C  CA    . GLU A 1 2544 ? 185.451 218.600 193.433 1.00 36.65  ? 2544 GLU A CA    1 
ATOM   8552  C  C     . GLU A 1 2544 ? 185.302 217.099 193.723 1.00 30.91  ? 2544 GLU A C     1 
ATOM   8553  O  O     . GLU A 1 2544 ? 184.158 216.651 193.952 1.00 30.69  ? 2544 GLU A O     1 
ATOM   8554  C  CB    . GLU A 1 2544 ? 185.814 219.374 194.701 1.00 35.42  ? 2544 GLU A CB    1 
ATOM   8555  C  CG    . GLU A 1 2544 ? 187.148 218.940 195.299 1.00 41.79  ? 2544 GLU A CG    1 
ATOM   8556  C  CD    . GLU A 1 2544 ? 188.249 218.809 194.262 1.00 50.78  ? 2544 GLU A CD    1 
ATOM   8557  O  OE1   . GLU A 1 2544 ? 188.561 219.820 193.598 1.00 51.62  ? 2544 GLU A OE1   1 
ATOM   8558  O  OE2   . GLU A 1 2544 ? 188.790 217.693 194.113 1.00 47.65  ? 2544 GLU A OE2   1 
ATOM   8559  N  N     . TRP A 1 2545 ? 186.412 216.357 193.706 1.00 32.58  ? 2545 TRP A N     1 
ATOM   8560  C  CA    . TRP A 1 2545 ? 186.371 214.931 193.991 1.00 35.46  ? 2545 TRP A CA    1 
ATOM   8561  C  C     . TRP A 1 2545 ? 186.172 214.693 195.482 1.00 38.21  ? 2545 TRP A C     1 
ATOM   8562  O  O     . TRP A 1 2545 ? 186.785 215.358 196.322 1.00 38.59  ? 2545 TRP A O     1 
ATOM   8563  C  CB    . TRP A 1 2545 ? 187.659 214.250 193.526 1.00 33.99  ? 2545 TRP A CB    1 
ATOM   8564  C  CG    . TRP A 1 2545 ? 187.821 214.180 192.041 1.00 32.28  ? 2545 TRP A CG    1 
ATOM   8565  C  CD1   . TRP A 1 2545 ? 188.594 214.990 191.263 1.00 35.88  ? 2545 TRP A CD1   1 
ATOM   8566  C  CD2   . TRP A 1 2545 ? 187.208 213.237 191.154 1.00 34.80  ? 2545 TRP A CD2   1 
ATOM   8567  N  NE1   . TRP A 1 2545 ? 188.496 214.614 189.945 1.00 35.17  ? 2545 TRP A NE1   1 
ATOM   8568  C  CE2   . TRP A 1 2545 ? 187.651 213.540 189.851 1.00 30.62  ? 2545 TRP A CE2   1 
ATOM   8569  C  CE3   . TRP A 1 2545 ? 186.325 212.168 191.334 1.00 33.35  ? 2545 TRP A CE3   1 
ATOM   8570  C  CZ2   . TRP A 1 2545 ? 187.241 212.814 188.735 1.00 28.38  ? 2545 TRP A CZ2   1 
ATOM   8571  C  CZ3   . TRP A 1 2545 ? 185.920 211.449 190.226 1.00 28.81  ? 2545 TRP A CZ3   1 
ATOM   8572  C  CH2   . TRP A 1 2545 ? 186.377 211.775 188.943 1.00 26.72  ? 2545 TRP A CH2   1 
ATOM   8573  N  N     . SER A 1 2546 ? 185.305 213.738 195.809 1.00 34.42  ? 2546 SER A N     1 
ATOM   8574  C  CA    . SER A 1 2546 ? 185.073 213.345 197.187 1.00 31.80  ? 2546 SER A CA    1 
ATOM   8575  C  C     . SER A 1 2546 ? 185.055 211.826 197.285 1.00 30.59  ? 2546 SER A C     1 
ATOM   8576  O  O     . SER A 1 2546 ? 184.350 211.160 196.516 1.00 29.31  ? 2546 SER A O     1 
ATOM   8577  C  CB    . SER A 1 2546 ? 183.753 213.923 197.717 1.00 30.58  ? 2546 SER A CB    1 
ATOM   8578  O  OG    . SER A 1 2546 ? 182.643 213.191 197.233 1.00 34.84  ? 2546 SER A OG    1 
ATOM   8579  N  N     . PRO A 1 2547 ? 185.827 211.252 198.207 1.00 35.05  ? 2547 PRO A N     1 
ATOM   8580  C  CA    . PRO A 1 2547 ? 185.888 209.789 198.308 1.00 29.31  ? 2547 PRO A CA    1 
ATOM   8581  C  C     . PRO A 1 2547 ? 184.540 209.191 198.684 1.00 29.80  ? 2547 PRO A C     1 
ATOM   8582  O  O     . PRO A 1 2547 ? 183.776 209.766 199.462 1.00 30.85  ? 2547 PRO A O     1 
ATOM   8583  C  CB    . PRO A 1 2547 ? 186.935 209.553 199.403 1.00 25.38  ? 2547 PRO A CB    1 
ATOM   8584  C  CG    . PRO A 1 2547 ? 186.943 210.814 200.199 1.00 26.96  ? 2547 PRO A CG    1 
ATOM   8585  C  CD    . PRO A 1 2547 ? 186.662 211.915 199.221 1.00 28.95  ? 2547 PRO A CD    1 
ATOM   8586  N  N     . TRP A 1 2548 ? 184.256 208.018 198.112 1.00 26.78  ? 2548 TRP A N     1 
ATOM   8587  C  CA    . TRP A 1 2548 ? 183.025 207.306 198.436 1.00 23.87  ? 2548 TRP A CA    1 
ATOM   8588  C  C     . TRP A 1 2548 ? 183.010 206.841 199.886 1.00 28.13  ? 2548 TRP A C     1 
ATOM   8589  O  O     . TRP A 1 2548 ? 181.936 206.590 200.444 1.00 30.96  ? 2548 TRP A O     1 
ATOM   8590  C  CB    . TRP A 1 2548 ? 182.853 206.112 197.498 1.00 21.88  ? 2548 TRP A CB    1 
ATOM   8591  C  CG    . TRP A 1 2548 ? 182.031 206.399 196.279 1.00 19.38  ? 2548 TRP A CG    1 
ATOM   8592  C  CD1   . TRP A 1 2548 ? 182.423 206.264 194.981 1.00 20.29  ? 2548 TRP A CD1   1 
ATOM   8593  C  CD2   . TRP A 1 2548 ? 180.671 206.849 196.243 1.00 19.69  ? 2548 TRP A CD2   1 
ATOM   8594  N  NE1   . TRP A 1 2548 ? 181.397 206.610 194.137 1.00 19.70  ? 2548 TRP A NE1   1 
ATOM   8595  C  CE2   . TRP A 1 2548 ? 180.309 206.971 194.887 1.00 21.14  ? 2548 TRP A CE2   1 
ATOM   8596  C  CE3   . TRP A 1 2548 ? 179.726 207.163 197.224 1.00 23.00  ? 2548 TRP A CE3   1 
ATOM   8597  C  CZ2   . TRP A 1 2548 ? 179.045 207.396 194.488 1.00 22.06  ? 2548 TRP A CZ2   1 
ATOM   8598  C  CZ3   . TRP A 1 2548 ? 178.473 207.583 196.826 1.00 21.95  ? 2548 TRP A CZ3   1 
ATOM   8599  C  CH2   . TRP A 1 2548 ? 178.144 207.697 195.471 1.00 22.16  ? 2548 TRP A CH2   1 
ATOM   8600  N  N     . GLN A 1 2549 ? 184.186 206.718 200.506 1.00 29.76  ? 2549 GLN A N     1 
ATOM   8601  C  CA    . GLN A 1 2549 ? 184.272 206.268 201.889 1.00 26.16  ? 2549 GLN A CA    1 
ATOM   8602  C  C     . GLN A 1 2549 ? 183.587 207.226 202.855 1.00 28.63  ? 2549 GLN A C     1 
ATOM   8603  O  O     . GLN A 1 2549 ? 183.192 206.809 203.949 1.00 33.69  ? 2549 GLN A O     1 
ATOM   8604  C  CB    . GLN A 1 2549 ? 185.738 206.090 202.286 1.00 28.75  ? 2549 GLN A CB    1 
ATOM   8605  C  CG    . GLN A 1 2549 ? 185.974 205.072 203.388 1.00 37.45  ? 2549 GLN A CG    1 
ATOM   8606  C  CD    . GLN A 1 2549 ? 185.797 203.647 202.908 1.00 40.59  ? 2549 GLN A CD    1 
ATOM   8607  O  OE1   . GLN A 1 2549 ? 186.413 203.229 201.928 1.00 41.95  ? 2549 GLN A OE1   1 
ATOM   8608  N  NE2   . GLN A 1 2549 ? 184.957 202.889 203.601 1.00 31.16  ? 2549 GLN A NE2   1 
ATOM   8609  N  N     . ALA A 1 2550 ? 183.445 208.499 202.482 1.00 28.84  ? 2550 ALA A N     1 
ATOM   8610  C  CA    . ALA A 1 2550 ? 182.806 209.467 203.366 1.00 27.48  ? 2550 ALA A CA    1 
ATOM   8611  C  C     . ALA A 1 2550 ? 181.310 209.226 203.510 1.00 31.12  ? 2550 ALA A C     1 
ATOM   8612  O  O     . ALA A 1 2550 ? 180.708 209.713 204.474 1.00 37.52  ? 2550 ALA A O     1 
ATOM   8613  C  CB    . ALA A 1 2550 ? 183.059 210.887 202.860 1.00 32.23  ? 2550 ALA A CB    1 
ATOM   8614  N  N     . LYS A 1 2551 ? 180.732 208.454 202.584 1.00 30.45  ? 2551 LYS A N     1 
ATOM   8615  C  CA    . LYS A 1 2551 ? 179.270 208.189 202.610 1.00 28.86  ? 2551 LYS A CA    1 
ATOM   8616  C  C     . LYS A 1 2551 ? 178.992 206.813 203.237 1.00 29.62  ? 2551 LYS A C     1 
ATOM   8617  O  O     . LYS A 1 2551 ? 177.810 206.525 203.525 1.00 36.61  ? 2551 LYS A O     1 
ATOM   8618  C  CB    . LYS A 1 2551 ? 178.687 208.265 201.195 1.00 30.16  ? 2551 LYS A CB    1 
ATOM   8619  C  CG    . LYS A 1 2551 ? 178.766 209.641 200.551 1.00 36.27  ? 2551 LYS A CG    1 
ATOM   8620  C  CD    . LYS A 1 2551 ? 177.937 209.753 199.278 1.00 31.64  ? 2551 LYS A CD    1 
ATOM   8621  C  CE    . LYS A 1 2551 ? 177.951 211.135 198.710 1.00 32.32  ? 2551 LYS A CE    1 
ATOM   8622  N  NZ    . LYS A 1 2551 ? 177.103 211.231 197.519 1.00 41.47  ? 2551 LYS A NZ    1 
ATOM   8623  N  N     . VAL A 1 2552 ? 180.034 206.000 203.435 1.00 31.12  ? 2552 VAL A N     1 
ATOM   8624  C  CA    . VAL A 1 2552 ? 179.857 204.663 204.080 1.00 30.95  ? 2552 VAL A CA    1 
ATOM   8625  C  C     . VAL A 1 2552 ? 180.346 204.748 205.536 1.00 31.92  ? 2552 VAL A C     1 
ATOM   8626  O  O     . VAL A 1 2552 ? 181.577 204.732 205.754 1.00 30.36  ? 2552 VAL A O     1 
ATOM   8627  C  CB    . VAL A 1 2552 ? 180.568 203.535 203.306 1.00 26.21  ? 2552 VAL A CB    1 
ATOM   8628  C  CG1   . VAL A 1 2552 ? 181.947 203.953 202.811 1.00 31.92  ? 2552 VAL A CG1   1 
ATOM   8629  C  CG2   . VAL A 1 2552 ? 180.643 202.247 204.117 1.00 23.62  ? 2552 VAL A CG2   1 
ATOM   8630  N  N     . PRO A 1 2553 ? 179.440 204.854 206.532 1.00 33.10  ? 2553 PRO A N     1 
ATOM   8631  C  CA    . PRO A 1 2553 ? 179.835 204.893 207.932 1.00 37.04  ? 2553 PRO A CA    1 
ATOM   8632  C  C     . PRO A 1 2553 ? 179.685 203.549 208.629 1.00 44.24  ? 2553 PRO A C     1 
ATOM   8633  O  O     . PRO A 1 2553 ? 178.971 202.669 208.104 1.00 42.71  ? 2553 PRO A O     1 
ATOM   8634  C  CB    . PRO A 1 2553 ? 178.821 205.921 208.439 1.00 36.56  ? 2553 PRO A CB    1 
ATOM   8635  C  CG    . PRO A 1 2553 ? 177.554 205.579 207.681 1.00 36.11  ? 2553 PRO A CG    1 
ATOM   8636  C  CD    . PRO A 1 2553 ? 178.005 204.988 206.353 1.00 29.19  ? 2553 PRO A CD    1 
ATOM   8637  N  N     . GLN A 1 2554 ? 180.337 203.384 209.785 1.00 43.83  ? 2554 GLN A N     1 
ATOM   8638  C  CA    . GLN A 1 2554 ? 180.186 202.128 210.568 1.00 45.14  ? 2554 GLN A CA    1 
ATOM   8639  C  C     . GLN A 1 2554 ? 178.890 202.221 211.387 1.00 47.41  ? 2554 GLN A C     1 
ATOM   8640  O  O     . GLN A 1 2554 ? 178.968 202.567 212.586 1.00 53.24  ? 2554 GLN A O     1 
ATOM   8641  C  CB    . GLN A 1 2554 ? 181.390 201.882 211.477 1.00 50.35  ? 2554 GLN A CB    1 
ATOM   8642  C  CG    . GLN A 1 2554 ? 181.289 200.598 212.294 1.00 53.15  ? 2554 GLN A CG    1 
ATOM   8643  C  CD    . GLN A 1 2554 ? 182.455 200.392 213.235 1.00 57.46  ? 2554 GLN A CD    1 
ATOM   8644  O  OE1   . GLN A 1 2554 ? 183.387 201.202 213.295 1.00 56.78  ? 2554 GLN A OE1   1 
ATOM   8645  N  NE2   . GLN A 1 2554 ? 182.415 199.298 213.982 1.00 45.28  ? 2554 GLN A NE2   1 
ATOM   8646  N  N     . ILE A 1 2555 ? 177.748 201.932 210.759 1.00 46.41  ? 2555 ILE A N     1 
ATOM   8647  C  CA    . ILE A 1 2555 ? 176.430 202.049 211.453 1.00 43.82  ? 2555 ILE A CA    1 
ATOM   8648  C  C     . ILE A 1 2555 ? 176.271 200.889 212.446 1.00 51.21  ? 2555 ILE A C     1 
ATOM   8649  O  O     . ILE A 1 2555 ? 176.963 199.862 212.270 1.00 54.48  ? 2555 ILE A O     1 
ATOM   8650  C  CB    . ILE A 1 2555 ? 175.282 202.054 210.429 1.00 35.23  ? 2555 ILE A CB    1 
ATOM   8651  C  CG1   . ILE A 1 2555 ? 175.030 200.655 209.866 1.00 36.95  ? 2555 ILE A CG1   1 
ATOM   8652  C  CG2   . ILE A 1 2555 ? 175.541 203.074 209.320 1.00 46.10  ? 2555 ILE A CG2   1 
ATOM   8653  C  CD1   . ILE A 1 2555 ? 173.789 200.548 208.999 1.00 34.95  ? 2555 ILE A CD1   1 
ATOM   8654  N  N     . GLU A 1 2556 ? 175.405 201.051 213.449 1.00 46.69  ? 2556 GLU A N     1 
ATOM   8655  C  CA    . GLU A 1 2556 ? 175.118 199.940 214.396 1.00 49.29  ? 2556 GLU A CA    1 
ATOM   8656  C  C     . GLU A 1 2556 ? 173.643 199.550 214.219 1.00 49.16  ? 2556 GLU A C     1 
ATOM   8657  O  O     . GLU A 1 2556 ? 172.772 200.402 214.498 1.00 51.75  ? 2556 GLU A O     1 
ATOM   8658  C  CB    . GLU A 1 2556 ? 175.453 200.339 215.834 1.00 51.50  ? 2556 GLU A CB    1 
ATOM   8659  C  CG    . GLU A 1 2556 ? 176.932 200.176 216.174 1.00 49.28  ? 2556 GLU A CG    1 
ATOM   8660  C  CD    . GLU A 1 2556 ? 177.882 200.922 215.254 1.00 57.41  ? 2556 GLU A CD    1 
ATOM   8661  O  OE1   . GLU A 1 2556 ? 177.776 202.165 215.181 1.00 61.35  ? 2556 GLU A OE1   1 
ATOM   8662  O  OE2   . GLU A 1 2556 ? 178.725 200.264 214.610 1.00 57.21  ? 2556 GLU A OE2   1 
ATOM   8663  N  N     . VAL A 1 2557 ? 173.377 198.320 213.774 1.00 43.21  ? 2557 VAL A N     1 
ATOM   8664  C  CA    . VAL A 1 2557 ? 171.973 197.899 213.481 1.00 39.36  ? 2557 VAL A CA    1 
ATOM   8665  C  C     . VAL A 1 2557 ? 171.221 197.608 214.787 1.00 44.33  ? 2557 VAL A C     1 
ATOM   8666  O  O     . VAL A 1 2557 ? 171.874 197.168 215.757 1.00 46.10  ? 2557 VAL A O     1 
ATOM   8667  C  CB    . VAL A 1 2557 ? 171.970 196.667 212.555 1.00 34.75  ? 2557 VAL A CB    1 
ATOM   8668  C  CG1   . VAL A 1 2557 ? 170.558 196.175 212.263 1.00 33.97  ? 2557 VAL A CG1   1 
ATOM   8669  C  CG2   . VAL A 1 2557 ? 172.727 196.932 211.259 1.00 37.59  ? 2557 VAL A CG2   1 
ATOM   8670  N  N     . GLU A 1 2558 ? 169.908 197.854 214.812 1.00 47.00  ? 2558 GLU A N     1 
ATOM   8671  C  CA    . GLU A 1 2558 ? 169.099 197.528 215.976 1.00 40.69  ? 2558 GLU A CA    1 
ATOM   8672  C  C     . GLU A 1 2558 ? 169.094 196.023 216.224 1.00 44.86  ? 2558 GLU A C     1 
ATOM   8673  O  O     . GLU A 1 2558 ? 169.351 195.219 215.324 1.00 46.47  ? 2558 GLU A O     1 
ATOM   8674  C  CB    . GLU A 1 2558 ? 167.668 198.032 215.791 1.00 45.59  ? 2558 GLU A CB    1 
ATOM   8675  C  CG    . GLU A 1 2558 ? 167.388 199.369 216.455 1.00 55.24  ? 2558 GLU A CG    1 
ATOM   8676  C  CD    . GLU A 1 2558 ? 168.139 200.513 215.805 1.00 64.60  ? 2558 GLU A CD    1 
ATOM   8677  O  OE1   . GLU A 1 2558 ? 167.751 200.924 214.692 1.00 69.46  ? 2558 GLU A OE1   1 
ATOM   8678  O  OE2   . GLU A 1 2558 ? 169.118 201.002 216.407 1.00 60.21  ? 2558 GLU A OE2   1 
ATOM   8679  N  N     . THR A 1 2559 ? 168.800 195.648 217.472 1.00 48.55  ? 2559 THR A N     1 
ATOM   8680  C  CA    . THR A 1 2559 ? 168.782 194.235 217.838 1.00 45.36  ? 2559 THR A CA    1 
ATOM   8681  C  C     . THR A 1 2559 ? 167.679 193.482 217.103 1.00 47.76  ? 2559 THR A C     1 
ATOM   8682  O  O     . THR A 1 2559 ? 167.868 192.331 216.694 1.00 51.30  ? 2559 THR A O     1 
ATOM   8683  C  CB    . THR A 1 2559 ? 168.613 194.084 219.349 1.00 49.11  ? 2559 THR A CB    1 
ATOM   8684  O  OG1   . THR A 1 2559 ? 167.735 195.106 219.838 1.00 56.93  ? 2559 THR A OG1   1 
ATOM   8685  C  CG2   . THR A 1 2559 ? 169.957 194.204 220.051 1.00 42.29  ? 2559 THR A CG2   1 
ATOM   8686  N  N     . HIS A 1 2560 ? 166.516 194.111 216.928 1.00 43.31  ? 2560 HIS A N     1 
ATOM   8687  C  CA    . HIS A 1 2560 ? 165.397 193.439 216.279 1.00 47.70  ? 2560 HIS A CA    1 
ATOM   8688  C  C     . HIS A 1 2560 ? 165.487 193.461 214.759 1.00 49.22  ? 2560 HIS A C     1 
ATOM   8689  O  O     . HIS A 1 2560 ? 164.648 192.837 214.101 1.00 46.69  ? 2560 HIS A O     1 
ATOM   8690  C  CB    . HIS A 1 2560 ? 164.077 194.066 216.730 1.00 54.67  ? 2560 HIS A CB    1 
ATOM   8691  C  CG    . HIS A 1 2560 ? 163.804 195.406 216.121 1.00 60.46  ? 2560 HIS A CG    1 
ATOM   8692  N  ND1   . HIS A 1 2560 ? 164.726 196.430 216.131 1.00 57.77  ? 2560 HIS A ND1   1 
ATOM   8693  C  CD2   . HIS A 1 2560 ? 162.712 195.889 215.483 1.00 60.75  ? 2560 HIS A CD2   1 
ATOM   8694  C  CE1   . HIS A 1 2560 ? 164.213 197.487 215.527 1.00 55.61  ? 2560 HIS A CE1   1 
ATOM   8695  N  NE2   . HIS A 1 2560 ? 162.992 197.185 215.123 1.00 60.65  ? 2560 HIS A NE2   1 
ATOM   8696  N  N     . LYS A 1 2561 ? 166.470 194.155 214.186 1.00 49.07  ? 2561 LYS A N     1 
ATOM   8697  C  CA    . LYS A 1 2561 ? 166.654 194.217 212.741 1.00 46.04  ? 2561 LYS A CA    1 
ATOM   8698  C  C     . LYS A 1 2561 ? 167.941 193.524 212.302 1.00 46.81  ? 2561 LYS A C     1 
ATOM   8699  O  O     . LYS A 1 2561 ? 168.533 193.890 211.284 1.00 50.18  ? 2561 LYS A O     1 
ATOM   8700  C  CB    . LYS A 1 2561 ? 166.646 195.667 212.260 1.00 46.24  ? 2561 LYS A CB    1 
ATOM   8701  C  CG    . LYS A 1 2561 ? 165.319 196.378 212.444 1.00 53.80  ? 2561 LYS A CG    1 
ATOM   8702  C  CD    . LYS A 1 2561 ? 164.531 196.426 211.147 1.00 54.10  ? 2561 LYS A CD    1 
ATOM   8703  C  CE    . LYS A 1 2561 ? 163.210 197.150 211.338 1.00 54.03  ? 2561 LYS A CE    1 
ATOM   8704  N  NZ    . LYS A 1 2561 ? 162.282 196.380 212.211 1.00 54.54  ? 2561 LYS A NZ    1 
ATOM   8705  N  N     . VAL A 1 2562 ? 168.382 192.522 213.058 1.00 46.48  ? 2562 VAL A N     1 
ATOM   8706  C  CA    . VAL A 1 2562 ? 169.651 191.864 212.771 1.00 43.38  ? 2562 VAL A CA    1 
ATOM   8707  C  C     . VAL A 1 2562 ? 169.473 190.926 211.583 1.00 43.83  ? 2562 VAL A C     1 
ATOM   8708  O  O     . VAL A 1 2562 ? 168.669 189.987 211.630 1.00 47.66  ? 2562 VAL A O     1 
ATOM   8709  C  CB    . VAL A 1 2562 ? 170.171 191.115 214.004 1.00 39.51  ? 2562 VAL A CB    1 
ATOM   8710  C  CG1   . VAL A 1 2562 ? 171.358 190.260 213.635 1.00 41.01  ? 2562 VAL A CG1   1 
ATOM   8711  C  CG2   . VAL A 1 2562 ? 170.561 192.101 215.087 1.00 41.93  ? 2562 VAL A CG2   1 
ATOM   8712  N  N     . ALA A 1 2563 ? 170.227 191.184 210.512 1.00 44.66  ? 2563 ALA A N     1 
ATOM   8713  C  CA    . ALA A 1 2563 ? 170.210 190.370 209.294 1.00 38.94  ? 2563 ALA A CA    1 
ATOM   8714  C  C     . ALA A 1 2563 ? 168.801 190.245 208.719 1.00 50.52  ? 2563 ALA A C     1 
ATOM   8715  O  O     . ALA A 1 2563 ? 168.416 189.201 208.189 1.00 52.65  ? 2563 ALA A O     1 
ATOM   8716  C  CB    . ALA A 1 2563 ? 170.825 188.991 209.539 1.00 32.20  ? 2563 ALA A CB    1 
ATOM   8717  N  N     . ALA A 1 2564 ? 168.025 191.320 208.823 1.00 55.11  ? 2564 ALA A N     1 
ATOM   8718  C  CA    . ALA A 1 2564 ? 166.704 191.343 208.222 1.00 52.13  ? 2564 ALA A CA    1 
ATOM   8719  C  C     . ALA A 1 2564 ? 166.824 191.405 206.699 1.00 57.02  ? 2564 ALA A C     1 
ATOM   8720  O  O     . ALA A 1 2564 ? 167.825 191.892 206.167 1.00 52.53  ? 2564 ALA A O     1 
ATOM   8721  C  CB    . ALA A 1 2564 ? 165.903 192.535 208.737 1.00 46.86  ? 2564 ALA A CB    1 
ATOM   8722  N  N     . PRO A 1 2565 ? 165.821 190.901 205.974 1.00 59.53  ? 2565 PRO A N     1 
ATOM   8723  C  CA    . PRO A 1 2565 ? 165.906 190.918 204.503 1.00 54.22  ? 2565 PRO A CA    1 
ATOM   8724  C  C     . PRO A 1 2565 ? 166.023 192.312 203.910 1.00 51.65  ? 2565 PRO A C     1 
ATOM   8725  O  O     . PRO A 1 2565 ? 166.622 192.469 202.839 1.00 57.14  ? 2565 PRO A O     1 
ATOM   8726  C  CB    . PRO A 1 2565 ? 164.605 190.228 204.064 1.00 54.28  ? 2565 PRO A CB    1 
ATOM   8727  C  CG    . PRO A 1 2565 ? 163.717 190.240 205.269 1.00 50.21  ? 2565 PRO A CG    1 
ATOM   8728  C  CD    . PRO A 1 2565 ? 164.626 190.186 206.450 1.00 52.84  ? 2565 PRO A CD    1 
ATOM   8729  N  N     . ASP A 1 2566 ? 165.470 193.329 204.567 1.00 46.67  ? 2566 ASP A N     1 
ATOM   8730  C  CA    . ASP A 1 2566 ? 165.462 194.688 204.043 1.00 47.39  ? 2566 ASP A CA    1 
ATOM   8731  C  C     . ASP A 1 2566 ? 166.552 195.566 204.646 1.00 43.17  ? 2566 ASP A C     1 
ATOM   8732  O  O     . ASP A 1 2566 ? 166.573 196.773 204.385 1.00 43.43  ? 2566 ASP A O     1 
ATOM   8733  C  CB    . ASP A 1 2566 ? 164.094 195.331 204.276 1.00 51.20  ? 2566 ASP A CB    1 
ATOM   8734  C  CG    . ASP A 1 2566 ? 163.727 195.401 205.745 1.00 62.20  ? 2566 ASP A CG    1 
ATOM   8735  O  OD1   . ASP A 1 2566 ? 163.313 194.365 206.307 1.00 60.18  ? 2566 ASP A OD1   1 
ATOM   8736  O  OD2   . ASP A 1 2566 ? 163.856 196.492 206.340 1.00 62.94  ? 2566 ASP A OD2   1 
ATOM   8737  N  N     . VAL A 1 2567 ? 167.453 194.996 205.440 1.00 38.34  ? 2567 VAL A N     1 
ATOM   8738  C  CA    . VAL A 1 2567 ? 168.499 195.756 206.116 1.00 36.26  ? 2567 VAL A CA    1 
ATOM   8739  C  C     . VAL A 1 2567 ? 169.800 195.571 205.350 1.00 34.03  ? 2567 VAL A C     1 
ATOM   8740  O  O     . VAL A 1 2567 ? 170.248 194.439 205.131 1.00 37.00  ? 2567 VAL A O     1 
ATOM   8741  C  CB    . VAL A 1 2567 ? 168.651 195.323 207.582 1.00 36.56  ? 2567 VAL A CB    1 
ATOM   8742  C  CG1   . VAL A 1 2567 ? 169.945 195.871 208.164 1.00 31.49  ? 2567 VAL A CG1   1 
ATOM   8743  C  CG2   . VAL A 1 2567 ? 167.461 195.801 208.394 1.00 43.81  ? 2567 VAL A CG2   1 
ATOM   8744  N  N     . VAL A 1 2568 ? 170.406 196.683 204.943 1.00 27.95  ? 2568 VAL A N     1 
ATOM   8745  C  CA    . VAL A 1 2568 ? 171.650 196.680 204.184 1.00 20.68  ? 2568 VAL A CA    1 
ATOM   8746  C  C     . VAL A 1 2568 ? 172.699 197.420 204.999 1.00 22.88  ? 2568 VAL A C     1 
ATOM   8747  O  O     . VAL A 1 2568 ? 172.489 198.577 205.386 1.00 23.16  ? 2568 VAL A O     1 
ATOM   8748  C  CB    . VAL A 1 2568 ? 171.479 197.332 202.803 1.00 18.58  ? 2568 VAL A CB    1 
ATOM   8749  C  CG1   . VAL A 1 2568 ? 172.786 197.281 202.023 1.00 15.70  ? 2568 VAL A CG1   1 
ATOM   8750  C  CG2   . VAL A 1 2568 ? 170.356 196.661 202.033 1.00 22.79  ? 2568 VAL A CG2   1 
ATOM   8751  N  N     . VAL A 1 2569 ? 173.821 196.759 205.262 1.00 22.27  ? 2569 VAL A N     1 
ATOM   8752  C  CA    . VAL A 1 2569 ? 174.957 197.409 205.907 1.00 15.48  ? 2569 VAL A CA    1 
ATOM   8753  C  C     . VAL A 1 2569 ? 175.749 198.124 204.820 1.00 17.75  ? 2569 VAL A C     1 
ATOM   8754  O  O     . VAL A 1 2569 ? 176.261 197.470 203.900 1.00 20.19  ? 2569 VAL A O     1 
ATOM   8755  C  CB    . VAL A 1 2569 ? 175.828 196.400 206.670 1.00 14.59  ? 2569 VAL A CB    1 
ATOM   8756  C  CG1   . VAL A 1 2569 ? 177.086 197.076 207.192 1.00 15.08  ? 2569 VAL A CG1   1 
ATOM   8757  C  CG2   . VAL A 1 2569 ? 175.040 195.776 207.810 1.00 21.25  ? 2569 VAL A CG2   1 
ATOM   8758  N  N     . PRO A 1 2570 ? 175.864 199.451 204.872 1.00 17.09  ? 2570 PRO A N     1 
ATOM   8759  C  CA    . PRO A 1 2570 ? 176.561 200.174 203.800 1.00 14.44  ? 2570 PRO A CA    1 
ATOM   8760  C  C     . PRO A 1 2570 ? 178.025 199.769 203.717 1.00 15.48  ? 2570 PRO A C     1 
ATOM   8761  O  O     . PRO A 1 2570 ? 178.689 199.566 204.736 1.00 15.88  ? 2570 PRO A O     1 
ATOM   8762  C  CB    . PRO A 1 2570 ? 176.403 201.646 204.202 1.00 16.53  ? 2570 PRO A CB    1 
ATOM   8763  C  CG    . PRO A 1 2570 ? 176.162 201.609 205.672 1.00 17.84  ? 2570 PRO A CG    1 
ATOM   8764  C  CD    . PRO A 1 2570 ? 175.362 200.364 205.912 1.00 19.57  ? 2570 PRO A CD    1 
ATOM   8765  N  N     . THR A 1 2571 ? 178.517 199.642 202.488 1.00 16.27  ? 2571 THR A N     1 
ATOM   8766  C  CA    . THR A 1 2571 ? 179.918 199.377 202.194 1.00 13.96  ? 2571 THR A CA    1 
ATOM   8767  C  C     . THR A 1 2571 ? 180.340 200.255 201.025 1.00 18.37  ? 2571 THR A C     1 
ATOM   8768  O  O     . THR A 1 2571 ? 179.552 201.046 200.498 1.00 17.64  ? 2571 THR A O     1 
ATOM   8769  C  CB    . THR A 1 2571 ? 180.166 197.897 201.868 1.00 15.22  ? 2571 THR A CB    1 
ATOM   8770  O  OG1   . THR A 1 2571 ? 179.371 197.511 200.739 1.00 16.99  ? 2571 THR A OG1   1 
ATOM   8771  C  CG2   . THR A 1 2571 ? 179.830 197.010 203.056 1.00 17.75  ? 2571 THR A CG2   1 
ATOM   8772  N  N     . LEU A 1 2572 ? 181.603 200.116 200.619 1.00 20.66  ? 2572 LEU A N     1 
ATOM   8773  C  CA    . LEU A 1 2572 ? 182.086 200.851 199.456 1.00 16.36  ? 2572 LEU A CA    1 
ATOM   8774  C  C     . LEU A 1 2572 ? 181.362 200.409 198.191 1.00 18.05  ? 2572 LEU A C     1 
ATOM   8775  O  O     . LEU A 1 2572 ? 180.935 201.239 197.383 1.00 22.14  ? 2572 LEU A O     1 
ATOM   8776  C  CB    . LEU A 1 2572 ? 183.596 200.664 199.309 1.00 19.09  ? 2572 LEU A CB    1 
ATOM   8777  C  CG    . LEU A 1 2572 ? 184.303 201.608 198.336 1.00 20.05  ? 2572 LEU A CG    1 
ATOM   8778  C  CD1   . LEU A 1 2572 ? 184.553 202.957 198.987 1.00 27.28  ? 2572 LEU A CD1   1 
ATOM   8779  C  CD2   . LEU A 1 2572 ? 185.605 200.993 197.855 1.00 24.05  ? 2572 LEU A CD2   1 
ATOM   8780  N  N     . ASP A 1 2573 ? 181.199 199.096 198.012 1.00 19.02  ? 2573 ASP A N     1 
ATOM   8781  C  CA    . ASP A 1 2573 ? 180.539 198.589 196.813 1.00 18.05  ? 2573 ASP A CA    1 
ATOM   8782  C  C     . ASP A 1 2573 ? 179.049 198.906 196.823 1.00 15.43  ? 2573 ASP A C     1 
ATOM   8783  O  O     . ASP A 1 2573 ? 178.444 199.113 195.765 1.00 20.02  ? 2573 ASP A O     1 
ATOM   8784  C  CB    . ASP A 1 2573 ? 180.764 197.083 196.687 1.00 20.98  ? 2573 ASP A CB    1 
ATOM   8785  C  CG    . ASP A 1 2573 ? 182.168 196.740 196.234 1.00 39.43  ? 2573 ASP A CG    1 
ATOM   8786  O  OD1   . ASP A 1 2573 ? 182.561 197.177 195.132 1.00 35.61  ? 2573 ASP A OD1   1 
ATOM   8787  O  OD2   . ASP A 1 2573 ? 182.877 196.032 196.978 1.00 52.62  ? 2573 ASP A OD2   1 
ATOM   8788  N  N     . THR A 1 2574 ? 178.439 198.942 198.008 1.00 17.07  ? 2574 THR A N     1 
ATOM   8789  C  CA    . THR A 1 2574 ? 176.997 199.153 198.096 1.00 12.99  ? 2574 THR A CA    1 
ATOM   8790  C  C     . THR A 1 2574 ? 176.617 200.569 197.675 1.00 13.99  ? 2574 THR A C     1 
ATOM   8791  O  O     . THR A 1 2574 ? 175.701 200.764 196.869 1.00 14.76  ? 2574 THR A O     1 
ATOM   8792  C  CB    . THR A 1 2574 ? 176.515 198.859 199.518 1.00 13.22  ? 2574 THR A CB    1 
ATOM   8793  O  OG1   . THR A 1 2574 ? 176.464 197.442 199.721 1.00 12.51  ? 2574 THR A OG1   1 
ATOM   8794  C  CG2   . THR A 1 2574 ? 175.135 199.446 199.751 1.00 16.57  ? 2574 THR A CG2   1 
ATOM   8795  N  N     . VAL A 1 2575 ? 177.316 201.573 198.209 1.00 14.34  ? 2575 VAL A N     1 
ATOM   8796  C  CA    . VAL A 1 2575 ? 176.965 202.959 197.909 1.00 14.28  ? 2575 VAL A CA    1 
ATOM   8797  C  C     . VAL A 1 2575 ? 177.277 203.296 196.454 1.00 17.66  ? 2575 VAL A C     1 
ATOM   8798  O  O     . VAL A 1 2575 ? 176.537 204.046 195.807 1.00 21.55  ? 2575 VAL A O     1 
ATOM   8799  C  CB    . VAL A 1 2575 ? 177.669 203.917 198.888 1.00 15.89  ? 2575 VAL A CB    1 
ATOM   8800  C  CG1   . VAL A 1 2575 ? 177.222 203.632 200.312 1.00 17.65  ? 2575 VAL A CG1   1 
ATOM   8801  C  CG2   . VAL A 1 2575 ? 179.181 203.800 198.776 1.00 19.28  ? 2575 VAL A CG2   1 
ATOM   8802  N  N     . ARG A 1 2576 ? 178.377 202.759 195.919 1.00 18.93  ? 2576 ARG A N     1 
ATOM   8803  C  CA    . ARG A 1 2576 ? 178.723 203.013 194.524 1.00 13.22  ? 2576 ARG A CA    1 
ATOM   8804  C  C     . ARG A 1 2576 ? 177.670 202.442 193.583 1.00 13.89  ? 2576 ARG A C     1 
ATOM   8805  O  O     . ARG A 1 2576 ? 177.263 203.096 192.616 1.00 19.75  ? 2576 ARG A O     1 
ATOM   8806  C  CB    . ARG A 1 2576 ? 180.099 202.428 194.208 1.00 14.30  ? 2576 ARG A CB    1 
ATOM   8807  C  CG    . ARG A 1 2576 ? 181.243 203.120 194.917 1.00 19.37  ? 2576 ARG A CG    1 
ATOM   8808  C  CD    . ARG A 1 2576 ? 182.586 202.614 194.424 1.00 21.77  ? 2576 ARG A CD    1 
ATOM   8809  N  NE    . ARG A 1 2576 ? 182.604 201.163 194.293 1.00 21.71  ? 2576 ARG A NE    1 
ATOM   8810  C  CZ    . ARG A 1 2576 ? 183.701 200.421 194.342 1.00 23.18  ? 2576 ARG A CZ    1 
ATOM   8811  N  NH1   . ARG A 1 2576 ? 184.895 200.962 194.520 1.00 21.64  ? 2576 ARG A NH1   1 
ATOM   8812  N  NH2   . ARG A 1 2576 ? 183.598 199.101 194.211 1.00 27.31  ? 2576 ARG A NH2   1 
ATOM   8813  N  N     . HIS A 1 2577 ? 177.216 201.218 193.853 1.00 11.95  ? 2577 HIS A N     1 
ATOM   8814  C  CA    . HIS A 1 2577 ? 176.213 200.600 192.994 1.00 10.67  ? 2577 HIS A CA    1 
ATOM   8815  C  C     . HIS A 1 2577 ? 174.855 201.270 193.162 1.00 12.22  ? 2577 HIS A C     1 
ATOM   8816  O  O     . HIS A 1 2577 ? 174.093 201.390 192.195 1.00 12.49  ? 2577 HIS A O     1 
ATOM   8817  C  CB    . HIS A 1 2577 ? 176.124 199.104 193.290 1.00 8.90   ? 2577 HIS A CB    1 
ATOM   8818  C  CG    . HIS A 1 2577 ? 177.367 198.347 192.939 1.00 11.20  ? 2577 HIS A CG    1 
ATOM   8819  N  ND1   . HIS A 1 2577 ? 177.621 197.074 193.403 1.00 16.08  ? 2577 HIS A ND1   1 
ATOM   8820  C  CD2   . HIS A 1 2577 ? 178.429 198.684 192.170 1.00 16.21  ? 2577 HIS A CD2   1 
ATOM   8821  C  CE1   . HIS A 1 2577 ? 178.785 196.660 192.934 1.00 16.19  ? 2577 HIS A CE1   1 
ATOM   8822  N  NE2   . HIS A 1 2577 ? 179.295 197.619 192.184 1.00 17.26  ? 2577 HIS A NE2   1 
ATOM   8823  N  N     . GLU A 1 2578 ? 174.533 201.711 194.380 1.00 14.44  ? 2578 GLU A N     1 
ATOM   8824  C  CA    . GLU A 1 2578 ? 173.249 202.365 194.617 1.00 13.00  ? 2578 GLU A CA    1 
ATOM   8825  C  C     . GLU A 1 2578 ? 173.141 203.673 193.845 1.00 17.73  ? 2578 GLU A C     1 
ATOM   8826  O  O     . GLU A 1 2578 ? 172.144 203.915 193.155 1.00 19.76  ? 2578 GLU A O     1 
ATOM   8827  C  CB    . GLU A 1 2578 ? 173.057 202.616 196.112 1.00 17.25  ? 2578 GLU A CB    1 
ATOM   8828  C  CG    . GLU A 1 2578 ? 172.053 201.695 196.773 1.00 21.91  ? 2578 GLU A CG    1 
ATOM   8829  C  CD    . GLU A 1 2578 ? 172.400 201.414 198.220 1.00 24.29  ? 2578 GLU A CD    1 
ATOM   8830  O  OE1   . GLU A 1 2578 ? 172.821 202.356 198.924 1.00 26.81  ? 2578 GLU A OE1   1 
ATOM   8831  O  OE2   . GLU A 1 2578 ? 172.262 200.252 198.650 1.00 26.36  ? 2578 GLU A OE2   1 
ATOM   8832  N  N     . ALA A 1 2579 ? 174.158 204.532 193.954 1.00 18.67  ? 2579 ALA A N     1 
ATOM   8833  C  CA    . ALA A 1 2579 ? 174.142 205.794 193.220 1.00 15.47  ? 2579 ALA A CA    1 
ATOM   8834  C  C     . ALA A 1 2579 ? 174.158 205.553 191.718 1.00 16.48  ? 2579 ALA A C     1 
ATOM   8835  O  O     . ALA A 1 2579 ? 173.571 206.324 190.949 1.00 19.94  ? 2579 ALA A O     1 
ATOM   8836  C  CB    . ALA A 1 2579 ? 175.327 206.661 193.639 1.00 14.72  ? 2579 ALA A CB    1 
ATOM   8837  N  N     . LEU A 1 2580 ? 174.834 204.490 191.281 1.00 12.70  ? 2580 LEU A N     1 
ATOM   8838  C  CA    . LEU A 1 2580 ? 174.824 204.135 189.868 1.00 11.76  ? 2580 LEU A CA    1 
ATOM   8839  C  C     . LEU A 1 2580 ? 173.428 203.743 189.406 1.00 12.95  ? 2580 LEU A C     1 
ATOM   8840  O  O     . LEU A 1 2580 ? 172.944 204.236 188.379 1.00 18.60  ? 2580 LEU A O     1 
ATOM   8841  C  CB    . LEU A 1 2580 ? 175.803 202.994 189.611 1.00 10.68  ? 2580 LEU A CB    1 
ATOM   8842  C  CG    . LEU A 1 2580 ? 176.496 203.012 188.255 1.00 12.33  ? 2580 LEU A CG    1 
ATOM   8843  C  CD1   . LEU A 1 2580 ? 177.712 202.138 188.306 1.00 17.19  ? 2580 LEU A CD1   1 
ATOM   8844  C  CD2   . LEU A 1 2580 ? 175.555 202.528 187.191 1.00 17.44  ? 2580 LEU A CD2   1 
ATOM   8845  N  N     . LEU A 1 2581 ? 172.770 202.848 190.144 1.00 13.02  ? 2581 LEU A N     1 
ATOM   8846  C  CA    . LEU A 1 2581 ? 171.438 202.401 189.754 1.00 13.99  ? 2581 LEU A CA    1 
ATOM   8847  C  C     . LEU A 1 2581 ? 170.447 203.556 189.761 1.00 13.81  ? 2581 LEU A C     1 
ATOM   8848  O  O     . LEU A 1 2581 ? 169.585 203.644 188.880 1.00 16.60  ? 2581 LEU A O     1 
ATOM   8849  C  CB    . LEU A 1 2581 ? 170.968 201.278 190.677 1.00 13.86  ? 2581 LEU A CB    1 
ATOM   8850  C  CG    . LEU A 1 2581 ? 171.728 199.961 190.534 1.00 8.87   ? 2581 LEU A CG    1 
ATOM   8851  C  CD1   . LEU A 1 2581 ? 171.182 198.912 191.486 1.00 10.01  ? 2581 LEU A CD1   1 
ATOM   8852  C  CD2   . LEU A 1 2581 ? 171.664 199.474 189.101 1.00 11.82  ? 2581 LEU A CD2   1 
ATOM   8853  N  N     . TYR A 1 2582 ? 170.562 204.456 190.740 1.00 15.54  ? 2582 TYR A N     1 
ATOM   8854  C  CA    . TYR A 1 2582 ? 169.686 205.622 190.783 1.00 18.05  ? 2582 TYR A CA    1 
ATOM   8855  C  C     . TYR A 1 2582 ? 169.828 206.457 189.517 1.00 19.08  ? 2582 TYR A C     1 
ATOM   8856  O  O     . TYR A 1 2582 ? 168.834 206.963 188.984 1.00 25.67  ? 2582 TYR A O     1 
ATOM   8857  C  CB    . TYR A 1 2582 ? 169.995 206.459 192.026 1.00 20.51  ? 2582 TYR A CB    1 
ATOM   8858  C  CG    . TYR A 1 2582 ? 169.096 207.663 192.219 1.00 25.76  ? 2582 TYR A CG    1 
ATOM   8859  C  CD1   . TYR A 1 2582 ? 169.367 208.871 191.587 1.00 29.16  ? 2582 TYR A CD1   1 
ATOM   8860  C  CD2   . TYR A 1 2582 ? 167.981 207.594 193.041 1.00 27.07  ? 2582 TYR A CD2   1 
ATOM   8861  C  CE1   . TYR A 1 2582 ? 168.551 209.969 191.764 1.00 32.62  ? 2582 TYR A CE1   1 
ATOM   8862  C  CE2   . TYR A 1 2582 ? 167.160 208.688 193.225 1.00 31.46  ? 2582 TYR A CE2   1 
ATOM   8863  C  CZ    . TYR A 1 2582 ? 167.449 209.872 192.583 1.00 38.61  ? 2582 TYR A CZ    1 
ATOM   8864  O  OH    . TYR A 1 2582 ? 166.634 210.965 192.762 1.00 44.55  ? 2582 TYR A OH    1 
ATOM   8865  N  N     . THR A 1 2583 ? 171.058 206.615 189.024 1.00 16.86  ? 2583 THR A N     1 
ATOM   8866  C  CA    . THR A 1 2583 ? 171.270 207.352 187.782 1.00 18.62  ? 2583 THR A CA    1 
ATOM   8867  C  C     . THR A 1 2583 ? 170.568 206.677 186.610 1.00 19.39  ? 2583 THR A C     1 
ATOM   8868  O  O     . THR A 1 2583 ? 169.842 207.330 185.851 1.00 24.99  ? 2583 THR A O     1 
ATOM   8869  C  CB    . THR A 1 2583 ? 172.768 207.486 187.503 1.00 18.31  ? 2583 THR A CB    1 
ATOM   8870  O  OG1   . THR A 1 2583 ? 173.354 208.389 188.450 1.00 22.76  ? 2583 THR A OG1   1 
ATOM   8871  C  CG2   . THR A 1 2583 ? 173.008 208.004 186.095 1.00 16.06  ? 2583 THR A CG2   1 
ATOM   8872  N  N     . TRP A 1 2584 ? 170.748 205.360 186.484 1.00 15.80  ? 2584 TRP A N     1 
ATOM   8873  C  CA    . TRP A 1 2584 ? 170.135 204.617 185.352 1.00 12.51  ? 2584 TRP A CA    1 
ATOM   8874  C  C     . TRP A 1 2584 ? 168.620 204.506 185.538 1.00 14.04  ? 2584 TRP A C     1 
ATOM   8875  O  O     . TRP A 1 2584 ? 167.882 204.831 184.583 1.00 20.10  ? 2584 TRP A O     1 
ATOM   8876  C  CB    . TRP A 1 2584 ? 170.762 203.223 185.215 1.00 11.04  ? 2584 TRP A CB    1 
ATOM   8877  C  CG    . TRP A 1 2584 ? 172.173 203.215 184.688 1.00 13.26  ? 2584 TRP A CG    1 
ATOM   8878  C  CD1   . TRP A 1 2584 ? 172.827 204.230 184.055 1.00 16.54  ? 2584 TRP A CD1   1 
ATOM   8879  C  CD2   . TRP A 1 2584 ? 173.090 202.100 184.711 1.00 13.26  ? 2584 TRP A CD2   1 
ATOM   8880  N  NE1   . TRP A 1 2584 ? 174.092 203.838 183.708 1.00 14.09  ? 2584 TRP A NE1   1 
ATOM   8881  C  CE2   . TRP A 1 2584 ? 174.281 202.536 184.091 1.00 12.03  ? 2584 TRP A CE2   1 
ATOM   8882  C  CE3   . TRP A 1 2584 ? 173.024 200.790 185.197 1.00 14.59  ? 2584 TRP A CE3   1 
ATOM   8883  C  CZ2   . TRP A 1 2584 ? 175.389 201.705 183.948 1.00 16.73  ? 2584 TRP A CZ2   1 
ATOM   8884  C  CZ3   . TRP A 1 2584 ? 174.120 199.969 185.050 1.00 16.59  ? 2584 TRP A CZ3   1 
ATOM   8885  C  CH2   . TRP A 1 2584 ? 175.285 200.421 184.433 1.00 17.02  ? 2584 TRP A CH2   1 
ATOM   8886  N  N     . LEU A 1 2585 ? 168.170 204.063 186.715 1.00 14.93  ? 2585 LEU A N     1 
ATOM   8887  C  CA    . LEU A 1 2585 ? 166.718 203.841 186.953 1.00 13.47  ? 2585 LEU A CA    1 
ATOM   8888  C  C     . LEU A 1 2585 ? 165.936 205.142 186.716 1.00 17.72  ? 2585 LEU A C     1 
ATOM   8889  O  O     . LEU A 1 2585 ? 164.907 205.088 186.012 1.00 20.94  ? 2585 LEU A O     1 
ATOM   8890  C  CB    . LEU A 1 2585 ? 166.517 203.319 188.374 1.00 13.26  ? 2585 LEU A CB    1 
ATOM   8891  C  CG    . LEU A 1 2585 ? 167.042 201.907 188.649 1.00 13.11  ? 2585 LEU A CG    1 
ATOM   8892  C  CD1   . LEU A 1 2585 ? 167.345 201.721 190.124 1.00 13.19  ? 2585 LEU A CD1   1 
ATOM   8893  C  CD2   . LEU A 1 2585 ? 166.028 200.879 188.182 1.00 12.03  ? 2585 LEU A CD2   1 
ATOM   8894  N  N     . ALA A 1 2586 ? 166.404 206.257 187.284 1.00 18.93  ? 2586 ALA A N     1 
ATOM   8895  C  CA    . ALA A 1 2586 ? 165.691 207.549 187.138 1.00 18.40  ? 2586 ALA A CA    1 
ATOM   8896  C  C     . ALA A 1 2586 ? 165.407 207.811 185.660 1.00 19.25  ? 2586 ALA A C     1 
ATOM   8897  O  O     . ALA A 1 2586 ? 164.230 208.034 185.303 1.00 24.32  ? 2586 ALA A O     1 
ATOM   8898  C  CB    . ALA A 1 2586 ? 166.516 208.660 187.746 1.00 22.58  ? 2586 ALA A CB    1 
ATOM   8899  N  N     . GLU A 1 2587 ? 166.449 207.784 184.827 1.00 16.24  ? 2587 GLU A N     1 
ATOM   8900  C  CA    . GLU A 1 2587 ? 166.288 208.013 183.399 1.00 18.00  ? 2587 GLU A CA    1 
ATOM   8901  C  C     . GLU A 1 2587 ? 165.345 207.011 182.749 1.00 20.12  ? 2587 GLU A C     1 
ATOM   8902  O  O     . GLU A 1 2587 ? 165.115 207.097 181.539 1.00 22.40  ? 2587 GLU A O     1 
ATOM   8903  C  CB    . GLU A 1 2587 ? 167.650 207.961 182.700 1.00 22.46  ? 2587 GLU A CB    1 
ATOM   8904  C  CG    . GLU A 1 2587 ? 168.648 208.988 183.202 1.00 32.56  ? 2587 GLU A CG    1 
ATOM   8905  C  CD    . GLU A 1 2587 ? 168.293 210.400 182.786 1.00 37.88  ? 2587 GLU A CD    1 
ATOM   8906  O  OE1   . GLU A 1 2587 ? 167.727 210.573 181.686 1.00 36.97  ? 2587 GLU A OE1   1 
ATOM   8907  O  OE2   . GLU A 1 2587 ? 168.583 211.337 183.558 1.00 33.93  ? 2587 GLU A OE2   1 
ATOM   8908  N  N     . HIS A 1 2588 ? 164.810 206.063 183.524 1.00 17.23  ? 2588 HIS A N     1 
ATOM   8909  C  CA    . HIS A 1 2588 ? 163.940 205.002 183.014 1.00 13.63  ? 2588 HIS A CA    1 
ATOM   8910  C  C     . HIS A 1 2588 ? 164.647 204.159 181.959 1.00 15.09  ? 2588 HIS A C     1 
ATOM   8911  O  O     . HIS A 1 2588 ? 164.012 203.594 181.066 1.00 17.66  ? 2588 HIS A O     1 
ATOM   8912  C  CB    . HIS A 1 2588 ? 162.627 205.570 182.468 1.00 12.74  ? 2588 HIS A CB    1 
ATOM   8913  C  CG    . HIS A 1 2588 ? 161.950 206.521 183.404 1.00 15.27  ? 2588 HIS A CG    1 
ATOM   8914  N  ND1   . HIS A 1 2588 ? 161.643 206.189 184.706 1.00 17.96  ? 2588 HIS A ND1   1 
ATOM   8915  C  CD2   . HIS A 1 2588 ? 161.530 207.796 183.233 1.00 15.59  ? 2588 HIS A CD2   1 
ATOM   8916  C  CE1   . HIS A 1 2588 ? 161.057 207.217 185.294 1.00 16.51  ? 2588 HIS A CE1   1 
ATOM   8917  N  NE2   . HIS A 1 2588 ? 160.977 208.205 184.422 1.00 17.61  ? 2588 HIS A NE2   1 
ATOM   8918  N  N     . LYS A 1 2589 ? 165.965 204.076 182.061 1.00 14.96  ? 2589 LYS A N     1 
ATOM   8919  C  CA    . LYS A 1 2589 ? 166.757 203.261 181.151 1.00 12.23  ? 2589 LYS A CA    1 
ATOM   8920  C  C     . LYS A 1 2589 ? 166.825 201.830 181.671 1.00 13.34  ? 2589 LYS A C     1 
ATOM   8921  O  O     . LYS A 1 2589 ? 167.180 201.618 182.835 1.00 14.05  ? 2589 LYS A O     1 
ATOM   8922  C  CB    . LYS A 1 2589 ? 168.163 203.835 181.006 1.00 12.54  ? 2589 LYS A CB    1 
ATOM   8923  C  CG    . LYS A 1 2589 ? 169.080 203.036 180.096 1.00 15.49  ? 2589 LYS A CG    1 
ATOM   8924  C  CD    . LYS A 1 2589 ? 168.964 203.497 178.655 1.00 21.17  ? 2589 LYS A CD    1 
ATOM   8925  C  CE    . LYS A 1 2589 ? 170.110 202.961 177.815 1.00 19.37  ? 2589 LYS A CE    1 
ATOM   8926  N  NZ    . LYS A 1 2589 ? 169.896 203.199 176.363 1.00 21.72  ? 2589 LYS A NZ    1 
ATOM   8927  N  N     . PRO A 1 2590 ? 166.481 200.835 180.856 1.00 10.00  ? 2590 PRO A N     1 
ATOM   8928  C  CA    . PRO A 1 2590 ? 166.576 199.446 181.317 1.00 9.46   ? 2590 PRO A CA    1 
ATOM   8929  C  C     . PRO A 1 2590 ? 168.016 199.075 181.633 1.00 9.82   ? 2590 PRO A C     1 
ATOM   8930  O  O     . PRO A 1 2590 ? 168.953 199.526 180.972 1.00 10.20  ? 2590 PRO A O     1 
ATOM   8931  C  CB    . PRO A 1 2590 ? 166.028 198.644 180.134 1.00 7.23   ? 2590 PRO A CB    1 
ATOM   8932  C  CG    . PRO A 1 2590 ? 166.276 199.516 178.956 1.00 7.68   ? 2590 PRO A CG    1 
ATOM   8933  C  CD    . PRO A 1 2590 ? 166.074 200.919 179.444 1.00 8.14   ? 2590 PRO A CD    1 
ATOM   8934  N  N     . LEU A 1 2591 ? 168.188 198.241 182.656 1.00 7.91   ? 2591 LEU A N     1 
ATOM   8935  C  CA    . LEU A 1 2591 ? 169.513 197.900 183.149 1.00 5.86   ? 2591 LEU A CA    1 
ATOM   8936  C  C     . LEU A 1 2591 ? 169.544 196.438 183.565 1.00 8.08   ? 2591 LEU A C     1 
ATOM   8937  O  O     . LEU A 1 2591 ? 168.512 195.827 183.852 1.00 9.69   ? 2591 LEU A O     1 
ATOM   8938  C  CB    . LEU A 1 2591 ? 169.922 198.808 184.318 1.00 6.95   ? 2591 LEU A CB    1 
ATOM   8939  C  CG    . LEU A 1 2591 ? 169.053 198.778 185.577 1.00 5.74   ? 2591 LEU A CG    1 
ATOM   8940  C  CD1   . LEU A 1 2591 ? 169.610 197.818 186.617 1.00 10.25  ? 2591 LEU A CD1   1 
ATOM   8941  C  CD2   . LEU A 1 2591 ? 168.915 200.174 186.152 1.00 7.10   ? 2591 LEU A CD2   1 
ATOM   8942  N  N     . VAL A 1 2592 ? 170.753 195.884 183.598 1.00 8.03   ? 2592 VAL A N     1 
ATOM   8943  C  CA    . VAL A 1 2592 ? 170.975 194.480 183.921 1.00 6.40   ? 2592 VAL A CA    1 
ATOM   8944  C  C     . VAL A 1 2592 ? 171.998 194.389 185.044 1.00 7.20   ? 2592 VAL A C     1 
ATOM   8945  O  O     . VAL A 1 2592 ? 173.088 194.964 184.945 1.00 7.57   ? 2592 VAL A O     1 
ATOM   8946  C  CB    . VAL A 1 2592 ? 171.450 193.683 182.693 1.00 6.89   ? 2592 VAL A CB    1 
ATOM   8947  C  CG1   . VAL A 1 2592 ? 171.955 192.318 183.113 1.00 7.39   ? 2592 VAL A CG1   1 
ATOM   8948  C  CG2   . VAL A 1 2592 ? 170.324 193.551 181.682 1.00 10.49  ? 2592 VAL A CG2   1 
ATOM   8949  N  N     . LEU A 1 2593 ? 171.649 193.665 186.104 1.00 10.20  ? 2593 LEU A N     1 
ATOM   8950  C  CA    . LEU A 1 2593 ? 172.555 193.375 187.207 1.00 5.29   ? 2593 LEU A CA    1 
ATOM   8951  C  C     . LEU A 1 2593 ? 173.158 191.997 186.974 1.00 5.41   ? 2593 LEU A C     1 
ATOM   8952  O  O     . LEU A 1 2593 ? 172.429 191.004 186.901 1.00 9.34   ? 2593 LEU A O     1 
ATOM   8953  C  CB    . LEU A 1 2593 ? 171.820 193.415 188.546 1.00 6.91   ? 2593 LEU A CB    1 
ATOM   8954  C  CG    . LEU A 1 2593 ? 171.201 194.745 188.973 1.00 6.68   ? 2593 LEU A CG    1 
ATOM   8955  C  CD1   . LEU A 1 2593 ? 170.916 194.748 190.458 1.00 6.53   ? 2593 LEU A CD1   1 
ATOM   8956  C  CD2   . LEU A 1 2593 ? 172.109 195.895 188.618 1.00 8.13   ? 2593 LEU A CD2   1 
ATOM   8957  N  N     . CYS A 1 2594 ? 174.479 191.934 186.858 1.00 5.87   ? 2594 CYS A N     1 
ATOM   8958  C  CA    . CYS A 1 2594 ? 175.169 190.680 186.601 1.00 5.80   ? 2594 CYS A CA    1 
ATOM   8959  C  C     . CYS A 1 2594 ? 176.150 190.387 187.727 1.00 7.44   ? 2594 CYS A C     1 
ATOM   8960  O  O     . CYS A 1 2594 ? 176.827 191.290 188.227 1.00 13.93  ? 2594 CYS A O     1 
ATOM   8961  C  CB    . CYS A 1 2594 ? 175.903 190.718 185.259 1.00 6.96   ? 2594 CYS A CB    1 
ATOM   8962  S  SG    . CYS A 1 2594 ? 176.613 189.132 184.766 1.00 13.69  ? 2594 CYS A SG    1 
ATOM   8963  N  N     . GLY A 1 2595 ? 176.214 189.121 188.127 1.00 6.06   ? 2595 GLY A N     1 
ATOM   8964  C  CA    . GLY A 1 2595 ? 177.115 188.696 189.168 1.00 5.62   ? 2595 GLY A CA    1 
ATOM   8965  C  C     . GLY A 1 2595 ? 176.797 187.298 189.652 1.00 7.85   ? 2595 GLY A C     1 
ATOM   8966  O  O     . GLY A 1 2595 ? 175.813 186.681 189.235 1.00 8.05   ? 2595 GLY A O     1 
ATOM   8967  N  N     . PRO A 1 2596 ? 177.628 186.771 190.548 1.00 10.04  ? 2596 PRO A N     1 
ATOM   8968  C  CA    . PRO A 1 2596 ? 177.376 185.437 191.072 1.00 6.99   ? 2596 PRO A CA    1 
ATOM   8969  C  C     . PRO A 1 2596 ? 176.102 185.427 191.907 1.00 8.52   ? 2596 PRO A C     1 
ATOM   8970  O  O     . PRO A 1 2596 ? 175.700 186.466 192.457 1.00 9.65   ? 2596 PRO A O     1 
ATOM   8971  C  CB    . PRO A 1 2596 ? 178.614 185.154 191.933 1.00 7.24   ? 2596 PRO A CB    1 
ATOM   8972  C  CG    . PRO A 1 2596 ? 179.649 186.125 191.460 1.00 7.85   ? 2596 PRO A CG    1 
ATOM   8973  C  CD    . PRO A 1 2596 ? 178.881 187.340 191.069 1.00 9.72   ? 2596 PRO A CD    1 
ATOM   8974  N  N     . PRO A 1 2597 ? 175.435 184.280 191.999 1.00 8.93   ? 2597 PRO A N     1 
ATOM   8975  C  CA    . PRO A 1 2597 ? 174.211 184.214 192.808 1.00 9.77   ? 2597 PRO A CA    1 
ATOM   8976  C  C     . PRO A 1 2597 ? 174.490 184.552 194.265 1.00 7.11   ? 2597 PRO A C     1 
ATOM   8977  O  O     . PRO A 1 2597 ? 175.490 184.124 194.842 1.00 11.66  ? 2597 PRO A O     1 
ATOM   8978  C  CB    . PRO A 1 2597 ? 173.753 182.759 192.643 1.00 8.01   ? 2597 PRO A CB    1 
ATOM   8979  C  CG    . PRO A 1 2597 ? 174.975 182.018 192.206 1.00 7.37   ? 2597 PRO A CG    1 
ATOM   8980  C  CD    . PRO A 1 2597 ? 175.762 182.985 191.383 1.00 7.84   ? 2597 PRO A CD    1 
ATOM   8981  N  N     . GLY A 1 2598 ? 173.587 185.329 194.858 1.00 6.70   ? 2598 GLY A N     1 
ATOM   8982  C  CA    . GLY A 1 2598 ? 173.746 185.758 196.230 1.00 5.68   ? 2598 GLY A CA    1 
ATOM   8983  C  C     . GLY A 1 2598 ? 174.724 186.890 196.441 1.00 7.31   ? 2598 GLY A C     1 
ATOM   8984  O  O     . GLY A 1 2598 ? 175.035 187.208 197.594 1.00 10.99  ? 2598 GLY A O     1 
ATOM   8985  N  N     . SER A 1 2599 ? 175.222 187.509 195.368 1.00 8.09   ? 2599 SER A N     1 
ATOM   8986  C  CA    . SER A 1 2599 ? 176.209 188.572 195.524 1.00 8.15   ? 2599 SER A CA    1 
ATOM   8987  C  C     . SER A 1 2599 ? 175.581 189.854 196.052 1.00 9.76   ? 2599 SER A C     1 
ATOM   8988  O  O     . SER A 1 2599 ? 176.272 190.667 196.676 1.00 15.38  ? 2599 SER A O     1 
ATOM   8989  C  CB    . SER A 1 2599 ? 176.915 188.837 194.195 1.00 8.58   ? 2599 SER A CB    1 
ATOM   8990  O  OG    . SER A 1 2599 ? 176.011 189.338 193.226 1.00 8.80   ? 2599 SER A OG    1 
ATOM   8991  N  N     . GLY A 1 2600 ? 174.288 190.054 195.819 1.00 5.25   ? 2600 GLY A N     1 
ATOM   8992  C  CA    . GLY A 1 2600 ? 173.616 191.234 196.324 1.00 6.54   ? 2600 GLY A CA    1 
ATOM   8993  C  C     . GLY A 1 2600 ? 172.943 192.063 195.251 1.00 6.41   ? 2600 GLY A C     1 
ATOM   8994  O  O     . GLY A 1 2600 ? 172.681 193.252 195.456 1.00 5.99   ? 2600 GLY A O     1 
ATOM   8995  N  N     . LYS A 1 2601 ? 172.662 191.449 194.100 1.00 5.28   ? 2601 LYS A N     1 
ATOM   8996  C  CA    . LYS A 1 2601 ? 171.986 192.167 193.025 1.00 4.95   ? 2601 LYS A CA    1 
ATOM   8997  C  C     . LYS A 1 2601 ? 170.578 192.575 193.439 1.00 6.31   ? 2601 LYS A C     1 
ATOM   8998  O  O     . LYS A 1 2601 ? 170.198 193.746 193.322 1.00 8.84   ? 2601 LYS A O     1 
ATOM   8999  C  CB    . LYS A 1 2601 ? 171.949 191.307 191.762 1.00 5.62   ? 2601 LYS A CB    1 
ATOM   9000  C  CG    . LYS A 1 2601 ? 173.318 190.886 191.259 1.00 4.65   ? 2601 LYS A CG    1 
ATOM   9001  C  CD    . LYS A 1 2601 ? 173.203 190.002 190.033 1.00 5.59   ? 2601 LYS A CD    1 
ATOM   9002  C  CE    . LYS A 1 2601 ? 172.627 188.643 190.384 1.00 6.91   ? 2601 LYS A CE    1 
ATOM   9003  N  NZ    . LYS A 1 2601 ? 173.517 187.884 191.304 1.00 5.58   ? 2601 LYS A NZ    1 
ATOM   9004  N  N     . THR A 1 2602 ? 169.788 191.620 193.936 1.00 6.52   ? 2602 THR A N     1 
ATOM   9005  C  CA    . THR A 1 2602 ? 168.437 191.942 194.385 1.00 6.53   ? 2602 THR A CA    1 
ATOM   9006  C  C     . THR A 1 2602 ? 168.468 192.914 195.557 1.00 6.99   ? 2602 THR A C     1 
ATOM   9007  O  O     . THR A 1 2602 ? 167.640 193.829 195.638 1.00 7.91   ? 2602 THR A O     1 
ATOM   9008  C  CB    . THR A 1 2602 ? 167.692 190.663 194.768 1.00 6.22   ? 2602 THR A CB    1 
ATOM   9009  O  OG1   . THR A 1 2602 ? 167.744 189.735 193.678 1.00 12.03  ? 2602 THR A OG1   1 
ATOM   9010  C  CG2   . THR A 1 2602 ? 166.242 190.966 195.093 1.00 7.32   ? 2602 THR A CG2   1 
ATOM   9011  N  N     . MET A 1 2603 ? 169.422 192.733 196.471 1.00 6.31   ? 2603 MET A N     1 
ATOM   9012  C  CA    . MET A 1 2603 ? 169.529 193.613 197.629 1.00 5.35   ? 2603 MET A CA    1 
ATOM   9013  C  C     . MET A 1 2603 ? 169.848 195.044 197.209 1.00 6.21   ? 2603 MET A C     1 
ATOM   9014  O  O     . MET A 1 2603 ? 169.296 196.003 197.760 1.00 7.97   ? 2603 MET A O     1 
ATOM   9015  C  CB    . MET A 1 2603 ? 170.595 193.076 198.584 1.00 6.87   ? 2603 MET A CB    1 
ATOM   9016  C  CG    . MET A 1 2603 ? 170.712 193.838 199.886 1.00 8.97   ? 2603 MET A CG    1 
ATOM   9017  S  SD    . MET A 1 2603 ? 172.399 193.873 200.519 1.00 12.15  ? 2603 MET A SD    1 
ATOM   9018  C  CE    . MET A 1 2603 ? 173.259 194.680 199.170 1.00 6.63   ? 2603 MET A CE    1 
ATOM   9019  N  N     . THR A 1 2604 ? 170.742 195.206 196.231 1.00 7.10   ? 2604 THR A N     1 
ATOM   9020  C  CA    . THR A 1 2604 ? 171.150 196.546 195.819 1.00 8.43   ? 2604 THR A CA    1 
ATOM   9021  C  C     . THR A 1 2604 ? 170.026 197.276 195.094 1.00 9.12   ? 2604 THR A C     1 
ATOM   9022  O  O     . THR A 1 2604 ? 169.817 198.476 195.309 1.00 10.93  ? 2604 THR A O     1 
ATOM   9023  C  CB    . THR A 1 2604 ? 172.393 196.468 194.932 1.00 8.36   ? 2604 THR A CB    1 
ATOM   9024  O  OG1   . THR A 1 2604 ? 173.405 195.699 195.593 1.00 12.68  ? 2604 THR A OG1   1 
ATOM   9025  C  CG2   . THR A 1 2604 ? 172.932 197.860 194.649 1.00 9.12   ? 2604 THR A CG2   1 
ATOM   9026  N  N     . LEU A 1 2605 ? 169.295 196.573 194.225 1.00 9.31   ? 2605 LEU A N     1 
ATOM   9027  C  CA    . LEU A 1 2605 ? 168.238 197.224 193.457 1.00 7.91   ? 2605 LEU A CA    1 
ATOM   9028  C  C     . LEU A 1 2605 ? 167.119 197.724 194.362 1.00 11.24  ? 2605 LEU A C     1 
ATOM   9029  O  O     . LEU A 1 2605 ? 166.633 198.849 194.195 1.00 14.37  ? 2605 LEU A O     1 
ATOM   9030  C  CB    . LEU A 1 2605 ? 167.687 196.264 192.404 1.00 8.90   ? 2605 LEU A CB    1 
ATOM   9031  C  CG    . LEU A 1 2605 ? 166.469 196.778 191.636 1.00 12.93  ? 2605 LEU A CG    1 
ATOM   9032  C  CD1   . LEU A 1 2605 ? 166.894 197.768 190.566 1.00 10.55  ? 2605 LEU A CD1   1 
ATOM   9033  C  CD2   . LEU A 1 2605 ? 165.688 195.627 191.032 1.00 12.91  ? 2605 LEU A CD2   1 
ATOM   9034  N  N     . PHE A 1 2606 ? 166.697 196.903 195.326 1.00 11.36  ? 2606 PHE A N     1 
ATOM   9035  C  CA    . PHE A 1 2606 ? 165.660 197.333 196.259 1.00 11.26  ? 2606 PHE A CA    1 
ATOM   9036  C  C     . PHE A 1 2606 ? 166.141 198.490 197.124 1.00 13.24  ? 2606 PHE A C     1 
ATOM   9037  O  O     . PHE A 1 2606 ? 165.370 199.407 197.428 1.00 18.59  ? 2606 PHE A O     1 
ATOM   9038  C  CB    . PHE A 1 2606 ? 165.209 196.158 197.124 1.00 13.25  ? 2606 PHE A CB    1 
ATOM   9039  C  CG    . PHE A 1 2606 ? 164.189 195.274 196.463 1.00 15.20  ? 2606 PHE A CG    1 
ATOM   9040  C  CD1   . PHE A 1 2606 ? 162.855 195.641 196.435 1.00 20.05  ? 2606 PHE A CD1   1 
ATOM   9041  C  CD2   . PHE A 1 2606 ? 164.562 194.084 195.866 1.00 13.08  ? 2606 PHE A CD2   1 
ATOM   9042  C  CE1   . PHE A 1 2606 ? 161.912 194.834 195.831 1.00 24.21  ? 2606 PHE A CE1   1 
ATOM   9043  C  CE2   . PHE A 1 2606 ? 163.623 193.273 195.257 1.00 16.36  ? 2606 PHE A CE2   1 
ATOM   9044  C  CZ    . PHE A 1 2606 ? 162.297 193.649 195.240 1.00 20.80  ? 2606 PHE A CZ    1 
ATOM   9045  N  N     . SER A 1 2607 ? 167.411 198.465 197.531 1.00 12.41  ? 2607 SER A N     1 
ATOM   9046  C  CA    . SER A 1 2607 ? 167.957 199.575 198.303 1.00 11.95  ? 2607 SER A CA    1 
ATOM   9047  C  C     . SER A 1 2607 ? 168.053 200.838 197.456 1.00 15.61  ? 2607 SER A C     1 
ATOM   9048  O  O     . SER A 1 2607 ? 167.854 201.950 197.959 1.00 21.15  ? 2607 SER A O     1 
ATOM   9049  C  CB    . SER A 1 2607 ? 169.325 199.197 198.867 1.00 14.66  ? 2607 SER A CB    1 
ATOM   9050  O  OG    . SER A 1 2607 ? 169.828 200.218 199.711 1.00 26.31  ? 2607 SER A OG    1 
ATOM   9051  N  N     . ALA A 1 2608 ? 168.340 200.667 196.163 1.00 17.98  ? 2608 ALA A N     1 
ATOM   9052  C  CA    . ALA A 1 2608 ? 168.424 201.830 195.246 1.00 14.15  ? 2608 ALA A CA    1 
ATOM   9053  C  C     . ALA A 1 2608 ? 167.015 202.306 194.891 1.00 14.27  ? 2608 ALA A C     1 
ATOM   9054  O  O     . ALA A 1 2608 ? 166.827 203.521 194.673 1.00 19.53  ? 2608 ALA A O     1 
ATOM   9055  C  CB    . ALA A 1 2608 ? 169.210 201.454 194.010 1.00 17.76  ? 2608 ALA A CB    1 
ATOM   9056  N  N     . LEU A 1 2609 ? 166.055 201.378 194.839 1.00 16.16  ? 2609 LEU A N     1 
ATOM   9057  C  CA    . LEU A 1 2609 ? 164.653 201.731 194.491 1.00 16.27  ? 2609 LEU A CA    1 
ATOM   9058  C  C     . LEU A 1 2609 ? 164.046 202.585 195.614 1.00 21.47  ? 2609 LEU A C     1 
ATOM   9059  O  O     . LEU A 1 2609 ? 163.056 203.296 195.346 1.00 25.09  ? 2609 LEU A O     1 
ATOM   9060  C  CB    . LEU A 1 2609 ? 163.843 200.458 194.253 1.00 16.93  ? 2609 LEU A CB    1 
ATOM   9061  C  CG    . LEU A 1 2609 ? 163.634 200.059 192.789 1.00 16.03  ? 2609 LEU A CG    1 
ATOM   9062  C  CD1   . LEU A 1 2609 ? 164.886 200.327 191.976 1.00 17.03  ? 2609 LEU A CD1   1 
ATOM   9063  C  CD2   . LEU A 1 2609 ? 163.246 198.595 192.692 1.00 14.31  ? 2609 LEU A CD2   1 
ATOM   9064  N  N     . ARG A 1 2610 ? 164.619 202.510 196.818 1.00 26.70  ? 2610 ARG A N     1 
ATOM   9065  C  CA    . ARG A 1 2610 ? 164.105 203.300 197.968 1.00 26.13  ? 2610 ARG A CA    1 
ATOM   9066  C  C     . ARG A 1 2610 ? 164.179 204.794 197.621 1.00 26.62  ? 2610 ARG A C     1 
ATOM   9067  O  O     . ARG A 1 2610 ? 163.243 205.535 197.991 1.00 31.90  ? 2610 ARG A O     1 
ATOM   9068  C  CB    . ARG A 1 2610 ? 164.916 202.995 199.232 1.00 21.59  ? 2610 ARG A CB    1 
ATOM   9069  C  CG    . ARG A 1 2610 ? 165.078 201.507 199.509 1.00 26.95  ? 2610 ARG A CG    1 
ATOM   9070  C  CD    . ARG A 1 2610 ? 165.738 201.225 200.849 1.00 26.99  ? 2610 ARG A CD    1 
ATOM   9071  N  NE    . ARG A 1 2610 ? 166.286 199.866 200.929 1.00 23.57  ? 2610 ARG A NE    1 
ATOM   9072  C  CZ    . ARG A 1 2610 ? 165.590 198.745 200.779 1.00 26.77  ? 2610 ARG A CZ    1 
ATOM   9073  N  NH1   . ARG A 1 2610 ? 164.270 198.777 200.764 1.00 22.58  ? 2610 ARG A NH1   1 
ATOM   9074  N  NH2   . ARG A 1 2610 ? 166.221 197.592 200.647 1.00 25.90  ? 2610 ARG A NH2   1 
ATOM   9075  N  N     . ALA A 1 2611 ? 165.243 205.209 196.928 1.00 24.78  ? 2611 ALA A N     1 
ATOM   9076  C  CA    . ALA A 1 2611 ? 165.409 206.631 196.544 1.00 30.99  ? 2611 ALA A CA    1 
ATOM   9077  C  C     . ALA A 1 2611 ? 164.467 206.961 195.384 1.00 36.40  ? 2611 ALA A C     1 
ATOM   9078  O  O     . ALA A 1 2611 ? 164.480 208.117 194.907 1.00 40.29  ? 2611 ALA A O     1 
ATOM   9079  C  CB    . ALA A 1 2611 ? 166.852 206.897 196.183 1.00 23.51  ? 2611 ALA A CB    1 
ATOM   9080  N  N     . LEU A 1 2612 ? 163.680 205.976 194.941 1.00 37.17  ? 2612 LEU A N     1 
ATOM   9081  C  CA    . LEU A 1 2612 ? 162.721 206.188 193.826 1.00 32.92  ? 2612 LEU A CA    1 
ATOM   9082  C  C     . LEU A 1 2612 ? 161.307 205.850 194.320 1.00 36.87  ? 2612 LEU A C     1 
ATOM   9083  O  O     . LEU A 1 2612 ? 160.829 204.731 194.033 1.00 37.35  ? 2612 LEU A O     1 
ATOM   9084  C  CB    . LEU A 1 2612 ? 163.154 205.299 192.664 1.00 29.35  ? 2612 LEU A CB    1 
ATOM   9085  C  CG    . LEU A 1 2612 ? 164.631 205.399 192.270 1.00 26.85  ? 2612 LEU A CG    1 
ATOM   9086  C  CD1   . LEU A 1 2612 ? 165.083 204.157 191.522 1.00 24.34  ? 2612 LEU A CD1   1 
ATOM   9087  C  CD2   . LEU A 1 2612 ? 164.877 206.643 191.435 1.00 28.86  ? 2612 LEU A CD2   1 
ATOM   9088  N  N     . PRO A 1 2613 ? 160.618 206.761 195.042 1.00 41.62  ? 2613 PRO A N     1 
ATOM   9089  C  CA    . PRO A 1 2613 ? 159.308 206.451 195.609 1.00 40.92  ? 2613 PRO A CA    1 
ATOM   9090  C  C     . PRO A 1 2613 ? 158.207 206.203 194.584 1.00 42.68  ? 2613 PRO A C     1 
ATOM   9091  O  O     . PRO A 1 2613 ? 157.381 205.293 194.798 1.00 40.52  ? 2613 PRO A O     1 
ATOM   9092  C  CB    . PRO A 1 2613 ? 159.022 207.698 196.467 1.00 39.86  ? 2613 PRO A CB    1 
ATOM   9093  C  CG    . PRO A 1 2613 ? 159.798 208.798 195.783 1.00 41.71  ? 2613 PRO A CG    1 
ATOM   9094  C  CD    . PRO A 1 2613 ? 161.071 208.112 195.323 1.00 38.97  ? 2613 PRO A CD    1 
ATOM   9095  N  N     . ASP A 1 2614 ? 158.188 206.984 193.500 1.00 43.75  ? 2614 ASP A N     1 
ATOM   9096  C  CA    . ASP A 1 2614 ? 157.107 206.858 192.482 1.00 41.75  ? 2614 ASP A CA    1 
ATOM   9097  C  C     . ASP A 1 2614 ? 157.285 205.559 191.691 1.00 35.32  ? 2614 ASP A C     1 
ATOM   9098  O  O     . ASP A 1 2614 ? 156.389 205.231 190.884 1.00 34.89  ? 2614 ASP A O     1 
ATOM   9099  C  CB    . ASP A 1 2614 ? 157.058 208.080 191.578 1.00 47.49  ? 2614 ASP A CB    1 
ATOM   9100  C  CG    . ASP A 1 2614 ? 156.725 209.389 192.278 1.00 59.39  ? 2614 ASP A CG    1 
ATOM   9101  O  OD1   . ASP A 1 2614 ? 155.622 209.479 192.857 1.00 58.46  ? 2614 ASP A OD1   1 
ATOM   9102  O  OD2   . ASP A 1 2614 ? 157.575 210.303 192.245 1.00 67.36  ? 2614 ASP A OD2   1 
ATOM   9103  N  N     . MET A 1 2615 ? 158.397 204.852 191.908 1.00 37.54  ? 2615 MET A N     1 
ATOM   9104  C  CA    . MET A 1 2615 ? 158.673 203.614 191.132 1.00 29.43  ? 2615 MET A CA    1 
ATOM   9105  C  C     . MET A 1 2615 ? 158.170 202.390 191.913 1.00 27.12  ? 2615 MET A C     1 
ATOM   9106  O  O     . MET A 1 2615 ? 158.619 202.196 193.063 1.00 31.34  ? 2615 MET A O     1 
ATOM   9107  C  CB    . MET A 1 2615 ? 160.171 203.480 190.836 1.00 25.85  ? 2615 MET A CB    1 
ATOM   9108  C  CG    . MET A 1 2615 ? 160.723 204.609 189.986 1.00 31.75  ? 2615 MET A CG    1 
ATOM   9109  S  SD    . MET A 1 2615 ? 162.379 204.283 189.351 1.00 44.44  ? 2615 MET A SD    1 
ATOM   9110  C  CE    . MET A 1 2615 ? 162.642 205.743 188.335 1.00 27.20  ? 2615 MET A CE    1 
ATOM   9111  N  N     . GLU A 1 2616 ? 157.268 201.607 191.312 1.00 24.02  ? 2616 GLU A N     1 
ATOM   9112  C  CA    . GLU A 1 2616 ? 156.762 200.369 191.960 1.00 22.07  ? 2616 GLU A CA    1 
ATOM   9113  C  C     . GLU A 1 2616 ? 157.396 199.168 191.245 1.00 17.69  ? 2616 GLU A C     1 
ATOM   9114  O  O     . GLU A 1 2616 ? 157.306 199.117 190.002 1.00 14.00  ? 2616 GLU A O     1 
ATOM   9115  C  CB    . GLU A 1 2616 ? 155.236 200.320 191.888 1.00 26.72  ? 2616 GLU A CB    1 
ATOM   9116  C  CG    . GLU A 1 2616 ? 154.583 201.681 192.110 1.00 40.45  ? 2616 GLU A CG    1 
ATOM   9117  C  CD    . GLU A 1 2616 ? 154.991 202.353 193.408 1.00 43.80  ? 2616 GLU A CD    1 
ATOM   9118  O  OE1   . GLU A 1 2616 ? 154.715 201.780 194.482 1.00 48.98  ? 2616 GLU A OE1   1 
ATOM   9119  O  OE2   . GLU A 1 2616 ? 155.593 203.445 193.343 1.00 35.58  ? 2616 GLU A OE2   1 
ATOM   9120  N  N     . VAL A 1 2617 ? 158.003 198.242 191.992 1.00 17.16  ? 2617 VAL A N     1 
ATOM   9121  C  CA    . VAL A 1 2617 ? 158.734 197.112 191.339 1.00 11.64  ? 2617 VAL A CA    1 
ATOM   9122  C  C     . VAL A 1 2617 ? 157.914 195.815 191.431 1.00 11.67  ? 2617 VAL A C     1 
ATOM   9123  O  O     . VAL A 1 2617 ? 157.371 195.533 192.520 1.00 12.60  ? 2617 VAL A O     1 
ATOM   9124  C  CB    . VAL A 1 2617 ? 160.133 196.921 191.955 1.00 10.68  ? 2617 VAL A CB    1 
ATOM   9125  C  CG1   . VAL A 1 2617 ? 160.075 196.778 193.471 1.00 14.77  ? 2617 VAL A CG1   1 
ATOM   9126  C  CG2   . VAL A 1 2617 ? 160.871 195.743 191.329 1.00 10.89  ? 2617 VAL A CG2   1 
ATOM   9127  N  N     . VAL A 1 2618 ? 157.824 195.068 190.327 1.00 12.77  ? 2618 VAL A N     1 
ATOM   9128  C  CA    . VAL A 1 2618 ? 157.134 193.743 190.342 1.00 10.93  ? 2618 VAL A CA    1 
ATOM   9129  C  C     . VAL A 1 2618 ? 158.192 192.686 189.996 1.00 10.40  ? 2618 VAL A C     1 
ATOM   9130  O  O     . VAL A 1 2618 ? 158.909 192.884 188.990 1.00 11.79  ? 2618 VAL A O     1 
ATOM   9131  C  CB    . VAL A 1 2618 ? 155.937 193.681 189.374 1.00 12.67  ? 2618 VAL A CB    1 
ATOM   9132  C  CG1   . VAL A 1 2618 ? 155.479 192.249 189.126 1.00 15.27  ? 2618 VAL A CG1   1 
ATOM   9133  C  CG2   . VAL A 1 2618 ? 154.776 194.544 189.852 1.00 12.56  ? 2618 VAL A CG2   1 
ATOM   9134  N  N     . GLY A 1 2619 ? 158.296 191.620 190.794 1.00 12.79  ? 2619 GLY A N     1 
ATOM   9135  C  CA    . GLY A 1 2619 ? 159.327 190.627 190.570 1.00 9.85   ? 2619 GLY A CA    1 
ATOM   9136  C  C     . GLY A 1 2619 ? 158.888 189.463 189.708 1.00 10.71  ? 2619 GLY A C     1 
ATOM   9137  O  O     . GLY A 1 2619 ? 157.887 188.803 190.002 1.00 16.18  ? 2619 GLY A O     1 
ATOM   9138  N  N     . LEU A 1 2620 ? 159.632 189.204 188.638 1.00 11.89  ? 2620 LEU A N     1 
ATOM   9139  C  CA    . LEU A 1 2620 ? 159.390 188.071 187.758 1.00 11.73  ? 2620 LEU A CA    1 
ATOM   9140  C  C     . LEU A 1 2620 ? 160.606 187.157 187.771 1.00 12.34  ? 2620 LEU A C     1 
ATOM   9141  O  O     . LEU A 1 2620 ? 161.743 187.619 187.634 1.00 15.44  ? 2620 LEU A O     1 
ATOM   9142  C  CB    . LEU A 1 2620 ? 159.088 188.517 186.321 1.00 10.94  ? 2620 LEU A CB    1 
ATOM   9143  C  CG    . LEU A 1 2620 ? 157.999 189.556 186.023 1.00 12.87  ? 2620 LEU A CG    1 
ATOM   9144  C  CD1   . LEU A 1 2620 ? 158.433 190.981 186.349 1.00 11.16  ? 2620 LEU A CD1   1 
ATOM   9145  C  CD2   . LEU A 1 2620 ? 157.562 189.451 184.570 1.00 16.77  ? 2620 LEU A CD2   1 
ATOM   9146  N  N     . ASN A 1 2621 ? 160.364 185.861 187.934 1.00 13.98  ? 2621 ASN A N     1 
ATOM   9147  C  CA    . ASN A 1 2621 ? 161.427 184.866 188.045 1.00 14.31  ? 2621 ASN A CA    1 
ATOM   9148  C  C     . ASN A 1 2621 ? 161.466 184.059 186.752 1.00 13.52  ? 2621 ASN A C     1 
ATOM   9149  O  O     . ASN A 1 2621 ? 160.646 183.158 186.548 1.00 16.39  ? 2621 ASN A O     1 
ATOM   9150  C  CB    . ASN A 1 2621 ? 161.209 183.973 189.261 1.00 18.07  ? 2621 ASN A CB    1 
ATOM   9151  C  CG    . ASN A 1 2621 ? 160.847 184.762 190.501 1.00 21.60  ? 2621 ASN A CG    1 
ATOM   9152  O  OD1   . ASN A 1 2621 ? 159.673 184.894 190.846 1.00 27.05  ? 2621 ASN A OD1   1 
ATOM   9153  N  ND2   . ASN A 1 2621 ? 161.856 185.299 191.175 1.00 19.61  ? 2621 ASN A ND2   1 
ATOM   9154  N  N     . PHE A 1 2622 ? 162.417 184.388 185.883 1.00 12.83  ? 2622 PHE A N     1 
ATOM   9155  C  CA    . PHE A 1 2622 ? 162.563 183.676 184.623 1.00 10.02  ? 2622 PHE A CA    1 
ATOM   9156  C  C     . PHE A 1 2622 ? 163.105 182.270 184.851 1.00 11.54  ? 2622 PHE A C     1 
ATOM   9157  O  O     . PHE A 1 2622 ? 163.870 182.014 185.784 1.00 16.54  ? 2622 PHE A O     1 
ATOM   9158  C  CB    . PHE A 1 2622 ? 163.489 184.437 183.674 1.00 8.49   ? 2622 PHE A CB    1 
ATOM   9159  C  CG    . PHE A 1 2622 ? 162.837 185.602 182.985 1.00 8.96   ? 2622 PHE A CG    1 
ATOM   9160  C  CD1   . PHE A 1 2622 ? 161.657 186.146 183.464 1.00 11.64  ? 2622 PHE A CD1   1 
ATOM   9161  C  CD2   . PHE A 1 2622 ? 163.404 186.146 181.846 1.00 8.80   ? 2622 PHE A CD2   1 
ATOM   9162  C  CE1   . PHE A 1 2622 ? 161.061 187.212 182.822 1.00 12.68  ? 2622 PHE A CE1   1 
ATOM   9163  C  CE2   . PHE A 1 2622 ? 162.813 187.211 181.201 1.00 8.86   ? 2622 PHE A CE2   1 
ATOM   9164  C  CZ    . PHE A 1 2622 ? 161.640 187.745 181.689 1.00 9.83   ? 2622 PHE A CZ    1 
ATOM   9165  N  N     . SER A 1 2623 ? 162.689 181.353 183.985 1.00 9.81   ? 2623 SER A N     1 
ATOM   9166  C  CA    . SER A 1 2623 ? 163.188 179.988 183.971 1.00 10.81  ? 2623 SER A CA    1 
ATOM   9167  C  C     . SER A 1 2623 ? 163.538 179.614 182.537 1.00 14.31  ? 2623 SER A C     1 
ATOM   9168  O  O     . SER A 1 2623 ? 163.494 180.446 181.626 1.00 14.20  ? 2623 SER A O     1 
ATOM   9169  C  CB    . SER A 1 2623 ? 162.160 179.016 184.563 1.00 14.83  ? 2623 SER A CB    1 
ATOM   9170  O  OG    . SER A 1 2623 ? 160.958 179.027 183.815 1.00 19.41  ? 2623 SER A OG    1 
ATOM   9171  N  N     . SER A 1 2624 ? 163.895 178.343 182.339 1.00 15.55  ? 2624 SER A N     1 
ATOM   9172  C  CA    . SER A 1 2624 ? 164.207 177.868 180.996 1.00 13.44  ? 2624 SER A CA    1 
ATOM   9173  C  C     . SER A 1 2624 ? 162.977 177.877 180.098 1.00 17.29  ? 2624 SER A C     1 
ATOM   9174  O  O     . SER A 1 2624 ? 163.098 178.070 178.883 1.00 22.96  ? 2624 SER A O     1 
ATOM   9175  C  CB    . SER A 1 2624 ? 164.808 176.464 181.063 1.00 18.26  ? 2624 SER A CB    1 
ATOM   9176  O  OG    . SER A 1 2624 ? 163.803 175.489 181.284 1.00 18.79  ? 2624 SER A OG    1 
ATOM   9177  N  N     . ALA A 1 2625 ? 161.792 177.678 180.671 1.00 15.90  ? 2625 ALA A N     1 
ATOM   9178  C  CA    . ALA A 1 2625 ? 160.550 177.614 179.914 1.00 14.25  ? 2625 ALA A CA    1 
ATOM   9179  C  C     . ALA A 1 2625 ? 159.828 178.953 179.849 1.00 17.90  ? 2625 ALA A C     1 
ATOM   9180  O  O     . ALA A 1 2625 ? 158.679 179.004 179.399 1.00 20.62  ? 2625 ALA A O     1 
ATOM   9181  C  CB    . ALA A 1 2625 ? 159.624 176.553 180.509 1.00 15.90  ? 2625 ALA A CB    1 
ATOM   9182  N  N     . THR A 1 2626 ? 160.468 180.033 180.290 1.00 19.87  ? 2626 THR A N     1 
ATOM   9183  C  CA    . THR A 1 2626 ? 159.820 181.336 180.298 1.00 14.63  ? 2626 THR A CA    1 
ATOM   9184  C  C     . THR A 1 2626 ? 159.625 181.846 178.875 1.00 19.85  ? 2626 THR A C     1 
ATOM   9185  O  O     . THR A 1 2626 ? 160.560 181.852 178.069 1.00 24.28  ? 2626 THR A O     1 
ATOM   9186  C  CB    . THR A 1 2626 ? 160.644 182.335 181.109 1.00 12.20  ? 2626 THR A CB    1 
ATOM   9187  O  OG1   . THR A 1 2626 ? 160.674 181.926 182.482 1.00 18.97  ? 2626 THR A OG1   1 
ATOM   9188  C  CG2   . THR A 1 2626 ? 160.044 183.729 181.017 1.00 12.54  ? 2626 THR A CG2   1 
ATOM   9189  N  N     . THR A 1 2627 ? 158.407 182.274 178.576 1.00 19.99  ? 2627 THR A N     1 
ATOM   9190  C  CA    . THR A 1 2627 ? 158.018 182.848 177.297 1.00 12.79  ? 2627 THR A CA    1 
ATOM   9191  C  C     . THR A 1 2627 ? 157.438 184.227 177.554 1.00 14.04  ? 2627 THR A C     1 
ATOM   9192  O  O     . THR A 1 2627 ? 157.186 184.599 178.704 1.00 14.15  ? 2627 THR A O     1 
ATOM   9193  C  CB    . THR A 1 2627 ? 156.988 181.949 176.589 1.00 17.06  ? 2627 THR A CB    1 
ATOM   9194  O  OG1   . THR A 1 2627 ? 155.782 181.897 177.362 1.00 20.95  ? 2627 THR A OG1   1 
ATOM   9195  C  CG2   . THR A 1 2627 ? 157.536 180.541 176.410 1.00 20.33  ? 2627 THR A CG2   1 
ATOM   9196  N  N     . PRO A 1 2628 ? 157.224 185.028 176.502 1.00 14.09  ? 2628 PRO A N     1 
ATOM   9197  C  CA    . PRO A 1 2628 ? 156.575 186.336 176.699 1.00 12.02  ? 2628 PRO A CA    1 
ATOM   9198  C  C     . PRO A 1 2628 ? 155.205 186.263 177.356 1.00 15.83  ? 2628 PRO A C     1 
ATOM   9199  O  O     . PRO A 1 2628 ? 154.678 187.312 177.747 1.00 16.08  ? 2628 PRO A O     1 
ATOM   9200  C  CB    . PRO A 1 2628 ? 156.478 186.896 175.276 1.00 9.72   ? 2628 PRO A CB    1 
ATOM   9201  C  CG    . PRO A 1 2628 ? 157.622 186.282 174.569 1.00 9.18   ? 2628 PRO A CG    1 
ATOM   9202  C  CD    . PRO A 1 2628 ? 157.795 184.906 175.148 1.00 9.13   ? 2628 PRO A CD    1 
ATOM   9203  N  N     . GLU A 1 2629 ? 154.615 185.072 177.489 1.00 16.24  ? 2629 GLU A N     1 
ATOM   9204  C  CA    . GLU A 1 2629 ? 153.339 184.949 178.187 1.00 17.06  ? 2629 GLU A CA    1 
ATOM   9205  C  C     . GLU A 1 2629 ? 153.451 185.383 179.643 1.00 18.05  ? 2629 GLU A C     1 
ATOM   9206  O  O     . GLU A 1 2629 ? 152.552 186.059 180.157 1.00 20.27  ? 2629 GLU A O     1 
ATOM   9207  C  CB    . GLU A 1 2629 ? 152.831 183.510 178.099 1.00 25.30  ? 2629 GLU A CB    1 
ATOM   9208  C  CG    . GLU A 1 2629 ? 151.662 183.206 179.024 1.00 35.30  ? 2629 GLU A CG    1 
ATOM   9209  C  CD    . GLU A 1 2629 ? 151.533 181.728 179.332 1.00 48.36  ? 2629 GLU A CD    1 
ATOM   9210  O  OE1   . GLU A 1 2629 ? 152.536 181.000 179.185 1.00 47.31  ? 2629 GLU A OE1   1 
ATOM   9211  O  OE2   . GLU A 1 2629 ? 150.428 181.295 179.723 1.00 54.05  ? 2629 GLU A OE2   1 
ATOM   9212  N  N     . LEU A 1 2630 ? 154.541 185.011 180.319 1.00 19.62  ? 2630 LEU A N     1 
ATOM   9213  C  CA    . LEU A 1 2630 ? 154.742 185.436 181.702 1.00 16.10  ? 2630 LEU A CA    1 
ATOM   9214  C  C     . LEU A 1 2630 ? 154.802 186.955 181.802 1.00 17.50  ? 2630 LEU A C     1 
ATOM   9215  O  O     . LEU A 1 2630 ? 154.307 187.547 182.768 1.00 18.64  ? 2630 LEU A O     1 
ATOM   9216  C  CB    . LEU A 1 2630 ? 156.016 184.805 182.265 1.00 16.48  ? 2630 LEU A CB    1 
ATOM   9217  C  CG    . LEU A 1 2630 ? 156.168 184.806 183.788 1.00 19.33  ? 2630 LEU A CG    1 
ATOM   9218  C  CD1   . LEU A 1 2630 ? 155.416 183.641 184.412 1.00 24.70  ? 2630 LEU A CD1   1 
ATOM   9219  C  CD2   . LEU A 1 2630 ? 157.637 184.771 184.178 1.00 15.64  ? 2630 LEU A CD2   1 
ATOM   9220  N  N     . LEU A 1 2631 ? 155.418 187.604 180.811 1.00 18.03  ? 2631 LEU A N     1 
ATOM   9221  C  CA    . LEU A 1 2631 ? 155.388 189.061 180.748 1.00 14.89  ? 2631 LEU A CA    1 
ATOM   9222  C  C     . LEU A 1 2631 ? 153.968 189.572 180.541 1.00 15.14  ? 2631 LEU A C     1 
ATOM   9223  O  O     . LEU A 1 2631 ? 153.560 190.565 181.155 1.00 13.27  ? 2631 LEU A O     1 
ATOM   9224  C  CB    . LEU A 1 2631 ? 156.305 189.553 179.628 1.00 15.38  ? 2631 LEU A CB    1 
ATOM   9225  C  CG    . LEU A 1 2631 ? 157.642 190.182 180.026 1.00 13.58  ? 2631 LEU A CG    1 
ATOM   9226  C  CD1   . LEU A 1 2631 ? 157.413 191.492 180.753 1.00 18.35  ? 2631 LEU A CD1   1 
ATOM   9227  C  CD2   . LEU A 1 2631 ? 158.457 189.228 180.881 1.00 11.14  ? 2631 LEU A CD2   1 
ATOM   9228  N  N     . LEU A 1 2632 ? 153.200 188.904 179.676 1.00 17.29  ? 2632 LEU A N     1 
ATOM   9229  C  CA    . LEU A 1 2632 ? 151.832 189.333 179.400 1.00 16.30  ? 2632 LEU A CA    1 
ATOM   9230  C  C     . LEU A 1 2632 ? 150.927 189.129 180.609 1.00 16.36  ? 2632 LEU A C     1 
ATOM   9231  O  O     . LEU A 1 2632 ? 150.033 189.945 180.864 1.00 23.72  ? 2632 LEU A O     1 
ATOM   9232  C  CB    . LEU A 1 2632 ? 151.285 188.583 178.186 1.00 16.19  ? 2632 LEU A CB    1 
ATOM   9233  C  CG    . LEU A 1 2632 ? 151.973 188.883 176.853 1.00 13.60  ? 2632 LEU A CG    1 
ATOM   9234  C  CD1   . LEU A 1 2632 ? 151.323 188.101 175.723 1.00 13.61  ? 2632 LEU A CD1   1 
ATOM   9235  C  CD2   . LEU A 1 2632 ? 151.945 190.374 176.560 1.00 11.26  ? 2632 LEU A CD2   1 
ATOM   9236  N  N     . LYS A 1 2633 ? 151.134 188.043 181.358 1.00 16.87  ? 2633 LYS A N     1 
ATOM   9237  C  CA    . LYS A 1 2633 ? 150.319 187.796 182.544 1.00 16.19  ? 2633 LYS A CA    1 
ATOM   9238  C  C     . LYS A 1 2633 ? 150.530 188.879 183.594 1.00 17.38  ? 2633 LYS A C     1 
ATOM   9239  O  O     . LYS A 1 2633 ? 149.575 189.312 184.250 1.00 24.74  ? 2633 LYS A O     1 
ATOM   9240  C  CB    . LYS A 1 2633 ? 150.634 186.417 183.124 1.00 21.39  ? 2633 LYS A CB    1 
ATOM   9241  C  CG    . LYS A 1 2633 ? 150.234 185.259 182.225 1.00 27.95  ? 2633 LYS A CG    1 
ATOM   9242  C  CD    . LYS A 1 2633 ? 148.729 185.059 182.217 1.00 36.33  ? 2633 LYS A CD    1 
ATOM   9243  C  CE    . LYS A 1 2633 ? 148.357 183.690 181.674 1.00 46.61  ? 2633 LYS A CE    1 
ATOM   9244  N  NZ    . LYS A 1 2633 ? 149.091 182.599 182.373 1.00 41.48  ? 2633 LYS A NZ    1 
ATOM   9245  N  N     . THR A 1 2634 ? 151.777 189.320 183.776 1.00 15.00  ? 2634 THR A N     1 
ATOM   9246  C  CA    . THR A 1 2634 ? 152.051 190.409 184.708 1.00 15.56  ? 2634 THR A CA    1 
ATOM   9247  C  C     . THR A 1 2634 ? 151.373 191.697 184.258 1.00 17.02  ? 2634 THR A C     1 
ATOM   9248  O  O     . THR A 1 2634 ? 150.831 192.445 185.081 1.00 22.14  ? 2634 THR A O     1 
ATOM   9249  C  CB    . THR A 1 2634 ? 153.561 190.608 184.847 1.00 17.27  ? 2634 THR A CB    1 
ATOM   9250  O  OG1   . THR A 1 2634 ? 154.135 189.472 185.504 1.00 15.27  ? 2634 THR A OG1   1 
ATOM   9251  C  CG2   . THR A 1 2634 ? 153.870 191.858 185.657 1.00 15.50  ? 2634 THR A CG2   1 
ATOM   9252  N  N     . PHE A 1 2635 ? 151.389 191.970 182.950 1.00 15.23  ? 2635 PHE A N     1 
ATOM   9253  C  CA    . PHE A 1 2635 ? 150.722 193.157 182.426 1.00 16.96  ? 2635 PHE A CA    1 
ATOM   9254  C  C     . PHE A 1 2635 ? 149.221 193.109 182.679 1.00 22.31  ? 2635 PHE A C     1 
ATOM   9255  O  O     . PHE A 1 2635 ? 148.606 194.131 183.005 1.00 26.59  ? 2635 PHE A O     1 
ATOM   9256  C  CB    . PHE A 1 2635 ? 151.006 193.296 180.931 1.00 19.51  ? 2635 PHE A CB    1 
ATOM   9257  C  CG    . PHE A 1 2635 ? 152.409 193.722 180.617 1.00 16.29  ? 2635 PHE A CG    1 
ATOM   9258  C  CD1   . PHE A 1 2635 ? 153.181 194.362 181.570 1.00 15.78  ? 2635 PHE A CD1   1 
ATOM   9259  C  CD2   . PHE A 1 2635 ? 152.961 193.470 179.373 1.00 17.47  ? 2635 PHE A CD2   1 
ATOM   9260  C  CE1   . PHE A 1 2635 ? 154.470 194.754 181.284 1.00 20.21  ? 2635 PHE A CE1   1 
ATOM   9261  C  CE2   . PHE A 1 2635 ? 154.251 193.857 179.083 1.00 18.33  ? 2635 PHE A CE2   1 
ATOM   9262  C  CZ    . PHE A 1 2635 ? 155.007 194.500 180.040 1.00 22.67  ? 2635 PHE A CZ    1 
ATOM   9263  N  N     . ASP A 1 2636 ? 148.612 191.930 182.535 1.00 18.79  ? 2636 ASP A N     1 
ATOM   9264  C  CA    . ASP A 1 2636 ? 147.172 191.813 182.737 1.00 19.74  ? 2636 ASP A CA    1 
ATOM   9265  C  C     . ASP A 1 2636 ? 146.790 192.000 184.199 1.00 22.86  ? 2636 ASP A C     1 
ATOM   9266  O  O     . ASP A 1 2636 ? 145.611 192.202 184.512 1.00 27.47  ? 2636 ASP A O     1 
ATOM   9267  C  CB    . ASP A 1 2636 ? 146.681 190.458 182.228 1.00 23.53  ? 2636 ASP A CB    1 
ATOM   9268  C  CG    . ASP A 1 2636 ? 145.838 190.578 180.975 1.00 42.49  ? 2636 ASP A CG    1 
ATOM   9269  O  OD1   . ASP A 1 2636 ? 145.488 191.716 180.598 1.00 42.04  ? 2636 ASP A OD1   1 
ATOM   9270  O  OD2   . ASP A 1 2636 ? 145.527 189.534 180.364 1.00 48.69  ? 2636 ASP A OD2   1 
ATOM   9271  N  N     . HIS A 1 2637 ? 147.764 191.934 185.106 1.00 23.02  ? 2637 HIS A N     1 
ATOM   9272  C  CA    . HIS A 1 2637 ? 147.474 192.098 186.526 1.00 20.01  ? 2637 HIS A CA    1 
ATOM   9273  C  C     . HIS A 1 2637 ? 147.735 193.526 186.988 1.00 22.03  ? 2637 HIS A C     1 
ATOM   9274  O  O     . HIS A 1 2637 ? 146.869 194.155 187.606 1.00 25.83  ? 2637 HIS A O     1 
ATOM   9275  C  CB    . HIS A 1 2637 ? 148.307 191.107 187.343 1.00 20.60  ? 2637 HIS A CB    1 
ATOM   9276  C  CG    . HIS A 1 2637 ? 147.969 191.086 188.801 1.00 28.12  ? 2637 HIS A CG    1 
ATOM   9277  N  ND1   . HIS A 1 2637 ? 148.278 192.125 189.653 1.00 23.18  ? 2637 HIS A ND1   1 
ATOM   9278  C  CD2   . HIS A 1 2637 ? 147.348 190.151 189.558 1.00 28.52  ? 2637 HIS A CD2   1 
ATOM   9279  C  CE1   . HIS A 1 2637 ? 147.862 191.830 190.872 1.00 28.16  ? 2637 HIS A CE1   1 
ATOM   9280  N  NE2   . HIS A 1 2637 ? 147.295 190.638 190.841 1.00 32.78  ? 2637 HIS A NE2   1 
ATOM   9281  N  N     . TYR A 1 2638 ? 148.923 194.053 186.696 1.00 20.46  ? 2638 TYR A N     1 
ATOM   9282  C  CA    . TYR A 1 2638 ? 149.358 195.337 187.228 1.00 19.01  ? 2638 TYR A CA    1 
ATOM   9283  C  C     . TYR A 1 2638 ? 149.090 196.508 186.292 1.00 21.58  ? 2638 TYR A C     1 
ATOM   9284  O  O     . TYR A 1 2638 ? 149.287 197.658 186.697 1.00 25.21  ? 2638 TYR A O     1 
ATOM   9285  C  CB    . TYR A 1 2638 ? 150.855 195.281 187.553 1.00 14.40  ? 2638 TYR A CB    1 
ATOM   9286  C  CG    . TYR A 1 2638 ? 151.192 194.363 188.704 1.00 14.89  ? 2638 TYR A CG    1 
ATOM   9287  C  CD1   . TYR A 1 2638 ? 151.015 194.768 190.019 1.00 14.73  ? 2638 TYR A CD1   1 
ATOM   9288  C  CD2   . TYR A 1 2638 ? 151.674 193.082 188.473 1.00 19.46  ? 2638 TYR A CD2   1 
ATOM   9289  C  CE1   . TYR A 1 2638 ? 151.319 193.927 191.072 1.00 18.71  ? 2638 TYR A CE1   1 
ATOM   9290  C  CE2   . TYR A 1 2638 ? 151.979 192.234 189.518 1.00 19.71  ? 2638 TYR A CE2   1 
ATOM   9291  C  CZ    . TYR A 1 2638 ? 151.800 192.661 190.815 1.00 23.62  ? 2638 TYR A CZ    1 
ATOM   9292  O  OH    . TYR A 1 2638 ? 152.104 191.820 191.859 1.00 28.43  ? 2638 TYR A OH    1 
ATOM   9293  N  N     . CYS A 1 2639 ? 148.648 196.253 185.063 1.00 22.84  ? 2639 CYS A N     1 
ATOM   9294  C  CA    . CYS A 1 2639 ? 148.434 197.300 184.076 1.00 21.02  ? 2639 CYS A CA    1 
ATOM   9295  C  C     . CYS A 1 2639 ? 147.079 197.110 183.408 1.00 24.81  ? 2639 CYS A C     1 
ATOM   9296  O  O     . CYS A 1 2639 ? 146.390 196.108 183.614 1.00 27.14  ? 2639 CYS A O     1 
ATOM   9297  C  CB    . CYS A 1 2639 ? 149.546 197.310 183.019 1.00 23.02  ? 2639 CYS A CB    1 
ATOM   9298  S  SG    . CYS A 1 2639 ? 151.223 197.306 183.683 1.00 31.16  ? 2639 CYS A SG    1 
ATOM   9299  N  N     . GLU A 1 2640 ? 146.703 198.094 182.594 1.00 28.95  ? 2640 GLU A N     1 
ATOM   9300  C  CA    . GLU A 1 2640 ? 145.447 198.062 181.861 1.00 27.56  ? 2640 GLU A CA    1 
ATOM   9301  C  C     . GLU A 1 2640 ? 145.660 198.626 180.464 1.00 30.91  ? 2640 GLU A C     1 
ATOM   9302  O  O     . GLU A 1 2640 ? 146.508 199.498 180.253 1.00 29.28  ? 2640 GLU A O     1 
ATOM   9303  C  CB    . GLU A 1 2640 ? 144.352 198.858 182.582 1.00 27.50  ? 2640 GLU A CB    1 
ATOM   9304  C  CG    . GLU A 1 2640 ? 144.840 200.159 183.196 1.00 35.11  ? 2640 GLU A CG    1 
ATOM   9305  C  CD    . GLU A 1 2640 ? 143.729 200.942 183.868 1.00 41.57  ? 2640 GLU A CD    1 
ATOM   9306  O  OE1   . GLU A 1 2640 ? 142.788 200.310 184.392 1.00 45.16  ? 2640 GLU A OE1   1 
ATOM   9307  O  OE2   . GLU A 1 2640 ? 143.797 202.189 183.873 1.00 37.96  ? 2640 GLU A OE2   1 
ATOM   9308  N  N     . TYR A 1 2641 ? 144.905 198.097 179.496 1.00 27.78  ? 2641 TYR A N     1 
ATOM   9309  C  CA    . TYR A 1 2641 ? 145.037 198.564 178.089 1.00 21.70  ? 2641 TYR A CA    1 
ATOM   9310  C  C     . TYR A 1 2641 ? 144.033 199.687 177.848 1.00 27.41  ? 2641 TYR A C     1 
ATOM   9311  O  O     . TYR A 1 2641 ? 142.813 199.450 177.978 1.00 34.43  ? 2641 TYR A O     1 
ATOM   9312  C  CB    . TYR A 1 2641 ? 144.846 197.390 177.124 1.00 26.87  ? 2641 TYR A CB    1 
ATOM   9313  C  CG    . TYR A 1 2641 ? 145.991 196.387 177.119 1.00 24.32  ? 2641 TYR A CG    1 
ATOM   9314  C  CD1   . TYR A 1 2641 ? 145.989 195.291 177.972 1.00 29.18  ? 2641 TYR A CD1   1 
ATOM   9315  C  CD2   . TYR A 1 2641 ? 147.076 196.541 176.264 1.00 22.36  ? 2641 TYR A CD2   1 
ATOM   9316  C  CE1   . TYR A 1 2641 ? 147.029 194.376 177.973 1.00 33.12  ? 2641 TYR A CE1   1 
ATOM   9317  C  CE2   . TYR A 1 2641 ? 148.122 195.634 176.256 1.00 18.82  ? 2641 TYR A CE2   1 
ATOM   9318  C  CZ    . TYR A 1 2641 ? 148.098 194.548 177.113 1.00 26.71  ? 2641 TYR A CZ    1 
ATOM   9319  O  OH    . TYR A 1 2641 ? 149.125 193.650 177.112 1.00 30.59  ? 2641 TYR A OH    1 
ATOM   9320  N  N     . ARG A 1 2642 ? 144.531 200.878 177.509 1.00 28.07  ? 2642 ARG A N     1 
ATOM   9321  C  CA    . ARG A 1 2642 ? 143.644 202.046 177.269 1.00 26.18  ? 2642 ARG A CA    1 
ATOM   9322  C  C     . ARG A 1 2642 ? 143.735 202.456 175.793 1.00 28.49  ? 2642 ARG A C     1 
ATOM   9323  O  O     . ARG A 1 2642 ? 144.860 202.737 175.325 1.00 28.38  ? 2642 ARG A O     1 
ATOM   9324  C  CB    . ARG A 1 2642 ? 144.046 203.201 178.191 1.00 30.39  ? 2642 ARG A CB    1 
ATOM   9325  C  CG    . ARG A 1 2642 ? 143.750 204.590 177.644 1.00 32.77  ? 2642 ARG A CG    1 
ATOM   9326  C  CD    . ARG A 1 2642 ? 144.079 205.674 178.659 1.00 32.49  ? 2642 ARG A CD    1 
ATOM   9327  N  NE    . ARG A 1 2642 ? 145.394 205.497 179.285 1.00 38.64  ? 2642 ARG A NE    1 
ATOM   9328  C  CZ    . ARG A 1 2642 ? 146.560 205.510 178.651 1.00 29.87  ? 2642 ARG A CZ    1 
ATOM   9329  N  NH1   . ARG A 1 2642 ? 146.646 206.002 177.429 1.00 33.01  ? 2642 ARG A NH1   1 
ATOM   9330  N  NH2   . ARG A 1 2642 ? 147.640 205.039 179.247 1.00 22.30  ? 2642 ARG A NH2   1 
ATOM   9331  N  N     . ARG A 1 2643 ? 142.596 202.489 175.096 1.00 35.62  ? 2643 ARG A N     1 
ATOM   9332  C  CA    . ARG A 1 2643 ? 142.582 202.923 173.674 1.00 35.67  ? 2643 ARG A CA    1 
ATOM   9333  C  C     . ARG A 1 2643 ? 142.638 204.457 173.621 1.00 36.83  ? 2643 ARG A C     1 
ATOM   9334  O  O     . ARG A 1 2643 ? 141.884 205.102 174.381 1.00 39.10  ? 2643 ARG A O     1 
ATOM   9335  C  CB    . ARG A 1 2643 ? 141.340 202.386 172.956 1.00 39.77  ? 2643 ARG A CB    1 
ATOM   9336  C  CG    . ARG A 1 2643 ? 141.294 200.867 172.879 1.00 41.86  ? 2643 ARG A CG    1 
ATOM   9337  C  CD    . ARG A 1 2643 ? 140.065 200.386 172.124 1.00 48.45  ? 2643 ARG A CD    1 
ATOM   9338  N  NE    . ARG A 1 2643 ? 139.969 200.985 170.789 1.00 55.42  ? 2643 ARG A NE    1 
ATOM   9339  C  CZ    . ARG A 1 2643 ? 140.865 200.835 169.820 1.00 50.85  ? 2643 ARG A CZ    1 
ATOM   9340  N  NH1   . ARG A 1 2643 ? 141.808 199.916 169.924 1.00 40.52  ? 2643 ARG A NH1   1 
ATOM   9341  N  NH2   . ARG A 1 2643 ? 140.809 201.601 168.746 1.00 49.15  ? 2643 ARG A NH2   1 
ATOM   9342  N  N     . THR A 1 2644 ? 143.503 205.010 172.767 1.00 37.44  ? 2644 THR A N     1 
ATOM   9343  C  CA    . THR A 1 2644 ? 143.641 206.477 172.650 1.00 37.62  ? 2644 THR A CA    1 
ATOM   9344  C  C     . THR A 1 2644 ? 143.594 206.853 171.187 1.00 39.58  ? 2644 THR A C     1 
ATOM   9345  O  O     . THR A 1 2644 ? 143.771 205.950 170.340 1.00 41.04  ? 2644 THR A O     1 
ATOM   9346  C  CB    . THR A 1 2644 ? 144.952 206.921 173.298 1.00 39.13  ? 2644 THR A CB    1 
ATOM   9347  O  OG1   . THR A 1 2644 ? 145.968 206.585 172.359 1.00 41.48  ? 2644 THR A OG1   1 
ATOM   9348  C  CG2   . THR A 1 2644 ? 145.208 206.232 174.627 1.00 33.48  ? 2644 THR A CG2   1 
ATOM   9349  N  N     . PRO A 1 2645 ? 143.381 208.137 170.828 1.00 45.22  ? 2645 PRO A N     1 
ATOM   9350  C  CA    . PRO A 1 2645 ? 143.420 208.539 169.431 1.00 40.82  ? 2645 PRO A CA    1 
ATOM   9351  C  C     . PRO A 1 2645 ? 144.705 208.042 168.789 1.00 40.91  ? 2645 PRO A C     1 
ATOM   9352  O  O     . PRO A 1 2645 ? 144.661 207.552 167.643 1.00 43.91  ? 2645 PRO A O     1 
ATOM   9353  C  CB    . PRO A 1 2645 ? 143.363 210.070 169.517 1.00 43.96  ? 2645 PRO A CB    1 
ATOM   9354  C  CG    . PRO A 1 2645 ? 142.621 210.332 170.807 1.00 40.12  ? 2645 PRO A CG    1 
ATOM   9355  C  CD    . PRO A 1 2645 ? 143.086 209.229 171.742 1.00 42.97  ? 2645 PRO A CD    1 
ATOM   9356  N  N     . ASN A 1 2646 ? 145.824 208.154 169.510 1.00 45.27  ? 2646 ASN A N     1 
ATOM   9357  C  CA    . ASN A 1 2646 ? 147.138 207.689 168.981 1.00 44.93  ? 2646 ASN A CA    1 
ATOM   9358  C  C     . ASN A 1 2646 ? 147.111 206.166 168.807 1.00 38.86  ? 2646 ASN A C     1 
ATOM   9359  O  O     . ASN A 1 2646 ? 147.618 205.681 167.772 1.00 38.21  ? 2646 ASN A O     1 
ATOM   9360  C  CB    . ASN A 1 2646 ? 148.287 208.139 169.875 1.00 45.02  ? 2646 ASN A CB    1 
ATOM   9361  C  CG    . ASN A 1 2646 ? 148.236 209.621 170.156 1.00 51.23  ? 2646 ASN A CG    1 
ATOM   9362  O  OD1   . ASN A 1 2646 ? 147.256 210.112 170.727 1.00 52.51  ? 2646 ASN A OD1   1 
ATOM   9363  N  ND2   . ASN A 1 2646 ? 149.273 210.347 169.766 1.00 51.69  ? 2646 ASN A ND2   1 
ATOM   9364  N  N     . GLY A 1 2647 ? 146.544 205.443 169.778 1.00 36.45  ? 2647 GLY A N     1 
ATOM   9365  C  CA    . GLY A 1 2647 ? 146.450 203.972 169.680 1.00 31.52  ? 2647 GLY A CA    1 
ATOM   9366  C  C     . GLY A 1 2647 ? 146.264 203.332 171.042 1.00 31.47  ? 2647 GLY A C     1 
ATOM   9367  O  O     . GLY A 1 2647 ? 146.044 204.074 172.020 1.00 36.96  ? 2647 GLY A O     1 
ATOM   9368  N  N     . VAL A 1 2648 ? 146.348 202.000 171.108 1.00 29.23  ? 2648 VAL A N     1 
ATOM   9369  C  CA    . VAL A 1 2648 ? 146.204 201.275 172.407 1.00 18.16  ? 2648 VAL A CA    1 
ATOM   9370  C  C     . VAL A 1 2648 ? 147.462 201.532 173.249 1.00 16.69  ? 2648 VAL A C     1 
ATOM   9371  O  O     . VAL A 1 2648 ? 148.577 201.299 172.735 1.00 21.14  ? 2648 VAL A O     1 
ATOM   9372  C  CB    . VAL A 1 2648 ? 145.967 199.766 172.210 1.00 16.33  ? 2648 VAL A CB    1 
ATOM   9373  C  CG1   . VAL A 1 2648 ? 145.884 199.031 173.543 1.00 23.50  ? 2648 VAL A CG1   1 
ATOM   9374  C  CG2   . VAL A 1 2648 ? 144.722 199.499 171.374 1.00 26.74  ? 2648 VAL A CG2   1 
ATOM   9375  N  N     . VAL A 1 2649 ? 147.282 201.993 174.489 1.00 19.51  ? 2649 VAL A N     1 
ATOM   9376  C  CA    . VAL A 1 2649 ? 148.443 202.294 175.379 1.00 16.94  ? 2649 VAL A CA    1 
ATOM   9377  C  C     . VAL A 1 2649 ? 148.327 201.442 176.651 1.00 20.94  ? 2649 VAL A C     1 
ATOM   9378  O  O     . VAL A 1 2649 ? 147.256 201.484 177.294 1.00 25.04  ? 2649 VAL A O     1 
ATOM   9379  C  CB    . VAL A 1 2649 ? 148.538 203.794 175.717 1.00 20.55  ? 2649 VAL A CB    1 
ATOM   9380  C  CG1   . VAL A 1 2649 ? 149.667 204.081 176.700 1.00 17.79  ? 2649 VAL A CG1   1 
ATOM   9381  C  CG2   . VAL A 1 2649 ? 148.687 204.647 174.464 1.00 18.70  ? 2649 VAL A CG2   1 
ATOM   9382  N  N     . LEU A 1 2650 ? 149.386 200.704 176.992 1.00 21.56  ? 2650 LEU A N     1 
ATOM   9383  C  CA    . LEU A 1 2650 ? 149.389 199.881 178.194 1.00 16.55  ? 2650 LEU A CA    1 
ATOM   9384  C  C     . LEU A 1 2650 ? 150.157 200.618 179.284 1.00 16.87  ? 2650 LEU A C     1 
ATOM   9385  O  O     . LEU A 1 2650 ? 151.361 200.855 179.148 1.00 18.53  ? 2650 LEU A O     1 
ATOM   9386  C  CB    . LEU A 1 2650 ? 150.015 198.515 177.918 1.00 13.26  ? 2650 LEU A CB    1 
ATOM   9387  C  CG    . LEU A 1 2650 ? 150.141 197.565 179.108 1.00 17.11  ? 2650 LEU A CG    1 
ATOM   9388  C  CD1   . LEU A 1 2650 ? 148.782 196.997 179.479 1.00 21.91  ? 2650 LEU A CD1   1 
ATOM   9389  C  CD2   . LEU A 1 2650 ? 151.123 196.452 178.796 1.00 14.60  ? 2650 LEU A CD2   1 
ATOM   9390  N  N     . ALA A 1 2651 ? 149.461 200.975 180.357 1.00 20.58  ? 2651 ALA A N     1 
ATOM   9391  C  CA    . ALA A 1 2651 ? 150.025 201.756 181.445 1.00 14.95  ? 2651 ALA A CA    1 
ATOM   9392  C  C     . ALA A 1 2651 ? 149.625 201.130 182.771 1.00 22.16  ? 2651 ALA A C     1 
ATOM   9393  O  O     . ALA A 1 2651 ? 148.614 200.421 182.844 1.00 27.89  ? 2651 ALA A O     1 
ATOM   9394  C  CB    . ALA A 1 2651 ? 149.547 203.217 181.394 1.00 18.82  ? 2651 ALA A CB    1 
ATOM   9395  N  N     . PRO A 1 2652 ? 150.402 201.362 183.830 1.00 22.37  ? 2652 PRO A N     1 
ATOM   9396  C  CA    . PRO A 1 2652 ? 150.044 200.805 185.138 1.00 20.07  ? 2652 PRO A CA    1 
ATOM   9397  C  C     . PRO A 1 2652 ? 148.707 201.336 185.631 1.00 24.34  ? 2652 PRO A C     1 
ATOM   9398  O  O     . PRO A 1 2652 ? 148.311 202.464 185.331 1.00 25.51  ? 2652 PRO A O     1 
ATOM   9399  C  CB    . PRO A 1 2652 ? 151.192 201.262 186.045 1.00 21.60  ? 2652 PRO A CB    1 
ATOM   9400  C  CG    . PRO A 1 2652 ? 152.330 201.492 185.123 1.00 20.34  ? 2652 PRO A CG    1 
ATOM   9401  C  CD    . PRO A 1 2652 ? 151.724 202.010 183.856 1.00 20.29  ? 2652 PRO A CD    1 
ATOM   9402  N  N     . VAL A 1 2653 ? 148.005 200.494 186.393 1.00 27.26  ? 2653 VAL A N     1 
ATOM   9403  C  CA    . VAL A 1 2653 ? 146.735 200.906 186.984 1.00 26.73  ? 2653 VAL A CA    1 
ATOM   9404  C  C     . VAL A 1 2653 ? 146.952 202.061 187.952 1.00 29.17  ? 2653 VAL A C     1 
ATOM   9405  O  O     . VAL A 1 2653 ? 146.154 203.005 188.004 1.00 31.06  ? 2653 VAL A O     1 
ATOM   9406  C  CB    . VAL A 1 2653 ? 146.050 199.711 187.673 1.00 27.47  ? 2653 VAL A CB    1 
ATOM   9407  C  CG1   . VAL A 1 2653 ? 144.632 200.078 188.081 1.00 29.14  ? 2653 VAL A CG1   1 
ATOM   9408  C  CG2   . VAL A 1 2653 ? 146.048 198.502 186.755 1.00 28.46  ? 2653 VAL A CG2   1 
ATOM   9409  N  N     . GLN A 1 2654 ? 148.024 202.001 188.738 1.00 26.55  ? 2654 GLN A N     1 
ATOM   9410  C  CA    . GLN A 1 2654 ? 148.369 203.101 189.628 1.00 29.91  ? 2654 GLN A CA    1 
ATOM   9411  C  C     . GLN A 1 2654 ? 148.732 204.337 188.813 1.00 31.52  ? 2654 GLN A C     1 
ATOM   9412  O  O     . GLN A 1 2654 ? 149.479 204.251 187.834 1.00 33.84  ? 2654 GLN A O     1 
ATOM   9413  C  CB    . GLN A 1 2654 ? 149.531 202.699 190.533 1.00 30.84  ? 2654 GLN A CB    1 
ATOM   9414  C  CG    . GLN A 1 2654 ? 149.107 202.049 191.839 1.00 38.28  ? 2654 GLN A CG    1 
ATOM   9415  C  CD    . GLN A 1 2654 ? 150.213 202.047 192.874 1.00 46.56  ? 2654 GLN A CD    1 
ATOM   9416  O  OE1   . GLN A 1 2654 ? 150.365 202.998 193.641 1.00 50.53  ? 2654 GLN A OE1   1 
ATOM   9417  N  NE2   . GLN A 1 2654 ? 150.993 200.972 192.903 1.00 46.04  ? 2654 GLN A NE2   1 
ATOM   9418  N  N     . LEU A 1 2655 ? 148.203 205.487 189.219 1.00 30.19  ? 2655 LEU A N     1 
ATOM   9419  C  CA    . LEU A 1 2655 ? 148.422 206.735 188.501 1.00 34.30  ? 2655 LEU A CA    1 
ATOM   9420  C  C     . LEU A 1 2655 ? 149.647 207.456 189.045 1.00 34.82  ? 2655 LEU A C     1 
ATOM   9421  O  O     . LEU A 1 2655 ? 149.846 207.542 190.260 1.00 37.22  ? 2655 LEU A O     1 
ATOM   9422  C  CB    . LEU A 1 2655 ? 147.195 207.644 188.602 1.00 38.63  ? 2655 LEU A CB    1 
ATOM   9423  C  CG    . LEU A 1 2655 ? 146.128 207.517 187.512 1.00 37.79  ? 2655 LEU A CG    1 
ATOM   9424  C  CD1   . LEU A 1 2655 ? 146.715 207.847 186.146 1.00 30.80  ? 2655 LEU A CD1   1 
ATOM   9425  C  CD2   . LEU A 1 2655 ? 145.489 206.137 187.509 1.00 32.23  ? 2655 LEU A CD2   1 
ATOM   9426  N  N     . GLY A 1 2656 ? 150.473 207.981 188.136 1.00 36.34  ? 2656 GLY A N     1 
ATOM   9427  C  CA    . GLY A 1 2656 ? 151.693 208.697 188.554 1.00 34.13  ? 2656 GLY A CA    1 
ATOM   9428  C  C     . GLY A 1 2656 ? 152.693 207.742 189.173 1.00 35.17  ? 2656 GLY A C     1 
ATOM   9429  O  O     . GLY A 1 2656 ? 153.431 208.167 190.086 1.00 44.89  ? 2656 GLY A O     1 
ATOM   9430  N  N     . LYS A 1 2657 ? 152.715 206.493 188.700 1.00 33.57  ? 2657 LYS A N     1 
ATOM   9431  C  CA    . LYS A 1 2657 ? 153.663 205.480 189.233 1.00 27.73  ? 2657 LYS A CA    1 
ATOM   9432  C  C     . LYS A 1 2657 ? 154.373 204.779 188.064 1.00 23.12  ? 2657 LYS A C     1 
ATOM   9433  O  O     . LYS A 1 2657 ? 153.691 204.441 187.073 1.00 24.17  ? 2657 LYS A O     1 
ATOM   9434  C  CB    . LYS A 1 2657 ? 152.925 204.468 190.117 1.00 29.40  ? 2657 LYS A CB    1 
ATOM   9435  C  CG    . LYS A 1 2657 ? 152.415 205.034 191.433 1.00 37.60  ? 2657 LYS A CG    1 
ATOM   9436  C  CD    . LYS A 1 2657 ? 153.541 205.593 192.295 1.00 39.45  ? 2657 LYS A CD    1 
ATOM   9437  C  CE    . LYS A 1 2657 ? 153.041 206.283 193.522 1.00 42.97  ? 2657 LYS A CE    1 
ATOM   9438  N  NZ    . LYS A 1 2657 ? 152.194 207.428 193.181 1.00 46.48  ? 2657 LYS A NZ    1 
ATOM   9439  N  N     . TRP A 1 2658 ? 155.688 204.577 188.182 1.00 20.72  ? 2658 TRP A N     1 
ATOM   9440  C  CA    . TRP A 1 2658 ? 156.454 203.865 187.128 1.00 16.90  ? 2658 TRP A CA    1 
ATOM   9441  C  C     . TRP A 1 2658 ? 156.631 202.403 187.536 1.00 16.85  ? 2658 TRP A C     1 
ATOM   9442  O  O     . TRP A 1 2658 ? 157.291 202.145 188.565 1.00 23.78  ? 2658 TRP A O     1 
ATOM   9443  C  CB    . TRP A 1 2658 ? 157.811 204.545 186.907 1.00 16.58  ? 2658 TRP A CB    1 
ATOM   9444  C  CG    . TRP A 1 2658 ? 157.868 205.408 185.675 1.00 12.66  ? 2658 TRP A CG    1 
ATOM   9445  C  CD1   . TRP A 1 2658 ? 157.492 206.714 185.566 1.00 14.59  ? 2658 TRP A CD1   1 
ATOM   9446  C  CD2   . TRP A 1 2658 ? 158.349 205.018 184.370 1.00 13.79  ? 2658 TRP A CD2   1 
ATOM   9447  N  NE1   . TRP A 1 2658 ? 157.695 207.162 184.288 1.00 15.65  ? 2658 TRP A NE1   1 
ATOM   9448  C  CE2   . TRP A 1 2658 ? 158.221 206.147 183.533 1.00 13.78  ? 2658 TRP A CE2   1 
ATOM   9449  C  CE3   . TRP A 1 2658 ? 158.868 203.836 183.833 1.00 13.97  ? 2658 TRP A CE3   1 
ATOM   9450  C  CZ2   . TRP A 1 2658 ? 158.594 206.122 182.192 1.00 11.73  ? 2658 TRP A CZ2   1 
ATOM   9451  C  CZ3   . TRP A 1 2658 ? 159.238 203.815 182.507 1.00 11.80  ? 2658 TRP A CZ3   1 
ATOM   9452  C  CH2   . TRP A 1 2658 ? 159.102 204.942 181.700 1.00 10.64  ? 2658 TRP A CH2   1 
ATOM   9453  N  N     . LEU A 1 2659 ? 156.061 201.481 186.758 1.00 14.31  ? 2659 LEU A N     1 
ATOM   9454  C  CA    . LEU A 1 2659 ? 156.161 200.036 187.086 1.00 11.66  ? 2659 LEU A CA    1 
ATOM   9455  C  C     . LEU A 1 2659 ? 157.568 199.536 186.729 1.00 9.60   ? 2659 LEU A C     1 
ATOM   9456  O  O     . LEU A 1 2659 ? 157.973 199.687 185.556 1.00 12.13  ? 2659 LEU A O     1 
ATOM   9457  C  CB    . LEU A 1 2659 ? 155.083 199.237 186.355 1.00 13.42  ? 2659 LEU A CB    1 
ATOM   9458  C  CG    . LEU A 1 2659 ? 155.060 197.735 186.651 1.00 14.65  ? 2659 LEU A CG    1 
ATOM   9459  C  CD1   . LEU A 1 2659 ? 154.984 197.501 188.148 1.00 16.12  ? 2659 LEU A CD1   1 
ATOM   9460  C  CD2   . LEU A 1 2659 ? 153.897 197.061 185.946 1.00 18.03  ? 2659 LEU A CD2   1 
ATOM   9461  N  N     . VAL A 1 2660 ? 158.276 198.965 187.706 1.00 11.93  ? 2660 VAL A N     1 
ATOM   9462  C  CA    . VAL A 1 2660 ? 159.636 198.406 187.450 1.00 9.51   ? 2660 VAL A CA    1 
ATOM   9463  C  C     . VAL A 1 2660 ? 159.504 196.882 187.324 1.00 8.54   ? 2660 VAL A C     1 
ATOM   9464  O  O     . VAL A 1 2660 ? 159.213 196.227 188.346 1.00 8.16   ? 2660 VAL A O     1 
ATOM   9465  C  CB    . VAL A 1 2660 ? 160.628 198.785 188.565 1.00 7.69   ? 2660 VAL A CB    1 
ATOM   9466  C  CG1   . VAL A 1 2660 ? 162.061 198.434 188.187 1.00 6.63   ? 2660 VAL A CG1   1 
ATOM   9467  C  CG2   . VAL A 1 2660 ? 160.516 200.255 188.948 1.00 10.94  ? 2660 VAL A CG2   1 
ATOM   9468  N  N     . LEU A 1 2661 ? 159.694 196.349 186.116 1.00 8.97   ? 2661 LEU A N     1 
ATOM   9469  C  CA    . LEU A 1 2661 ? 159.635 194.879 185.917 1.00 8.32   ? 2661 LEU A CA    1 
ATOM   9470  C  C     . LEU A 1 2661 ? 161.024 194.296 186.207 1.00 9.07   ? 2661 LEU A C     1 
ATOM   9471  O  O     . LEU A 1 2661 ? 161.943 194.525 185.391 1.00 9.56   ? 2661 LEU A O     1 
ATOM   9472  C  CB    . LEU A 1 2661 ? 159.160 194.561 184.501 1.00 7.17   ? 2661 LEU A CB    1 
ATOM   9473  C  CG    . LEU A 1 2661 ? 157.750 195.044 184.152 1.00 12.61  ? 2661 LEU A CG    1 
ATOM   9474  C  CD1   . LEU A 1 2661 ? 157.333 194.512 182.795 1.00 17.37  ? 2661 LEU A CD1   1 
ATOM   9475  C  CD2   . LEU A 1 2661 ? 156.760 194.619 185.222 1.00 13.44  ? 2661 LEU A CD2   1 
ATOM   9476  N  N     . PHE A 1 2662 ? 161.168 193.584 187.327 1.00 8.34   ? 2662 PHE A N     1 
ATOM   9477  C  CA    . PHE A 1 2662 ? 162.469 193.044 187.706 1.00 8.73   ? 2662 PHE A CA    1 
ATOM   9478  C  C     . PHE A 1 2662 ? 162.492 191.564 187.346 1.00 10.96  ? 2662 PHE A C     1 
ATOM   9479  O  O     . PHE A 1 2662 ? 161.767 190.757 187.931 1.00 13.31  ? 2662 PHE A O     1 
ATOM   9480  C  CB    . PHE A 1 2662 ? 162.729 193.269 189.190 1.00 8.65   ? 2662 PHE A CB    1 
ATOM   9481  C  CG    . PHE A 1 2662 ? 163.964 192.591 189.697 1.00 11.81  ? 2662 PHE A CG    1 
ATOM   9482  C  CD1   . PHE A 1 2662 ? 165.170 192.742 189.036 1.00 10.61  ? 2662 PHE A CD1   1 
ATOM   9483  C  CD2   . PHE A 1 2662 ? 163.921 191.805 190.835 1.00 11.96  ? 2662 PHE A CD2   1 
ATOM   9484  C  CE1   . PHE A 1 2662 ? 166.310 192.122 189.500 1.00 13.66  ? 2662 PHE A CE1   1 
ATOM   9485  C  CE2   . PHE A 1 2662 ? 165.059 191.181 191.304 1.00 13.95  ? 2662 PHE A CE2   1 
ATOM   9486  C  CZ    . PHE A 1 2662 ? 166.255 191.339 190.635 1.00 15.60  ? 2662 PHE A CZ    1 
ATOM   9487  N  N     . CYS A 1 2663 ? 163.328 191.209 186.375 1.00 10.17  ? 2663 CYS A N     1 
ATOM   9488  C  CA    . CYS A 1 2663 ? 163.481 189.827 185.948 1.00 11.31  ? 2663 CYS A CA    1 
ATOM   9489  C  C     . CYS A 1 2663 ? 164.796 189.280 186.488 1.00 14.45  ? 2663 CYS A C     1 
ATOM   9490  O  O     . CYS A 1 2663 ? 165.860 189.862 186.257 1.00 15.26  ? 2663 CYS A O     1 
ATOM   9491  C  CB    . CYS A 1 2663 ? 163.435 189.731 184.424 1.00 14.79  ? 2663 CYS A CB    1 
ATOM   9492  S  SG    . CYS A 1 2663 ? 161.993 190.535 183.687 1.00 21.73  ? 2663 CYS A SG    1 
ATOM   9493  N  N     . ASP A 1 2664 ? 164.717 188.159 187.203 1.00 16.07  ? 2664 ASP A N     1 
ATOM   9494  C  CA    . ASP A 1 2664 ? 165.836 187.688 188.008 1.00 16.78  ? 2664 ASP A CA    1 
ATOM   9495  C  C     . ASP A 1 2664 ? 166.769 186.736 187.270 1.00 19.40  ? 2664 ASP A C     1 
ATOM   9496  O  O     . ASP A 1 2664 ? 167.920 186.580 187.691 1.00 23.73  ? 2664 ASP A O     1 
ATOM   9497  C  CB    . ASP A 1 2664 ? 165.312 186.997 189.271 1.00 16.47  ? 2664 ASP A CB    1 
ATOM   9498  C  CG    . ASP A 1 2664 ? 166.327 186.988 190.397 1.00 26.38  ? 2664 ASP A CG    1 
ATOM   9499  O  OD1   . ASP A 1 2664 ? 167.383 187.640 190.257 1.00 26.58  ? 2664 ASP A OD1   1 
ATOM   9500  O  OD2   . ASP A 1 2664 ? 166.067 186.327 191.424 1.00 30.66  ? 2664 ASP A OD2   1 
ATOM   9501  N  N     . GLU A 1 2665 ? 166.311 186.096 186.198 1.00 12.68  ? 2665 GLU A N     1 
ATOM   9502  C  CA    . GLU A 1 2665 ? 167.086 185.077 185.489 1.00 11.85  ? 2665 GLU A CA    1 
ATOM   9503  C  C     . GLU A 1 2665 ? 167.003 185.300 183.981 1.00 11.92  ? 2665 GLU A C     1 
ATOM   9504  O  O     . GLU A 1 2665 ? 166.678 184.393 183.215 1.00 11.81  ? 2665 GLU A O     1 
ATOM   9505  C  CB    . GLU A 1 2665 ? 166.606 183.673 185.857 1.00 13.65  ? 2665 GLU A CB    1 
ATOM   9506  C  CG    . GLU A 1 2665 ? 166.695 183.316 187.339 1.00 18.64  ? 2665 GLU A CG    1 
ATOM   9507  C  CD    . GLU A 1 2665 ? 168.121 183.098 187.818 1.00 25.38  ? 2665 GLU A CD    1 
ATOM   9508  O  OE1   . GLU A 1 2665 ? 168.852 184.087 188.025 1.00 27.76  ? 2665 GLU A OE1   1 
ATOM   9509  O  OE2   . GLU A 1 2665 ? 168.512 181.925 187.992 1.00 24.13  ? 2665 GLU A OE2   1 
ATOM   9510  N  N     . ILE A 1 2666 ? 167.290 186.529 183.538 1.00 8.84   ? 2666 ILE A N     1 
ATOM   9511  C  CA    . ILE A 1 2666 ? 167.017 186.923 182.154 1.00 8.58   ? 2666 ILE A CA    1 
ATOM   9512  C  C     . ILE A 1 2666 ? 167.738 186.035 181.147 1.00 9.44   ? 2666 ILE A C     1 
ATOM   9513  O  O     . ILE A 1 2666 ? 167.230 185.805 180.043 1.00 10.78  ? 2666 ILE A O     1 
ATOM   9514  C  CB    . ILE A 1 2666 ? 167.384 188.403 181.934 1.00 8.49   ? 2666 ILE A CB    1 
ATOM   9515  C  CG1   . ILE A 1 2666 ? 168.606 188.783 182.767 1.00 11.51  ? 2666 ILE A CG1   1 
ATOM   9516  C  CG2   . ILE A 1 2666 ? 166.205 189.301 182.251 1.00 9.16   ? 2666 ILE A CG2   1 
ATOM   9517  C  CD1   . ILE A 1 2666 ? 169.250 190.076 182.337 1.00 14.77  ? 2666 ILE A CD1   1 
ATOM   9518  N  N     . ASN A 1 2667 ? 168.924 185.534 181.485 1.00 8.53   ? 2667 ASN A N     1 
ATOM   9519  C  CA    . ASN A 1 2667 ? 169.706 184.732 180.554 1.00 7.96   ? 2667 ASN A CA    1 
ATOM   9520  C  C     . ASN A 1 2667 ? 169.412 183.241 180.673 1.00 8.08   ? 2667 ASN A C     1 
ATOM   9521  O  O     . ASN A 1 2667 ? 170.065 182.434 180.004 1.00 11.82  ? 2667 ASN A O     1 
ATOM   9522  C  CB    . ASN A 1 2667 ? 171.200 184.994 180.754 1.00 9.04   ? 2667 ASN A CB    1 
ATOM   9523  C  CG    . ASN A 1 2667 ? 171.650 184.746 182.175 1.00 11.76  ? 2667 ASN A CG    1 
ATOM   9524  O  OD1   . ASN A 1 2667 ? 170.833 184.663 183.091 1.00 15.68  ? 2667 ASN A OD1   1 
ATOM   9525  N  ND2   . ASN A 1 2667 ? 172.959 184.637 182.370 1.00 11.79  ? 2667 ASN A ND2   1 
ATOM   9526  N  N     . LEU A 1 2668 ? 168.449 182.862 181.506 1.00 8.32   ? 2668 LEU A N     1 
ATOM   9527  C  CA    . LEU A 1 2668 ? 168.027 181.477 181.691 1.00 9.60   ? 2668 LEU A CA    1 
ATOM   9528  C  C     . LEU A 1 2668 ? 167.112 180.963 180.578 1.00 11.35  ? 2668 LEU A C     1 
ATOM   9529  O  O     . LEU A 1 2668 ? 167.249 179.797 180.185 1.00 16.47  ? 2668 LEU A O     1 
ATOM   9530  C  CB    . LEU A 1 2668 ? 167.334 181.311 183.046 1.00 10.52  ? 2668 LEU A CB    1 
ATOM   9531  C  CG    . LEU A 1 2668 ? 168.102 180.563 184.136 1.00 14.23  ? 2668 LEU A CG    1 
ATOM   9532  C  CD1   . LEU A 1 2668 ? 167.140 179.971 185.148 1.00 18.70  ? 2668 LEU A CD1   1 
ATOM   9533  C  CD2   . LEU A 1 2668 ? 168.980 179.479 183.541 1.00 17.32  ? 2668 LEU A CD2   1 
ATOM   9534  N  N     . PRO A 1 2669 ? 166.136 181.772 180.065 1.00 8.75   ? 2669 PRO A N     1 
ATOM   9535  C  CA    . PRO A 1 2669 ? 165.236 181.269 179.015 1.00 8.80   ? 2669 PRO A CA    1 
ATOM   9536  C  C     . PRO A 1 2669 ? 165.915 180.502 177.892 1.00 9.62   ? 2669 PRO A C     1 
ATOM   9537  O  O     . PRO A 1 2669 ? 167.027 180.831 177.468 1.00 13.87  ? 2669 PRO A O     1 
ATOM   9538  C  CB    . PRO A 1 2669 ? 164.585 182.551 178.490 1.00 10.09  ? 2669 PRO A CB    1 
ATOM   9539  C  CG    . PRO A 1 2669 ? 164.473 183.393 179.694 1.00 8.27   ? 2669 PRO A CG    1 
ATOM   9540  C  CD    . PRO A 1 2669 ? 165.669 183.082 180.560 1.00 8.19   ? 2669 PRO A CD    1 
ATOM   9541  N  N     . ASP A 1 2670 ? 165.229 179.467 177.414 1.00 12.97  ? 2670 ASP A N     1 
ATOM   9542  C  CA    . ASP A 1 2670 ? 165.811 178.537 176.458 1.00 13.99  ? 2670 ASP A CA    1 
ATOM   9543  C  C     . ASP A 1 2670 ? 166.099 179.222 175.129 1.00 14.37  ? 2670 ASP A C     1 
ATOM   9544  O  O     . ASP A 1 2670 ? 165.292 180.014 174.633 1.00 15.27  ? 2670 ASP A O     1 
ATOM   9545  C  CB    . ASP A 1 2670 ? 164.868 177.355 176.241 1.00 15.97  ? 2670 ASP A CB    1 
ATOM   9546  C  CG    . ASP A 1 2670 ? 165.202 176.173 177.126 1.00 26.82  ? 2670 ASP A CG    1 
ATOM   9547  O  OD1   . ASP A 1 2670 ? 166.398 175.968 177.419 1.00 28.73  ? 2670 ASP A OD1   1 
ATOM   9548  O  OD2   . ASP A 1 2670 ? 164.268 175.451 177.531 1.00 27.17  ? 2670 ASP A OD2   1 
ATOM   9549  N  N     . MET A 1 2671 ? 167.258 178.915 174.561 1.00 16.42  ? 2671 MET A N     1 
ATOM   9550  C  CA    . MET A 1 2671 ? 167.599 179.302 173.201 1.00 14.57  ? 2671 MET A CA    1 
ATOM   9551  C  C     . MET A 1 2671 ? 167.193 178.178 172.261 1.00 17.79  ? 2671 MET A C     1 
ATOM   9552  O  O     . MET A 1 2671 ? 167.452 177.004 172.543 1.00 25.89  ? 2671 MET A O     1 
ATOM   9553  C  CB    . MET A 1 2671 ? 169.095 179.586 173.068 1.00 11.10  ? 2671 MET A CB    1 
ATOM   9554  C  CG    . MET A 1 2671 ? 169.592 180.714 173.947 1.00 18.00  ? 2671 MET A CG    1 
ATOM   9555  S  SD    . MET A 1 2671 ? 170.538 181.939 173.027 1.00 23.16  ? 2671 MET A SD    1 
ATOM   9556  C  CE    . MET A 1 2671 ? 171.655 180.877 172.117 1.00 15.12  ? 2671 MET A CE    1 
ATOM   9557  N  N     . ASP A 1 2672 ? 166.556 178.536 171.151 1.00 15.19  ? 2672 ASP A N     1 
ATOM   9558  C  CA    . ASP A 1 2672 ? 166.217 177.543 170.146 1.00 15.78  ? 2672 ASP A CA    1 
ATOM   9559  C  C     . ASP A 1 2672 ? 167.479 177.115 169.399 1.00 20.06  ? 2672 ASP A C     1 
ATOM   9560  O  O     . ASP A 1 2672 ? 168.596 177.539 169.709 1.00 19.18  ? 2672 ASP A O     1 
ATOM   9561  C  CB    . ASP A 1 2672 ? 165.160 178.093 169.190 1.00 15.31  ? 2672 ASP A CB    1 
ATOM   9562  C  CG    . ASP A 1 2672 ? 165.472 179.501 168.718 1.00 18.00  ? 2672 ASP A CG    1 
ATOM   9563  O  OD1   . ASP A 1 2672 ? 164.543 180.183 168.239 1.00 13.72  ? 2672 ASP A OD1   1 
ATOM   9564  O  OD2   . ASP A 1 2672 ? 166.640 179.930 168.830 1.00 19.86  ? 2672 ASP A OD2   1 
ATOM   9565  N  N     . LYS A 1 2673 ? 167.298 176.262 168.391 1.00 17.22  ? 2673 LYS A N     1 
ATOM   9566  C  CA    . LYS A 1 2673 ? 168.432 175.808 167.598 1.00 17.11  ? 2673 LYS A CA    1 
ATOM   9567  C  C     . LYS A 1 2673 ? 169.009 176.907 166.717 1.00 17.86  ? 2673 LYS A C     1 
ATOM   9568  O  O     . LYS A 1 2673 ? 170.029 176.676 166.059 1.00 19.19  ? 2673 LYS A O     1 
ATOM   9569  C  CB    . LYS A 1 2673 ? 168.026 174.608 166.740 1.00 19.35  ? 2673 LYS A CB    1 
ATOM   9570  C  CG    . LYS A 1 2673 ? 166.717 174.797 165.996 1.00 20.13  ? 2673 LYS A CG    1 
ATOM   9571  C  CD    . LYS A 1 2673 ? 166.521 173.730 164.932 1.00 23.79  ? 2673 LYS A CD    1 
ATOM   9572  C  CE    . LYS A 1 2673 ? 166.182 172.385 165.552 1.00 31.32  ? 2673 LYS A CE    1 
ATOM   9573  N  NZ    . LYS A 1 2673 ? 165.893 171.360 164.513 1.00 32.15  ? 2673 LYS A NZ    1 
ATOM   9574  N  N     . TYR A 1 2674 ? 168.386 178.086 166.687 1.00 19.51  ? 2674 TYR A N     1 
ATOM   9575  C  CA    . TYR A 1 2674 ? 168.841 179.200 165.867 1.00 14.45  ? 2674 TYR A CA    1 
ATOM   9576  C  C     . TYR A 1 2674 ? 169.339 180.374 166.704 1.00 14.33  ? 2674 TYR A C     1 
ATOM   9577  O  O     . TYR A 1 2674 ? 169.374 181.508 166.217 1.00 17.75  ? 2674 TYR A O     1 
ATOM   9578  C  CB    . TYR A 1 2674 ? 167.721 179.644 164.928 1.00 13.94  ? 2674 TYR A CB    1 
ATOM   9579  C  CG    . TYR A 1 2674 ? 167.120 178.502 164.142 1.00 15.96  ? 2674 TYR A CG    1 
ATOM   9580  C  CD1   . TYR A 1 2674 ? 167.818 177.907 163.100 1.00 16.78  ? 2674 TYR A CD1   1 
ATOM   9581  C  CD2   . TYR A 1 2674 ? 165.853 178.020 164.439 1.00 14.48  ? 2674 TYR A CD2   1 
ATOM   9582  C  CE1   . TYR A 1 2674 ? 167.273 176.862 162.382 1.00 16.33  ? 2674 TYR A CE1   1 
ATOM   9583  C  CE2   . TYR A 1 2674 ? 165.298 176.979 163.722 1.00 17.38  ? 2674 TYR A CE2   1 
ATOM   9584  C  CZ    . TYR A 1 2674 ? 166.013 176.403 162.696 1.00 20.32  ? 2674 TYR A CZ    1 
ATOM   9585  O  OH    . TYR A 1 2674 ? 165.465 175.363 161.981 1.00 23.89  ? 2674 TYR A OH    1 
ATOM   9586  N  N     . GLY A 1 2675 ? 169.717 180.125 167.956 1.00 15.50  ? 2675 GLY A N     1 
ATOM   9587  C  CA    . GLY A 1 2675 ? 170.332 181.139 168.792 1.00 14.92  ? 2675 GLY A CA    1 
ATOM   9588  C  C     . GLY A 1 2675 ? 169.450 182.322 169.133 1.00 14.20  ? 2675 GLY A C     1 
ATOM   9589  O  O     . GLY A 1 2675 ? 169.890 183.472 169.036 1.00 15.52  ? 2675 GLY A O     1 
ATOM   9590  N  N     . THR A 1 2676 ? 168.207 182.063 169.531 1.00 14.85  ? 2676 THR A N     1 
ATOM   9591  C  CA    . THR A 1 2676 ? 167.272 183.132 169.856 1.00 11.59  ? 2676 THR A CA    1 
ATOM   9592  C  C     . THR A 1 2676 ? 166.474 182.764 171.098 1.00 11.84  ? 2676 THR A C     1 
ATOM   9593  O  O     . THR A 1 2676 ? 166.025 181.622 171.234 1.00 13.78  ? 2676 THR A O     1 
ATOM   9594  C  CB    . THR A 1 2676 ? 166.322 183.405 168.683 1.00 12.81  ? 2676 THR A CB    1 
ATOM   9595  O  OG1   . THR A 1 2676 ? 167.072 183.880 167.559 1.00 13.84  ? 2676 THR A OG1   1 
ATOM   9596  C  CG2   . THR A 1 2676 ? 165.277 184.446 169.061 1.00 10.91  ? 2676 THR A CG2   1 
ATOM   9597  N  N     . GLN A 1 2677 ? 166.306 183.730 171.998 1.00 13.11  ? 2677 GLN A N     1 
ATOM   9598  C  CA    . GLN A 1 2677 ? 165.385 183.615 173.121 1.00 10.45  ? 2677 GLN A CA    1 
ATOM   9599  C  C     . GLN A 1 2677 ? 164.173 184.493 172.835 1.00 7.39   ? 2677 GLN A C     1 
ATOM   9600  O  O     . GLN A 1 2677 ? 164.313 185.707 172.651 1.00 9.10   ? 2677 GLN A O     1 
ATOM   9601  C  CB    . GLN A 1 2677 ? 166.052 184.024 174.433 1.00 9.20   ? 2677 GLN A CB    1 
ATOM   9602  C  CG    . GLN A 1 2677 ? 167.147 183.080 174.889 1.00 9.19   ? 2677 GLN A CG    1 
ATOM   9603  C  CD    . GLN A 1 2677 ? 168.113 183.733 175.854 1.00 13.61  ? 2677 GLN A CD    1 
ATOM   9604  O  OE1   . GLN A 1 2677 ? 168.782 184.709 175.516 1.00 23.12  ? 2677 GLN A OE1   1 
ATOM   9605  N  NE2   . GLN A 1 2677 ? 168.192 183.197 177.066 1.00 8.09   ? 2677 GLN A NE2   1 
ATOM   9606  N  N     . ARG A 1 2678 ? 162.990 183.876 172.795 1.00 6.99   ? 2678 ARG A N     1 
ATOM   9607  C  CA    . ARG A 1 2678 ? 161.789 184.596 172.382 1.00 6.77   ? 2678 ARG A CA    1 
ATOM   9608  C  C     . ARG A 1 2678 ? 161.461 185.735 173.341 1.00 7.31   ? 2678 ARG A C     1 
ATOM   9609  O  O     . ARG A 1 2678 ? 161.096 186.834 172.907 1.00 11.24  ? 2678 ARG A O     1 
ATOM   9610  C  CB    . ARG A 1 2678 ? 160.612 183.628 172.269 1.00 8.53   ? 2678 ARG A CB    1 
ATOM   9611  C  CG    . ARG A 1 2678 ? 159.305 184.287 171.862 1.00 10.95  ? 2678 ARG A CG    1 
ATOM   9612  C  CD    . ARG A 1 2678 ? 158.167 183.284 171.820 1.00 11.25  ? 2678 ARG A CD    1 
ATOM   9613  N  NE    . ARG A 1 2678 ? 158.386 182.253 170.813 1.00 15.74  ? 2678 ARG A NE    1 
ATOM   9614  C  CZ    . ARG A 1 2678 ? 157.591 181.209 170.627 1.00 16.66  ? 2678 ARG A CZ    1 
ATOM   9615  N  NH1   . ARG A 1 2678 ? 156.510 181.023 171.366 1.00 17.87  ? 2678 ARG A NH1   1 
ATOM   9616  N  NH2   . ARG A 1 2678 ? 157.888 180.329 169.675 1.00 11.97  ? 2678 ARG A NH2   1 
ATOM   9617  N  N     . VAL A 1 2679 ? 161.583 185.494 174.649 1.00 8.71   ? 2679 VAL A N     1 
ATOM   9618  C  CA    . VAL A 1 2679 ? 161.264 186.537 175.618 1.00 6.55   ? 2679 VAL A CA    1 
ATOM   9619  C  C     . VAL A 1 2679 ? 162.269 187.681 175.539 1.00 5.56   ? 2679 VAL A C     1 
ATOM   9620  O  O     . VAL A 1 2679 ? 161.911 188.844 175.757 1.00 6.03   ? 2679 VAL A O     1 
ATOM   9621  C  CB    . VAL A 1 2679 ? 161.173 185.946 177.039 1.00 6.65   ? 2679 VAL A CB    1 
ATOM   9622  C  CG1   . VAL A 1 2679 ? 162.538 185.505 177.537 1.00 6.00   ? 2679 VAL A CG1   1 
ATOM   9623  C  CG2   . VAL A 1 2679 ? 160.547 186.949 177.996 1.00 6.88   ? 2679 VAL A CG2   1 
ATOM   9624  N  N     . ILE A 1 2680 ? 163.532 187.382 175.224 1.00 6.92   ? 2680 ILE A N     1 
ATOM   9625  C  CA    . ILE A 1 2680 ? 164.534 188.437 175.111 1.00 5.65   ? 2680 ILE A CA    1 
ATOM   9626  C  C     . ILE A 1 2680 ? 164.245 189.314 173.900 1.00 6.63   ? 2680 ILE A C     1 
ATOM   9627  O  O     . ILE A 1 2680 ? 164.386 190.541 173.955 1.00 8.54   ? 2680 ILE A O     1 
ATOM   9628  C  CB    . ILE A 1 2680 ? 165.947 187.826 175.054 1.00 6.52   ? 2680 ILE A CB    1 
ATOM   9629  C  CG1   . ILE A 1 2680 ? 166.271 187.121 176.372 1.00 7.97   ? 2680 ILE A CG1   1 
ATOM   9630  C  CG2   . ILE A 1 2680 ? 166.986 188.897 174.760 1.00 10.64  ? 2680 ILE A CG2   1 
ATOM   9631  C  CD1   . ILE A 1 2680 ? 166.059 187.983 177.595 1.00 10.35  ? 2680 ILE A CD1   1 
ATOM   9632  N  N     . SER A 1 2681 ? 163.831 188.700 172.789 1.00 6.34   ? 2681 SER A N     1 
ATOM   9633  C  CA    . SER A 1 2681 ? 163.392 189.477 171.635 1.00 5.36   ? 2681 SER A CA    1 
ATOM   9634  C  C     . SER A 1 2681 ? 162.165 190.312 171.977 1.00 7.64   ? 2681 SER A C     1 
ATOM   9635  O  O     . SER A 1 2681 ? 162.039 191.459 171.533 1.00 10.52  ? 2681 SER A O     1 
ATOM   9636  C  CB    . SER A 1 2681 ? 163.097 188.547 170.459 1.00 7.16   ? 2681 SER A CB    1 
ATOM   9637  O  OG    . SER A 1 2681 ? 164.272 187.891 170.017 1.00 15.97  ? 2681 SER A OG    1 
ATOM   9638  N  N     . PHE A 1 2682 ? 161.245 189.744 172.759 1.00 6.98   ? 2682 PHE A N     1 
ATOM   9639  C  CA    . PHE A 1 2682 ? 160.063 190.482 173.192 1.00 5.22   ? 2682 PHE A CA    1 
ATOM   9640  C  C     . PHE A 1 2682 ? 160.450 191.702 174.021 1.00 5.84   ? 2682 PHE A C     1 
ATOM   9641  O  O     . PHE A 1 2682 ? 159.914 192.799 173.821 1.00 7.72   ? 2682 PHE A O     1 
ATOM   9642  C  CB    . PHE A 1 2682 ? 159.141 189.555 173.984 1.00 6.49   ? 2682 PHE A CB    1 
ATOM   9643  C  CG    . PHE A 1 2682 ? 157.794 190.144 174.285 1.00 9.61   ? 2682 PHE A CG    1 
ATOM   9644  C  CD1   . PHE A 1 2682 ? 156.891 190.398 173.268 1.00 10.89  ? 2682 PHE A CD1   1 
ATOM   9645  C  CD2   . PHE A 1 2682 ? 157.425 190.428 175.587 1.00 9.51   ? 2682 PHE A CD2   1 
ATOM   9646  C  CE1   . PHE A 1 2682 ? 155.649 190.935 173.544 1.00 9.12   ? 2682 PHE A CE1   1 
ATOM   9647  C  CE2   . PHE A 1 2682 ? 156.184 190.966 175.870 1.00 9.72   ? 2682 PHE A CE2   1 
ATOM   9648  C  CZ    . PHE A 1 2682 ? 155.296 191.220 174.846 1.00 7.94   ? 2682 PHE A CZ    1 
ATOM   9649  N  N     . ILE A 1 2683 ? 161.382 191.529 174.961 1.00 5.22   ? 2683 ILE A N     1 
ATOM   9650  C  CA    . ILE A 1 2683 ? 161.829 192.652 175.781 1.00 5.19   ? 2683 ILE A CA    1 
ATOM   9651  C  C     . ILE A 1 2683 ? 162.637 193.636 174.946 1.00 6.96   ? 2683 ILE A C     1 
ATOM   9652  O  O     . ILE A 1 2683 ? 162.528 194.856 175.120 1.00 8.61   ? 2683 ILE A O     1 
ATOM   9653  C  CB    . ILE A 1 2683 ? 162.627 192.145 176.996 1.00 5.63   ? 2683 ILE A CB    1 
ATOM   9654  C  CG1   . ILE A 1 2683 ? 161.757 191.233 177.861 1.00 7.54   ? 2683 ILE A CG1   1 
ATOM   9655  C  CG2   . ILE A 1 2683 ? 163.142 193.310 177.825 1.00 4.85   ? 2683 ILE A CG2   1 
ATOM   9656  C  CD1   . ILE A 1 2683 ? 162.508 190.565 178.989 1.00 8.60   ? 2683 ILE A CD1   1 
ATOM   9657  N  N     . ARG A 1 2684 ? 163.463 193.125 174.028 1.00 6.38   ? 2684 ARG A N     1 
ATOM   9658  C  CA    . ARG A 1 2684 ? 164.223 194.003 173.145 1.00 5.34   ? 2684 ARG A CA    1 
ATOM   9659  C  C     . ARG A 1 2684 ? 163.296 194.837 172.272 1.00 5.72   ? 2684 ARG A C     1 
ATOM   9660  O  O     . ARG A 1 2684 ? 163.532 196.033 172.066 1.00 6.19   ? 2684 ARG A O     1 
ATOM   9661  C  CB    . ARG A 1 2684 ? 165.182 193.174 172.288 1.00 5.89   ? 2684 ARG A CB    1 
ATOM   9662  C  CG    . ARG A 1 2684 ? 166.125 193.985 171.416 1.00 5.07   ? 2684 ARG A CG    1 
ATOM   9663  C  CD    . ARG A 1 2684 ? 165.647 194.036 169.974 1.00 7.09   ? 2684 ARG A CD    1 
ATOM   9664  N  NE    . ARG A 1 2684 ? 166.582 194.752 169.114 1.00 12.72  ? 2684 ARG A NE    1 
ATOM   9665  C  CZ    . ARG A 1 2684 ? 166.350 195.055 167.845 1.00 11.57  ? 2684 ARG A CZ    1 
ATOM   9666  N  NH1   . ARG A 1 2684 ? 165.225 194.704 167.245 1.00 12.74  ? 2684 ARG A NH1   1 
ATOM   9667  N  NH2   . ARG A 1 2684 ? 167.271 195.726 167.159 1.00 8.82   ? 2684 ARG A NH2   1 
ATOM   9668  N  N     . GLN A 1 2685 ? 162.234 194.221 171.750 1.00 7.16   ? 2685 GLN A N     1 
ATOM   9669  C  CA    . GLN A 1 2685 ? 161.236 194.970 170.994 1.00 6.68   ? 2685 GLN A CA    1 
ATOM   9670  C  C     . GLN A 1 2685 ? 160.539 195.998 171.875 1.00 5.87   ? 2685 GLN A C     1 
ATOM   9671  O  O     . GLN A 1 2685 ? 160.263 197.120 171.434 1.00 5.78   ? 2685 GLN A O     1 
ATOM   9672  C  CB    . GLN A 1 2685 ? 160.220 194.005 170.382 1.00 6.65   ? 2685 GLN A CB    1 
ATOM   9673  C  CG    . GLN A 1 2685 ? 158.800 194.532 170.340 1.00 7.76   ? 2685 GLN A CG    1 
ATOM   9674  C  CD    . GLN A 1 2685 ? 157.941 193.816 169.320 1.00 8.76   ? 2685 GLN A CD    1 
ATOM   9675  O  OE1   . GLN A 1 2685 ? 158.114 192.624 169.074 1.00 13.14  ? 2685 GLN A OE1   1 
ATOM   9676  N  NE2   . GLN A 1 2685 ? 157.010 194.542 168.717 1.00 10.97  ? 2685 GLN A NE2   1 
ATOM   9677  N  N     . MET A 1 2686 ? 160.253 195.634 173.127 1.00 7.67   ? 2686 MET A N     1 
ATOM   9678  C  CA    . MET A 1 2686 ? 159.543 196.531 174.030 1.00 6.07   ? 2686 MET A CA    1 
ATOM   9679  C  C     . MET A 1 2686 ? 160.394 197.719 174.456 1.00 5.84   ? 2686 MET A C     1 
ATOM   9680  O  O     . MET A 1 2686 ? 159.840 198.751 174.848 1.00 7.52   ? 2686 MET A O     1 
ATOM   9681  C  CB    . MET A 1 2686 ? 159.078 195.760 175.265 1.00 6.51   ? 2686 MET A CB    1 
ATOM   9682  C  CG    . MET A 1 2686 ? 157.590 195.466 175.289 1.00 9.13   ? 2686 MET A CG    1 
ATOM   9683  S  SD    . MET A 1 2686 ? 157.107 194.644 176.815 1.00 37.24  ? 2686 MET A SD    1 
ATOM   9684  C  CE    . MET A 1 2686 ? 158.423 193.441 176.966 1.00 10.09  ? 2686 MET A CE    1 
ATOM   9685  N  N     . VAL A 1 2687 ? 161.716 197.598 174.396 1.00 6.82   ? 2687 VAL A N     1 
ATOM   9686  C  CA    . VAL A 1 2687 ? 162.607 198.692 174.772 1.00 6.30   ? 2687 VAL A CA    1 
ATOM   9687  C  C     . VAL A 1 2687 ? 163.040 199.497 173.556 1.00 7.32   ? 2687 VAL A C     1 
ATOM   9688  O  O     . VAL A 1 2687 ? 163.020 200.731 173.574 1.00 8.80   ? 2687 VAL A O     1 
ATOM   9689  C  CB    . VAL A 1 2687 ? 163.825 198.137 175.541 1.00 7.39   ? 2687 VAL A CB    1 
ATOM   9690  C  CG1   . VAL A 1 2687 ? 164.892 199.206 175.681 1.00 9.61   ? 2687 VAL A CG1   1 
ATOM   9691  C  CG2   . VAL A 1 2687 ? 163.402 197.622 176.905 1.00 6.33   ? 2687 VAL A CG2   1 
ATOM   9692  N  N     . GLU A 1 2688 ? 163.439 198.813 172.481 1.00 6.28   ? 2688 GLU A N     1 
ATOM   9693  C  CA    . GLU A 1 2688 ? 163.900 199.511 171.286 1.00 5.91   ? 2688 GLU A CA    1 
ATOM   9694  C  C     . GLU A 1 2688 ? 162.755 200.236 170.589 1.00 7.49   ? 2688 GLU A C     1 
ATOM   9695  O  O     . GLU A 1 2688 ? 162.932 201.356 170.095 1.00 11.02  ? 2688 GLU A O     1 
ATOM   9696  C  CB    . GLU A 1 2688 ? 164.579 198.523 170.336 1.00 7.63   ? 2688 GLU A CB    1 
ATOM   9697  C  CG    . GLU A 1 2688 ? 164.382 198.817 168.859 1.00 11.96  ? 2688 GLU A CG    1 
ATOM   9698  C  CD    . GLU A 1 2688 ? 165.442 199.744 168.300 1.00 13.67  ? 2688 GLU A CD    1 
ATOM   9699  O  OE1   . GLU A 1 2688 ? 166.539 199.821 168.891 1.00 13.58  ? 2688 GLU A OE1   1 
ATOM   9700  O  OE2   . GLU A 1 2688 ? 165.180 200.394 167.266 1.00 17.58  ? 2688 GLU A OE2   1 
ATOM   9701  N  N     . HIS A 1 2689 ? 161.574 199.621 170.545 1.00 6.10   ? 2689 HIS A N     1 
ATOM   9702  C  CA    . HIS A 1 2689 ? 160.425 200.194 169.858 1.00 4.78   ? 2689 HIS A CA    1 
ATOM   9703  C  C     . HIS A 1 2689 ? 159.370 200.753 170.802 1.00 7.60   ? 2689 HIS A C     1 
ATOM   9704  O  O     . HIS A 1 2689 ? 158.433 201.408 170.336 1.00 10.04  ? 2689 HIS A O     1 
ATOM   9705  C  CB    . HIS A 1 2689 ? 159.787 199.146 168.939 1.00 6.87   ? 2689 HIS A CB    1 
ATOM   9706  C  CG    . HIS A 1 2689 ? 160.689 198.684 167.838 1.00 8.34   ? 2689 HIS A CG    1 
ATOM   9707  N  ND1   . HIS A 1 2689 ? 161.513 199.542 167.144 1.00 8.75   ? 2689 HIS A ND1   1 
ATOM   9708  C  CD2   . HIS A 1 2689 ? 160.904 197.453 167.318 1.00 7.53   ? 2689 HIS A CD2   1 
ATOM   9709  C  CE1   . HIS A 1 2689 ? 162.192 198.862 166.238 1.00 12.09  ? 2689 HIS A CE1   1 
ATOM   9710  N  NE2   . HIS A 1 2689 ? 161.842 197.591 166.324 1.00 11.50  ? 2689 HIS A NE2   1 
ATOM   9711  N  N     . GLY A 1 2690 ? 159.497 200.518 172.106 1.00 7.52   ? 2690 GLY A N     1 
ATOM   9712  C  CA    . GLY A 1 2690 ? 158.569 201.094 173.057 1.00 5.86   ? 2690 GLY A CA    1 
ATOM   9713  C  C     . GLY A 1 2690 ? 157.211 200.435 173.128 1.00 5.82   ? 2690 GLY A C     1 
ATOM   9714  O  O     . GLY A 1 2690 ? 156.252 201.070 173.574 1.00 9.98   ? 2690 GLY A O     1 
ATOM   9715  N  N     . GLY A 1 2691 ? 157.093 199.183 172.704 1.00 5.29   ? 2691 GLY A N     1 
ATOM   9716  C  CA    . GLY A 1 2691 ? 155.810 198.512 172.762 1.00 5.31   ? 2691 GLY A CA    1 
ATOM   9717  C  C     . GLY A 1 2691 ? 155.882 197.141 172.130 1.00 6.79   ? 2691 GLY A C     1 
ATOM   9718  O  O     . GLY A 1 2691 ? 156.961 196.638 171.817 1.00 7.48   ? 2691 GLY A O     1 
ATOM   9719  N  N     . PHE A 1 2692 ? 154.709 196.540 171.946 1.00 7.11   ? 2692 PHE A N     1 
ATOM   9720  C  CA    . PHE A 1 2692 ? 154.613 195.205 171.366 1.00 6.82   ? 2692 PHE A CA    1 
ATOM   9721  C  C     . PHE A 1 2692 ? 153.300 195.098 170.597 1.00 6.18   ? 2692 PHE A C     1 
ATOM   9722  O  O     . PHE A 1 2692 ? 152.567 196.079 170.443 1.00 6.73   ? 2692 PHE A O     1 
ATOM   9723  C  CB    . PHE A 1 2692 ? 154.728 194.126 172.451 1.00 8.31   ? 2692 PHE A CB    1 
ATOM   9724  C  CG    . PHE A 1 2692 ? 153.627 194.167 173.472 1.00 6.48   ? 2692 PHE A CG    1 
ATOM   9725  C  CD1   . PHE A 1 2692 ? 153.723 194.986 174.582 1.00 7.59   ? 2692 PHE A CD1   1 
ATOM   9726  C  CD2   . PHE A 1 2692 ? 152.499 193.378 173.323 1.00 5.71   ? 2692 PHE A CD2   1 
ATOM   9727  C  CE1   . PHE A 1 2692 ? 152.715 195.021 175.520 1.00 10.86  ? 2692 PHE A CE1   1 
ATOM   9728  C  CE2   . PHE A 1 2692 ? 151.487 193.410 174.257 1.00 7.72   ? 2692 PHE A CE2   1 
ATOM   9729  C  CZ    . PHE A 1 2692 ? 151.595 194.232 175.357 1.00 13.02  ? 2692 PHE A CZ    1 
ATOM   9730  N  N     . TYR A 1 2693 ? 152.998 193.895 170.099 1.00 6.23   ? 2693 TYR A N     1 
ATOM   9731  C  CA    . TYR A 1 2693 ? 151.722 193.678 169.361 1.00 6.97   ? 2693 TYR A CA    1 
ATOM   9732  C  C     . TYR A 1 2693 ? 150.826 192.733 170.154 1.00 10.31  ? 2693 TYR A C     1 
ATOM   9733  O  O     . TYR A 1 2693 ? 151.353 191.818 170.823 1.00 16.94  ? 2693 TYR A O     1 
ATOM   9734  C  CB    . TYR A 1 2693 ? 151.937 193.082 167.967 1.00 7.69   ? 2693 TYR A CB    1 
ATOM   9735  C  CG    . TYR A 1 2693 ? 152.523 194.026 166.927 1.00 7.89   ? 2693 TYR A CG    1 
ATOM   9736  C  CD1   . TYR A 1 2693 ? 151.704 194.850 166.165 1.00 8.80   ? 2693 TYR A CD1   1 
ATOM   9737  C  CD2   . TYR A 1 2693 ? 153.892 194.075 166.692 1.00 6.99   ? 2693 TYR A CD2   1 
ATOM   9738  C  CE1   . TYR A 1 2693 ? 152.230 195.706 165.212 1.00 8.22   ? 2693 TYR A CE1   1 
ATOM   9739  C  CE2   . TYR A 1 2693 ? 154.429 194.924 165.740 1.00 10.14  ? 2693 TYR A CE2   1 
ATOM   9740  C  CZ    . TYR A 1 2693 ? 153.596 195.742 164.998 1.00 11.81  ? 2693 TYR A CZ    1 
ATOM   9741  O  OH    . TYR A 1 2693 ? 154.121 196.583 164.060 1.00 23.58  ? 2693 TYR A OH    1 
ATOM   9742  N  N     . ARG A 1 2694 ? 149.508 192.941 170.084 1.00 9.67   ? 2694 ARG A N     1 
ATOM   9743  C  CA    . ARG A 1 2694 ? 148.560 192.016 170.758 1.00 10.80  ? 2694 ARG A CA    1 
ATOM   9744  C  C     . ARG A 1 2694 ? 148.104 190.965 169.736 1.00 13.67  ? 2694 ARG A C     1 
ATOM   9745  O  O     . ARG A 1 2694 ? 147.407 191.343 168.772 1.00 18.63  ? 2694 ARG A O     1 
ATOM   9746  C  CB    . ARG A 1 2694 ? 147.362 192.773 171.341 1.00 15.70  ? 2694 ARG A CB    1 
ATOM   9747  C  CG    . ARG A 1 2694 ? 147.710 193.662 172.525 1.00 20.82  ? 2694 ARG A CG    1 
ATOM   9748  C  CD    . ARG A 1 2694 ? 146.467 194.296 173.126 1.00 23.57  ? 2694 ARG A CD    1 
ATOM   9749  N  NE    . ARG A 1 2694 ? 145.717 195.075 172.136 1.00 30.12  ? 2694 ARG A NE    1 
ATOM   9750  C  CZ    . ARG A 1 2694 ? 144.602 195.744 172.397 1.00 26.56  ? 2694 ARG A CZ    1 
ATOM   9751  N  NH1   . ARG A 1 2694 ? 144.165 195.838 173.640 1.00 26.20  ? 2694 ARG A NH1   1 
ATOM   9752  N  NH2   . ARG A 1 2694 ? 143.931 196.319 171.416 1.00 25.52  ? 2694 ARG A NH2   1 
ATOM   9753  N  N     . THR A 1 2695 ? 148.476 189.700 169.948 1.00 15.14  ? 2695 THR A N     1 
ATOM   9754  C  CA    . THR A 1 2695 ? 148.137 188.631 168.982 1.00 19.46  ? 2695 THR A CA    1 
ATOM   9755  C  C     . THR A 1 2695 ? 146.632 188.533 168.857 1.00 21.79  ? 2695 THR A C     1 
ATOM   9756  O  O     . THR A 1 2695 ? 146.157 187.970 167.847 1.00 23.80  ? 2695 THR A O     1 
ATOM   9757  C  CB    . THR A 1 2695 ? 148.759 187.316 169.448 1.00 22.31  ? 2695 THR A CB    1 
ATOM   9758  O  OG1   . THR A 1 2695 ? 148.106 187.007 170.675 1.00 28.72  ? 2695 THR A OG1   1 
ATOM   9759  C  CG2   . THR A 1 2695 ? 150.256 187.432 169.668 1.00 18.08  ? 2695 THR A CG2   1 
ATOM   9760  N  N     . SER A 1 2696 ? 145.901 189.056 169.844 1.00 21.94  ? 2696 SER A N     1 
ATOM   9761  C  CA    . SER A 1 2696 ? 144.417 189.030 169.809 1.00 25.06  ? 2696 SER A CA    1 
ATOM   9762  C  C     . SER A 1 2696 ? 143.901 189.831 168.606 1.00 23.95  ? 2696 SER A C     1 
ATOM   9763  O  O     . SER A 1 2696 ? 142.972 189.340 167.929 1.00 33.68  ? 2696 SER A O     1 
ATOM   9764  C  CB    . SER A 1 2696 ? 143.845 189.566 171.092 1.00 26.12  ? 2696 SER A CB    1 
ATOM   9765  O  OG    . SER A 1 2696 ? 144.255 190.910 171.301 1.00 28.22  ? 2696 SER A OG    1 
ATOM   9766  N  N     . ASP A 1 2697 ? 144.478 191.008 168.348 1.00 19.51  ? 2697 ASP A N     1 
ATOM   9767  C  CA    . ASP A 1 2697 ? 143.961 191.879 167.256 1.00 22.16  ? 2697 ASP A CA    1 
ATOM   9768  C  C     . ASP A 1 2697 ? 145.117 192.449 166.426 1.00 23.58  ? 2697 ASP A C     1 
ATOM   9769  O  O     . ASP A 1 2697 ? 144.904 193.484 165.758 1.00 20.43  ? 2697 ASP A O     1 
ATOM   9770  C  CB    . ASP A 1 2697 ? 143.074 192.977 167.821 1.00 19.99  ? 2697 ASP A CB    1 
ATOM   9771  C  CG    . ASP A 1 2697 ? 143.642 193.715 169.025 1.00 28.84  ? 2697 ASP A CG    1 
ATOM   9772  O  OD1   . ASP A 1 2697 ? 144.765 193.370 169.451 1.00 26.60  ? 2697 ASP A OD1   1 
ATOM   9773  O  OD2   . ASP A 1 2697 ? 142.957 194.630 169.527 1.00 37.77  ? 2697 ASP A OD2   1 
ATOM   9774  N  N     . GLN A 1 2698 ? 146.288 191.804 166.462 1.00 20.69  ? 2698 GLN A N     1 
ATOM   9775  C  CA    . GLN A 1 2698 ? 147.472 192.322 165.727 1.00 17.18  ? 2698 GLN A CA    1 
ATOM   9776  C  C     . GLN A 1 2698 ? 147.548 193.842 165.921 1.00 17.06  ? 2698 GLN A C     1 
ATOM   9777  O  O     . GLN A 1 2698 ? 147.974 194.538 164.976 1.00 21.88  ? 2698 GLN A O     1 
ATOM   9778  C  CB    . GLN A 1 2698 ? 147.387 191.975 164.240 1.00 18.08  ? 2698 GLN A CB    1 
ATOM   9779  C  CG    . GLN A 1 2698 ? 147.655 190.508 163.920 1.00 14.53  ? 2698 GLN A CG    1 
ATOM   9780  C  CD    . GLN A 1 2698 ? 146.624 189.566 164.502 1.00 15.37  ? 2698 GLN A CD    1 
ATOM   9781  O  OE1   . GLN A 1 2698 ? 146.944 188.664 165.284 1.00 17.19  ? 2698 GLN A OE1   1 
ATOM   9782  N  NE2   . GLN A 1 2698 ? 145.372 189.764 164.118 1.00 18.39  ? 2698 GLN A NE2   1 
ATOM   9783  N  N     . THR A 1 2699 ? 147.150 194.331 167.098 1.00 15.23  ? 2699 THR A N     1 
ATOM   9784  C  CA    . THR A 1 2699 ? 147.146 195.763 167.365 1.00 17.38  ? 2699 THR A CA    1 
ATOM   9785  C  C     . THR A 1 2699 ? 148.419 196.149 168.104 1.00 12.88  ? 2699 THR A C     1 
ATOM   9786  O  O     . THR A 1 2699 ? 148.800 195.491 169.077 1.00 15.12  ? 2699 THR A O     1 
ATOM   9787  C  CB    . THR A 1 2699 ? 145.917 196.162 168.186 1.00 21.13  ? 2699 THR A CB    1 
ATOM   9788  O  OG1   . THR A 1 2699 ? 144.729 195.890 167.432 1.00 22.88  ? 2699 THR A OG1   1 
ATOM   9789  C  CG2   . THR A 1 2699 ? 145.961 197.642 168.536 1.00 16.00  ? 2699 THR A CG2   1 
ATOM   9790  N  N     . TRP A 1 2700 ? 149.073 197.211 167.638 1.00 11.30  ? 2700 TRP A N     1 
ATOM   9791  C  CA    . TRP A 1 2700 ? 150.266 197.716 168.305 1.00 6.97   ? 2700 TRP A CA    1 
ATOM   9792  C  C     . TRP A 1 2700 ? 149.893 198.329 169.648 1.00 7.42   ? 2700 TRP A C     1 
ATOM   9793  O  O     . TRP A 1 2700 ? 148.971 199.146 169.734 1.00 6.61   ? 2700 TRP A O     1 
ATOM   9794  C  CB    . TRP A 1 2700 ? 150.972 198.744 167.426 1.00 6.76   ? 2700 TRP A CB    1 
ATOM   9795  C  CG    . TRP A 1 2700 ? 152.190 199.332 168.068 1.00 6.04   ? 2700 TRP A CG    1 
ATOM   9796  C  CD1   . TRP A 1 2700 ? 152.301 200.569 168.633 1.00 6.11   ? 2700 TRP A CD1   1 
ATOM   9797  C  CD2   . TRP A 1 2700 ? 153.464 198.703 168.230 1.00 5.40   ? 2700 TRP A CD2   1 
ATOM   9798  N  NE1   . TRP A 1 2700 ? 153.568 200.753 169.128 1.00 5.52   ? 2700 TRP A NE1   1 
ATOM   9799  C  CE2   . TRP A 1 2700 ? 154.302 199.621 168.895 1.00 5.92   ? 2700 TRP A CE2   1 
ATOM   9800  C  CE3   . TRP A 1 2700 ? 153.980 197.454 167.875 1.00 4.93   ? 2700 TRP A CE3   1 
ATOM   9801  C  CZ2   . TRP A 1 2700 ? 155.626 199.329 169.210 1.00 6.62   ? 2700 TRP A CZ2   1 
ATOM   9802  C  CZ3   . TRP A 1 2700 ? 155.292 197.167 168.188 1.00 5.11   ? 2700 TRP A CZ3   1 
ATOM   9803  C  CH2   . TRP A 1 2700 ? 156.101 198.099 168.849 1.00 6.62   ? 2700 TRP A CH2   1 
ATOM   9804  N  N     . VAL A 1 2701 ? 150.612 197.934 170.694 1.00 9.36   ? 2701 VAL A N     1 
ATOM   9805  C  CA    . VAL A 1 2701 ? 150.418 198.450 172.042 1.00 7.33   ? 2701 VAL A CA    1 
ATOM   9806  C  C     . VAL A 1 2701 ? 151.667 199.228 172.424 1.00 7.78   ? 2701 VAL A C     1 
ATOM   9807  O  O     . VAL A 1 2701 ? 152.787 198.730 172.259 1.00 7.67   ? 2701 VAL A O     1 
ATOM   9808  C  CB    . VAL A 1 2701 ? 150.140 197.315 173.043 1.00 10.37  ? 2701 VAL A CB    1 
ATOM   9809  C  CG1   . VAL A 1 2701 ? 150.598 197.702 174.441 1.00 11.92  ? 2701 VAL A CG1   1 
ATOM   9810  C  CG2   . VAL A 1 2701 ? 148.667 196.952 173.036 1.00 16.19  ? 2701 VAL A CG2   1 
ATOM   9811  N  N     . LYS A 1 2702 ? 151.480 200.449 172.916 1.00 10.13  ? 2702 LYS A N     1 
ATOM   9812  C  CA    . LYS A 1 2702 ? 152.587 201.316 173.297 1.00 9.02   ? 2702 LYS A CA    1 
ATOM   9813  C  C     . LYS A 1 2702 ? 152.711 201.348 174.815 1.00 10.04  ? 2702 LYS A C     1 
ATOM   9814  O  O     . LYS A 1 2702 ? 151.739 201.648 175.516 1.00 15.82  ? 2702 LYS A O     1 
ATOM   9815  C  CB    . LYS A 1 2702 ? 152.380 202.729 172.748 1.00 11.11  ? 2702 LYS A CB    1 
ATOM   9816  C  CG    . LYS A 1 2702 ? 153.192 203.803 173.449 1.00 12.75  ? 2702 LYS A CG    1 
ATOM   9817  C  CD    . LYS A 1 2702 ? 153.192 205.096 172.651 1.00 16.28  ? 2702 LYS A CD    1 
ATOM   9818  C  CE    . LYS A 1 2702 ? 153.468 206.295 173.542 1.00 21.54  ? 2702 LYS A CE    1 
ATOM   9819  N  NZ    . LYS A 1 2702 ? 152.384 206.507 174.539 1.00 27.79  ? 2702 LYS A NZ    1 
ATOM   9820  N  N     . LEU A 1 2703 ? 153.904 201.035 175.316 1.00 9.20   ? 2703 LEU A N     1 
ATOM   9821  C  CA    . LEU A 1 2703 ? 154.131 201.036 176.755 1.00 10.16  ? 2703 LEU A CA    1 
ATOM   9822  C  C     . LEU A 1 2703 ? 154.191 202.459 177.293 1.00 10.16  ? 2703 LEU A C     1 
ATOM   9823  O  O     . LEU A 1 2703 ? 154.629 203.386 176.607 1.00 12.14  ? 2703 LEU A O     1 
ATOM   9824  C  CB    . LEU A 1 2703 ? 155.426 200.304 177.103 1.00 8.32   ? 2703 LEU A CB    1 
ATOM   9825  C  CG    . LEU A 1 2703 ? 155.745 198.948 176.477 1.00 7.16   ? 2703 LEU A CG    1 
ATOM   9826  C  CD1   . LEU A 1 2703 ? 156.855 198.294 177.274 1.00 7.94   ? 2703 LEU A CD1   1 
ATOM   9827  C  CD2   . LEU A 1 2703 ? 154.516 198.056 176.447 1.00 8.70   ? 2703 LEU A CD2   1 
ATOM   9828  N  N     . GLU A 1 2704 ? 153.742 202.626 178.534 1.00 11.43  ? 2704 GLU A N     1 
ATOM   9829  C  CA    . GLU A 1 2704 ? 153.791 203.909 179.219 1.00 13.65  ? 2704 GLU A CA    1 
ATOM   9830  C  C     . GLU A 1 2704 ? 154.040 203.665 180.698 1.00 13.54  ? 2704 GLU A C     1 
ATOM   9831  O  O     . GLU A 1 2704 ? 153.387 202.809 181.302 1.00 17.03  ? 2704 GLU A O     1 
ATOM   9832  C  CB    . GLU A 1 2704 ? 152.491 204.695 179.016 1.00 16.58  ? 2704 GLU A CB    1 
ATOM   9833  C  CG    . GLU A 1 2704 ? 152.579 206.160 179.402 1.00 22.61  ? 2704 GLU A CG    1 
ATOM   9834  C  CD    . GLU A 1 2704 ? 151.228 206.748 179.755 1.00 34.77  ? 2704 GLU A CD    1 
ATOM   9835  O  OE1   . GLU A 1 2704 ? 150.286 206.601 178.948 1.00 33.49  ? 2704 GLU A OE1   1 
ATOM   9836  O  OE2   . GLU A 1 2704 ? 151.108 207.353 180.841 1.00 33.05  ? 2704 GLU A OE2   1 
ATOM   9837  N  N     . ARG A 1 2705 ? 154.988 204.410 181.268 1.00 11.36  ? 2705 ARG A N     1 
ATOM   9838  C  CA    . ARG A 1 2705 ? 155.320 204.327 182.692 1.00 10.14  ? 2705 ARG A CA    1 
ATOM   9839  C  C     . ARG A 1 2705 ? 155.741 202.914 183.092 1.00 12.88  ? 2705 ARG A C     1 
ATOM   9840  O  O     . ARG A 1 2705 ? 155.464 202.455 184.202 1.00 14.75  ? 2705 ARG A O     1 
ATOM   9841  C  CB    . ARG A 1 2705 ? 154.157 204.811 183.560 1.00 15.34  ? 2705 ARG A CB    1 
ATOM   9842  C  CG    . ARG A 1 2705 ? 154.002 206.321 183.615 1.00 16.31  ? 2705 ARG A CG    1 
ATOM   9843  C  CD    . ARG A 1 2705 ? 152.915 206.721 184.597 1.00 20.23  ? 2705 ARG A CD    1 
ATOM   9844  N  NE    . ARG A 1 2705 ? 151.586 206.388 184.097 1.00 22.14  ? 2705 ARG A NE    1 
ATOM   9845  C  CZ    . ARG A 1 2705 ? 150.760 205.530 184.679 1.00 23.58  ? 2705 ARG A CZ    1 
ATOM   9846  N  NH1   . ARG A 1 2705 ? 151.091 204.898 185.793 1.00 25.11  ? 2705 ARG A NH1   1 
ATOM   9847  N  NH2   . ARG A 1 2705 ? 149.570 205.301 184.130 1.00 26.11  ? 2705 ARG A NH2   1 
ATOM   9848  N  N     . ILE A 1 2706 ? 156.419 202.208 182.182 1.00 12.49  ? 2706 ILE A N     1 
ATOM   9849  C  CA    . ILE A 1 2706 ? 156.852 200.806 182.472 1.00 7.86   ? 2706 ILE A CA    1 
ATOM   9850  C  C     . ILE A 1 2706 ? 158.355 200.668 182.179 1.00 10.32  ? 2706 ILE A C     1 
ATOM   9851  O  O     . ILE A 1 2706 ? 158.736 200.768 180.993 1.00 15.40  ? 2706 ILE A O     1 
ATOM   9852  C  CB    . ILE A 1 2706 ? 156.020 199.792 181.666 1.00 7.57   ? 2706 ILE A CB    1 
ATOM   9853  C  CG1   . ILE A 1 2706 ? 154.527 199.919 181.971 1.00 13.63  ? 2706 ILE A CG1   1 
ATOM   9854  C  CG2   . ILE A 1 2706 ? 156.524 198.367 181.897 1.00 8.94   ? 2706 ILE A CG2   1 
ATOM   9855  C  CD1   . ILE A 1 2706 ? 153.643 199.014 181.132 1.00 16.30  ? 2706 ILE A CD1   1 
ATOM   9856  N  N     . GLN A 1 2707 ? 159.167 200.449 183.219 1.00 10.43  ? 2707 GLN A N     1 
ATOM   9857  C  CA    . GLN A 1 2707 ? 160.636 200.292 183.041 1.00 10.59  ? 2707 GLN A CA    1 
ATOM   9858  C  C     . GLN A 1 2707 ? 161.027 198.824 183.271 1.00 8.76   ? 2707 GLN A C     1 
ATOM   9859  O  O     . GLN A 1 2707 ? 160.174 198.055 183.764 1.00 9.61   ? 2707 GLN A O     1 
ATOM   9860  C  CB    . GLN A 1 2707 ? 161.404 201.227 183.976 1.00 10.12  ? 2707 GLN A CB    1 
ATOM   9861  C  CG    . GLN A 1 2707 ? 160.745 201.431 185.335 1.00 9.77   ? 2707 GLN A CG    1 
ATOM   9862  C  CD    . GLN A 1 2707 ? 161.325 202.600 186.100 1.00 14.98  ? 2707 GLN A CD    1 
ATOM   9863  O  OE1   . GLN A 1 2707 ? 162.277 203.252 185.656 1.00 19.08  ? 2707 GLN A OE1   1 
ATOM   9864  N  NE2   . GLN A 1 2707 ? 160.753 202.876 187.262 1.00 21.58  ? 2707 GLN A NE2   1 
ATOM   9865  N  N     . PHE A 1 2708 ? 162.265 198.458 182.930 1.00 8.35   ? 2708 PHE A N     1 
ATOM   9866  C  CA    . PHE A 1 2708 ? 162.693 197.038 183.049 1.00 6.87   ? 2708 PHE A CA    1 
ATOM   9867  C  C     . PHE A 1 2708 ? 164.050 196.938 183.731 1.00 7.50   ? 2708 PHE A C     1 
ATOM   9868  O  O     . PHE A 1 2708 ? 164.969 197.704 183.371 1.00 6.81   ? 2708 PHE A O     1 
ATOM   9869  C  CB    . PHE A 1 2708 ? 162.762 196.396 181.660 1.00 10.02  ? 2708 PHE A CB    1 
ATOM   9870  C  CG    . PHE A 1 2708 ? 161.452 196.376 180.883 1.00 11.80  ? 2708 PHE A CG    1 
ATOM   9871  C  CD1   . PHE A 1 2708 ? 161.091 197.440 180.065 1.00 11.33  ? 2708 PHE A CD1   1 
ATOM   9872  C  CD2   . PHE A 1 2708 ? 160.593 195.286 180.963 1.00 10.52  ? 2708 PHE A CD2   1 
ATOM   9873  C  CE1   . PHE A 1 2708 ? 159.901 197.416 179.355 1.00 11.91  ? 2708 PHE A CE1   1 
ATOM   9874  C  CE2   . PHE A 1 2708 ? 159.405 195.267 180.249 1.00 15.90  ? 2708 PHE A CE2   1 
ATOM   9875  C  CZ    . PHE A 1 2708 ? 159.061 196.330 179.449 1.00 14.48  ? 2708 PHE A CZ    1 
ATOM   9876  N  N     . VAL A 1 2709 ? 164.179 196.024 184.694 1.00 9.41   ? 2709 VAL A N     1 
ATOM   9877  C  CA    . VAL A 1 2709 ? 165.450 195.768 185.358 1.00 6.00   ? 2709 VAL A CA    1 
ATOM   9878  C  C     . VAL A 1 2709 ? 165.727 194.276 185.267 1.00 7.16   ? 2709 VAL A C     1 
ATOM   9879  O  O     . VAL A 1 2709 ? 164.841 193.458 185.541 1.00 7.66   ? 2709 VAL A O     1 
ATOM   9880  C  CB    . VAL A 1 2709 ? 165.440 196.238 186.823 1.00 5.76   ? 2709 VAL A CB    1 
ATOM   9881  C  CG1   . VAL A 1 2709 ? 166.706 195.789 187.527 1.00 10.21  ? 2709 VAL A CG1   1 
ATOM   9882  C  CG2   . VAL A 1 2709 ? 165.310 197.747 186.888 1.00 6.84   ? 2709 VAL A CG2   1 
ATOM   9883  N  N     . GLY A 1 2710 ? 166.944 193.925 184.868 1.00 8.94   ? 2710 GLY A N     1 
ATOM   9884  C  CA    . GLY A 1 2710 ? 167.335 192.538 184.724 1.00 9.52   ? 2710 GLY A CA    1 
ATOM   9885  C  C     . GLY A 1 2710 ? 168.396 192.153 185.736 1.00 8.35   ? 2710 GLY A C     1 
ATOM   9886  O  O     . GLY A 1 2710 ? 169.228 192.971 186.132 1.00 9.19   ? 2710 GLY A O     1 
ATOM   9887  N  N     . ALA A 1 2711 ? 168.350 190.896 186.163 1.00 9.28   ? 2711 ALA A N     1 
ATOM   9888  C  CA    . ALA A 1 2711 ? 169.380 190.309 187.002 1.00 8.43   ? 2711 ALA A CA    1 
ATOM   9889  C  C     . ALA A 1 2711 ? 169.757 188.956 186.424 1.00 10.70  ? 2711 ALA A C     1 
ATOM   9890  O  O     . ALA A 1 2711 ? 168.918 188.258 185.851 1.00 14.16  ? 2711 ALA A O     1 
ATOM   9891  C  CB    . ALA A 1 2711 ? 168.922 190.148 188.454 1.00 12.59  ? 2711 ALA A CB    1 
ATOM   9892  N  N     . CYS A 1 2712 ? 171.029 188.596 186.563 1.00 9.91   ? 2712 CYS A N     1 
ATOM   9893  C  CA    . CYS A 1 2712 ? 171.494 187.333 186.014 1.00 10.59  ? 2712 CYS A CA    1 
ATOM   9894  C  C     . CYS A 1 2712 ? 172.845 186.981 186.612 1.00 12.08  ? 2712 CYS A C     1 
ATOM   9895  O  O     . CYS A 1 2712 ? 173.533 187.825 187.193 1.00 9.27   ? 2712 CYS A O     1 
ATOM   9896  C  CB    . CYS A 1 2712 ? 171.594 187.390 184.486 1.00 10.55  ? 2712 CYS A CB    1 
ATOM   9897  S  SG    . CYS A 1 2712 ? 172.497 188.818 183.864 1.00 29.93  ? 2712 CYS A SG    1 
ATOM   9898  N  N     . ASN A 1 2713 ? 173.205 185.719 186.460 1.00 13.10  ? 2713 ASN A N     1 
ATOM   9899  C  CA    . ASN A 1 2713 ? 174.536 185.198 186.708 1.00 9.85   ? 2713 ASN A CA    1 
ATOM   9900  C  C     . ASN A 1 2713 ? 175.383 185.338 185.452 1.00 13.51  ? 2713 ASN A C     1 
ATOM   9901  O  O     . ASN A 1 2713 ? 174.851 185.543 184.356 1.00 13.02  ? 2713 ASN A O     1 
ATOM   9902  C  CB    . ASN A 1 2713 ? 174.450 183.736 187.142 1.00 12.05  ? 2713 ASN A CB    1 
ATOM   9903  C  CG    . ASN A 1 2713 ? 173.695 183.559 188.445 1.00 12.77  ? 2713 ASN A CG    1 
ATOM   9904  O  OD1   . ASN A 1 2713 ? 173.544 184.503 189.221 1.00 12.76  ? 2713 ASN A OD1   1 
ATOM   9905  N  ND2   . ASN A 1 2713 ? 173.213 182.347 188.691 1.00 13.99  ? 2713 ASN A ND2   1 
ATOM   9906  N  N     . PRO A 1 2714 ? 176.707 185.261 185.572 1.00 13.07  ? 2714 PRO A N     1 
ATOM   9907  C  CA    . PRO A 1 2714 ? 177.567 185.381 184.388 1.00 11.44  ? 2714 PRO A CA    1 
ATOM   9908  C  C     . PRO A 1 2714 ? 177.211 184.340 183.344 1.00 14.96  ? 2714 PRO A C     1 
ATOM   9909  O  O     . PRO A 1 2714 ? 176.860 183.200 183.683 1.00 17.29  ? 2714 PRO A O     1 
ATOM   9910  C  CB    . PRO A 1 2714 ? 178.974 185.147 184.953 1.00 12.29  ? 2714 PRO A CB    1 
ATOM   9911  C  CG    . PRO A 1 2714 ? 178.879 185.611 186.358 1.00 11.66  ? 2714 PRO A CG    1 
ATOM   9912  C  CD    . PRO A 1 2714 ? 177.494 185.254 186.819 1.00 11.42  ? 2714 PRO A CD    1 
ATOM   9913  N  N     . PRO A 1 2715 ? 177.278 184.700 182.059 1.00 13.17  ? 2715 PRO A N     1 
ATOM   9914  C  CA    . PRO A 1 2715 ? 176.859 183.758 181.007 1.00 13.31  ? 2715 PRO A CA    1 
ATOM   9915  C  C     . PRO A 1 2715 ? 177.692 182.493 180.952 1.00 18.40  ? 2715 PRO A C     1 
ATOM   9916  O  O     . PRO A 1 2715 ? 177.234 181.494 180.385 1.00 21.88  ? 2715 PRO A O     1 
ATOM   9917  C  CB    . PRO A 1 2715 ? 177.005 184.581 179.720 1.00 12.38  ? 2715 PRO A CB    1 
ATOM   9918  C  CG    . PRO A 1 2715 ? 177.963 185.674 180.066 1.00 13.74  ? 2715 PRO A CG    1 
ATOM   9919  C  CD    . PRO A 1 2715 ? 177.717 185.992 181.508 1.00 13.05  ? 2715 PRO A CD    1 
ATOM   9920  N  N     . THR A 1 2716 ? 178.900 182.503 181.513 1.00 18.92  ? 2716 THR A N     1 
ATOM   9921  C  CA    . THR A 1 2716 ? 179.722 181.303 181.571 1.00 19.43  ? 2716 THR A CA    1 
ATOM   9922  C  C     . THR A 1 2716 ? 179.204 180.279 182.572 1.00 21.43  ? 2716 THR A C     1 
ATOM   9923  O  O     . THR A 1 2716 ? 179.675 179.137 182.564 1.00 26.21  ? 2716 THR A O     1 
ATOM   9924  C  CB    . THR A 1 2716 ? 181.165 181.674 181.918 1.00 24.29  ? 2716 THR A CB    1 
ATOM   9925  O  OG1   . THR A 1 2716 ? 181.192 182.372 183.169 1.00 24.60  ? 2716 THR A OG1   1 
ATOM   9926  C  CG2   . THR A 1 2716 ? 181.756 182.564 180.836 1.00 17.93  ? 2716 THR A CG2   1 
ATOM   9927  N  N     . ASP A 1 2717 ? 178.255 180.655 183.427 1.00 18.11  ? 2717 ASP A N     1 
ATOM   9928  C  CA    . ASP A 1 2717 ? 177.690 179.714 184.378 1.00 17.69  ? 2717 ASP A CA    1 
ATOM   9929  C  C     . ASP A 1 2717 ? 176.821 178.687 183.653 1.00 16.35  ? 2717 ASP A C     1 
ATOM   9930  O  O     . ASP A 1 2717 ? 176.224 178.990 182.616 1.00 15.84  ? 2717 ASP A O     1 
ATOM   9931  C  CB    . ASP A 1 2717 ? 176.858 180.451 185.425 1.00 18.51  ? 2717 ASP A CB    1 
ATOM   9932  C  CG    . ASP A 1 2717 ? 177.711 181.085 186.506 1.00 23.05  ? 2717 ASP A CG    1 
ATOM   9933  O  OD1   . ASP A 1 2717 ? 178.946 181.141 186.335 1.00 22.08  ? 2717 ASP A OD1   1 
ATOM   9934  O  OD2   . ASP A 1 2717 ? 177.144 181.532 187.525 1.00 23.97  ? 2717 ASP A OD2   1 
ATOM   9935  N  N     . PRO A 1 2718 ? 176.745 177.460 184.170 1.00 17.96  ? 2718 PRO A N     1 
ATOM   9936  C  CA    . PRO A 1 2718 ? 175.940 176.430 183.501 1.00 19.82  ? 2718 PRO A CA    1 
ATOM   9937  C  C     . PRO A 1 2718 ? 174.470 176.817 183.439 1.00 18.24  ? 2718 PRO A C     1 
ATOM   9938  O  O     . PRO A 1 2718 ? 173.906 177.355 184.394 1.00 18.02  ? 2718 PRO A O     1 
ATOM   9939  C  CB    . PRO A 1 2718 ? 176.162 175.186 184.369 1.00 14.72  ? 2718 PRO A CB    1 
ATOM   9940  C  CG    . PRO A 1 2718 ? 176.618 175.710 185.687 1.00 16.51  ? 2718 PRO A CG    1 
ATOM   9941  C  CD    . PRO A 1 2718 ? 177.403 176.945 185.382 1.00 18.18  ? 2718 PRO A CD    1 
ATOM   9942  N  N     . GLY A 1 2719 ? 173.851 176.534 182.294 1.00 14.71  ? 2719 GLY A N     1 
ATOM   9943  C  CA    . GLY A 1 2719 ? 172.464 176.863 182.063 1.00 14.44  ? 2719 GLY A CA    1 
ATOM   9944  C  C     . GLY A 1 2719 ? 172.208 178.289 181.627 1.00 17.87  ? 2719 GLY A C     1 
ATOM   9945  O  O     . GLY A 1 2719 ? 171.065 178.620 181.291 1.00 19.25  ? 2719 GLY A O     1 
ATOM   9946  N  N     . ARG A 1 2720 ? 173.232 179.135 181.605 1.00 17.02  ? 2720 ARG A N     1 
ATOM   9947  C  CA    . ARG A 1 2720 ? 173.091 180.534 181.231 1.00 14.23  ? 2720 ARG A CA    1 
ATOM   9948  C  C     . ARG A 1 2720 ? 173.597 180.742 179.811 1.00 17.14  ? 2720 ARG A C     1 
ATOM   9949  O  O     . ARG A 1 2720 ? 174.567 180.108 179.387 1.00 19.25  ? 2720 ARG A O     1 
ATOM   9950  C  CB    . ARG A 1 2720 ? 173.856 181.436 182.200 1.00 13.83  ? 2720 ARG A CB    1 
ATOM   9951  C  CG    . ARG A 1 2720 ? 173.646 181.088 183.665 1.00 16.11  ? 2720 ARG A CG    1 
ATOM   9952  C  CD    . ARG A 1 2720 ? 172.189 181.236 184.063 1.00 17.06  ? 2720 ARG A CD    1 
ATOM   9953  N  NE    . ARG A 1 2720 ? 171.996 181.101 185.502 1.00 22.14  ? 2720 ARG A NE    1 
ATOM   9954  C  CZ    . ARG A 1 2720 ? 171.921 179.943 186.144 1.00 21.86  ? 2720 ARG A CZ    1 
ATOM   9955  N  NH1   . ARG A 1 2720 ? 172.028 178.789 185.504 1.00 20.70  ? 2720 ARG A NH1   1 
ATOM   9956  N  NH2   . ARG A 1 2720 ? 171.728 179.942 187.459 1.00 22.98  ? 2720 ARG A NH2   1 
ATOM   9957  N  N     . LYS A 1 2721 ? 172.932 181.630 179.080 1.00 12.35  ? 2721 LYS A N     1 
ATOM   9958  C  CA    . LYS A 1 2721 ? 173.292 181.882 177.697 1.00 12.25  ? 2721 LYS A CA    1 
ATOM   9959  C  C     . LYS A 1 2721 ? 173.658 183.349 177.500 1.00 12.51  ? 2721 LYS A C     1 
ATOM   9960  O  O     . LYS A 1 2721 ? 173.156 184.221 178.216 1.00 10.93  ? 2721 LYS A O     1 
ATOM   9961  C  CB    . LYS A 1 2721 ? 172.138 181.519 176.755 1.00 14.69  ? 2721 LYS A CB    1 
ATOM   9962  C  CG    . LYS A 1 2721 ? 172.174 180.085 176.261 1.00 14.99  ? 2721 LYS A CG    1 
ATOM   9963  C  CD    . LYS A 1 2721 ? 171.645 179.136 177.320 1.00 17.63  ? 2721 LYS A CD    1 
ATOM   9964  C  CE    . LYS A 1 2721 ? 170.192 179.435 177.645 1.00 15.04  ? 2721 LYS A CE    1 
ATOM   9965  N  NZ    . LYS A 1 2721 ? 169.648 178.495 178.663 1.00 16.12  ? 2721 LYS A NZ    1 
ATOM   9966  N  N     . PRO A 1 2722 ? 174.535 183.656 176.544 1.00 13.71  ? 2722 PRO A N     1 
ATOM   9967  C  CA    . PRO A 1 2722 ? 174.882 185.060 176.292 1.00 10.01  ? 2722 PRO A CA    1 
ATOM   9968  C  C     . PRO A 1 2722 ? 173.709 185.804 175.669 1.00 10.27  ? 2722 PRO A C     1 
ATOM   9969  O  O     . PRO A 1 2722 ? 173.072 185.318 174.732 1.00 13.66  ? 2722 PRO A O     1 
ATOM   9970  C  CB    . PRO A 1 2722 ? 176.070 184.965 175.329 1.00 7.07   ? 2722 PRO A CB    1 
ATOM   9971  C  CG    . PRO A 1 2722 ? 175.907 183.645 174.660 1.00 7.22   ? 2722 PRO A CG    1 
ATOM   9972  C  CD    . PRO A 1 2722 ? 175.291 182.733 175.680 1.00 10.39  ? 2722 PRO A CD    1 
ATOM   9973  N  N     . LEU A 1 2723 ? 173.426 186.989 176.203 1.00 9.31   ? 2723 LEU A N     1 
ATOM   9974  C  CA    . LEU A 1 2723 ? 172.336 187.801 175.687 1.00 7.61   ? 2723 LEU A CA    1 
ATOM   9975  C  C     . LEU A 1 2723 ? 172.689 188.363 174.314 1.00 12.35  ? 2723 LEU A C     1 
ATOM   9976  O  O     . LEU A 1 2723 ? 173.859 188.574 173.984 1.00 18.70  ? 2723 LEU A O     1 
ATOM   9977  C  CB    . LEU A 1 2723 ? 172.014 188.939 176.655 1.00 8.15   ? 2723 LEU A CB    1 
ATOM   9978  C  CG    . LEU A 1 2723 ? 171.411 188.527 177.999 1.00 12.51  ? 2723 LEU A CG    1 
ATOM   9979  C  CD1   . LEU A 1 2723 ? 171.472 189.675 178.995 1.00 14.07  ? 2723 LEU A CD1   1 
ATOM   9980  C  CD2   . LEU A 1 2723 ? 169.982 188.046 177.821 1.00 11.98  ? 2723 LEU A CD2   1 
ATOM   9981  N  N     . SER A 1 2724 ? 171.655 188.598 173.509 1.00 11.33  ? 2724 SER A N     1 
ATOM   9982  C  CA    . SER A 1 2724 ? 171.858 189.123 172.166 1.00 9.47   ? 2724 SER A CA    1 
ATOM   9983  C  C     . SER A 1 2724 ? 172.486 190.509 172.221 1.00 9.19   ? 2724 SER A C     1 
ATOM   9984  O  O     . SER A 1 2724 ? 172.200 191.305 173.120 1.00 8.39   ? 2724 SER A O     1 
ATOM   9985  C  CB    . SER A 1 2724 ? 170.528 189.177 171.412 1.00 9.67   ? 2724 SER A CB    1 
ATOM   9986  O  OG    . SER A 1 2724 ? 170.700 189.694 170.104 1.00 11.02  ? 2724 SER A OG    1 
ATOM   9987  N  N     . HIS A 1 2725 ? 173.359 190.792 171.251 1.00 10.77  ? 2725 HIS A N     1 
ATOM   9988  C  CA    . HIS A 1 2725 ? 174.008 192.097 171.195 1.00 7.93   ? 2725 HIS A CA    1 
ATOM   9989  C  C     . HIS A 1 2725 ? 173.008 193.212 170.927 1.00 6.02   ? 2725 HIS A C     1 
ATOM   9990  O  O     . HIS A 1 2725 ? 173.191 194.335 171.409 1.00 6.69   ? 2725 HIS A O     1 
ATOM   9991  C  CB    . HIS A 1 2725 ? 175.100 192.099 170.127 1.00 9.08   ? 2725 HIS A CB    1 
ATOM   9992  C  CG    . HIS A 1 2725 ? 176.367 191.432 170.558 1.00 9.99   ? 2725 HIS A CG    1 
ATOM   9993  N  ND1   . HIS A 1 2725 ? 177.457 191.294 169.726 1.00 15.50  ? 2725 HIS A ND1   1 
ATOM   9994  C  CD2   . HIS A 1 2725 ? 176.719 190.864 171.735 1.00 10.73  ? 2725 HIS A CD2   1 
ATOM   9995  C  CE1   . HIS A 1 2725 ? 178.425 190.670 170.372 1.00 14.79  ? 2725 HIS A CE1   1 
ATOM   9996  N  NE2   . HIS A 1 2725 ? 178.003 190.397 171.593 1.00 12.53  ? 2725 HIS A NE2   1 
ATOM   9997  N  N     . ARG A 1 2726 ? 171.956 192.929 170.155 1.00 6.36   ? 2726 ARG A N     1 
ATOM   9998  C  CA    . ARG A 1 2726 ? 170.935 193.939 169.903 1.00 6.67   ? 2726 ARG A CA    1 
ATOM   9999  C  C     . ARG A 1 2726 ? 170.196 194.305 171.184 1.00 7.29   ? 2726 ARG A C     1 
ATOM   10000 O  O     . ARG A 1 2726 ? 169.881 195.479 171.413 1.00 9.34   ? 2726 ARG A O     1 
ATOM   10001 C  CB    . ARG A 1 2726 ? 169.962 193.441 168.835 1.00 5.63   ? 2726 ARG A CB    1 
ATOM   10002 C  CG    . ARG A 1 2726 ? 170.637 193.074 167.527 1.00 5.21   ? 2726 ARG A CG    1 
ATOM   10003 C  CD    . ARG A 1 2726 ? 169.632 192.703 166.453 1.00 8.68   ? 2726 ARG A CD    1 
ATOM   10004 N  NE    . ARG A 1 2726 ? 169.401 193.803 165.526 1.00 8.24   ? 2726 ARG A NE    1 
ATOM   10005 C  CZ    . ARG A 1 2726 ? 168.534 193.766 164.523 1.00 5.28   ? 2726 ARG A CZ    1 
ATOM   10006 N  NH1   . ARG A 1 2726 ? 167.806 192.689 164.280 1.00 6.28   ? 2726 ARG A NH1   1 
ATOM   10007 N  NH2   . ARG A 1 2726 ? 168.397 194.835 163.745 1.00 4.13   ? 2726 ARG A NH2   1 
ATOM   10008 N  N     . PHE A 1 2727 ? 169.903 193.313 172.028 1.00 6.46   ? 2727 PHE A N     1 
ATOM   10009 C  CA    . PHE A 1 2727 ? 169.293 193.603 173.322 1.00 4.78   ? 2727 PHE A CA    1 
ATOM   10010 C  C     . PHE A 1 2727 ? 170.261 194.336 174.241 1.00 6.37   ? 2727 PHE A C     1 
ATOM   10011 O  O     . PHE A 1 2727 ? 169.884 195.317 174.894 1.00 9.72   ? 2727 PHE A O     1 
ATOM   10012 C  CB    . PHE A 1 2727 ? 168.812 192.315 173.985 1.00 5.83   ? 2727 PHE A CB    1 
ATOM   10013 C  CG    . PHE A 1 2727 ? 168.283 192.517 175.375 1.00 7.47   ? 2727 PHE A CG    1 
ATOM   10014 C  CD1   . PHE A 1 2727 ? 167.139 193.265 175.593 1.00 7.36   ? 2727 PHE A CD1   1 
ATOM   10015 C  CD2   . PHE A 1 2727 ? 168.943 191.978 176.466 1.00 8.41   ? 2727 PHE A CD2   1 
ATOM   10016 C  CE1   . PHE A 1 2727 ? 166.655 193.459 176.871 1.00 6.12   ? 2727 PHE A CE1   1 
ATOM   10017 C  CE2   . PHE A 1 2727 ? 168.464 192.170 177.746 1.00 9.36   ? 2727 PHE A CE2   1 
ATOM   10018 C  CZ    . PHE A 1 2727 ? 167.319 192.911 177.948 1.00 6.41   ? 2727 PHE A CZ    1 
ATOM   10019 N  N     . LEU A 1 2728 ? 171.513 193.876 174.307 1.00 7.27   ? 2728 LEU A N     1 
ATOM   10020 C  CA    . LEU A 1 2728 ? 172.487 194.477 175.210 1.00 7.36   ? 2728 LEU A CA    1 
ATOM   10021 C  C     . LEU A 1 2728 ? 172.805 195.920 174.847 1.00 8.75   ? 2728 LEU A C     1 
ATOM   10022 O  O     . LEU A 1 2728 ? 173.290 196.667 175.702 1.00 12.72  ? 2728 LEU A O     1 
ATOM   10023 C  CB    . LEU A 1 2728 ? 173.772 193.649 175.229 1.00 7.33   ? 2728 LEU A CB    1 
ATOM   10024 C  CG    . LEU A 1 2728 ? 173.725 192.354 176.042 1.00 8.54   ? 2728 LEU A CG    1 
ATOM   10025 C  CD1   . LEU A 1 2728 ? 175.105 191.723 176.135 1.00 14.02  ? 2728 LEU A CD1   1 
ATOM   10026 C  CD2   . LEU A 1 2728 ? 173.154 192.609 177.426 1.00 12.87  ? 2728 LEU A CD2   1 
ATOM   10027 N  N     . ARG A 1 2729 ? 172.539 196.327 173.605 1.00 6.77   ? 2729 ARG A N     1 
ATOM   10028 C  CA    . ARG A 1 2729 ? 172.774 197.709 173.204 1.00 5.92   ? 2729 ARG A CA    1 
ATOM   10029 C  C     . ARG A 1 2729 ? 171.937 198.685 174.022 1.00 7.09   ? 2729 ARG A C     1 
ATOM   10030 O  O     . ARG A 1 2729 ? 172.377 199.810 174.288 1.00 10.76  ? 2729 ARG A O     1 
ATOM   10031 C  CB    . ARG A 1 2729 ? 172.484 197.856 171.708 1.00 5.60   ? 2729 ARG A CB    1 
ATOM   10032 C  CG    . ARG A 1 2729 ? 172.267 199.274 171.216 1.00 6.80   ? 2729 ARG A CG    1 
ATOM   10033 C  CD    . ARG A 1 2729 ? 171.902 199.269 169.741 1.00 7.35   ? 2729 ARG A CD    1 
ATOM   10034 N  NE    . ARG A 1 2729 ? 171.479 200.581 169.265 1.00 6.70   ? 2729 ARG A NE    1 
ATOM   10035 C  CZ    . ARG A 1 2729 ? 170.340 200.816 168.629 1.00 5.66   ? 2729 ARG A CZ    1 
ATOM   10036 N  NH1   . ARG A 1 2729 ? 169.486 199.844 168.360 1.00 7.61   ? 2729 ARG A NH1   1 
ATOM   10037 N  NH2   . ARG A 1 2729 ? 170.055 202.058 168.248 1.00 7.56   ? 2729 ARG A NH2   1 
ATOM   10038 N  N     . HIS A 1 2730 ? 170.745 198.272 174.446 1.00 7.23   ? 2730 HIS A N     1 
ATOM   10039 C  CA    . HIS A 1 2730 ? 169.840 199.146 175.179 1.00 7.02   ? 2730 HIS A CA    1 
ATOM   10040 C  C     . HIS A 1 2730 ? 169.918 198.977 176.691 1.00 7.48   ? 2730 HIS A C     1 
ATOM   10041 O  O     . HIS A 1 2730 ? 169.273 199.744 177.414 1.00 8.95   ? 2730 HIS A O     1 
ATOM   10042 C  CB    . HIS A 1 2730 ? 168.401 198.906 174.718 1.00 8.56   ? 2730 HIS A CB    1 
ATOM   10043 C  CG    . HIS A 1 2730 ? 168.220 199.001 173.236 1.00 7.49   ? 2730 HIS A CG    1 
ATOM   10044 N  ND1   . HIS A 1 2730 ? 168.047 197.893 172.435 1.00 8.49   ? 2730 HIS A ND1   1 
ATOM   10045 C  CD2   . HIS A 1 2730 ? 168.182 200.072 172.410 1.00 7.10   ? 2730 HIS A CD2   1 
ATOM   10046 C  CE1   . HIS A 1 2730 ? 167.914 198.278 171.178 1.00 10.82  ? 2730 HIS A CE1   1 
ATOM   10047 N  NE2   . HIS A 1 2730 ? 167.991 199.596 171.136 1.00 8.98   ? 2730 HIS A NE2   1 
ATOM   10048 N  N     . VAL A 1 2731 ? 170.678 198.007 177.189 1.00 10.48  ? 2731 VAL A N     1 
ATOM   10049 C  CA    . VAL A 1 2731 ? 170.739 197.765 178.628 1.00 7.86   ? 2731 VAL A CA    1 
ATOM   10050 C  C     . VAL A 1 2731 ? 172.183 197.828 179.118 1.00 7.40   ? 2731 VAL A C     1 
ATOM   10051 O  O     . VAL A 1 2731 ? 173.005 196.970 178.761 1.00 12.93  ? 2731 VAL A O     1 
ATOM   10052 C  CB    . VAL A 1 2731 ? 170.070 196.429 178.997 1.00 8.30   ? 2731 VAL A CB    1 
ATOM   10053 C  CG1   . VAL A 1 2731 ? 168.570 196.532 178.824 1.00 8.94   ? 2731 VAL A CG1   1 
ATOM   10054 C  CG2   . VAL A 1 2731 ? 170.589 195.298 178.130 1.00 9.50   ? 2731 VAL A CG2   1 
ATOM   10055 N  N     . PRO A 1 2732 ? 172.545 198.840 179.902 1.00 7.03   ? 2732 PRO A N     1 
ATOM   10056 C  CA    . PRO A 1 2732 ? 173.858 198.830 180.555 1.00 8.21   ? 2732 PRO A CA    1 
ATOM   10057 C  C     . PRO A 1 2732 ? 173.939 197.728 181.601 1.00 7.57   ? 2732 PRO A C     1 
ATOM   10058 O  O     . PRO A 1 2732 ? 172.936 197.345 182.207 1.00 6.70   ? 2732 PRO A O     1 
ATOM   10059 C  CB    . PRO A 1 2732 ? 173.950 200.222 181.190 1.00 8.36   ? 2732 PRO A CB    1 
ATOM   10060 C  CG    . PRO A 1 2732 ? 172.549 200.723 181.246 1.00 8.78   ? 2732 PRO A CG    1 
ATOM   10061 C  CD    . PRO A 1 2732 ? 171.863 200.133 180.061 1.00 9.37   ? 2732 PRO A CD    1 
ATOM   10062 N  N     . VAL A 1 2733 ? 175.150 197.221 181.812 1.00 11.44  ? 2733 VAL A N     1 
ATOM   10063 C  CA    . VAL A 1 2733 ? 175.397 196.110 182.722 1.00 8.11   ? 2733 VAL A CA    1 
ATOM   10064 C  C     . VAL A 1 2733 ? 176.427 196.543 183.755 1.00 9.23   ? 2733 VAL A C     1 
ATOM   10065 O  O     . VAL A 1 2733 ? 177.481 197.083 183.399 1.00 13.79  ? 2733 VAL A O     1 
ATOM   10066 C  CB    . VAL A 1 2733 ? 175.875 194.855 181.969 1.00 6.57   ? 2733 VAL A CB    1 
ATOM   10067 C  CG1   . VAL A 1 2733 ? 176.254 193.755 182.948 1.00 9.23   ? 2733 VAL A CG1   1 
ATOM   10068 C  CG2   . VAL A 1 2733 ? 174.803 194.376 181.006 1.00 9.33   ? 2733 VAL A CG2   1 
ATOM   10069 N  N     . VAL A 1 2734 ? 176.118 196.313 185.028 1.00 9.14   ? 2734 VAL A N     1 
ATOM   10070 C  CA    . VAL A 1 2734 ? 177.048 196.540 186.127 1.00 11.09  ? 2734 VAL A CA    1 
ATOM   10071 C  C     . VAL A 1 2734 ? 177.297 195.207 186.820 1.00 11.22  ? 2734 VAL A C     1 
ATOM   10072 O  O     . VAL A 1 2734 ? 176.349 194.485 187.150 1.00 10.42  ? 2734 VAL A O     1 
ATOM   10073 C  CB    . VAL A 1 2734 ? 176.523 197.596 187.117 1.00 8.97   ? 2734 VAL A CB    1 
ATOM   10074 C  CG1   . VAL A 1 2734 ? 175.073 197.343 187.446 1.00 10.58  ? 2734 VAL A CG1   1 
ATOM   10075 C  CG2   . VAL A 1 2734 ? 177.361 197.605 188.386 1.00 11.50  ? 2734 VAL A CG2   1 
ATOM   10076 N  N     . TYR A 1 2735 ? 178.570 194.880 187.028 1.00 13.65  ? 2735 TYR A N     1 
ATOM   10077 C  CA    . TYR A 1 2735 ? 178.967 193.604 187.613 1.00 9.40   ? 2735 TYR A CA    1 
ATOM   10078 C  C     . TYR A 1 2735 ? 179.001 193.741 189.131 1.00 12.23  ? 2735 TYR A C     1 
ATOM   10079 O  O     . TYR A 1 2735 ? 179.774 194.536 189.674 1.00 17.63  ? 2735 TYR A O     1 
ATOM   10080 C  CB    . TYR A 1 2735 ? 180.324 193.166 187.070 1.00 14.79  ? 2735 TYR A CB    1 
ATOM   10081 C  CG    . TYR A 1 2735 ? 180.786 191.817 187.572 1.00 17.84  ? 2735 TYR A CG    1 
ATOM   10082 C  CD1   . TYR A 1 2735 ? 180.004 190.684 187.398 1.00 12.69  ? 2735 TYR A CD1   1 
ATOM   10083 C  CD2   . TYR A 1 2735 ? 182.010 191.675 188.212 1.00 16.21  ? 2735 TYR A CD2   1 
ATOM   10084 C  CE1   . TYR A 1 2735 ? 180.425 189.450 187.854 1.00 15.35  ? 2735 TYR A CE1   1 
ATOM   10085 C  CE2   . TYR A 1 2735 ? 182.438 190.445 188.670 1.00 15.95  ? 2735 TYR A CE2   1 
ATOM   10086 C  CZ    . TYR A 1 2735 ? 181.642 189.336 188.488 1.00 19.29  ? 2735 TYR A CZ    1 
ATOM   10087 O  OH    . TYR A 1 2735 ? 182.067 188.109 188.943 1.00 21.31  ? 2735 TYR A OH    1 
ATOM   10088 N  N     . VAL A 1 2736 ? 178.162 192.967 189.812 1.00 12.18  ? 2736 VAL A N     1 
ATOM   10089 C  CA    . VAL A 1 2736 ? 178.125 192.929 191.268 1.00 11.03  ? 2736 VAL A CA    1 
ATOM   10090 C  C     . VAL A 1 2736 ? 178.800 191.630 191.693 1.00 13.92  ? 2736 VAL A C     1 
ATOM   10091 O  O     . VAL A 1 2736 ? 178.201 190.553 191.633 1.00 17.02  ? 2736 VAL A O     1 
ATOM   10092 C  CB    . VAL A 1 2736 ? 176.694 193.029 191.803 1.00 10.47  ? 2736 VAL A CB    1 
ATOM   10093 C  CG1   . VAL A 1 2736 ? 176.691 192.969 193.321 1.00 9.20   ? 2736 VAL A CG1   1 
ATOM   10094 C  CG2   . VAL A 1 2736 ? 176.035 194.307 191.312 1.00 12.97  ? 2736 VAL A CG2   1 
ATOM   10095 N  N     . ASP A 1 2737 ? 180.052 191.730 192.121 1.00 12.99  ? 2737 ASP A N     1 
ATOM   10096 C  CA    . ASP A 1 2737 ? 180.810 190.577 192.577 1.00 13.41  ? 2737 ASP A CA    1 
ATOM   10097 C  C     . ASP A 1 2737 ? 180.545 190.331 194.060 1.00 15.19  ? 2737 ASP A C     1 
ATOM   10098 O  O     . ASP A 1 2737 ? 179.928 191.144 194.751 1.00 16.64  ? 2737 ASP A O     1 
ATOM   10099 C  CB    . ASP A 1 2737 ? 182.303 190.790 192.318 1.00 19.76  ? 2737 ASP A CB    1 
ATOM   10100 C  CG    . ASP A 1 2737 ? 183.081 189.490 192.277 1.00 26.63  ? 2737 ASP A CG    1 
ATOM   10101 O  OD1   . ASP A 1 2737 ? 182.463 188.417 192.431 1.00 24.35  ? 2737 ASP A OD1   1 
ATOM   10102 O  OD2   . ASP A 1 2737 ? 184.314 189.544 192.087 1.00 29.99  ? 2737 ASP A OD2   1 
ATOM   10103 N  N     . TYR A 1 2738 ? 181.011 189.185 194.547 1.00 18.29  ? 2738 TYR A N     1 
ATOM   10104 C  CA    . TYR A 1 2738 ? 180.872 188.880 195.962 1.00 13.12  ? 2738 TYR A CA    1 
ATOM   10105 C  C     . TYR A 1 2738 ? 181.649 189.900 196.791 1.00 16.64  ? 2738 TYR A C     1 
ATOM   10106 O  O     . TYR A 1 2738 ? 182.728 190.342 196.380 1.00 18.46  ? 2738 TYR A O     1 
ATOM   10107 C  CB    . TYR A 1 2738 ? 181.382 187.472 196.276 1.00 10.42  ? 2738 TYR A CB    1 
ATOM   10108 C  CG    . TYR A 1 2738 ? 180.438 186.358 195.890 1.00 10.13  ? 2738 TYR A CG    1 
ATOM   10109 C  CD1   . TYR A 1 2738 ? 179.085 186.435 196.185 1.00 10.40  ? 2738 TYR A CD1   1 
ATOM   10110 C  CD2   . TYR A 1 2738 ? 180.905 185.215 195.259 1.00 9.38   ? 2738 TYR A CD2   1 
ATOM   10111 C  CE1   . TYR A 1 2738 ? 178.221 185.417 195.842 1.00 7.39   ? 2738 TYR A CE1   1 
ATOM   10112 C  CE2   . TYR A 1 2738 ? 180.049 184.189 194.917 1.00 9.06   ? 2738 TYR A CE2   1 
ATOM   10113 C  CZ    . TYR A 1 2738 ? 178.708 184.296 195.210 1.00 7.32   ? 2738 TYR A CZ    1 
ATOM   10114 O  OH    . TYR A 1 2738 ? 177.851 183.277 194.867 1.00 7.83   ? 2738 TYR A OH    1 
ATOM   10115 N  N     . PRO A 1 2739 ? 181.125 190.309 197.945 1.00 18.19  ? 2739 PRO A N     1 
ATOM   10116 C  CA    . PRO A 1 2739 ? 181.908 191.167 198.839 1.00 19.31  ? 2739 PRO A CA    1 
ATOM   10117 C  C     . PRO A 1 2739 ? 183.183 190.467 199.281 1.00 21.85  ? 2739 PRO A C     1 
ATOM   10118 O  O     . PRO A 1 2739 ? 183.205 189.254 199.499 1.00 24.86  ? 2739 PRO A O     1 
ATOM   10119 C  CB    . PRO A 1 2739 ? 180.959 191.412 200.018 1.00 14.85  ? 2739 PRO A CB    1 
ATOM   10120 C  CG    . PRO A 1 2739 ? 179.594 191.177 199.464 1.00 14.77  ? 2739 PRO A CG    1 
ATOM   10121 C  CD    . PRO A 1 2739 ? 179.750 190.104 198.430 1.00 15.88  ? 2739 PRO A CD    1 
ATOM   10122 N  N     . GLY A 1 2740 ? 184.254 191.244 199.407 1.00 25.92  ? 2740 GLY A N     1 
ATOM   10123 C  CA    . GLY A 1 2740 ? 185.532 190.709 199.808 1.00 26.04  ? 2740 GLY A CA    1 
ATOM   10124 C  C     . GLY A 1 2740 ? 185.552 190.330 201.273 1.00 23.19  ? 2740 GLY A C     1 
ATOM   10125 O  O     . GLY A 1 2740 ? 184.627 190.642 202.030 1.00 22.56  ? 2740 GLY A O     1 
ATOM   10126 N  N     . PRO A 1 2741 ? 186.606 189.628 201.699 1.00 25.23  ? 2741 PRO A N     1 
ATOM   10127 C  CA    . PRO A 1 2741 ? 186.714 189.275 203.125 1.00 22.89  ? 2741 PRO A CA    1 
ATOM   10128 C  C     . PRO A 1 2741 ? 186.687 190.482 204.045 1.00 22.51  ? 2741 PRO A C     1 
ATOM   10129 O  O     . PRO A 1 2741 ? 186.131 190.403 205.148 1.00 21.74  ? 2741 PRO A O     1 
ATOM   10130 C  CB    . PRO A 1 2741 ? 188.056 188.533 203.194 1.00 19.37  ? 2741 PRO A CB    1 
ATOM   10131 C  CG    . PRO A 1 2741 ? 188.238 187.969 201.828 1.00 21.91  ? 2741 PRO A CG    1 
ATOM   10132 C  CD    . PRO A 1 2741 ? 187.649 188.981 200.885 1.00 30.22  ? 2741 PRO A CD    1 
ATOM   10133 N  N     . ALA A 1 2742 ? 187.279 191.601 203.623 1.00 22.65  ? 2742 ALA A N     1 
ATOM   10134 C  CA    . ALA A 1 2742 ? 187.182 192.827 204.408 1.00 21.73  ? 2742 ALA A CA    1 
ATOM   10135 C  C     . ALA A 1 2742 ? 185.748 193.339 204.452 1.00 22.54  ? 2742 ALA A C     1 
ATOM   10136 O  O     . ALA A 1 2742 ? 185.276 193.792 205.502 1.00 23.51  ? 2742 ALA A O     1 
ATOM   10137 C  CB    . ALA A 1 2742 ? 188.118 193.891 203.837 1.00 20.41  ? 2742 ALA A CB    1 
ATOM   10138 N  N     . SER A 1 2743 ? 185.042 193.282 203.319 1.00 23.01  ? 2743 SER A N     1 
ATOM   10139 C  CA    . SER A 1 2743 ? 183.646 193.706 203.294 1.00 21.33  ? 2743 SER A CA    1 
ATOM   10140 C  C     . SER A 1 2743 ? 182.770 192.773 204.120 1.00 22.91  ? 2743 SER A C     1 
ATOM   10141 O  O     . SER A 1 2743 ? 181.865 193.231 204.828 1.00 25.55  ? 2743 SER A O     1 
ATOM   10142 C  CB    . SER A 1 2743 ? 183.145 193.778 201.852 1.00 23.21  ? 2743 SER A CB    1 
ATOM   10143 O  OG    . SER A 1 2743 ? 183.969 194.622 201.067 1.00 31.63  ? 2743 SER A OG    1 
ATOM   10144 N  N     . LEU A 1 2744 ? 183.024 191.464 204.045 1.00 21.99  ? 2744 LEU A N     1 
ATOM   10145 C  CA    . LEU A 1 2744 ? 182.239 190.512 204.825 1.00 20.57  ? 2744 LEU A CA    1 
ATOM   10146 C  C     . LEU A 1 2744 ? 182.395 190.762 206.318 1.00 22.14  ? 2744 LEU A C     1 
ATOM   10147 O  O     . LEU A 1 2744 ? 181.415 190.702 207.071 1.00 23.95  ? 2744 LEU A O     1 
ATOM   10148 C  CB    . LEU A 1 2744 ? 182.650 189.082 204.477 1.00 22.50  ? 2744 LEU A CB    1 
ATOM   10149 C  CG    . LEU A 1 2744 ? 182.285 188.580 203.082 1.00 18.29  ? 2744 LEU A CG    1 
ATOM   10150 C  CD1   . LEU A 1 2744 ? 182.538 187.088 202.978 1.00 17.03  ? 2744 LEU A CD1   1 
ATOM   10151 C  CD2   . LEU A 1 2744 ? 180.835 188.900 202.767 1.00 22.77  ? 2744 LEU A CD2   1 
ATOM   10152 N  N     . THR A 1 2745 ? 183.621 191.076 206.740 1.00 21.81  ? 2745 THR A N     1 
ATOM   10153 C  CA    . THR A 1 2745 ? 183.876 191.355 208.168 1.00 21.25  ? 2745 THR A CA    1 
ATOM   10154 C  C     . THR A 1 2745 ? 183.042 192.544 208.596 1.00 21.68  ? 2745 THR A C     1 
ATOM   10155 O  O     . THR A 1 2745 ? 182.463 192.489 209.700 1.00 28.12  ? 2745 THR A O     1 
ATOM   10156 C  CB    . THR A 1 2745 ? 185.368 191.601 208.381 1.00 20.69  ? 2745 THR A CB    1 
ATOM   10157 O  OG1   . THR A 1 2745 ? 186.012 190.418 207.919 1.00 19.05  ? 2745 THR A OG1   1 
ATOM   10158 C  CG2   . THR A 1 2745 ? 185.714 191.848 209.838 1.00 20.62  ? 2745 THR A CG2   1 
ATOM   10159 N  N     . GLN A 1 2746 ? 182.978 193.585 207.762 1.00 23.54  ? 2746 GLN A N     1 
ATOM   10160 C  CA    . GLN A 1 2746 ? 182.232 194.821 208.122 1.00 23.16  ? 2746 GLN A CA    1 
ATOM   10161 C  C     . GLN A 1 2746 ? 180.719 194.558 208.094 1.00 21.12  ? 2746 GLN A C     1 
ATOM   10162 O  O     . GLN A 1 2746 ? 180.024 195.025 209.022 1.00 25.29  ? 2746 GLN A O     1 
ATOM   10163 C  CB    . GLN A 1 2746 ? 182.595 195.953 207.161 1.00 27.41  ? 2746 GLN A CB    1 
ATOM   10164 C  CG    . GLN A 1 2746 ? 184.096 196.169 207.007 1.00 32.69  ? 2746 GLN A CG    1 
ATOM   10165 C  CD    . GLN A 1 2746 ? 184.833 196.175 208.327 1.00 42.71  ? 2746 GLN A CD    1 
ATOM   10166 O  OE1   . GLN A 1 2746 ? 185.710 195.342 208.580 1.00 44.20  ? 2746 GLN A OE1   1 
ATOM   10167 N  NE2   . GLN A 1 2746 ? 184.477 197.117 209.189 1.00 42.11  ? 2746 GLN A NE2   1 
ATOM   10168 N  N     . ILE A 1 2747 ? 180.231 193.846 207.075 1.00 19.43  ? 2747 ILE A N     1 
ATOM   10169 C  CA    . ILE A 1 2747 ? 178.761 193.614 206.929 1.00 17.49  ? 2747 ILE A CA    1 
ATOM   10170 C  C     . ILE A 1 2747 ? 178.269 192.708 208.065 1.00 21.09  ? 2747 ILE A C     1 
ATOM   10171 O  O     . ILE A 1 2747 ? 177.178 192.987 208.608 1.00 20.29  ? 2747 ILE A O     1 
ATOM   10172 C  CB    . ILE A 1 2747 ? 178.446 192.995 205.555 1.00 14.84  ? 2747 ILE A CB    1 
ATOM   10173 C  CG1   . ILE A 1 2747 ? 178.878 193.909 204.411 1.00 17.10  ? 2747 ILE A CG1   1 
ATOM   10174 C  CG2   . ILE A 1 2747 ? 176.968 192.618 205.452 1.00 11.37  ? 2747 ILE A CG2   1 
ATOM   10175 C  CD1   . ILE A 1 2747 ? 178.856 193.241 203.048 1.00 16.96  ? 2747 ILE A CD1   1 
ATOM   10176 N  N     . TYR A 1 2748 ? 179.041 191.677 208.415 1.00 22.47  ? 2748 TYR A N     1 
ATOM   10177 C  CA    . TYR A 1 2748 ? 178.576 190.717 209.408 1.00 17.67  ? 2748 TYR A CA    1 
ATOM   10178 C  C     . TYR A 1 2748 ? 179.190 190.939 210.781 1.00 16.69  ? 2748 TYR A C     1 
ATOM   10179 O  O     . TYR A 1 2748 ? 178.658 190.425 211.770 1.00 22.01  ? 2748 TYR A O     1 
ATOM   10180 C  CB    . TYR A 1 2748 ? 178.849 189.297 208.914 1.00 17.41  ? 2748 TYR A CB    1 
ATOM   10181 C  CG    . TYR A 1 2748 ? 178.071 188.976 207.662 1.00 13.08  ? 2748 TYR A CG    1 
ATOM   10182 C  CD1   . TYR A 1 2748 ? 176.690 188.865 207.694 1.00 15.48  ? 2748 TYR A CD1   1 
ATOM   10183 C  CD2   . TYR A 1 2748 ? 178.710 188.829 206.441 1.00 14.51  ? 2748 TYR A CD2   1 
ATOM   10184 C  CE1   . TYR A 1 2748 ? 175.969 188.587 206.553 1.00 17.56  ? 2748 TYR A CE1   1 
ATOM   10185 C  CE2   . TYR A 1 2748 ? 177.996 188.552 205.293 1.00 19.13  ? 2748 TYR A CE2   1 
ATOM   10186 C  CZ    . TYR A 1 2748 ? 176.627 188.433 205.355 1.00 15.47  ? 2748 TYR A CZ    1 
ATOM   10187 O  OH    . TYR A 1 2748 ? 175.910 188.157 204.214 1.00 13.35  ? 2748 TYR A OH    1 
ATOM   10188 N  N     . GLY A 1 2749 ? 180.245 191.749 210.857 1.00 17.46  ? 2749 GLY A N     1 
ATOM   10189 C  CA    . GLY A 1 2749 ? 180.765 192.106 212.189 1.00 24.37  ? 2749 GLY A CA    1 
ATOM   10190 C  C     . GLY A 1 2749 ? 179.752 193.015 212.854 1.00 27.32  ? 2749 GLY A C     1 
ATOM   10191 O  O     . GLY A 1 2749 ? 179.537 192.873 214.075 1.00 28.76  ? 2749 GLY A O     1 
ATOM   10192 N  N     . THR A 1 2750 ? 179.122 193.894 212.067 1.00 22.85  ? 2750 THR A N     1 
ATOM   10193 C  CA    . THR A 1 2750 ? 178.094 194.814 212.598 1.00 23.40  ? 2750 THR A CA    1 
ATOM   10194 C  C     . THR A 1 2750 ? 176.918 194.005 213.094 1.00 27.24  ? 2750 THR A C     1 
ATOM   10195 O  O     . THR A 1 2750 ? 176.437 194.284 214.216 1.00 31.43  ? 2750 THR A O     1 
ATOM   10196 C  CB    . THR A 1 2750 ? 177.672 195.780 211.492 1.00 25.93  ? 2750 THR A CB    1 
ATOM   10197 O  OG1   . THR A 1 2750 ? 178.863 196.455 211.099 1.00 25.34  ? 2750 THR A OG1   1 
ATOM   10198 C  CG2   . THR A 1 2750 ? 176.633 196.782 211.962 1.00 32.63  ? 2750 THR A CG2   1 
ATOM   10199 N  N     . PHE A 1 2751 ? 176.468 193.034 212.296 1.00 26.53  ? 2751 PHE A N     1 
ATOM   10200 C  CA    . PHE A 1 2751 ? 175.291 192.208 212.674 1.00 21.12  ? 2751 PHE A CA    1 
ATOM   10201 C  C     . PHE A 1 2751 ? 175.599 191.472 213.976 1.00 27.25  ? 2751 PHE A C     1 
ATOM   10202 O  O     . PHE A 1 2751 ? 174.739 191.453 214.883 1.00 33.65  ? 2751 PHE A O     1 
ATOM   10203 C  CB    . PHE A 1 2751 ? 174.944 191.259 211.523 1.00 21.21  ? 2751 PHE A CB    1 
ATOM   10204 C  CG    . PHE A 1 2751 ? 174.125 191.898 210.410 1.00 26.28  ? 2751 PHE A CG    1 
ATOM   10205 C  CD1   . PHE A 1 2751 ? 173.221 192.918 210.686 1.00 29.08  ? 2751 PHE A CD1   1 
ATOM   10206 C  CD2   . PHE A 1 2751 ? 174.260 191.478 209.092 1.00 21.52  ? 2751 PHE A CD2   1 
ATOM   10207 C  CE1   . PHE A 1 2751 ? 172.475 193.498 209.672 1.00 27.92  ? 2751 PHE A CE1   1 
ATOM   10208 C  CE2   . PHE A 1 2751 ? 173.513 192.063 208.082 1.00 21.38  ? 2751 PHE A CE2   1 
ATOM   10209 C  CZ    . PHE A 1 2751 ? 172.623 193.070 208.374 1.00 24.54  ? 2751 PHE A CZ    1 
ATOM   10210 N  N     . ASN A 1 2752 ? 176.799 190.896 214.074 1.00 24.36  ? 2752 ASN A N     1 
ATOM   10211 C  CA    . ASN A 1 2752 ? 177.192 190.146 215.299 1.00 23.53  ? 2752 ASN A CA    1 
ATOM   10212 C  C     . ASN A 1 2752 ? 177.228 191.106 216.490 1.00 28.76  ? 2752 ASN A C     1 
ATOM   10213 O  O     . ASN A 1 2752 ? 176.708 190.736 217.564 1.00 35.91  ? 2752 ASN A O     1 
ATOM   10214 C  CB    . ASN A 1 2752 ? 178.532 189.443 215.126 1.00 25.88  ? 2752 ASN A CB    1 
ATOM   10215 C  CG    . ASN A 1 2752 ? 178.469 188.314 214.126 1.00 24.77  ? 2752 ASN A CG    1 
ATOM   10216 O  OD1   . ASN A 1 2752 ? 179.478 187.645 213.883 1.00 25.55  ? 2752 ASN A OD1   1 
ATOM   10217 N  ND2   . ASN A 1 2752 ? 177.301 188.083 213.544 1.00 22.84  ? 2752 ASN A ND2   1 
ATOM   10218 N  N     . ARG A 1 2753 ? 177.810 192.294 216.302 1.00 27.93  ? 2753 ARG A N     1 
ATOM   10219 C  CA    . ARG A 1 2753 ? 177.944 193.265 217.419 1.00 30.43  ? 2753 ARG A CA    1 
ATOM   10220 C  C     . ARG A 1 2753 ? 176.547 193.606 217.962 1.00 32.31  ? 2753 ARG A C     1 
ATOM   10221 O  O     . ARG A 1 2753 ? 176.406 193.721 219.198 1.00 39.88  ? 2753 ARG A O     1 
ATOM   10222 C  CB    . ARG A 1 2753 ? 178.710 194.508 216.951 1.00 31.20  ? 2753 ARG A CB    1 
ATOM   10223 C  CG    . ARG A 1 2753 ? 180.199 194.250 216.769 1.00 33.13  ? 2753 ARG A CG    1 
ATOM   10224 C  CD    . ARG A 1 2753 ? 180.955 195.459 216.242 1.00 36.09  ? 2753 ARG A CD    1 
ATOM   10225 N  NE    . ARG A 1 2753 ? 180.704 195.717 214.820 1.00 36.96  ? 2753 ARG A NE    1 
ATOM   10226 C  CZ    . ARG A 1 2753 ? 180.186 196.839 214.339 1.00 34.74  ? 2753 ARG A CZ    1 
ATOM   10227 N  NH1   . ARG A 1 2753 ? 179.429 197.601 215.107 1.00 31.77  ? 2753 ARG A NH1   1 
ATOM   10228 N  NH2   . ARG A 1 2753 ? 180.423 197.193 213.089 1.00 36.41  ? 2753 ARG A NH2   1 
ATOM   10229 N  N     . ALA A 1 2754 ? 175.560 193.753 217.074 1.00 32.43  ? 2754 ALA A N     1 
ATOM   10230 C  CA    . ALA A 1 2754 ? 174.173 194.036 217.514 1.00 35.37  ? 2754 ALA A CA    1 
ATOM   10231 C  C     . ALA A 1 2754 ? 173.552 192.761 218.083 1.00 40.07  ? 2754 ALA A C     1 
ATOM   10232 O  O     . ALA A 1 2754 ? 172.953 192.817 219.178 1.00 44.17  ? 2754 ALA A O     1 
ATOM   10233 C  CB    . ALA A 1 2754 ? 173.365 194.567 216.353 1.00 34.95  ? 2754 ALA A CB    1 
ATOM   10234 N  N     . MET A 1 2755 ? 173.694 191.645 217.364 1.00 36.79  ? 2755 MET A N     1 
ATOM   10235 C  CA    . MET A 1 2755 ? 173.115 190.381 217.806 1.00 36.19  ? 2755 MET A CA    1 
ATOM   10236 C  C     . MET A 1 2755 ? 173.586 190.005 219.206 1.00 40.76  ? 2755 MET A C     1 
ATOM   10237 O  O     . MET A 1 2755 ? 172.795 189.516 220.021 1.00 47.16  ? 2755 MET A O     1 
ATOM   10238 C  CB    . MET A 1 2755 ? 173.460 189.279 216.805 1.00 36.97  ? 2755 MET A CB    1 
ATOM   10239 C  CG    . MET A 1 2755 ? 173.120 187.877 217.265 1.00 31.83  ? 2755 MET A CG    1 
ATOM   10240 S  SD    . MET A 1 2755 ? 173.947 186.644 216.246 1.00 47.22  ? 2755 MET A SD    1 
ATOM   10241 C  CE    . MET A 1 2755 ? 175.444 186.386 217.192 1.00 36.35  ? 2755 MET A CE    1 
ATOM   10242 N  N     . LEU A 1 2756 ? 174.862 190.229 219.507 1.00 38.82  ? 2756 LEU A N     1 
ATOM   10243 C  CA    . LEU A 1 2756 ? 175.421 189.841 220.795 1.00 35.40  ? 2756 LEU A CA    1 
ATOM   10244 C  C     . LEU A 1 2756 ? 175.130 190.844 221.903 1.00 39.78  ? 2756 LEU A C     1 
ATOM   10245 O  O     . LEU A 1 2756 ? 175.597 190.647 223.030 1.00 49.56  ? 2756 LEU A O     1 
ATOM   10246 C  CB    . LEU A 1 2756 ? 176.932 189.626 220.666 1.00 40.11  ? 2756 LEU A CB    1 
ATOM   10247 C  CG    . LEU A 1 2756 ? 177.342 188.298 220.023 1.00 41.49  ? 2756 LEU A CG    1 
ATOM   10248 C  CD1   . LEU A 1 2756 ? 178.818 188.021 220.236 1.00 42.08  ? 2756 LEU A CD1   1 
ATOM   10249 C  CD2   . LEU A 1 2756 ? 176.503 187.155 220.575 1.00 38.49  ? 2756 LEU A CD2   1 
ATOM   10250 N  N     . ARG A 1 2757 ? 174.380 191.911 221.618 1.00 38.78  ? 2757 ARG A N     1 
ATOM   10251 C  CA    . ARG A 1 2757 ? 173.956 192.833 222.665 1.00 43.11  ? 2757 ARG A CA    1 
ATOM   10252 C  C     . ARG A 1 2757 ? 172.882 192.243 223.566 1.00 45.90  ? 2757 ARG A C     1 
ATOM   10253 O  O     . ARG A 1 2757 ? 172.638 192.788 224.647 1.00 48.17  ? 2757 ARG A O     1 
ATOM   10254 C  CB    . ARG A 1 2757 ? 173.446 194.133 222.046 1.00 45.45  ? 2757 ARG A CB    1 
ATOM   10255 C  CG    . ARG A 1 2757 ? 174.530 194.970 221.407 1.00 39.65  ? 2757 ARG A CG    1 
ATOM   10256 C  CD    . ARG A 1 2757 ? 174.195 196.446 221.432 1.00 34.36  ? 2757 ARG A CD    1 
ATOM   10257 N  NE    . ARG A 1 2757 ? 174.237 197.003 220.086 1.00 45.01  ? 2757 ARG A NE    1 
ATOM   10258 C  CZ    . ARG A 1 2757 ? 175.350 197.337 219.448 1.00 45.18  ? 2757 ARG A CZ    1 
ATOM   10259 N  NH1   . ARG A 1 2757 ? 176.538 197.221 220.020 1.00 42.07  ? 2757 ARG A NH1   1 
ATOM   10260 N  NH2   . ARG A 1 2757 ? 175.270 197.791 218.201 1.00 38.35  ? 2757 ARG A NH2   1 
ATOM   10261 N  N     . LEU A 1 2758 ? 172.232 191.155 223.144 1.00 47.21  ? 2758 LEU A N     1 
ATOM   10262 C  CA    . LEU A 1 2758 ? 171.240 190.509 223.996 1.00 51.29  ? 2758 LEU A CA    1 
ATOM   10263 C  C     . LEU A 1 2758 ? 171.879 189.977 225.272 1.00 53.45  ? 2758 LEU A C     1 
ATOM   10264 O  O     . LEU A 1 2758 ? 171.307 190.101 226.361 1.00 58.67  ? 2758 LEU A O     1 
ATOM   10265 C  CB    . LEU A 1 2758 ? 170.547 189.382 223.230 1.00 46.86  ? 2758 LEU A CB    1 
ATOM   10266 C  CG    . LEU A 1 2758 ? 169.828 189.779 221.939 1.00 48.07  ? 2758 LEU A CG    1 
ATOM   10267 C  CD1   . LEU A 1 2758 ? 169.598 188.561 221.058 1.00 44.31  ? 2758 LEU A CD1   1 
ATOM   10268 C  CD2   . LEU A 1 2758 ? 168.513 190.479 222.246 1.00 47.46  ? 2758 LEU A CD2   1 
ATOM   10269 N  N     . ILE A 1 2759 ? 173.062 189.384 225.155 1.00 47.12  ? 2759 ILE A N     1 
ATOM   10270 C  CA    . ILE A 1 2759 ? 173.804 188.878 226.306 1.00 50.08  ? 2759 ILE A CA    1 
ATOM   10271 C  C     . ILE A 1 2759 ? 175.084 189.694 226.450 1.00 54.48  ? 2759 ILE A C     1 
ATOM   10272 O  O     . ILE A 1 2759 ? 176.037 189.492 225.682 1.00 55.98  ? 2759 ILE A O     1 
ATOM   10273 C  CB    . ILE A 1 2759 ? 174.103 187.379 226.161 1.00 51.94  ? 2759 ILE A CB    1 
ATOM   10274 C  CG1   . ILE A 1 2759 ? 172.874 186.649 225.614 1.00 46.45  ? 2759 ILE A CG1   1 
ATOM   10275 C  CG2   . ILE A 1 2759 ? 174.529 186.789 227.495 1.00 59.23  ? 2759 ILE A CG2   1 
ATOM   10276 C  CD1   . ILE A 1 2759 ? 173.198 185.513 224.675 1.00 44.09  ? 2759 ILE A CD1   1 
ATOM   10277 N  N     . PRO A 1 2760 ? 175.148 190.626 227.407 1.00 62.11  ? 2760 PRO A N     1 
ATOM   10278 C  CA    . PRO A 1 2760 ? 176.345 191.478 227.520 1.00 59.54  ? 2760 PRO A CA    1 
ATOM   10279 C  C     . PRO A 1 2760 ? 177.627 190.708 227.788 1.00 55.74  ? 2760 PRO A C     1 
ATOM   10280 O  O     . PRO A 1 2760 ? 178.713 191.187 227.436 1.00 54.89  ? 2760 PRO A O     1 
ATOM   10281 C  CB    . PRO A 1 2760 ? 175.992 192.413 228.685 1.00 58.28  ? 2760 PRO A CB    1 
ATOM   10282 C  CG    . PRO A 1 2760 ? 174.498 192.438 228.707 1.00 54.41  ? 2760 PRO A CG    1 
ATOM   10283 C  CD    . PRO A 1 2760 ? 174.074 191.052 228.319 1.00 58.66  ? 2760 PRO A CD    1 
ATOM   10284 N  N     . SER A 1 2761 ? 177.537 189.529 228.407 1.00 54.44  ? 2761 SER A N     1 
ATOM   10285 C  CA    . SER A 1 2761 ? 178.737 188.761 228.719 1.00 53.85  ? 2761 SER A CA    1 
ATOM   10286 C  C     . SER A 1 2761 ? 179.469 188.285 227.470 1.00 52.88  ? 2761 SER A C     1 
ATOM   10287 O  O     . SER A 1 2761 ? 180.681 188.054 227.528 1.00 50.91  ? 2761 SER A O     1 
ATOM   10288 C  CB    . SER A 1 2761 ? 178.377 187.561 229.598 1.00 59.54  ? 2761 SER A CB    1 
ATOM   10289 O  OG    . SER A 1 2761 ? 177.582 186.630 228.885 1.00 63.58  ? 2761 SER A OG    1 
ATOM   10290 N  N     . LEU A 1 2762 ? 178.767 188.131 226.350 1.00 52.38  ? 2762 LEU A N     1 
ATOM   10291 C  CA    . LEU A 1 2762 ? 179.369 187.652 225.113 1.00 47.70  ? 2762 LEU A CA    1 
ATOM   10292 C  C     . LEU A 1 2762 ? 179.770 188.771 224.161 1.00 51.48  ? 2762 LEU A C     1 
ATOM   10293 O  O     . LEU A 1 2762 ? 180.227 188.479 223.052 1.00 51.31  ? 2762 LEU A O     1 
ATOM   10294 C  CB    . LEU A 1 2762 ? 178.409 186.698 224.394 1.00 46.47  ? 2762 LEU A CB    1 
ATOM   10295 C  CG    . LEU A 1 2762 ? 178.123 185.367 225.087 1.00 47.20  ? 2762 LEU A CG    1 
ATOM   10296 C  CD1   . LEU A 1 2762 ? 176.758 184.838 224.688 1.00 43.53  ? 2762 LEU A CD1   1 
ATOM   10297 C  CD2   . LEU A 1 2762 ? 179.205 184.360 224.750 1.00 45.51  ? 2762 LEU A CD2   1 
ATOM   10298 N  N     . ARG A 1 2763 ? 179.615 190.036 224.560 1.00 52.24  ? 2763 ARG A N     1 
ATOM   10299 C  CA    . ARG A 1 2763 ? 179.878 191.138 223.639 1.00 49.40  ? 2763 ARG A CA    1 
ATOM   10300 C  C     . ARG A 1 2763 ? 181.341 191.179 223.214 1.00 47.48  ? 2763 ARG A C     1 
ATOM   10301 O  O     . ARG A 1 2763 ? 181.653 191.551 222.077 1.00 53.84  ? 2763 ARG A O     1 
ATOM   10302 C  CB    . ARG A 1 2763 ? 179.465 192.467 224.270 1.00 48.05  ? 2763 ARG A CB    1 
ATOM   10303 C  CG    . ARG A 1 2763 ? 177.968 192.601 224.485 1.00 53.59  ? 2763 ARG A CG    1 
ATOM   10304 C  CD    . ARG A 1 2763 ? 177.515 194.046 224.370 1.00 61.28  ? 2763 ARG A CD    1 
ATOM   10305 N  NE    . ARG A 1 2763 ? 178.333 194.946 225.174 1.00 74.13  ? 2763 ARG A NE    1 
ATOM   10306 C  CZ    . ARG A 1 2763 ? 178.264 196.269 225.118 1.00 75.02  ? 2763 ARG A CZ    1 
ATOM   10307 N  NH1   . ARG A 1 2763 ? 177.423 196.884 224.302 1.00 61.79  ? 2763 ARG A NH1   1 
ATOM   10308 N  NH2   . ARG A 1 2763 ? 179.060 196.994 225.900 1.00 73.12  ? 2763 ARG A NH2   1 
ATOM   10309 N  N     . THR A 1 2764 ? 182.254 190.801 224.111 1.00 41.91  ? 2764 THR A N     1 
ATOM   10310 C  CA    . THR A 1 2764 ? 183.671 190.804 223.765 1.00 41.43  ? 2764 THR A CA    1 
ATOM   10311 C  C     . THR A 1 2764 ? 184.016 189.746 222.725 1.00 42.35  ? 2764 THR A C     1 
ATOM   10312 O  O     . THR A 1 2764 ? 185.107 189.795 222.147 1.00 47.28  ? 2764 THR A O     1 
ATOM   10313 C  CB    . THR A 1 2764 ? 184.524 190.595 225.018 1.00 47.12  ? 2764 THR A CB    1 
ATOM   10314 O  OG1   . THR A 1 2764 ? 185.912 190.691 224.674 1.00 47.37  ? 2764 THR A OG1   1 
ATOM   10315 C  CG2   . THR A 1 2764 ? 184.252 189.229 225.629 1.00 42.09  ? 2764 THR A CG2   1 
ATOM   10316 N  N     . TYR A 1 2765 ? 183.120 188.794 222.475 1.00 40.99  ? 2765 TYR A N     1 
ATOM   10317 C  CA    . TYR A 1 2765 ? 183.346 187.746 221.489 1.00 39.10  ? 2765 TYR A CA    1 
ATOM   10318 C  C     . TYR A 1 2765 ? 182.761 188.081 220.123 1.00 40.76  ? 2765 TYR A C     1 
ATOM   10319 O  O     . TYR A 1 2765 ? 182.754 187.217 219.240 1.00 39.46  ? 2765 TYR A O     1 
ATOM   10320 C  CB    . TYR A 1 2765 ? 182.770 186.418 221.987 1.00 40.77  ? 2765 TYR A CB    1 
ATOM   10321 C  CG    . TYR A 1 2765 ? 183.414 185.910 223.256 1.00 41.77  ? 2765 TYR A CG    1 
ATOM   10322 C  CD1   . TYR A 1 2765 ? 184.625 185.233 223.218 1.00 40.22  ? 2765 TYR A CD1   1 
ATOM   10323 C  CD2   . TYR A 1 2765 ? 182.808 186.100 224.490 1.00 38.81  ? 2765 TYR A CD2   1 
ATOM   10324 C  CE1   . TYR A 1 2765 ? 185.219 184.766 224.373 1.00 43.00  ? 2765 TYR A CE1   1 
ATOM   10325 C  CE2   . TYR A 1 2765 ? 183.394 185.635 225.651 1.00 42.01  ? 2765 TYR A CE2   1 
ATOM   10326 C  CZ    . TYR A 1 2765 ? 184.599 184.969 225.586 1.00 44.23  ? 2765 TYR A CZ    1 
ATOM   10327 O  OH    . TYR A 1 2765 ? 185.186 184.504 226.740 1.00 39.91  ? 2765 TYR A OH    1 
ATOM   10328 N  N     . ALA A 1 2766 ? 182.264 189.305 219.932 1.00 40.75  ? 2766 ALA A N     1 
ATOM   10329 C  CA    . ALA A 1 2766 ? 181.688 189.674 218.643 1.00 32.18  ? 2766 ALA A CA    1 
ATOM   10330 C  C     . ALA A 1 2766 ? 182.730 189.631 217.532 1.00 31.60  ? 2766 ALA A C     1 
ATOM   10331 O  O     . ALA A 1 2766 ? 182.462 189.107 216.445 1.00 33.78  ? 2766 ALA A O     1 
ATOM   10332 C  CB    . ALA A 1 2766 ? 181.053 191.061 218.730 1.00 29.00  ? 2766 ALA A CB    1 
ATOM   10333 N  N     . GLU A 1 2767 ? 183.919 190.179 217.782 1.00 31.80  ? 2767 GLU A N     1 
ATOM   10334 C  CA    . GLU A 1 2767 ? 184.959 190.181 216.755 1.00 33.25  ? 2767 GLU A CA    1 
ATOM   10335 C  C     . GLU A 1 2767 ? 185.448 188.781 216.398 1.00 32.50  ? 2767 GLU A C     1 
ATOM   10336 O  O     . GLU A 1 2767 ? 185.479 188.454 215.199 1.00 29.23  ? 2767 GLU A O     1 
ATOM   10337 C  CB    . GLU A 1 2767 ? 186.115 191.087 217.193 1.00 36.97  ? 2767 GLU A CB    1 
ATOM   10338 C  CG    . GLU A 1 2767 ? 185.721 192.539 217.419 1.00 42.77  ? 2767 GLU A CG    1 
ATOM   10339 C  CD    . GLU A 1 2767 ? 185.310 193.240 216.138 1.00 54.62  ? 2767 GLU A CD    1 
ATOM   10340 O  OE1   . GLU A 1 2767 ? 186.196 193.787 215.448 1.00 62.04  ? 2767 GLU A OE1   1 
ATOM   10341 O  OE2   . GLU A 1 2767 ? 184.100 193.249 215.825 1.00 46.06  ? 2767 GLU A OE2   1 
ATOM   10342 N  N     . PRO A 1 2768 ? 185.844 187.917 217.346 1.00 37.17  ? 2768 PRO A N     1 
ATOM   10343 C  CA    . PRO A 1 2768 ? 186.305 186.579 216.935 1.00 32.65  ? 2768 PRO A CA    1 
ATOM   10344 C  C     . PRO A 1 2768 ? 185.220 185.735 216.291 1.00 31.38  ? 2768 PRO A C     1 
ATOM   10345 O  O     . PRO A 1 2768 ? 185.525 184.905 215.425 1.00 27.28  ? 2768 PRO A O     1 
ATOM   10346 C  CB    . PRO A 1 2768 ? 186.806 185.960 218.248 1.00 33.78  ? 2768 PRO A CB    1 
ATOM   10347 C  CG    . PRO A 1 2768 ? 186.087 186.694 219.310 1.00 33.09  ? 2768 PRO A CG    1 
ATOM   10348 C  CD    . PRO A 1 2768 ? 185.949 188.095 218.806 1.00 36.01  ? 2768 PRO A CD    1 
ATOM   10349 N  N     . LEU A 1 2769 ? 183.961 185.915 216.695 1.00 33.42  ? 2769 LEU A N     1 
ATOM   10350 C  CA    . LEU A 1 2769 ? 182.878 185.113 216.133 1.00 30.22  ? 2769 LEU A CA    1 
ATOM   10351 C  C     . LEU A 1 2769 ? 182.683 185.417 214.653 1.00 30.27  ? 2769 LEU A C     1 
ATOM   10352 O  O     . LEU A 1 2769 ? 182.443 184.514 213.844 1.00 29.51  ? 2769 LEU A O     1 
ATOM   10353 C  CB    . LEU A 1 2769 ? 181.587 185.359 216.916 1.00 29.09  ? 2769 LEU A CB    1 
ATOM   10354 C  CG    . LEU A 1 2769 ? 180.269 184.947 216.260 1.00 28.43  ? 2769 LEU A CG    1 
ATOM   10355 C  CD1   . LEU A 1 2769 ? 180.129 183.438 216.265 1.00 24.24  ? 2769 LEU A CD1   1 
ATOM   10356 C  CD2   . LEU A 1 2769 ? 179.091 185.593 216.966 1.00 33.73  ? 2769 LEU A CD2   1 
ATOM   10357 N  N     . THR A 1 2770 ? 182.783 186.695 214.281 1.00 31.31  ? 2770 THR A N     1 
ATOM   10358 C  CA    . THR A 1 2770 ? 182.691 187.072 212.874 1.00 23.51  ? 2770 THR A CA    1 
ATOM   10359 C  C     . THR A 1 2770 ? 183.862 186.505 212.080 1.00 22.60  ? 2770 THR A C     1 
ATOM   10360 O  O     . THR A 1 2770 ? 183.694 186.035 210.949 1.00 22.14  ? 2770 THR A O     1 
ATOM   10361 C  CB    . THR A 1 2770 ? 182.639 188.596 212.743 1.00 21.79  ? 2770 THR A CB    1 
ATOM   10362 O  OG1   . THR A 1 2770 ? 181.494 189.098 213.441 1.00 24.21  ? 2770 THR A OG1   1 
ATOM   10363 C  CG2   . THR A 1 2770 ? 182.547 189.004 211.281 1.00 20.55  ? 2770 THR A CG2   1 
ATOM   10364 N  N     . ALA A 1 2771 ? 185.062 186.544 212.663 1.00 24.07  ? 2771 ALA A N     1 
ATOM   10365 C  CA    . ALA A 1 2771 ? 186.244 186.029 211.979 1.00 23.30  ? 2771 ALA A CA    1 
ATOM   10366 C  C     . ALA A 1 2771 ? 186.106 184.541 211.689 1.00 23.56  ? 2771 ALA A C     1 
ATOM   10367 O  O     . ALA A 1 2771 ? 186.463 184.070 210.603 1.00 23.64  ? 2771 ALA A O     1 
ATOM   10368 C  CB    . ALA A 1 2771 ? 187.493 186.304 212.817 1.00 21.60  ? 2771 ALA A CB    1 
ATOM   10369 N  N     . ALA A 1 2772 ? 185.592 183.781 212.658 1.00 26.78  ? 2772 ALA A N     1 
ATOM   10370 C  CA    . ALA A 1 2772 ? 185.352 182.359 212.438 1.00 27.01  ? 2772 ALA A CA    1 
ATOM   10371 C  C     . ALA A 1 2772 ? 184.308 182.142 211.351 1.00 26.04  ? 2772 ALA A C     1 
ATOM   10372 O  O     . ALA A 1 2772 ? 184.446 181.251 210.506 1.00 27.36  ? 2772 ALA A O     1 
ATOM   10373 C  CB    . ALA A 1 2772 ? 184.919 181.692 213.745 1.00 29.46  ? 2772 ALA A CB    1 
ATOM   10374 N  N     . MET A 1 2773 ? 183.246 182.951 211.364 1.00 26.56  ? 2773 MET A N     1 
ATOM   10375 C  CA    . MET A 1 2773 ? 182.195 182.822 210.362 1.00 19.09  ? 2773 MET A CA    1 
ATOM   10376 C  C     . MET A 1 2773 ? 182.714 183.180 208.974 1.00 19.97  ? 2773 MET A C     1 
ATOM   10377 O  O     . MET A 1 2773 ? 182.402 182.510 207.984 1.00 22.81  ? 2773 MET A O     1 
ATOM   10378 C  CB    . MET A 1 2773 ? 181.003 183.703 210.741 1.00 17.44  ? 2773 MET A CB    1 
ATOM   10379 C  CG    . MET A 1 2773 ? 179.823 182.918 211.277 1.00 22.83  ? 2773 MET A CG    1 
ATOM   10380 S  SD    . MET A 1 2773 ? 178.283 183.850 211.312 1.00 35.70  ? 2773 MET A SD    1 
ATOM   10381 C  CE    . MET A 1 2773 ? 178.809 185.320 212.171 1.00 24.58  ? 2773 MET A CE    1 
ATOM   10382 N  N     . VAL A 1 2774 ? 183.512 184.248 208.889 1.00 23.27  ? 2774 VAL A N     1 
ATOM   10383 C  CA    . VAL A 1 2774 ? 184.091 184.653 207.609 1.00 21.34  ? 2774 VAL A CA    1 
ATOM   10384 C  C     . VAL A 1 2774 ? 185.024 183.567 207.087 1.00 23.12  ? 2774 VAL A C     1 
ATOM   10385 O  O     . VAL A 1 2774 ? 185.004 183.218 205.900 1.00 23.94  ? 2774 VAL A O     1 
ATOM   10386 C  CB    . VAL A 1 2774 ? 184.824 186.000 207.755 1.00 23.26  ? 2774 VAL A CB    1 
ATOM   10387 C  CG1   . VAL A 1 2774 ? 185.948 186.120 206.732 1.00 23.75  ? 2774 VAL A CG1   1 
ATOM   10388 C  CG2   . VAL A 1 2774 ? 183.852 187.158 207.620 1.00 22.83  ? 2774 VAL A CG2   1 
ATOM   10389 N  N     . GLU A 1 2775 ? 185.852 183.013 207.975 1.00 25.25  ? 2775 GLU A N     1 
ATOM   10390 C  CA    . GLU A 1 2775 ? 186.855 182.039 207.558 1.00 24.76  ? 2775 GLU A CA    1 
ATOM   10391 C  C     . GLU A 1 2775 ? 186.211 180.757 207.045 1.00 22.89  ? 2775 GLU A C     1 
ATOM   10392 O  O     . GLU A 1 2775 ? 186.540 180.279 205.954 1.00 23.70  ? 2775 GLU A O     1 
ATOM   10393 C  CB    . GLU A 1 2775 ? 187.801 181.741 208.722 1.00 25.73  ? 2775 GLU A CB    1 
ATOM   10394 C  CG    . GLU A 1 2775 ? 188.757 180.589 208.473 1.00 24.65  ? 2775 GLU A CG    1 
ATOM   10395 C  CD    . GLU A 1 2775 ? 190.042 180.729 209.263 1.00 32.44  ? 2775 GLU A CD    1 
ATOM   10396 O  OE1   . GLU A 1 2775 ? 189.974 181.153 210.436 1.00 34.70  ? 2775 GLU A OE1   1 
ATOM   10397 O  OE2   . GLU A 1 2775 ? 191.120 180.422 208.712 1.00 36.64  ? 2775 GLU A OE2   1 
ATOM   10398 N  N     . PHE A 1 2776 ? 185.279 180.190 207.816 1.00 20.40  ? 2776 PHE A N     1 
ATOM   10399 C  CA    . PHE A 1 2776 ? 184.653 178.933 207.415 1.00 19.95  ? 2776 PHE A CA    1 
ATOM   10400 C  C     . PHE A 1 2776 ? 183.883 179.086 206.110 1.00 26.99  ? 2776 PHE A C     1 
ATOM   10401 O  O     . PHE A 1 2776 ? 183.855 178.164 205.286 1.00 26.90  ? 2776 PHE A O     1 
ATOM   10402 C  CB    . PHE A 1 2776 ? 183.726 178.421 208.516 1.00 20.20  ? 2776 PHE A CB    1 
ATOM   10403 C  CG    . PHE A 1 2776 ? 183.086 177.103 208.196 1.00 23.68  ? 2776 PHE A CG    1 
ATOM   10404 C  CD1   . PHE A 1 2776 ? 183.861 175.982 207.958 1.00 24.90  ? 2776 PHE A CD1   1 
ATOM   10405 C  CD2   . PHE A 1 2776 ? 181.710 176.990 208.106 1.00 25.56  ? 2776 PHE A CD2   1 
ATOM   10406 C  CE1   . PHE A 1 2776 ? 183.276 174.771 207.655 1.00 24.95  ? 2776 PHE A CE1   1 
ATOM   10407 C  CE2   . PHE A 1 2776 ? 181.119 175.782 207.802 1.00 22.47  ? 2776 PHE A CE2   1 
ATOM   10408 C  CZ    . PHE A 1 2776 ? 181.902 174.672 207.575 1.00 23.41  ? 2776 PHE A CZ    1 
ATOM   10409 N  N     . TYR A 1 2777 ? 183.242 180.238 205.911 1.00 26.00  ? 2777 TYR A N     1 
ATOM   10410 C  CA    . TYR A 1 2777 ? 182.526 180.486 204.664 1.00 21.04  ? 2777 TYR A CA    1 
ATOM   10411 C  C     . TYR A 1 2777 ? 183.482 180.484 203.477 1.00 25.31  ? 2777 TYR A C     1 
ATOM   10412 O  O     . TYR A 1 2777 ? 183.161 179.960 202.405 1.00 28.78  ? 2777 TYR A O     1 
ATOM   10413 C  CB    . TYR A 1 2777 ? 181.773 181.815 204.752 1.00 21.55  ? 2777 TYR A CB    1 
ATOM   10414 C  CG    . TYR A 1 2777 ? 181.350 182.376 203.413 1.00 22.88  ? 2777 TYR A CG    1 
ATOM   10415 C  CD1   . TYR A 1 2777 ? 180.274 181.836 202.721 1.00 19.93  ? 2777 TYR A CD1   1 
ATOM   10416 C  CD2   . TYR A 1 2777 ? 182.025 183.445 202.842 1.00 18.38  ? 2777 TYR A CD2   1 
ATOM   10417 C  CE1   . TYR A 1 2777 ? 179.884 182.347 201.498 1.00 15.61  ? 2777 TYR A CE1   1 
ATOM   10418 C  CE2   . TYR A 1 2777 ? 181.642 183.960 201.621 1.00 18.62  ? 2777 TYR A CE2   1 
ATOM   10419 C  CZ    . TYR A 1 2777 ? 180.572 183.408 200.954 1.00 17.62  ? 2777 TYR A CZ    1 
ATOM   10420 O  OH    . TYR A 1 2777 ? 180.192 183.923 199.737 1.00 16.55  ? 2777 TYR A OH    1 
ATOM   10421 N  N     . THR A 1 2778 ? 184.665 181.075 203.654 1.00 24.12  ? 2778 THR A N     1 
ATOM   10422 C  CA    . THR A 1 2778 ? 185.643 181.125 202.571 1.00 21.24  ? 2778 THR A CA    1 
ATOM   10423 C  C     . THR A 1 2778 ? 186.153 179.732 202.219 1.00 24.87  ? 2778 THR A C     1 
ATOM   10424 O  O     . THR A 1 2778 ? 186.275 179.383 201.039 1.00 29.54  ? 2778 THR A O     1 
ATOM   10425 C  CB    . THR A 1 2778 ? 186.805 182.040 202.957 1.00 20.70  ? 2778 THR A CB    1 
ATOM   10426 O  OG1   . THR A 1 2778 ? 186.291 183.293 203.426 1.00 24.42  ? 2778 THR A OG1   1 
ATOM   10427 C  CG2   . THR A 1 2778 ? 187.709 182.288 201.761 1.00 22.29  ? 2778 THR A CG2   1 
ATOM   10428 N  N     . MET A 1 2779 ? 186.464 178.921 203.234 1.00 25.98  ? 2779 MET A N     1 
ATOM   10429 C  CA    . MET A 1 2779 ? 186.952 177.569 202.977 1.00 27.59  ? 2779 MET A CA    1 
ATOM   10430 C  C     . MET A 1 2779 ? 185.876 176.709 202.326 1.00 29.67  ? 2779 MET A C     1 
ATOM   10431 O  O     . MET A 1 2779 ? 186.157 175.936 201.403 1.00 31.36  ? 2779 MET A O     1 
ATOM   10432 C  CB    . MET A 1 2779 ? 187.442 176.928 204.276 1.00 27.28  ? 2779 MET A CB    1 
ATOM   10433 C  CG    . MET A 1 2779 ? 188.264 177.852 205.156 1.00 26.31  ? 2779 MET A CG    1 
ATOM   10434 S  SD    . MET A 1 2779 ? 188.906 177.045 206.635 1.00 48.33  ? 2779 MET A SD    1 
ATOM   10435 C  CE    . MET A 1 2779 ? 188.913 175.332 206.119 1.00 34.36  ? 2779 MET A CE    1 
ATOM   10436 N  N     . SER A 1 2780 ? 184.634 176.827 202.801 1.00 29.18  ? 2780 SER A N     1 
ATOM   10437 C  CA    . SER A 1 2780 ? 183.541 176.059 202.212 1.00 25.92  ? 2780 SER A CA    1 
ATOM   10438 C  C     . SER A 1 2780 ? 183.292 176.475 200.768 1.00 23.67  ? 2780 SER A C     1 
ATOM   10439 O  O     . SER A 1 2780 ? 183.057 175.625 199.901 1.00 25.23  ? 2780 SER A O     1 
ATOM   10440 C  CB    . SER A 1 2780 ? 182.273 176.226 203.048 1.00 28.80  ? 2780 SER A CB    1 
ATOM   10441 O  OG    . SER A 1 2780 ? 182.529 175.979 204.419 1.00 31.10  ? 2780 SER A OG    1 
ATOM   10442 N  N     . GLN A 1 2781 ? 183.332 177.780 200.493 1.00 25.27  ? 2781 GLN A N     1 
ATOM   10443 C  CA    . GLN A 1 2781 ? 183.180 178.268 199.128 1.00 23.71  ? 2781 GLN A CA    1 
ATOM   10444 C  C     . GLN A 1 2781 ? 184.318 177.813 198.226 1.00 27.53  ? 2781 GLN A C     1 
ATOM   10445 O  O     . GLN A 1 2781 ? 184.084 177.538 197.045 1.00 35.76  ? 2781 GLN A O     1 
ATOM   10446 C  CB    . GLN A 1 2781 ? 183.092 179.794 199.126 1.00 19.36  ? 2781 GLN A CB    1 
ATOM   10447 C  CG    . GLN A 1 2781 ? 182.225 180.374 198.022 1.00 21.95  ? 2781 GLN A CG    1 
ATOM   10448 C  CD    . GLN A 1 2781 ? 182.248 181.889 198.007 1.00 27.85  ? 2781 GLN A CD    1 
ATOM   10449 O  OE1   . GLN A 1 2781 ? 181.203 182.538 198.005 1.00 17.85  ? 2781 GLN A OE1   1 
ATOM   10450 N  NE2   . GLN A 1 2781 ? 183.446 182.461 198.001 1.00 31.65  ? 2781 GLN A NE2   1 
ATOM   10451 N  N     . GLU A 1 2782 ? 185.539 177.735 198.752 1.00 29.61  ? 2782 GLU A N     1 
ATOM   10452 C  CA    . GLU A 1 2782 ? 186.683 177.269 197.983 1.00 31.54  ? 2782 GLU A CA    1 
ATOM   10453 C  C     . GLU A 1 2782 ? 186.718 175.757 197.814 1.00 30.85  ? 2782 GLU A C     1 
ATOM   10454 O  O     . GLU A 1 2782 ? 187.123 175.277 196.750 1.00 32.40  ? 2782 GLU A O     1 
ATOM   10455 C  CB    . GLU A 1 2782 ? 187.984 177.729 198.649 1.00 33.33  ? 2782 GLU A CB    1 
ATOM   10456 C  CG    . GLU A 1 2782 ? 189.127 177.987 197.684 1.00 45.42  ? 2782 GLU A CG    1 
ATOM   10457 C  CD    . GLU A 1 2782 ? 190.478 177.966 198.369 1.00 60.13  ? 2782 GLU A CD    1 
ATOM   10458 O  OE1   . GLU A 1 2782 ? 190.514 178.003 199.617 1.00 58.01  ? 2782 GLU A OE1   1 
ATOM   10459 O  OE2   . GLU A 1 2782 ? 191.505 177.914 197.661 1.00 58.21  ? 2782 GLU A OE2   1 
ATOM   10460 N  N     . ARG A 1 2783 ? 186.304 175.000 198.830 1.00 33.65  ? 2783 ARG A N     1 
ATOM   10461 C  CA    . ARG A 1 2783 ? 186.362 173.543 198.783 1.00 27.62  ? 2783 ARG A CA    1 
ATOM   10462 C  C     . ARG A 1 2783 ? 185.277 172.938 197.901 1.00 29.80  ? 2783 ARG A C     1 
ATOM   10463 O  O     . ARG A 1 2783 ? 185.555 172.018 197.123 1.00 32.42  ? 2783 ARG A O     1 
ATOM   10464 C  CB    . ARG A 1 2783 ? 186.261 172.971 200.200 1.00 24.06  ? 2783 ARG A CB    1 
ATOM   10465 C  CG    . ARG A 1 2783 ? 186.028 171.472 200.259 1.00 28.00  ? 2783 ARG A CG    1 
ATOM   10466 C  CD    . ARG A 1 2783 ? 187.272 170.694 199.861 1.00 27.76  ? 2783 ARG A CD    1 
ATOM   10467 N  NE    . ARG A 1 2783 ? 187.233 169.320 200.349 1.00 30.77  ? 2783 ARG A NE    1 
ATOM   10468 C  CZ    . ARG A 1 2783 ? 186.483 168.359 199.827 1.00 38.46  ? 2783 ARG A CZ    1 
ATOM   10469 N  NH1   . ARG A 1 2783 ? 185.702 168.580 198.782 1.00 37.18  ? 2783 ARG A NH1   1 
ATOM   10470 N  NH2   . ARG A 1 2783 ? 186.520 167.143 200.366 1.00 35.97  ? 2783 ARG A NH2   1 
ATOM   10471 N  N     . PHE A 1 2784 ? 184.049 173.436 197.998 1.00 31.00  ? 2784 PHE A N     1 
ATOM   10472 C  CA    . PHE A 1 2784 ? 182.916 172.900 197.253 1.00 27.46  ? 2784 PHE A CA    1 
ATOM   10473 C  C     . PHE A 1 2784 ? 182.516 173.898 196.177 1.00 34.36  ? 2784 PHE A C     1 
ATOM   10474 O  O     . PHE A 1 2784 ? 182.265 175.071 196.474 1.00 38.05  ? 2784 PHE A O     1 
ATOM   10475 C  CB    . PHE A 1 2784 ? 181.743 172.602 198.186 1.00 23.99  ? 2784 PHE A CB    1 
ATOM   10476 C  CG    . PHE A 1 2784 ? 182.134 171.852 199.426 1.00 26.84  ? 2784 PHE A CG    1 
ATOM   10477 C  CD1   . PHE A 1 2784 ? 182.513 170.522 199.356 1.00 25.93  ? 2784 PHE A CD1   1 
ATOM   10478 C  CD2   . PHE A 1 2784 ? 182.131 172.478 200.660 1.00 27.51  ? 2784 PHE A CD2   1 
ATOM   10479 C  CE1   . PHE A 1 2784 ? 182.877 169.829 200.494 1.00 26.89  ? 2784 PHE A CE1   1 
ATOM   10480 C  CE2   . PHE A 1 2784 ? 182.494 171.792 201.802 1.00 26.01  ? 2784 PHE A CE2   1 
ATOM   10481 C  CZ    . PHE A 1 2784 ? 182.868 170.466 201.719 1.00 25.86  ? 2784 PHE A CZ    1 
ATOM   10482 N  N     . THR A 1 2785 ? 182.457 173.430 194.935 1.00 33.01  ? 2785 THR A N     1 
ATOM   10483 C  CA    . THR A 1 2785 ? 182.162 174.265 193.781 1.00 30.64  ? 2785 THR A CA    1 
ATOM   10484 C  C     . THR A 1 2785 ? 181.157 173.550 192.885 1.00 30.12  ? 2785 THR A C     1 
ATOM   10485 O  O     . THR A 1 2785 ? 180.865 172.364 193.062 1.00 28.14  ? 2785 THR A O     1 
ATOM   10486 C  CB    . THR A 1 2785 ? 183.446 174.594 193.005 1.00 31.66  ? 2785 THR A CB    1 
ATOM   10487 O  OG1   . THR A 1 2785 ? 184.536 174.726 193.925 1.00 31.94  ? 2785 THR A OG1   1 
ATOM   10488 C  CG2   . THR A 1 2785 ? 183.298 175.905 192.243 1.00 35.47  ? 2785 THR A CG2   1 
ATOM   10489 N  N     . GLN A 1 2786 ? 180.621 174.291 191.914 1.00 34.17  ? 2786 GLN A N     1 
ATOM   10490 C  CA    . GLN A 1 2786 ? 179.653 173.738 190.974 1.00 28.23  ? 2786 GLN A CA    1 
ATOM   10491 C  C     . GLN A 1 2786 ? 180.236 172.636 190.100 1.00 33.72  ? 2786 GLN A C     1 
ATOM   10492 O  O     . GLN A 1 2786 ? 179.469 171.895 189.476 1.00 35.51  ? 2786 GLN A O     1 
ATOM   10493 C  CB    . GLN A 1 2786 ? 179.088 174.850 190.089 1.00 29.81  ? 2786 GLN A CB    1 
ATOM   10494 C  CG    . GLN A 1 2786 ? 178.034 175.704 190.768 1.00 28.95  ? 2786 GLN A CG    1 
ATOM   10495 C  CD    . GLN A 1 2786 ? 177.173 176.460 189.777 1.00 33.64  ? 2786 GLN A CD    1 
ATOM   10496 O  OE1   . GLN A 1 2786 ? 177.227 177.687 189.698 1.00 34.61  ? 2786 GLN A OE1   1 
ATOM   10497 N  NE2   . GLN A 1 2786 ? 176.370 175.728 189.013 1.00 30.68  ? 2786 GLN A NE2   1 
ATOM   10498 N  N     . ASP A 1 2787 ? 181.564 172.518 190.029 1.00 33.46  ? 2787 ASP A N     1 
ATOM   10499 C  CA    . ASP A 1 2787 ? 182.170 171.417 189.287 1.00 33.12  ? 2787 ASP A CA    1 
ATOM   10500 C  C     . ASP A 1 2787 ? 181.813 170.074 189.909 1.00 34.52  ? 2787 ASP A C     1 
ATOM   10501 O  O     . ASP A 1 2787 ? 181.536 169.104 189.195 1.00 37.33  ? 2787 ASP A O     1 
ATOM   10502 C  CB    . ASP A 1 2787 ? 183.686 171.597 189.228 1.00 37.55  ? 2787 ASP A CB    1 
ATOM   10503 C  CG    . ASP A 1 2787 ? 184.090 173.001 188.825 1.00 55.40  ? 2787 ASP A CG    1 
ATOM   10504 O  OD1   . ASP A 1 2787 ? 183.872 173.368 187.652 1.00 57.05  ? 2787 ASP A OD1   1 
ATOM   10505 O  OD2   . ASP A 1 2787 ? 184.623 173.738 189.682 1.00 56.39  ? 2787 ASP A OD2   1 
ATOM   10506 N  N     . THR A 1 2788 ? 181.816 169.997 191.241 1.00 34.83  ? 2788 THR A N     1 
ATOM   10507 C  CA    . THR A 1 2788 ? 181.478 168.748 191.915 1.00 29.57  ? 2788 THR A CA    1 
ATOM   10508 C  C     . THR A 1 2788 ? 179.990 168.444 191.789 1.00 31.35  ? 2788 THR A C     1 
ATOM   10509 O  O     . THR A 1 2788 ? 179.597 167.419 191.221 1.00 34.74  ? 2788 THR A O     1 
ATOM   10510 C  CB    . THR A 1 2788 ? 181.893 168.818 193.386 1.00 34.00  ? 2788 THR A CB    1 
ATOM   10511 O  OG1   . THR A 1 2788 ? 183.096 169.587 193.510 1.00 29.99  ? 2788 THR A OG1   1 
ATOM   10512 C  CG2   . THR A 1 2788 ? 182.133 167.421 193.937 1.00 32.65  ? 2788 THR A CG2   1 
ATOM   10513 N  N     . GLN A 1 2789 ? 179.145 169.328 192.312 1.00 31.18  ? 2789 GLN A N     1 
ATOM   10514 C  CA    . GLN A 1 2789 ? 177.703 169.166 192.253 1.00 28.70  ? 2789 GLN A CA    1 
ATOM   10515 C  C     . GLN A 1 2789 ? 177.050 170.463 191.804 1.00 27.16  ? 2789 GLN A C     1 
ATOM   10516 O  O     . GLN A 1 2789 ? 177.521 171.553 192.145 1.00 27.92  ? 2789 GLN A O     1 
ATOM   10517 C  CB    . GLN A 1 2789 ? 177.130 168.746 193.615 1.00 25.62  ? 2789 GLN A CB    1 
ATOM   10518 C  CG    . GLN A 1 2789 ? 177.757 167.487 194.189 1.00 25.98  ? 2789 GLN A CG    1 
ATOM   10519 C  CD    . GLN A 1 2789 ? 177.213 166.224 193.552 1.00 29.05  ? 2789 GLN A CD    1 
ATOM   10520 O  OE1   . GLN A 1 2789 ? 176.164 166.242 192.908 1.00 33.18  ? 2789 GLN A OE1   1 
ATOM   10521 N  NE2   . GLN A 1 2789 ? 177.927 165.119 193.727 1.00 30.19  ? 2789 GLN A NE2   1 
ATOM   10522 N  N     . PRO A 1 2790 ? 175.962 170.375 191.035 1.00 32.50  ? 2790 PRO A N     1 
ATOM   10523 C  CA    . PRO A 1 2790 ? 175.334 171.599 190.509 1.00 27.62  ? 2790 PRO A CA    1 
ATOM   10524 C  C     . PRO A 1 2790 ? 174.802 172.534 191.579 1.00 24.08  ? 2790 PRO A C     1 
ATOM   10525 O  O     . PRO A 1 2790 ? 174.709 173.742 191.332 1.00 25.82  ? 2790 PRO A O     1 
ATOM   10526 C  CB    . PRO A 1 2790 ? 174.201 171.057 189.626 1.00 34.03  ? 2790 PRO A CB    1 
ATOM   10527 C  CG    . PRO A 1 2790 ? 173.944 169.676 190.133 1.00 37.52  ? 2790 PRO A CG    1 
ATOM   10528 C  CD    . PRO A 1 2790 ? 175.278 169.158 190.566 1.00 33.06  ? 2790 PRO A CD    1 
ATOM   10529 N  N     . HIS A 1 2791 ? 174.444 172.022 192.754 1.00 25.36  ? 2791 HIS A N     1 
ATOM   10530 C  CA    . HIS A 1 2791 ? 173.837 172.839 193.797 1.00 21.32  ? 2791 HIS A CA    1 
ATOM   10531 C  C     . HIS A 1 2791 ? 174.843 173.362 194.814 1.00 20.06  ? 2791 HIS A C     1 
ATOM   10532 O  O     . HIS A 1 2791 ? 174.433 173.965 195.811 1.00 21.07  ? 2791 HIS A O     1 
ATOM   10533 C  CB    . HIS A 1 2791 ? 172.743 172.046 194.519 1.00 19.90  ? 2791 HIS A CB    1 
ATOM   10534 C  CG    . HIS A 1 2791 ? 173.238 170.810 195.201 1.00 18.97  ? 2791 HIS A CG    1 
ATOM   10535 N  ND1   . HIS A 1 2791 ? 173.638 169.686 194.511 1.00 24.78  ? 2791 HIS A ND1   1 
ATOM   10536 C  CD2   . HIS A 1 2791 ? 173.391 170.518 196.515 1.00 17.71  ? 2791 HIS A CD2   1 
ATOM   10537 C  CE1   . HIS A 1 2791 ? 174.020 168.758 195.369 1.00 24.02  ? 2791 HIS A CE1   1 
ATOM   10538 N  NE2   . HIS A 1 2791 ? 173.879 169.237 196.591 1.00 20.66  ? 2791 HIS A NE2   1 
ATOM   10539 N  N     . TYR A 1 2792 ? 176.141 173.149 194.594 1.00 20.39  ? 2792 TYR A N     1 
ATOM   10540 C  CA    . TYR A 1 2792 ? 177.171 173.623 195.519 1.00 20.22  ? 2792 TYR A CA    1 
ATOM   10541 C  C     . TYR A 1 2792 ? 177.458 175.100 195.244 1.00 24.21  ? 2792 TYR A C     1 
ATOM   10542 O  O     . TYR A 1 2792 ? 178.488 175.484 194.685 1.00 31.33  ? 2792 TYR A O     1 
ATOM   10543 C  CB    . TYR A 1 2792 ? 178.431 172.778 195.400 1.00 23.44  ? 2792 TYR A CB    1 
ATOM   10544 C  CG    . TYR A 1 2792 ? 178.349 171.433 196.090 1.00 25.58  ? 2792 TYR A CG    1 
ATOM   10545 C  CD1   . TYR A 1 2792 ? 177.194 171.034 196.748 1.00 22.80  ? 2792 TYR A CD1   1 
ATOM   10546 C  CD2   . TYR A 1 2792 ? 179.432 170.564 196.087 1.00 24.03  ? 2792 TYR A CD2   1 
ATOM   10547 C  CE1   . TYR A 1 2792 ? 177.118 169.807 197.378 1.00 21.65  ? 2792 TYR A CE1   1 
ATOM   10548 C  CE2   . TYR A 1 2792 ? 179.366 169.338 196.716 1.00 23.91  ? 2792 TYR A CE2   1 
ATOM   10549 C  CZ    . TYR A 1 2792 ? 178.208 168.963 197.359 1.00 24.10  ? 2792 TYR A CZ    1 
ATOM   10550 O  OH    . TYR A 1 2792 ? 178.142 167.740 197.983 1.00 23.90  ? 2792 TYR A OH    1 
ATOM   10551 N  N     . ILE A 1 2793 ? 176.510 175.940 195.652 1.00 21.18  ? 2793 ILE A N     1 
ATOM   10552 C  CA    . ILE A 1 2793 ? 176.638 177.390 195.555 1.00 17.72  ? 2793 ILE A CA    1 
ATOM   10553 C  C     . ILE A 1 2793 ? 176.656 177.953 196.967 1.00 19.42  ? 2793 ILE A C     1 
ATOM   10554 O  O     . ILE A 1 2793 ? 175.724 177.720 197.746 1.00 22.28  ? 2793 ILE A O     1 
ATOM   10555 C  CB    . ILE A 1 2793 ? 175.501 178.022 194.735 1.00 25.03  ? 2793 ILE A CB    1 
ATOM   10556 C  CG1   . ILE A 1 2793 ? 175.594 177.608 193.266 1.00 23.23  ? 2793 ILE A CG1   1 
ATOM   10557 C  CG2   . ILE A 1 2793 ? 175.528 179.536 194.866 1.00 21.19  ? 2793 ILE A CG2   1 
ATOM   10558 C  CD1   . ILE A 1 2793 ? 174.713 176.440 192.912 1.00 23.18  ? 2793 ILE A CD1   1 
ATOM   10559 N  N     . TYR A 1 2794 ? 177.713 178.690 197.295 1.00 19.40  ? 2794 TYR A N     1 
ATOM   10560 C  CA    . TYR A 1 2794 ? 177.841 179.358 198.581 1.00 16.21  ? 2794 TYR A CA    1 
ATOM   10561 C  C     . TYR A 1 2794 ? 177.959 180.856 198.346 1.00 13.94  ? 2794 TYR A C     1 
ATOM   10562 O  O     . TYR A 1 2794 ? 178.719 181.296 197.478 1.00 17.46  ? 2794 TYR A O     1 
ATOM   10563 C  CB    . TYR A 1 2794 ? 179.044 178.828 199.363 1.00 16.50  ? 2794 TYR A CB    1 
ATOM   10564 C  CG    . TYR A 1 2794 ? 178.827 177.434 199.907 1.00 19.18  ? 2794 TYR A CG    1 
ATOM   10565 C  CD1   . TYR A 1 2794 ? 177.697 177.132 200.655 1.00 25.44  ? 2794 TYR A CD1   1 
ATOM   10566 C  CD2   . TYR A 1 2794 ? 179.743 176.421 199.669 1.00 21.54  ? 2794 TYR A CD2   1 
ATOM   10567 C  CE1   . TYR A 1 2794 ? 177.487 175.861 201.152 1.00 21.84  ? 2794 TYR A CE1   1 
ATOM   10568 C  CE2   . TYR A 1 2794 ? 179.542 175.147 200.165 1.00 26.07  ? 2794 TYR A CE2   1 
ATOM   10569 C  CZ    . TYR A 1 2794 ? 178.412 174.873 200.905 1.00 25.10  ? 2794 TYR A CZ    1 
ATOM   10570 O  OH    . TYR A 1 2794 ? 178.206 173.607 201.400 1.00 33.53  ? 2794 TYR A OH    1 
ATOM   10571 N  N     . SER A 1 2795 ? 177.201 181.629 199.112 1.00 12.68  ? 2795 SER A N     1 
ATOM   10572 C  CA    . SER A 1 2795 ? 177.097 183.065 198.906 1.00 10.06  ? 2795 SER A CA    1 
ATOM   10573 C  C     . SER A 1 2795 ? 176.889 183.721 200.259 1.00 12.96  ? 2795 SER A C     1 
ATOM   10574 O  O     . SER A 1 2795 ? 176.667 183.034 201.264 1.00 14.96  ? 2795 SER A O     1 
ATOM   10575 C  CB    . SER A 1 2795 ? 175.946 183.405 197.952 1.00 10.50  ? 2795 SER A CB    1 
ATOM   10576 O  OG    . SER A 1 2795 ? 174.759 182.726 198.323 1.00 13.69  ? 2795 SER A OG    1 
ATOM   10577 N  N     . PRO A 1 2796 ? 176.968 185.055 200.327 1.00 11.00  ? 2796 PRO A N     1 
ATOM   10578 C  CA    . PRO A 1 2796 ? 176.591 185.749 201.570 1.00 9.39   ? 2796 PRO A CA    1 
ATOM   10579 C  C     . PRO A 1 2796 ? 175.176 185.451 202.040 1.00 11.14  ? 2796 PRO A C     1 
ATOM   10580 O  O     . PRO A 1 2796 ? 174.824 185.842 203.160 1.00 17.42  ? 2796 PRO A O     1 
ATOM   10581 C  CB    . PRO A 1 2796 ? 176.755 187.228 201.204 1.00 12.58  ? 2796 PRO A CB    1 
ATOM   10582 C  CG    . PRO A 1 2796 ? 177.834 187.223 200.185 1.00 15.32  ? 2796 PRO A CG    1 
ATOM   10583 C  CD    . PRO A 1 2796 ? 177.638 185.966 199.380 1.00 11.30  ? 2796 PRO A CD    1 
ATOM   10584 N  N     . ARG A 1 2797 ? 174.356 184.785 201.223 1.00 13.31  ? 2797 ARG A N     1 
ATOM   10585 C  CA    . ARG A 1 2797 ? 173.050 184.330 201.687 1.00 13.26  ? 2797 ARG A CA    1 
ATOM   10586 C  C     . ARG A 1 2797 ? 173.194 183.331 202.827 1.00 14.39  ? 2797 ARG A C     1 
ATOM   10587 O  O     . ARG A 1 2797 ? 172.432 183.372 203.800 1.00 18.83  ? 2797 ARG A O     1 
ATOM   10588 C  CB    . ARG A 1 2797 ? 172.271 183.713 200.527 1.00 14.09  ? 2797 ARG A CB    1 
ATOM   10589 C  CG    . ARG A 1 2797 ? 171.687 184.728 199.564 1.00 16.13  ? 2797 ARG A CG    1 
ATOM   10590 C  CD    . ARG A 1 2797 ? 170.465 184.175 198.859 1.00 19.47  ? 2797 ARG A CD    1 
ATOM   10591 N  NE    . ARG A 1 2797 ? 170.832 183.353 197.713 1.00 16.28  ? 2797 ARG A NE    1 
ATOM   10592 C  CZ    . ARG A 1 2797 ? 170.614 183.690 196.450 1.00 15.65  ? 2797 ARG A CZ    1 
ATOM   10593 N  NH1   . ARG A 1 2797 ? 170.035 184.836 196.132 1.00 11.76  ? 2797 ARG A NH1   1 
ATOM   10594 N  NH2   . ARG A 1 2797 ? 170.989 182.858 195.483 1.00 22.00  ? 2797 ARG A NH2   1 
ATOM   10595 N  N     . GLU A 1 2798 ? 174.165 182.420 202.721 1.00 14.89  ? 2798 GLU A N     1 
ATOM   10596 C  CA    . GLU A 1 2798 ? 174.443 181.501 203.820 1.00 17.08  ? 2798 GLU A CA    1 
ATOM   10597 C  C     . GLU A 1 2798 ? 174.927 182.254 205.050 1.00 13.78  ? 2798 GLU A C     1 
ATOM   10598 O  O     . GLU A 1 2798 ? 174.564 181.912 206.182 1.00 16.21  ? 2798 GLU A O     1 
ATOM   10599 C  CB    . GLU A 1 2798 ? 175.478 180.461 203.389 1.00 18.41  ? 2798 GLU A CB    1 
ATOM   10600 C  CG    . GLU A 1 2798 ? 174.886 179.194 202.796 1.00 23.36  ? 2798 GLU A CG    1 
ATOM   10601 C  CD    . GLU A 1 2798 ? 174.100 179.456 201.527 1.00 27.58  ? 2798 GLU A CD    1 
ATOM   10602 O  OE1   . GLU A 1 2798 ? 174.556 180.275 200.702 1.00 21.38  ? 2798 GLU A OE1   1 
ATOM   10603 O  OE2   . GLU A 1 2798 ? 173.027 178.841 201.352 1.00 30.64  ? 2798 GLU A OE2   1 
ATOM   10604 N  N     . MET A 1 2799 ? 175.751 183.283 204.848 1.00 12.33  ? 2799 MET A N     1 
ATOM   10605 C  CA    . MET A 1 2799 ? 176.243 184.069 205.973 1.00 11.30  ? 2799 MET A CA    1 
ATOM   10606 C  C     . MET A 1 2799 ? 175.116 184.857 206.628 1.00 15.23  ? 2799 MET A C     1 
ATOM   10607 O  O     . MET A 1 2799 ? 175.111 185.046 207.850 1.00 23.19  ? 2799 MET A O     1 
ATOM   10608 C  CB    . MET A 1 2799 ? 177.358 185.002 205.504 1.00 10.67  ? 2799 MET A CB    1 
ATOM   10609 C  CG    . MET A 1 2799 ? 178.723 184.341 205.461 1.00 15.65  ? 2799 MET A CG    1 
ATOM   10610 S  SD    . MET A 1 2799 ? 179.728 184.703 206.908 1.00 27.32  ? 2799 MET A SD    1 
ATOM   10611 C  CE    . MET A 1 2799 ? 180.772 185.998 206.256 1.00 26.95  ? 2799 MET A CE    1 
ATOM   10612 N  N     . THR A 1 2800 ? 174.157 185.333 205.831 1.00 11.68  ? 2800 THR A N     1 
ATOM   10613 C  CA    . THR A 1 2800 ? 172.978 185.978 206.400 1.00 13.91  ? 2800 THR A CA    1 
ATOM   10614 C  C     . THR A 1 2800 ? 172.139 184.982 207.192 1.00 15.06  ? 2800 THR A C     1 
ATOM   10615 O  O     . THR A 1 2800 ? 171.650 185.298 208.283 1.00 17.65  ? 2800 THR A O     1 
ATOM   10616 C  CB    . THR A 1 2800 ? 172.144 186.622 205.291 1.00 13.70  ? 2800 THR A CB    1 
ATOM   10617 O  OG1   . THR A 1 2800 ? 172.921 187.628 204.629 1.00 16.33  ? 2800 THR A OG1   1 
ATOM   10618 C  CG2   . THR A 1 2800 ? 170.889 187.259 205.865 1.00 14.54  ? 2800 THR A CG2   1 
ATOM   10619 N  N     . ARG A 1 2801 ? 171.966 183.770 206.659 1.00 13.65  ? 2801 ARG A N     1 
ATOM   10620 C  CA    . ARG A 1 2801 ? 171.222 182.741 207.379 1.00 12.75  ? 2801 ARG A CA    1 
ATOM   10621 C  C     . ARG A 1 2801 ? 171.962 182.317 208.640 1.00 16.62  ? 2801 ARG A C     1 
ATOM   10622 O  O     . ARG A 1 2801 ? 171.339 181.951 209.644 1.00 21.21  ? 2801 ARG A O     1 
ATOM   10623 C  CB    . ARG A 1 2801 ? 170.987 181.537 206.469 1.00 14.59  ? 2801 ARG A CB    1 
ATOM   10624 C  CG    . ARG A 1 2801 ? 169.706 181.598 205.660 1.00 20.34  ? 2801 ARG A CG    1 
ATOM   10625 C  CD    . ARG A 1 2801 ? 169.749 180.593 204.523 1.00 31.29  ? 2801 ARG A CD    1 
ATOM   10626 N  NE    . ARG A 1 2801 ? 169.091 181.092 203.322 1.00 41.73  ? 2801 ARG A NE    1 
ATOM   10627 C  CZ    . ARG A 1 2801 ? 169.526 180.876 202.089 1.00 37.27  ? 2801 ARG A CZ    1 
ATOM   10628 N  NH1   . ARG A 1 2801 ? 170.622 180.173 201.856 1.00 25.67  ? 2801 ARG A NH1   1 
ATOM   10629 N  NH2   . ARG A 1 2801 ? 168.845 181.378 201.063 1.00 34.28  ? 2801 ARG A NH2   1 
ATOM   10630 N  N     . TRP A 1 2802 ? 173.295 182.352 208.599 1.00 14.30  ? 2802 TRP A N     1 
ATOM   10631 C  CA    . TRP A 1 2802 ? 174.098 182.023 209.771 1.00 13.26  ? 2802 TRP A CA    1 
ATOM   10632 C  C     . TRP A 1 2802 ? 173.812 182.978 210.921 1.00 15.86  ? 2802 TRP A C     1 
ATOM   10633 O  O     . TRP A 1 2802 ? 173.635 182.554 212.069 1.00 21.58  ? 2802 TRP A O     1 
ATOM   10634 C  CB    . TRP A 1 2802 ? 175.578 182.060 209.397 1.00 14.38  ? 2802 TRP A CB    1 
ATOM   10635 C  CG    . TRP A 1 2802 ? 176.446 181.137 210.184 1.00 17.02  ? 2802 TRP A CG    1 
ATOM   10636 C  CD1   . TRP A 1 2802 ? 176.155 180.552 211.380 1.00 12.99  ? 2802 TRP A CD1   1 
ATOM   10637 C  CD2   . TRP A 1 2802 ? 177.762 180.704 209.833 1.00 17.60  ? 2802 TRP A CD2   1 
ATOM   10638 N  NE1   . TRP A 1 2802 ? 177.210 179.776 211.795 1.00 13.22  ? 2802 TRP A NE1   1 
ATOM   10639 C  CE2   . TRP A 1 2802 ? 178.210 179.854 210.862 1.00 16.41  ? 2802 TRP A CE2   1 
ATOM   10640 C  CE3   . TRP A 1 2802 ? 178.607 180.953 208.747 1.00 20.16  ? 2802 TRP A CE3   1 
ATOM   10641 C  CZ2   . TRP A 1 2802 ? 179.464 179.253 210.838 1.00 17.13  ? 2802 TRP A CZ2   1 
ATOM   10642 C  CZ3   . TRP A 1 2802 ? 179.851 180.354 208.726 1.00 21.47  ? 2802 TRP A CZ3   1 
ATOM   10643 C  CH2   . TRP A 1 2802 ? 180.267 179.514 209.764 1.00 16.86  ? 2802 TRP A CH2   1 
ATOM   10644 N  N     . VAL A 1 2803 ? 173.763 184.277 210.629 1.00 16.52  ? 2803 VAL A N     1 
ATOM   10645 C  CA    . VAL A 1 2803 ? 173.503 185.262 211.673 1.00 17.09  ? 2803 VAL A CA    1 
ATOM   10646 C  C     . VAL A 1 2803 ? 172.062 185.152 212.158 1.00 19.61  ? 2803 VAL A C     1 
ATOM   10647 O  O     . VAL A 1 2803 ? 171.786 185.263 213.359 1.00 22.41  ? 2803 VAL A O     1 
ATOM   10648 C  CB    . VAL A 1 2803 ? 173.834 186.676 211.158 1.00 20.66  ? 2803 VAL A CB    1 
ATOM   10649 C  CG1   . VAL A 1 2803 ? 173.179 187.726 212.023 1.00 25.04  ? 2803 VAL A CG1   1 
ATOM   10650 C  CG2   . VAL A 1 2803 ? 175.338 186.883 211.113 1.00 21.97  ? 2803 VAL A CG2   1 
ATOM   10651 N  N     . ARG A 1 2804 ? 171.124 184.919 211.236 1.00 23.31  ? 2804 ARG A N     1 
ATOM   10652 C  CA    . ARG A 1 2804 ? 169.729 184.727 211.624 1.00 24.22  ? 2804 ARG A CA    1 
ATOM   10653 C  C     . ARG A 1 2804 ? 169.564 183.515 212.531 1.00 28.17  ? 2804 ARG A C     1 
ATOM   10654 O  O     . ARG A 1 2804 ? 168.834 183.571 213.527 1.00 31.33  ? 2804 ARG A O     1 
ATOM   10655 C  CB    . ARG A 1 2804 ? 168.851 184.579 210.380 1.00 24.06  ? 2804 ARG A CB    1 
ATOM   10656 C  CG    . ARG A 1 2804 ? 168.546 185.876 209.644 1.00 35.59  ? 2804 ARG A CG    1 
ATOM   10657 C  CD    . ARG A 1 2804 ? 168.086 186.988 210.581 1.00 41.73  ? 2804 ARG A CD    1 
ATOM   10658 N  NE    . ARG A 1 2804 ? 167.119 186.531 211.572 1.00 48.37  ? 2804 ARG A NE    1 
ATOM   10659 C  CZ    . ARG A 1 2804 ? 166.286 187.327 212.228 1.00 48.08  ? 2804 ARG A CZ    1 
ATOM   10660 N  NH1   . ARG A 1 2804 ? 166.274 188.634 212.022 1.00 44.13  ? 2804 ARG A NH1   1 
ATOM   10661 N  NH2   . ARG A 1 2804 ? 165.443 186.799 213.110 1.00 47.12  ? 2804 ARG A NH2   1 
ATOM   10662 N  N     . GLY A 1 2805 ? 170.232 182.408 212.202 1.00 21.35  ? 2805 GLY A N     1 
ATOM   10663 C  CA    . GLY A 1 2805 ? 170.097 181.208 213.010 1.00 19.09  ? 2805 GLY A CA    1 
ATOM   10664 C  C     . GLY A 1 2805 ? 170.628 181.384 214.419 1.00 19.52  ? 2805 GLY A C     1 
ATOM   10665 O  O     . GLY A 1 2805 ? 169.996 180.955 215.388 1.00 24.28  ? 2805 GLY A O     1 
ATOM   10666 N  N     . ILE A 1 2806 ? 171.799 182.009 214.555 1.00 19.86  ? 2806 ILE A N     1 
ATOM   10667 C  CA    . ILE A 1 2806 ? 172.360 182.252 215.880 1.00 21.53  ? 2806 ILE A CA    1 
ATOM   10668 C  C     . ILE A 1 2806 ? 171.501 183.249 216.648 1.00 27.18  ? 2806 ILE A C     1 
ATOM   10669 O  O     . ILE A 1 2806 ? 171.242 183.076 217.845 1.00 35.25  ? 2806 ILE A O     1 
ATOM   10670 C  CB    . ILE A 1 2806 ? 173.819 182.729 215.765 1.00 21.36  ? 2806 ILE A CB    1 
ATOM   10671 C  CG1   . ILE A 1 2806 ? 174.656 181.700 215.005 1.00 18.24  ? 2806 ILE A CG1   1 
ATOM   10672 C  CG2   . ILE A 1 2806 ? 174.409 182.976 217.142 1.00 22.82  ? 2806 ILE A CG2   1 
ATOM   10673 C  CD1   . ILE A 1 2806 ? 176.114 182.071 214.884 1.00 20.52  ? 2806 ILE A CD1   1 
ATOM   10674 N  N     . PHE A 1 2807 ? 171.043 184.304 215.971 1.00 26.11  ? 2807 PHE A N     1 
ATOM   10675 C  CA    . PHE A 1 2807 ? 170.222 185.312 216.635 1.00 25.82  ? 2807 PHE A CA    1 
ATOM   10676 C  C     . PHE A 1 2807 ? 168.897 184.729 217.113 1.00 31.09  ? 2807 PHE A C     1 
ATOM   10677 O  O     . PHE A 1 2807 ? 168.430 185.053 218.211 1.00 37.35  ? 2807 PHE A O     1 
ATOM   10678 C  CB    . PHE A 1 2807 ? 169.979 186.491 215.694 1.00 30.77  ? 2807 PHE A CB    1 
ATOM   10679 C  CG    . PHE A 1 2807 ? 169.017 187.506 216.235 1.00 33.11  ? 2807 PHE A CG    1 
ATOM   10680 C  CD1   . PHE A 1 2807 ? 169.412 188.407 217.208 1.00 36.37  ? 2807 PHE A CD1   1 
ATOM   10681 C  CD2   . PHE A 1 2807 ? 167.716 187.559 215.767 1.00 33.27  ? 2807 PHE A CD2   1 
ATOM   10682 C  CE1   . PHE A 1 2807 ? 168.525 189.340 217.707 1.00 39.96  ? 2807 PHE A CE1   1 
ATOM   10683 C  CE2   . PHE A 1 2807 ? 166.826 188.490 216.261 1.00 38.97  ? 2807 PHE A CE2   1 
ATOM   10684 C  CZ    . PHE A 1 2807 ? 167.230 189.380 217.233 1.00 44.35  ? 2807 PHE A CZ    1 
ATOM   10685 N  N     . GLU A 1 2808 ? 168.272 183.876 216.298 1.00 30.15  ? 2808 GLU A N     1 
ATOM   10686 C  CA    . GLU A 1 2808 ? 166.988 183.297 216.680 1.00 32.25  ? 2808 GLU A CA    1 
ATOM   10687 C  C     . GLU A 1 2808 ? 167.118 182.436 217.929 1.00 34.26  ? 2808 GLU A C     1 
ATOM   10688 O  O     . GLU A 1 2808 ? 166.243 182.461 218.802 1.00 33.03  ? 2808 GLU A O     1 
ATOM   10689 C  CB    . GLU A 1 2808 ? 166.413 182.483 215.522 1.00 30.68  ? 2808 GLU A CB    1 
ATOM   10690 C  CG    . GLU A 1 2808 ? 165.285 183.178 214.782 1.00 39.36  ? 2808 GLU A CG    1 
ATOM   10691 C  CD    . GLU A 1 2808 ? 165.322 182.928 213.288 1.00 52.46  ? 2808 GLU A CD    1 
ATOM   10692 O  OE1   . GLU A 1 2808 ? 166.101 182.055 212.848 1.00 44.74  ? 2808 GLU A OE1   1 
ATOM   10693 O  OE2   . GLU A 1 2808 ? 164.571 183.603 212.553 1.00 54.00  ? 2808 GLU A OE2   1 
ATOM   10694 N  N     . ALA A 1 2809 ? 168.201 181.665 218.031 1.00 29.20  ? 2809 ALA A N     1 
ATOM   10695 C  CA    . ALA A 1 2809 ? 168.427 180.867 219.230 1.00 31.09  ? 2809 ALA A CA    1 
ATOM   10696 C  C     . ALA A 1 2809 ? 168.726 181.749 220.437 1.00 35.31  ? 2809 ALA A C     1 
ATOM   10697 O  O     . ALA A 1 2809 ? 168.313 181.434 221.559 1.00 42.56  ? 2809 ALA A O     1 
ATOM   10698 C  CB    . ALA A 1 2809 ? 169.563 179.874 218.993 1.00 26.71  ? 2809 ALA A CB    1 
ATOM   10699 N  N     . LEU A 1 2810 ? 169.445 182.855 220.228 1.00 33.20  ? 2810 LEU A N     1 
ATOM   10700 C  CA    . LEU A 1 2810 ? 169.900 183.691 221.332 1.00 34.94  ? 2810 LEU A CA    1 
ATOM   10701 C  C     . LEU A 1 2810 ? 168.837 184.656 221.843 1.00 41.42  ? 2810 LEU A C     1 
ATOM   10702 O  O     . LEU A 1 2810 ? 169.005 185.214 222.933 1.00 42.53  ? 2810 LEU A O     1 
ATOM   10703 C  CB    . LEU A 1 2810 ? 171.132 184.495 220.910 1.00 35.97  ? 2810 LEU A CB    1 
ATOM   10704 C  CG    . LEU A 1 2810 ? 172.450 183.739 220.750 1.00 33.67  ? 2810 LEU A CG    1 
ATOM   10705 C  CD1   . LEU A 1 2810 ? 173.566 184.700 220.356 1.00 36.52  ? 2810 LEU A CD1   1 
ATOM   10706 C  CD2   . LEU A 1 2810 ? 172.799 182.980 222.009 1.00 39.39  ? 2810 LEU A CD2   1 
ATOM   10707 N  N     . ARG A 1 2811 ? 167.792 184.881 221.044 1.00 43.41  ? 2811 ARG A N     1 
ATOM   10708 C  CA    . ARG A 1 2811 ? 166.732 185.850 221.425 1.00 43.10  ? 2811 ARG A CA    1 
ATOM   10709 C  C     . ARG A 1 2811 ? 166.163 185.468 222.803 1.00 43.97  ? 2811 ARG A C     1 
ATOM   10710 O  O     . ARG A 1 2811 ? 166.225 186.315 223.720 1.00 47.82  ? 2811 ARG A O     1 
ATOM   10711 C  CB    . ARG A 1 2811 ? 165.654 185.881 220.336 1.00 45.92  ? 2811 ARG A CB    1 
ATOM   10712 C  CG    . ARG A 1 2811 ? 164.714 187.077 220.379 1.00 43.47  ? 2811 ARG A CG    1 
ATOM   10713 C  CD    . ARG A 1 2811 ? 163.614 186.909 219.345 1.00 43.86  ? 2811 ARG A CD    1 
ATOM   10714 N  NE    . ARG A 1 2811 ? 164.126 186.282 218.122 1.00 47.33  ? 2811 ARG A NE    1 
ATOM   10715 C  CZ    . ARG A 1 2811 ? 164.105 186.836 216.917 1.00 54.53  ? 2811 ARG A CZ    1 
ATOM   10716 N  NH1   . ARG A 1 2811 ? 163.618 188.053 216.757 1.00 54.09  ? 2811 ARG A NH1   1 
ATOM   10717 N  NH2   . ARG A 1 2811 ? 164.575 186.171 215.877 1.00 51.71  ? 2811 ARG A NH2   1 
ATOM   10718 N  N     . PRO A 1 2812 ? 165.617 184.246 222.996 1.00 43.34  ? 2812 PRO A N     1 
ATOM   10719 C  CA    . PRO A 1 2812 ? 165.011 183.880 224.269 1.00 46.15  ? 2812 PRO A CA    1 
ATOM   10720 C  C     . PRO A 1 2812 ? 166.049 183.684 225.364 1.00 47.16  ? 2812 PRO A C     1 
ATOM   10721 O  O     . PRO A 1 2812 ? 165.779 184.046 226.526 1.00 51.75  ? 2812 PRO A O     1 
ATOM   10722 C  CB    . PRO A 1 2812 ? 164.281 182.575 223.921 1.00 46.46  ? 2812 PRO A CB    1 
ATOM   10723 C  CG    . PRO A 1 2812 ? 165.130 181.968 222.830 1.00 45.67  ? 2812 PRO A CG    1 
ATOM   10724 C  CD    . PRO A 1 2812 ? 165.580 183.168 222.015 1.00 43.29  ? 2812 PRO A CD    1 
ATOM   10725 N  N     . LEU A 1 2813 ? 167.209 183.125 225.009 1.00 45.97  ? 2813 LEU A N     1 
ATOM   10726 C  CA    . LEU A 1 2813 ? 168.254 182.830 226.025 1.00 48.12  ? 2813 LEU A CA    1 
ATOM   10727 C  C     . LEU A 1 2813 ? 168.552 184.098 226.837 1.00 57.85  ? 2813 LEU A C     1 
ATOM   10728 O  O     . LEU A 1 2813 ? 168.939 185.116 226.222 1.00 63.29  ? 2813 LEU A O     1 
ATOM   10729 C  CB    . LEU A 1 2813 ? 169.507 182.306 225.326 1.00 43.36  ? 2813 LEU A CB    1 
ATOM   10730 C  CG    . LEU A 1 2813 ? 169.309 181.082 224.428 1.00 44.80  ? 2813 LEU A CG    1 
ATOM   10731 C  CD1   . LEU A 1 2813 ? 170.632 180.610 223.851 1.00 39.79  ? 2813 LEU A CD1   1 
ATOM   10732 C  CD2   . LEU A 1 2813 ? 168.619 179.960 225.182 1.00 46.05  ? 2813 LEU A CD2   1 
ATOM   10733 N  N     . GLU A 1 2814 ? 168.377 184.036 228.160 1.00 60.13  ? 2814 GLU A N     1 
ATOM   10734 C  CA    . GLU A 1 2814 ? 168.701 185.196 229.031 1.00 66.83  ? 2814 GLU A CA    1 
ATOM   10735 C  C     . GLU A 1 2814 ? 170.226 185.367 229.084 1.00 67.01  ? 2814 GLU A C     1 
ATOM   10736 O  O     . GLU A 1 2814 ? 170.701 186.511 228.913 1.00 69.70  ? 2814 GLU A O     1 
ATOM   10737 C  CB    . GLU A 1 2814 ? 168.133 184.986 230.435 1.00 66.36  ? 2814 GLU A CB    1 
ATOM   10738 C  CG    . GLU A 1 2814 ? 168.631 186.017 231.445 1.00 66.94  ? 2814 GLU A CG    1 
ATOM   10739 C  CD    . GLU A 1 2814 ? 168.219 187.451 231.162 1.00 72.64  ? 2814 GLU A CD    1 
ATOM   10740 O  OE1   . GLU A 1 2814 ? 167.495 187.686 230.172 1.00 73.80  ? 2814 GLU A OE1   1 
ATOM   10741 O  OE2   . GLU A 1 2814 ? 168.629 188.339 231.938 1.00 72.00  ? 2814 GLU A OE2   1 
ATOM   10742 N  N     . THR A 1 2815 ? 170.954 184.269 229.304 1.00 62.15  ? 2815 THR A N     1 
ATOM   10743 C  CA    . THR A 1 2815 ? 172.431 184.324 229.350 1.00 62.76  ? 2815 THR A CA    1 
ATOM   10744 C  C     . THR A 1 2815 ? 172.983 183.028 228.797 1.00 61.93  ? 2815 THR A C     1 
ATOM   10745 O  O     . THR A 1 2815 ? 172.276 182.000 228.886 1.00 63.24  ? 2815 THR A O     1 
ATOM   10746 C  CB    . THR A 1 2815 ? 172.891 184.573 230.785 1.00 65.27  ? 2815 THR A CB    1 
ATOM   10747 O  OG1   . THR A 1 2815 ? 174.313 184.522 230.730 1.00 64.24  ? 2815 THR A OG1   1 
ATOM   10748 C  CG2   . THR A 1 2815 ? 172.369 183.526 231.753 1.00 58.88  ? 2815 THR A CG2   1 
ATOM   10749 N  N     . LEU A 1 2816 ? 174.195 183.067 228.238 1.00 57.84  ? 2816 LEU A N     1 
ATOM   10750 C  CA    . LEU A 1 2816 ? 174.803 181.853 227.634 1.00 48.82  ? 2816 LEU A CA    1 
ATOM   10751 C  C     . LEU A 1 2816 ? 176.327 181.903 227.806 1.00 48.46  ? 2816 LEU A C     1 
ATOM   10752 O  O     . LEU A 1 2816 ? 176.928 182.942 227.457 1.00 48.36  ? 2816 LEU A O     1 
ATOM   10753 C  CB    . LEU A 1 2816 ? 174.411 181.771 226.160 1.00 46.77  ? 2816 LEU A CB    1 
ATOM   10754 C  CG    . LEU A 1 2816 ? 174.982 180.585 225.378 1.00 48.42  ? 2816 LEU A CG    1 
ATOM   10755 C  CD1   . LEU A 1 2816 ? 174.429 179.276 225.912 1.00 53.51  ? 2816 LEU A CD1   1 
ATOM   10756 C  CD2   . LEU A 1 2816 ? 174.679 180.729 223.898 1.00 39.96  ? 2816 LEU A CD2   1 
ATOM   10757 N  N     . PRO A 1 2817 ? 176.978 180.836 228.317 1.00 49.27  ? 2817 PRO A N     1 
ATOM   10758 C  CA    . PRO A 1 2817 ? 178.429 180.815 228.414 1.00 47.37  ? 2817 PRO A CA    1 
ATOM   10759 C  C     . PRO A 1 2817 ? 179.000 180.751 227.010 1.00 46.09  ? 2817 PRO A C     1 
ATOM   10760 O  O     . PRO A 1 2817 ? 178.299 180.286 226.087 1.00 45.56  ? 2817 PRO A O     1 
ATOM   10761 C  CB    . PRO A 1 2817 ? 178.707 179.541 229.215 1.00 42.70  ? 2817 PRO A CB    1 
ATOM   10762 C  CG    . PRO A 1 2817 ? 177.517 178.659 228.911 1.00 45.60  ? 2817 PRO A CG    1 
ATOM   10763 C  CD    . PRO A 1 2817 ? 176.346 179.623 228.809 1.00 47.06  ? 2817 PRO A CD    1 
ATOM   10764 N  N     . VAL A 1 2818 ? 180.244 181.205 226.841 1.00 42.85  ? 2818 VAL A N     1 
ATOM   10765 C  CA    . VAL A 1 2818 ? 180.847 181.214 225.512 1.00 42.45  ? 2818 VAL A CA    1 
ATOM   10766 C  C     . VAL A 1 2818 ? 180.748 179.846 224.848 1.00 41.27  ? 2818 VAL A C     1 
ATOM   10767 O  O     . VAL A 1 2818 ? 180.648 179.756 223.618 1.00 40.75  ? 2818 VAL A O     1 
ATOM   10768 C  CB    . VAL A 1 2818 ? 182.305 181.718 225.585 1.00 42.13  ? 2818 VAL A CB    1 
ATOM   10769 C  CG1   . VAL A 1 2818 ? 183.246 180.627 226.077 1.00 46.39  ? 2818 VAL A CG1   1 
ATOM   10770 C  CG2   . VAL A 1 2818 ? 182.753 182.228 224.223 1.00 39.48  ? 2818 VAL A CG2   1 
ATOM   10771 N  N     . GLU A 1 2819 ? 180.759 178.766 225.635 1.00 40.63  ? 2819 GLU A N     1 
ATOM   10772 C  CA    . GLU A 1 2819 ? 180.695 177.427 225.053 1.00 44.48  ? 2819 GLU A CA    1 
ATOM   10773 C  C     . GLU A 1 2819 ? 179.380 177.202 224.319 1.00 42.07  ? 2819 GLU A C     1 
ATOM   10774 O  O     . GLU A 1 2819 ? 179.354 176.572 223.255 1.00 41.35  ? 2819 GLU A O     1 
ATOM   10775 C  CB    . GLU A 1 2819 ? 180.895 176.372 226.141 1.00 53.36  ? 2819 GLU A CB    1 
ATOM   10776 C  CG    . GLU A 1 2819 ? 182.353 176.100 226.470 1.00 54.17  ? 2819 GLU A CG    1 
ATOM   10777 C  CD    . GLU A 1 2819 ? 182.885 177.010 227.558 1.00 59.58  ? 2819 GLU A CD    1 
ATOM   10778 O  OE1   . GLU A 1 2819 ? 182.106 177.829 228.087 1.00 56.74  ? 2819 GLU A OE1   1 
ATOM   10779 O  OE2   . GLU A 1 2819 ? 184.087 176.911 227.879 1.00 61.05  ? 2819 GLU A OE2   1 
ATOM   10780 N  N     . GLY A 1 2820 ? 178.277 177.705 224.872 1.00 38.33  ? 2820 GLY A N     1 
ATOM   10781 C  CA    . GLY A 1 2820 ? 177.000 177.585 224.188 1.00 36.72  ? 2820 GLY A CA    1 
ATOM   10782 C  C     . GLY A 1 2820 ? 176.951 178.378 222.897 1.00 38.55  ? 2820 GLY A C     1 
ATOM   10783 O  O     . GLY A 1 2820 ? 176.307 177.965 221.929 1.00 39.52  ? 2820 GLY A O     1 
ATOM   10784 N  N     . LEU A 1 2821 ? 177.620 179.533 222.867 1.00 35.56  ? 2821 LEU A N     1 
ATOM   10785 C  CA    . LEU A 1 2821 ? 177.658 180.332 221.647 1.00 26.33  ? 2821 LEU A CA    1 
ATOM   10786 C  C     . LEU A 1 2821 ? 178.355 179.579 220.522 1.00 28.82  ? 2821 LEU A C     1 
ATOM   10787 O  O     . LEU A 1 2821 ? 177.910 179.618 219.369 1.00 27.27  ? 2821 LEU A O     1 
ATOM   10788 C  CB    . LEU A 1 2821 ? 178.352 181.668 221.913 1.00 29.98  ? 2821 LEU A CB    1 
ATOM   10789 C  CG    . LEU A 1 2821 ? 178.545 182.588 220.706 1.00 29.54  ? 2821 LEU A CG    1 
ATOM   10790 C  CD1   . LEU A 1 2821 ? 177.237 183.260 220.326 1.00 28.88  ? 2821 LEU A CD1   1 
ATOM   10791 C  CD2   . LEU A 1 2821 ? 179.623 183.625 220.976 1.00 32.74  ? 2821 LEU A CD2   1 
ATOM   10792 N  N     . ILE A 1 2822 ? 179.448 178.882 220.838 1.00 29.07  ? 2822 ILE A N     1 
ATOM   10793 C  CA    . ILE A 1 2822 ? 180.145 178.096 219.825 1.00 27.28  ? 2822 ILE A CA    1 
ATOM   10794 C  C     . ILE A 1 2822 ? 179.286 176.922 219.374 1.00 27.95  ? 2822 ILE A C     1 
ATOM   10795 O  O     . ILE A 1 2822 ? 179.285 176.555 218.193 1.00 28.05  ? 2822 ILE A O     1 
ATOM   10796 C  CB    . ILE A 1 2822 ? 181.514 177.625 220.351 1.00 28.58  ? 2822 ILE A CB    1 
ATOM   10797 C  CG1   . ILE A 1 2822 ? 182.224 178.754 221.099 1.00 30.80  ? 2822 ILE A CG1   1 
ATOM   10798 C  CG2   . ILE A 1 2822 ? 182.379 177.117 219.209 1.00 31.04  ? 2822 ILE A CG2   1 
ATOM   10799 C  CD1   . ILE A 1 2822 ? 182.397 180.014 220.285 1.00 32.39  ? 2822 ILE A CD1   1 
ATOM   10800 N  N     . ARG A 1 2823 ? 178.549 176.309 220.305 1.00 31.05  ? 2823 ARG A N     1 
ATOM   10801 C  CA    . ARG A 1 2823 ? 177.681 175.193 219.943 1.00 27.52  ? 2823 ARG A CA    1 
ATOM   10802 C  C     . ARG A 1 2823 ? 176.589 175.634 218.976 1.00 24.66  ? 2823 ARG A C     1 
ATOM   10803 O  O     . ARG A 1 2823 ? 176.282 174.926 218.010 1.00 24.86  ? 2823 ARG A O     1 
ATOM   10804 C  CB    . ARG A 1 2823 ? 177.072 174.572 221.200 1.00 24.33  ? 2823 ARG A CB    1 
ATOM   10805 C  CG    . ARG A 1 2823 ? 176.475 173.195 220.973 1.00 27.40  ? 2823 ARG A CG    1 
ATOM   10806 C  CD    . ARG A 1 2823 ? 176.393 172.399 222.265 1.00 28.10  ? 2823 ARG A CD    1 
ATOM   10807 N  NE    . ARG A 1 2823 ? 175.821 171.075 222.050 1.00 32.12  ? 2823 ARG A NE    1 
ATOM   10808 C  CZ    . ARG A 1 2823 ? 176.485 170.044 221.546 1.00 38.04  ? 2823 ARG A CZ    1 
ATOM   10809 N  NH1   . ARG A 1 2823 ? 177.758 170.143 221.200 1.00 37.51  ? 2823 ARG A NH1   1 
ATOM   10810 N  NH2   . ARG A 1 2823 ? 175.855 168.883 221.384 1.00 36.13  ? 2823 ARG A NH2   1 
ATOM   10811 N  N     . ILE A 1 2824 ? 175.987 176.800 219.223 1.00 22.81  ? 2824 ILE A N     1 
ATOM   10812 C  CA    . ILE A 1 2824 ? 175.010 177.345 218.284 1.00 20.03  ? 2824 ILE A CA    1 
ATOM   10813 C  C     . ILE A 1 2824 ? 175.682 177.676 216.957 1.00 21.08  ? 2824 ILE A C     1 
ATOM   10814 O  O     . ILE A 1 2824 ? 175.146 177.390 215.879 1.00 21.83  ? 2824 ILE A O     1 
ATOM   10815 C  CB    . ILE A 1 2824 ? 174.317 178.578 218.893 1.00 16.01  ? 2824 ILE A CB    1 
ATOM   10816 C  CG1   . ILE A 1 2824 ? 173.157 178.154 219.791 1.00 24.89  ? 2824 ILE A CG1   1 
ATOM   10817 C  CG2   . ILE A 1 2824 ? 173.794 179.492 217.806 1.00 17.43  ? 2824 ILE A CG2   1 
ATOM   10818 C  CD1   . ILE A 1 2824 ? 172.793 179.181 220.839 1.00 35.34  ? 2824 ILE A CD1   1 
ATOM   10819 N  N     . TRP A 1 2825 ? 176.872 178.279 217.019 1.00 20.49  ? 2825 TRP A N     1 
ATOM   10820 C  CA    . TRP A 1 2825 ? 177.618 178.608 215.809 1.00 15.86  ? 2825 TRP A CA    1 
ATOM   10821 C  C     . TRP A 1 2825 ? 177.963 177.352 215.018 1.00 16.98  ? 2825 TRP A C     1 
ATOM   10822 O  O     . TRP A 1 2825 ? 177.853 177.327 213.787 1.00 18.49  ? 2825 TRP A O     1 
ATOM   10823 C  CB    . TRP A 1 2825 ? 178.881 179.386 216.184 1.00 16.70  ? 2825 TRP A CB    1 
ATOM   10824 C  CG    . TRP A 1 2825 ? 179.836 179.617 215.055 1.00 17.78  ? 2825 TRP A CG    1 
ATOM   10825 C  CD1   . TRP A 1 2825 ? 179.873 180.693 214.219 1.00 17.29  ? 2825 TRP A CD1   1 
ATOM   10826 C  CD2   . TRP A 1 2825 ? 180.913 178.762 214.655 1.00 16.61  ? 2825 TRP A CD2   1 
ATOM   10827 N  NE1   . TRP A 1 2825 ? 180.899 180.557 213.316 1.00 17.17  ? 2825 TRP A NE1   1 
ATOM   10828 C  CE2   . TRP A 1 2825 ? 181.551 179.379 213.561 1.00 16.75  ? 2825 TRP A CE2   1 
ATOM   10829 C  CE3   . TRP A 1 2825 ? 181.394 177.531 215.111 1.00 18.42  ? 2825 TRP A CE3   1 
ATOM   10830 C  CZ2   . TRP A 1 2825 ? 182.645 178.808 212.917 1.00 24.41  ? 2825 TRP A CZ2   1 
ATOM   10831 C  CZ3   . TRP A 1 2825 ? 182.478 176.967 214.471 1.00 19.20  ? 2825 TRP A CZ3   1 
ATOM   10832 C  CH2   . TRP A 1 2825 ? 183.093 177.604 213.386 1.00 25.60  ? 2825 TRP A CH2   1 
ATOM   10833 N  N     . ALA A 1 2826 ? 178.389 176.295 215.713 1.00 19.87  ? 2826 ALA A N     1 
ATOM   10834 C  CA    . ALA A 1 2826 ? 178.693 175.041 215.032 1.00 16.38  ? 2826 ALA A CA    1 
ATOM   10835 C  C     . ALA A 1 2826 ? 177.432 174.400 214.467 1.00 17.86  ? 2826 ALA A C     1 
ATOM   10836 O  O     . ALA A 1 2826 ? 177.461 173.812 213.380 1.00 23.03  ? 2826 ALA A O     1 
ATOM   10837 C  CB    . ALA A 1 2826 ? 179.402 174.083 215.988 1.00 26.35  ? 2826 ALA A CB    1 
ATOM   10838 N  N     . HIS A 1 2827 ? 176.316 174.497 215.194 1.00 15.51  ? 2827 HIS A N     1 
ATOM   10839 C  CA    . HIS A 1 2827 ? 175.081 173.864 214.744 1.00 16.31  ? 2827 HIS A CA    1 
ATOM   10840 C  C     . HIS A 1 2827 ? 174.567 174.497 213.459 1.00 16.24  ? 2827 HIS A C     1 
ATOM   10841 O  O     . HIS A 1 2827 ? 174.220 173.790 212.506 1.00 16.26  ? 2827 HIS A O     1 
ATOM   10842 C  CB    . HIS A 1 2827 ? 174.016 173.952 215.836 1.00 18.10  ? 2827 HIS A CB    1 
ATOM   10843 C  CG    . HIS A 1 2827 ? 172.691 173.384 215.433 1.00 15.34  ? 2827 HIS A CG    1 
ATOM   10844 N  ND1   . HIS A 1 2827 ? 171.608 174.174 215.112 1.00 16.26  ? 2827 HIS A ND1   1 
ATOM   10845 C  CD2   . HIS A 1 2827 ? 172.275 172.103 215.296 1.00 18.63  ? 2827 HIS A CD2   1 
ATOM   10846 C  CE1   . HIS A 1 2827 ? 170.582 173.404 214.797 1.00 18.98  ? 2827 HIS A CE1   1 
ATOM   10847 N  NE2   . HIS A 1 2827 ? 170.960 172.143 214.901 1.00 16.33  ? 2827 HIS A NE2   1 
ATOM   10848 N  N     . GLU A 1 2828 ? 174.505 175.830 213.416 1.00 15.65  ? 2828 GLU A N     1 
ATOM   10849 C  CA    . GLU A 1 2828 ? 173.986 176.512 212.236 1.00 13.50  ? 2828 GLU A CA    1 
ATOM   10850 C  C     . GLU A 1 2828 ? 174.862 176.255 211.019 1.00 13.38  ? 2828 GLU A C     1 
ATOM   10851 O  O     . GLU A 1 2828 ? 174.356 176.124 209.898 1.00 19.89  ? 2828 GLU A O     1 
ATOM   10852 C  CB    . GLU A 1 2828 ? 173.866 178.011 212.508 1.00 18.50  ? 2828 GLU A CB    1 
ATOM   10853 C  CG    . GLU A 1 2828 ? 172.790 178.371 213.519 1.00 17.80  ? 2828 GLU A CG    1 
ATOM   10854 C  CD    . GLU A 1 2828 ? 171.397 178.000 213.046 1.00 24.89  ? 2828 GLU A CD    1 
ATOM   10855 O  OE1   . GLU A 1 2828 ? 171.152 178.034 211.822 1.00 29.48  ? 2828 GLU A OE1   1 
ATOM   10856 O  OE2   . GLU A 1 2828 ? 170.546 177.672 213.898 1.00 26.26  ? 2828 GLU A OE2   1 
ATOM   10857 N  N     . ALA A 1 2829 ? 176.179 176.186 211.218 1.00 12.31  ? 2829 ALA A N     1 
ATOM   10858 C  CA    . ALA A 1 2829 ? 177.080 175.879 210.113 1.00 14.21  ? 2829 ALA A CA    1 
ATOM   10859 C  C     . ALA A 1 2829 ? 176.823 174.484 209.560 1.00 16.69  ? 2829 ALA A C     1 
ATOM   10860 O  O     . ALA A 1 2829 ? 176.842 174.278 208.341 1.00 18.08  ? 2829 ALA A O     1 
ATOM   10861 C  CB    . ALA A 1 2829 ? 178.528 176.011 210.569 1.00 15.89  ? 2829 ALA A CB    1 
ATOM   10862 N  N     . LEU A 1 2830 ? 176.591 173.511 210.444 1.00 15.11  ? 2830 LEU A N     1 
ATOM   10863 C  CA    . LEU A 1 2830 ? 176.259 172.166 209.989 1.00 13.30  ? 2830 LEU A CA    1 
ATOM   10864 C  C     . LEU A 1 2830 ? 174.950 172.160 209.211 1.00 15.46  ? 2830 LEU A C     1 
ATOM   10865 O  O     . LEU A 1 2830 ? 174.777 171.373 208.274 1.00 18.98  ? 2830 LEU A O     1 
ATOM   10866 C  CB    . LEU A 1 2830 ? 176.179 171.213 211.181 1.00 18.19  ? 2830 LEU A CB    1 
ATOM   10867 C  CG    . LEU A 1 2830 ? 177.482 170.901 211.920 1.00 17.74  ? 2830 LEU A CG    1 
ATOM   10868 C  CD1   . LEU A 1 2830 ? 177.194 170.156 213.213 1.00 16.77  ? 2830 LEU A CD1   1 
ATOM   10869 C  CD2   . LEU A 1 2830 ? 178.427 170.100 211.038 1.00 17.90  ? 2830 LEU A CD2   1 
ATOM   10870 N  N     . ARG A 1 2831 ? 174.012 173.031 209.589 1.00 15.68  ? 2831 ARG A N     1 
ATOM   10871 C  CA    . ARG A 1 2831 ? 172.736 173.094 208.888 1.00 13.63  ? 2831 ARG A CA    1 
ATOM   10872 C  C     . ARG A 1 2831 ? 172.864 173.793 207.541 1.00 14.68  ? 2831 ARG A C     1 
ATOM   10873 O  O     . ARG A 1 2831 ? 172.088 173.510 206.622 1.00 16.88  ? 2831 ARG A O     1 
ATOM   10874 C  CB    . ARG A 1 2831 ? 171.696 173.804 209.755 1.00 15.07  ? 2831 ARG A CB    1 
ATOM   10875 C  CG    . ARG A 1 2831 ? 171.384 173.107 211.074 1.00 15.55  ? 2831 ARG A CG    1 
ATOM   10876 C  CD    . ARG A 1 2831 ? 170.533 171.857 210.886 1.00 14.83  ? 2831 ARG A CD    1 
ATOM   10877 N  NE    . ARG A 1 2831 ? 171.322 170.694 210.494 1.00 17.75  ? 2831 ARG A NE    1 
ATOM   10878 C  CZ    . ARG A 1 2831 ? 172.158 170.047 211.294 1.00 18.84  ? 2831 ARG A CZ    1 
ATOM   10879 N  NH1   . ARG A 1 2831 ? 172.334 170.411 212.554 1.00 16.00  ? 2831 ARG A NH1   1 
ATOM   10880 N  NH2   . ARG A 1 2831 ? 172.835 169.005 210.818 1.00 19.87  ? 2831 ARG A NH2   1 
ATOM   10881 N  N     . LEU A 1 2832 ? 173.828 174.703 207.404 1.00 15.28  ? 2832 LEU A N     1 
ATOM   10882 C  CA    . LEU A 1 2832 ? 173.939 175.523 206.204 1.00 12.73  ? 2832 LEU A CA    1 
ATOM   10883 C  C     . LEU A 1 2832 ? 174.969 174.997 205.213 1.00 17.27  ? 2832 LEU A C     1 
ATOM   10884 O  O     . LEU A 1 2832 ? 174.822 175.207 204.004 1.00 30.85  ? 2832 LEU A O     1 
ATOM   10885 C  CB    . LEU A 1 2832 ? 174.291 176.962 206.582 1.00 13.36  ? 2832 LEU A CB    1 
ATOM   10886 C  CG    . LEU A 1 2832 ? 173.200 177.762 207.290 1.00 16.23  ? 2832 LEU A CG    1 
ATOM   10887 C  CD1   . LEU A 1 2832 ? 173.765 179.078 207.778 1.00 13.10  ? 2832 LEU A CD1   1 
ATOM   10888 C  CD2   . LEU A 1 2832 ? 172.013 177.991 206.370 1.00 22.47  ? 2832 LEU A CD2   1 
ATOM   10889 N  N     . PHE A 1 2833 ? 176.011 174.320 205.692 1.00 14.76  ? 2833 PHE A N     1 
ATOM   10890 C  CA    . PHE A 1 2833 ? 177.110 173.908 204.831 1.00 15.71  ? 2833 PHE A CA    1 
ATOM   10891 C  C     . PHE A 1 2833 ? 177.233 172.398 204.684 1.00 19.31  ? 2833 PHE A C     1 
ATOM   10892 O  O     . PHE A 1 2833 ? 177.920 171.938 203.766 1.00 26.09  ? 2833 PHE A O     1 
ATOM   10893 C  CB    . PHE A 1 2833 ? 178.433 174.474 205.361 1.00 19.99  ? 2833 PHE A CB    1 
ATOM   10894 C  CG    . PHE A 1 2833 ? 178.472 175.974 205.406 1.00 17.72  ? 2833 PHE A CG    1 
ATOM   10895 C  CD1   . PHE A 1 2833 ? 178.011 176.660 206.517 1.00 20.07  ? 2833 PHE A CD1   1 
ATOM   10896 C  CD2   . PHE A 1 2833 ? 178.959 176.698 204.333 1.00 18.01  ? 2833 PHE A CD2   1 
ATOM   10897 C  CE1   . PHE A 1 2833 ? 178.043 178.038 206.559 1.00 17.40  ? 2833 PHE A CE1   1 
ATOM   10898 C  CE2   . PHE A 1 2833 ? 178.994 178.076 204.369 1.00 20.11  ? 2833 PHE A CE2   1 
ATOM   10899 C  CZ    . PHE A 1 2833 ? 178.535 178.747 205.484 1.00 18.73  ? 2833 PHE A CZ    1 
ATOM   10900 N  N     . GLN A 1 2834 ? 176.589 171.619 205.552 1.00 20.97  ? 2834 GLN A N     1 
ATOM   10901 C  CA    . GLN A 1 2834 ? 176.707 170.170 205.512 1.00 18.36  ? 2834 GLN A CA    1 
ATOM   10902 C  C     . GLN A 1 2834 ? 175.441 169.460 205.057 1.00 17.34  ? 2834 GLN A C     1 
ATOM   10903 O  O     . GLN A 1 2834 ? 175.535 168.346 204.533 1.00 21.72  ? 2834 GLN A O     1 
ATOM   10904 C  CB    . GLN A 1 2834 ? 177.106 169.634 206.895 1.00 19.47  ? 2834 GLN A CB    1 
ATOM   10905 C  CG    . GLN A 1 2834 ? 177.674 168.229 206.880 1.00 25.08  ? 2834 GLN A CG    1 
ATOM   10906 C  CD    . GLN A 1 2834 ? 177.894 167.679 208.272 1.00 29.68  ? 2834 GLN A CD    1 
ATOM   10907 O  OE1   . GLN A 1 2834 ? 176.987 167.680 209.104 1.00 29.32  ? 2834 GLN A OE1   1 
ATOM   10908 N  NE2   . GLN A 1 2834 ? 179.105 167.205 208.535 1.00 37.15  ? 2834 GLN A NE2   1 
ATOM   10909 N  N     . ASP A 1 2835 ? 174.269 170.074 205.236 1.00 17.27  ? 2835 ASP A N     1 
ATOM   10910 C  CA    . ASP A 1 2835 ? 173.018 169.400 204.902 1.00 17.89  ? 2835 ASP A CA    1 
ATOM   10911 C  C     . ASP A 1 2835 ? 172.890 169.146 203.406 1.00 17.76  ? 2835 ASP A C     1 
ATOM   10912 O  O     . ASP A 1 2835 ? 172.193 168.211 202.994 1.00 20.66  ? 2835 ASP A O     1 
ATOM   10913 C  CB    . ASP A 1 2835 ? 171.832 170.226 205.400 1.00 21.65  ? 2835 ASP A CB    1 
ATOM   10914 C  CG    . ASP A 1 2835 ? 171.594 170.064 206.888 1.00 24.94  ? 2835 ASP A CG    1 
ATOM   10915 O  OD1   . ASP A 1 2835 ? 172.427 169.420 207.558 1.00 22.48  ? 2835 ASP A OD1   1 
ATOM   10916 O  OD2   . ASP A 1 2835 ? 170.575 170.585 207.387 1.00 22.66  ? 2835 ASP A OD2   1 
ATOM   10917 N  N     . ARG A 1 2836 ? 173.547 169.957 202.580 1.00 18.56  ? 2836 ARG A N     1 
ATOM   10918 C  CA    . ARG A 1 2836 ? 173.449 169.834 201.132 1.00 17.08  ? 2836 ARG A CA    1 
ATOM   10919 C  C     . ARG A 1 2836 ? 174.519 168.934 200.529 1.00 16.69  ? 2836 ARG A C     1 
ATOM   10920 O  O     . ARG A 1 2836 ? 174.511 168.723 199.311 1.00 19.44  ? 2836 ARG A O     1 
ATOM   10921 C  CB    . ARG A 1 2836 ? 173.528 171.219 200.482 1.00 19.85  ? 2836 ARG A CB    1 
ATOM   10922 C  CG    . ARG A 1 2836 ? 174.934 171.788 200.408 1.00 23.18  ? 2836 ARG A CG    1 
ATOM   10923 C  CD    . ARG A 1 2836 ? 174.946 173.138 199.715 1.00 26.14  ? 2836 ARG A CD    1 
ATOM   10924 N  NE    . ARG A 1 2836 ? 174.348 174.180 200.540 1.00 28.38  ? 2836 ARG A NE    1 
ATOM   10925 C  CZ    . ARG A 1 2836 ? 173.980 175.371 200.089 1.00 26.33  ? 2836 ARG A CZ    1 
ATOM   10926 N  NH1   . ARG A 1 2836 ? 174.137 175.708 198.819 1.00 25.22  ? 2836 ARG A NH1   1 
ATOM   10927 N  NH2   . ARG A 1 2836 ? 173.443 176.247 200.933 1.00 28.03  ? 2836 ARG A NH2   1 
ATOM   10928 N  N     . LEU A 1 2837 ? 175.428 168.400 201.338 1.00 21.09  ? 2837 LEU A N     1 
ATOM   10929 C  CA    . LEU A 1 2837 ? 176.528 167.607 200.808 1.00 20.24  ? 2837 LEU A CA    1 
ATOM   10930 C  C     . LEU A 1 2837 ? 176.052 166.226 200.376 1.00 21.60  ? 2837 LEU A C     1 
ATOM   10931 O  O     . LEU A 1 2837 ? 175.108 165.669 200.941 1.00 27.00  ? 2837 LEU A O     1 
ATOM   10932 C  CB    . LEU A 1 2837 ? 177.634 167.485 201.851 1.00 20.79  ? 2837 LEU A CB    1 
ATOM   10933 C  CG    . LEU A 1 2837 ? 178.321 168.812 202.168 1.00 19.92  ? 2837 LEU A CG    1 
ATOM   10934 C  CD1   . LEU A 1 2837 ? 179.423 168.609 203.178 1.00 24.79  ? 2837 LEU A CD1   1 
ATOM   10935 C  CD2   . LEU A 1 2837 ? 178.867 169.446 200.898 1.00 19.53  ? 2837 LEU A CD2   1 
ATOM   10936 N  N     . VAL A 1 2838 ? 176.719 165.676 199.365 1.00 24.36  ? 2838 VAL A N     1 
ATOM   10937 C  CA    . VAL A 1 2838 ? 176.325 164.393 198.789 1.00 25.29  ? 2838 VAL A CA    1 
ATOM   10938 C  C     . VAL A 1 2838 ? 177.197 163.256 199.307 1.00 33.09  ? 2838 VAL A C     1 
ATOM   10939 O  O     . VAL A 1 2838 ? 176.689 162.239 199.787 1.00 39.99  ? 2838 VAL A O     1 
ATOM   10940 C  CB    . VAL A 1 2838 ? 176.367 164.475 197.248 1.00 21.99  ? 2838 VAL A CB    1 
ATOM   10941 C  CG1   . VAL A 1 2838 ? 176.062 163.118 196.634 1.00 26.24  ? 2838 VAL A CG1   1 
ATOM   10942 C  CG2   . VAL A 1 2838 ? 175.395 165.528 196.747 1.00 20.46  ? 2838 VAL A CG2   1 
ATOM   10943 N  N     . GLU A 1 2839 ? 178.517 163.452 199.252 1.00 36.48  ? 2839 GLU A N     1 
ATOM   10944 C  CA    . GLU A 1 2839 ? 179.461 162.389 199.688 1.00 37.99  ? 2839 GLU A CA    1 
ATOM   10945 C  C     . GLU A 1 2839 ? 179.777 162.552 201.183 1.00 39.09  ? 2839 GLU A C     1 
ATOM   10946 O  O     . GLU A 1 2839 ? 179.740 163.701 201.676 1.00 33.77  ? 2839 GLU A O     1 
ATOM   10947 C  CB    . GLU A 1 2839 ? 180.734 162.453 198.845 1.00 40.22  ? 2839 GLU A CB    1 
ATOM   10948 C  CG    . GLU A 1 2839 ? 180.462 162.706 197.365 1.00 40.68  ? 2839 GLU A CG    1 
ATOM   10949 C  CD    . GLU A 1 2839 ? 179.634 161.649 196.655 1.00 50.87  ? 2839 GLU A CD    1 
ATOM   10950 O  OE1   . GLU A 1 2839 ? 179.261 160.642 197.294 1.00 54.45  ? 2839 GLU A OE1   1 
ATOM   10951 O  OE2   . GLU A 1 2839 ? 179.358 161.838 195.452 1.00 52.10  ? 2839 GLU A OE2   1 
ATOM   10952 N  N     . ASP A 1 2840 ? 180.074 161.443 201.868 1.00 43.38  ? 2840 ASP A N     1 
ATOM   10953 C  CA    . ASP A 1 2840 ? 180.403 161.485 203.320 1.00 39.47  ? 2840 ASP A CA    1 
ATOM   10954 C  C     . ASP A 1 2840 ? 181.740 162.206 203.518 1.00 39.46  ? 2840 ASP A C     1 
ATOM   10955 O  O     . ASP A 1 2840 ? 181.903 162.876 204.559 1.00 30.45  ? 2840 ASP A O     1 
ATOM   10956 C  CB    . ASP A 1 2840 ? 180.415 160.090 203.923 1.00 44.54  ? 2840 ASP A CB    1 
ATOM   10957 C  CG    . ASP A 1 2840 ? 179.137 159.287 203.732 1.00 58.04  ? 2840 ASP A CG    1 
ATOM   10958 O  OD1   . ASP A 1 2840 ? 179.090 158.136 204.213 1.00 64.92  ? 2840 ASP A OD1   1 
ATOM   10959 O  OD2   . ASP A 1 2840 ? 178.199 159.820 203.102 1.00 52.08  ? 2840 ASP A OD2   1 
ATOM   10960 N  N     . GLU A 1 2841 ? 182.659 162.063 202.559 1.00 39.91  ? 2841 GLU A N     1 
ATOM   10961 C  CA    . GLU A 1 2841 ? 183.988 162.719 202.661 1.00 41.77  ? 2841 GLU A CA    1 
ATOM   10962 C  C     . GLU A 1 2841 ? 183.780 164.230 202.827 1.00 36.69  ? 2841 GLU A C     1 
ATOM   10963 O  O     . GLU A 1 2841 ? 184.446 164.828 203.701 1.00 34.46  ? 2841 GLU A O     1 
ATOM   10964 C  CB    . GLU A 1 2841 ? 184.807 162.412 201.409 1.00 46.51  ? 2841 GLU A CB    1 
ATOM   10965 C  CG    . GLU A 1 2841 ? 184.679 160.963 200.949 1.00 58.85  ? 2841 GLU A CG    1 
ATOM   10966 C  CD    . GLU A 1 2841 ? 185.125 159.937 201.975 1.00 71.68  ? 2841 GLU A CD    1 
ATOM   10967 O  OE1   . GLU A 1 2841 ? 186.312 159.963 202.360 1.00 70.27  ? 2841 GLU A OE1   1 
ATOM   10968 O  OE2   . GLU A 1 2841 ? 184.284 159.112 202.391 1.00 69.13  ? 2841 GLU A OE2   1 
ATOM   10969 N  N     . GLU A 1 2842 ? 182.880 164.813 202.029 1.00 33.17  ? 2842 GLU A N     1 
ATOM   10970 C  CA    . GLU A 1 2842 ? 182.590 166.266 202.118 1.00 28.15  ? 2842 GLU A CA    1 
ATOM   10971 C  C     . GLU A 1 2842 ? 182.053 166.593 203.516 1.00 27.45  ? 2842 GLU A C     1 
ATOM   10972 O  O     . GLU A 1 2842 ? 182.522 167.585 204.116 1.00 29.80  ? 2842 GLU A O     1 
ATOM   10973 C  CB    . GLU A 1 2842 ? 181.533 166.639 201.081 1.00 29.57  ? 2842 GLU A CB    1 
ATOM   10974 C  CG    . GLU A 1 2842 ? 181.916 166.269 199.652 1.00 33.69  ? 2842 GLU A CG    1 
ATOM   10975 C  CD    . GLU A 1 2842 ? 180.703 166.087 198.758 1.00 37.32  ? 2842 GLU A CD    1 
ATOM   10976 O  OE1   . GLU A 1 2842 ? 179.573 166.166 199.284 1.00 34.39  ? 2842 GLU A OE1   1 
ATOM   10977 O  OE2   . GLU A 1 2842 ? 180.885 165.876 197.541 1.00 39.16  ? 2842 GLU A OE2   1 
ATOM   10978 N  N     . ARG A 1 2843 ? 181.104 165.792 204.008 1.00 28.08  ? 2843 ARG A N     1 
ATOM   10979 C  CA    . ARG A 1 2843 ? 180.485 166.055 205.334 1.00 26.10  ? 2843 ARG A CA    1 
ATOM   10980 C  C     . ARG A 1 2843 ? 181.564 165.947 206.421 1.00 30.57  ? 2843 ARG A C     1 
ATOM   10981 O  O     . ARG A 1 2843 ? 181.571 166.799 207.335 1.00 31.38  ? 2843 ARG A O     1 
ATOM   10982 C  CB    . ARG A 1 2843 ? 179.328 165.076 205.555 1.00 26.37  ? 2843 ARG A CB    1 
ATOM   10983 C  CG    . ARG A 1 2843 ? 178.310 165.120 204.426 1.00 23.36  ? 2843 ARG A CG    1 
ATOM   10984 C  CD    . ARG A 1 2843 ? 177.246 164.045 204.561 1.00 29.64  ? 2843 ARG A CD    1 
ATOM   10985 N  NE    . ARG A 1 2843 ? 176.267 164.103 203.470 1.00 37.41  ? 2843 ARG A NE    1 
ATOM   10986 C  CZ    . ARG A 1 2843 ? 176.049 163.120 202.607 1.00 40.99  ? 2843 ARG A CZ    1 
ATOM   10987 N  NH1   . ARG A 1 2843 ? 176.879 162.094 202.551 1.00 41.63  ? 2843 ARG A NH1   1 
ATOM   10988 N  NH2   . ARG A 1 2843 ? 175.004 163.167 201.801 1.00 36.67  ? 2843 ARG A NH2   1 
ATOM   10989 N  N     . ARG A 1 2844 ? 182.441 164.946 206.314 1.00 33.98  ? 2844 ARG A N     1 
ATOM   10990 C  CA    . ARG A 1 2844 ? 183.544 164.784 207.295 1.00 30.89  ? 2844 ARG A CA    1 
ATOM   10991 C  C     . ARG A 1 2844 ? 184.430 166.036 207.249 1.00 32.48  ? 2844 ARG A C     1 
ATOM   10992 O  O     . ARG A 1 2844 ? 184.817 166.531 208.330 1.00 37.46  ? 2844 ARG A O     1 
ATOM   10993 C  CB    . ARG A 1 2844 ? 184.356 163.528 206.970 1.00 31.54  ? 2844 ARG A CB    1 
ATOM   10994 C  CG    . ARG A 1 2844 ? 185.560 163.308 207.874 1.00 34.32  ? 2844 ARG A CG    1 
ATOM   10995 C  CD    . ARG A 1 2844 ? 186.453 162.220 207.307 1.00 38.78  ? 2844 ARG A CD    1 
ATOM   10996 N  NE    . ARG A 1 2844 ? 186.909 162.570 205.958 1.00 44.69  ? 2844 ARG A NE    1 
ATOM   10997 C  CZ    . ARG A 1 2844 ? 186.621 161.880 204.863 1.00 42.94  ? 2844 ARG A CZ    1 
ATOM   10998 N  NH1   . ARG A 1 2844 ? 185.773 160.869 204.924 1.00 39.73  ? 2844 ARG A NH1   1 
ATOM   10999 N  NH2   . ARG A 1 2844 ? 187.178 162.207 203.711 1.00 42.67  ? 2844 ARG A NH2   1 
ATOM   11000 N  N     . TRP A 1 2845 ? 184.724 166.531 206.043 1.00 27.27  ? 2845 TRP A N     1 
ATOM   11001 C  CA    . TRP A 1 2845 ? 185.531 167.767 205.904 1.00 28.41  ? 2845 TRP A CA    1 
ATOM   11002 C  C     . TRP A 1 2845 ? 184.853 168.892 206.683 1.00 32.74  ? 2845 TRP A C     1 
ATOM   11003 O  O     . TRP A 1 2845 ? 185.534 169.569 207.478 1.00 35.36  ? 2845 TRP A O     1 
ATOM   11004 C  CB    . TRP A 1 2845 ? 185.674 168.142 204.423 1.00 29.03  ? 2845 TRP A CB    1 
ATOM   11005 C  CG    . TRP A 1 2845 ? 186.412 169.433 204.185 1.00 30.88  ? 2845 TRP A CG    1 
ATOM   11006 C  CD1   . TRP A 1 2845 ? 187.739 169.582 203.908 1.00 30.22  ? 2845 TRP A CD1   1 
ATOM   11007 C  CD2   . TRP A 1 2845 ? 185.858 170.767 204.220 1.00 29.65  ? 2845 TRP A CD2   1 
ATOM   11008 N  NE1   . TRP A 1 2845 ? 188.048 170.907 203.757 1.00 27.77  ? 2845 TRP A NE1   1 
ATOM   11009 C  CE2   . TRP A 1 2845 ? 186.918 171.658 203.945 1.00 29.50  ? 2845 TRP A CE2   1 
ATOM   11010 C  CE3   . TRP A 1 2845 ? 184.582 171.291 204.453 1.00 31.06  ? 2845 TRP A CE3   1 
ATOM   11011 C  CZ2   . TRP A 1 2845 ? 186.735 173.038 203.898 1.00 31.43  ? 2845 TRP A CZ2   1 
ATOM   11012 C  CZ3   . TRP A 1 2845 ? 184.405 172.656 204.409 1.00 30.41  ? 2845 TRP A CZ3   1 
ATOM   11013 C  CH2   . TRP A 1 2845 ? 185.467 173.516 204.135 1.00 29.35  ? 2845 TRP A CH2   1 
ATOM   11014 N  N     . THR A 1 2846 ? 183.545 169.065 206.482 1.00 33.48  ? 2846 THR A N     1 
ATOM   11015 C  CA    . THR A 1 2846 ? 182.810 170.151 207.164 1.00 29.20  ? 2846 THR A CA    1 
ATOM   11016 C  C     . THR A 1 2846 ? 182.952 169.975 208.660 1.00 32.78  ? 2846 THR A C     1 
ATOM   11017 O  O     . THR A 1 2846 ? 183.315 170.961 209.337 1.00 36.66  ? 2846 THR A O     1 
ATOM   11018 C  CB    . THR A 1 2846 ? 181.348 170.128 206.721 1.00 31.80  ? 2846 THR A CB    1 
ATOM   11019 O  OG1   . THR A 1 2846 ? 181.388 170.299 205.308 1.00 31.83  ? 2846 THR A OG1   1 
ATOM   11020 C  CG2   . THR A 1 2846 ? 180.528 171.235 207.358 1.00 31.07  ? 2846 THR A CG2   1 
ATOM   11021 N  N     . ASP A 1 2847 ? 182.713 168.760 209.163 1.00 34.02  ? 2847 ASP A N     1 
ATOM   11022 C  CA    . ASP A 1 2847 ? 182.771 168.508 210.629 1.00 36.08  ? 2847 ASP A CA    1 
ATOM   11023 C  C     . ASP A 1 2847 ? 184.162 168.859 211.163 1.00 38.03  ? 2847 ASP A C     1 
ATOM   11024 O  O     . ASP A 1 2847 ? 184.241 169.615 212.156 1.00 41.94  ? 2847 ASP A O     1 
ATOM   11025 C  CB    . ASP A 1 2847 ? 182.424 167.066 210.963 1.00 37.93  ? 2847 ASP A CB    1 
ATOM   11026 C  CG    . ASP A 1 2847 ? 180.995 166.643 210.660 1.00 43.23  ? 2847 ASP A CG    1 
ATOM   11027 O  OD1   . ASP A 1 2847 ? 180.070 167.263 211.224 1.00 46.05  ? 2847 ASP A OD1   1 
ATOM   11028 O  OD2   . ASP A 1 2847 ? 180.821 165.695 209.867 1.00 46.17  ? 2847 ASP A OD2   1 
ATOM   11029 N  N     . GLU A 1 2848 ? 185.215 168.336 210.529 1.00 35.81  ? 2848 GLU A N     1 
ATOM   11030 C  CA    . GLU A 1 2848 ? 186.594 168.563 211.034 1.00 36.28  ? 2848 GLU A CA    1 
ATOM   11031 C  C     . GLU A 1 2848 ? 186.965 170.044 210.886 1.00 36.77  ? 2848 GLU A C     1 
ATOM   11032 O  O     . GLU A 1 2848 ? 187.481 170.626 211.865 1.00 42.31  ? 2848 GLU A O     1 
ATOM   11033 C  CB    . GLU A 1 2848 ? 187.595 167.691 210.277 1.00 43.42  ? 2848 GLU A CB    1 
ATOM   11034 C  CG    . GLU A 1 2848 ? 189.029 167.883 210.759 1.00 48.26  ? 2848 GLU A CG    1 
ATOM   11035 C  CD    . GLU A 1 2848 ? 189.172 167.728 212.262 1.00 57.39  ? 2848 GLU A CD    1 
ATOM   11036 O  OE1   . GLU A 1 2848 ? 189.598 168.699 212.921 1.00 61.19  ? 2848 GLU A OE1   1 
ATOM   11037 O  OE2   . GLU A 1 2848 ? 188.853 166.635 212.775 1.00 51.08  ? 2848 GLU A OE2   1 
ATOM   11038 N  N     . ASN A 1 2849 ? 186.709 170.627 209.713 1.00 36.59  ? 2849 ASN A N     1 
ATOM   11039 C  CA    . ASN A 1 2849 ? 187.106 172.041 209.464 1.00 34.18  ? 2849 ASN A CA    1 
ATOM   11040 C  C     . ASN A 1 2849 ? 186.380 172.946 210.465 1.00 34.32  ? 2849 ASN A C     1 
ATOM   11041 O  O     . ASN A 1 2849 ? 186.958 173.984 210.848 1.00 39.13  ? 2849 ASN A O     1 
ATOM   11042 C  CB    . ASN A 1 2849 ? 186.886 172.431 208.006 1.00 32.42  ? 2849 ASN A CB    1 
ATOM   11043 C  CG    . ASN A 1 2849 ? 187.855 171.730 207.083 1.00 42.68  ? 2849 ASN A CG    1 
ATOM   11044 O  OD1   . ASN A 1 2849 ? 188.624 172.386 206.374 1.00 46.75  ? 2849 ASN A OD1   1 
ATOM   11045 N  ND2   . ASN A 1 2849 ? 187.841 170.405 207.077 1.00 38.98  ? 2849 ASN A ND2   1 
ATOM   11046 N  N     . ILE A 1 2850 ? 185.173 172.558 210.886 1.00 30.43  ? 2850 ILE A N     1 
ATOM   11047 C  CA    . ILE A 1 2850 ? 184.451 173.346 211.881 1.00 26.90  ? 2850 ILE A CA    1 
ATOM   11048 C  C     . ILE A 1 2850 ? 185.148 173.249 213.230 1.00 36.37  ? 2850 ILE A C     1 
ATOM   11049 O  O     . ILE A 1 2850 ? 185.248 174.232 213.974 1.00 36.22  ? 2850 ILE A O     1 
ATOM   11050 C  CB    . ILE A 1 2850 ? 182.981 172.897 211.961 1.00 28.74  ? 2850 ILE A CB    1 
ATOM   11051 C  CG1   . ILE A 1 2850 ? 182.171 173.607 210.882 1.00 31.90  ? 2850 ILE A CG1   1 
ATOM   11052 C  CG2   . ILE A 1 2850 ? 182.396 173.160 213.344 1.00 26.75  ? 2850 ILE A CG2   1 
ATOM   11053 C  CD1   . ILE A 1 2850 ? 181.747 174.994 211.282 1.00 30.63  ? 2850 ILE A CD1   1 
ATOM   11054 N  N     . ASP A 1 2851 ? 185.653 172.059 213.557 1.00 41.72  ? 2851 ASP A N     1 
ATOM   11055 C  CA    . ASP A 1 2851 ? 186.422 171.888 214.785 1.00 41.80  ? 2851 ASP A CA    1 
ATOM   11056 C  C     . ASP A 1 2851 ? 187.671 172.760 214.770 1.00 40.50  ? 2851 ASP A C     1 
ATOM   11057 O  O     . ASP A 1 2851 ? 187.998 173.416 215.765 1.00 41.56  ? 2851 ASP A O     1 
ATOM   11058 C  CB    . ASP A 1 2851 ? 186.799 170.416 214.961 1.00 51.14  ? 2851 ASP A CB    1 
ATOM   11059 C  CG    . ASP A 1 2851 ? 185.757 169.634 215.732 1.00 58.42  ? 2851 ASP A CG    1 
ATOM   11060 O  OD1   . ASP A 1 2851 ? 184.749 170.240 216.145 1.00 53.55  ? 2851 ASP A OD1   1 
ATOM   11061 O  OD2   . ASP A 1 2851 ? 185.948 168.415 215.926 1.00 60.56  ? 2851 ASP A OD2   1 
ATOM   11062 N  N     . THR A 1 2852 ? 188.380 172.786 213.639 1.00 36.90  ? 2852 THR A N     1 
ATOM   11063 C  CA    . THR A 1 2852 ? 189.627 173.540 213.564 1.00 35.43  ? 2852 THR A CA    1 
ATOM   11064 C  C     . THR A 1 2852 ? 189.376 175.044 213.579 1.00 40.88  ? 2852 THR A C     1 
ATOM   11065 O  O     . THR A 1 2852 ? 190.121 175.794 214.220 1.00 45.53  ? 2852 THR A O     1 
ATOM   11066 C  CB    . THR A 1 2852 ? 190.409 173.142 212.312 1.00 35.86  ? 2852 THR A CB    1 
ATOM   11067 O  OG1   . THR A 1 2852 ? 189.689 173.556 211.144 1.00 41.29  ? 2852 THR A OG1   1 
ATOM   11068 C  CG2   . THR A 1 2852 ? 190.615 171.635 212.270 1.00 33.46  ? 2852 THR A CG2   1 
ATOM   11069 N  N     . VAL A 1 2853 ? 188.339 175.503 212.875 1.00 35.37  ? 2853 VAL A N     1 
ATOM   11070 C  CA    . VAL A 1 2853 ? 188.060 176.937 212.809 1.00 35.64  ? 2853 VAL A CA    1 
ATOM   11071 C  C     . VAL A 1 2853 ? 187.675 177.474 214.182 1.00 36.48  ? 2853 VAL A C     1 
ATOM   11072 O  O     . VAL A 1 2853 ? 188.151 178.535 214.605 1.00 40.96  ? 2853 VAL A O     1 
ATOM   11073 C  CB    . VAL A 1 2853 ? 186.969 177.223 211.760 1.00 31.60  ? 2853 VAL A CB    1 
ATOM   11074 C  CG1   . VAL A 1 2853 ? 186.414 178.627 211.935 1.00 29.69  ? 2853 VAL A CG1   1 
ATOM   11075 C  CG2   . VAL A 1 2853 ? 187.526 177.047 210.358 1.00 26.34  ? 2853 VAL A CG2   1 
ATOM   11076 N  N     . ALA A 1 2854 ? 186.810 176.752 214.899 1.00 34.92  ? 2854 ALA A N     1 
ATOM   11077 C  CA    . ALA A 1 2854 ? 186.368 177.218 216.210 1.00 36.05  ? 2854 ALA A CA    1 
ATOM   11078 C  C     . ALA A 1 2854 ? 187.526 177.284 217.199 1.00 41.47  ? 2854 ALA A C     1 
ATOM   11079 O  O     . ALA A 1 2854 ? 187.642 178.246 217.965 1.00 42.32  ? 2854 ALA A O     1 
ATOM   11080 C  CB    . ALA A 1 2854 ? 185.258 176.313 216.742 1.00 36.31  ? 2854 ALA A CB    1 
ATOM   11081 N  N     . LEU A 1 2855 ? 188.393 176.269 217.197 1.00 39.35  ? 2855 LEU A N     1 
ATOM   11082 C  CA    . LEU A 1 2855 ? 189.554 176.298 218.081 1.00 40.82  ? 2855 LEU A CA    1 
ATOM   11083 C  C     . LEU A 1 2855 ? 190.574 177.339 217.640 1.00 44.43  ? 2855 LEU A C     1 
ATOM   11084 O  O     . LEU A 1 2855 ? 191.355 177.827 218.465 1.00 47.62  ? 2855 LEU A O     1 
ATOM   11085 C  CB    . LEU A 1 2855 ? 190.199 174.913 218.152 1.00 43.84  ? 2855 LEU A CB    1 
ATOM   11086 C  CG    . LEU A 1 2855 ? 189.683 173.973 219.245 1.00 45.03  ? 2855 LEU A CG    1 
ATOM   11087 C  CD1   . LEU A 1 2855 ? 189.670 174.681 220.590 1.00 45.17  ? 2855 LEU A CD1   1 
ATOM   11088 C  CD2   . LEU A 1 2855 ? 188.300 173.441 218.911 1.00 47.74  ? 2855 LEU A CD2   1 
ATOM   11089 N  N     . LYS A 1 2856 ? 190.587 177.688 216.353 1.00 41.45  ? 2856 LYS A N     1 
ATOM   11090 C  CA    . LYS A 1 2856 ? 191.523 178.699 215.873 1.00 39.41  ? 2856 LYS A CA    1 
ATOM   11091 C  C     . LYS A 1 2856 ? 191.133 180.091 216.358 1.00 40.01  ? 2856 LYS A C     1 
ATOM   11092 O  O     . LYS A 1 2856 ? 192.004 180.925 216.633 1.00 43.37  ? 2856 LYS A O     1 
ATOM   11093 C  CB    . LYS A 1 2856 ? 191.595 178.661 214.346 1.00 37.32  ? 2856 LYS A CB    1 
ATOM   11094 C  CG    . LYS A 1 2856 ? 192.481 179.732 213.733 1.00 35.42  ? 2856 LYS A CG    1 
ATOM   11095 C  CD    . LYS A 1 2856 ? 192.358 179.746 212.219 1.00 37.63  ? 2856 LYS A CD    1 
ATOM   11096 C  CE    . LYS A 1 2856 ? 193.252 180.806 211.601 1.00 37.33  ? 2856 LYS A CE    1 
ATOM   11097 N  NZ    . LYS A 1 2856 ? 193.323 180.676 210.120 1.00 33.08  ? 2856 LYS A NZ    1 
ATOM   11098 N  N     . HIS A 1 2857 ? 189.833 180.358 216.481 1.00 35.79  ? 2857 HIS A N     1 
ATOM   11099 C  CA    . HIS A 1 2857 ? 189.349 181.682 216.843 1.00 37.45  ? 2857 HIS A CA    1 
ATOM   11100 C  C     . HIS A 1 2857 ? 188.806 181.762 218.263 1.00 43.00  ? 2857 HIS A C     1 
ATOM   11101 O  O     . HIS A 1 2857 ? 188.610 182.872 218.770 1.00 39.89  ? 2857 HIS A O     1 
ATOM   11102 C  CB    . HIS A 1 2857 ? 188.266 182.134 215.855 1.00 33.50  ? 2857 HIS A CB    1 
ATOM   11103 C  CG    . HIS A 1 2857 ? 188.791 182.439 214.486 1.00 32.87  ? 2857 HIS A CG    1 
ATOM   11104 N  ND1   . HIS A 1 2857 ? 189.373 183.646 214.164 1.00 31.40  ? 2857 HIS A ND1   1 
ATOM   11105 C  CD2   . HIS A 1 2857 ? 188.830 181.691 213.359 1.00 33.06  ? 2857 HIS A CD2   1 
ATOM   11106 C  CE1   . HIS A 1 2857 ? 189.744 183.629 212.897 1.00 33.62  ? 2857 HIS A CE1   1 
ATOM   11107 N  NE2   . HIS A 1 2857 ? 189.425 182.454 212.385 1.00 31.74  ? 2857 HIS A NE2   1 
ATOM   11108 N  N     . PHE A 1 2858 ? 188.563 180.628 218.918 1.00 48.28  ? 2858 PHE A N     1 
ATOM   11109 C  CA    . PHE A 1 2858 ? 188.071 180.595 220.295 1.00 46.97  ? 2858 PHE A CA    1 
ATOM   11110 C  C     . PHE A 1 2858 ? 188.939 179.658 221.127 1.00 54.88  ? 2858 PHE A C     1 
ATOM   11111 O  O     . PHE A 1 2858 ? 188.507 178.562 221.506 1.00 61.41  ? 2858 PHE A O     1 
ATOM   11112 C  CB    . PHE A 1 2858 ? 186.604 180.167 220.343 1.00 40.17  ? 2858 PHE A CB    1 
ATOM   11113 C  CG    . PHE A 1 2858 ? 185.647 181.233 219.901 1.00 37.16  ? 2858 PHE A CG    1 
ATOM   11114 C  CD1   . PHE A 1 2858 ? 185.180 182.178 220.799 1.00 41.51  ? 2858 PHE A CD1   1 
ATOM   11115 C  CD2   . PHE A 1 2858 ? 185.215 181.293 218.587 1.00 33.69  ? 2858 PHE A CD2   1 
ATOM   11116 C  CE1   . PHE A 1 2858 ? 184.298 183.161 220.396 1.00 37.85  ? 2858 PHE A CE1   1 
ATOM   11117 C  CE2   . PHE A 1 2858 ? 184.333 182.274 218.178 1.00 33.68  ? 2858 PHE A CE2   1 
ATOM   11118 C  CZ    . PHE A 1 2858 ? 183.874 183.209 219.084 1.00 35.11  ? 2858 PHE A CZ    1 
ATOM   11119 N  N     . PRO A 1 2859 ? 190.173 180.055 221.426 1.00 52.64  ? 2859 PRO A N     1 
ATOM   11120 C  CA    . PRO A 1 2859 ? 191.020 179.236 222.298 1.00 53.81  ? 2859 PRO A CA    1 
ATOM   11121 C  C     . PRO A 1 2859 ? 190.556 179.318 223.744 1.00 62.92  ? 2859 PRO A C     1 
ATOM   11122 O  O     . PRO A 1 2859 ? 189.797 180.205 224.140 1.00 64.49  ? 2859 PRO A O     1 
ATOM   11123 C  CB    . PRO A 1 2859 ? 192.420 179.839 222.125 1.00 50.35  ? 2859 PRO A CB    1 
ATOM   11124 C  CG    . PRO A 1 2859 ? 192.304 180.828 220.993 1.00 45.46  ? 2859 PRO A CG    1 
ATOM   11125 C  CD    . PRO A 1 2859 ? 190.878 181.263 220.973 1.00 51.28  ? 2859 PRO A CD    1 
ATOM   11126 N  N     . ASN A 1 2860 ? 191.031 178.356 224.537 1.00 59.84  ? 2860 ASN A N     1 
ATOM   11127 C  CA    . ASN A 1 2860 ? 190.764 178.301 225.976 1.00 63.73  ? 2860 ASN A CA    1 
ATOM   11128 C  C     . ASN A 1 2860 ? 189.265 178.200 226.261 1.00 64.14  ? 2860 ASN A C     1 
ATOM   11129 O  O     . ASN A 1 2860 ? 188.711 178.938 227.078 1.00 67.66  ? 2860 ASN A O     1 
ATOM   11130 C  CB    . ASN A 1 2860 ? 191.383 179.503 226.695 1.00 65.56  ? 2860 ASN A CB    1 
ATOM   11131 C  CG    . ASN A 1 2860 ? 192.898 179.450 226.719 1.00 73.90  ? 2860 ASN A CG    1 
ATOM   11132 O  OD1   . ASN A 1 2860 ? 193.490 178.393 226.941 1.00 72.70  ? 2860 ASN A OD1   1 
ATOM   11133 N  ND2   . ASN A 1 2860 ? 193.534 180.592 226.486 1.00 74.74  ? 2860 ASN A ND2   1 
ATOM   11134 N  N     . ILE A 1 2861 ? 188.605 177.272 225.568 1.00 61.20  ? 2861 ILE A N     1 
ATOM   11135 C  CA    . ILE A 1 2861 ? 187.207 176.952 225.813 1.00 61.37  ? 2861 ILE A CA    1 
ATOM   11136 C  C     . ILE A 1 2861 ? 187.084 175.444 225.983 1.00 62.91  ? 2861 ILE A C     1 
ATOM   11137 O  O     . ILE A 1 2861 ? 187.959 174.675 225.578 1.00 63.11  ? 2861 ILE A O     1 
ATOM   11138 C  CB    . ILE A 1 2861 ? 186.269 177.442 224.685 1.00 62.11  ? 2861 ILE A CB    1 
ATOM   11139 C  CG1   . ILE A 1 2861 ? 186.224 176.428 223.539 1.00 57.98  ? 2861 ILE A CG1   1 
ATOM   11140 C  CG2   . ILE A 1 2861 ? 186.690 178.815 224.182 1.00 65.27  ? 2861 ILE A CG2   1 
ATOM   11141 C  CD1   . ILE A 1 2861 ? 184.949 176.480 222.730 1.00 49.24  ? 2861 ILE A CD1   1 
ATOM   11142 N  N     . ASP A 1 2862 ? 185.982 175.028 226.599 1.00 63.24  ? 2862 ASP A N     1 
ATOM   11143 C  CA    . ASP A 1 2862 ? 185.704 173.608 226.799 1.00 62.33  ? 2862 ASP A CA    1 
ATOM   11144 C  C     . ASP A 1 2862 ? 185.369 172.985 225.451 1.00 62.23  ? 2862 ASP A C     1 
ATOM   11145 O  O     . ASP A 1 2862 ? 184.273 173.173 224.918 1.00 64.11  ? 2862 ASP A O     1 
ATOM   11146 C  CB    . ASP A 1 2862 ? 184.566 173.422 227.795 1.00 65.76  ? 2862 ASP A CB    1 
ATOM   11147 C  CG    . ASP A 1 2862 ? 184.771 172.221 228.695 1.00 69.59  ? 2862 ASP A CG    1 
ATOM   11148 O  OD1   . ASP A 1 2862 ? 185.800 171.531 228.540 1.00 68.91  ? 2862 ASP A OD1   1 
ATOM   11149 O  OD2   . ASP A 1 2862 ? 183.905 171.968 229.558 1.00 73.53  ? 2862 ASP A OD2   1 
ATOM   11150 N  N     . ARG A 1 2863 ? 186.325 172.243 224.889 1.00 58.71  ? 2863 ARG A N     1 
ATOM   11151 C  CA    . ARG A 1 2863 ? 186.132 171.653 223.568 1.00 58.81  ? 2863 ARG A CA    1 
ATOM   11152 C  C     . ARG A 1 2863 ? 185.018 170.614 223.584 1.00 62.35  ? 2863 ARG A C     1 
ATOM   11153 O  O     . ARG A 1 2863 ? 184.144 170.610 222.709 1.00 56.50  ? 2863 ARG A O     1 
ATOM   11154 C  CB    . ARG A 1 2863 ? 187.442 171.032 223.082 1.00 53.19  ? 2863 ARG A CB    1 
ATOM   11155 C  CG    . ARG A 1 2863 ? 187.555 170.907 221.575 1.00 51.05  ? 2863 ARG A CG    1 
ATOM   11156 C  CD    . ARG A 1 2863 ? 188.961 170.473 221.169 1.00 54.24  ? 2863 ARG A CD    1 
ATOM   11157 N  NE    . ARG A 1 2863 ? 189.164 170.342 219.728 1.00 63.85  ? 2863 ARG A NE    1 
ATOM   11158 C  CZ    . ARG A 1 2863 ? 188.397 169.649 218.892 1.00 64.93  ? 2863 ARG A CZ    1 
ATOM   11159 N  NH1   . ARG A 1 2863 ? 187.375 168.924 219.319 1.00 59.81  ? 2863 ARG A NH1   1 
ATOM   11160 N  NH2   . ARG A 1 2863 ? 188.680 169.665 217.593 1.00 60.53  ? 2863 ARG A NH2   1 
ATOM   11161 N  N     . GLU A 1 2864 ? 185.032 169.720 224.575 1.00 67.84  ? 2864 GLU A N     1 
ATOM   11162 C  CA    . GLU A 1 2864 ? 184.035 168.656 224.624 1.00 65.24  ? 2864 GLU A CA    1 
ATOM   11163 C  C     . GLU A 1 2864 ? 182.644 169.204 224.920 1.00 60.75  ? 2864 GLU A C     1 
ATOM   11164 O  O     . GLU A 1 2864 ? 181.656 168.754 224.328 1.00 60.70  ? 2864 GLU A O     1 
ATOM   11165 C  CB    . GLU A 1 2864 ? 184.433 167.612 225.666 1.00 64.64  ? 2864 GLU A CB    1 
ATOM   11166 C  CG    . GLU A 1 2864 ? 183.973 166.205 225.330 1.00 65.35  ? 2864 GLU A CG    1 
ATOM   11167 C  CD    . GLU A 1 2864 ? 184.631 165.663 224.076 1.00 76.07  ? 2864 GLU A CD    1 
ATOM   11168 O  OE1   . GLU A 1 2864 ? 185.843 165.367 224.121 1.00 76.63  ? 2864 GLU A OE1   1 
ATOM   11169 O  OE2   . GLU A 1 2864 ? 183.936 165.536 223.046 1.00 70.08  ? 2864 GLU A OE2   1 
ATOM   11170 N  N     . LYS A 1 2865 ? 182.545 170.168 225.839 1.00 58.64  ? 2865 LYS A N     1 
ATOM   11171 C  CA    . LYS A 1 2865 ? 181.239 170.699 226.219 1.00 64.97  ? 2865 LYS A CA    1 
ATOM   11172 C  C     . LYS A 1 2865 ? 180.551 171.384 225.046 1.00 59.45  ? 2865 LYS A C     1 
ATOM   11173 O  O     . LYS A 1 2865 ? 179.347 171.202 224.829 1.00 51.89  ? 2865 LYS A O     1 
ATOM   11174 C  CB    . LYS A 1 2865 ? 181.389 171.673 227.388 1.00 62.65  ? 2865 LYS A CB    1 
ATOM   11175 C  CG    . LYS A 1 2865 ? 180.069 172.149 227.971 1.00 57.99  ? 2865 LYS A CG    1 
ATOM   11176 C  CD    . LYS A 1 2865 ? 180.289 173.053 229.173 1.00 64.32  ? 2865 LYS A CD    1 
ATOM   11177 C  CE    . LYS A 1 2865 ? 180.725 172.258 230.392 1.00 61.92  ? 2865 LYS A CE    1 
ATOM   11178 N  NZ    . LYS A 1 2865 ? 180.778 173.105 231.616 1.00 48.38  ? 2865 LYS A NZ    1 
ATOM   11179 N  N     . ALA A 1 2866 ? 181.297 172.174 224.278 1.00 56.83  ? 2866 ALA A N     1 
ATOM   11180 C  CA    . ALA A 1 2866 ? 180.727 172.971 223.203 1.00 51.91  ? 2866 ALA A CA    1 
ATOM   11181 C  C     . ALA A 1 2866 ? 180.708 172.261 221.856 1.00 49.70  ? 2866 ALA A C     1 
ATOM   11182 O  O     . ALA A 1 2866 ? 180.093 172.776 220.917 1.00 45.42  ? 2866 ALA A O     1 
ATOM   11183 C  CB    . ALA A 1 2866 ? 181.497 174.288 223.061 1.00 47.99  ? 2866 ALA A CB    1 
ATOM   11184 N  N     . MET A 1 2867 ? 181.358 171.106 221.729 1.00 53.47  ? 2867 MET A N     1 
ATOM   11185 C  CA    . MET A 1 2867 ? 181.514 170.484 220.420 1.00 46.33  ? 2867 MET A CA    1 
ATOM   11186 C  C     . MET A 1 2867 ? 181.302 168.978 220.495 1.00 50.39  ? 2867 MET A C     1 
ATOM   11187 O  O     . MET A 1 2867 ? 181.987 168.205 219.818 1.00 52.22  ? 2867 MET A O     1 
ATOM   11188 C  CB    . MET A 1 2867 ? 182.883 170.802 219.827 1.00 48.51  ? 2867 MET A CB    1 
ATOM   11189 C  CG    . MET A 1 2867 ? 182.842 171.194 218.369 1.00 56.99  ? 2867 MET A CG    1 
ATOM   11190 S  SD    . MET A 1 2867 ? 182.826 172.983 218.167 1.00 78.64  ? 2867 MET A SD    1 
ATOM   11191 C  CE    . MET A 1 2867 ? 184.480 173.382 218.724 1.00 54.85  ? 2867 MET A CE    1 
ATOM   11192 N  N     . SER A 1 2868 ? 180.356 168.535 221.320 1.00 52.92  ? 2868 SER A N     1 
ATOM   11193 C  CA    . SER A 1 2868 ? 179.977 167.128 221.310 1.00 51.46  ? 2868 SER A CA    1 
ATOM   11194 C  C     . SER A 1 2868 ? 179.298 166.796 219.988 1.00 54.24  ? 2868 SER A C     1 
ATOM   11195 O  O     . SER A 1 2868 ? 178.377 167.496 219.563 1.00 57.20  ? 2868 SER A O     1 
ATOM   11196 C  CB    . SER A 1 2868 ? 179.049 166.817 222.484 1.00 48.22  ? 2868 SER A CB    1 
ATOM   11197 O  OG    . SER A 1 2868 ? 179.667 167.137 223.718 1.00 54.37  ? 2868 SER A OG    1 
ATOM   11198 N  N     . ARG A 1 2869 ? 179.746 165.716 219.349 1.00 52.25  ? 2869 ARG A N     1 
ATOM   11199 C  CA    . ARG A 1 2869 ? 179.347 165.436 217.970 1.00 53.94  ? 2869 ARG A CA    1 
ATOM   11200 C  C     . ARG A 1 2869 ? 177.842 165.395 217.732 1.00 58.77  ? 2869 ARG A C     1 
ATOM   11201 O  O     . ARG A 1 2869 ? 177.399 165.948 216.710 1.00 59.11  ? 2869 ARG A O     1 
ATOM   11202 C  CB    . ARG A 1 2869 ? 180.015 164.136 217.497 1.00 64.16  ? 2869 ARG A CB    1 
ATOM   11203 C  CG    . ARG A 1 2869 ? 181.510 164.283 217.237 1.00 67.50  ? 2869 ARG A CG    1 
ATOM   11204 C  CD    . ARG A 1 2869 ? 181.761 165.256 216.085 1.00 65.89  ? 2869 ARG A CD    1 
ATOM   11205 N  NE    . ARG A 1 2869 ? 181.869 166.643 216.528 1.00 70.67  ? 2869 ARG A NE    1 
ATOM   11206 C  CZ    . ARG A 1 2869 ? 181.720 167.696 215.736 1.00 62.07  ? 2869 ARG A CZ    1 
ATOM   11207 N  NH1   . ARG A 1 2869 ? 181.456 167.560 214.446 1.00 56.77  ? 2869 ARG A NH1   1 
ATOM   11208 N  NH2   . ARG A 1 2869 ? 181.830 168.916 216.252 1.00 53.85  ? 2869 ARG A NH2   1 
ATOM   11209 N  N     . PRO A 1 2870 ? 177.007 164.785 218.584 1.00 57.67  ? 2870 PRO A N     1 
ATOM   11210 C  CA    . PRO A 1 2870 ? 175.559 164.925 218.372 1.00 44.36  ? 2870 PRO A CA    1 
ATOM   11211 C  C     . PRO A 1 2870 ? 175.081 166.335 218.683 1.00 42.21  ? 2870 PRO A C     1 
ATOM   11212 O  O     . PRO A 1 2870 ? 174.434 166.564 219.709 1.00 47.36  ? 2870 PRO A O     1 
ATOM   11213 C  CB    . PRO A 1 2870 ? 174.951 163.894 219.335 1.00 40.40  ? 2870 PRO A CB    1 
ATOM   11214 C  CG    . PRO A 1 2870 ? 176.084 163.017 219.755 1.00 48.26  ? 2870 PRO A CG    1 
ATOM   11215 C  CD    . PRO A 1 2870 ? 177.305 163.864 219.693 1.00 47.55  ? 2870 PRO A CD    1 
ATOM   11216 N  N     . ILE A 1 2871 ? 175.393 167.287 217.804 1.00 36.30  ? 2871 ILE A N     1 
ATOM   11217 C  CA    . ILE A 1 2871 ? 174.977 168.677 217.988 1.00 31.96  ? 2871 ILE A CA    1 
ATOM   11218 C  C     . ILE A 1 2871 ? 173.516 168.759 217.559 1.00 30.16  ? 2871 ILE A C     1 
ATOM   11219 O  O     . ILE A 1 2871 ? 173.210 168.938 216.379 1.00 28.11  ? 2871 ILE A O     1 
ATOM   11220 C  CB    . ILE A 1 2871 ? 175.851 169.652 217.196 1.00 31.98  ? 2871 ILE A CB    1 
ATOM   11221 C  CG1   . ILE A 1 2871 ? 177.299 169.594 217.673 1.00 35.38  ? 2871 ILE A CG1   1 
ATOM   11222 C  CG2   . ILE A 1 2871 ? 175.341 171.066 217.365 1.00 26.49  ? 2871 ILE A CG2   1 
ATOM   11223 C  CD1   . ILE A 1 2871 ? 178.268 170.334 216.781 1.00 31.86  ? 2871 ILE A CD1   1 
ATOM   11224 N  N     . LEU A 1 2872 ? 172.607 168.627 218.520 1.00 29.65  ? 2872 LEU A N     1 
ATOM   11225 C  CA    . LEU A 1 2872 ? 171.176 168.613 218.256 1.00 27.16  ? 2872 LEU A CA    1 
ATOM   11226 C  C     . LEU A 1 2872 ? 170.517 169.771 218.989 1.00 25.69  ? 2872 LEU A C     1 
ATOM   11227 O  O     . LEU A 1 2872 ? 170.746 169.963 220.188 1.00 29.27  ? 2872 LEU A O     1 
ATOM   11228 C  CB    . LEU A 1 2872 ? 170.548 167.284 218.691 1.00 30.48  ? 2872 LEU A CB    1 
ATOM   11229 C  CG    . LEU A 1 2872 ? 171.007 165.998 217.998 1.00 28.73  ? 2872 LEU A CG    1 
ATOM   11230 C  CD1   . LEU A 1 2872 ? 169.915 164.948 218.061 1.00 37.04  ? 2872 LEU A CD1   1 
ATOM   11231 C  CD2   . LEU A 1 2872 ? 171.396 166.256 216.554 1.00 24.33  ? 2872 LEU A CD2   1 
ATOM   11232 N  N     . TYR A 1 2873 ? 169.704 170.538 218.268 1.00 22.08  ? 2873 TYR A N     1 
ATOM   11233 C  CA    . TYR A 1 2873 ? 168.935 171.632 218.837 1.00 19.50  ? 2873 TYR A CA    1 
ATOM   11234 C  C     . TYR A 1 2873 ? 167.464 171.431 218.514 1.00 22.47  ? 2873 TYR A C     1 
ATOM   11235 O  O     . TYR A 1 2873 ? 167.115 171.031 217.400 1.00 29.91  ? 2873 TYR A O     1 
ATOM   11236 C  CB    . TYR A 1 2873 ? 169.401 172.990 218.302 1.00 21.92  ? 2873 TYR A CB    1 
ATOM   11237 C  CG    . TYR A 1 2873 ? 170.557 173.589 219.066 1.00 18.02  ? 2873 TYR A CG    1 
ATOM   11238 C  CD1   . TYR A 1 2873 ? 171.821 173.021 219.010 1.00 17.94  ? 2873 TYR A CD1   1 
ATOM   11239 C  CD2   . TYR A 1 2873 ? 170.382 174.720 219.846 1.00 17.50  ? 2873 TYR A CD2   1 
ATOM   11240 C  CE1   . TYR A 1 2873 ? 172.878 173.567 219.710 1.00 18.83  ? 2873 TYR A CE1   1 
ATOM   11241 C  CE2   . TYR A 1 2873 ? 171.431 175.272 220.547 1.00 16.93  ? 2873 TYR A CE2   1 
ATOM   11242 C  CZ    . TYR A 1 2873 ? 172.677 174.692 220.476 1.00 17.77  ? 2873 TYR A CZ    1 
ATOM   11243 O  OH    . TYR A 1 2873 ? 173.726 175.241 221.176 1.00 17.56  ? 2873 TYR A OH    1 
ATOM   11244 N  N     . SER A 1 2874 ? 166.605 171.713 219.489 1.00 22.60  ? 2874 SER A N     1 
ATOM   11245 C  CA    . SER A 1 2874 ? 165.174 171.562 219.284 1.00 26.99  ? 2874 SER A CA    1 
ATOM   11246 C  C     . SER A 1 2874 ? 164.427 172.431 220.284 1.00 30.96  ? 2874 SER A C     1 
ATOM   11247 O  O     . SER A 1 2874 ? 164.957 172.783 221.341 1.00 37.28  ? 2874 SER A O     1 
ATOM   11248 C  CB    . SER A 1 2874 ? 164.741 170.099 219.423 1.00 27.82  ? 2874 SER A CB    1 
ATOM   11249 O  OG    . SER A 1 2874 ? 163.367 169.942 219.117 1.00 31.04  ? 2874 SER A OG    1 
ATOM   11250 N  N     . ASN A 1 2875 ? 163.189 172.771 219.929 1.00 28.88  ? 2875 ASN A N     1 
ATOM   11251 C  CA    . ASN A 1 2875 ? 162.270 173.464 220.822 1.00 31.78  ? 2875 ASN A CA    1 
ATOM   11252 C  C     . ASN A 1 2875 ? 161.082 172.587 221.200 1.00 37.65  ? 2875 ASN A C     1 
ATOM   11253 O  O     . ASN A 1 2875 ? 160.008 173.103 221.525 1.00 39.79  ? 2875 ASN A O     1 
ATOM   11254 C  CB    . ASN A 1 2875 ? 161.792 174.772 220.189 1.00 33.34  ? 2875 ASN A CB    1 
ATOM   11255 C  CG    . ASN A 1 2875 ? 161.060 174.556 218.877 1.00 33.86  ? 2875 ASN A CG    1 
ATOM   11256 O  OD1   . ASN A 1 2875 ? 160.992 173.439 218.364 1.00 37.16  ? 2875 ASN A OD1   1 
ATOM   11257 N  ND2   . ASN A 1 2875 ? 160.502 175.629 218.330 1.00 35.69  ? 2875 ASN A ND2   1 
ATOM   11258 N  N     . TRP A 1 2876 ? 161.255 171.267 221.150 1.00 39.12  ? 2876 TRP A N     1 
ATOM   11259 C  CA    . TRP A 1 2876 ? 160.172 170.334 221.427 1.00 37.53  ? 2876 TRP A CA    1 
ATOM   11260 C  C     . TRP A 1 2876 ? 160.079 169.956 222.898 1.00 40.99  ? 2876 TRP A C     1 
ATOM   11261 O  O     . TRP A 1 2876 ? 158.974 169.726 223.401 1.00 43.22  ? 2876 TRP A O     1 
ATOM   11262 C  CB    . TRP A 1 2876 ? 160.347 169.068 220.587 1.00 34.54  ? 2876 TRP A CB    1 
ATOM   11263 C  CG    . TRP A 1 2876 ? 159.907 169.221 219.165 1.00 29.95  ? 2876 TRP A CG    1 
ATOM   11264 C  CD1   . TRP A 1 2876 ? 159.069 170.172 218.664 1.00 31.94  ? 2876 TRP A CD1   1 
ATOM   11265 C  CD2   . TRP A 1 2876 ? 160.279 168.391 218.059 1.00 26.44  ? 2876 TRP A CD2   1 
ATOM   11266 N  NE1   . TRP A 1 2876 ? 158.899 169.989 217.313 1.00 30.67  ? 2876 TRP A NE1   1 
ATOM   11267 C  CE2   . TRP A 1 2876 ? 159.632 168.901 216.917 1.00 26.46  ? 2876 TRP A CE2   1 
ATOM   11268 C  CE3   . TRP A 1 2876 ? 161.098 167.266 217.925 1.00 31.90  ? 2876 TRP A CE3   1 
ATOM   11269 C  CZ2   . TRP A 1 2876 ? 159.778 168.325 215.657 1.00 27.55  ? 2876 TRP A CZ2   1 
ATOM   11270 C  CZ3   . TRP A 1 2876 ? 161.242 166.696 216.674 1.00 27.17  ? 2876 TRP A CZ3   1 
ATOM   11271 C  CH2   . TRP A 1 2876 ? 160.585 167.226 215.556 1.00 26.07  ? 2876 TRP A CH2   1 
ATOM   11272 N  N     . LEU A 1 2877 ? 161.210 169.884 223.596 1.00 38.77  ? 2877 LEU A N     1 
ATOM   11273 C  CA    . LEU A 1 2877 ? 161.238 169.521 225.006 1.00 40.24  ? 2877 LEU A CA    1 
ATOM   11274 C  C     . LEU A 1 2877 ? 161.165 170.726 225.933 1.00 43.63  ? 2877 LEU A C     1 
ATOM   11275 O  O     . LEU A 1 2877 ? 161.180 170.551 227.155 1.00 50.70  ? 2877 LEU A O     1 
ATOM   11276 C  CB    . LEU A 1 2877 ? 162.501 168.712 225.318 1.00 40.33  ? 2877 LEU A CB    1 
ATOM   11277 C  CG    . LEU A 1 2877 ? 162.606 167.344 224.645 1.00 36.60  ? 2877 LEU A CG    1 
ATOM   11278 C  CD1   . LEU A 1 2877 ? 163.690 166.507 225.302 1.00 37.74  ? 2877 LEU A CD1   1 
ATOM   11279 C  CD2   . LEU A 1 2877 ? 161.270 166.629 224.703 1.00 37.44  ? 2877 LEU A CD2   1 
ATOM   11280 N  N     . SER A 1 2878 ? 161.086 171.935 225.387 1.00 43.03  ? 2878 SER A N     1 
ATOM   11281 C  CA    . SER A 1 2878 ? 160.989 173.146 226.189 1.00 46.22  ? 2878 SER A CA    1 
ATOM   11282 C  C     . SER A 1 2878 ? 160.374 174.238 225.325 1.00 48.02  ? 2878 SER A C     1 
ATOM   11283 O  O     . SER A 1 2878 ? 160.047 174.021 224.155 1.00 47.82  ? 2878 SER A O     1 
ATOM   11284 C  CB    . SER A 1 2878 ? 162.359 173.562 226.733 1.00 45.47  ? 2878 SER A CB    1 
ATOM   11285 O  OG    . SER A 1 2878 ? 163.261 173.830 225.675 1.00 46.32  ? 2878 SER A OG    1 
ATOM   11286 N  N     . LYS A 1 2879 ? 160.210 175.422 225.916 1.00 48.76  ? 2879 LYS A N     1 
ATOM   11287 C  CA    . LYS A 1 2879 ? 159.667 176.549 225.167 1.00 51.64  ? 2879 LYS A CA    1 
ATOM   11288 C  C     . LYS A 1 2879 ? 160.698 177.167 224.233 1.00 51.05  ? 2879 LYS A C     1 
ATOM   11289 O  O     . LYS A 1 2879 ? 160.337 177.663 223.159 1.00 46.74  ? 2879 LYS A O     1 
ATOM   11290 C  CB    . LYS A 1 2879 ? 159.128 177.610 226.128 1.00 56.61  ? 2879 LYS A CB    1 
ATOM   11291 C  CG    . LYS A 1 2879 ? 160.089 177.990 227.242 1.00 58.42  ? 2879 LYS A CG    1 
ATOM   11292 C  CD    . LYS A 1 2879 ? 159.679 179.299 227.897 1.00 57.94  ? 2879 LYS A CD    1 
ATOM   11293 C  CE    . LYS A 1 2879 ? 160.821 179.895 228.703 1.00 62.12  ? 2879 LYS A CE    1 
ATOM   11294 N  NZ    . LYS A 1 2879 ? 161.134 179.080 229.909 1.00 64.41  ? 2879 LYS A NZ    1 
ATOM   11295 N  N     . ASP A 1 2880 ? 161.971 177.145 224.613 1.00 51.27  ? 2880 ASP A N     1 
ATOM   11296 C  CA    . ASP A 1 2880 ? 163.030 177.804 223.865 1.00 45.15  ? 2880 ASP A CA    1 
ATOM   11297 C  C     . ASP A 1 2880 ? 163.819 176.803 223.030 1.00 39.62  ? 2880 ASP A C     1 
ATOM   11298 O  O     . ASP A 1 2880 ? 163.817 175.596 223.288 1.00 41.72  ? 2880 ASP A O     1 
ATOM   11299 C  CB    . ASP A 1 2880 ? 163.973 178.547 224.814 1.00 45.36  ? 2880 ASP A CB    1 
ATOM   11300 C  CG    . ASP A 1 2880 ? 163.311 179.734 225.479 1.00 58.17  ? 2880 ASP A CG    1 
ATOM   11301 O  OD1   . ASP A 1 2880 ? 162.216 180.134 225.030 1.00 61.13  ? 2880 ASP A OD1   1 
ATOM   11302 O  OD2   . ASP A 1 2880 ? 163.884 180.269 226.451 1.00 61.49  ? 2880 ASP A OD2   1 
ATOM   11303 N  N     . TYR A 1 2881 ? 164.502 177.329 222.014 1.00 36.66  ? 2881 TYR A N     1 
ATOM   11304 C  CA    . TYR A 1 2881 ? 165.341 176.531 221.121 1.00 32.50  ? 2881 TYR A CA    1 
ATOM   11305 C  C     . TYR A 1 2881 ? 166.685 176.313 221.806 1.00 30.70  ? 2881 TYR A C     1 
ATOM   11306 O  O     . TYR A 1 2881 ? 167.594 177.140 221.726 1.00 33.26  ? 2881 TYR A O     1 
ATOM   11307 C  CB    . TYR A 1 2881 ? 165.497 177.227 219.774 1.00 30.43  ? 2881 TYR A CB    1 
ATOM   11308 C  CG    . TYR A 1 2881 ? 165.966 176.326 218.655 1.00 26.72  ? 2881 TYR A CG    1 
ATOM   11309 C  CD1   . TYR A 1 2881 ? 165.181 175.271 218.210 1.00 26.75  ? 2881 TYR A CD1   1 
ATOM   11310 C  CD2   . TYR A 1 2881 ? 167.188 176.539 218.033 1.00 24.89  ? 2881 TYR A CD2   1 
ATOM   11311 C  CE1   . TYR A 1 2881 ? 165.604 174.449 217.184 1.00 23.30  ? 2881 TYR A CE1   1 
ATOM   11312 C  CE2   . TYR A 1 2881 ? 167.619 175.723 217.006 1.00 26.09  ? 2881 TYR A CE2   1 
ATOM   11313 C  CZ    . TYR A 1 2881 ? 166.823 174.679 216.586 1.00 23.95  ? 2881 TYR A CZ    1 
ATOM   11314 O  OH    . TYR A 1 2881 ? 167.248 173.863 215.564 1.00 23.75  ? 2881 TYR A OH    1 
ATOM   11315 N  N     . ILE A 1 2882 ? 166.810 175.178 222.487 1.00 27.04  ? 2882 ILE A N     1 
ATOM   11316 C  CA    . ILE A 1 2882 ? 167.999 174.867 223.277 1.00 28.74  ? 2882 ILE A CA    1 
ATOM   11317 C  C     . ILE A 1 2882 ? 168.507 173.494 222.858 1.00 26.23  ? 2882 ILE A C     1 
ATOM   11318 O  O     . ILE A 1 2882 ? 167.758 172.693 222.276 1.00 31.69  ? 2882 ILE A O     1 
ATOM   11319 C  CB    . ILE A 1 2882 ? 167.704 174.921 224.796 1.00 29.33  ? 2882 ILE A CB    1 
ATOM   11320 C  CG1   . ILE A 1 2882 ? 166.384 174.218 225.121 1.00 30.59  ? 2882 ILE A CG1   1 
ATOM   11321 C  CG2   . ILE A 1 2882 ? 167.680 176.362 225.281 1.00 28.87  ? 2882 ILE A CG2   1 
ATOM   11322 C  CD1   . ILE A 1 2882 ? 166.531 172.755 225.492 1.00 30.63  ? 2882 ILE A CD1   1 
ATOM   11323 N  N     . PRO A 1 2883 ? 169.784 173.197 223.115 1.00 19.94  ? 2883 PRO A N     1 
ATOM   11324 C  CA    . PRO A 1 2883 ? 170.316 171.881 222.740 1.00 22.92  ? 2883 PRO A CA    1 
ATOM   11325 C  C     . PRO A 1 2883 ? 169.563 170.756 223.435 1.00 32.66  ? 2883 PRO A C     1 
ATOM   11326 O  O     . PRO A 1 2883 ? 169.171 170.869 224.598 1.00 31.53  ? 2883 PRO A O     1 
ATOM   11327 C  CB    . PRO A 1 2883 ? 171.782 171.944 223.190 1.00 21.10  ? 2883 PRO A CB    1 
ATOM   11328 C  CG    . PRO A 1 2883 ? 171.844 173.066 224.168 1.00 22.87  ? 2883 PRO A CG    1 
ATOM   11329 C  CD    . PRO A 1 2883 ? 170.824 174.054 223.710 1.00 20.54  ? 2883 PRO A CD    1 
ATOM   11330 N  N     . VAL A 1 2884 ? 169.367 169.661 222.706 1.00 30.71  ? 2884 VAL A N     1 
ATOM   11331 C  CA    . VAL A 1 2884 ? 168.562 168.536 223.164 1.00 30.22  ? 2884 VAL A CA    1 
ATOM   11332 C  C     . VAL A 1 2884 ? 169.413 167.273 223.133 1.00 32.20  ? 2884 VAL A C     1 
ATOM   11333 O  O     . VAL A 1 2884 ? 170.229 167.081 222.225 1.00 28.90  ? 2884 VAL A O     1 
ATOM   11334 C  CB    . VAL A 1 2884 ? 167.285 168.371 222.309 1.00 26.75  ? 2884 VAL A CB    1 
ATOM   11335 C  CG1   . VAL A 1 2884 ? 167.632 168.080 220.856 1.00 25.82  ? 2884 VAL A CG1   1 
ATOM   11336 C  CG2   . VAL A 1 2884 ? 166.388 167.282 222.878 1.00 30.01  ? 2884 VAL A CG2   1 
ATOM   11337 N  N     . ASP A 1 2885 ? 169.240 166.428 224.146 1.00 34.37  ? 2885 ASP A N     1 
ATOM   11338 C  CA    . ASP A 1 2885 ? 169.935 165.151 224.186 1.00 36.84  ? 2885 ASP A CA    1 
ATOM   11339 C  C     . ASP A 1 2885 ? 169.305 164.172 223.200 1.00 36.58  ? 2885 ASP A C     1 
ATOM   11340 O  O     . ASP A 1 2885 ? 168.096 164.191 222.955 1.00 37.80  ? 2885 ASP A O     1 
ATOM   11341 C  CB    . ASP A 1 2885 ? 169.905 164.574 225.601 1.00 42.34  ? 2885 ASP A CB    1 
ATOM   11342 C  CG    . ASP A 1 2885 ? 170.571 163.216 225.693 1.00 47.90  ? 2885 ASP A CG    1 
ATOM   11343 O  OD1   . ASP A 1 2885 ? 169.961 162.291 226.270 1.00 47.78  ? 2885 ASP A OD1   1 
ATOM   11344 O  OD2   . ASP A 1 2885 ? 171.704 163.072 225.187 1.00 46.93  ? 2885 ASP A OD2   1 
ATOM   11345 N  N     . GLN A 1 2886 ? 170.149 163.309 222.628 1.00 33.97  ? 2886 GLN A N     1 
ATOM   11346 C  CA    . GLN A 1 2886 ? 169.687 162.391 221.591 1.00 35.37  ? 2886 GLN A CA    1 
ATOM   11347 C  C     . GLN A 1 2886 ? 168.662 161.399 222.131 1.00 38.78  ? 2886 GLN A C     1 
ATOM   11348 O  O     . GLN A 1 2886 ? 167.666 161.104 221.461 1.00 37.32  ? 2886 GLN A O     1 
ATOM   11349 C  CB    . GLN A 1 2886 ? 170.878 161.651 220.983 1.00 34.58  ? 2886 GLN A CB    1 
ATOM   11350 C  CG    . GLN A 1 2886 ? 170.592 161.012 219.637 1.00 31.84  ? 2886 GLN A CG    1 
ATOM   11351 C  CD    . GLN A 1 2886 ? 171.858 160.683 218.871 1.00 39.73  ? 2886 GLN A CD    1 
ATOM   11352 O  OE1   . GLN A 1 2886 ? 172.668 159.867 219.310 1.00 38.53  ? 2886 GLN A OE1   1 
ATOM   11353 N  NE2   . GLN A 1 2886 ? 172.036 161.319 217.719 1.00 37.99  ? 2886 GLN A NE2   1 
ATOM   11354 N  N     . GLU A 1 2887 ? 168.887 160.871 223.336 1.00 41.60  ? 2887 GLU A N     1 
ATOM   11355 C  CA    . GLU A 1 2887 ? 167.985 159.856 223.871 1.00 40.43  ? 2887 GLU A CA    1 
ATOM   11356 C  C     . GLU A 1 2887 ? 166.659 160.461 224.315 1.00 35.05  ? 2887 GLU A C     1 
ATOM   11357 O  O     . GLU A 1 2887 ? 165.597 159.867 224.091 1.00 36.11  ? 2887 GLU A O     1 
ATOM   11358 C  CB    . GLU A 1 2887 ? 168.655 159.112 225.025 1.00 45.45  ? 2887 GLU A CB    1 
ATOM   11359 C  CG    . GLU A 1 2887 ? 169.795 158.208 224.586 1.00 49.55  ? 2887 GLU A CG    1 
ATOM   11360 C  CD    . GLU A 1 2887 ? 169.458 157.415 223.338 1.00 52.65  ? 2887 GLU A CD    1 
ATOM   11361 O  OE1   . GLU A 1 2887 ? 168.548 156.562 223.400 1.00 50.44  ? 2887 GLU A OE1   1 
ATOM   11362 O  OE2   . GLU A 1 2887 ? 170.102 157.645 222.293 1.00 46.63  ? 2887 GLU A OE2   1 
ATOM   11363 N  N     . GLU A 1 2888 ? 166.694 161.635 224.949 1.00 39.42  ? 2888 GLU A N     1 
ATOM   11364 C  CA    . GLU A 1 2888 ? 165.450 162.300 225.324 1.00 43.49  ? 2888 GLU A CA    1 
ATOM   11365 C  C     . GLU A 1 2888 ? 164.650 162.699 224.091 1.00 41.96  ? 2888 GLU A C     1 
ATOM   11366 O  O     . GLU A 1 2888 ? 163.417 162.608 224.085 1.00 42.15  ? 2888 GLU A O     1 
ATOM   11367 C  CB    . GLU A 1 2888 ? 165.741 163.521 226.196 1.00 39.79  ? 2888 GLU A CB    1 
ATOM   11368 C  CG    . GLU A 1 2888 ? 166.919 163.348 227.134 1.00 46.33  ? 2888 GLU A CG    1 
ATOM   11369 C  CD    . GLU A 1 2888 ? 166.857 164.286 228.322 1.00 55.46  ? 2888 GLU A CD    1 
ATOM   11370 O  OE1   . GLU A 1 2888 ? 167.928 164.652 228.849 1.00 58.71  ? 2888 GLU A OE1   1 
ATOM   11371 O  OE2   . GLU A 1 2888 ? 165.736 164.659 228.728 1.00 60.02  ? 2888 GLU A OE2   1 
ATOM   11372 N  N     . LEU A 1 2889 ? 165.335 163.154 223.040 1.00 36.75  ? 2889 LEU A N     1 
ATOM   11373 C  CA    . LEU A 1 2889 ? 164.650 163.456 221.788 1.00 31.87  ? 2889 LEU A CA    1 
ATOM   11374 C  C     . LEU A 1 2889 ? 164.031 162.201 221.185 1.00 36.79  ? 2889 LEU A C     1 
ATOM   11375 O  O     . LEU A 1 2889 ? 162.905 162.239 220.676 1.00 38.83  ? 2889 LEU A O     1 
ATOM   11376 C  CB    . LEU A 1 2889 ? 165.621 164.104 220.802 1.00 30.85  ? 2889 LEU A CB    1 
ATOM   11377 C  CG    . LEU A 1 2889 ? 165.111 164.312 219.375 1.00 28.19  ? 2889 LEU A CG    1 
ATOM   11378 C  CD1   . LEU A 1 2889 ? 164.153 165.490 219.318 1.00 25.26  ? 2889 LEU A CD1   1 
ATOM   11379 C  CD2   . LEU A 1 2889 ? 166.272 164.513 218.417 1.00 31.42  ? 2889 LEU A CD2   1 
ATOM   11380 N  N     . ARG A 1 2890 ? 164.753 161.078 221.236 1.00 37.86  ? 2890 ARG A N     1 
ATOM   11381 C  CA    . ARG A 1 2890 ? 164.227 159.832 220.689 1.00 32.88  ? 2890 ARG A CA    1 
ATOM   11382 C  C     . ARG A 1 2890 ? 162.974 159.384 221.430 1.00 36.71  ? 2890 ARG A C     1 
ATOM   11383 O  O     . ARG A 1 2890 ? 161.997 158.953 220.808 1.00 40.69  ? 2890 ARG A O     1 
ATOM   11384 C  CB    . ARG A 1 2890 ? 165.296 158.741 220.746 1.00 36.03  ? 2890 ARG A CB    1 
ATOM   11385 C  CG    . ARG A 1 2890 ? 164.958 157.503 219.935 1.00 35.26  ? 2890 ARG A CG    1 
ATOM   11386 C  CD    . ARG A 1 2890 ? 165.852 156.334 220.313 1.00 31.87  ? 2890 ARG A CD    1 
ATOM   11387 N  NE    . ARG A 1 2890 ? 167.266 156.667 220.201 1.00 33.89  ? 2890 ARG A NE    1 
ATOM   11388 C  CZ    . ARG A 1 2890 ? 167.955 156.637 219.068 1.00 41.92  ? 2890 ARG A CZ    1 
ATOM   11389 N  NH1   . ARG A 1 2890 ? 167.389 156.291 217.924 1.00 37.71  ? 2890 ARG A NH1   1 
ATOM   11390 N  NH2   . ARG A 1 2890 ? 169.244 156.962 219.084 1.00 40.00  ? 2890 ARG A NH2   1 
ATOM   11391 N  N     . ASP A 1 2891 ? 162.985 159.473 222.763 1.00 38.84  ? 2891 ASP A N     1 
ATOM   11392 C  CA    . ASP A 1 2891 ? 161.817 159.073 223.540 1.00 37.12  ? 2891 ASP A CA    1 
ATOM   11393 C  C     . ASP A 1 2891 ? 160.622 159.969 223.241 1.00 37.48  ? 2891 ASP A C     1 
ATOM   11394 O  O     . ASP A 1 2891 ? 159.492 159.485 223.105 1.00 39.18  ? 2891 ASP A O     1 
ATOM   11395 C  CB    . ASP A 1 2891 ? 162.145 159.100 225.032 1.00 37.82  ? 2891 ASP A CB    1 
ATOM   11396 C  CG    . ASP A 1 2891 ? 163.305 158.195 225.389 1.00 46.45  ? 2891 ASP A CG    1 
ATOM   11397 O  OD1   . ASP A 1 2891 ? 163.561 157.231 224.637 1.00 46.82  ? 2891 ASP A OD1   1 
ATOM   11398 O  OD2   . ASP A 1 2891 ? 163.962 158.446 226.421 1.00 48.39  ? 2891 ASP A OD2   1 
ATOM   11399 N  N     . TYR A 1 2892 ? 160.853 161.279 223.138 1.00 39.59  ? 2892 TYR A N     1 
ATOM   11400 C  CA    . TYR A 1 2892 ? 159.759 162.204 222.864 1.00 33.80  ? 2892 TYR A CA    1 
ATOM   11401 C  C     . TYR A 1 2892 ? 159.168 161.968 221.480 1.00 35.46  ? 2892 TYR A C     1 
ATOM   11402 O  O     . TYR A 1 2892 ? 157.946 162.022 221.302 1.00 37.61  ? 2892 TYR A O     1 
ATOM   11403 C  CB    . TYR A 1 2892 ? 160.247 163.644 223.005 1.00 32.55  ? 2892 TYR A CB    1 
ATOM   11404 C  CG    . TYR A 1 2892 ? 159.227 164.677 222.594 1.00 34.41  ? 2892 TYR A CG    1 
ATOM   11405 C  CD1   . TYR A 1 2892 ? 158.146 164.976 223.411 1.00 34.74  ? 2892 TYR A CD1   1 
ATOM   11406 C  CD2   . TYR A 1 2892 ? 159.342 165.351 221.388 1.00 37.30  ? 2892 TYR A CD2   1 
ATOM   11407 C  CE1   . TYR A 1 2892 ? 157.209 165.919 223.037 1.00 35.98  ? 2892 TYR A CE1   1 
ATOM   11408 C  CE2   . TYR A 1 2892 ? 158.412 166.291 221.008 1.00 37.43  ? 2892 TYR A CE2   1 
ATOM   11409 C  CZ    . TYR A 1 2892 ? 157.349 166.575 221.834 1.00 40.26  ? 2892 TYR A CZ    1 
ATOM   11410 O  OH    . TYR A 1 2892 ? 156.422 167.517 221.451 1.00 41.55  ? 2892 TYR A OH    1 
ATOM   11411 N  N     . VAL A 1 2893 ? 160.022 161.710 220.486 1.00 32.86  ? 2893 VAL A N     1 
ATOM   11412 C  CA    . VAL A 1 2893 ? 159.526 161.416 219.145 1.00 33.27  ? 2893 VAL A CA    1 
ATOM   11413 C  C     . VAL A 1 2893 ? 158.763 160.098 219.132 1.00 36.45  ? 2893 VAL A C     1 
ATOM   11414 O  O     . VAL A 1 2893 ? 157.749 159.968 218.434 1.00 36.49  ? 2893 VAL A O     1 
ATOM   11415 C  CB    . VAL A 1 2893 ? 160.689 161.415 218.134 1.00 34.68  ? 2893 VAL A CB    1 
ATOM   11416 C  CG1   . VAL A 1 2893 ? 160.222 160.915 216.776 1.00 34.10  ? 2893 VAL A CG1   1 
ATOM   11417 C  CG2   . VAL A 1 2893 ? 161.273 162.811 218.004 1.00 31.11  ? 2893 VAL A CG2   1 
ATOM   11418 N  N     . LYS A 1 2894 ? 159.221 159.107 219.901 1.00 38.30  ? 2894 LYS A N     1 
ATOM   11419 C  CA    . LYS A 1 2894 ? 158.499 157.841 219.995 1.00 33.70  ? 2894 LYS A CA    1 
ATOM   11420 C  C     . LYS A 1 2894 ? 157.090 158.054 220.533 1.00 33.72  ? 2894 LYS A C     1 
ATOM   11421 O  O     . LYS A 1 2894 ? 156.120 157.493 220.010 1.00 37.01  ? 2894 LYS A O     1 
ATOM   11422 C  CB    . LYS A 1 2894 ? 159.266 156.863 220.886 1.00 30.76  ? 2894 LYS A CB    1 
ATOM   11423 C  CG    . LYS A 1 2894 ? 160.443 156.183 220.215 1.00 36.06  ? 2894 LYS A CG    1 
ATOM   11424 C  CD    . LYS A 1 2894 ? 161.219 155.338 221.212 1.00 38.02  ? 2894 LYS A CD    1 
ATOM   11425 C  CE    . LYS A 1 2894 ? 162.481 154.769 220.590 1.00 33.66  ? 2894 LYS A CE    1 
ATOM   11426 N  NZ    . LYS A 1 2894 ? 163.293 154.016 221.585 1.00 35.75  ? 2894 LYS A NZ    1 
ATOM   11427 N  N     . ALA A 1 2895 ? 156.960 158.862 221.587 1.00 30.00  ? 2895 ALA A N     1 
ATOM   11428 C  CA    . ALA A 1 2895 ? 155.644 159.143 222.151 1.00 32.79  ? 2895 ALA A CA    1 
ATOM   11429 C  C     . ALA A 1 2895 ? 154.774 159.900 221.156 1.00 35.78  ? 2895 ALA A C     1 
ATOM   11430 O  O     . ALA A 1 2895 ? 153.583 159.605 221.003 1.00 35.81  ? 2895 ALA A O     1 
ATOM   11431 C  CB    . ALA A 1 2895 ? 155.789 159.930 223.453 1.00 35.06  ? 2895 ALA A CB    1 
ATOM   11432 N  N     . ARG A 1 2896 ? 155.355 160.886 220.469 1.00 38.61  ? 2896 ARG A N     1 
ATOM   11433 C  CA    . ARG A 1 2896 ? 154.605 161.625 219.459 1.00 38.00  ? 2896 ARG A CA    1 
ATOM   11434 C  C     . ARG A 1 2896 ? 154.244 160.739 218.274 1.00 32.96  ? 2896 ARG A C     1 
ATOM   11435 O  O     . ARG A 1 2896 ? 153.152 160.873 217.710 1.00 33.62  ? 2896 ARG A O     1 
ATOM   11436 C  CB    . ARG A 1 2896 ? 155.407 162.839 218.992 1.00 35.70  ? 2896 ARG A CB    1 
ATOM   11437 C  CG    . ARG A 1 2896 ? 155.560 163.927 220.043 1.00 37.72  ? 2896 ARG A CG    1 
ATOM   11438 C  CD    . ARG A 1 2896 ? 154.213 164.384 220.577 1.00 33.38  ? 2896 ARG A CD    1 
ATOM   11439 N  NE    . ARG A 1 2896 ? 153.648 165.466 219.779 1.00 39.26  ? 2896 ARG A NE    1 
ATOM   11440 C  CZ    . ARG A 1 2896 ? 152.363 165.578 219.473 1.00 46.69  ? 2896 ARG A CZ    1 
ATOM   11441 N  NH1   . ARG A 1 2896 ? 151.472 164.697 219.897 1.00 41.10  ? 2896 ARG A NH1   1 
ATOM   11442 N  NH2   . ARG A 1 2896 ? 151.962 166.601 218.723 1.00 44.49  ? 2896 ARG A NH2   1 
ATOM   11443 N  N     . LEU A 1 2897 ? 155.146 159.836 217.881 1.00 30.03  ? 2897 LEU A N     1 
ATOM   11444 C  CA    . LEU A 1 2897 ? 154.853 158.926 216.779 1.00 32.01  ? 2897 LEU A CA    1 
ATOM   11445 C  C     . LEU A 1 2897 ? 153.702 157.992 217.128 1.00 36.43  ? 2897 LEU A C     1 
ATOM   11446 O  O     . LEU A 1 2897 ? 152.902 157.631 216.257 1.00 38.09  ? 2897 LEU A O     1 
ATOM   11447 C  CB    . LEU A 1 2897 ? 156.103 158.124 216.414 1.00 33.31  ? 2897 LEU A CB    1 
ATOM   11448 C  CG    . LEU A 1 2897 ? 156.962 158.674 215.274 1.00 35.79  ? 2897 LEU A CG    1 
ATOM   11449 C  CD1   . LEU A 1 2897 ? 158.138 157.751 214.998 1.00 31.33  ? 2897 LEU A CD1   1 
ATOM   11450 C  CD2   . LEU A 1 2897 ? 156.131 158.879 214.017 1.00 33.27  ? 2897 LEU A CD2   1 
ATOM   11451 N  N     . LYS A 1 2898 ? 153.606 157.586 218.396 1.00 39.74  ? 2898 LYS A N     1 
ATOM   11452 C  CA    . LYS A 1 2898 ? 152.497 156.743 218.829 1.00 39.32  ? 2898 LYS A CA    1 
ATOM   11453 C  C     . LYS A 1 2898 ? 151.163 157.454 218.638 1.00 37.71  ? 2898 LYS A C     1 
ATOM   11454 O  O     . LYS A 1 2898 ? 150.186 156.856 218.173 1.00 40.41  ? 2898 LYS A O     1 
ATOM   11455 C  CB    . LYS A 1 2898 ? 152.691 156.336 220.290 1.00 39.55  ? 2898 LYS A CB    1 
ATOM   11456 C  CG    . LYS A 1 2898 ? 151.730 155.262 220.771 1.00 44.71  ? 2898 LYS A CG    1 
ATOM   11457 C  CD    . LYS A 1 2898 ? 151.920 154.929 222.249 1.00 46.14  ? 2898 LYS A CD    1 
ATOM   11458 C  CE    . LYS A 1 2898 ? 151.396 156.026 223.172 1.00 51.42  ? 2898 LYS A CE    1 
ATOM   11459 N  NZ    . LYS A 1 2898 ? 152.294 157.212 223.280 1.00 44.99  ? 2898 LYS A NZ    1 
ATOM   11460 N  N     . VAL A 1 2899 ? 151.105 158.738 218.995 1.00 37.72  ? 2899 VAL A N     1 
ATOM   11461 C  CA    . VAL A 1 2899 ? 149.903 159.527 218.739 1.00 38.95  ? 2899 VAL A CA    1 
ATOM   11462 C  C     . VAL A 1 2899 ? 149.713 159.732 217.242 1.00 41.96  ? 2899 VAL A C     1 
ATOM   11463 O  O     . VAL A 1 2899 ? 148.581 159.789 216.746 1.00 44.71  ? 2899 VAL A O     1 
ATOM   11464 C  CB    . VAL A 1 2899 ? 149.970 160.869 219.490 1.00 37.03  ? 2899 VAL A CB    1 
ATOM   11465 C  CG1   . VAL A 1 2899 ? 148.595 161.511 219.550 1.00 32.26  ? 2899 VAL A CG1   1 
ATOM   11466 C  CG2   . VAL A 1 2899 ? 150.525 160.666 220.889 1.00 41.41  ? 2899 VAL A CG2   1 
ATOM   11467 N  N     . PHE A 1 2900 ? 150.817 159.857 216.502 1.00 40.62  ? 2900 PHE A N     1 
ATOM   11468 C  CA    . PHE A 1 2900 ? 150.731 160.062 215.059 1.00 34.90  ? 2900 PHE A CA    1 
ATOM   11469 C  C     . PHE A 1 2900 ? 150.084 158.868 214.366 1.00 38.49  ? 2900 PHE A C     1 
ATOM   11470 O  O     . PHE A 1 2900 ? 149.290 159.039 213.434 1.00 37.93  ? 2900 PHE A O     1 
ATOM   11471 C  CB    . PHE A 1 2900 ? 152.124 160.329 214.488 1.00 32.38  ? 2900 PHE A CB    1 
ATOM   11472 C  CG    . PHE A 1 2900 ? 152.127 160.660 213.023 1.00 29.65  ? 2900 PHE A CG    1 
ATOM   11473 C  CD1   . PHE A 1 2900 ? 151.527 161.818 212.559 1.00 26.58  ? 2900 PHE A CD1   1 
ATOM   11474 C  CD2   . PHE A 1 2900 ? 152.730 159.812 212.110 1.00 29.36  ? 2900 PHE A CD2   1 
ATOM   11475 C  CE1   . PHE A 1 2900 ? 151.530 162.126 211.213 1.00 25.33  ? 2900 PHE A CE1   1 
ATOM   11476 C  CE2   . PHE A 1 2900 ? 152.735 160.113 210.762 1.00 24.08  ? 2900 PHE A CE2   1 
ATOM   11477 C  CZ    . PHE A 1 2900 ? 152.134 161.271 210.313 1.00 26.06  ? 2900 PHE A CZ    1 
ATOM   11478 N  N     . TYR A 1 2901 ? 150.420 157.650 214.801 1.00 38.61  ? 2901 TYR A N     1 
ATOM   11479 C  CA    . TYR A 1 2901 ? 149.832 156.460 214.190 1.00 38.32  ? 2901 TYR A CA    1 
ATOM   11480 C  C     . TYR A 1 2901 ? 148.328 156.397 214.425 1.00 45.29  ? 2901 TYR A C     1 
ATOM   11481 O  O     . TYR A 1 2901 ? 147.561 156.085 213.507 1.00 50.30  ? 2901 TYR A O     1 
ATOM   11482 C  CB    . TYR A 1 2901 ? 150.500 155.194 214.728 1.00 39.19  ? 2901 TYR A CB    1 
ATOM   11483 C  CG    . TYR A 1 2901 ? 152.000 155.148 214.559 1.00 38.73  ? 2901 TYR A CG    1 
ATOM   11484 C  CD1   . TYR A 1 2901 ? 152.604 155.631 213.407 1.00 39.08  ? 2901 TYR A CD1   1 
ATOM   11485 C  CD2   . TYR A 1 2901 ? 152.810 154.597 215.542 1.00 34.17  ? 2901 TYR A CD2   1 
ATOM   11486 C  CE1   . TYR A 1 2901 ? 153.976 155.585 213.248 1.00 36.75  ? 2901 TYR A CE1   1 
ATOM   11487 C  CE2   . TYR A 1 2901 ? 154.182 154.545 215.391 1.00 37.27  ? 2901 TYR A CE2   1 
ATOM   11488 C  CZ    . TYR A 1 2901 ? 154.759 155.039 214.242 1.00 39.41  ? 2901 TYR A CZ    1 
ATOM   11489 O  OH    . TYR A 1 2901 ? 156.125 154.987 214.089 1.00 37.33  ? 2901 TYR A OH    1 
ATOM   11490 N  N     . GLU A 1 2902 ? 147.886 156.688 215.649 1.00 47.22  ? 2902 GLU A N     1 
ATOM   11491 C  CA    . GLU A 1 2902 ? 146.479 156.531 215.992 1.00 48.32  ? 2902 GLU A CA    1 
ATOM   11492 C  C     . GLU A 1 2902 ? 145.608 157.666 215.476 1.00 49.19  ? 2902 GLU A C     1 
ATOM   11493 O  O     . GLU A 1 2902 ? 144.380 157.576 215.587 1.00 58.47  ? 2902 GLU A O     1 
ATOM   11494 C  CB    . GLU A 1 2902 ? 146.316 156.414 217.509 1.00 49.02  ? 2902 GLU A CB    1 
ATOM   11495 C  CG    . GLU A 1 2902 ? 146.586 157.702 218.271 1.00 54.23  ? 2902 GLU A CG    1 
ATOM   11496 C  CD    . GLU A 1 2902 ? 147.091 157.449 219.678 1.00 61.49  ? 2902 GLU A CD    1 
ATOM   11497 O  OE1   . GLU A 1 2902 ? 147.262 156.269 220.047 1.00 68.32  ? 2902 GLU A OE1   1 
ATOM   11498 O  OE2   . GLU A 1 2902 ? 147.311 158.430 220.420 1.00 55.59  ? 2902 GLU A OE2   1 
ATOM   11499 N  N     . GLU A 1 2903 ? 146.196 158.719 214.921 1.00 46.55  ? 2903 GLU A N     1 
ATOM   11500 C  CA    . GLU A 1 2903 ? 145.428 159.883 214.495 1.00 47.94  ? 2903 GLU A CA    1 
ATOM   11501 C  C     . GLU A 1 2903 ? 145.504 160.156 213.002 1.00 47.50  ? 2903 GLU A C     1 
ATOM   11502 O  O     . GLU A 1 2903 ? 144.470 160.409 212.378 1.00 48.47  ? 2903 GLU A O     1 
ATOM   11503 C  CB    . GLU A 1 2903 ? 145.897 161.130 215.261 1.00 50.27  ? 2903 GLU A CB    1 
ATOM   11504 C  CG    . GLU A 1 2903 ? 144.768 162.049 215.693 1.00 55.88  ? 2903 GLU A CG    1 
ATOM   11505 C  CD    . GLU A 1 2903 ? 144.465 163.122 214.668 1.00 62.22  ? 2903 GLU A CD    1 
ATOM   11506 O  OE1   . GLU A 1 2903 ? 143.336 163.656 214.682 1.00 64.44  ? 2903 GLU A OE1   1 
ATOM   11507 O  OE2   . GLU A 1 2903 ? 145.355 163.432 213.849 1.00 49.80  ? 2903 GLU A OE2   1 
ATOM   11508 N  N     . GLU A 1 2904 ? 146.695 160.114 212.405 1.00 45.38  ? 2904 GLU A N     1 
ATOM   11509 C  CA    . GLU A 1 2904 ? 146.875 160.514 211.015 1.00 40.28  ? 2904 GLU A CA    1 
ATOM   11510 C  C     . GLU A 1 2904 ? 147.278 159.356 210.111 1.00 40.89  ? 2904 GLU A C     1 
ATOM   11511 O  O     . GLU A 1 2904 ? 146.600 159.086 209.115 1.00 46.34  ? 2904 GLU A O     1 
ATOM   11512 C  CB    . GLU A 1 2904 ? 147.917 161.637 210.929 1.00 34.29  ? 2904 GLU A CB    1 
ATOM   11513 C  CG    . GLU A 1 2904 ? 147.392 163.000 211.333 1.00 40.73  ? 2904 GLU A CG    1 
ATOM   11514 C  CD    . GLU A 1 2904 ? 146.590 163.662 210.231 1.00 48.11  ? 2904 GLU A CD    1 
ATOM   11515 O  OE1   . GLU A 1 2904 ? 146.763 163.276 209.056 1.00 50.39  ? 2904 GLU A OE1   1 
ATOM   11516 O  OE2   . GLU A 1 2904 ? 145.787 164.567 210.540 1.00 51.20  ? 2904 GLU A OE2   1 
ATOM   11517 N  N     . LEU A 1 2905 ? 148.367 158.659 210.429 1.00 40.30  ? 2905 LEU A N     1 
ATOM   11518 C  CA    . LEU A 1 2905 ? 148.931 157.660 209.528 1.00 40.00  ? 2905 LEU A CA    1 
ATOM   11519 C  C     . LEU A 1 2905 ? 149.506 156.519 210.349 1.00 39.62  ? 2905 LEU A C     1 
ATOM   11520 O  O     . LEU A 1 2905 ? 150.482 156.711 211.080 1.00 42.77  ? 2905 LEU A O     1 
ATOM   11521 C  CB    . LEU A 1 2905 ? 150.012 158.280 208.639 1.00 39.16  ? 2905 LEU A CB    1 
ATOM   11522 C  CG    . LEU A 1 2905 ? 150.498 157.440 207.461 1.00 34.45  ? 2905 LEU A CG    1 
ATOM   11523 C  CD1   . LEU A 1 2905 ? 149.363 157.246 206.478 1.00 36.73  ? 2905 LEU A CD1   1 
ATOM   11524 C  CD2   . LEU A 1 2905 ? 151.688 158.100 206.787 1.00 29.84  ? 2905 LEU A CD2   1 
ATOM   11525 N  N     . ASP A 1 2906 ? 148.915 155.333 210.216 1.00 38.63  ? 2906 ASP A N     1 
ATOM   11526 C  CA    . ASP A 1 2906 ? 149.332 154.167 210.996 1.00 42.58  ? 2906 ASP A CA    1 
ATOM   11527 C  C     . ASP A 1 2906 ? 150.339 153.325 210.208 1.00 46.92  ? 2906 ASP A C     1 
ATOM   11528 O  O     . ASP A 1 2906 ? 150.088 152.185 209.820 1.00 45.25  ? 2906 ASP A O     1 
ATOM   11529 C  CB    . ASP A 1 2906 ? 148.113 153.347 211.406 1.00 51.45  ? 2906 ASP A CB    1 
ATOM   11530 C  CG    . ASP A 1 2906 ? 148.467 152.183 212.314 1.00 60.87  ? 2906 ASP A CG    1 
ATOM   11531 O  OD1   . ASP A 1 2906 ? 147.649 151.248 212.427 1.00 69.43  ? 2906 ASP A OD1   1 
ATOM   11532 O  OD2   . ASP A 1 2906 ? 149.562 152.203 212.915 1.00 54.56  ? 2906 ASP A OD2   1 
ATOM   11533 N  N     . VAL A 1 2907 ? 151.497 153.923 209.969 1.00 45.35  ? 2907 VAL A N     1 
ATOM   11534 C  CA    . VAL A 1 2907 ? 152.625 153.256 209.335 1.00 38.84  ? 2907 VAL A CA    1 
ATOM   11535 C  C     . VAL A 1 2907 ? 153.798 153.288 210.306 1.00 36.27  ? 2907 VAL A C     1 
ATOM   11536 O  O     . VAL A 1 2907 ? 154.461 154.314 210.461 1.00 40.70  ? 2907 VAL A O     1 
ATOM   11537 C  CB    . VAL A 1 2907 ? 152.994 153.918 207.995 1.00 36.27  ? 2907 VAL A CB    1 
ATOM   11538 C  CG1   . VAL A 1 2907 ? 154.231 153.263 207.404 1.00 34.98  ? 2907 VAL A CG1   1 
ATOM   11539 C  CG2   . VAL A 1 2907 ? 151.828 153.838 207.023 1.00 35.61  ? 2907 VAL A CG2   1 
ATOM   11540 N  N     . PRO A 1 2908 ? 154.071 152.181 210.998 1.00 37.96  ? 2908 PRO A N     1 
ATOM   11541 C  CA    . PRO A 1 2908 ? 155.162 152.175 211.981 1.00 31.71  ? 2908 PRO A CA    1 
ATOM   11542 C  C     . PRO A 1 2908 ? 156.499 152.511 211.338 1.00 31.87  ? 2908 PRO A C     1 
ATOM   11543 O  O     . PRO A 1 2908 ? 156.802 152.076 210.225 1.00 37.01  ? 2908 PRO A O     1 
ATOM   11544 C  CB    . PRO A 1 2908 ? 155.142 150.741 212.521 1.00 27.42  ? 2908 PRO A CB    1 
ATOM   11545 C  CG    . PRO A 1 2908 ? 153.752 150.260 212.262 1.00 29.72  ? 2908 PRO A CG    1 
ATOM   11546 C  CD    . PRO A 1 2908 ? 153.343 150.902 210.971 1.00 36.34  ? 2908 PRO A CD    1 
ATOM   11547 N  N     . LEU A 1 2909 ? 157.300 153.294 212.055 1.00 28.75  ? 2909 LEU A N     1 
ATOM   11548 C  CA    . LEU A 1 2909 ? 158.598 153.748 211.578 1.00 25.48  ? 2909 LEU A CA    1 
ATOM   11549 C  C     . LEU A 1 2909 ? 159.678 153.338 212.567 1.00 27.27  ? 2909 LEU A C     1 
ATOM   11550 O  O     . LEU A 1 2909 ? 159.496 153.470 213.782 1.00 28.73  ? 2909 LEU A O     1 
ATOM   11551 C  CB    . LEU A 1 2909 ? 158.618 155.267 211.385 1.00 26.00  ? 2909 LEU A CB    1 
ATOM   11552 C  CG    . LEU A 1 2909 ? 157.493 155.884 210.554 1.00 24.72  ? 2909 LEU A CG    1 
ATOM   11553 C  CD1   . LEU A 1 2909 ? 157.712 157.379 210.395 1.00 30.37  ? 2909 LEU A CD1   1 
ATOM   11554 C  CD2   . LEU A 1 2909 ? 157.400 155.209 209.196 1.00 22.72  ? 2909 LEU A CD2   1 
ATOM   11555 N  N     . VAL A 1 2910 ? 160.796 152.845 212.045 1.00 26.25  ? 2910 VAL A N     1 
ATOM   11556 C  CA    . VAL A 1 2910 ? 161.951 152.526 212.875 1.00 26.28  ? 2910 VAL A CA    1 
ATOM   11557 C  C     . VAL A 1 2910 ? 162.792 153.783 213.040 1.00 26.70  ? 2910 VAL A C     1 
ATOM   11558 O  O     . VAL A 1 2910 ? 163.182 154.419 212.052 1.00 31.44  ? 2910 VAL A O     1 
ATOM   11559 C  CB    . VAL A 1 2910 ? 162.768 151.382 212.256 1.00 28.71  ? 2910 VAL A CB    1 
ATOM   11560 C  CG1   . VAL A 1 2910 ? 164.033 151.135 213.064 1.00 32.89  ? 2910 VAL A CG1   1 
ATOM   11561 C  CG2   . VAL A 1 2910 ? 161.929 150.117 212.169 1.00 23.65  ? 2910 VAL A CG2   1 
ATOM   11562 N  N     . LEU A 1 2911 ? 163.073 154.148 214.287 1.00 23.72  ? 2911 LEU A N     1 
ATOM   11563 C  CA    . LEU A 1 2911 ? 163.786 155.382 214.589 1.00 26.37  ? 2911 LEU A CA    1 
ATOM   11564 C  C     . LEU A 1 2911 ? 165.279 155.103 214.709 1.00 31.67  ? 2911 LEU A C     1 
ATOM   11565 O  O     . LEU A 1 2911 ? 165.702 154.320 215.566 1.00 40.11  ? 2911 LEU A O     1 
ATOM   11566 C  CB    . LEU A 1 2911 ? 163.258 156.011 215.877 1.00 26.83  ? 2911 LEU A CB    1 
ATOM   11567 C  CG    . LEU A 1 2911 ? 161.915 156.737 215.797 1.00 26.38  ? 2911 LEU A CG    1 
ATOM   11568 C  CD1   . LEU A 1 2911 ? 161.648 157.498 217.081 1.00 30.83  ? 2911 LEU A CD1   1 
ATOM   11569 C  CD2   . LEU A 1 2911 ? 161.879 157.673 214.605 1.00 29.23  ? 2911 LEU A CD2   1 
ATOM   11570 N  N     . PHE A 1 2912 ? 166.070 155.742 213.853 1.00 25.44  ? 2912 PHE A N     1 
ATOM   11571 C  CA    . PHE A 1 2912 ? 167.519 155.750 213.981 1.00 27.53  ? 2912 PHE A CA    1 
ATOM   11572 C  C     . PHE A 1 2912 ? 168.002 157.193 214.016 1.00 29.71  ? 2912 PHE A C     1 
ATOM   11573 O  O     . PHE A 1 2912 ? 167.223 158.137 213.857 1.00 28.95  ? 2912 PHE A O     1 
ATOM   11574 C  CB    . PHE A 1 2912 ? 168.206 154.953 212.857 1.00 27.40  ? 2912 PHE A CB    1 
ATOM   11575 C  CG    . PHE A 1 2912 ? 167.750 155.310 211.469 1.00 27.38  ? 2912 PHE A CG    1 
ATOM   11576 C  CD1   . PHE A 1 2912 ? 168.497 156.166 210.678 1.00 28.36  ? 2912 PHE A CD1   1 
ATOM   11577 C  CD2   . PHE A 1 2912 ? 166.596 154.757 210.940 1.00 23.70  ? 2912 PHE A CD2   1 
ATOM   11578 C  CE1   . PHE A 1 2912 ? 168.088 156.480 209.396 1.00 25.17  ? 2912 PHE A CE1   1 
ATOM   11579 C  CE2   . PHE A 1 2912 ? 166.185 155.065 209.660 1.00 19.89  ? 2912 PHE A CE2   1 
ATOM   11580 C  CZ    . PHE A 1 2912 ? 166.932 155.929 208.887 1.00 20.47  ? 2912 PHE A CZ    1 
ATOM   11581 N  N     . ASN A 1 2913 ? 169.309 157.356 214.241 1.00 29.64  ? 2913 ASN A N     1 
ATOM   11582 C  CA    . ASN A 1 2913 ? 169.856 158.679 214.533 1.00 28.48  ? 2913 ASN A CA    1 
ATOM   11583 C  C     . ASN A 1 2913 ? 169.654 159.645 213.372 1.00 30.28  ? 2913 ASN A C     1 
ATOM   11584 O  O     . ASN A 1 2913 ? 169.370 160.829 213.587 1.00 31.77  ? 2913 ASN A O     1 
ATOM   11585 C  CB    . ASN A 1 2913 ? 171.338 158.563 214.888 1.00 30.81  ? 2913 ASN A CB    1 
ATOM   11586 C  CG    . ASN A 1 2913 ? 171.589 157.576 216.009 1.00 33.45  ? 2913 ASN A CG    1 
ATOM   11587 O  OD1   . ASN A 1 2913 ? 170.652 157.041 216.600 1.00 33.65  ? 2913 ASN A OD1   1 
ATOM   11588 N  ND2   . ASN A 1 2913 ? 172.859 157.330 216.308 1.00 28.42  ? 2913 ASN A ND2   1 
ATOM   11589 N  N     . GLU A 1 2914 ? 169.800 159.164 212.135 1.00 28.64  ? 2914 GLU A N     1 
ATOM   11590 C  CA    . GLU A 1 2914 ? 169.617 160.046 210.986 1.00 25.83  ? 2914 GLU A CA    1 
ATOM   11591 C  C     . GLU A 1 2914 ? 168.183 160.548 210.880 1.00 27.92  ? 2914 GLU A C     1 
ATOM   11592 O  O     . GLU A 1 2914 ? 167.953 161.665 210.403 1.00 27.99  ? 2914 GLU A O     1 
ATOM   11593 C  CB    . GLU A 1 2914 ? 170.032 159.333 209.699 1.00 26.76  ? 2914 GLU A CB    1 
ATOM   11594 C  CG    . GLU A 1 2914 ? 171.512 158.997 209.629 1.00 36.96  ? 2914 GLU A CG    1 
ATOM   11595 C  CD    . GLU A 1 2914 ? 171.831 157.969 208.562 1.00 42.69  ? 2914 GLU A CD    1 
ATOM   11596 O  OE1   . GLU A 1 2914 ? 172.818 157.223 208.733 1.00 39.83  ? 2914 GLU A OE1   1 
ATOM   11597 O  OE2   . GLU A 1 2914 ? 171.098 157.907 207.553 1.00 35.10  ? 2914 GLU A OE2   1 
ATOM   11598 N  N     . VAL A 1 2915 ? 167.207 159.745 211.313 1.00 24.93  ? 2915 VAL A N     1 
ATOM   11599 C  CA    . VAL A 1 2915 ? 165.821 160.209 211.320 1.00 22.71  ? 2915 VAL A CA    1 
ATOM   11600 C  C     . VAL A 1 2915 ? 165.654 161.372 212.288 1.00 25.52  ? 2915 VAL A C     1 
ATOM   11601 O  O     . VAL A 1 2915 ? 165.035 162.389 211.956 1.00 28.25  ? 2915 VAL A O     1 
ATOM   11602 C  CB    . VAL A 1 2915 ? 164.862 159.053 211.656 1.00 21.08  ? 2915 VAL A CB    1 
ATOM   11603 C  CG1   . VAL A 1 2915 ? 163.486 159.595 211.995 1.00 21.06  ? 2915 VAL A CG1   1 
ATOM   11604 C  CG2   . VAL A 1 2915 ? 164.760 158.103 210.488 1.00 22.08  ? 2915 VAL A CG2   1 
ATOM   11605 N  N     . LEU A 1 2916 ? 166.219 161.250 213.492 1.00 24.16  ? 2916 LEU A N     1 
ATOM   11606 C  CA    . LEU A 1 2916 ? 166.090 162.316 214.480 1.00 24.54  ? 2916 LEU A CA    1 
ATOM   11607 C  C     . LEU A 1 2916 ? 166.686 163.618 213.965 1.00 32.15  ? 2916 LEU A C     1 
ATOM   11608 O  O     . LEU A 1 2916 ? 166.120 164.697 214.178 1.00 33.18  ? 2916 LEU A O     1 
ATOM   11609 C  CB    . LEU A 1 2916 ? 166.757 161.904 215.792 1.00 26.25  ? 2916 LEU A CB    1 
ATOM   11610 C  CG    . LEU A 1 2916 ? 166.306 160.581 216.413 1.00 26.32  ? 2916 LEU A CG    1 
ATOM   11611 C  CD1   . LEU A 1 2916 ? 166.921 160.403 217.792 1.00 27.18  ? 2916 LEU A CD1   1 
ATOM   11612 C  CD2   . LEU A 1 2916 ? 164.790 160.516 216.489 1.00 29.11  ? 2916 LEU A CD2   1 
ATOM   11613 N  N     . ASP A 1 2917 ? 167.831 163.538 213.284 1.00 30.15  ? 2917 ASP A N     1 
ATOM   11614 C  CA    . ASP A 1 2917 ? 168.427 164.730 212.692 1.00 26.31  ? 2917 ASP A CA    1 
ATOM   11615 C  C     . ASP A 1 2917 ? 167.526 165.313 211.609 1.00 21.57  ? 2917 ASP A C     1 
ATOM   11616 O  O     . ASP A 1 2917 ? 167.360 166.534 211.514 1.00 22.39  ? 2917 ASP A O     1 
ATOM   11617 C  CB    . ASP A 1 2917 ? 169.808 164.394 212.127 1.00 28.77  ? 2917 ASP A CB    1 
ATOM   11618 C  CG    . ASP A 1 2917 ? 170.781 165.554 212.232 1.00 35.77  ? 2917 ASP A CG    1 
ATOM   11619 O  OD1   . ASP A 1 2917 ? 171.367 165.742 213.318 1.00 30.22  ? 2917 ASP A OD1   1 
ATOM   11620 O  OD2   . ASP A 1 2917 ? 170.960 166.278 211.232 1.00 30.89  ? 2917 ASP A OD2   1 
ATOM   11621 N  N     . HIS A 1 2918 ? 166.928 164.448 210.783 1.00 21.63  ? 2918 HIS A N     1 
ATOM   11622 C  CA    . HIS A 1 2918 ? 166.114 164.924 209.666 1.00 20.86  ? 2918 HIS A CA    1 
ATOM   11623 C  C     . HIS A 1 2918 ? 164.844 165.620 210.142 1.00 20.54  ? 2918 HIS A C     1 
ATOM   11624 O  O     . HIS A 1 2918 ? 164.498 166.693 209.636 1.00 21.02  ? 2918 HIS A O     1 
ATOM   11625 C  CB    . HIS A 1 2918 ? 165.769 163.766 208.730 1.00 21.35  ? 2918 HIS A CB    1 
ATOM   11626 C  CG    . HIS A 1 2918 ? 166.946 163.218 207.984 1.00 21.93  ? 2918 HIS A CG    1 
ATOM   11627 N  ND1   . HIS A 1 2918 ? 166.969 161.942 207.464 1.00 22.09  ? 2918 HIS A ND1   1 
ATOM   11628 C  CD2   . HIS A 1 2918 ? 168.137 163.777 207.665 1.00 22.67  ? 2918 HIS A CD2   1 
ATOM   11629 C  CE1   . HIS A 1 2918 ? 168.125 161.737 206.858 1.00 22.19  ? 2918 HIS A CE1   1 
ATOM   11630 N  NE2   . HIS A 1 2918 ? 168.852 162.835 206.966 1.00 23.14  ? 2918 HIS A NE2   1 
ATOM   11631 N  N     . VAL A 1 2919 ? 164.127 165.025 211.099 1.00 20.84  ? 2919 VAL A N     1 
ATOM   11632 C  CA    . VAL A 1 2919 ? 162.900 165.656 211.581 1.00 18.71  ? 2919 VAL A CA    1 
ATOM   11633 C  C     . VAL A 1 2919 ? 163.203 166.984 212.263 1.00 15.15  ? 2919 VAL A C     1 
ATOM   11634 O  O     . VAL A 1 2919 ? 162.348 167.876 212.303 1.00 19.88  ? 2919 VAL A O     1 
ATOM   11635 C  CB    . VAL A 1 2919 ? 162.113 164.703 212.502 1.00 18.70  ? 2919 VAL A CB    1 
ATOM   11636 C  CG1   . VAL A 1 2919 ? 162.082 163.300 211.921 1.00 15.67  ? 2919 VAL A CG1   1 
ATOM   11637 C  CG2   . VAL A 1 2919 ? 162.708 164.682 213.901 1.00 22.30  ? 2919 VAL A CG2   1 
ATOM   11638 N  N     . LEU A 1 2920 ? 164.412 167.145 212.807 1.00 15.32  ? 2920 LEU A N     1 
ATOM   11639 C  CA    . LEU A 1 2920 ? 164.791 168.434 213.375 1.00 16.33  ? 2920 LEU A CA    1 
ATOM   11640 C  C     . LEU A 1 2920 ? 165.071 169.456 212.280 1.00 15.72  ? 2920 LEU A C     1 
ATOM   11641 O  O     . LEU A 1 2920 ? 164.733 170.637 212.422 1.00 17.41  ? 2920 LEU A O     1 
ATOM   11642 C  CB    . LEU A 1 2920 ? 166.006 168.271 214.288 1.00 17.05  ? 2920 LEU A CB    1 
ATOM   11643 C  CG    . LEU A 1 2920 ? 165.742 167.596 215.635 1.00 15.24  ? 2920 LEU A CG    1 
ATOM   11644 C  CD1   . LEU A 1 2920 ? 166.938 167.750 216.559 1.00 19.58  ? 2920 LEU A CD1   1 
ATOM   11645 C  CD2   . LEU A 1 2920 ? 164.489 168.161 216.282 1.00 18.03  ? 2920 LEU A CD2   1 
ATOM   11646 N  N     . ARG A 1 2921 ? 165.696 169.023 211.182 1.00 17.44  ? 2921 ARG A N     1 
ATOM   11647 C  CA    . ARG A 1 2921 ? 165.916 169.924 210.055 1.00 13.83  ? 2921 ARG A CA    1 
ATOM   11648 C  C     . ARG A 1 2921 ? 164.596 170.349 209.425 1.00 15.24  ? 2921 ARG A C     1 
ATOM   11649 O  O     . ARG A 1 2921 ? 164.415 171.521 209.075 1.00 19.54  ? 2921 ARG A O     1 
ATOM   11650 C  CB    . ARG A 1 2921 ? 166.811 169.261 209.010 1.00 14.42  ? 2921 ARG A CB    1 
ATOM   11651 C  CG    . ARG A 1 2921 ? 168.184 168.852 209.510 1.00 16.69  ? 2921 ARG A CG    1 
ATOM   11652 C  CD    . ARG A 1 2921 ? 168.898 168.026 208.458 1.00 16.79  ? 2921 ARG A CD    1 
ATOM   11653 N  NE    . ARG A 1 2921 ? 169.955 167.188 209.007 1.00 22.17  ? 2921 ARG A NE    1 
ATOM   11654 C  CZ    . ARG A 1 2921 ? 170.746 166.414 208.275 1.00 27.47  ? 2921 ARG A CZ    1 
ATOM   11655 N  NH1   . ARG A 1 2921 ? 170.629 166.355 206.959 1.00 25.86  ? 2921 ARG A NH1   1 
ATOM   11656 N  NH2   . ARG A 1 2921 ? 171.678 165.683 208.880 1.00 28.73  ? 2921 ARG A NH2   1 
ATOM   11657 N  N     . ILE A 1 2922 ? 163.667 169.405 209.263 1.00 14.10  ? 2922 ILE A N     1 
ATOM   11658 C  CA    . ILE A 1 2922 ? 162.364 169.731 208.694 1.00 16.02  ? 2922 ILE A CA    1 
ATOM   11659 C  C     . ILE A 1 2922 ? 161.601 170.674 209.616 1.00 16.78  ? 2922 ILE A C     1 
ATOM   11660 O  O     . ILE A 1 2922 ? 160.940 171.614 209.158 1.00 17.65  ? 2922 ILE A O     1 
ATOM   11661 C  CB    . ILE A 1 2922 ? 161.571 168.441 208.412 1.00 15.93  ? 2922 ILE A CB    1 
ATOM   11662 C  CG1   . ILE A 1 2922 ? 162.298 167.588 207.372 1.00 13.85  ? 2922 ILE A CG1   1 
ATOM   11663 C  CG2   . ILE A 1 2922 ? 160.166 168.764 207.933 1.00 15.56  ? 2922 ILE A CG2   1 
ATOM   11664 C  CD1   . ILE A 1 2922 ? 161.687 166.223 207.172 1.00 17.36  ? 2922 ILE A CD1   1 
ATOM   11665 N  N     . ASP A 1 2923 ? 161.683 170.441 210.928 1.00 17.18  ? 2923 ASP A N     1 
ATOM   11666 C  CA    . ASP A 1 2923 ? 161.010 171.315 211.885 1.00 18.39  ? 2923 ASP A CA    1 
ATOM   11667 C  C     . ASP A 1 2923 ? 161.564 172.732 211.821 1.00 20.89  ? 2923 ASP A C     1 
ATOM   11668 O  O     . ASP A 1 2923 ? 160.828 173.705 212.025 1.00 23.45  ? 2923 ASP A O     1 
ATOM   11669 C  CB    . ASP A 1 2923 ? 161.151 170.748 213.297 1.00 19.86  ? 2923 ASP A CB    1 
ATOM   11670 C  CG    . ASP A 1 2923 ? 160.386 171.551 214.327 1.00 29.50  ? 2923 ASP A CG    1 
ATOM   11671 O  OD1   . ASP A 1 2923 ? 159.141 171.581 214.250 1.00 30.70  ? 2923 ASP A OD1   1 
ATOM   11672 O  OD2   . ASP A 1 2923 ? 161.027 172.152 215.214 1.00 30.98  ? 2923 ASP A OD2   1 
ATOM   11673 N  N     . ARG A 1 2924 ? 162.862 172.867 211.546 1.00 22.13  ? 2924 ARG A N     1 
ATOM   11674 C  CA    . ARG A 1 2924 ? 163.481 174.186 211.470 1.00 18.57  ? 2924 ARG A CA    1 
ATOM   11675 C  C     . ARG A 1 2924 ? 162.885 175.012 210.337 1.00 17.83  ? 2924 ARG A C     1 
ATOM   11676 O  O     . ARG A 1 2924 ? 162.551 176.188 210.518 1.00 20.69  ? 2924 ARG A O     1 
ATOM   11677 C  CB    . ARG A 1 2924 ? 164.991 174.035 211.287 1.00 17.84  ? 2924 ARG A CB    1 
ATOM   11678 C  CG    . ARG A 1 2924 ? 165.767 173.897 212.581 1.00 21.47  ? 2924 ARG A CG    1 
ATOM   11679 C  CD    . ARG A 1 2924 ? 167.255 173.748 212.310 1.00 17.46  ? 2924 ARG A CD    1 
ATOM   11680 N  NE    . ARG A 1 2924 ? 167.669 174.481 211.120 1.00 19.65  ? 2924 ARG A NE    1 
ATOM   11681 C  CZ    . ARG A 1 2924 ? 168.442 175.557 211.136 1.00 25.89  ? 2924 ARG A CZ    1 
ATOM   11682 N  NH1   . ARG A 1 2924 ? 168.905 176.059 212.270 1.00 27.79  ? 2924 ARG A NH1   1 
ATOM   11683 N  NH2   . ARG A 1 2924 ? 168.759 176.146 209.987 1.00 30.15  ? 2924 ARG A NH2   1 
ATOM   11684 N  N     . ILE A 1 2925 ? 162.744 174.408 209.157 1.00 20.02  ? 2925 ILE A N     1 
ATOM   11685 C  CA    . ILE A 1 2925 ? 162.273 175.148 207.990 1.00 18.27  ? 2925 ILE A CA    1 
ATOM   11686 C  C     . ILE A 1 2925 ? 160.777 175.421 208.090 1.00 18.06  ? 2925 ILE A C     1 
ATOM   11687 O  O     . ILE A 1 2925 ? 160.300 176.488 207.685 1.00 25.24  ? 2925 ILE A O     1 
ATOM   11688 C  CB    . ILE A 1 2925 ? 162.636 174.388 206.703 1.00 17.53  ? 2925 ILE A CB    1 
ATOM   11689 C  CG1   . ILE A 1 2925 ? 164.147 174.156 206.642 1.00 16.80  ? 2925 ILE A CG1   1 
ATOM   11690 C  CG2   . ILE A 1 2925 ? 162.168 175.150 205.477 1.00 15.40  ? 2925 ILE A CG2   1 
ATOM   11691 C  CD1   . ILE A 1 2925 ? 164.971 175.398 206.909 1.00 16.91  ? 2925 ILE A CD1   1 
ATOM   11692 N  N     . PHE A 1 2926 ? 160.012 174.470 208.632 1.00 18.34  ? 2926 PHE A N     1 
ATOM   11693 C  CA    . PHE A 1 2926 ? 158.575 174.666 208.787 1.00 15.61  ? 2926 PHE A CA    1 
ATOM   11694 C  C     . PHE A 1 2926 ? 158.244 175.804 209.743 1.00 20.23  ? 2926 PHE A C     1 
ATOM   11695 O  O     . PHE A 1 2926 ? 157.110 176.296 209.733 1.00 21.95  ? 2926 PHE A O     1 
ATOM   11696 C  CB    . PHE A 1 2926 ? 157.914 173.375 209.274 1.00 15.71  ? 2926 PHE A CB    1 
ATOM   11697 C  CG    . PHE A 1 2926 ? 157.596 172.403 208.175 1.00 14.93  ? 2926 PHE A CG    1 
ATOM   11698 C  CD1   . PHE A 1 2926 ? 157.672 172.787 206.847 1.00 15.97  ? 2926 PHE A CD1   1 
ATOM   11699 C  CD2   . PHE A 1 2926 ? 157.210 171.108 208.472 1.00 18.47  ? 2926 PHE A CD2   1 
ATOM   11700 C  CE1   . PHE A 1 2926 ? 157.376 171.894 205.837 1.00 20.74  ? 2926 PHE A CE1   1 
ATOM   11701 C  CE2   . PHE A 1 2926 ? 156.911 170.212 207.466 1.00 20.81  ? 2926 PHE A CE2   1 
ATOM   11702 C  CZ    . PHE A 1 2926 ? 156.995 170.605 206.147 1.00 22.56  ? 2926 PHE A CZ    1 
ATOM   11703 N  N     . ARG A 1 2927 ? 159.201 176.229 210.563 1.00 23.48  ? 2927 ARG A N     1 
ATOM   11704 C  CA    . ARG A 1 2927 ? 159.017 177.337 211.489 1.00 22.54  ? 2927 ARG A CA    1 
ATOM   11705 C  C     . ARG A 1 2927 ? 159.490 178.669 210.921 1.00 25.44  ? 2927 ARG A C     1 
ATOM   11706 O  O     . ARG A 1 2927 ? 159.424 179.683 211.623 1.00 30.19  ? 2927 ARG A O     1 
ATOM   11707 C  CB    . ARG A 1 2927 ? 159.755 177.047 212.799 1.00 22.00  ? 2927 ARG A CB    1 
ATOM   11708 C  CG    . ARG A 1 2927 ? 159.090 175.989 213.665 1.00 28.91  ? 2927 ARG A CG    1 
ATOM   11709 C  CD    . ARG A 1 2927 ? 159.811 175.835 214.993 1.00 30.87  ? 2927 ARG A CD    1 
ATOM   11710 N  NE    . ARG A 1 2927 ? 161.182 175.370 214.816 1.00 32.36  ? 2927 ARG A NE    1 
ATOM   11711 C  CZ    . ARG A 1 2927 ? 162.258 176.116 215.025 1.00 31.72  ? 2927 ARG A CZ    1 
ATOM   11712 N  NH1   . ARG A 1 2927 ? 162.161 177.374 215.422 1.00 29.00  ? 2927 ARG A NH1   1 
ATOM   11713 N  NH2   . ARG A 1 2927 ? 163.462 175.585 214.829 1.00 26.92  ? 2927 ARG A NH2   1 
ATOM   11714 N  N     . GLN A 1 2928 ? 159.967 178.692 209.666 1.00 26.25  ? 2928 GLN A N     1 
ATOM   11715 C  CA    . GLN A 1 2928 ? 160.501 179.891 209.042 1.00 28.43  ? 2928 GLN A CA    1 
ATOM   11716 C  C     . GLN A 1 2928 ? 159.511 180.466 208.036 1.00 28.86  ? 2928 GLN A C     1 
ATOM   11717 O  O     . GLN A 1 2928 ? 158.749 179.723 207.409 1.00 22.93  ? 2928 GLN A O     1 
ATOM   11718 C  CB    . GLN A 1 2928 ? 161.823 179.586 208.331 1.00 26.99  ? 2928 GLN A CB    1 
ATOM   11719 C  CG    . GLN A 1 2928 ? 163.031 179.549 209.250 1.00 30.42  ? 2928 GLN A CG    1 
ATOM   11720 C  CD    . GLN A 1 2928 ? 163.655 180.916 209.444 1.00 42.73  ? 2928 GLN A CD    1 
ATOM   11721 O  OE1   . GLN A 1 2928 ? 163.884 181.352 210.572 1.00 42.65  ? 2928 GLN A OE1   1 
ATOM   11722 N  NE2   . GLN A 1 2928 ? 163.933 181.602 208.342 1.00 43.64  ? 2928 GLN A NE2   1 
ATOM   11723 N  N     . PRO A 1 2929 ? 159.496 181.786 207.861 1.00 32.11  ? 2929 PRO A N     1 
ATOM   11724 C  CA    . PRO A 1 2929 ? 158.608 182.380 206.856 1.00 26.43  ? 2929 PRO A CA    1 
ATOM   11725 C  C     . PRO A 1 2929 ? 159.089 182.074 205.447 1.00 26.55  ? 2929 PRO A C     1 
ATOM   11726 O  O     . PRO A 1 2929 ? 160.283 182.154 205.148 1.00 33.34  ? 2929 PRO A O     1 
ATOM   11727 C  CB    . PRO A 1 2929 ? 158.681 183.880 207.162 1.00 27.74  ? 2929 PRO A CB    1 
ATOM   11728 C  CG    . PRO A 1 2929 ? 160.017 184.061 207.794 1.00 28.62  ? 2929 PRO A CG    1 
ATOM   11729 C  CD    . PRO A 1 2929 ? 160.276 182.807 208.584 1.00 29.17  ? 2929 PRO A CD    1 
ATOM   11730 N  N     . GLN A 1 2930 ? 158.136 181.728 204.579 1.00 25.86  ? 2930 GLN A N     1 
ATOM   11731 C  CA    . GLN A 1 2930 ? 158.423 181.357 203.193 1.00 22.95  ? 2930 GLN A CA    1 
ATOM   11732 C  C     . GLN A 1 2930 ? 159.450 180.230 203.131 1.00 20.25  ? 2930 GLN A C     1 
ATOM   11733 O  O     . GLN A 1 2930 ? 160.344 180.215 202.282 1.00 21.64  ? 2930 GLN A O     1 
ATOM   11734 C  CB    . GLN A 1 2930 ? 158.888 182.569 202.382 1.00 22.95  ? 2930 GLN A CB    1 
ATOM   11735 C  CG    . GLN A 1 2930 ? 158.507 182.515 200.912 1.00 22.33  ? 2930 GLN A CG    1 
ATOM   11736 C  CD    . GLN A 1 2930 ? 158.865 183.787 200.172 1.00 25.80  ? 2930 GLN A CD    1 
ATOM   11737 O  OE1   . GLN A 1 2930 ? 159.463 184.701 200.740 1.00 25.87  ? 2930 GLN A OE1   1 
ATOM   11738 N  NE2   . GLN A 1 2930 ? 158.495 183.856 198.899 1.00 28.86  ? 2930 GLN A NE2   1 
ATOM   11739 N  N     . GLY A 1 2931 ? 159.318 179.274 204.046 1.00 20.24  ? 2931 GLY A N     1 
ATOM   11740 C  CA    . GLY A 1 2931 ? 160.248 178.167 204.127 1.00 15.15  ? 2931 GLY A CA    1 
ATOM   11741 C  C     . GLY A 1 2931 ? 159.832 176.983 203.283 1.00 14.42  ? 2931 GLY A C     1 
ATOM   11742 O  O     . GLY A 1 2931 ? 158.746 176.427 203.469 1.00 19.06  ? 2931 GLY A O     1 
ATOM   11743 N  N     . HIS A 1 2932 ? 160.690 176.589 202.350 1.00 16.57  ? 2932 HIS A N     1 
ATOM   11744 C  CA    . HIS A 1 2932 ? 160.423 175.477 201.455 1.00 13.20  ? 2932 HIS A CA    1 
ATOM   11745 C  C     . HIS A 1 2932 ? 161.578 174.486 201.498 1.00 12.70  ? 2932 HIS A C     1 
ATOM   11746 O  O     . HIS A 1 2932 ? 162.732 174.858 201.730 1.00 14.69  ? 2932 HIS A O     1 
ATOM   11747 C  CB    . HIS A 1 2932 ? 160.197 175.971 200.025 1.00 15.55  ? 2932 HIS A CB    1 
ATOM   11748 C  CG    . HIS A 1 2932 ? 159.225 177.107 199.931 1.00 15.17  ? 2932 HIS A CG    1 
ATOM   11749 N  ND1   . HIS A 1 2932 ? 157.904 176.986 200.303 1.00 14.49  ? 2932 HIS A ND1   1 
ATOM   11750 C  CD2   . HIS A 1 2932 ? 159.384 178.385 199.516 1.00 17.47  ? 2932 HIS A CD2   1 
ATOM   11751 C  CE1   . HIS A 1 2932 ? 157.290 178.140 200.118 1.00 14.47  ? 2932 HIS A CE1   1 
ATOM   11752 N  NE2   . HIS A 1 2932 ? 158.165 179.006 199.640 1.00 16.37  ? 2932 HIS A NE2   1 
ATOM   11753 N  N     . LEU A 1 2933 ? 161.254 173.216 201.276 1.00 13.08  ? 2933 LEU A N     1 
ATOM   11754 C  CA    . LEU A 1 2933 ? 162.201 172.125 201.433 1.00 11.12  ? 2933 LEU A CA    1 
ATOM   11755 C  C     . LEU A 1 2933 ? 162.391 171.385 200.117 1.00 14.62  ? 2933 LEU A C     1 
ATOM   11756 O  O     . LEU A 1 2933 ? 161.433 171.136 199.380 1.00 17.10  ? 2933 LEU A O     1 
ATOM   11757 C  CB    . LEU A 1 2933 ? 161.730 171.146 202.515 1.00 12.46  ? 2933 LEU A CB    1 
ATOM   11758 C  CG    . LEU A 1 2933 ? 162.239 171.408 203.933 1.00 13.89  ? 2933 LEU A CG    1 
ATOM   11759 C  CD1   . LEU A 1 2933 ? 162.240 170.127 204.744 1.00 17.31  ? 2933 LEU A CD1   1 
ATOM   11760 C  CD2   . LEU A 1 2933 ? 163.635 171.998 203.882 1.00 16.56  ? 2933 LEU A CD2   1 
ATOM   11761 N  N     . LEU A 1 2934 ? 163.645 171.039 199.831 1.00 15.57  ? 2934 LEU A N     1 
ATOM   11762 C  CA    . LEU A 1 2934 ? 164.010 170.203 198.688 1.00 12.78  ? 2934 LEU A CA    1 
ATOM   11763 C  C     . LEU A 1 2934 ? 164.725 168.978 199.252 1.00 17.78  ? 2934 LEU A C     1 
ATOM   11764 O  O     . LEU A 1 2934 ? 165.937 169.006 199.484 1.00 19.04  ? 2934 LEU A O     1 
ATOM   11765 C  CB    . LEU A 1 2934 ? 164.879 170.966 197.691 1.00 15.14  ? 2934 LEU A CB    1 
ATOM   11766 C  CG    . LEU A 1 2934 ? 165.351 170.182 196.464 1.00 17.01  ? 2934 LEU A CG    1 
ATOM   11767 C  CD1   . LEU A 1 2934 ? 164.166 169.627 195.694 1.00 20.91  ? 2934 LEU A CD1   1 
ATOM   11768 C  CD2   . LEU A 1 2934 ? 166.213 171.052 195.567 1.00 17.93  ? 2934 LEU A CD2   1 
ATOM   11769 N  N     . LEU A 1 2935 ? 163.970 167.906 199.480 1.00 15.43  ? 2935 LEU A N     1 
ATOM   11770 C  CA    . LEU A 1 2935 ? 164.512 166.673 200.039 1.00 12.46  ? 2935 LEU A CA    1 
ATOM   11771 C  C     . LEU A 1 2935 ? 164.940 165.765 198.894 1.00 12.64  ? 2935 LEU A C     1 
ATOM   11772 O  O     . LEU A 1 2935 ? 164.127 165.406 198.036 1.00 16.47  ? 2935 LEU A O     1 
ATOM   11773 C  CB    . LEU A 1 2935 ? 163.488 165.985 200.936 1.00 16.71  ? 2935 LEU A CB    1 
ATOM   11774 C  CG    . LEU A 1 2935 ? 162.860 166.848 202.030 1.00 17.90  ? 2935 LEU A CG    1 
ATOM   11775 C  CD1   . LEU A 1 2935 ? 161.971 166.004 202.925 1.00 17.59  ? 2935 LEU A CD1   1 
ATOM   11776 C  CD2   . LEU A 1 2935 ? 163.943 167.534 202.843 1.00 19.84  ? 2935 LEU A CD2   1 
ATOM   11777 N  N     . ILE A 1 2936 ? 166.216 165.393 198.883 1.00 15.06  ? 2936 ILE A N     1 
ATOM   11778 C  CA    . ILE A 1 2936 ? 166.807 164.608 197.807 1.00 14.64  ? 2936 ILE A CA    1 
ATOM   11779 C  C     . ILE A 1 2936 ? 167.274 163.286 198.393 1.00 16.42  ? 2936 ILE A C     1 
ATOM   11780 O  O     . ILE A 1 2936 ? 168.114 163.263 199.302 1.00 20.64  ? 2936 ILE A O     1 
ATOM   11781 C  CB    . ILE A 1 2936 ? 167.968 165.359 197.141 1.00 15.86  ? 2936 ILE A CB    1 
ATOM   11782 C  CG1   . ILE A 1 2936 ? 167.461 166.674 196.546 1.00 16.99  ? 2936 ILE A CG1   1 
ATOM   11783 C  CG2   . ILE A 1 2936 ? 168.620 164.488 196.078 1.00 18.72  ? 2936 ILE A CG2   1 
ATOM   11784 C  CD1   . ILE A 1 2936 ? 168.249 167.164 195.368 1.00 23.14  ? 2936 ILE A CD1   1 
ATOM   11785 N  N     . GLY A 1 2937 ? 166.738 162.189 197.877 1.00 13.98  ? 2937 GLY A N     1 
ATOM   11786 C  CA    . GLY A 1 2937 ? 167.118 160.880 198.372 1.00 16.39  ? 2937 GLY A CA    1 
ATOM   11787 C  C     . GLY A 1 2937 ? 166.431 159.790 197.582 1.00 18.00  ? 2937 GLY A C     1 
ATOM   11788 O  O     . GLY A 1 2937 ? 165.566 160.045 196.739 1.00 19.51  ? 2937 GLY A O     1 
ATOM   11789 N  N     . VAL A 1 2938 ? 166.840 158.556 197.877 1.00 19.41  ? 2938 VAL A N     1 
ATOM   11790 C  CA    . VAL A 1 2938 ? 166.278 157.389 197.212 1.00 20.12  ? 2938 VAL A CA    1 
ATOM   11791 C  C     . VAL A 1 2938 ? 164.819 157.227 197.618 1.00 21.48  ? 2938 VAL A C     1 
ATOM   11792 O  O     . VAL A 1 2938 ? 164.433 157.536 198.754 1.00 22.14  ? 2938 VAL A O     1 
ATOM   11793 C  CB    . VAL A 1 2938 ? 167.110 156.141 197.560 1.00 19.79  ? 2938 VAL A CB    1 
ATOM   11794 C  CG1   . VAL A 1 2938 ? 166.471 154.876 197.008 1.00 23.91  ? 2938 VAL A CG1   1 
ATOM   11795 C  CG2   . VAL A 1 2938 ? 168.531 156.296 197.039 1.00 23.48  ? 2938 VAL A CG2   1 
ATOM   11796 N  N     . SER A 1 2939 ? 163.995 156.761 196.681 1.00 18.40  ? 2939 SER A N     1 
ATOM   11797 C  CA    . SER A 1 2939 ? 162.583 156.548 196.965 1.00 17.14  ? 2939 SER A CA    1 
ATOM   11798 C  C     . SER A 1 2939 ? 162.407 155.536 198.090 1.00 21.44  ? 2939 SER A C     1 
ATOM   11799 O  O     . SER A 1 2939 ? 163.125 154.536 198.168 1.00 26.45  ? 2939 SER A O     1 
ATOM   11800 C  CB    . SER A 1 2939 ? 161.860 156.067 195.708 1.00 22.93  ? 2939 SER A CB    1 
ATOM   11801 O  OG    . SER A 1 2939 ? 161.979 157.009 194.657 1.00 31.34  ? 2939 SER A OG    1 
ATOM   11802 N  N     . GLY A 1 2940 ? 161.443 155.803 198.966 1.00 20.88  ? 2940 GLY A N     1 
ATOM   11803 C  CA    . GLY A 1 2940 ? 161.199 154.946 200.107 1.00 16.38  ? 2940 GLY A CA    1 
ATOM   11804 C  C     . GLY A 1 2940 ? 162.095 155.191 201.298 1.00 20.22  ? 2940 GLY A C     1 
ATOM   11805 O  O     . GLY A 1 2940 ? 162.117 154.362 202.215 1.00 29.72  ? 2940 GLY A O     1 
ATOM   11806 N  N     . ALA A 1 2941 ? 162.837 156.298 201.317 1.00 21.31  ? 2941 ALA A N     1 
ATOM   11807 C  CA    . ALA A 1 2941 ? 163.727 156.602 202.429 1.00 18.93  ? 2941 ALA A CA    1 
ATOM   11808 C  C     . ALA A 1 2941 ? 163.015 157.261 203.603 1.00 19.43  ? 2941 ALA A C     1 
ATOM   11809 O  O     . ALA A 1 2941 ? 163.625 157.411 204.667 1.00 29.44  ? 2941 ALA A O     1 
ATOM   11810 C  CB    . ALA A 1 2941 ? 164.871 157.503 201.958 1.00 23.80  ? 2941 ALA A CB    1 
ATOM   11811 N  N     . GLY A 1 2942 ? 161.756 157.653 203.443 1.00 15.88  ? 2942 GLY A N     1 
ATOM   11812 C  CA    . GLY A 1 2942 ? 161.017 158.304 204.503 1.00 18.01  ? 2942 GLY A CA    1 
ATOM   11813 C  C     . GLY A 1 2942 ? 160.748 159.777 204.305 1.00 15.86  ? 2942 GLY A C     1 
ATOM   11814 O  O     . GLY A 1 2942 ? 160.187 160.406 205.207 1.00 19.72  ? 2942 GLY A O     1 
ATOM   11815 N  N     . LYS A 1 2943 ? 161.117 160.343 203.154 1.00 14.03  ? 2943 LYS A N     1 
ATOM   11816 C  CA    . LYS A 1 2943 ? 161.001 161.786 202.962 1.00 13.15  ? 2943 LYS A CA    1 
ATOM   11817 C  C     . LYS A 1 2943 ? 159.549 162.246 203.042 1.00 17.53  ? 2943 LYS A C     1 
ATOM   11818 O  O     . LYS A 1 2943 ? 159.230 163.206 203.753 1.00 21.51  ? 2943 LYS A O     1 
ATOM   11819 C  CB    . LYS A 1 2943 ? 161.624 162.181 201.623 1.00 15.43  ? 2943 LYS A CB    1 
ATOM   11820 C  CG    . LYS A 1 2943 ? 162.962 161.511 201.352 1.00 14.17  ? 2943 LYS A CG    1 
ATOM   11821 C  CD    . LYS A 1 2943 ? 163.653 162.114 200.143 1.00 12.54  ? 2943 LYS A CD    1 
ATOM   11822 C  CE    . LYS A 1 2943 ? 162.891 161.811 198.866 1.00 17.31  ? 2943 LYS A CE    1 
ATOM   11823 N  NZ    . LYS A 1 2943 ? 162.884 160.354 198.561 1.00 20.52  ? 2943 LYS A NZ    1 
ATOM   11824 N  N     . THR A 1 2944 ? 158.652 161.573 202.318 1.00 18.50  ? 2944 THR A N     1 
ATOM   11825 C  CA    . THR A 1 2944 ? 157.245 161.961 202.358 1.00 13.78  ? 2944 THR A CA    1 
ATOM   11826 C  C     . THR A 1 2944 ? 156.631 161.681 203.723 1.00 19.83  ? 2944 THR A C     1 
ATOM   11827 O  O     . THR A 1 2944 ? 155.880 162.509 204.253 1.00 26.58  ? 2944 THR A O     1 
ATOM   11828 C  CB    . THR A 1 2944 ? 156.463 161.238 201.261 1.00 16.27  ? 2944 THR A CB    1 
ATOM   11829 O  OG1   . THR A 1 2944 ? 157.099 161.455 199.996 1.00 21.46  ? 2944 THR A OG1   1 
ATOM   11830 C  CG2   . THR A 1 2944 ? 155.033 161.753 201.195 1.00 22.35  ? 2944 THR A CG2   1 
ATOM   11831 N  N     . THR A 1 2945 ? 156.939 160.521 204.310 1.00 18.89  ? 2945 THR A N     1 
ATOM   11832 C  CA    . THR A 1 2945 ? 156.359 160.168 205.602 1.00 16.55  ? 2945 THR A CA    1 
ATOM   11833 C  C     . THR A 1 2945 ? 156.860 161.083 206.713 1.00 16.56  ? 2945 THR A C     1 
ATOM   11834 O  O     . THR A 1 2945 ? 156.073 161.527 207.557 1.00 23.45  ? 2945 THR A O     1 
ATOM   11835 C  CB    . THR A 1 2945 ? 156.664 158.709 205.937 1.00 21.54  ? 2945 THR A CB    1 
ATOM   11836 O  OG1   . THR A 1 2945 ? 156.461 157.896 204.774 1.00 28.07  ? 2945 THR A OG1   1 
ATOM   11837 C  CG2   . THR A 1 2945 ? 155.759 158.220 207.057 1.00 20.85  ? 2945 THR A CG2   1 
ATOM   11838 N  N     . LEU A 1 2946 ? 158.164 161.371 206.737 1.00 15.76  ? 2946 LEU A N     1 
ATOM   11839 C  CA    . LEU A 1 2946 ? 158.703 162.231 207.787 1.00 16.38  ? 2946 LEU A CA    1 
ATOM   11840 C  C     . LEU A 1 2946 ? 158.162 163.650 207.672 1.00 19.30  ? 2946 LEU A C     1 
ATOM   11841 O  O     . LEU A 1 2946 ? 157.816 164.269 208.683 1.00 22.40  ? 2946 LEU A O     1 
ATOM   11842 C  CB    . LEU A 1 2946 ? 160.231 162.232 207.747 1.00 11.87  ? 2946 LEU A CB    1 
ATOM   11843 C  CG    . LEU A 1 2946 ? 160.932 160.971 208.259 1.00 11.74  ? 2946 LEU A CG    1 
ATOM   11844 C  CD1   . LEU A 1 2946 ? 162.401 161.246 208.535 1.00 18.42  ? 2946 LEU A CD1   1 
ATOM   11845 C  CD2   . LEU A 1 2946 ? 160.240 160.434 209.502 1.00 10.27  ? 2946 LEU A CD2   1 
ATOM   11846 N  N     . SER A 1 2947 ? 158.069 164.175 206.447 1.00 18.05  ? 2947 SER A N     1 
ATOM   11847 C  CA    . SER A 1 2947 ? 157.550 165.526 206.260 1.00 15.74  ? 2947 SER A CA    1 
ATOM   11848 C  C     . SER A 1 2947 ? 156.115 165.639 206.759 1.00 18.32  ? 2947 SER A C     1 
ATOM   11849 O  O     . SER A 1 2947 ? 155.738 166.650 207.362 1.00 23.16  ? 2947 SER A O     1 
ATOM   11850 C  CB    . SER A 1 2947 ? 157.642 165.924 204.788 1.00 15.97  ? 2947 SER A CB    1 
ATOM   11851 O  OG    . SER A 1 2947 ? 158.966 165.784 204.308 1.00 22.92  ? 2947 SER A OG    1 
ATOM   11852 N  N     . ARG A 1 2948 ? 155.300 164.612 206.511 1.00 18.98  ? 2948 ARG A N     1 
ATOM   11853 C  CA    . ARG A 1 2948 ? 153.939 164.600 207.036 1.00 15.45  ? 2948 ARG A CA    1 
ATOM   11854 C  C     . ARG A 1 2948 ? 153.936 164.573 208.559 1.00 18.30  ? 2948 ARG A C     1 
ATOM   11855 O  O     . ARG A 1 2948 ? 153.063 165.174 209.197 1.00 27.17  ? 2948 ARG A O     1 
ATOM   11856 C  CB    . ARG A 1 2948 ? 153.178 163.399 206.475 1.00 19.81  ? 2948 ARG A CB    1 
ATOM   11857 C  CG    . ARG A 1 2948 ? 152.902 163.484 204.984 1.00 25.53  ? 2948 ARG A CG    1 
ATOM   11858 C  CD    . ARG A 1 2948 ? 152.202 162.236 204.476 1.00 23.00  ? 2948 ARG A CD    1 
ATOM   11859 N  NE    . ARG A 1 2948 ? 150.809 162.171 204.899 1.00 30.26  ? 2948 ARG A NE    1 
ATOM   11860 C  CZ    . ARG A 1 2948 ? 149.890 161.407 204.324 1.00 38.47  ? 2948 ARG A CZ    1 
ATOM   11861 N  NH1   . ARG A 1 2948 ? 150.183 160.630 203.295 1.00 41.63  ? 2948 ARG A NH1   1 
ATOM   11862 N  NH2   . ARG A 1 2948 ? 148.646 161.423 204.795 1.00 36.55  ? 2948 ARG A NH2   1 
ATOM   11863 N  N     . PHE A 1 2949 ? 154.902 163.875 209.160 1.00 19.18  ? 2949 PHE A N     1 
ATOM   11864 C  CA    . PHE A 1 2949 ? 154.943 163.766 210.615 1.00 17.95  ? 2949 PHE A CA    1 
ATOM   11865 C  C     . PHE A 1 2949 ? 155.297 165.098 211.265 1.00 21.76  ? 2949 PHE A C     1 
ATOM   11866 O  O     . PHE A 1 2949 ? 154.653 165.513 212.236 1.00 23.90  ? 2949 PHE A O     1 
ATOM   11867 C  CB    . PHE A 1 2949 ? 155.939 162.681 211.027 1.00 17.57  ? 2949 PHE A CB    1 
ATOM   11868 C  CG    . PHE A 1 2949 ? 156.252 162.669 212.495 1.00 23.11  ? 2949 PHE A CG    1 
ATOM   11869 C  CD1   . PHE A 1 2949 ? 155.244 162.499 213.430 1.00 25.19  ? 2949 PHE A CD1   1 
ATOM   11870 C  CD2   . PHE A 1 2949 ? 157.553 162.824 212.941 1.00 23.72  ? 2949 PHE A CD2   1 
ATOM   11871 C  CE1   . PHE A 1 2949 ? 155.528 162.487 214.781 1.00 26.70  ? 2949 PHE A CE1   1 
ATOM   11872 C  CE2   . PHE A 1 2949 ? 157.844 162.812 214.291 1.00 25.82  ? 2949 PHE A CE2   1 
ATOM   11873 C  CZ    . PHE A 1 2949 ? 156.829 162.643 215.212 1.00 26.86  ? 2949 PHE A CZ    1 
ATOM   11874 N  N     . VAL A 1 2950 ? 156.320 165.784 210.748 1.00 18.75  ? 2950 VAL A N     1 
ATOM   11875 C  CA    . VAL A 1 2950 ? 156.701 167.075 211.314 1.00 18.13  ? 2950 VAL A CA    1 
ATOM   11876 C  C     . VAL A 1 2950 ? 155.630 168.121 211.039 1.00 21.16  ? 2950 VAL A C     1 
ATOM   11877 O  O     . VAL A 1 2950 ? 155.365 168.991 211.878 1.00 26.56  ? 2950 VAL A O     1 
ATOM   11878 C  CB    . VAL A 1 2950 ? 158.076 167.519 210.784 1.00 18.39  ? 2950 VAL A CB    1 
ATOM   11879 C  CG1   . VAL A 1 2950 ? 158.691 168.527 211.728 1.00 23.18  ? 2950 VAL A CG1   1 
ATOM   11880 C  CG2   . VAL A 1 2950 ? 159.001 166.330 210.643 1.00 17.87  ? 2950 VAL A CG2   1 
ATOM   11881 N  N     . ALA A 1 2951 ? 155.006 168.065 209.860 1.00 19.22  ? 2951 ALA A N     1 
ATOM   11882 C  CA    . ALA A 1 2951 ? 153.933 169.005 209.548 1.00 18.87  ? 2951 ALA A CA    1 
ATOM   11883 C  C     . ALA A 1 2951 ? 152.767 168.843 210.514 1.00 22.68  ? 2951 ALA A C     1 
ATOM   11884 O  O     . ALA A 1 2951 ? 152.181 169.834 210.965 1.00 26.04  ? 2951 ALA A O     1 
ATOM   11885 C  CB    . ALA A 1 2951 ? 153.467 168.815 208.105 1.00 17.12  ? 2951 ALA A CB    1 
ATOM   11886 N  N     . TRP A 1 2952 ? 152.419 167.598 210.842 1.00 24.39  ? 2952 TRP A N     1 
ATOM   11887 C  CA    . TRP A 1 2952 ? 151.389 167.356 211.846 1.00 21.58  ? 2952 TRP A CA    1 
ATOM   11888 C  C     . TRP A 1 2952 ? 151.828 167.855 213.216 1.00 22.98  ? 2952 TRP A C     1 
ATOM   11889 O  O     . TRP A 1 2952 ? 151.008 168.355 213.995 1.00 27.24  ? 2952 TRP A O     1 
ATOM   11890 C  CB    . TRP A 1 2952 ? 151.053 165.865 211.892 1.00 25.03  ? 2952 TRP A CB    1 
ATOM   11891 C  CG    . TRP A 1 2952 ? 150.232 165.463 213.076 1.00 28.51  ? 2952 TRP A CG    1 
ATOM   11892 C  CD1   . TRP A 1 2952 ? 148.876 165.543 213.199 1.00 27.50  ? 2952 TRP A CD1   1 
ATOM   11893 C  CD2   . TRP A 1 2952 ? 150.715 164.900 214.300 1.00 25.33  ? 2952 TRP A CD2   1 
ATOM   11894 N  NE1   . TRP A 1 2952 ? 148.485 165.074 214.430 1.00 32.31  ? 2952 TRP A NE1   1 
ATOM   11895 C  CE2   . TRP A 1 2952 ? 149.595 164.672 215.124 1.00 26.80  ? 2952 TRP A CE2   1 
ATOM   11896 C  CE3   . TRP A 1 2952 ? 151.985 164.571 214.781 1.00 26.14  ? 2952 TRP A CE3   1 
ATOM   11897 C  CZ2   . TRP A 1 2952 ? 149.708 164.129 216.401 1.00 31.02  ? 2952 TRP A CZ2   1 
ATOM   11898 C  CZ3   . TRP A 1 2952 ? 152.095 164.033 216.048 1.00 29.90  ? 2952 TRP A CZ3   1 
ATOM   11899 C  CH2   . TRP A 1 2952 ? 150.963 163.817 216.844 1.00 36.23  ? 2952 TRP A CH2   1 
ATOM   11900 N  N     . MET A 1 2953 ? 153.118 167.722 213.529 1.00 22.16  ? 2953 MET A N     1 
ATOM   11901 C  CA    . MET A 1 2953 ? 153.620 168.183 214.819 1.00 24.91  ? 2953 MET A CA    1 
ATOM   11902 C  C     . MET A 1 2953 ? 153.510 169.696 214.951 1.00 25.00  ? 2953 MET A C     1 
ATOM   11903 O  O     . MET A 1 2953 ? 153.148 170.209 216.017 1.00 26.01  ? 2953 MET A O     1 
ATOM   11904 C  CB    . MET A 1 2953 ? 155.067 167.730 215.007 1.00 25.49  ? 2953 MET A CB    1 
ATOM   11905 C  CG    . MET A 1 2953 ? 155.226 166.603 216.006 1.00 29.67  ? 2953 MET A CG    1 
ATOM   11906 S  SD    . MET A 1 2953 ? 156.933 166.399 216.530 1.00 45.80  ? 2953 MET A SD    1 
ATOM   11907 C  CE    . MET A 1 2953 ? 156.861 167.206 218.123 1.00 35.83  ? 2953 MET A CE    1 
ATOM   11908 N  N     . ASN A 1 2954 ? 153.819 170.428 213.884 1.00 27.78  ? 2954 ASN A N     1 
ATOM   11909 C  CA    . ASN A 1 2954 ? 153.739 171.882 213.887 1.00 26.27  ? 2954 ASN A CA    1 
ATOM   11910 C  C     . ASN A 1 2954 ? 152.343 172.399 213.570 1.00 26.13  ? 2954 ASN A C     1 
ATOM   11911 O  O     . ASN A 1 2954 ? 152.140 173.618 213.548 1.00 30.03  ? 2954 ASN A O     1 
ATOM   11912 C  CB    . ASN A 1 2954 ? 154.746 172.468 212.893 1.00 24.27  ? 2954 ASN A CB    1 
ATOM   11913 C  CG    . ASN A 1 2954 ? 156.178 172.302 213.353 1.00 27.98  ? 2954 ASN A CG    1 
ATOM   11914 O  OD1   . ASN A 1 2954 ? 156.449 172.229 214.551 1.00 34.77  ? 2954 ASN A OD1   1 
ATOM   11915 N  ND2   . ASN A 1 2954 ? 157.104 172.243 212.404 1.00 26.99  ? 2954 ASN A ND2   1 
ATOM   11916 N  N     . GLY A 1 2955 ? 151.383 171.512 213.325 1.00 23.12  ? 2955 GLY A N     1 
ATOM   11917 C  CA    . GLY A 1 2955 ? 150.028 171.914 213.028 1.00 20.74  ? 2955 GLY A CA    1 
ATOM   11918 C  C     . GLY A 1 2955 ? 149.755 172.249 211.580 1.00 25.01  ? 2955 GLY A C     1 
ATOM   11919 O  O     . GLY A 1 2955 ? 148.637 172.676 211.263 1.00 32.64  ? 2955 GLY A O     1 
ATOM   11920 N  N     . LEU A 1 2956 ? 150.729 172.074 210.692 1.00 24.52  ? 2956 LEU A N     1 
ATOM   11921 C  CA    . LEU A 1 2956 ? 150.517 172.341 209.278 1.00 22.62  ? 2956 LEU A CA    1 
ATOM   11922 C  C     . LEU A 1 2956 ? 149.655 171.249 208.661 1.00 24.06  ? 2956 LEU A C     1 
ATOM   11923 O  O     . LEU A 1 2956 ? 149.757 170.075 209.027 1.00 22.71  ? 2956 LEU A O     1 
ATOM   11924 C  CB    . LEU A 1 2956 ? 151.852 172.431 208.535 1.00 22.15  ? 2956 LEU A CB    1 
ATOM   11925 C  CG    . LEU A 1 2956 ? 153.041 173.116 209.214 1.00 24.99  ? 2956 LEU A CG    1 
ATOM   11926 C  CD1   . LEU A 1 2956 ? 154.205 173.223 208.242 1.00 21.05  ? 2956 LEU A CD1   1 
ATOM   11927 C  CD2   . LEU A 1 2956 ? 152.669 174.488 209.748 1.00 28.47  ? 2956 LEU A CD2   1 
ATOM   11928 N  N     . SER A 1 2957 ? 148.799 171.644 207.723 1.00 26.33  ? 2957 SER A N     1 
ATOM   11929 C  CA    . SER A 1 2957 ? 147.939 170.706 207.017 1.00 21.23  ? 2957 SER A CA    1 
ATOM   11930 C  C     . SER A 1 2957 ? 148.654 170.197 205.773 1.00 23.20  ? 2957 SER A C     1 
ATOM   11931 O  O     . SER A 1 2957 ? 149.163 170.988 204.974 1.00 29.16  ? 2957 SER A O     1 
ATOM   11932 C  CB    . SER A 1 2957 ? 146.614 171.367 206.639 1.00 22.14  ? 2957 SER A CB    1 
ATOM   11933 O  OG    . SER A 1 2957 ? 145.996 171.950 207.772 1.00 32.48  ? 2957 SER A OG    1 
ATOM   11934 N  N     . VAL A 1 2958 ? 148.691 168.880 205.615 1.00 26.22  ? 2958 VAL A N     1 
ATOM   11935 C  CA    . VAL A 1 2958 ? 149.373 168.271 204.480 1.00 24.31  ? 2958 VAL A CA    1 
ATOM   11936 C  C     . VAL A 1 2958 ? 148.449 168.293 203.271 1.00 21.30  ? 2958 VAL A C     1 
ATOM   11937 O  O     . VAL A 1 2958 ? 147.303 167.832 203.341 1.00 27.10  ? 2958 VAL A O     1 
ATOM   11938 C  CB    . VAL A 1 2958 ? 149.813 166.837 204.815 1.00 25.81  ? 2958 VAL A CB    1 
ATOM   11939 C  CG1   . VAL A 1 2958 ? 150.183 166.085 203.546 1.00 26.26  ? 2958 VAL A CG1   1 
ATOM   11940 C  CG2   . VAL A 1 2958 ? 150.977 166.856 205.788 1.00 23.29  ? 2958 VAL A CG2   1 
ATOM   11941 N  N     . TYR A 1 2959 ? 148.941 168.836 202.161 1.00 22.92  ? 2959 TYR A N     1 
ATOM   11942 C  CA    . TYR A 1 2959 ? 148.232 168.808 200.891 1.00 23.72  ? 2959 TYR A CA    1 
ATOM   11943 C  C     . TYR A 1 2959 ? 149.103 168.132 199.846 1.00 25.41  ? 2959 TYR A C     1 
ATOM   11944 O  O     . TYR A 1 2959 ? 150.258 168.522 199.647 1.00 26.44  ? 2959 TYR A O     1 
ATOM   11945 C  CB    . TYR A 1 2959 ? 147.856 170.213 200.420 1.00 21.05  ? 2959 TYR A CB    1 
ATOM   11946 C  CG    . TYR A 1 2959 ? 146.887 170.202 199.261 1.00 27.57  ? 2959 TYR A CG    1 
ATOM   11947 C  CD1   . TYR A 1 2959 ? 147.307 170.524 197.978 1.00 28.72  ? 2959 TYR A CD1   1 
ATOM   11948 C  CD2   . TYR A 1 2959 ? 145.553 169.866 199.448 1.00 29.44  ? 2959 TYR A CD2   1 
ATOM   11949 C  CE1   . TYR A 1 2959 ? 146.427 170.511 196.913 1.00 31.81  ? 2959 TYR A CE1   1 
ATOM   11950 C  CE2   . TYR A 1 2959 ? 144.665 169.852 198.389 1.00 33.23  ? 2959 TYR A CE2   1 
ATOM   11951 C  CZ    . TYR A 1 2959 ? 145.108 170.176 197.124 1.00 37.52  ? 2959 TYR A CZ    1 
ATOM   11952 O  OH    . TYR A 1 2959 ? 144.228 170.165 196.066 1.00 41.19  ? 2959 TYR A OH    1 
ATOM   11953 N  N     . GLN A 1 2960 ? 148.548 167.121 199.185 1.00 25.05  ? 2960 GLN A N     1 
ATOM   11954 C  CA    . GLN A 1 2960 ? 149.210 166.439 198.085 1.00 24.57  ? 2960 GLN A CA    1 
ATOM   11955 C  C     . GLN A 1 2960 ? 148.254 166.365 196.907 1.00 33.91  ? 2960 GLN A C     1 
ATOM   11956 O  O     . GLN A 1 2960 ? 147.069 166.066 197.077 1.00 38.07  ? 2960 GLN A O     1 
ATOM   11957 C  CB    . GLN A 1 2960 ? 149.660 165.027 198.484 1.00 24.99  ? 2960 GLN A CB    1 
ATOM   11958 C  CG    . GLN A 1 2960 ? 150.410 164.957 199.803 1.00 28.11  ? 2960 GLN A CG    1 
ATOM   11959 C  CD    . GLN A 1 2960 ? 150.867 163.552 200.140 1.00 35.61  ? 2960 GLN A CD    1 
ATOM   11960 O  OE1   . GLN A 1 2960 ? 150.351 162.925 201.064 1.00 38.43  ? 2960 GLN A OE1   1 
ATOM   11961 N  NE2   . GLN A 1 2960 ? 151.842 163.051 199.390 1.00 28.08  ? 2960 GLN A NE2   1 
ATOM   11962 N  N     . ILE A 1 2961 ? 148.768 166.641 195.715 1.00 32.92  ? 2961 ILE A N     1 
ATOM   11963 C  CA    . ILE A 1 2961 ? 147.959 166.543 194.507 1.00 40.99  ? 2961 ILE A CA    1 
ATOM   11964 C  C     . ILE A 1 2961 ? 147.873 165.079 194.092 1.00 48.28  ? 2961 ILE A C     1 
ATOM   11965 O  O     . ILE A 1 2961 ? 148.845 164.323 194.213 1.00 46.19  ? 2961 ILE A O     1 
ATOM   11966 C  CB    . ILE A 1 2961 ? 148.530 167.434 193.389 1.00 41.50  ? 2961 ILE A CB    1 
ATOM   11967 C  CG1   . ILE A 1 2961 ? 149.620 166.719 192.588 1.00 40.24  ? 2961 ILE A CG1   1 
ATOM   11968 C  CG2   . ILE A 1 2961 ? 149.056 168.741 193.966 1.00 37.15  ? 2961 ILE A CG2   1 
ATOM   11969 C  CD1   . ILE A 1 2961 ? 150.151 167.530 191.428 1.00 41.66  ? 2961 ILE A CD1   1 
ATOM   11970 N  N     . LYS A 1 2962 ? 146.687 164.662 193.653 1.00 50.83  ? 2962 LYS A N     1 
ATOM   11971 C  CA    . LYS A 1 2962 ? 146.437 163.272 193.275 1.00 49.97  ? 2962 LYS A CA    1 
ATOM   11972 C  C     . LYS A 1 2962 ? 146.549 163.167 191.761 1.00 56.41  ? 2962 LYS A C     1 
ATOM   11973 O  O     . LYS A 1 2962 ? 145.590 163.399 191.024 1.00 60.18  ? 2962 LYS A O     1 
ATOM   11974 C  CB    . LYS A 1 2962 ? 145.075 162.813 193.779 1.00 50.89  ? 2962 LYS A CB    1 
ATOM   11975 C  CG    . LYS A 1 2962 ? 144.879 163.004 195.272 1.00 50.89  ? 2962 LYS A CG    1 
ATOM   11976 C  CD    . LYS A 1 2962 ? 145.954 162.274 196.060 1.00 51.24  ? 2962 LYS A CD    1 
ATOM   11977 C  CE    . LYS A 1 2962 ? 145.963 162.704 197.517 1.00 52.20  ? 2962 LYS A CE    1 
ATOM   11978 N  NZ    . LYS A 1 2962 ? 144.615 162.588 198.138 1.00 64.88  ? 2962 LYS A NZ    1 
ATOM   11979 N  N     . VAL A 1 2963 ? 147.740 162.812 191.293 1.00 50.48  ? 2963 VAL A N     1 
ATOM   11980 C  CA    . VAL A 1 2963 ? 148.006 162.726 189.863 1.00 52.45  ? 2963 VAL A CA    1 
ATOM   11981 C  C     . VAL A 1 2963 ? 147.416 161.433 189.319 1.00 54.57  ? 2963 VAL A C     1 
ATOM   11982 O  O     . VAL A 1 2963 ? 147.647 160.349 189.867 1.00 53.72  ? 2963 VAL A O     1 
ATOM   11983 C  CB    . VAL A 1 2963 ? 149.516 162.802 189.586 1.00 50.49  ? 2963 VAL A CB    1 
ATOM   11984 C  CG1   . VAL A 1 2963 ? 149.790 162.647 188.101 1.00 51.60  ? 2963 VAL A CG1   1 
ATOM   11985 C  CG2   . VAL A 1 2963 ? 150.081 164.112 190.098 1.00 44.93  ? 2963 VAL A CG2   1 
ATOM   11986 N  N     . HIS A 1 2964 ? 146.645 161.547 188.239 1.00 57.00  ? 2964 HIS A N     1 
ATOM   11987 C  CA    . HIS A 1 2964 ? 146.175 160.376 187.511 1.00 59.90  ? 2964 HIS A CA    1 
ATOM   11988 C  C     . HIS A 1 2964 ? 146.585 160.491 186.048 1.00 64.72  ? 2964 HIS A C     1 
ATOM   11989 O  O     . HIS A 1 2964 ? 147.287 161.435 185.672 1.00 65.29  ? 2964 HIS A O     1 
ATOM   11990 C  CB    . HIS A 1 2964 ? 144.659 160.216 187.650 1.00 60.36  ? 2964 HIS A CB    1 
ATOM   11991 C  CG    . HIS A 1 2964 ? 143.895 161.493 187.489 1.00 56.93  ? 2964 HIS A CG    1 
ATOM   11992 N  ND1   . HIS A 1 2964 ? 143.652 162.065 186.259 1.00 60.45  ? 2964 HIS A ND1   1 
ATOM   11993 C  CD2   . HIS A 1 2964 ? 143.316 162.306 188.403 1.00 52.87  ? 2964 HIS A CD2   1 
ATOM   11994 C  CE1   . HIS A 1 2964 ? 142.957 163.177 186.423 1.00 59.14  ? 2964 HIS A CE1   1 
ATOM   11995 N  NE2   . HIS A 1 2964 ? 142.741 163.346 187.715 1.00 57.12  ? 2964 HIS A NE2   1 
ATOM   11996 N  N     . ARG A 1 2965 ? 146.157 159.539 185.216 1.00 67.33  ? 2965 ARG A N     1 
ATOM   11997 C  CA    . ARG A 1 2965 ? 146.586 159.539 183.821 1.00 67.85  ? 2965 ARG A CA    1 
ATOM   11998 C  C     . ARG A 1 2965 ? 145.995 160.709 183.042 1.00 68.28  ? 2965 ARG A C     1 
ATOM   11999 O  O     . ARG A 1 2965 ? 146.546 161.102 182.009 1.00 62.66  ? 2965 ARG A O     1 
ATOM   12000 C  CB    . ARG A 1 2965 ? 146.214 158.215 183.155 1.00 70.99  ? 2965 ARG A CB    1 
ATOM   12001 C  CG    . ARG A 1 2965 ? 144.743 157.853 183.258 1.00 74.65  ? 2965 ARG A CG    1 
ATOM   12002 C  CD    . ARG A 1 2965 ? 144.489 156.448 182.737 1.00 72.29  ? 2965 ARG A CD    1 
ATOM   12003 N  NE    . ARG A 1 2965 ? 144.795 156.331 181.316 1.00 75.74  ? 2965 ARG A NE    1 
ATOM   12004 C  CZ    . ARG A 1 2965 ? 145.782 155.597 180.820 1.00 72.23  ? 2965 ARG A CZ    1 
ATOM   12005 N  NH1   . ARG A 1 2965 ? 146.583 154.895 181.605 1.00 64.34  ? 2965 ARG A NH1   1 
ATOM   12006 N  NH2   . ARG A 1 2965 ? 145.970 155.568 179.504 1.00 67.68  ? 2965 ARG A NH2   1 
ATOM   12007 N  N     . LYS A 1 2966 ? 144.887 161.274 183.516 1.00 69.71  ? 2966 LYS A N     1 
ATOM   12008 C  CA    . LYS A 1 2966 ? 144.235 162.396 182.854 1.00 64.41  ? 2966 LYS A CA    1 
ATOM   12009 C  C     . LYS A 1 2966 ? 144.523 163.729 183.533 1.00 60.03  ? 2966 LYS A C     1 
ATOM   12010 O  O     . LYS A 1 2966 ? 143.865 164.726 183.220 1.00 58.36  ? 2966 LYS A O     1 
ATOM   12011 C  CB    . LYS A 1 2966 ? 142.726 162.159 182.782 1.00 66.33  ? 2966 LYS A CB    1 
ATOM   12012 C  CG    . LYS A 1 2966 ? 142.326 161.003 181.880 1.00 65.29  ? 2966 LYS A CG    1 
ATOM   12013 C  CD    . LYS A 1 2966 ? 143.037 161.081 180.537 1.00 62.85  ? 2966 LYS A CD    1 
ATOM   12014 C  CE    . LYS A 1 2966 ? 142.757 159.850 179.690 1.00 67.51  ? 2966 LYS A CE    1 
ATOM   12015 N  NZ    . LYS A 1 2966 ? 142.879 158.595 180.482 1.00 71.45  ? 2966 LYS A NZ    1 
ATOM   12016 N  N     . TYR A 1 2967 ? 145.484 163.769 184.452 1.00 59.52  ? 2967 TYR A N     1 
ATOM   12017 C  CA    . TYR A 1 2967 ? 145.821 165.005 185.146 1.00 55.05  ? 2967 TYR A CA    1 
ATOM   12018 C  C     . TYR A 1 2967 ? 146.585 165.930 184.205 1.00 53.01  ? 2967 TYR A C     1 
ATOM   12019 O  O     . TYR A 1 2967 ? 147.623 165.547 183.656 1.00 54.17  ? 2967 TYR A O     1 
ATOM   12020 C  CB    . TYR A 1 2967 ? 146.649 164.696 186.390 1.00 52.67  ? 2967 TYR A CB    1 
ATOM   12021 C  CG    . TYR A 1 2967 ? 146.608 165.771 187.452 1.00 50.33  ? 2967 TYR A CG    1 
ATOM   12022 C  CD1   . TYR A 1 2967 ? 145.609 165.783 188.416 1.00 50.87  ? 2967 TYR A CD1   1 
ATOM   12023 C  CD2   . TYR A 1 2967 ? 147.571 166.769 187.495 1.00 45.28  ? 2967 TYR A CD2   1 
ATOM   12024 C  CE1   . TYR A 1 2967 ? 145.570 166.761 189.390 1.00 43.54  ? 2967 TYR A CE1   1 
ATOM   12025 C  CE2   . TYR A 1 2967 ? 147.539 167.751 188.465 1.00 39.82  ? 2967 TYR A CE2   1 
ATOM   12026 C  CZ    . TYR A 1 2967 ? 146.537 167.742 189.410 1.00 39.59  ? 2967 TYR A CZ    1 
ATOM   12027 O  OH    . TYR A 1 2967 ? 146.501 168.718 190.377 1.00 44.08  ? 2967 TYR A OH    1 
ATOM   12028 N  N     . THR A 1 2968 ? 146.077 167.143 184.021 1.00 54.98  ? 2968 THR A N     1 
ATOM   12029 C  CA    . THR A 1 2968 ? 146.646 168.105 183.087 1.00 52.59  ? 2968 THR A CA    1 
ATOM   12030 C  C     . THR A 1 2968 ? 147.037 169.383 183.824 1.00 49.60  ? 2968 THR A C     1 
ATOM   12031 O  O     . THR A 1 2968 ? 146.922 169.486 185.048 1.00 50.15  ? 2968 THR A O     1 
ATOM   12032 C  CB    . THR A 1 2968 ? 145.663 168.413 181.954 1.00 56.72  ? 2968 THR A CB    1 
ATOM   12033 O  OG1   . THR A 1 2968 ? 144.325 168.419 182.468 1.00 54.24  ? 2968 THR A OG1   1 
ATOM   12034 C  CG2   . THR A 1 2968 ? 145.773 167.366 180.857 1.00 56.42  ? 2968 THR A CG2   1 
ATOM   12035 N  N     . GLY A 1 2969 ? 147.509 170.365 183.053 1.00 45.88  ? 2969 GLY A N     1 
ATOM   12036 C  CA    . GLY A 1 2969 ? 147.908 171.634 183.637 1.00 43.87  ? 2969 GLY A CA    1 
ATOM   12037 C  C     . GLY A 1 2969 ? 146.756 172.404 184.250 1.00 46.00  ? 2969 GLY A C     1 
ATOM   12038 O  O     . GLY A 1 2969 ? 146.941 173.116 185.241 1.00 46.79  ? 2969 GLY A O     1 
ATOM   12039 N  N     . GLU A 1 2970 ? 145.559 172.281 183.671 1.00 49.79  ? 2970 GLU A N     1 
ATOM   12040 C  CA    . GLU A 1 2970 ? 144.394 172.956 184.233 1.00 46.98  ? 2970 GLU A CA    1 
ATOM   12041 C  C     . GLU A 1 2970 ? 144.026 172.373 185.592 1.00 45.89  ? 2970 GLU A C     1 
ATOM   12042 O  O     . GLU A 1 2970 ? 143.585 173.103 186.487 1.00 46.93  ? 2970 GLU A O     1 
ATOM   12043 C  CB    . GLU A 1 2970 ? 143.190 172.884 183.280 1.00 54.54  ? 2970 GLU A CB    1 
ATOM   12044 C  CG    . GLU A 1 2970 ? 143.379 173.292 181.796 1.00 60.02  ? 2970 GLU A CG    1 
ATOM   12045 C  CD    . GLU A 1 2970 ? 144.600 172.707 181.109 1.00 63.53  ? 2970 GLU A CD    1 
ATOM   12046 O  OE1   . GLU A 1 2970 ? 145.376 173.482 180.511 1.00 69.96  ? 2970 GLU A OE1   1 
ATOM   12047 O  OE2   . GLU A 1 2970 ? 144.784 171.474 181.169 1.00 58.77  ? 2970 GLU A OE2   1 
ATOM   12048 N  N     . ASP A 1 2971 ? 144.192 171.059 185.761 1.00 44.47  ? 2971 ASP A N     1 
ATOM   12049 C  CA    . ASP A 1 2971 ? 143.966 170.449 187.067 1.00 44.48  ? 2971 ASP A CA    1 
ATOM   12050 C  C     . ASP A 1 2971 ? 144.960 170.969 188.097 1.00 39.08  ? 2971 ASP A C     1 
ATOM   12051 O  O     . ASP A 1 2971 ? 144.598 171.216 189.253 1.00 38.21  ? 2971 ASP A O     1 
ATOM   12052 C  CB    . ASP A 1 2971 ? 144.056 168.927 186.960 1.00 46.00  ? 2971 ASP A CB    1 
ATOM   12053 C  CG    . ASP A 1 2971 ? 143.100 168.358 185.935 1.00 53.05  ? 2971 ASP A CG    1 
ATOM   12054 O  OD1   . ASP A 1 2971 ? 141.876 168.390 186.180 1.00 56.85  ? 2971 ASP A OD1   1 
ATOM   12055 O  OD2   . ASP A 1 2971 ? 143.571 167.877 184.884 1.00 54.74  ? 2971 ASP A OD2   1 
ATOM   12056 N  N     . PHE A 1 2972 ? 146.223 171.134 187.696 1.00 37.57  ? 2972 PHE A N     1 
ATOM   12057 C  CA    . PHE A 1 2972 ? 147.234 171.646 188.614 1.00 38.41  ? 2972 PHE A CA    1 
ATOM   12058 C  C     . PHE A 1 2972 ? 146.935 173.082 189.021 1.00 37.42  ? 2972 PHE A C     1 
ATOM   12059 O  O     . PHE A 1 2972 ? 147.146 173.462 190.178 1.00 35.85  ? 2972 PHE A O     1 
ATOM   12060 C  CB    . PHE A 1 2972 ? 148.616 171.551 187.973 1.00 36.20  ? 2972 PHE A CB    1 
ATOM   12061 C  CG    . PHE A 1 2972 ? 149.745 171.872 188.909 1.00 39.65  ? 2972 PHE A CG    1 
ATOM   12062 C  CD1   . PHE A 1 2972 ? 149.943 171.124 190.058 1.00 35.55  ? 2972 PHE A CD1   1 
ATOM   12063 C  CD2   . PHE A 1 2972 ? 150.614 172.915 188.637 1.00 40.29  ? 2972 PHE A CD2   1 
ATOM   12064 C  CE1   . PHE A 1 2972 ? 150.983 171.413 190.920 1.00 37.20  ? 2972 PHE A CE1   1 
ATOM   12065 C  CE2   . PHE A 1 2972 ? 151.656 173.209 189.495 1.00 40.90  ? 2972 PHE A CE2   1 
ATOM   12066 C  CZ    . PHE A 1 2972 ? 151.840 172.457 190.638 1.00 39.29  ? 2972 PHE A CZ    1 
ATOM   12067 N  N     . ASP A 1 2973 ? 146.458 173.898 188.078 1.00 36.62  ? 2973 ASP A N     1 
ATOM   12068 C  CA    . ASP A 1 2973 ? 146.091 175.271 188.407 1.00 34.43  ? 2973 ASP A CA    1 
ATOM   12069 C  C     . ASP A 1 2973 ? 144.950 175.303 189.414 1.00 31.72  ? 2973 ASP A C     1 
ATOM   12070 O  O     . ASP A 1 2973 ? 144.972 176.091 190.366 1.00 30.39  ? 2973 ASP A O     1 
ATOM   12071 C  CB    . ASP A 1 2973 ? 145.706 176.031 187.138 1.00 39.53  ? 2973 ASP A CB    1 
ATOM   12072 C  CG    . ASP A 1 2973 ? 146.888 176.272 186.225 1.00 44.45  ? 2973 ASP A CG    1 
ATOM   12073 O  OD1   . ASP A 1 2973 ? 147.936 175.630 186.435 1.00 44.75  ? 2973 ASP A OD1   1 
ATOM   12074 O  OD2   . ASP A 1 2973 ? 146.769 177.101 185.298 1.00 42.42  ? 2973 ASP A OD2   1 
ATOM   12075 N  N     . GLU A 1 2974 ? 143.941 174.450 189.219 1.00 33.91  ? 2974 GLU A N     1 
ATOM   12076 C  CA    . GLU A 1 2974 ? 142.852 174.362 190.184 1.00 32.44  ? 2974 GLU A CA    1 
ATOM   12077 C  C     . GLU A 1 2974 ? 143.351 173.844 191.526 1.00 33.38  ? 2974 GLU A C     1 
ATOM   12078 O  O     . GLU A 1 2974 ? 142.935 174.334 192.583 1.00 34.12  ? 2974 GLU A O     1 
ATOM   12079 C  CB    . GLU A 1 2974 ? 141.739 173.467 189.640 1.00 34.23  ? 2974 GLU A CB    1 
ATOM   12080 C  CG    . GLU A 1 2974 ? 140.352 173.751 190.209 1.00 42.74  ? 2974 GLU A CG    1 
ATOM   12081 C  CD    . GLU A 1 2974 ? 140.137 175.213 190.567 1.00 48.55  ? 2974 GLU A CD    1 
ATOM   12082 O  OE1   . GLU A 1 2974 ? 140.453 175.607 191.710 1.00 42.83  ? 2974 GLU A OE1   1 
ATOM   12083 O  OE2   . GLU A 1 2974 ? 139.653 175.971 189.700 1.00 51.36  ? 2974 GLU A OE2   1 
ATOM   12084 N  N     . ASP A 1 2975 ? 144.239 172.847 191.505 1.00 34.84  ? 2975 ASP A N     1 
ATOM   12085 C  CA    . ASP A 1 2975 ? 144.836 172.366 192.746 1.00 30.88  ? 2975 ASP A CA    1 
ATOM   12086 C  C     . ASP A 1 2975 ? 145.655 173.459 193.417 1.00 31.36  ? 2975 ASP A C     1 
ATOM   12087 O  O     . ASP A 1 2975 ? 145.595 173.625 194.640 1.00 33.33  ? 2975 ASP A O     1 
ATOM   12088 C  CB    . ASP A 1 2975 ? 145.698 171.134 192.478 1.00 37.09  ? 2975 ASP A CB    1 
ATOM   12089 C  CG    . ASP A 1 2975 ? 145.009 169.845 192.880 1.00 44.32  ? 2975 ASP A CG    1 
ATOM   12090 O  OD1   . ASP A 1 2975 ? 143.912 169.916 193.473 1.00 45.37  ? 2975 ASP A OD1   1 
ATOM   12091 O  OD2   . ASP A 1 2975 ? 145.566 168.760 192.606 1.00 46.86  ? 2975 ASP A OD2   1 
ATOM   12092 N  N     . LEU A 1 2976 ? 146.423 174.219 192.631 1.00 31.21  ? 2976 LEU A N     1 
ATOM   12093 C  CA    . LEU A 1 2976 ? 147.158 175.349 193.191 1.00 24.19  ? 2976 LEU A CA    1 
ATOM   12094 C  C     . LEU A 1 2976 ? 146.209 176.376 193.792 1.00 27.26  ? 2976 LEU A C     1 
ATOM   12095 O  O     . LEU A 1 2976 ? 146.431 176.854 194.910 1.00 28.90  ? 2976 LEU A O     1 
ATOM   12096 C  CB    . LEU A 1 2976 ? 148.031 175.997 192.116 1.00 24.40  ? 2976 LEU A CB    1 
ATOM   12097 C  CG    . LEU A 1 2976 ? 149.423 175.407 191.886 1.00 28.04  ? 2976 LEU A CG    1 
ATOM   12098 C  CD1   . LEU A 1 2976 ? 150.188 176.235 190.865 1.00 32.00  ? 2976 LEU A CD1   1 
ATOM   12099 C  CD2   . LEU A 1 2976 ? 150.195 175.318 193.194 1.00 33.10  ? 2976 LEU A CD2   1 
ATOM   12100 N  N     . ARG A 1 2977 ? 145.133 176.708 193.073 1.00 30.30  ? 2977 ARG A N     1 
ATOM   12101 C  CA    . ARG A 1 2977 ? 144.171 177.687 193.573 1.00 27.93  ? 2977 ARG A CA    1 
ATOM   12102 C  C     . ARG A 1 2977 ? 143.604 177.266 194.922 1.00 31.06  ? 2977 ARG A C     1 
ATOM   12103 O  O     . ARG A 1 2977 ? 143.316 178.114 195.775 1.00 32.35  ? 2977 ARG A O     1 
ATOM   12104 C  CB    . ARG A 1 2977 ? 143.047 177.879 192.557 1.00 28.99  ? 2977 ARG A CB    1 
ATOM   12105 C  CG    . ARG A 1 2977 ? 143.415 178.763 191.378 1.00 31.64  ? 2977 ARG A CG    1 
ATOM   12106 C  CD    . ARG A 1 2977 ? 142.272 178.851 190.379 1.00 32.76  ? 2977 ARG A CD    1 
ATOM   12107 N  NE    . ARG A 1 2977 ? 142.756 178.896 189.005 1.00 38.42  ? 2977 ARG A NE    1 
ATOM   12108 C  CZ    . ARG A 1 2977 ? 142.455 178.000 188.074 1.00 38.46  ? 2977 ARG A CZ    1 
ATOM   12109 N  NH1   . ARG A 1 2977 ? 141.666 176.971 188.335 1.00 32.68  ? 2977 ARG A NH1   1 
ATOM   12110 N  NH2   . ARG A 1 2977 ? 142.960 178.140 186.852 1.00 38.47  ? 2977 ARG A NH2   1 
ATOM   12111 N  N     . THR A 1 2978 ? 143.431 175.959 195.132 1.00 28.21  ? 2978 THR A N     1 
ATOM   12112 C  CA    . THR A 1 2978 ? 142.945 175.472 196.418 1.00 27.48  ? 2978 THR A CA    1 
ATOM   12113 C  C     . THR A 1 2978 ? 143.947 175.764 197.530 1.00 31.64  ? 2978 THR A C     1 
ATOM   12114 O  O     . THR A 1 2978 ? 143.569 176.199 198.624 1.00 35.05  ? 2978 THR A O     1 
ATOM   12115 C  CB    . THR A 1 2978 ? 142.651 173.974 196.333 1.00 30.66  ? 2978 THR A CB    1 
ATOM   12116 O  OG1   . THR A 1 2978 ? 141.686 173.732 195.301 1.00 29.83  ? 2978 THR A OG1   1 
ATOM   12117 C  CG2   . THR A 1 2978 ? 142.100 173.463 197.655 1.00 32.83  ? 2978 THR A CG2   1 
ATOM   12118 N  N     . VAL A 1 2979 ? 145.237 175.535 197.266 1.00 30.50  ? 2979 VAL A N     1 
ATOM   12119 C  CA    . VAL A 1 2979 ? 146.257 175.793 198.280 1.00 28.90  ? 2979 VAL A CA    1 
ATOM   12120 C  C     . VAL A 1 2979 ? 146.382 177.286 198.550 1.00 25.29  ? 2979 VAL A C     1 
ATOM   12121 O  O     . VAL A 1 2979 ? 146.452 177.719 199.706 1.00 25.99  ? 2979 VAL A O     1 
ATOM   12122 C  CB    . VAL A 1 2979 ? 147.609 175.188 197.859 1.00 31.83  ? 2979 VAL A CB    1 
ATOM   12123 C  CG1   . VAL A 1 2979 ? 148.487 174.974 199.074 1.00 28.37  ? 2979 VAL A CG1   1 
ATOM   12124 C  CG2   . VAL A 1 2979 ? 147.404 173.887 197.126 1.00 29.20  ? 2979 VAL A CG2   1 
ATOM   12125 N  N     . LEU A 1 2980 ? 146.422 178.096 197.488 1.00 27.94  ? 2980 LEU A N     1 
ATOM   12126 C  CA    . LEU A 1 2980 ? 146.544 179.539 197.665 1.00 27.54  ? 2980 LEU A CA    1 
ATOM   12127 C  C     . LEU A 1 2980 ? 145.351 180.108 198.422 1.00 30.92  ? 2980 LEU A C     1 
ATOM   12128 O  O     . LEU A 1 2980 ? 145.517 180.962 199.301 1.00 32.56  ? 2980 LEU A O     1 
ATOM   12129 C  CB    . LEU A 1 2980 ? 146.697 180.228 196.307 1.00 28.04  ? 2980 LEU A CB    1 
ATOM   12130 C  CG    . LEU A 1 2980 ? 148.091 180.340 195.675 1.00 31.44  ? 2980 LEU A CG    1 
ATOM   12131 C  CD1   . LEU A 1 2980 ? 149.093 180.849 196.686 1.00 28.12  ? 2980 LEU A CD1   1 
ATOM   12132 C  CD2   . LEU A 1 2980 ? 148.572 179.032 195.073 1.00 27.99  ? 2980 LEU A CD2   1 
ATOM   12133 N  N     . ARG A 1 2981 ? 144.141 179.647 198.098 1.00 30.72  ? 2981 ARG A N     1 
ATOM   12134 C  CA    . ARG A 1 2981 ? 142.951 180.136 198.788 1.00 28.57  ? 2981 ARG A CA    1 
ATOM   12135 C  C     . ARG A 1 2981 ? 142.974 179.764 200.265 1.00 30.49  ? 2981 ARG A C     1 
ATOM   12136 O  O     . ARG A 1 2981 ? 142.633 180.583 201.126 1.00 32.06  ? 2981 ARG A O     1 
ATOM   12137 C  CB    . ARG A 1 2981 ? 141.695 179.582 198.119 1.00 27.48  ? 2981 ARG A CB    1 
ATOM   12138 C  CG    . ARG A 1 2981 ? 141.034 180.541 197.149 1.00 34.02  ? 2981 ARG A CG    1 
ATOM   12139 C  CD    . ARG A 1 2981 ? 140.234 179.785 196.106 1.00 33.38  ? 2981 ARG A CD    1 
ATOM   12140 N  NE    . ARG A 1 2981 ? 139.587 180.682 195.157 1.00 45.48  ? 2981 ARG A NE    1 
ATOM   12141 C  CZ    . ARG A 1 2981 ? 139.348 180.379 193.889 1.00 48.61  ? 2981 ARG A CZ    1 
ATOM   12142 N  NH1   . ARG A 1 2981 ? 139.694 179.207 193.381 1.00 41.74  ? 2981 ARG A NH1   1 
ATOM   12143 N  NH2   . ARG A 1 2981 ? 138.750 181.276 193.109 1.00 55.11  ? 2981 ARG A NH2   1 
ATOM   12144 N  N     . ARG A 1 2982 ? 143.373 178.530 200.577 1.00 30.01  ? 2982 ARG A N     1 
ATOM   12145 C  CA    . ARG A 1 2982 ? 143.368 178.080 201.965 1.00 27.16  ? 2982 ARG A CA    1 
ATOM   12146 C  C     . ARG A 1 2982 ? 144.487 178.733 202.768 1.00 27.65  ? 2982 ARG A C     1 
ATOM   12147 O  O     . ARG A 1 2982 ? 144.289 179.104 203.930 1.00 31.52  ? 2982 ARG A O     1 
ATOM   12148 C  CB    . ARG A 1 2982 ? 143.479 176.557 202.015 1.00 27.07  ? 2982 ARG A CB    1 
ATOM   12149 C  CG    . ARG A 1 2982 ? 142.229 175.827 201.550 1.00 27.77  ? 2982 ARG A CG    1 
ATOM   12150 C  CD    . ARG A 1 2982 ? 142.471 174.330 201.412 1.00 33.64  ? 2982 ARG A CD    1 
ATOM   12151 N  NE    . ARG A 1 2982 ? 142.995 173.734 202.635 1.00 30.71  ? 2982 ARG A NE    1 
ATOM   12152 C  CZ    . ARG A 1 2982 ? 143.493 172.507 202.714 1.00 30.35  ? 2982 ARG A CZ    1 
ATOM   12153 N  NH1   . ARG A 1 2982 ? 143.549 171.715 201.656 1.00 32.71  ? 2982 ARG A NH1   1 
ATOM   12154 N  NH2   . ARG A 1 2982 ? 143.947 172.065 203.882 1.00 28.40  ? 2982 ARG A NH2   1 
ATOM   12155 N  N     . SER A 1 2983 ? 145.667 178.886 202.168 1.00 26.00  ? 2983 SER A N     1 
ATOM   12156 C  CA    . SER A 1 2983 ? 146.814 179.455 202.862 1.00 25.95  ? 2983 SER A CA    1 
ATOM   12157 C  C     . SER A 1 2983 ? 146.886 180.973 202.764 1.00 28.23  ? 2983 SER A C     1 
ATOM   12158 O  O     . SER A 1 2983 ? 147.728 181.579 203.435 1.00 33.33  ? 2983 SER A O     1 
ATOM   12159 C  CB    . SER A 1 2983 ? 148.114 178.853 202.318 1.00 30.08  ? 2983 SER A CB    1 
ATOM   12160 O  OG    . SER A 1 2983 ? 148.377 179.306 201.001 1.00 27.51  ? 2983 SER A OG    1 
ATOM   12161 N  N     . GLY A 1 2984 ? 146.038 181.598 201.952 1.00 32.30  ? 2984 GLY A N     1 
ATOM   12162 C  CA    . GLY A 1 2984 ? 146.079 183.037 201.792 1.00 29.82  ? 2984 GLY A CA    1 
ATOM   12163 C  C     . GLY A 1 2984 ? 144.857 183.750 202.333 1.00 35.24  ? 2984 GLY A C     1 
ATOM   12164 O  O     . GLY A 1 2984 ? 144.953 184.887 202.804 1.00 41.62  ? 2984 GLY A O     1 
ATOM   12165 N  N     . CYS A 1 2985 ? 143.700 183.095 202.271 1.00 34.94  ? 2985 CYS A N     1 
ATOM   12166 C  CA    . CYS A 1 2985 ? 142.447 183.690 202.718 1.00 37.20  ? 2985 CYS A CA    1 
ATOM   12167 C  C     . CYS A 1 2985 ? 141.956 183.125 204.044 1.00 36.51  ? 2985 CYS A C     1 
ATOM   12168 O  O     . CYS A 1 2985 ? 141.371 183.861 204.843 1.00 36.19  ? 2985 CYS A O     1 
ATOM   12169 C  CB    . CYS A 1 2985 ? 141.362 183.500 201.654 1.00 35.65  ? 2985 CYS A CB    1 
ATOM   12170 S  SG    . CYS A 1 2985 ? 141.807 184.132 200.022 1.00 52.10  ? 2985 CYS A SG    1 
ATOM   12171 N  N     . LYS A 1 2986 ? 142.182 181.839 204.299 1.00 35.66  ? 2986 LYS A N     1 
ATOM   12172 C  CA    . LYS A 1 2986 ? 141.703 181.198 205.516 1.00 36.15  ? 2986 LYS A CA    1 
ATOM   12173 C  C     . LYS A 1 2986 ? 142.737 181.189 206.634 1.00 38.09  ? 2986 LYS A C     1 
ATOM   12174 O  O     . LYS A 1 2986 ? 142.455 180.646 207.708 1.00 38.52  ? 2986 LYS A O     1 
ATOM   12175 C  CB    . LYS A 1 2986 ? 141.262 179.762 205.214 1.00 33.44  ? 2986 LYS A CB    1 
ATOM   12176 C  CG    . LYS A 1 2986 ? 140.437 179.622 203.946 1.00 33.51  ? 2986 LYS A CG    1 
ATOM   12177 C  CD    . LYS A 1 2986 ? 139.062 180.246 204.112 1.00 38.83  ? 2986 LYS A CD    1 
ATOM   12178 C  CE    . LYS A 1 2986 ? 138.204 180.028 202.878 1.00 41.02  ? 2986 LYS A CE    1 
ATOM   12179 N  NZ    . LYS A 1 2986 ? 137.165 181.085 202.731 1.00 41.97  ? 2986 LYS A NZ    1 
ATOM   12180 N  N     . ASN A 1 2987 ? 143.913 181.781 206.412 1.00 37.05  ? 2987 ASN A N     1 
ATOM   12181 C  CA    . ASN A 1 2987 ? 144.983 181.819 207.411 1.00 37.58  ? 2987 ASN A CA    1 
ATOM   12182 C  C     . ASN A 1 2987 ? 145.335 180.415 207.895 1.00 38.56  ? 2987 ASN A C     1 
ATOM   12183 O  O     . ASN A 1 2987 ? 145.544 180.176 209.087 1.00 39.99  ? 2987 ASN A O     1 
ATOM   12184 C  CB    . ASN A 1 2987 ? 144.608 182.727 208.584 1.00 36.86  ? 2987 ASN A CB    1 
ATOM   12185 C  CG    . ASN A 1 2987 ? 145.815 183.175 209.385 1.00 42.00  ? 2987 ASN A CG    1 
ATOM   12186 O  OD1   . ASN A 1 2987 ? 146.827 183.595 208.822 1.00 41.93  ? 2987 ASN A OD1   1 
ATOM   12187 N  ND2   . ASN A 1 2987 ? 145.715 183.087 210.706 1.00 41.97  ? 2987 ASN A ND2   1 
ATOM   12188 N  N     . GLU A 1 2988 ? 145.400 179.475 206.958 1.00 34.23  ? 2988 GLU A N     1 
ATOM   12189 C  CA    . GLU A 1 2988 ? 145.668 178.076 207.257 1.00 29.05  ? 2988 GLU A CA    1 
ATOM   12190 C  C     . GLU A 1 2988 ? 147.094 177.733 206.855 1.00 34.81  ? 2988 GLU A C     1 
ATOM   12191 O  O     . GLU A 1 2988 ? 147.501 177.980 205.715 1.00 31.59  ? 2988 GLU A O     1 
ATOM   12192 C  CB    . GLU A 1 2988 ? 144.676 177.165 206.530 1.00 31.20  ? 2988 GLU A CB    1 
ATOM   12193 C  CG    . GLU A 1 2988 ? 145.075 175.700 206.504 1.00 30.70  ? 2988 GLU A CG    1 
ATOM   12194 C  CD    . GLU A 1 2988 ? 144.061 174.836 205.782 1.00 39.69  ? 2988 GLU A CD    1 
ATOM   12195 O  OE1   . GLU A 1 2988 ? 142.976 175.351 205.440 1.00 35.99  ? 2988 GLU A OE1   1 
ATOM   12196 O  OE2   . GLU A 1 2988 ? 144.347 173.642 205.557 1.00 38.72  ? 2988 GLU A OE2   1 
ATOM   12197 N  N     . LYS A 1 2989 ? 147.848 177.166 207.793 1.00 33.91  ? 2989 LYS A N     1 
ATOM   12198 C  CA    . LYS A 1 2989 ? 149.215 176.739 207.524 1.00 24.11  ? 2989 LYS A CA    1 
ATOM   12199 C  C     . LYS A 1 2989 ? 149.187 175.381 206.833 1.00 24.03  ? 2989 LYS A C     1 
ATOM   12200 O  O     . LYS A 1 2989 ? 148.685 174.403 207.396 1.00 24.98  ? 2989 LYS A O     1 
ATOM   12201 C  CB    . LYS A 1 2989 ? 150.012 176.675 208.823 1.00 25.64  ? 2989 LYS A CB    1 
ATOM   12202 C  CG    . LYS A 1 2989 ? 150.368 178.034 209.402 1.00 30.80  ? 2989 LYS A CG    1 
ATOM   12203 C  CD    . LYS A 1 2989 ? 151.372 177.904 210.535 1.00 29.38  ? 2989 LYS A CD    1 
ATOM   12204 C  CE    . LYS A 1 2989 ? 150.736 177.260 211.756 1.00 40.49  ? 2989 LYS A CE    1 
ATOM   12205 N  NZ    . LYS A 1 2989 ? 151.659 177.241 212.923 1.00 46.14  ? 2989 LYS A NZ    1 
ATOM   12206 N  N     . ILE A 1 2990 ? 149.724 175.320 205.617 1.00 22.84  ? 2990 ILE A N     1 
ATOM   12207 C  CA    . ILE A 1 2990 ? 149.651 174.127 204.784 1.00 20.63  ? 2990 ILE A CA    1 
ATOM   12208 C  C     . ILE A 1 2990 ? 151.055 173.752 204.334 1.00 21.86  ? 2990 ILE A C     1 
ATOM   12209 O  O     . ILE A 1 2990 ? 151.816 174.611 203.875 1.00 21.46  ? 2990 ILE A O     1 
ATOM   12210 C  CB    . ILE A 1 2990 ? 148.730 174.338 203.566 1.00 23.57  ? 2990 ILE A CB    1 
ATOM   12211 C  CG1   . ILE A 1 2990 ? 147.288 173.993 203.925 1.00 24.44  ? 2990 ILE A CG1   1 
ATOM   12212 C  CG2   . ILE A 1 2990 ? 149.183 173.495 202.382 1.00 25.76  ? 2990 ILE A CG2   1 
ATOM   12213 C  CD1   . ILE A 1 2990 ? 146.279 174.672 203.045 1.00 25.58  ? 2990 ILE A CD1   1 
ATOM   12214 N  N     . ALA A 1 2991 ? 151.397 172.473 204.473 1.00 19.68  ? 2991 ALA A N     1 
ATOM   12215 C  CA    . ALA A 1 2991 ? 152.634 171.922 203.935 1.00 18.06  ? 2991 ALA A CA    1 
ATOM   12216 C  C     . ALA A 1 2991 ? 152.307 171.245 202.608 1.00 20.60  ? 2991 ALA A C     1 
ATOM   12217 O  O     . ALA A 1 2991 ? 151.712 170.164 202.585 1.00 24.65  ? 2991 ALA A O     1 
ATOM   12218 C  CB    . ALA A 1 2991 ? 153.270 170.941 204.917 1.00 21.63  ? 2991 ALA A CB    1 
ATOM   12219 N  N     . PHE A 1 2992 ? 152.695 171.884 201.506 1.00 19.14  ? 2992 PHE A N     1 
ATOM   12220 C  CA    . PHE A 1 2992 ? 152.401 171.381 200.166 1.00 16.65  ? 2992 PHE A CA    1 
ATOM   12221 C  C     . PHE A 1 2992 ? 153.519 170.409 199.803 1.00 18.62  ? 2992 PHE A C     1 
ATOM   12222 O  O     . PHE A 1 2992 ? 154.643 170.818 199.503 1.00 20.04  ? 2992 PHE A O     1 
ATOM   12223 C  CB    . PHE A 1 2992 ? 152.292 172.539 199.176 1.00 16.85  ? 2992 PHE A CB    1 
ATOM   12224 C  CG    . PHE A 1 2992 ? 151.944 172.130 197.761 1.00 18.75  ? 2992 PHE A CG    1 
ATOM   12225 C  CD1   . PHE A 1 2992 ? 151.897 173.083 196.757 1.00 22.12  ? 2992 PHE A CD1   1 
ATOM   12226 C  CD2   . PHE A 1 2992 ? 151.615 170.821 197.443 1.00 22.28  ? 2992 PHE A CD2   1 
ATOM   12227 C  CE1   . PHE A 1 2992 ? 151.571 172.734 195.461 1.00 30.88  ? 2992 PHE A CE1   1 
ATOM   12228 C  CE2   . PHE A 1 2992 ? 151.290 170.467 196.149 1.00 27.65  ? 2992 PHE A CE2   1 
ATOM   12229 C  CZ    . PHE A 1 2992 ? 151.265 171.425 195.157 1.00 31.89  ? 2992 PHE A CZ    1 
ATOM   12230 N  N     . ILE A 1 2993 ? 153.208 169.118 199.828 1.00 20.33  ? 2993 ILE A N     1 
ATOM   12231 C  CA    . ILE A 1 2993 ? 154.184 168.074 199.540 1.00 17.24  ? 2993 ILE A CA    1 
ATOM   12232 C  C     . ILE A 1 2993 ? 154.048 167.684 198.075 1.00 21.04  ? 2993 ILE A C     1 
ATOM   12233 O  O     . ILE A 1 2993 ? 152.972 167.271 197.630 1.00 27.35  ? 2993 ILE A O     1 
ATOM   12234 C  CB    . ILE A 1 2993 ? 153.987 166.859 200.458 1.00 18.46  ? 2993 ILE A CB    1 
ATOM   12235 C  CG1   . ILE A 1 2993 ? 154.631 167.114 201.820 1.00 17.40  ? 2993 ILE A CG1   1 
ATOM   12236 C  CG2   . ILE A 1 2993 ? 154.583 165.611 199.829 1.00 26.02  ? 2993 ILE A CG2   1 
ATOM   12237 C  CD1   . ILE A 1 2993 ? 154.631 165.907 202.723 1.00 24.83  ? 2993 ILE A CD1   1 
ATOM   12238 N  N     . MET A 1 2994 ? 155.137 167.820 197.324 1.00 18.74  ? 2994 MET A N     1 
ATOM   12239 C  CA    . MET A 1 2994 ? 155.138 167.552 195.895 1.00 22.15  ? 2994 MET A CA    1 
ATOM   12240 C  C     . MET A 1 2994 ? 156.375 166.747 195.530 1.00 25.54  ? 2994 MET A C     1 
ATOM   12241 O  O     . MET A 1 2994 ? 157.481 167.051 195.986 1.00 27.47  ? 2994 MET A O     1 
ATOM   12242 C  CB    . MET A 1 2994 ? 155.093 168.860 195.096 1.00 28.18  ? 2994 MET A CB    1 
ATOM   12243 C  CG    . MET A 1 2994 ? 154.744 168.693 193.631 1.00 37.41  ? 2994 MET A CG    1 
ATOM   12244 S  SD    . MET A 1 2994 ? 154.742 170.268 192.755 1.00 65.80  ? 2994 MET A SD    1 
ATOM   12245 C  CE    . MET A 1 2994 ? 154.735 169.712 191.055 1.00 56.72  ? 2994 MET A CE    1 
ATOM   12246 N  N     . ASP A 1 2995 ? 156.183 165.719 194.709 1.00 28.92  ? 2995 ASP A N     1 
ATOM   12247 C  CA    . ASP A 1 2995 ? 157.257 164.837 194.280 1.00 29.92  ? 2995 ASP A CA    1 
ATOM   12248 C  C     . ASP A 1 2995 ? 157.555 165.063 192.803 1.00 33.42  ? 2995 ASP A C     1 
ATOM   12249 O  O     . ASP A 1 2995 ? 156.727 165.586 192.053 1.00 38.30  ? 2995 ASP A O     1 
ATOM   12250 C  CB    . ASP A 1 2995 ? 156.889 163.369 194.537 1.00 31.62  ? 2995 ASP A CB    1 
ATOM   12251 C  CG    . ASP A 1 2995 ? 158.001 162.409 194.159 1.00 41.42  ? 2995 ASP A CG    1 
ATOM   12252 O  OD1   . ASP A 1 2995 ? 158.996 162.324 194.909 1.00 36.23  ? 2995 ASP A OD1   1 
ATOM   12253 O  OD2   . ASP A 1 2995 ? 157.882 161.740 193.111 1.00 47.43  ? 2995 ASP A OD2   1 
ATOM   12254 N  N     . GLU A 1 2996 ? 158.766 164.671 192.392 1.00 35.29  ? 2996 GLU A N     1 
ATOM   12255 C  CA    . GLU A 1 2996 ? 159.165 164.840 190.998 1.00 37.46  ? 2996 GLU A CA    1 
ATOM   12256 C  C     . GLU A 1 2996 ? 158.279 164.036 190.054 1.00 40.81  ? 2996 GLU A C     1 
ATOM   12257 O  O     . GLU A 1 2996 ? 158.139 164.395 188.879 1.00 37.03  ? 2996 GLU A O     1 
ATOM   12258 C  CB    . GLU A 1 2996 ? 160.634 164.449 190.818 1.00 37.30  ? 2996 GLU A CB    1 
ATOM   12259 C  CG    . GLU A 1 2996 ? 160.866 162.976 190.514 1.00 43.14  ? 2996 GLU A CG    1 
ATOM   12260 C  CD    . GLU A 1 2996 ? 162.212 162.478 191.004 1.00 44.50  ? 2996 GLU A CD    1 
ATOM   12261 O  OE1   . GLU A 1 2996 ? 162.250 161.426 191.676 1.00 40.57  ? 2996 GLU A OE1   1 
ATOM   12262 O  OE2   . GLU A 1 2996 ? 163.233 163.138 190.716 1.00 45.30  ? 2996 GLU A OE2   1 
ATOM   12263 N  N     . SER A 1 2997 ? 157.675 162.949 190.542 1.00 41.65  ? 2997 SER A N     1 
ATOM   12264 C  CA    . SER A 1 2997 ? 156.766 162.174 189.704 1.00 41.40  ? 2997 SER A CA    1 
ATOM   12265 C  C     . SER A 1 2997 ? 155.463 162.920 189.454 1.00 43.73  ? 2997 SER A C     1 
ATOM   12266 O  O     . SER A 1 2997 ? 154.797 162.680 188.440 1.00 50.19  ? 2997 SER A O     1 
ATOM   12267 C  CB    . SER A 1 2997 ? 156.487 160.815 190.345 1.00 42.92  ? 2997 SER A CB    1 
ATOM   12268 O  OG    . SER A 1 2997 ? 155.939 160.966 191.643 1.00 50.36  ? 2997 SER A OG    1 
ATOM   12269 N  N     . ASN A 1 2998 ? 155.083 163.823 190.362 1.00 39.61  ? 2998 ASN A N     1 
ATOM   12270 C  CA    . ASN A 1 2998 ? 153.878 164.621 190.171 1.00 40.77  ? 2998 ASN A CA    1 
ATOM   12271 C  C     . ASN A 1 2998 ? 154.004 165.590 189.005 1.00 45.53  ? 2998 ASN A C     1 
ATOM   12272 O  O     . ASN A 1 2998 ? 152.987 166.110 188.533 1.00 58.02  ? 2998 ASN A O     1 
ATOM   12273 C  CB    . ASN A 1 2998 ? 153.552 165.394 191.450 1.00 41.65  ? 2998 ASN A CB    1 
ATOM   12274 C  CG    . ASN A 1 2998 ? 153.094 164.492 192.577 1.00 41.45  ? 2998 ASN A CG    1 
ATOM   12275 O  OD1   . ASN A 1 2998 ? 152.872 163.298 192.381 1.00 38.65  ? 2998 ASN A OD1   1 
ATOM   12276 N  ND2   . ASN A 1 2998 ? 152.956 165.059 193.770 1.00 37.50  ? 2998 ASN A ND2   1 
ATOM   12277 N  N     . VAL A 1 2999 ? 155.222 165.847 188.535 1.00 48.33  ? 2999 VAL A N     1 
ATOM   12278 C  CA    . VAL A 1 2999 ? 155.451 166.772 187.429 1.00 47.57  ? 2999 VAL A CA    1 
ATOM   12279 C  C     . VAL A 1 2999 ? 155.237 166.011 186.124 1.00 57.40  ? 2999 VAL A C     1 
ATOM   12280 O  O     . VAL A 1 2999 ? 156.001 165.103 185.791 1.00 60.10  ? 2999 VAL A O     1 
ATOM   12281 C  CB    . VAL A 1 2999 ? 156.855 167.381 187.491 1.00 44.22  ? 2999 VAL A CB    1 
ATOM   12282 C  CG1   . VAL A 1 2999 ? 157.066 168.348 186.339 1.00 42.92  ? 2999 VAL A CG1   1 
ATOM   12283 C  CG2   . VAL A 1 2999 ? 157.077 168.066 188.828 1.00 44.07  ? 2999 VAL A CG2   1 
ATOM   12284 N  N     . LEU A 1 3000 ? 154.194 166.383 185.381 1.00 56.42  ? 3000 LEU A N     1 
ATOM   12285 C  CA    . LEU A 1 3000 ? 153.901 165.755 184.100 1.00 58.64  ? 3000 LEU A CA    1 
ATOM   12286 C  C     . LEU A 1 3000 ? 154.271 166.623 182.906 1.00 61.17  ? 3000 LEU A C     1 
ATOM   12287 O  O     . LEU A 1 3000 ? 154.192 166.148 181.768 1.00 67.51  ? 3000 LEU A O     1 
ATOM   12288 C  CB    . LEU A 1 3000 ? 152.411 165.399 184.013 1.00 60.09  ? 3000 LEU A CB    1 
ATOM   12289 C  CG    . LEU A 1 3000 ? 151.889 164.339 184.983 1.00 58.98  ? 3000 LEU A CG    1 
ATOM   12290 C  CD1   . LEU A 1 3000 ? 150.379 164.212 184.863 1.00 59.43  ? 3000 LEU A CD1   1 
ATOM   12291 C  CD2   . LEU A 1 3000 ? 152.564 163.001 184.730 1.00 55.32  ? 3000 LEU A CD2   1 
ATOM   12292 N  N     . ASP A 1 3001 ? 154.672 167.871 183.138 1.00 55.12  ? 3001 ASP A N     1 
ATOM   12293 C  CA    . ASP A 1 3001 ? 154.969 168.809 182.066 1.00 64.76  ? 3001 ASP A CA    1 
ATOM   12294 C  C     . ASP A 1 3001 ? 155.814 169.942 182.630 1.00 59.55  ? 3001 ASP A C     1 
ATOM   12295 O  O     . ASP A 1 3001 ? 155.918 170.123 183.846 1.00 57.26  ? 3001 ASP A O     1 
ATOM   12296 C  CB    . ASP A 1 3001 ? 153.688 169.358 181.429 1.00 65.81  ? 3001 ASP A CB    1 
ATOM   12297 C  CG    . ASP A 1 3001 ? 153.311 168.632 180.154 1.00 74.15  ? 3001 ASP A CG    1 
ATOM   12298 O  OD1   . ASP A 1 3001 ? 154.037 168.777 179.148 1.00 69.69  ? 3001 ASP A OD1   1 
ATOM   12299 O  OD2   . ASP A 1 3001 ? 152.287 167.917 180.157 1.00 76.54  ? 3001 ASP A OD2   1 
ATOM   12300 N  N     . SER A 1 3002 ? 156.420 170.713 181.725 1.00 58.48  ? 3002 SER A N     1 
ATOM   12301 C  CA    . SER A 1 3002 ? 157.184 171.882 182.143 1.00 56.09  ? 3002 SER A CA    1 
ATOM   12302 C  C     . SER A 1 3002 ? 156.286 173.007 182.641 1.00 52.69  ? 3002 SER A C     1 
ATOM   12303 O  O     . SER A 1 3002 ? 156.778 173.930 183.300 1.00 48.18  ? 3002 SER A O     1 
ATOM   12304 C  CB    . SER A 1 3002 ? 158.058 172.382 180.993 1.00 47.07  ? 3002 SER A CB    1 
ATOM   12305 O  OG    . SER A 1 3002 ? 159.257 172.959 181.479 1.00 52.03  ? 3002 SER A OG    1 
ATOM   12306 N  N     . GLY A 1 3003 ? 154.987 172.955 182.338 1.00 49.66  ? 3003 GLY A N     1 
ATOM   12307 C  CA    . GLY A 1 3003 ? 154.074 173.958 182.859 1.00 46.29  ? 3003 GLY A CA    1 
ATOM   12308 C  C     . GLY A 1 3003 ? 153.926 173.883 184.366 1.00 45.20  ? 3003 GLY A C     1 
ATOM   12309 O  O     . GLY A 1 3003 ? 153.732 174.902 185.032 1.00 42.18  ? 3003 GLY A O     1 
ATOM   12310 N  N     . PHE A 1 3004 ? 154.007 172.672 184.921 1.00 48.37  ? 3004 PHE A N     1 
ATOM   12311 C  CA    . PHE A 1 3004 ? 153.918 172.490 186.367 1.00 45.96  ? 3004 PHE A CA    1 
ATOM   12312 C  C     . PHE A 1 3004 ? 155.005 173.277 187.088 1.00 41.41  ? 3004 PHE A C     1 
ATOM   12313 O  O     . PHE A 1 3004 ? 154.741 173.963 188.082 1.00 41.63  ? 3004 PHE A O     1 
ATOM   12314 C  CB    . PHE A 1 3004 ? 154.033 171.002 186.701 1.00 49.21  ? 3004 PHE A CB    1 
ATOM   12315 C  CG    . PHE A 1 3004 ? 152.874 170.178 186.222 1.00 51.37  ? 3004 PHE A CG    1 
ATOM   12316 C  CD1   . PHE A 1 3004 ? 151.716 170.078 186.967 1.00 52.26  ? 3004 PHE A CD1   1 
ATOM   12317 C  CD2   . PHE A 1 3004 ? 152.934 169.529 185.005 1.00 58.83  ? 3004 PHE A CD2   1 
ATOM   12318 C  CE1   . PHE A 1 3004 ? 150.652 169.317 186.519 1.00 51.61  ? 3004 PHE A CE1   1 
ATOM   12319 C  CE2   . PHE A 1 3004 ? 151.872 168.775 184.549 1.00 62.34  ? 3004 PHE A CE2   1 
ATOM   12320 C  CZ    . PHE A 1 3004 ? 150.729 168.669 185.308 1.00 54.25  ? 3004 PHE A CZ    1 
ATOM   12321 N  N     . LEU A 1 3005 ? 156.241 173.186 186.595 1.00 41.35  ? 3005 LEU A N     1 
ATOM   12322 C  CA    . LEU A 1 3005 ? 157.367 173.797 187.291 1.00 40.23  ? 3005 LEU A CA    1 
ATOM   12323 C  C     . LEU A 1 3005 ? 157.411 175.307 187.099 1.00 37.64  ? 3005 LEU A C     1 
ATOM   12324 O  O     . LEU A 1 3005 ? 157.943 176.020 187.957 1.00 39.23  ? 3005 LEU A O     1 
ATOM   12325 C  CB    . LEU A 1 3005 ? 158.671 173.158 186.819 1.00 42.92  ? 3005 LEU A CB    1 
ATOM   12326 C  CG    . LEU A 1 3005 ? 158.933 171.740 187.334 1.00 44.98  ? 3005 LEU A CG    1 
ATOM   12327 C  CD1   . LEU A 1 3005 ? 160.417 171.502 187.478 1.00 41.60  ? 3005 LEU A CD1   1 
ATOM   12328 C  CD2   . LEU A 1 3005 ? 158.229 171.500 188.663 1.00 41.38  ? 3005 LEU A CD2   1 
ATOM   12329 N  N     . GLU A 1 3006 ? 156.876 175.810 185.984 1.00 37.59  ? 3006 GLU A N     1 
ATOM   12330 C  CA    . GLU A 1 3006 ? 156.882 177.250 185.747 1.00 32.02  ? 3006 GLU A CA    1 
ATOM   12331 C  C     . GLU A 1 3006 ? 156.061 177.983 186.802 1.00 36.55  ? 3006 GLU A C     1 
ATOM   12332 O  O     . GLU A 1 3006 ? 156.486 179.019 187.326 1.00 38.47  ? 3006 GLU A O     1 
ATOM   12333 C  CB    . GLU A 1 3006 ? 156.356 177.552 184.343 1.00 33.66  ? 3006 GLU A CB    1 
ATOM   12334 C  CG    . GLU A 1 3006 ? 156.273 179.033 184.014 1.00 37.22  ? 3006 GLU A CG    1 
ATOM   12335 C  CD    . GLU A 1 3006 ? 157.523 179.551 183.330 1.00 30.24  ? 3006 GLU A CD    1 
ATOM   12336 O  OE1   . GLU A 1 3006 ? 158.593 178.926 183.486 1.00 29.62  ? 3006 GLU A OE1   1 
ATOM   12337 O  OE2   . GLU A 1 3006 ? 157.436 180.588 182.639 1.00 31.06  ? 3006 GLU A OE2   1 
ATOM   12338 N  N     . ARG A 1 3007 ? 154.879 177.456 187.128 1.00 32.44  ? 3007 ARG A N     1 
ATOM   12339 C  CA    . ARG A 1 3007 ? 154.065 178.064 188.176 1.00 28.48  ? 3007 ARG A CA    1 
ATOM   12340 C  C     . ARG A 1 3007 ? 154.670 177.822 189.551 1.00 31.72  ? 3007 ARG A C     1 
ATOM   12341 O  O     . ARG A 1 3007 ? 154.619 178.696 190.424 1.00 32.09  ? 3007 ARG A O     1 
ATOM   12342 C  CB    . ARG A 1 3007 ? 152.639 177.521 188.112 1.00 34.37  ? 3007 ARG A CB    1 
ATOM   12343 C  CG    . ARG A 1 3007 ? 152.224 177.062 186.730 1.00 41.52  ? 3007 ARG A CG    1 
ATOM   12344 C  CD    . ARG A 1 3007 ? 150.713 177.022 186.589 1.00 43.12  ? 3007 ARG A CD    1 
ATOM   12345 N  NE    . ARG A 1 3007 ? 150.105 178.345 186.485 1.00 50.00  ? 3007 ARG A NE    1 
ATOM   12346 C  CZ    . ARG A 1 3007 ? 150.351 179.227 185.524 1.00 51.66  ? 3007 ARG A CZ    1 
ATOM   12347 N  NH1   . ARG A 1 3007 ? 151.163 178.949 184.516 1.00 50.44  ? 3007 ARG A NH1   1 
ATOM   12348 N  NH2   . ARG A 1 3007 ? 149.752 180.413 185.565 1.00 44.27  ? 3007 ARG A NH2   1 
ATOM   12349 N  N     . MET A 1 3008 ? 155.240 176.633 189.766 1.00 37.32  ? 3008 MET A N     1 
ATOM   12350 C  CA    . MET A 1 3008 ? 155.890 176.340 191.039 1.00 28.45  ? 3008 MET A CA    1 
ATOM   12351 C  C     . MET A 1 3008 ? 157.067 177.275 191.281 1.00 27.87  ? 3008 MET A C     1 
ATOM   12352 O  O     . MET A 1 3008 ? 157.277 177.740 192.407 1.00 28.01  ? 3008 MET A O     1 
ATOM   12353 C  CB    . MET A 1 3008 ? 156.346 174.881 191.071 1.00 32.36  ? 3008 MET A CB    1 
ATOM   12354 C  CG    . MET A 1 3008 ? 155.246 173.892 191.419 1.00 42.31  ? 3008 MET A CG    1 
ATOM   12355 S  SD    . MET A 1 3008 ? 153.997 174.591 192.514 1.00 59.91  ? 3008 MET A SD    1 
ATOM   12356 C  CE    . MET A 1 3008 ? 154.828 174.464 194.095 1.00 30.52  ? 3008 MET A CE    1 
ATOM   12357 N  N     . ASN A 1 3009 ? 157.845 177.561 190.235 1.00 28.42  ? 3009 ASN A N     1 
ATOM   12358 C  CA    . ASN A 1 3009 ? 158.980 178.469 190.372 1.00 26.36  ? 3009 ASN A CA    1 
ATOM   12359 C  C     . ASN A 1 3009 ? 158.525 179.855 190.813 1.00 23.07  ? 3009 ASN A C     1 
ATOM   12360 O  O     . ASN A 1 3009 ? 159.122 180.463 191.709 1.00 28.66  ? 3009 ASN A O     1 
ATOM   12361 C  CB    . ASN A 1 3009 ? 159.742 178.550 189.049 1.00 27.87  ? 3009 ASN A CB    1 
ATOM   12362 C  CG    . ASN A 1 3009 ? 161.164 179.032 189.226 1.00 30.09  ? 3009 ASN A CG    1 
ATOM   12363 O  OD1   . ASN A 1 3009 ? 162.025 178.295 189.704 1.00 34.38  ? 3009 ASN A OD1   1 
ATOM   12364 N  ND2   . ASN A 1 3009 ? 161.421 180.276 188.838 1.00 26.50  ? 3009 ASN A ND2   1 
ATOM   12365 N  N     . THR A 1 3010 ? 157.468 180.373 190.186 1.00 25.81  ? 3010 THR A N     1 
ATOM   12366 C  CA    . THR A 1 3010 ? 156.952 181.685 190.563 1.00 28.18  ? 3010 THR A CA    1 
ATOM   12367 C  C     . THR A 1 3010 ? 156.384 181.669 191.977 1.00 29.57  ? 3010 THR A C     1 
ATOM   12368 O  O     . THR A 1 3010 ? 156.608 182.602 192.756 1.00 27.79  ? 3010 THR A O     1 
ATOM   12369 C  CB    . THR A 1 3010 ? 155.890 182.135 189.560 1.00 25.13  ? 3010 THR A CB    1 
ATOM   12370 O  OG1   . THR A 1 3010 ? 156.479 182.248 188.259 1.00 27.79  ? 3010 THR A OG1   1 
ATOM   12371 C  CG2   . THR A 1 3010 ? 155.316 183.481 189.960 1.00 31.03  ? 3010 THR A CG2   1 
ATOM   12372 N  N     . LEU A 1 3011 ? 155.647 180.611 192.326 1.00 28.53  ? 3011 LEU A N     1 
ATOM   12373 C  CA    . LEU A 1 3011 ? 155.037 180.530 193.650 1.00 25.85  ? 3011 LEU A CA    1 
ATOM   12374 C  C     . LEU A 1 3011 ? 156.091 180.434 194.746 1.00 26.54  ? 3011 LEU A C     1 
ATOM   12375 O  O     . LEU A 1 3011 ? 155.941 181.041 195.813 1.00 25.02  ? 3011 LEU A O     1 
ATOM   12376 C  CB    . LEU A 1 3011 ? 154.084 179.336 193.711 1.00 25.92  ? 3011 LEU A CB    1 
ATOM   12377 C  CG    . LEU A 1 3011 ? 153.514 178.955 195.078 1.00 19.98  ? 3011 LEU A CG    1 
ATOM   12378 C  CD1   . LEU A 1 3011 ? 152.733 180.113 195.677 1.00 25.62  ? 3011 LEU A CD1   1 
ATOM   12379 C  CD2   . LEU A 1 3011 ? 152.641 177.718 194.965 1.00 18.31  ? 3011 LEU A CD2   1 
ATOM   12380 N  N     . LEU A 1 3012 ? 157.160 179.670 194.508 1.00 26.72  ? 3012 LEU A N     1 
ATOM   12381 C  CA    . LEU A 1 3012 ? 158.201 179.517 195.521 1.00 21.83  ? 3012 LEU A CA    1 
ATOM   12382 C  C     . LEU A 1 3012 ? 158.913 180.835 195.798 1.00 25.15  ? 3012 LEU A C     1 
ATOM   12383 O  O     . LEU A 1 3012 ? 159.235 181.142 196.951 1.00 27.36  ? 3012 LEU A O     1 
ATOM   12384 C  CB    . LEU A 1 3012 ? 159.207 178.452 195.086 1.00 24.09  ? 3012 LEU A CB    1 
ATOM   12385 C  CG    . LEU A 1 3012 ? 158.745 176.995 195.120 1.00 22.90  ? 3012 LEU A CG    1 
ATOM   12386 C  CD1   . LEU A 1 3012 ? 159.724 176.106 194.370 1.00 23.55  ? 3012 LEU A CD1   1 
ATOM   12387 C  CD2   . LEU A 1 3012 ? 158.585 176.525 196.551 1.00 18.44  ? 3012 LEU A CD2   1 
ATOM   12388 N  N     . ALA A 1 3013 ? 159.166 181.628 194.756 1.00 26.98  ? 3013 ALA A N     1 
ATOM   12389 C  CA    . ALA A 1 3013 ? 159.955 182.844 194.923 1.00 25.79  ? 3013 ALA A CA    1 
ATOM   12390 C  C     . ALA A 1 3013 ? 159.105 184.010 195.416 1.00 27.48  ? 3013 ALA A C     1 
ATOM   12391 O  O     . ALA A 1 3013 ? 159.434 184.642 196.425 1.00 34.54  ? 3013 ALA A O     1 
ATOM   12392 C  CB    . ALA A 1 3013 ? 160.645 183.203 193.607 1.00 23.10  ? 3013 ALA A CB    1 
ATOM   12393 N  N     . ASN A 1 3014 ? 158.010 184.309 194.719 1.00 29.88  ? 3014 ASN A N     1 
ATOM   12394 C  CA    . ASN A 1 3014 ? 157.202 185.483 195.025 1.00 34.68  ? 3014 ASN A CA    1 
ATOM   12395 C  C     . ASN A 1 3014 ? 156.039 185.198 195.963 1.00 33.58  ? 3014 ASN A C     1 
ATOM   12396 O  O     . ASN A 1 3014 ? 155.555 186.120 196.626 1.00 34.30  ? 3014 ASN A O     1 
ATOM   12397 C  CB    . ASN A 1 3014 ? 156.654 186.101 193.734 1.00 30.17  ? 3014 ASN A CB    1 
ATOM   12398 C  CG    . ASN A 1 3014 ? 157.751 186.536 192.787 1.00 28.81  ? 3014 ASN A CG    1 
ATOM   12399 O  OD1   . ASN A 1 3014 ? 158.600 187.354 193.137 1.00 28.31  ? 3014 ASN A OD1   1 
ATOM   12400 N  ND2   . ASN A 1 3014 ? 157.737 185.992 191.576 1.00 27.12  ? 3014 ASN A ND2   1 
ATOM   12401 N  N     . GLY A 1 3015 ? 155.582 183.953 196.041 1.00 30.53  ? 3015 GLY A N     1 
ATOM   12402 C  CA    . GLY A 1 3015 ? 154.422 183.626 196.840 1.00 29.00  ? 3015 GLY A CA    1 
ATOM   12403 C  C     . GLY A 1 3015 ? 153.092 183.840 196.156 1.00 32.08  ? 3015 GLY A C     1 
ATOM   12404 O  O     . GLY A 1 3015 ? 152.052 183.708 196.810 1.00 36.62  ? 3015 GLY A O     1 
ATOM   12405 N  N     . GLU A 1 3016 ? 153.089 184.169 194.866 1.00 32.48  ? 3016 GLU A N     1 
ATOM   12406 C  CA    . GLU A 1 3016 ? 151.846 184.370 194.132 1.00 32.99  ? 3016 GLU A CA    1 
ATOM   12407 C  C     . GLU A 1 3016 ? 152.108 184.132 192.653 1.00 37.49  ? 3016 GLU A C     1 
ATOM   12408 O  O     . GLU A 1 3016 ? 153.183 184.471 192.151 1.00 41.10  ? 3016 GLU A O     1 
ATOM   12409 C  CB    . GLU A 1 3016 ? 151.286 185.780 194.365 1.00 31.85  ? 3016 GLU A CB    1 
ATOM   12410 C  CG    . GLU A 1 3016 ? 152.346 186.859 194.534 1.00 41.06  ? 3016 GLU A CG    1 
ATOM   12411 C  CD    . GLU A 1 3016 ? 152.868 187.392 193.215 1.00 45.07  ? 3016 GLU A CD    1 
ATOM   12412 O  OE1   . GLU A 1 3016 ? 153.880 188.122 193.232 1.00 41.93  ? 3016 GLU A OE1   1 
ATOM   12413 O  OE2   . GLU A 1 3016 ? 152.256 187.103 192.166 1.00 47.70  ? 3016 GLU A OE2   1 
ATOM   12414 N  N     . VAL A 1 3017 ? 151.132 183.545 191.971 1.00 37.43  ? 3017 VAL A N     1 
ATOM   12415 C  CA    . VAL A 1 3017 ? 151.212 183.291 190.535 1.00 36.01  ? 3017 VAL A CA    1 
ATOM   12416 C  C     . VAL A 1 3017 ? 150.454 184.403 189.818 1.00 37.16  ? 3017 VAL A C     1 
ATOM   12417 O  O     . VAL A 1 3017 ? 149.301 184.688 190.171 1.00 42.04  ? 3017 VAL A O     1 
ATOM   12418 C  CB    . VAL A 1 3017 ? 150.657 181.902 190.186 1.00 34.87  ? 3017 VAL A CB    1 
ATOM   12419 C  CG1   . VAL A 1 3017 ? 150.850 181.596 188.710 1.00 35.89  ? 3017 VAL A CG1   1 
ATOM   12420 C  CG2   . VAL A 1 3017 ? 151.321 180.838 191.047 1.00 28.22  ? 3017 VAL A CG2   1 
ATOM   12421 N  N     . PRO A 1 3018 ? 151.054 185.062 188.821 1.00 41.57  ? 3018 PRO A N     1 
ATOM   12422 C  CA    . PRO A 1 3018 ? 150.386 186.235 188.230 1.00 42.93  ? 3018 PRO A CA    1 
ATOM   12423 C  C     . PRO A 1 3018 ? 149.120 185.898 187.462 1.00 43.12  ? 3018 PRO A C     1 
ATOM   12424 O  O     . PRO A 1 3018 ? 148.121 186.618 187.586 1.00 45.66  ? 3018 PRO A O     1 
ATOM   12425 C  CB    . PRO A 1 3018 ? 151.470 186.825 187.317 1.00 38.93  ? 3018 PRO A CB    1 
ATOM   12426 C  CG    . PRO A 1 3018 ? 152.329 185.658 186.957 1.00 45.34  ? 3018 PRO A CG    1 
ATOM   12427 C  CD    . PRO A 1 3018 ? 152.343 184.768 188.170 1.00 46.25  ? 3018 PRO A CD    1 
ATOM   12428 N  N     . GLY A 1 3019 ? 149.127 184.830 186.670 1.00 37.34  ? 3019 GLY A N     1 
ATOM   12429 C  CA    . GLY A 1 3019 ? 147.976 184.507 185.850 1.00 40.72  ? 3019 GLY A CA    1 
ATOM   12430 C  C     . GLY A 1 3019 ? 147.115 183.385 186.390 1.00 44.30  ? 3019 GLY A C     1 
ATOM   12431 O  O     . GLY A 1 3019 ? 146.296 182.820 185.659 1.00 47.83  ? 3019 GLY A O     1 
ATOM   12432 N  N     . LEU A 1 3020 ? 147.288 183.049 187.670 1.00 39.95  ? 3020 LEU A N     1 
ATOM   12433 C  CA    . LEU A 1 3020 ? 146.527 181.943 188.245 1.00 38.69  ? 3020 LEU A CA    1 
ATOM   12434 C  C     . LEU A 1 3020 ? 145.063 182.317 188.440 1.00 39.88  ? 3020 LEU A C     1 
ATOM   12435 O  O     . LEU A 1 3020 ? 144.168 181.528 188.116 1.00 40.98  ? 3020 LEU A O     1 
ATOM   12436 C  CB    . LEU A 1 3020 ? 147.152 181.508 189.569 1.00 35.73  ? 3020 LEU A CB    1 
ATOM   12437 C  CG    . LEU A 1 3020 ? 146.758 180.120 190.074 1.00 32.30  ? 3020 LEU A CG    1 
ATOM   12438 C  CD1   . LEU A 1 3020 ? 147.335 179.045 189.170 1.00 33.11  ? 3020 LEU A CD1   1 
ATOM   12439 C  CD2   . LEU A 1 3020 ? 147.221 179.921 191.506 1.00 31.06  ? 3020 LEU A CD2   1 
ATOM   12440 N  N     . PHE A 1 3021 ? 144.799 183.511 188.964 1.00 37.93  ? 3021 PHE A N     1 
ATOM   12441 C  CA    . PHE A 1 3021 ? 143.439 183.983 189.201 1.00 40.98  ? 3021 PHE A CA    1 
ATOM   12442 C  C     . PHE A 1 3021 ? 143.091 185.014 188.134 1.00 48.45  ? 3021 PHE A C     1 
ATOM   12443 O  O     . PHE A 1 3021 ? 143.697 186.089 188.077 1.00 53.68  ? 3021 PHE A O     1 
ATOM   12444 C  CB    . PHE A 1 3021 ? 143.295 184.577 190.601 1.00 41.81  ? 3021 PHE A CB    1 
ATOM   12445 C  CG    . PHE A 1 3021 ? 143.553 183.597 191.710 1.00 37.62  ? 3021 PHE A CG    1 
ATOM   12446 C  CD1   . PHE A 1 3021 ? 144.845 183.308 192.116 1.00 34.78  ? 3021 PHE A CD1   1 
ATOM   12447 C  CD2   . PHE A 1 3021 ? 142.499 182.962 192.347 1.00 37.92  ? 3021 PHE A CD2   1 
ATOM   12448 C  CE1   . PHE A 1 3021 ? 145.082 182.408 193.137 1.00 35.40  ? 3021 PHE A CE1   1 
ATOM   12449 C  CE2   . PHE A 1 3021 ? 142.729 182.060 193.367 1.00 37.14  ? 3021 PHE A CE2   1 
ATOM   12450 C  CZ    . PHE A 1 3021 ? 144.022 181.783 193.763 1.00 39.84  ? 3021 PHE A CZ    1 
ATOM   12451 N  N     . GLU A 1 3022 ? 142.115 184.685 187.292 1.00 52.18  ? 3022 GLU A N     1 
ATOM   12452 C  CA    . GLU A 1 3022 ? 141.645 185.589 186.254 1.00 58.71  ? 3022 GLU A CA    1 
ATOM   12453 C  C     . GLU A 1 3022 ? 140.161 185.351 186.020 1.00 61.40  ? 3022 GLU A C     1 
ATOM   12454 O  O     . GLU A 1 3022 ? 139.640 184.266 186.291 1.00 55.91  ? 3022 GLU A O     1 
ATOM   12455 C  CB    . GLU A 1 3022 ? 142.425 185.405 184.945 1.00 56.68  ? 3022 GLU A CB    1 
ATOM   12456 C  CG    . GLU A 1 3022 ? 142.532 183.962 184.480 1.00 56.82  ? 3022 GLU A CG    1 
ATOM   12457 C  CD    . GLU A 1 3022 ? 143.500 183.793 183.325 1.00 65.67  ? 3022 GLU A CD    1 
ATOM   12458 O  OE1   . GLU A 1 3022 ? 144.715 183.994 183.532 1.00 58.61  ? 3022 GLU A OE1   1 
ATOM   12459 O  OE2   . GLU A 1 3022 ? 143.045 183.460 182.211 1.00 65.87  ? 3022 GLU A OE2   1 
ATOM   12460 N  N     . GLY A 1 3023 ? 139.486 186.379 185.510 1.00 61.30  ? 3023 GLY A N     1 
ATOM   12461 C  CA    . GLY A 1 3023 ? 138.056 186.265 185.278 1.00 59.97  ? 3023 GLY A CA    1 
ATOM   12462 C  C     . GLY A 1 3023 ? 137.286 186.230 186.584 1.00 59.13  ? 3023 GLY A C     1 
ATOM   12463 O  O     . GLY A 1 3023 ? 137.566 186.984 187.523 1.00 53.34  ? 3023 GLY A O     1 
ATOM   12464 N  N     . ASP A 1 3024 ? 136.293 185.339 186.648 1.00 62.32  ? 3024 ASP A N     1 
ATOM   12465 C  CA    . ASP A 1 3024 ? 135.491 185.203 187.858 1.00 59.92  ? 3024 ASP A CA    1 
ATOM   12466 C  C     . ASP A 1 3024 ? 136.282 184.610 189.015 1.00 54.79  ? 3024 ASP A C     1 
ATOM   12467 O  O     . ASP A 1 3024 ? 135.908 184.820 190.174 1.00 50.76  ? 3024 ASP A O     1 
ATOM   12468 C  CB    . ASP A 1 3024 ? 134.254 184.348 187.578 1.00 64.54  ? 3024 ASP A CB    1 
ATOM   12469 C  CG    . ASP A 1 3024 ? 134.584 183.074 186.827 1.00 67.72  ? 3024 ASP A CG    1 
ATOM   12470 O  OD1   . ASP A 1 3024 ? 135.755 182.902 186.429 1.00 71.45  ? 3024 ASP A OD1   1 
ATOM   12471 O  OD2   . ASP A 1 3024 ? 133.671 182.243 186.636 1.00 65.48  ? 3024 ASP A OD2   1 
ATOM   12472 N  N     . GLU A 1 3025 ? 137.356 183.869 188.731 1.00 56.84  ? 3025 GLU A N     1 
ATOM   12473 C  CA    . GLU A 1 3025 ? 138.191 183.340 189.805 1.00 51.77  ? 3025 GLU A CA    1 
ATOM   12474 C  C     . GLU A 1 3025 ? 138.858 184.466 190.585 1.00 50.72  ? 3025 GLU A C     1 
ATOM   12475 O  O     . GLU A 1 3025 ? 138.932 184.420 191.818 1.00 52.12  ? 3025 GLU A O     1 
ATOM   12476 C  CB    . GLU A 1 3025 ? 139.239 182.383 189.236 1.00 48.88  ? 3025 GLU A CB    1 
ATOM   12477 C  CG    . GLU A 1 3025 ? 138.676 181.060 188.730 1.00 54.91  ? 3025 GLU A CG    1 
ATOM   12478 C  CD    . GLU A 1 3025 ? 138.472 180.034 189.834 1.00 64.53  ? 3025 GLU A CD    1 
ATOM   12479 O  OE1   . GLU A 1 3025 ? 138.123 180.424 190.968 1.00 60.68  ? 3025 GLU A OE1   1 
ATOM   12480 O  OE2   . GLU A 1 3025 ? 138.662 178.829 189.564 1.00 61.64  ? 3025 GLU A OE2   1 
ATOM   12481 N  N     . TYR A 1 3026 ? 139.355 185.485 189.880 1.00 50.11  ? 3026 TYR A N     1 
ATOM   12482 C  CA    . TYR A 1 3026 ? 139.912 186.652 190.556 1.00 47.17  ? 3026 TYR A CA    1 
ATOM   12483 C  C     . TYR A 1 3026 ? 138.845 187.386 191.357 1.00 50.72  ? 3026 TYR A C     1 
ATOM   12484 O  O     . TYR A 1 3026 ? 139.107 187.853 192.472 1.00 47.18  ? 3026 TYR A O     1 
ATOM   12485 C  CB    . TYR A 1 3026 ? 140.558 187.591 189.537 1.00 43.84  ? 3026 TYR A CB    1 
ATOM   12486 C  CG    . TYR A 1 3026 ? 141.303 188.747 190.164 1.00 42.83  ? 3026 TYR A CG    1 
ATOM   12487 C  CD1   . TYR A 1 3026 ? 142.501 188.545 190.834 1.00 42.99  ? 3026 TYR A CD1   1 
ATOM   12488 C  CD2   . TYR A 1 3026 ? 140.803 190.040 190.092 1.00 38.70  ? 3026 TYR A CD2   1 
ATOM   12489 C  CE1   . TYR A 1 3026 ? 143.183 189.599 191.410 1.00 42.33  ? 3026 TYR A CE1   1 
ATOM   12490 C  CE2   . TYR A 1 3026 ? 141.477 191.099 190.665 1.00 40.89  ? 3026 TYR A CE2   1 
ATOM   12491 C  CZ    . TYR A 1 3026 ? 142.667 190.873 191.323 1.00 47.07  ? 3026 TYR A CZ    1 
ATOM   12492 O  OH    . TYR A 1 3026 ? 143.342 191.926 191.895 1.00 50.88  ? 3026 TYR A OH    1 
ATOM   12493 N  N     . ALA A 1 3027 ? 137.637 187.506 190.801 1.00 51.67  ? 3027 ALA A N     1 
ATOM   12494 C  CA    . ALA A 1 3027 ? 136.559 188.188 191.510 1.00 48.20  ? 3027 ALA A CA    1 
ATOM   12495 C  C     . ALA A 1 3027 ? 136.198 187.461 192.798 1.00 49.35  ? 3027 ALA A C     1 
ATOM   12496 O  O     . ALA A 1 3027 ? 135.972 188.095 193.836 1.00 54.27  ? 3027 ALA A O     1 
ATOM   12497 C  CB    . ALA A 1 3027 ? 135.336 188.320 190.604 1.00 51.86  ? 3027 ALA A CB    1 
ATOM   12498 N  N     . THR A 1 3028 ? 136.131 186.128 192.751 1.00 47.70  ? 3028 THR A N     1 
ATOM   12499 C  CA    . THR A 1 3028 ? 135.841 185.364 193.960 1.00 49.66  ? 3028 THR A CA    1 
ATOM   12500 C  C     . THR A 1 3028 ? 136.969 185.489 194.976 1.00 52.03  ? 3028 THR A C     1 
ATOM   12501 O  O     . THR A 1 3028 ? 136.716 185.635 196.178 1.00 54.00  ? 3028 THR A O     1 
ATOM   12502 C  CB    . THR A 1 3028 ? 135.599 183.895 193.612 1.00 52.48  ? 3028 THR A CB    1 
ATOM   12503 O  OG1   . THR A 1 3028 ? 136.610 183.443 192.703 1.00 56.47  ? 3028 THR A OG1   1 
ATOM   12504 C  CG2   . THR A 1 3028 ? 134.232 183.719 192.969 1.00 49.09  ? 3028 THR A CG2   1 
ATOM   12505 N  N     . LEU A 1 3029 ? 138.221 185.445 194.512 1.00 50.17  ? 3029 LEU A N     1 
ATOM   12506 C  CA    . LEU A 1 3029 ? 139.358 185.502 195.427 1.00 50.50  ? 3029 LEU A CA    1 
ATOM   12507 C  C     . LEU A 1 3029 ? 139.389 186.819 196.191 1.00 48.98  ? 3029 LEU A C     1 
ATOM   12508 O  O     . LEU A 1 3029 ? 139.687 186.842 197.391 1.00 50.91  ? 3029 LEU A O     1 
ATOM   12509 C  CB    . LEU A 1 3029 ? 140.663 185.298 194.657 1.00 49.46  ? 3029 LEU A CB    1 
ATOM   12510 C  CG    . LEU A 1 3029 ? 141.953 185.656 195.398 1.00 41.30  ? 3029 LEU A CG    1 
ATOM   12511 C  CD1   . LEU A 1 3029 ? 142.283 184.600 196.438 1.00 41.02  ? 3029 LEU A CD1   1 
ATOM   12512 C  CD2   . LEU A 1 3029 ? 143.107 185.837 194.426 1.00 38.64  ? 3029 LEU A CD2   1 
ATOM   12513 N  N     . MET A 1 3030 ? 139.085 187.927 195.514 1.00 51.83  ? 3030 MET A N     1 
ATOM   12514 C  CA    . MET A 1 3030 ? 139.065 189.221 196.188 1.00 50.60  ? 3030 MET A CA    1 
ATOM   12515 C  C     . MET A 1 3030 ? 137.978 189.268 197.254 1.00 50.41  ? 3030 MET A C     1 
ATOM   12516 O  O     . MET A 1 3030 ? 138.157 189.898 198.303 1.00 51.79  ? 3030 MET A O     1 
ATOM   12517 C  CB    . MET A 1 3030 ? 138.873 190.339 195.165 1.00 47.34  ? 3030 MET A CB    1 
ATOM   12518 C  CG    . MET A 1 3030 ? 140.000 190.496 194.133 1.00 45.75  ? 3030 MET A CG    1 
ATOM   12519 S  SD    . MET A 1 3030 ? 141.573 191.188 194.710 1.00 55.43  ? 3030 MET A SD    1 
ATOM   12520 C  CE    . MET A 1 3030 ? 142.366 189.800 195.523 1.00 47.80  ? 3030 MET A CE    1 
ATOM   12521 N  N     . THR A 1 3031 ? 136.841 188.617 196.999 1.00 52.36  ? 3031 THR A N     1 
ATOM   12522 C  CA    . THR A 1 3031 ? 135.795 188.529 198.013 1.00 54.34  ? 3031 THR A CA    1 
ATOM   12523 C  C     . THR A 1 3031 ? 136.273 187.749 199.232 1.00 54.50  ? 3031 THR A C     1 
ATOM   12524 O  O     . THR A 1 3031 ? 136.036 188.161 200.374 1.00 56.64  ? 3031 THR A O     1 
ATOM   12525 C  CB    . THR A 1 3031 ? 134.542 187.884 197.420 1.00 54.87  ? 3031 THR A CB    1 
ATOM   12526 O  OG1   . THR A 1 3031 ? 134.130 188.615 196.258 1.00 56.83  ? 3031 THR A OG1   1 
ATOM   12527 C  CG2   . THR A 1 3031 ? 133.410 187.882 198.435 1.00 56.36  ? 3031 THR A CG2   1 
ATOM   12528 N  N     . GLN A 1 3032 ? 136.947 186.616 199.012 1.00 50.73  ? 3032 GLN A N     1 
ATOM   12529 C  CA    . GLN A 1 3032 ? 137.486 185.849 200.131 1.00 49.50  ? 3032 GLN A CA    1 
ATOM   12530 C  C     . GLN A 1 3032 ? 138.592 186.616 200.843 1.00 50.71  ? 3032 GLN A C     1 
ATOM   12531 O  O     . GLN A 1 3032 ? 138.701 186.564 202.074 1.00 52.19  ? 3032 GLN A O     1 
ATOM   12532 C  CB    . GLN A 1 3032 ? 138.000 184.493 199.647 1.00 46.71  ? 3032 GLN A CB    1 
ATOM   12533 C  CG    . GLN A 1 3032 ? 137.096 183.801 198.645 1.00 47.82  ? 3032 GLN A CG    1 
ATOM   12534 C  CD    . GLN A 1 3032 ? 136.725 182.394 199.067 1.00 52.42  ? 3032 GLN A CD    1 
ATOM   12535 O  OE1   . GLN A 1 3032 ? 135.946 182.198 200.000 1.00 53.21  ? 3032 GLN A OE1   1 
ATOM   12536 N  NE2   . GLN A 1 3032 ? 137.284 181.404 198.381 1.00 50.96  ? 3032 GLN A NE2   1 
ATOM   12537 N  N     . CYS A 1 3033 ? 139.430 187.326 200.084 1.00 52.44  ? 3033 CYS A N     1 
ATOM   12538 C  CA    . CYS A 1 3033 ? 140.477 188.135 200.698 1.00 50.62  ? 3033 CYS A CA    1 
ATOM   12539 C  C     . CYS A 1 3033 ? 139.882 189.251 201.547 1.00 51.66  ? 3033 CYS A C     1 
ATOM   12540 O  O     . CYS A 1 3033 ? 140.395 189.554 202.630 1.00 55.16  ? 3033 CYS A O     1 
ATOM   12541 C  CB    . CYS A 1 3033 ? 141.397 188.710 199.621 1.00 48.86  ? 3033 CYS A CB    1 
ATOM   12542 S  SG    . CYS A 1 3033 ? 142.477 187.493 198.837 1.00 64.96  ? 3033 CYS A SG    1 
ATOM   12543 N  N     . LYS A 1 3034 ? 138.805 189.877 201.068 1.00 53.98  ? 3034 LYS A N     1 
ATOM   12544 C  CA    . LYS A 1 3034 ? 138.121 190.889 201.866 1.00 52.23  ? 3034 LYS A CA    1 
ATOM   12545 C  C     . LYS A 1 3034 ? 137.547 190.284 203.141 1.00 56.75  ? 3034 LYS A C     1 
ATOM   12546 O  O     . LYS A 1 3034 ? 137.652 190.876 204.222 1.00 57.49  ? 3034 LYS A O     1 
ATOM   12547 C  CB    . LYS A 1 3034 ? 137.016 191.547 201.040 1.00 55.64  ? 3034 LYS A CB    1 
ATOM   12548 C  CG    . LYS A 1 3034 ? 136.752 193.001 201.392 1.00 55.09  ? 3034 LYS A CG    1 
ATOM   12549 C  CD    . LYS A 1 3034 ? 135.484 193.503 200.720 1.00 57.91  ? 3034 LYS A CD    1 
ATOM   12550 C  CE    . LYS A 1 3034 ? 135.452 195.021 200.663 1.00 63.57  ? 3034 LYS A CE    1 
ATOM   12551 N  NZ    . LYS A 1 3034 ? 136.408 195.554 199.654 1.00 62.71  ? 3034 LYS A NZ    1 
ATOM   12552 N  N     . GLU A 1 3035 ? 136.930 189.105 203.032 1.00 58.22  ? 3035 GLU A N     1 
ATOM   12553 C  CA    . GLU A 1 3035 ? 136.417 188.423 204.216 1.00 58.27  ? 3035 GLU A CA    1 
ATOM   12554 C  C     . GLU A 1 3035 ? 137.548 188.027 205.156 1.00 62.57  ? 3035 GLU A C     1 
ATOM   12555 O  O     . GLU A 1 3035 ? 137.440 188.195 206.377 1.00 62.89  ? 3035 GLU A O     1 
ATOM   12556 C  CB    . GLU A 1 3035 ? 135.604 187.197 203.800 1.00 57.82  ? 3035 GLU A CB    1 
ATOM   12557 C  CG    . GLU A 1 3035 ? 135.423 186.163 204.898 1.00 67.65  ? 3035 GLU A CG    1 
ATOM   12558 C  CD    . GLU A 1 3035 ? 134.281 186.504 205.835 1.00 72.00  ? 3035 GLU A CD    1 
ATOM   12559 O  OE1   . GLU A 1 3035 ? 133.146 186.050 205.579 1.00 70.04  ? 3035 GLU A OE1   1 
ATOM   12560 O  OE2   . GLU A 1 3035 ? 134.519 187.226 206.825 1.00 71.57  ? 3035 GLU A OE2   1 
ATOM   12561 N  N     . GLY A 1 3036 ? 138.644 187.500 204.605 1.00 57.78  ? 3036 GLY A N     1 
ATOM   12562 C  CA    . GLY A 1 3036 ? 139.767 187.110 205.441 1.00 53.72  ? 3036 GLY A CA    1 
ATOM   12563 C  C     . GLY A 1 3036 ? 140.439 188.292 206.113 1.00 54.96  ? 3036 GLY A C     1 
ATOM   12564 O  O     . GLY A 1 3036 ? 140.816 188.218 207.286 1.00 56.08  ? 3036 GLY A O     1 
ATOM   12565 N  N     . ALA A 1 3037 ? 140.605 189.396 205.380 1.00 51.59  ? 3037 ALA A N     1 
ATOM   12566 C  CA    . ALA A 1 3037 ? 141.180 190.598 205.976 1.00 56.36  ? 3037 ALA A CA    1 
ATOM   12567 C  C     . ALA A 1 3037 ? 140.271 191.163 207.059 1.00 68.21  ? 3037 ALA A C     1 
ATOM   12568 O  O     . ALA A 1 3037 ? 140.752 191.669 208.080 1.00 67.03  ? 3037 ALA A O     1 
ATOM   12569 C  CB    . ALA A 1 3037 ? 141.449 191.645 204.897 1.00 54.98  ? 3037 ALA A CB    1 
ATOM   12570 N  N     . GLN A 1 3038 ? 138.954 191.094 206.850 1.00 68.32  ? 3038 GLN A N     1 
ATOM   12571 C  CA    . GLN A 1 3038 ? 138.016 191.524 207.882 1.00 67.52  ? 3038 GLN A CA    1 
ATOM   12572 C  C     . GLN A 1 3038 ? 138.140 190.659 209.129 1.00 66.21  ? 3038 GLN A C     1 
ATOM   12573 O  O     . GLN A 1 3038 ? 138.030 191.158 210.255 1.00 70.20  ? 3038 GLN A O     1 
ATOM   12574 C  CB    . GLN A 1 3038 ? 136.587 191.488 207.341 1.00 70.62  ? 3038 GLN A CB    1 
ATOM   12575 C  CG    . GLN A 1 3038 ? 135.636 192.455 208.029 1.00 73.81  ? 3038 GLN A CG    1 
ATOM   12576 C  CD    . GLN A 1 3038 ? 136.280 193.797 208.318 1.00 76.43  ? 3038 GLN A CD    1 
ATOM   12577 O  OE1   . GLN A 1 3038 ? 136.576 194.566 207.403 1.00 73.27  ? 3038 GLN A OE1   1 
ATOM   12578 N  NE2   . GLN A 1 3038 ? 136.500 194.086 209.595 1.00 68.52  ? 3038 GLN A NE2   1 
ATOM   12579 N  N     . LYS A 1 3039 ? 138.359 189.354 208.946 1.00 67.88  ? 3039 LYS A N     1 
ATOM   12580 C  CA    . LYS A 1 3039 ? 138.556 188.466 210.087 1.00 61.83  ? 3039 LYS A CA    1 
ATOM   12581 C  C     . LYS A 1 3039 ? 139.801 188.851 210.875 1.00 63.17  ? 3039 LYS A C     1 
ATOM   12582 O  O     . LYS A 1 3039 ? 139.794 188.835 212.111 1.00 68.98  ? 3039 LYS A O     1 
ATOM   12583 C  CB    . LYS A 1 3039 ? 138.649 187.016 209.612 1.00 61.97  ? 3039 LYS A CB    1 
ATOM   12584 C  CG    . LYS A 1 3039 ? 137.316 186.407 209.208 1.00 65.27  ? 3039 LYS A CG    1 
ATOM   12585 C  CD    . LYS A 1 3039 ? 137.470 184.957 208.770 1.00 65.28  ? 3039 LYS A CD    1 
ATOM   12586 C  CE    . LYS A 1 3039 ? 138.416 184.193 209.683 1.00 65.53  ? 3039 LYS A CE    1 
ATOM   12587 N  NZ    . LYS A 1 3039 ? 137.725 183.684 210.899 1.00 56.72  ? 3039 LYS A NZ    1 
ATOM   12588 N  N     . GLU A 1 3040 ? 140.882 189.201 210.177 1.00 66.10  ? 3040 GLU A N     1 
ATOM   12589 C  CA    . GLU A 1 3040 ? 142.107 189.631 210.839 1.00 65.43  ? 3040 GLU A CA    1 
ATOM   12590 C  C     . GLU A 1 3040 ? 141.988 191.023 211.443 1.00 66.31  ? 3040 GLU A C     1 
ATOM   12591 O  O     . GLU A 1 3040 ? 142.832 191.404 212.262 1.00 65.13  ? 3040 GLU A O     1 
ATOM   12592 C  CB    . GLU A 1 3040 ? 143.276 189.593 209.850 1.00 64.09  ? 3040 GLU A CB    1 
ATOM   12593 C  CG    . GLU A 1 3040 ? 144.647 189.505 210.500 1.00 65.23  ? 3040 GLU A CG    1 
ATOM   12594 C  CD    . GLU A 1 3040 ? 145.662 188.800 209.623 1.00 69.46  ? 3040 GLU A CD    1 
ATOM   12595 O  OE1   . GLU A 1 3040 ? 145.594 187.558 209.513 1.00 67.51  ? 3040 GLU A OE1   1 
ATOM   12596 O  OE2   . GLU A 1 3040 ? 146.527 189.489 209.042 1.00 65.47  ? 3040 GLU A OE2   1 
ATOM   12597 N  N     . GLY A 1 3041 ? 140.965 191.785 211.067 1.00 68.28  ? 3041 GLY A N     1 
ATOM   12598 C  CA    . GLY A 1 3041 ? 140.797 193.131 211.574 1.00 71.73  ? 3041 GLY A CA    1 
ATOM   12599 C  C     . GLY A 1 3041 ? 141.412 194.218 210.726 1.00 73.30  ? 3041 GLY A C     1 
ATOM   12600 O  O     . GLY A 1 3041 ? 141.551 195.350 211.202 1.00 78.45  ? 3041 GLY A O     1 
ATOM   12601 N  N     . LEU A 1 3042 ? 141.783 193.917 209.486 1.00 71.24  ? 3042 LEU A N     1 
ATOM   12602 C  CA    . LEU A 1 3042 ? 142.404 194.892 208.605 1.00 73.70  ? 3042 LEU A CA    1 
ATOM   12603 C  C     . LEU A 1 3042 ? 141.385 195.442 207.615 1.00 74.72  ? 3042 LEU A C     1 
ATOM   12604 O  O     . LEU A 1 3042 ? 140.503 194.725 207.136 1.00 70.08  ? 3042 LEU A O     1 
ATOM   12605 C  CB    . LEU A 1 3042 ? 143.582 194.267 207.856 1.00 65.71  ? 3042 LEU A CB    1 
ATOM   12606 C  CG    . LEU A 1 3042 ? 144.806 193.850 208.676 1.00 66.69  ? 3042 LEU A CG    1 
ATOM   12607 C  CD1   . LEU A 1 3042 ? 146.060 193.890 207.816 1.00 60.49  ? 3042 LEU A CD1   1 
ATOM   12608 C  CD2   . LEU A 1 3042 ? 144.972 194.732 209.906 1.00 67.26  ? 3042 LEU A CD2   1 
ATOM   12609 N  N     . MET A 1 3043 ? 141.515 196.733 207.313 1.00 79.57  ? 3043 MET A N     1 
ATOM   12610 C  CA    . MET A 1 3043 ? 140.566 197.445 206.456 1.00 78.37  ? 3043 MET A CA    1 
ATOM   12611 C  C     . MET A 1 3043 ? 141.199 197.658 205.083 1.00 73.27  ? 3043 MET A C     1 
ATOM   12612 O  O     . MET A 1 3043 ? 141.814 198.690 204.812 1.00 76.14  ? 3043 MET A O     1 
ATOM   12613 C  CB    . MET A 1 3043 ? 140.151 198.765 207.099 1.00 85.63  ? 3043 MET A CB    1 
ATOM   12614 C  CG    . MET A 1 3043 ? 141.286 199.514 207.788 1.00 95.09  ? 3043 MET A CG    1 
ATOM   12615 S  SD    . MET A 1 3043 ? 140.739 200.484 209.206 1.00 123.15 ? 3043 MET A SD    1 
ATOM   12616 C  CE    . MET A 1 3043 ? 139.713 199.291 210.060 1.00 88.72  ? 3043 MET A CE    1 
ATOM   12617 N  N     . LEU A 1 3044 ? 141.040 196.669 204.207 1.00 67.18  ? 3044 LEU A N     1 
ATOM   12618 C  CA    . LEU A 1 3044 ? 141.450 196.774 202.813 1.00 67.26  ? 3044 LEU A CA    1 
ATOM   12619 C  C     . LEU A 1 3044 ? 140.217 196.698 201.925 1.00 66.76  ? 3044 LEU A C     1 
ATOM   12620 O  O     . LEU A 1 3044 ? 139.394 195.789 202.076 1.00 64.02  ? 3044 LEU A O     1 
ATOM   12621 C  CB    . LEU A 1 3044 ? 142.444 195.673 202.424 1.00 62.29  ? 3044 LEU A CB    1 
ATOM   12622 C  CG    . LEU A 1 3044 ? 143.807 195.619 203.118 1.00 60.41  ? 3044 LEU A CG    1 
ATOM   12623 C  CD1   . LEU A 1 3044 ? 144.324 197.018 203.433 1.00 61.66  ? 3044 LEU A CD1   1 
ATOM   12624 C  CD2   . LEU A 1 3044 ? 143.752 194.759 204.366 1.00 64.55  ? 3044 LEU A CD2   1 
ATOM   12625 N  N     . ASP A 1 3045 ? 140.095 197.645 201.009 1.00 67.84  ? 3045 ASP A N     1 
ATOM   12626 C  CA    . ASP A 1 3045 ? 138.962 197.686 200.091 1.00 71.21  ? 3045 ASP A CA    1 
ATOM   12627 C  C     . ASP A 1 3045 ? 139.372 197.528 198.635 1.00 69.19  ? 3045 ASP A C     1 
ATOM   12628 O  O     . ASP A 1 3045 ? 138.731 196.769 197.904 1.00 65.97  ? 3045 ASP A O     1 
ATOM   12629 C  CB    . ASP A 1 3045 ? 138.185 199.000 200.270 1.00 76.05  ? 3045 ASP A CB    1 
ATOM   12630 C  CG    . ASP A 1 3045 ? 136.882 199.016 199.493 1.00 82.31  ? 3045 ASP A CG    1 
ATOM   12631 O  OD1   . ASP A 1 3045 ? 136.016 198.158 199.762 1.00 77.55  ? 3045 ASP A OD1   1 
ATOM   12632 O  OD2   . ASP A 1 3045 ? 136.726 199.887 198.611 1.00 88.71  ? 3045 ASP A OD2   1 
ATOM   12633 N  N     . SER A 1 3046 ? 140.417 198.223 198.196 1.00 66.09  ? 3046 SER A N     1 
ATOM   12634 C  CA    . SER A 1 3046 ? 140.840 198.137 196.807 1.00 66.66  ? 3046 SER A CA    1 
ATOM   12635 C  C     . SER A 1 3046 ? 141.499 196.792 196.522 1.00 62.08  ? 3046 SER A C     1 
ATOM   12636 O  O     . SER A 1 3046 ? 141.959 196.092 197.429 1.00 59.17  ? 3046 SER A O     1 
ATOM   12637 C  CB    . SER A 1 3046 ? 141.800 199.276 196.468 1.00 65.54  ? 3046 SER A CB    1 
ATOM   12638 O  OG    . SER A 1 3046 ? 142.393 199.078 195.197 1.00 65.50  ? 3046 SER A OG    1 
ATOM   12639 N  N     . HIS A 1 3047 ? 141.537 196.435 195.237 1.00 58.67  ? 3047 HIS A N     1 
ATOM   12640 C  CA    . HIS A 1 3047 ? 142.026 195.119 194.840 1.00 55.74  ? 3047 HIS A CA    1 
ATOM   12641 C  C     . HIS A 1 3047 ? 143.520 194.965 195.108 1.00 54.52  ? 3047 HIS A C     1 
ATOM   12642 O  O     . HIS A 1 3047 ? 143.973 193.887 195.511 1.00 56.17  ? 3047 HIS A O     1 
ATOM   12643 C  CB    . HIS A 1 3047 ? 141.720 194.873 193.364 1.00 55.76  ? 3047 HIS A CB    1 
ATOM   12644 C  CG    . HIS A 1 3047 ? 140.264 194.688 193.071 1.00 55.19  ? 3047 HIS A CG    1 
ATOM   12645 N  ND1   . HIS A 1 3047 ? 139.526 193.650 193.595 1.00 55.41  ? 3047 HIS A ND1   1 
ATOM   12646 C  CD2   . HIS A 1 3047 ? 139.411 195.405 192.302 1.00 65.96  ? 3047 HIS A CD2   1 
ATOM   12647 C  CE1   . HIS A 1 3047 ? 138.279 193.737 193.166 1.00 54.93  ? 3047 HIS A CE1   1 
ATOM   12648 N  NE2   . HIS A 1 3047 ? 138.183 194.793 192.379 1.00 69.14  ? 3047 HIS A NE2   1 
ATOM   12649 N  N     . GLU A 1 3048 ? 144.302 196.025 194.884 1.00 50.97  ? 3048 GLU A N     1 
ATOM   12650 C  CA    . GLU A 1 3048 ? 145.755 195.891 194.952 1.00 49.72  ? 3048 GLU A CA    1 
ATOM   12651 C  C     . GLU A 1 3048 ? 146.232 195.642 196.379 1.00 51.77  ? 3048 GLU A C     1 
ATOM   12652 O  O     . GLU A 1 3048 ? 147.217 194.924 196.589 1.00 50.17  ? 3048 GLU A O     1 
ATOM   12653 C  CB    . GLU A 1 3048 ? 146.428 197.127 194.347 1.00 52.50  ? 3048 GLU A CB    1 
ATOM   12654 C  CG    . GLU A 1 3048 ? 146.831 198.207 195.337 1.00 63.63  ? 3048 GLU A CG    1 
ATOM   12655 C  CD    . GLU A 1 3048 ? 147.929 199.106 194.803 1.00 65.71  ? 3048 GLU A CD    1 
ATOM   12656 O  OE1   . GLU A 1 3048 ? 148.420 198.847 193.685 1.00 58.70  ? 3048 GLU A OE1   1 
ATOM   12657 O  OE2   . GLU A 1 3048 ? 148.299 200.072 195.503 1.00 66.97  ? 3048 GLU A OE2   1 
ATOM   12658 N  N     . GLU A 1 3049 ? 145.554 196.219 197.375 1.00 51.31  ? 3049 GLU A N     1 
ATOM   12659 C  CA    . GLU A 1 3049 ? 145.915 195.929 198.760 1.00 47.64  ? 3049 GLU A CA    1 
ATOM   12660 C  C     . GLU A 1 3049 ? 145.413 194.554 199.184 1.00 44.59  ? 3049 GLU A C     1 
ATOM   12661 O  O     . GLU A 1 3049 ? 146.040 193.889 200.017 1.00 43.22  ? 3049 GLU A O     1 
ATOM   12662 C  CB    . GLU A 1 3049 ? 145.378 197.014 199.694 1.00 49.12  ? 3049 GLU A CB    1 
ATOM   12663 C  CG    . GLU A 1 3049 ? 145.824 198.428 199.345 1.00 56.72  ? 3049 GLU A CG    1 
ATOM   12664 C  CD    . GLU A 1 3049 ? 144.740 199.243 198.669 1.00 66.61  ? 3049 GLU A CD    1 
ATOM   12665 O  OE1   . GLU A 1 3049 ? 143.882 199.802 199.384 1.00 60.47  ? 3049 GLU A OE1   1 
ATOM   12666 O  OE2   . GLU A 1 3049 ? 144.758 199.339 197.426 1.00 62.77  ? 3049 GLU A OE2   1 
ATOM   12667 N  N     . LEU A 1 3050 ? 144.283 194.114 198.627 1.00 44.53  ? 3050 LEU A N     1 
ATOM   12668 C  CA    . LEU A 1 3050 ? 143.797 192.768 198.911 1.00 43.07  ? 3050 LEU A CA    1 
ATOM   12669 C  C     . LEU A 1 3050 ? 144.772 191.713 198.406 1.00 41.74  ? 3050 LEU A C     1 
ATOM   12670 O  O     . LEU A 1 3050 ? 145.019 190.708 199.083 1.00 39.01  ? 3050 LEU A O     1 
ATOM   12671 C  CB    . LEU A 1 3050 ? 142.416 192.566 198.289 1.00 42.00  ? 3050 LEU A CB    1 
ATOM   12672 C  CG    . LEU A 1 3050 ? 141.235 193.163 199.055 1.00 45.81  ? 3050 LEU A CG    1 
ATOM   12673 C  CD1   . LEU A 1 3050 ? 139.919 192.723 198.436 1.00 49.52  ? 3050 LEU A CD1   1 
ATOM   12674 C  CD2   . LEU A 1 3050 ? 141.296 192.766 200.521 1.00 44.87  ? 3050 LEU A CD2   1 
ATOM   12675 N  N     . TYR A 1 3051 ? 145.334 191.922 197.213 1.00 41.16  ? 3051 TYR A N     1 
ATOM   12676 C  CA    . TYR A 1 3051 ? 146.306 190.976 196.676 1.00 33.01  ? 3051 TYR A CA    1 
ATOM   12677 C  C     . TYR A 1 3051 ? 147.603 190.997 197.476 1.00 35.56  ? 3051 TYR A C     1 
ATOM   12678 O  O     . TYR A 1 3051 ? 148.214 189.946 197.703 1.00 36.75  ? 3051 TYR A O     1 
ATOM   12679 C  CB    . TYR A 1 3051 ? 146.578 191.281 195.204 1.00 33.63  ? 3051 TYR A CB    1 
ATOM   12680 C  CG    . TYR A 1 3051 ? 147.087 190.092 194.422 1.00 34.43  ? 3051 TYR A CG    1 
ATOM   12681 C  CD1   . TYR A 1 3051 ? 146.259 189.013 194.145 1.00 33.62  ? 3051 TYR A CD1   1 
ATOM   12682 C  CD2   . TYR A 1 3051 ? 148.395 190.048 193.962 1.00 33.03  ? 3051 TYR A CD2   1 
ATOM   12683 C  CE1   . TYR A 1 3051 ? 146.720 187.923 193.433 1.00 30.13  ? 3051 TYR A CE1   1 
ATOM   12684 C  CE2   . TYR A 1 3051 ? 148.865 188.963 193.249 1.00 34.35  ? 3051 TYR A CE2   1 
ATOM   12685 C  CZ    . TYR A 1 3051 ? 148.023 187.904 192.988 1.00 37.63  ? 3051 TYR A CZ    1 
ATOM   12686 O  OH    . TYR A 1 3051 ? 148.488 186.823 192.277 1.00 44.04  ? 3051 TYR A OH    1 
ATOM   12687 N  N     . LYS A 1 3052 ? 148.044 192.183 197.903 1.00 35.05  ? 3052 LYS A N     1 
ATOM   12688 C  CA    . LYS A 1 3052 ? 149.273 192.276 198.685 1.00 31.06  ? 3052 LYS A CA    1 
ATOM   12689 C  C     . LYS A 1 3052 ? 149.123 191.587 200.035 1.00 34.60  ? 3052 LYS A C     1 
ATOM   12690 O  O     . LYS A 1 3052 ? 150.045 190.905 200.497 1.00 39.94  ? 3052 LYS A O     1 
ATOM   12691 C  CB    . LYS A 1 3052 ? 149.673 193.740 198.867 1.00 32.96  ? 3052 LYS A CB    1 
ATOM   12692 C  CG    . LYS A 1 3052 ? 150.497 194.301 197.721 1.00 34.94  ? 3052 LYS A CG    1 
ATOM   12693 C  CD    . LYS A 1 3052 ? 151.383 195.445 198.185 1.00 41.23  ? 3052 LYS A CD    1 
ATOM   12694 C  CE    . LYS A 1 3052 ? 152.485 195.732 197.177 1.00 45.32  ? 3052 LYS A CE    1 
ATOM   12695 N  NZ    . LYS A 1 3052 ? 153.589 194.735 197.258 1.00 34.31  ? 3052 LYS A NZ    1 
ATOM   12696 N  N     . TRP A 1 3053 ? 147.972 191.761 200.688 1.00 31.64  ? 3053 TRP A N     1 
ATOM   12697 C  CA    . TRP A 1 3053 ? 147.708 191.021 201.918 1.00 30.74  ? 3053 TRP A CA    1 
ATOM   12698 C  C     . TRP A 1 3053 ? 147.620 189.527 201.642 1.00 32.59  ? 3053 TRP A C     1 
ATOM   12699 O  O     . TRP A 1 3053 ? 148.087 188.709 202.443 1.00 33.84  ? 3053 TRP A O     1 
ATOM   12700 C  CB    . TRP A 1 3053 ? 146.420 191.521 202.572 1.00 33.41  ? 3053 TRP A CB    1 
ATOM   12701 C  CG    . TRP A 1 3053 ? 145.974 190.681 203.733 1.00 31.69  ? 3053 TRP A CG    1 
ATOM   12702 C  CD1   . TRP A 1 3053 ? 146.373 190.803 205.032 1.00 32.82  ? 3053 TRP A CD1   1 
ATOM   12703 C  CD2   . TRP A 1 3053 ? 145.052 189.585 203.698 1.00 33.78  ? 3053 TRP A CD2   1 
ATOM   12704 N  NE1   . TRP A 1 3053 ? 145.754 189.855 205.809 1.00 34.63  ? 3053 TRP A NE1   1 
ATOM   12705 C  CE2   . TRP A 1 3053 ? 144.938 189.094 205.014 1.00 38.26  ? 3053 TRP A CE2   1 
ATOM   12706 C  CE3   . TRP A 1 3053 ? 144.311 188.973 202.683 1.00 37.98  ? 3053 TRP A CE3   1 
ATOM   12707 C  CZ2   . TRP A 1 3053 ? 144.114 188.021 205.341 1.00 40.48  ? 3053 TRP A CZ2   1 
ATOM   12708 C  CZ3   . TRP A 1 3053 ? 143.493 187.907 203.010 1.00 39.07  ? 3053 TRP A CZ3   1 
ATOM   12709 C  CH2   . TRP A 1 3053 ? 143.402 187.442 204.328 1.00 40.22  ? 3053 TRP A CH2   1 
ATOM   12710 N  N     . PHE A 1 3054 ? 147.015 189.154 200.512 1.00 28.50  ? 3054 PHE A N     1 
ATOM   12711 C  CA    . PHE A 1 3054 ? 146.940 187.749 200.129 1.00 28.54  ? 3054 PHE A CA    1 
ATOM   12712 C  C     . PHE A 1 3054 ? 148.330 187.164 199.910 1.00 31.43  ? 3054 PHE A C     1 
ATOM   12713 O  O     . PHE A 1 3054 ? 148.612 186.037 200.333 1.00 33.25  ? 3054 PHE A O     1 
ATOM   12714 C  CB    . PHE A 1 3054 ? 146.087 187.605 198.868 1.00 32.53  ? 3054 PHE A CB    1 
ATOM   12715 C  CG    . PHE A 1 3054 ? 146.080 186.222 198.288 1.00 29.82  ? 3054 PHE A CG    1 
ATOM   12716 C  CD1   . PHE A 1 3054 ? 145.371 185.204 198.901 1.00 27.31  ? 3054 PHE A CD1   1 
ATOM   12717 C  CD2   . PHE A 1 3054 ? 146.773 185.942 197.123 1.00 30.80  ? 3054 PHE A CD2   1 
ATOM   12718 C  CE1   . PHE A 1 3054 ? 145.358 183.931 198.366 1.00 29.47  ? 3054 PHE A CE1   1 
ATOM   12719 C  CE2   . PHE A 1 3054 ? 146.765 184.671 196.584 1.00 29.35  ? 3054 PHE A CE2   1 
ATOM   12720 C  CZ    . PHE A 1 3054 ? 146.056 183.664 197.206 1.00 29.05  ? 3054 PHE A CZ    1 
ATOM   12721 N  N     . THR A 1 3055 ? 149.213 187.917 199.250 1.00 31.79  ? 3055 THR A N     1 
ATOM   12722 C  CA    . THR A 1 3055 ? 150.576 187.445 199.030 1.00 30.39  ? 3055 THR A CA    1 
ATOM   12723 C  C     . THR A 1 3055 ? 151.324 187.278 200.347 1.00 27.36  ? 3055 THR A C     1 
ATOM   12724 O  O     . THR A 1 3055 ? 152.036 186.286 200.545 1.00 29.68  ? 3055 THR A O     1 
ATOM   12725 C  CB    . THR A 1 3055 ? 151.322 188.413 198.110 1.00 29.44  ? 3055 THR A CB    1 
ATOM   12726 O  OG1   . THR A 1 3055 ? 150.703 188.418 196.818 1.00 33.78  ? 3055 THR A OG1   1 
ATOM   12727 C  CG2   . THR A 1 3055 ? 152.779 188.003 197.967 1.00 28.34  ? 3055 THR A CG2   1 
ATOM   12728 N  N     . SER A 1 3056 ? 151.171 188.237 201.263 1.00 27.68  ? 3056 SER A N     1 
ATOM   12729 C  CA    . SER A 1 3056 ? 151.856 188.151 202.549 1.00 27.67  ? 3056 SER A CA    1 
ATOM   12730 C  C     . SER A 1 3056 ? 151.370 186.954 203.356 1.00 27.28  ? 3056 SER A C     1 
ATOM   12731 O  O     . SER A 1 3056 ? 152.158 186.305 204.053 1.00 28.59  ? 3056 SER A O     1 
ATOM   12732 C  CB    . SER A 1 3056 ? 151.659 189.447 203.334 1.00 26.53  ? 3056 SER A CB    1 
ATOM   12733 O  OG    . SER A 1 3056 ? 150.309 189.602 203.734 1.00 30.13  ? 3056 SER A OG    1 
ATOM   12734 N  N     . GLN A 1 3057 ? 150.075 186.647 203.236 1.00 28.70  ? 3057 GLN A N     1 
ATOM   12735 C  CA    . GLN A 1 3057 ? 149.489 185.498 203.974 1.00 28.99  ? 3057 GLN A CA    1 
ATOM   12736 C  C     . GLN A 1 3057 ? 150.089 184.185 203.448 1.00 27.23  ? 3057 GLN A C     1 
ATOM   12737 O  O     . GLN A 1 3057 ? 150.543 183.370 204.278 1.00 28.21  ? 3057 GLN A O     1 
ATOM   12738 C  CB    . GLN A 1 3057 ? 147.968 185.498 203.817 1.00 27.98  ? 3057 GLN A CB    1 
ATOM   12739 C  CG    . GLN A 1 3057 ? 147.269 186.639 204.547 1.00 30.66  ? 3057 GLN A CG    1 
ATOM   12740 C  CD    . GLN A 1 3057 ? 147.284 186.480 206.051 1.00 36.95  ? 3057 GLN A CD    1 
ATOM   12741 O  OE1   . GLN A 1 3057 ? 147.828 187.314 206.783 1.00 41.79  ? 3057 GLN A OE1   1 
ATOM   12742 N  NE2   . GLN A 1 3057 ? 146.684 185.399 206.527 1.00 41.86  ? 3057 GLN A NE2   1 
ATOM   12743 N  N     . VAL A 1 3058 ? 150.089 183.994 202.127 1.00 25.81  ? 3058 VAL A N     1 
ATOM   12744 C  CA    . VAL A 1 3058 ? 150.607 182.727 201.527 1.00 21.54  ? 3058 VAL A CA    1 
ATOM   12745 C  C     . VAL A 1 3058 ? 152.086 182.561 201.908 1.00 23.02  ? 3058 VAL A C     1 
ATOM   12746 O  O     . VAL A 1 3058 ? 152.471 181.440 202.305 1.00 26.28  ? 3058 VAL A O     1 
ATOM   12747 C  CB    . VAL A 1 3058 ? 150.430 182.728 199.998 1.00 21.18  ? 3058 VAL A CB    1 
ATOM   12748 C  CG1   . VAL A 1 3058 ? 151.101 181.523 199.351 1.00 23.17  ? 3058 VAL A CG1   1 
ATOM   12749 C  CG2   . VAL A 1 3058 ? 148.961 182.813 199.599 1.00 25.16  ? 3058 VAL A CG2   1 
ATOM   12750 N  N     . ILE A 1 3059 ? 152.870 183.638 201.807 1.00 21.55  ? 3059 ILE A N     1 
ATOM   12751 C  CA    . ILE A 1 3059 ? 154.331 183.569 202.111 1.00 20.46  ? 3059 ILE A CA    1 
ATOM   12752 C  C     . ILE A 1 3059 ? 154.523 183.099 203.561 1.00 26.65  ? 3059 ILE A C     1 
ATOM   12753 O  O     . ILE A 1 3059 ? 155.566 182.471 203.842 1.00 31.65  ? 3059 ILE A O     1 
ATOM   12754 C  CB    . ILE A 1 3059 ? 154.991 184.937 201.859 1.00 21.49  ? 3059 ILE A CB    1 
ATOM   12755 C  CG1   . ILE A 1 3059 ? 155.030 185.271 200.368 1.00 21.99  ? 3059 ILE A CG1   1 
ATOM   12756 C  CG2   . ILE A 1 3059 ? 156.383 185.006 202.488 1.00 24.51  ? 3059 ILE A CG2   1 
ATOM   12757 C  CD1   . ILE A 1 3059 ? 155.669 186.610 200.050 1.00 18.11  ? 3059 ILE A CD1   1 
ATOM   12758 N  N     . ARG A 1 3060 ? 153.555 183.377 204.437 1.00 25.34  ? 3060 ARG A N     1 
ATOM   12759 C  CA    . ARG A 1 3060 ? 153.708 183.033 205.875 1.00 24.24  ? 3060 ARG A CA    1 
ATOM   12760 C  C     . ARG A 1 3060 ? 152.902 181.772 206.230 1.00 25.44  ? 3060 ARG A C     1 
ATOM   12761 O  O     . ARG A 1 3060 ? 153.034 181.301 207.381 1.00 26.36  ? 3060 ARG A O     1 
ATOM   12762 C  CB    . ARG A 1 3060 ? 153.242 184.239 206.697 1.00 28.62  ? 3060 ARG A CB    1 
ATOM   12763 C  CG    . ARG A 1 3060 ? 153.392 184.118 208.206 1.00 31.84  ? 3060 ARG A CG    1 
ATOM   12764 C  CD    . ARG A 1 3060 ? 152.747 185.298 208.916 1.00 37.42  ? 3060 ARG A CD    1 
ATOM   12765 N  NE    . ARG A 1 3060 ? 151.356 185.510 208.500 1.00 41.58  ? 3060 ARG A NE    1 
ATOM   12766 C  CZ    . ARG A 1 3060 ? 150.370 184.634 208.643 1.00 48.72  ? 3060 ARG A CZ    1 
ATOM   12767 N  NH1   . ARG A 1 3060 ? 150.578 183.494 209.277 1.00 49.58  ? 3060 ARG A NH1   1 
ATOM   12768 N  NH2   . ARG A 1 3060 ? 149.173 184.904 208.154 1.00 42.26  ? 3060 ARG A NH2   1 
ATOM   12769 N  N     . ASN A 1 3061 ? 152.110 181.236 205.296 1.00 25.05  ? 3061 ASN A N     1 
ATOM   12770 C  CA    . ASN A 1 3061 ? 151.232 180.082 205.649 1.00 25.34  ? 3061 ASN A CA    1 
ATOM   12771 C  C     . ASN A 1 3061 ? 151.468 178.887 204.717 1.00 24.18  ? 3061 ASN A C     1 
ATOM   12772 O  O     . ASN A 1 3061 ? 150.789 177.857 204.913 1.00 23.50  ? 3061 ASN A O     1 
ATOM   12773 C  CB    . ASN A 1 3061 ? 149.760 180.480 205.652 1.00 25.29  ? 3061 ASN A CB    1 
ATOM   12774 C  CG    . ASN A 1 3061 ? 149.453 181.539 206.683 1.00 29.56  ? 3061 ASN A CG    1 
ATOM   12775 O  OD1   . ASN A 1 3061 ? 149.708 181.338 207.875 1.00 31.09  ? 3061 ASN A OD1   1 
ATOM   12776 N  ND2   . ASN A 1 3061 ? 148.914 182.668 206.249 1.00 30.63  ? 3061 ASN A ND2   1 
ATOM   12777 N  N     . LEU A 1 3062 ? 152.378 179.004 203.746 1.00 19.26  ? 3062 LEU A N     1 
ATOM   12778 C  CA    . LEU A 1 3062 ? 152.560 177.896 202.769 1.00 15.47  ? 3062 LEU A CA    1 
ATOM   12779 C  C     . LEU A 1 3062 ? 153.994 177.347 202.844 1.00 16.42  ? 3062 LEU A C     1 
ATOM   12780 O  O     . LEU A 1 3062 ? 154.944 178.149 202.719 1.00 21.40  ? 3062 LEU A O     1 
ATOM   12781 C  CB    . LEU A 1 3062 ? 152.214 178.358 201.354 1.00 17.68  ? 3062 LEU A CB    1 
ATOM   12782 C  CG    . LEU A 1 3062 ? 152.339 177.293 200.260 1.00 19.23  ? 3062 LEU A CG    1 
ATOM   12783 C  CD1   . LEU A 1 3062 ? 151.578 176.039 200.654 1.00 20.94  ? 3062 LEU A CD1   1 
ATOM   12784 C  CD2   . LEU A 1 3062 ? 151.842 177.821 198.926 1.00 21.25  ? 3062 LEU A CD2   1 
ATOM   12785 N  N     . HIS A 1 3063 ? 154.135 176.034 203.046 1.00 16.98  ? 3063 HIS A N     1 
ATOM   12786 C  CA    . HIS A 1 3063 ? 155.479 175.396 203.091 1.00 13.38  ? 3063 HIS A CA    1 
ATOM   12787 C  C     . HIS A 1 3063 ? 155.539 174.318 202.007 1.00 13.90  ? 3063 HIS A C     1 
ATOM   12788 O  O     . HIS A 1 3063 ? 154.929 173.243 202.187 1.00 19.41  ? 3063 HIS A O     1 
ATOM   12789 C  CB    . HIS A 1 3063 ? 155.755 174.818 204.482 1.00 13.32  ? 3063 HIS A CB    1 
ATOM   12790 C  CG    . HIS A 1 3063 ? 155.965 175.848 205.541 1.00 13.00  ? 3063 HIS A CG    1 
ATOM   12791 N  ND1   . HIS A 1 3063 ? 154.932 176.391 206.274 1.00 18.06  ? 3063 HIS A ND1   1 
ATOM   12792 C  CD2   . HIS A 1 3063 ? 157.083 176.433 205.988 1.00 11.71  ? 3063 HIS A CD2   1 
ATOM   12793 C  CE1   . HIS A 1 3063 ? 155.423 177.273 207.133 1.00 17.78  ? 3063 HIS A CE1   1 
ATOM   12794 N  NE2   . HIS A 1 3063 ? 156.728 177.313 206.976 1.00 14.14  ? 3063 HIS A NE2   1 
ATOM   12795 N  N     . VAL A 1 3064 ? 156.248 174.596 200.910 1.00 14.89  ? 3064 VAL A N     1 
ATOM   12796 C  CA    . VAL A 1 3064 ? 156.302 173.624 199.775 1.00 12.54  ? 3064 VAL A CA    1 
ATOM   12797 C  C     . VAL A 1 3064 ? 157.468 172.651 200.007 1.00 13.02  ? 3064 VAL A C     1 
ATOM   12798 O  O     . VAL A 1 3064 ? 158.618 173.123 200.129 1.00 13.08  ? 3064 VAL A O     1 
ATOM   12799 C  CB    . VAL A 1 3064 ? 156.425 174.328 198.412 1.00 11.12  ? 3064 VAL A CB    1 
ATOM   12800 C  CG1   . VAL A 1 3064 ? 156.426 173.327 197.264 1.00 15.80  ? 3064 VAL A CG1   1 
ATOM   12801 C  CG2   . VAL A 1 3064 ? 155.326 175.365 198.214 1.00 17.75  ? 3064 VAL A CG2   1 
ATOM   12802 N  N     . VAL A 1 3065 ? 157.175 171.349 200.068 1.00 15.23  ? 3065 VAL A N     1 
ATOM   12803 C  CA    . VAL A 1 3065 ? 158.245 170.321 200.243 1.00 12.75  ? 3065 VAL A CA    1 
ATOM   12804 C  C     . VAL A 1 3065 ? 158.406 169.556 198.919 1.00 15.65  ? 3065 VAL A C     1 
ATOM   12805 O  O     . VAL A 1 3065 ? 157.516 168.741 198.596 1.00 20.39  ? 3065 VAL A O     1 
ATOM   12806 C  CB    . VAL A 1 3065 ? 157.931 169.364 201.408 1.00 11.76  ? 3065 VAL A CB    1 
ATOM   12807 C  CG1   . VAL A 1 3065 ? 159.019 168.311 201.581 1.00 19.38  ? 3065 VAL A CG1   1 
ATOM   12808 C  CG2   . VAL A 1 3065 ? 157.703 170.120 202.711 1.00 17.38  ? 3065 VAL A CG2   1 
ATOM   12809 N  N     . PHE A 1 3066 ? 159.495 169.816 198.190 1.00 13.89  ? 3066 PHE A N     1 
ATOM   12810 C  CA    . PHE A 1 3066 ? 159.757 169.104 196.910 1.00 15.81  ? 3066 PHE A CA    1 
ATOM   12811 C  C     . PHE A 1 3066 ? 160.626 167.885 197.196 1.00 21.77  ? 3066 PHE A C     1 
ATOM   12812 O  O     . PHE A 1 3066 ? 161.662 168.020 197.883 1.00 22.98  ? 3066 PHE A O     1 
ATOM   12813 C  CB    . PHE A 1 3066 ? 160.432 170.026 195.889 1.00 19.10  ? 3066 PHE A CB    1 
ATOM   12814 C  CG    . PHE A 1 3066 ? 159.481 170.791 194.979 1.00 26.30  ? 3066 PHE A CG    1 
ATOM   12815 C  CD1   . PHE A 1 3066 ? 159.033 170.233 193.788 1.00 30.70  ? 3066 PHE A CD1   1 
ATOM   12816 C  CD2   . PHE A 1 3066 ? 159.050 172.071 195.308 1.00 30.06  ? 3066 PHE A CD2   1 
ATOM   12817 C  CE1   . PHE A 1 3066 ? 158.172 170.931 192.957 1.00 36.19  ? 3066 PHE A CE1   1 
ATOM   12818 C  CE2   . PHE A 1 3066 ? 158.190 172.766 194.472 1.00 40.89  ? 3066 PHE A CE2   1 
ATOM   12819 C  CZ    . PHE A 1 3066 ? 157.752 172.195 193.300 1.00 44.64  ? 3066 PHE A CZ    1 
ATOM   12820 N  N     . THR A 1 3067 ? 160.215 166.721 196.687 1.00 22.85  ? 3067 THR A N     1 
ATOM   12821 C  CA    . THR A 1 3067 ? 160.990 165.481 196.898 1.00 18.12  ? 3067 THR A CA    1 
ATOM   12822 C  C     . THR A 1 3067 ? 161.381 164.915 195.551 1.00 21.94  ? 3067 THR A C     1 
ATOM   12823 O  O     . THR A 1 3067 ? 160.482 164.731 194.703 1.00 28.66  ? 3067 THR A O     1 
ATOM   12824 C  CB    . THR A 1 3067 ? 160.157 164.496 197.715 1.00 21.36  ? 3067 THR A CB    1 
ATOM   12825 O  OG1   . THR A 1 3067 ? 158.940 164.344 196.991 1.00 31.46  ? 3067 THR A OG1   1 
ATOM   12826 C  CG2   . THR A 1 3067 ? 159.863 165.005 199.114 1.00 17.54  ? 3067 THR A CG2   1 
ATOM   12827 N  N     . MET A 1 3068 ? 162.675 164.655 195.350 1.00 24.18  ? 3068 MET A N     1 
ATOM   12828 C  CA    . MET A 1 3068 ? 163.167 164.113 194.057 1.00 26.44  ? 3068 MET A CA    1 
ATOM   12829 C  C     . MET A 1 3068 ? 164.272 163.079 194.323 1.00 22.59  ? 3068 MET A C     1 
ATOM   12830 O  O     . MET A 1 3068 ? 164.859 163.109 195.427 1.00 20.14  ? 3068 MET A O     1 
ATOM   12831 C  CB    . MET A 1 3068 ? 163.721 165.233 193.170 1.00 25.08  ? 3068 MET A CB    1 
ATOM   12832 C  CG    . MET A 1 3068 ? 164.821 166.048 193.821 1.00 24.95  ? 3068 MET A CG    1 
ATOM   12833 S  SD    . MET A 1 3068 ? 165.498 167.292 192.705 1.00 55.74  ? 3068 MET A SD    1 
ATOM   12834 C  CE    . MET A 1 3068 ? 164.009 168.206 192.278 1.00 39.11  ? 3068 MET A CE    1 
ATOM   12835 N  N     . ASN A 1 3069 ? 164.538 162.206 193.347 1.00 24.55  ? 3069 ASN A N     1 
ATOM   12836 C  CA    . ASN A 1 3069 ? 165.606 161.179 193.498 1.00 24.39  ? 3069 ASN A CA    1 
ATOM   12837 C  C     . ASN A 1 3069 ? 166.963 161.811 193.172 1.00 29.54  ? 3069 ASN A C     1 
ATOM   12838 O  O     . ASN A 1 3069 ? 166.993 162.793 192.399 1.00 31.35  ? 3069 ASN A O     1 
ATOM   12839 C  CB    . ASN A 1 3069 ? 165.312 159.935 192.666 1.00 28.93  ? 3069 ASN A CB    1 
ATOM   12840 C  CG    . ASN A 1 3069 ? 164.227 159.084 193.282 1.00 27.67  ? 3069 ASN A CG    1 
ATOM   12841 O  OD1   . ASN A 1 3069 ? 164.371 158.623 194.420 1.00 27.81  ? 3069 ASN A OD1   1 
ATOM   12842 N  ND2   . ASN A 1 3069 ? 163.141 158.866 192.556 1.00 30.57  ? 3069 ASN A ND2   1 
ATOM   12843 N  N     . PRO A 1 3070 ? 168.083 161.298 193.726 1.00 28.90  ? 3070 PRO A N     1 
ATOM   12844 C  CA    . PRO A 1 3070 ? 169.415 161.898 193.522 1.00 30.91  ? 3070 PRO A CA    1 
ATOM   12845 C  C     . PRO A 1 3070 ? 170.002 161.580 192.149 1.00 34.75  ? 3070 PRO A C     1 
ATOM   12846 O  O     . PRO A 1 3070 ? 171.041 160.927 192.020 1.00 39.20  ? 3070 PRO A O     1 
ATOM   12847 C  CB    . PRO A 1 3070 ? 170.227 161.281 194.667 1.00 25.84  ? 3070 PRO A CB    1 
ATOM   12848 C  CG    . PRO A 1 3070 ? 169.608 159.956 194.882 1.00 21.32  ? 3070 PRO A CG    1 
ATOM   12849 C  CD    . PRO A 1 3070 ? 168.139 160.123 194.613 1.00 24.73  ? 3070 PRO A CD    1 
ATOM   12850 N  N     . SER A 1 3071 ? 169.327 162.048 191.104 1.00 38.05  ? 3071 SER A N     1 
ATOM   12851 C  CA    . SER A 1 3071 ? 169.821 161.877 189.747 1.00 45.52  ? 3071 SER A CA    1 
ATOM   12852 C  C     . SER A 1 3071 ? 170.935 162.875 189.455 1.00 53.79  ? 3071 SER A C     1 
ATOM   12853 O  O     . SER A 1 3071 ? 170.917 164.016 189.923 1.00 49.54  ? 3071 SER A O     1 
ATOM   12854 C  CB    . SER A 1 3071 ? 168.689 162.046 188.734 1.00 49.33  ? 3071 SER A CB    1 
ATOM   12855 O  OG    . SER A 1 3071 ? 169.175 161.947 187.406 1.00 51.84  ? 3071 SER A OG    1 
ATOM   12856 N  N     . SER A 1 3072 ? 171.915 162.429 188.667 1.00 59.27  ? 3072 SER A N     1 
ATOM   12857 C  CA    . SER A 1 3072 ? 173.050 163.282 188.332 1.00 57.80  ? 3072 SER A CA    1 
ATOM   12858 C  C     . SER A 1 3072 ? 172.664 164.340 187.303 1.00 60.54  ? 3072 SER A C     1 
ATOM   12859 O  O     . SER A 1 3072 ? 172.804 165.543 187.550 1.00 60.37  ? 3072 SER A O     1 
ATOM   12860 C  CB    . SER A 1 3072 ? 174.213 162.429 187.818 1.00 62.53  ? 3072 SER A CB    1 
ATOM   12861 O  OG    . SER A 1 3072 ? 174.557 161.420 188.752 1.00 66.08  ? 3072 SER A OG    1 
ATOM   12862 N  N     . GLU A 1 3073 ? 172.173 163.907 186.139 1.00 60.56  ? 3073 GLU A N     1 
ATOM   12863 C  CA    . GLU A 1 3073 ? 171.797 164.859 185.099 1.00 61.19  ? 3073 GLU A CA    1 
ATOM   12864 C  C     . GLU A 1 3073 ? 170.479 165.553 185.417 1.00 57.81  ? 3073 GLU A C     1 
ATOM   12865 O  O     . GLU A 1 3073 ? 170.276 166.704 185.015 1.00 56.28  ? 3073 GLU A O     1 
ATOM   12866 C  CB    . GLU A 1 3073 ? 171.713 164.157 183.744 1.00 68.95  ? 3073 GLU A CB    1 
ATOM   12867 C  CG    . GLU A 1 3073 ? 170.918 162.863 183.760 1.00 76.98  ? 3073 GLU A CG    1 
ATOM   12868 C  CD    . GLU A 1 3073 ? 170.698 162.299 182.370 1.00 81.12  ? 3073 GLU A CD    1 
ATOM   12869 O  OE1   . GLU A 1 3073 ? 171.183 162.912 181.396 1.00 82.23  ? 3073 GLU A OE1   1 
ATOM   12870 O  OE2   . GLU A 1 3073 ? 170.040 161.245 182.252 1.00 75.97  ? 3073 GLU A OE2   1 
ATOM   12871 N  N     . GLY A 1 3074 ? 169.576 164.873 186.126 1.00 60.29  ? 3074 GLY A N     1 
ATOM   12872 C  CA    . GLY A 1 3074 ? 168.304 165.489 186.468 1.00 55.58  ? 3074 GLY A CA    1 
ATOM   12873 C  C     . GLY A 1 3074 ? 168.462 166.698 187.369 1.00 48.41  ? 3074 GLY A C     1 
ATOM   12874 O  O     . GLY A 1 3074 ? 167.708 167.668 187.260 1.00 50.61  ? 3074 GLY A O     1 
ATOM   12875 N  N     . LEU A 1 3075 ? 169.439 166.654 188.278 1.00 45.68  ? 3075 LEU A N     1 
ATOM   12876 C  CA    . LEU A 1 3075 ? 169.689 167.796 189.151 1.00 42.51  ? 3075 LEU A CA    1 
ATOM   12877 C  C     . LEU A 1 3075 ? 170.198 168.997 188.364 1.00 42.37  ? 3075 LEU A C     1 
ATOM   12878 O  O     . LEU A 1 3075 ? 169.778 170.133 188.613 1.00 39.83  ? 3075 LEU A O     1 
ATOM   12879 C  CB    . LEU A 1 3075 ? 170.683 167.412 190.245 1.00 44.10  ? 3075 LEU A CB    1 
ATOM   12880 C  CG    . LEU A 1 3075 ? 170.547 168.229 191.528 1.00 36.36  ? 3075 LEU A CG    1 
ATOM   12881 C  CD1   . LEU A 1 3075 ? 169.148 168.078 192.085 1.00 31.73  ? 3075 LEU A CD1   1 
ATOM   12882 C  CD2   . LEU A 1 3075 ? 171.586 167.804 192.550 1.00 30.66  ? 3075 LEU A CD2   1 
ATOM   12883 N  N     . LYS A 1 3076 ? 171.109 168.767 187.415 1.00 47.18  ? 3076 LYS A N     1 
ATOM   12884 C  CA    . LYS A 1 3076 ? 171.615 169.863 186.596 1.00 49.03  ? 3076 LYS A CA    1 
ATOM   12885 C  C     . LYS A 1 3076 ? 170.513 170.457 185.729 1.00 42.55  ? 3076 LYS A C     1 
ATOM   12886 O  O     . LYS A 1 3076 ? 170.448 171.678 185.543 1.00 38.30  ? 3076 LYS A O     1 
ATOM   12887 C  CB    . LYS A 1 3076 ? 172.780 169.378 185.732 1.00 49.84  ? 3076 LYS A CB    1 
ATOM   12888 C  CG    . LYS A 1 3076 ? 174.149 169.738 186.287 1.00 47.05  ? 3076 LYS A CG    1 
ATOM   12889 C  CD    . LYS A 1 3076 ? 175.103 168.555 186.236 1.00 49.47  ? 3076 LYS A CD    1 
ATOM   12890 C  CE    . LYS A 1 3076 ? 175.557 168.271 184.815 1.00 55.58  ? 3076 LYS A CE    1 
ATOM   12891 N  NZ    . LYS A 1 3076 ? 176.982 167.844 184.764 1.00 62.35  ? 3076 LYS A NZ    1 
ATOM   12892 N  N     . ASP A 1 3077 ? 169.640 169.607 185.184 1.00 40.30  ? 3077 ASP A N     1 
ATOM   12893 C  CA    . ASP A 1 3077 ? 168.524 170.100 184.384 1.00 42.22  ? 3077 ASP A CA    1 
ATOM   12894 C  C     . ASP A 1 3077 ? 167.573 170.944 185.224 1.00 42.98  ? 3077 ASP A C     1 
ATOM   12895 O  O     . ASP A 1 3077 ? 167.073 171.975 184.761 1.00 47.51  ? 3077 ASP A O     1 
ATOM   12896 C  CB    . ASP A 1 3077 ? 167.780 168.927 183.745 1.00 46.69  ? 3077 ASP A CB    1 
ATOM   12897 C  CG    . ASP A 1 3077 ? 166.350 169.273 183.376 1.00 53.27  ? 3077 ASP A CG    1 
ATOM   12898 O  OD1   . ASP A 1 3077 ? 166.140 169.846 182.286 1.00 54.87  ? 3077 ASP A OD1   1 
ATOM   12899 O  OD2   . ASP A 1 3077 ? 165.437 168.970 184.172 1.00 51.14  ? 3077 ASP A OD2   1 
ATOM   12900 N  N     . ARG A 1 3078 ? 167.312 170.520 186.462 1.00 41.47  ? 3078 ARG A N     1 
ATOM   12901 C  CA    . ARG A 1 3078 ? 166.383 171.251 187.318 1.00 38.44  ? 3078 ARG A CA    1 
ATOM   12902 C  C     . ARG A 1 3078 ? 166.962 172.581 187.785 1.00 32.96  ? 3078 ARG A C     1 
ATOM   12903 O  O     . ARG A 1 3078 ? 166.204 173.506 188.100 1.00 33.48  ? 3078 ARG A O     1 
ATOM   12904 C  CB    . ARG A 1 3078 ? 165.987 170.384 188.514 1.00 42.87  ? 3078 ARG A CB    1 
ATOM   12905 C  CG    . ARG A 1 3078 ? 164.806 170.919 189.302 1.00 44.09  ? 3078 ARG A CG    1 
ATOM   12906 C  CD    . ARG A 1 3078 ? 163.491 170.412 188.739 1.00 43.76  ? 3078 ARG A CD    1 
ATOM   12907 N  NE    . ARG A 1 3078 ? 163.246 169.008 189.041 1.00 41.20  ? 3078 ARG A NE    1 
ATOM   12908 C  CZ    . ARG A 1 3078 ? 163.088 168.061 188.126 1.00 43.52  ? 3078 ARG A CZ    1 
ATOM   12909 N  NH1   . ARG A 1 3078 ? 163.144 168.333 186.833 1.00 42.46  ? 3078 ARG A NH1   1 
ATOM   12910 N  NH2   . ARG A 1 3078 ? 162.865 166.810 188.519 1.00 51.43  ? 3078 ARG A NH2   1 
ATOM   12911 N  N     . ALA A 1 3079 ? 168.291 172.702 187.831 1.00 35.23  ? 3079 ALA A N     1 
ATOM   12912 C  CA    . ALA A 1 3079 ? 168.907 173.955 188.253 1.00 34.00  ? 3079 ALA A CA    1 
ATOM   12913 C  C     . ALA A 1 3079 ? 168.577 175.107 187.314 1.00 36.39  ? 3079 ALA A C     1 
ATOM   12914 O  O     . ALA A 1 3079 ? 168.670 176.270 187.721 1.00 33.77  ? 3079 ALA A O     1 
ATOM   12915 C  CB    . ALA A 1 3079 ? 170.423 173.787 188.360 1.00 28.04  ? 3079 ALA A CB    1 
ATOM   12916 N  N     . ALA A 1 3080 ? 168.196 174.814 186.073 1.00 39.81  ? 3080 ALA A N     1 
ATOM   12917 C  CA    . ALA A 1 3080 ? 167.773 175.823 185.111 1.00 36.21  ? 3080 ALA A CA    1 
ATOM   12918 C  C     . ALA A 1 3080 ? 166.272 175.834 184.876 1.00 29.10  ? 3080 ALA A C     1 
ATOM   12919 O  O     . ALA A 1 3080 ? 165.691 176.903 184.678 1.00 26.84  ? 3080 ALA A O     1 
ATOM   12920 C  CB    . ALA A 1 3080 ? 168.490 175.614 183.773 1.00 31.76  ? 3080 ALA A CB    1 
ATOM   12921 N  N     . THR A 1 3081 ? 165.631 174.663 184.887 1.00 29.25  ? 3081 THR A N     1 
ATOM   12922 C  CA    . THR A 1 3081 ? 164.185 174.606 184.698 1.00 31.33  ? 3081 THR A CA    1 
ATOM   12923 C  C     . THR A 1 3081 ? 163.450 175.294 185.843 1.00 34.88  ? 3081 THR A C     1 
ATOM   12924 O  O     . THR A 1 3081 ? 162.482 176.028 185.614 1.00 35.05  ? 3081 THR A O     1 
ATOM   12925 C  CB    . THR A 1 3081 ? 163.735 173.150 184.560 1.00 37.73  ? 3081 THR A CB    1 
ATOM   12926 O  OG1   . THR A 1 3081 ? 164.103 172.657 183.266 1.00 36.91  ? 3081 THR A OG1   1 
ATOM   12927 C  CG2   . THR A 1 3081 ? 162.229 173.032 184.722 1.00 40.80  ? 3081 THR A CG2   1 
ATOM   12928 N  N     . SER A 1 3082 ? 163.898 175.077 187.078 1.00 34.09  ? 3082 SER A N     1 
ATOM   12929 C  CA    . SER A 1 3082 ? 163.307 175.699 188.263 1.00 29.47  ? 3082 SER A CA    1 
ATOM   12930 C  C     . SER A 1 3082 ? 164.419 176.315 189.101 1.00 30.25  ? 3082 SER A C     1 
ATOM   12931 O  O     . SER A 1 3082 ? 164.896 175.705 190.068 1.00 33.08  ? 3082 SER A O     1 
ATOM   12932 C  CB    . SER A 1 3082 ? 162.497 174.688 189.075 1.00 37.57  ? 3082 SER A CB    1 
ATOM   12933 O  OG    . SER A 1 3082 ? 161.701 175.342 190.049 1.00 35.79  ? 3082 SER A OG    1 
ATOM   12934 N  N     . PRO A 1 3083 ? 164.867 177.524 188.750 1.00 29.05  ? 3083 PRO A N     1 
ATOM   12935 C  CA    . PRO A 1 3083 ? 165.926 178.169 189.544 1.00 30.44  ? 3083 PRO A CA    1 
ATOM   12936 C  C     . PRO A 1 3083 ? 165.539 178.421 190.991 1.00 32.38  ? 3083 PRO A C     1 
ATOM   12937 O  O     . PRO A 1 3083 ? 166.414 178.396 191.866 1.00 36.70  ? 3083 PRO A O     1 
ATOM   12938 C  CB    . PRO A 1 3083 ? 166.176 179.485 188.792 1.00 28.05  ? 3083 PRO A CB    1 
ATOM   12939 C  CG    . PRO A 1 3083 ? 164.937 179.711 187.987 1.00 25.26  ? 3083 PRO A CG    1 
ATOM   12940 C  CD    . PRO A 1 3083 ? 164.449 178.351 187.607 1.00 25.31  ? 3083 PRO A CD    1 
ATOM   12941 N  N     . ALA A 1 3084 ? 164.257 178.666 191.273 1.00 27.93  ? 3084 ALA A N     1 
ATOM   12942 C  CA    . ALA A 1 3084 ? 163.829 178.920 192.644 1.00 27.51  ? 3084 ALA A CA    1 
ATOM   12943 C  C     . ALA A 1 3084 ? 163.965 177.692 193.533 1.00 32.06  ? 3084 ALA A C     1 
ATOM   12944 O  O     . ALA A 1 3084 ? 164.029 177.835 194.758 1.00 37.06  ? 3084 ALA A O     1 
ATOM   12945 C  CB    . ALA A 1 3084 ? 162.384 179.420 192.667 1.00 24.62  ? 3084 ALA A CB    1 
ATOM   12946 N  N     . LEU A 1 3085 ? 164.009 176.492 192.948 1.00 27.17  ? 3085 LEU A N     1 
ATOM   12947 C  CA    . LEU A 1 3085 ? 164.202 175.282 193.738 1.00 23.84  ? 3085 LEU A CA    1 
ATOM   12948 C  C     . LEU A 1 3085 ? 165.567 175.238 194.407 1.00 26.68  ? 3085 LEU A C     1 
ATOM   12949 O  O     . LEU A 1 3085 ? 165.758 174.461 195.348 1.00 34.03  ? 3085 LEU A O     1 
ATOM   12950 C  CB    . LEU A 1 3085 ? 164.021 174.043 192.859 1.00 27.06  ? 3085 LEU A CB    1 
ATOM   12951 C  CG    . LEU A 1 3085 ? 162.654 173.360 192.901 1.00 28.54  ? 3085 LEU A CG    1 
ATOM   12952 C  CD1   . LEU A 1 3085 ? 162.691 172.040 192.149 1.00 30.04  ? 3085 LEU A CD1   1 
ATOM   12953 C  CD2   . LEU A 1 3085 ? 162.211 173.144 194.337 1.00 25.15  ? 3085 LEU A CD2   1 
ATOM   12954 N  N     . PHE A 1 3086 ? 166.518 176.050 193.946 1.00 29.25  ? 3086 PHE A N     1 
ATOM   12955 C  CA    . PHE A 1 3086 ? 167.861 176.068 194.503 1.00 26.42  ? 3086 PHE A CA    1 
ATOM   12956 C  C     . PHE A 1 3086 ? 168.219 177.397 195.151 1.00 27.74  ? 3086 PHE A C     1 
ATOM   12957 O  O     . PHE A 1 3086 ? 169.326 177.529 195.687 1.00 33.73  ? 3086 PHE A O     1 
ATOM   12958 C  CB    . PHE A 1 3086 ? 168.888 175.727 193.415 1.00 26.15  ? 3086 PHE A CB    1 
ATOM   12959 C  CG    . PHE A 1 3086 ? 168.794 174.311 192.919 1.00 29.83  ? 3086 PHE A CG    1 
ATOM   12960 C  CD1   . PHE A 1 3086 ? 167.820 173.944 192.005 1.00 26.59  ? 3086 PHE A CD1   1 
ATOM   12961 C  CD2   . PHE A 1 3086 ? 169.672 173.344 193.376 1.00 32.58  ? 3086 PHE A CD2   1 
ATOM   12962 C  CE1   . PHE A 1 3086 ? 167.728 172.642 191.552 1.00 30.07  ? 3086 PHE A CE1   1 
ATOM   12963 C  CE2   . PHE A 1 3086 ? 169.586 172.040 192.926 1.00 36.85  ? 3086 PHE A CE2   1 
ATOM   12964 C  CZ    . PHE A 1 3086 ? 168.613 171.689 192.013 1.00 35.47  ? 3086 PHE A CZ    1 
ATOM   12965 N  N     . ASN A 1 3087 ? 167.323 178.381 195.121 1.00 28.44  ? 3087 ASN A N     1 
ATOM   12966 C  CA    . ASN A 1 3087 ? 167.541 179.667 195.769 1.00 31.28  ? 3087 ASN A CA    1 
ATOM   12967 C  C     . ASN A 1 3087 ? 166.561 179.957 196.893 1.00 33.96  ? 3087 ASN A C     1 
ATOM   12968 O  O     . ASN A 1 3087 ? 166.939 180.615 197.865 1.00 34.53  ? 3087 ASN A O     1 
ATOM   12969 C  CB    . ASN A 1 3087 ? 167.456 180.809 194.742 1.00 31.38  ? 3087 ASN A CB    1 
ATOM   12970 C  CG    . ASN A 1 3087 ? 168.401 180.618 193.576 1.00 39.89  ? 3087 ASN A CG    1 
ATOM   12971 O  OD1   . ASN A 1 3087 ? 169.322 179.804 193.633 1.00 43.23  ? 3087 ASN A OD1   1 
ATOM   12972 N  ND2   . ASN A 1 3087 ? 168.176 181.371 192.505 1.00 42.37  ? 3087 ASN A ND2   1 
ATOM   12973 N  N     . ARG A 1 3088 ? 165.318 179.488 196.789 1.00 28.26  ? 3088 ARG A N     1 
ATOM   12974 C  CA    . ARG A 1 3088 ? 164.305 179.724 197.806 1.00 29.95  ? 3088 ARG A CA    1 
ATOM   12975 C  C     . ARG A 1 3088 ? 163.994 178.492 198.641 1.00 33.79  ? 3088 ARG A C     1 
ATOM   12976 O  O     . ARG A 1 3088 ? 163.301 178.613 199.657 1.00 28.81  ? 3088 ARG A O     1 
ATOM   12977 C  CB    . ARG A 1 3088 ? 163.009 180.229 197.155 1.00 33.52  ? 3088 ARG A CB    1 
ATOM   12978 C  CG    . ARG A 1 3088 ? 163.188 181.460 196.285 1.00 27.52  ? 3088 ARG A CG    1 
ATOM   12979 C  CD    . ARG A 1 3088 ? 163.271 182.728 197.125 1.00 33.43  ? 3088 ARG A CD    1 
ATOM   12980 N  NE    . ARG A 1 3088 ? 164.447 183.538 196.821 1.00 41.70  ? 3088 ARG A NE    1 
ATOM   12981 C  CZ    . ARG A 1 3088 ? 164.712 184.089 195.642 1.00 37.55  ? 3088 ARG A CZ    1 
ATOM   12982 N  NH1   . ARG A 1 3088 ? 163.875 183.987 194.622 1.00 31.27  ? 3088 ARG A NH1   1 
ATOM   12983 N  NH2   . ARG A 1 3088 ? 165.842 184.773 195.488 1.00 30.84  ? 3088 ARG A NH2   1 
ATOM   12984 N  N     . CYS A 1 3089 ? 164.478 177.319 198.244 1.00 30.09  ? 3089 CYS A N     1 
ATOM   12985 C  CA    . CYS A 1 3089 ? 164.223 176.073 198.951 1.00 17.71  ? 3089 CYS A CA    1 
ATOM   12986 C  C     . CYS A 1 3089 ? 165.497 175.623 199.650 1.00 19.23  ? 3089 CYS A C     1 
ATOM   12987 O  O     . CYS A 1 3089 ? 166.583 175.681 199.064 1.00 23.86  ? 3089 CYS A O     1 
ATOM   12988 C  CB    . CYS A 1 3089 ? 163.738 174.987 197.988 1.00 15.52  ? 3089 CYS A CB    1 
ATOM   12989 S  SG    . CYS A 1 3089 ? 162.174 175.359 197.169 1.00 42.11  ? 3089 CYS A SG    1 
ATOM   12990 N  N     . VAL A 1 3090 ? 165.363 175.181 200.898 1.00 22.92  ? 3090 VAL A N     1 
ATOM   12991 C  CA    . VAL A 1 3090 ? 166.505 174.632 201.620 1.00 15.40  ? 3090 VAL A CA    1 
ATOM   12992 C  C     . VAL A 1 3090 ? 166.698 173.186 201.186 1.00 13.78  ? 3090 VAL A C     1 
ATOM   12993 O  O     . VAL A 1 3090 ? 165.807 172.346 201.355 1.00 15.86  ? 3090 VAL A O     1 
ATOM   12994 C  CB    . VAL A 1 3090 ? 166.303 174.740 203.136 1.00 13.76  ? 3090 VAL A CB    1 
ATOM   12995 C  CG1   . VAL A 1 3090 ? 167.362 173.935 203.871 1.00 12.00  ? 3090 VAL A CG1   1 
ATOM   12996 C  CG2   . VAL A 1 3090 ? 166.343 176.195 203.571 1.00 17.06  ? 3090 VAL A CG2   1 
ATOM   12997 N  N     . LEU A 1 3091 ? 167.865 172.890 200.621 1.00 16.45  ? 3091 LEU A N     1 
ATOM   12998 C  CA    . LEU A 1 3091 ? 168.154 171.562 200.099 1.00 15.92  ? 3091 LEU A CA    1 
ATOM   12999 C  C     . LEU A 1 3091 ? 168.687 170.680 201.219 1.00 18.32  ? 3091 LEU A C     1 
ATOM   13000 O  O     . LEU A 1 3091 ? 169.632 171.055 201.920 1.00 19.30  ? 3091 LEU A O     1 
ATOM   13001 C  CB    . LEU A 1 3091 ? 169.162 171.642 198.951 1.00 15.78  ? 3091 LEU A CB    1 
ATOM   13002 C  CG    . LEU A 1 3091 ? 169.408 170.382 198.113 1.00 22.04  ? 3091 LEU A CG    1 
ATOM   13003 C  CD1   . LEU A 1 3091 ? 169.736 170.763 196.680 1.00 20.19  ? 3091 LEU A CD1   1 
ATOM   13004 C  CD2   . LEU A 1 3091 ? 170.526 169.527 198.694 1.00 19.86  ? 3091 LEU A CD2   1 
ATOM   13005 N  N     . ASN A 1 3092 ? 168.075 169.510 201.383 1.00 21.04  ? 3092 ASN A N     1 
ATOM   13006 C  CA    . ASN A 1 3092 ? 168.493 168.531 202.377 1.00 16.83  ? 3092 ASN A CA    1 
ATOM   13007 C  C     . ASN A 1 3092 ? 168.734 167.207 201.670 1.00 16.10  ? 3092 ASN A C     1 
ATOM   13008 O  O     . ASN A 1 3092 ? 167.793 166.595 201.155 1.00 18.27  ? 3092 ASN A O     1 
ATOM   13009 C  CB    . ASN A 1 3092 ? 167.438 168.379 203.473 1.00 16.20  ? 3092 ASN A CB    1 
ATOM   13010 C  CG    . ASN A 1 3092 ? 167.627 169.370 204.600 1.00 19.93  ? 3092 ASN A CG    1 
ATOM   13011 O  OD1   . ASN A 1 3092 ? 168.264 169.067 205.605 1.00 24.37  ? 3092 ASN A OD1   1 
ATOM   13012 N  ND2   . ASN A 1 3092 ? 167.074 170.566 204.437 1.00 20.84  ? 3092 ASN A ND2   1 
ATOM   13013 N  N     . TRP A 1 3093 ? 169.990 166.768 201.646 1.00 15.37  ? 3093 TRP A N     1 
ATOM   13014 C  CA    . TRP A 1 3093 ? 170.364 165.534 200.956 1.00 14.86  ? 3093 TRP A CA    1 
ATOM   13015 C  C     . TRP A 1 3093 ? 170.218 164.371 201.924 1.00 17.60  ? 3093 TRP A C     1 
ATOM   13016 O  O     . TRP A 1 3093 ? 171.151 164.003 202.639 1.00 22.91  ? 3093 TRP A O     1 
ATOM   13017 C  CB    . TRP A 1 3093 ? 171.779 165.630 200.402 1.00 18.49  ? 3093 TRP A CB    1 
ATOM   13018 C  CG    . TRP A 1 3093 ? 172.018 164.727 199.234 1.00 16.63  ? 3093 TRP A CG    1 
ATOM   13019 C  CD1   . TRP A 1 3093 ? 172.299 163.393 199.275 1.00 15.77  ? 3093 TRP A CD1   1 
ATOM   13020 C  CD2   . TRP A 1 3093 ? 171.985 165.087 197.848 1.00 17.94  ? 3093 TRP A CD2   1 
ATOM   13021 N  NE1   . TRP A 1 3093 ? 172.450 162.901 198.003 1.00 17.80  ? 3093 TRP A NE1   1 
ATOM   13022 C  CE2   . TRP A 1 3093 ? 172.262 163.921 197.108 1.00 19.21  ? 3093 TRP A CE2   1 
ATOM   13023 C  CE3   . TRP A 1 3093 ? 171.752 166.282 197.162 1.00 17.83  ? 3093 TRP A CE3   1 
ATOM   13024 C  CZ2   . TRP A 1 3093 ? 172.312 163.915 195.716 1.00 18.80  ? 3093 TRP A CZ2   1 
ATOM   13025 C  CZ3   . TRP A 1 3093 ? 171.801 166.274 195.782 1.00 19.94  ? 3093 TRP A CZ3   1 
ATOM   13026 C  CH2   . TRP A 1 3093 ? 172.079 165.099 195.073 1.00 21.00  ? 3093 TRP A CH2   1 
ATOM   13027 N  N     . PHE A 1 3094 ? 169.019 163.788 201.953 1.00 19.26  ? 3094 PHE A N     1 
ATOM   13028 C  CA    . PHE A 1 3094 ? 168.820 162.561 202.715 1.00 14.71  ? 3094 PHE A CA    1 
ATOM   13029 C  C     . PHE A 1 3094 ? 169.611 161.412 202.105 1.00 19.03  ? 3094 PHE A C     1 
ATOM   13030 O  O     . PHE A 1 3094 ? 170.204 160.604 202.829 1.00 24.46  ? 3094 PHE A O     1 
ATOM   13031 C  CB    . PHE A 1 3094 ? 167.333 162.212 202.781 1.00 17.26  ? 3094 PHE A CB    1 
ATOM   13032 C  CG    . PHE A 1 3094 ? 166.530 163.106 203.689 1.00 23.42  ? 3094 PHE A CG    1 
ATOM   13033 C  CD1   . PHE A 1 3094 ? 167.076 164.262 204.225 1.00 26.12  ? 3094 PHE A CD1   1 
ATOM   13034 C  CD2   . PHE A 1 3094 ? 165.222 162.784 204.006 1.00 23.39  ? 3094 PHE A CD2   1 
ATOM   13035 C  CE1   . PHE A 1 3094 ? 166.332 165.077 205.057 1.00 29.51  ? 3094 PHE A CE1   1 
ATOM   13036 C  CE2   . PHE A 1 3094 ? 164.474 163.593 204.837 1.00 24.76  ? 3094 PHE A CE2   1 
ATOM   13037 C  CZ    . PHE A 1 3094 ? 165.029 164.741 205.363 1.00 29.80  ? 3094 PHE A CZ    1 
ATOM   13038 N  N     . GLY A 1 3095 ? 169.638 161.332 200.775 1.00 15.99  ? 3095 GLY A N     1 
ATOM   13039 C  CA    . GLY A 1 3095 ? 170.343 160.269 200.096 1.00 14.10  ? 3095 GLY A CA    1 
ATOM   13040 C  C     . GLY A 1 3095 ? 169.728 158.911 200.396 1.00 21.20  ? 3095 GLY A C     1 
ATOM   13041 O  O     . GLY A 1 3095 ? 168.523 158.767 200.618 1.00 22.33  ? 3095 GLY A O     1 
ATOM   13042 N  N     . ASP A 1 3096 ? 170.590 157.903 200.394 1.00 22.60  ? 3096 ASP A N     1 
ATOM   13043 C  CA    . ASP A 1 3096 ? 170.201 156.561 200.794 1.00 23.26  ? 3096 ASP A CA    1 
ATOM   13044 C  C     . ASP A 1 3096 ? 170.584 156.323 202.251 1.00 24.38  ? 3096 ASP A C     1 
ATOM   13045 O  O     . ASP A 1 3096 ? 171.406 157.039 202.829 1.00 23.46  ? 3096 ASP A O     1 
ATOM   13046 C  CB    . ASP A 1 3096 ? 170.861 155.516 199.895 1.00 24.75  ? 3096 ASP A CB    1 
ATOM   13047 C  CG    . ASP A 1 3096 ? 170.095 154.209 199.860 1.00 31.88  ? 3096 ASP A CG    1 
ATOM   13048 O  OD1   . ASP A 1 3096 ? 169.730 153.700 200.941 1.00 30.15  ? 3096 ASP A OD1   1 
ATOM   13049 O  OD2   . ASP A 1 3096 ? 169.857 153.688 198.750 1.00 37.97  ? 3096 ASP A OD2   1 
ATOM   13050 N  N     . TRP A 1 3097 ? 169.967 155.306 202.846 1.00 21.53  ? 3097 TRP A N     1 
ATOM   13051 C  CA    . TRP A 1 3097 ? 170.295 154.945 204.218 1.00 20.28  ? 3097 TRP A CA    1 
ATOM   13052 C  C     . TRP A 1 3097 ? 171.732 154.448 204.296 1.00 25.85  ? 3097 TRP A C     1 
ATOM   13053 O  O     . TRP A 1 3097 ? 172.154 153.599 203.504 1.00 23.20  ? 3097 TRP A O     1 
ATOM   13054 C  CB    . TRP A 1 3097 ? 169.332 153.879 204.735 1.00 19.26  ? 3097 TRP A CB    1 
ATOM   13055 C  CG    . TRP A 1 3097 ? 167.951 154.394 204.997 1.00 21.97  ? 3097 TRP A CG    1 
ATOM   13056 C  CD1   . TRP A 1 3097 ? 167.487 155.654 204.761 1.00 20.85  ? 3097 TRP A CD1   1 
ATOM   13057 C  CD2   . TRP A 1 3097 ? 166.854 153.662 205.554 1.00 19.30  ? 3097 TRP A CD2   1 
ATOM   13058 N  NE1   . TRP A 1 3097 ? 166.169 155.752 205.132 1.00 17.63  ? 3097 TRP A NE1   1 
ATOM   13059 C  CE2   . TRP A 1 3097 ? 165.756 154.542 205.623 1.00 18.94  ? 3097 TRP A CE2   1 
ATOM   13060 C  CE3   . TRP A 1 3097 ? 166.693 152.347 205.999 1.00 19.43  ? 3097 TRP A CE3   1 
ATOM   13061 C  CZ2   . TRP A 1 3097 ? 164.515 154.150 206.119 1.00 22.18  ? 3097 TRP A CZ2   1 
ATOM   13062 C  CZ3   . TRP A 1 3097 ? 165.461 151.959 206.491 1.00 18.29  ? 3097 TRP A CZ3   1 
ATOM   13063 C  CH2   . TRP A 1 3097 ? 164.388 152.857 206.547 1.00 20.27  ? 3097 TRP A CH2   1 
ATOM   13064 N  N     . SER A 1 3098 ? 172.483 154.980 205.255 1.00 32.44  ? 3098 SER A N     1 
ATOM   13065 C  CA    . SER A 1 3098 ? 173.887 154.634 205.383 1.00 25.53  ? 3098 SER A CA    1 
ATOM   13066 C  C     . SER A 1 3098 ? 174.043 153.233 205.972 1.00 27.47  ? 3098 SER A C     1 
ATOM   13067 O  O     . SER A 1 3098 ? 173.071 152.563 206.332 1.00 25.42  ? 3098 SER A O     1 
ATOM   13068 C  CB    . SER A 1 3098 ? 174.614 155.657 206.254 1.00 28.99  ? 3098 SER A CB    1 
ATOM   13069 O  OG    . SER A 1 3098 ? 174.058 155.699 207.557 1.00 36.85  ? 3098 SER A OG    1 
ATOM   13070 N  N     . THR A 1 3099 ? 175.299 152.791 206.056 1.00 30.82  ? 3099 THR A N     1 
ATOM   13071 C  CA    . THR A 1 3099 ? 175.593 151.511 206.691 1.00 27.93  ? 3099 THR A CA    1 
ATOM   13072 C  C     . THR A 1 3099 ? 175.164 151.519 208.152 1.00 31.33  ? 3099 THR A C     1 
ATOM   13073 O  O     . THR A 1 3099 ? 174.661 150.513 208.666 1.00 34.16  ? 3099 THR A O     1 
ATOM   13074 C  CB    . THR A 1 3099 ? 177.084 151.196 206.568 1.00 31.95  ? 3099 THR A CB    1 
ATOM   13075 O  OG1   . THR A 1 3099 ? 177.575 151.689 205.315 1.00 32.71  ? 3099 THR A OG1   1 
ATOM   13076 C  CG2   . THR A 1 3099 ? 177.321 149.698 206.642 1.00 40.07  ? 3099 THR A CG2   1 
ATOM   13077 N  N     . GLU A 1 3100 ? 175.360 152.648 208.836 1.00 32.07  ? 3100 GLU A N     1 
ATOM   13078 C  CA    . GLU A 1 3100 ? 174.877 152.784 210.206 1.00 32.55  ? 3100 GLU A CA    1 
ATOM   13079 C  C     . GLU A 1 3100 ? 173.355 152.722 210.264 1.00 31.71  ? 3100 GLU A C     1 
ATOM   13080 O  O     . GLU A 1 3100 ? 172.785 152.107 211.173 1.00 34.24  ? 3100 GLU A O     1 
ATOM   13081 C  CB    . GLU A 1 3100 ? 175.387 154.094 210.807 1.00 36.28  ? 3100 GLU A CB    1 
ATOM   13082 C  CG    . GLU A 1 3100 ? 174.616 154.569 212.025 1.00 42.36  ? 3100 GLU A CG    1 
ATOM   13083 C  CD    . GLU A 1 3100 ? 175.064 155.936 212.500 1.00 53.44  ? 3100 GLU A CD    1 
ATOM   13084 O  OE1   . GLU A 1 3100 ? 176.285 156.198 212.493 1.00 57.90  ? 3100 GLU A OE1   1 
ATOM   13085 O  OE2   . GLU A 1 3100 ? 174.196 156.749 212.878 1.00 45.85  ? 3100 GLU A OE2   1 
ATOM   13086 N  N     . ALA A 1 3101 ? 172.681 153.357 209.301 1.00 33.50  ? 3101 ALA A N     1 
ATOM   13087 C  CA    . ALA A 1 3101 ? 171.221 153.355 209.290 1.00 28.93  ? 3101 ALA A CA    1 
ATOM   13088 C  C     . ALA A 1 3101 ? 170.667 151.946 209.118 1.00 28.73  ? 3101 ALA A C     1 
ATOM   13089 O  O     . ALA A 1 3101 ? 169.712 151.560 209.802 1.00 30.28  ? 3101 ALA A O     1 
ATOM   13090 C  CB    . ALA A 1 3101 ? 170.703 154.272 208.182 1.00 27.00  ? 3101 ALA A CB    1 
ATOM   13091 N  N     . LEU A 1 3102 ? 171.251 151.165 208.206 1.00 23.66  ? 3102 LEU A N     1 
ATOM   13092 C  CA    . LEU A 1 3102 ? 170.808 149.787 208.025 1.00 17.24  ? 3102 LEU A CA    1 
ATOM   13093 C  C     . LEU A 1 3102 ? 171.055 148.963 209.282 1.00 23.58  ? 3102 LEU A C     1 
ATOM   13094 O  O     . LEU A 1 3102 ? 170.213 148.148 209.676 1.00 27.44  ? 3102 LEU A O     1 
ATOM   13095 C  CB    . LEU A 1 3102 ? 171.522 149.158 206.828 1.00 18.81  ? 3102 LEU A CB    1 
ATOM   13096 C  CG    . LEU A 1 3102 ? 171.328 149.826 205.467 1.00 18.00  ? 3102 LEU A CG    1 
ATOM   13097 C  CD1   . LEU A 1 3102 ? 172.162 149.126 204.406 1.00 13.95  ? 3102 LEU A CD1   1 
ATOM   13098 C  CD2   . LEU A 1 3102 ? 169.863 149.846 205.074 1.00 16.94  ? 3102 LEU A CD2   1 
ATOM   13099 N  N     . TYR A 1 3103 ? 172.211 149.159 209.919 1.00 26.30  ? 3103 TYR A N     1 
ATOM   13100 C  CA    . TYR A 1 3103 ? 172.528 148.418 211.135 1.00 27.42  ? 3103 TYR A CA    1 
ATOM   13101 C  C     . TYR A 1 3103 ? 171.563 148.765 212.263 1.00 28.92  ? 3103 TYR A C     1 
ATOM   13102 O  O     . TYR A 1 3103 ? 171.086 147.876 212.977 1.00 33.95  ? 3103 TYR A O     1 
ATOM   13103 C  CB    . TYR A 1 3103 ? 173.972 148.699 211.550 1.00 32.36  ? 3103 TYR A CB    1 
ATOM   13104 C  CG    . TYR A 1 3103 ? 174.446 147.901 212.743 1.00 33.22  ? 3103 TYR A CG    1 
ATOM   13105 C  CD1   . TYR A 1 3103 ? 174.924 146.608 212.588 1.00 30.45  ? 3103 TYR A CD1   1 
ATOM   13106 C  CD2   . TYR A 1 3103 ? 174.427 148.444 214.020 1.00 29.74  ? 3103 TYR A CD2   1 
ATOM   13107 C  CE1   . TYR A 1 3103 ? 175.361 145.875 213.670 1.00 32.93  ? 3103 TYR A CE1   1 
ATOM   13108 C  CE2   . TYR A 1 3103 ? 174.864 147.718 215.109 1.00 34.09  ? 3103 TYR A CE2   1 
ATOM   13109 C  CZ    . TYR A 1 3103 ? 175.330 146.434 214.928 1.00 39.71  ? 3103 TYR A CZ    1 
ATOM   13110 O  OH    . TYR A 1 3103 ? 175.768 145.705 216.008 1.00 50.68  ? 3103 TYR A OH    1 
ATOM   13111 N  N     . GLN A 1 3104 ? 171.269 150.056 212.442 1.00 27.14  ? 3104 GLN A N     1 
ATOM   13112 C  CA    . GLN A 1 3104 ? 170.339 150.464 213.491 1.00 28.81  ? 3104 GLN A CA    1 
ATOM   13113 C  C     . GLN A 1 3104 ? 168.929 149.958 213.217 1.00 29.28  ? 3104 GLN A C     1 
ATOM   13114 O  O     . GLN A 1 3104 ? 168.247 149.483 214.132 1.00 31.69  ? 3104 GLN A O     1 
ATOM   13115 C  CB    . GLN A 1 3104 ? 170.342 151.986 213.634 1.00 28.89  ? 3104 GLN A CB    1 
ATOM   13116 C  CG    . GLN A 1 3104 ? 171.593 152.548 214.282 1.00 26.44  ? 3104 GLN A CG    1 
ATOM   13117 C  CD    . GLN A 1 3104 ? 171.452 154.015 214.632 1.00 33.83  ? 3104 GLN A CD    1 
ATOM   13118 O  OE1   . GLN A 1 3104 ? 172.225 154.852 214.169 1.00 37.15  ? 3104 GLN A OE1   1 
ATOM   13119 N  NE2   . GLN A 1 3104 ? 170.457 154.334 215.451 1.00 34.85  ? 3104 GLN A NE2   1 
ATOM   13120 N  N     . VAL A 1 3105 ? 168.471 150.061 211.967 1.00 26.89  ? 3105 VAL A N     1 
ATOM   13121 C  CA    . VAL A 1 3105 ? 167.149 149.547 211.618 1.00 28.26  ? 3105 VAL A CA    1 
ATOM   13122 C  C     . VAL A 1 3105 ? 167.103 148.039 211.807 1.00 31.11  ? 3105 VAL A C     1 
ATOM   13123 O  O     . VAL A 1 3105 ? 166.147 147.496 212.374 1.00 34.49  ? 3105 VAL A O     1 
ATOM   13124 C  CB    . VAL A 1 3105 ? 166.780 149.948 210.177 1.00 29.42  ? 3105 VAL A CB    1 
ATOM   13125 C  CG1   . VAL A 1 3105 ? 165.645 149.079 209.655 1.00 31.95  ? 3105 VAL A CG1   1 
ATOM   13126 C  CG2   . VAL A 1 3105 ? 166.398 151.412 210.117 1.00 33.37  ? 3105 VAL A CG2   1 
ATOM   13127 N  N     . GLY A 1 3106 ? 168.138 147.339 211.340 1.00 27.82  ? 3106 GLY A N     1 
ATOM   13128 C  CA    . GLY A 1 3106 ? 168.165 145.895 211.490 1.00 29.44  ? 3106 GLY A CA    1 
ATOM   13129 C  C     . GLY A 1 3106 ? 168.190 145.457 212.940 1.00 30.10  ? 3106 GLY A C     1 
ATOM   13130 O  O     . GLY A 1 3106 ? 167.426 144.578 213.343 1.00 34.25  ? 3106 GLY A O     1 
ATOM   13131 N  N     . LYS A 1 3107 ? 169.052 146.077 213.750 1.00 34.52  ? 3107 LYS A N     1 
ATOM   13132 C  CA    . LYS A 1 3107 ? 169.154 145.691 215.155 1.00 33.38  ? 3107 LYS A CA    1 
ATOM   13133 C  C     . LYS A 1 3107 ? 167.862 145.984 215.910 1.00 35.31  ? 3107 LYS A C     1 
ATOM   13134 O  O     . LYS A 1 3107 ? 167.417 145.169 216.727 1.00 41.87  ? 3107 LYS A O     1 
ATOM   13135 C  CB    . LYS A 1 3107 ? 170.333 146.403 215.816 1.00 34.39  ? 3107 LYS A CB    1 
ATOM   13136 C  CG    . LYS A 1 3107 ? 170.472 146.103 217.299 1.00 44.47  ? 3107 LYS A CG    1 
ATOM   13137 C  CD    . LYS A 1 3107 ? 171.737 146.710 217.876 1.00 37.94  ? 3107 LYS A CD    1 
ATOM   13138 C  CE    . LYS A 1 3107 ? 172.955 145.886 217.502 1.00 44.70  ? 3107 LYS A CE    1 
ATOM   13139 N  NZ    . LYS A 1 3107 ? 172.929 144.534 218.125 1.00 49.69  ? 3107 LYS A NZ    1 
ATOM   13140 N  N     . GLU A 1 3108 ? 167.251 147.142 215.654 1.00 33.13  ? 3108 GLU A N     1 
ATOM   13141 C  CA    . GLU A 1 3108 ? 166.004 147.487 216.330 1.00 38.94  ? 3108 GLU A CA    1 
ATOM   13142 C  C     . GLU A 1 3108 ? 164.878 146.535 215.949 1.00 42.34  ? 3108 GLU A C     1 
ATOM   13143 O  O     . GLU A 1 3108 ? 164.119 146.083 216.815 1.00 43.03  ? 3108 GLU A O     1 
ATOM   13144 C  CB    . GLU A 1 3108 ? 165.616 148.930 216.008 1.00 39.34  ? 3108 GLU A CB    1 
ATOM   13145 C  CG    . GLU A 1 3108 ? 164.268 149.350 216.569 1.00 42.57  ? 3108 GLU A CG    1 
ATOM   13146 C  CD    . GLU A 1 3108 ? 164.239 149.356 218.083 1.00 47.95  ? 3108 GLU A CD    1 
ATOM   13147 O  OE1   . GLU A 1 3108 ? 165.290 149.628 218.700 1.00 47.26  ? 3108 GLU A OE1   1 
ATOM   13148 O  OE2   . GLU A 1 3108 ? 163.163 149.086 218.656 1.00 51.64  ? 3108 GLU A OE2   1 
ATOM   13149 N  N     . PHE A 1 3109 ? 164.753 146.215 214.660 1.00 38.79  ? 3109 PHE A N     1 
ATOM   13150 C  CA    . PHE A 1 3109 ? 163.652 145.367 214.219 1.00 39.10  ? 3109 PHE A CA    1 
ATOM   13151 C  C     . PHE A 1 3109 ? 163.891 143.911 214.607 1.00 39.31  ? 3109 PHE A C     1 
ATOM   13152 O  O     . PHE A 1 3109 ? 162.941 143.127 214.713 1.00 47.02  ? 3109 PHE A O     1 
ATOM   13153 C  CB    . PHE A 1 3109 ? 163.459 145.505 212.709 1.00 33.90  ? 3109 PHE A CB    1 
ATOM   13154 C  CG    . PHE A 1 3109 ? 162.117 145.036 212.219 1.00 32.72  ? 3109 PHE A CG    1 
ATOM   13155 C  CD1   . PHE A 1 3109 ? 161.051 145.917 212.144 1.00 31.80  ? 3109 PHE A CD1   1 
ATOM   13156 C  CD2   . PHE A 1 3109 ? 161.916 143.720 211.840 1.00 32.37  ? 3109 PHE A CD2   1 
ATOM   13157 C  CE1   . PHE A 1 3109 ? 159.815 145.497 211.694 1.00 35.45  ? 3109 PHE A CE1   1 
ATOM   13158 C  CE2   . PHE A 1 3109 ? 160.681 143.293 211.390 1.00 37.83  ? 3109 PHE A CE2   1 
ATOM   13159 C  CZ    . PHE A 1 3109 ? 159.629 144.183 211.318 1.00 36.07  ? 3109 PHE A CZ    1 
ATOM   13160 N  N     . THR A 1 3110 ? 165.152 143.533 214.825 1.00 33.96  ? 3110 THR A N     1 
ATOM   13161 C  CA    . THR A 1 3110 ? 165.505 142.174 215.222 1.00 39.67  ? 3110 THR A CA    1 
ATOM   13162 C  C     . THR A 1 3110 ? 165.560 141.994 216.735 1.00 46.09  ? 3110 THR A C     1 
ATOM   13163 O  O     . THR A 1 3110 ? 165.944 140.916 217.200 1.00 48.72  ? 3110 THR A O     1 
ATOM   13164 C  CB    . THR A 1 3110 ? 166.857 141.773 214.623 1.00 39.17  ? 3110 THR A CB    1 
ATOM   13165 O  OG1   . THR A 1 3110 ? 167.732 142.904 214.617 1.00 43.46  ? 3110 THR A OG1   1 
ATOM   13166 C  CG2   . THR A 1 3110 ? 166.683 141.293 213.192 1.00 37.51  ? 3110 THR A CG2   1 
ATOM   13167 N  N     . SER A 1 3111 ? 165.213 143.025 217.510 1.00 46.76  ? 3111 SER A N     1 
ATOM   13168 C  CA    . SER A 1 3111 ? 165.244 142.900 218.964 1.00 47.55  ? 3111 SER A CA    1 
ATOM   13169 C  C     . SER A 1 3111 ? 164.240 141.868 219.461 1.00 51.21  ? 3111 SER A C     1 
ATOM   13170 O  O     . SER A 1 3111 ? 164.540 141.108 220.389 1.00 49.98  ? 3111 SER A O     1 
ATOM   13171 C  CB    . SER A 1 3111 ? 164.985 144.259 219.611 1.00 50.33  ? 3111 SER A CB    1 
ATOM   13172 O  OG    . SER A 1 3111 ? 163.780 144.828 219.133 1.00 48.16  ? 3111 SER A OG    1 
ATOM   13173 N  N     . LYS A 1 3112 ? 163.046 141.827 218.863 1.00 49.83  ? 3112 LYS A N     1 
ATOM   13174 C  CA    . LYS A 1 3112 ? 162.059 140.817 219.233 1.00 52.94  ? 3112 LYS A CA    1 
ATOM   13175 C  C     . LYS A 1 3112 ? 162.547 139.410 218.915 1.00 53.86  ? 3112 LYS A C     1 
ATOM   13176 O  O     . LYS A 1 3112 ? 162.105 138.442 219.545 1.00 50.17  ? 3112 LYS A O     1 
ATOM   13177 C  CB    . LYS A 1 3112 ? 160.739 141.088 218.516 1.00 60.18  ? 3112 LYS A CB    1 
ATOM   13178 C  CG    . LYS A 1 3112 ? 160.894 141.264 217.013 1.00 60.84  ? 3112 LYS A CG    1 
ATOM   13179 C  CD    . LYS A 1 3112 ? 159.553 141.398 216.314 1.00 61.64  ? 3112 LYS A CD    1 
ATOM   13180 C  CE    . LYS A 1 3112 ? 159.735 141.660 214.829 1.00 57.09  ? 3112 LYS A CE    1 
ATOM   13181 N  NZ    . LYS A 1 3112 ? 158.436 141.812 214.121 1.00 50.96  ? 3112 LYS A NZ    1 
ATOM   13182 N  N     . MET A 1 3113 ? 163.438 139.281 217.938 1.00 59.85  ? 3113 MET A N     1 
ATOM   13183 C  CA    . MET A 1 3113 ? 164.039 138.000 217.605 1.00 54.38  ? 3113 MET A CA    1 
ATOM   13184 C  C     . MET A 1 3113 ? 164.933 137.520 218.741 1.00 55.86  ? 3113 MET A C     1 
ATOM   13185 O  O     . MET A 1 3113 ? 165.512 138.317 219.483 1.00 60.13  ? 3113 MET A O     1 
ATOM   13186 C  CB    . MET A 1 3113 ? 164.857 138.135 216.325 1.00 50.71  ? 3113 MET A CB    1 
ATOM   13187 C  CG    . MET A 1 3113 ? 164.032 138.202 215.060 1.00 49.34  ? 3113 MET A CG    1 
ATOM   13188 S  SD    . MET A 1 3113 ? 165.109 138.272 213.621 1.00 48.21  ? 3113 MET A SD    1 
ATOM   13189 C  CE    . MET A 1 3113 ? 164.911 136.630 212.968 1.00 35.49  ? 3113 MET A CE    1 
ATOM   13190 N  N     . ASP A 1 3114 ? 165.030 136.199 218.884 1.00 59.05  ? 3114 ASP A N     1 
ATOM   13191 C  CA    . ASP A 1 3114 ? 165.931 135.621 219.872 1.00 60.54  ? 3114 ASP A CA    1 
ATOM   13192 C  C     . ASP A 1 3114 ? 167.371 135.975 219.527 1.00 62.05  ? 3114 ASP A C     1 
ATOM   13193 O  O     . ASP A 1 3114 ? 168.009 136.755 220.240 1.00 70.03  ? 3114 ASP A O     1 
ATOM   13194 C  CB    . ASP A 1 3114 ? 165.749 134.104 219.942 1.00 64.64  ? 3114 ASP A CB    1 
ATOM   13195 C  CG    . ASP A 1 3114 ? 166.409 133.489 221.160 1.00 69.47  ? 3114 ASP A CG    1 
ATOM   13196 O  OD1   . ASP A 1 3114 ? 166.893 134.248 222.026 1.00 67.06  ? 3114 ASP A OD1   1 
ATOM   13197 O  OD2   . ASP A 1 3114 ? 166.439 132.243 221.252 1.00 72.26  ? 3114 ASP A OD2   1 
ATOM   13198 N  N     . LEU A 1 3115 ? 167.869 135.434 218.412 1.00 57.15  ? 3115 LEU A N     1 
ATOM   13199 C  CA    . LEU A 1 3115 ? 169.206 135.744 217.897 1.00 58.45  ? 3115 LEU A CA    1 
ATOM   13200 C  C     . LEU A 1 3115 ? 170.276 135.638 218.982 1.00 58.63  ? 3115 LEU A C     1 
ATOM   13201 O  O     . LEU A 1 3115 ? 171.244 136.402 218.994 1.00 58.01  ? 3115 LEU A O     1 
ATOM   13202 C  CB    . LEU A 1 3115 ? 169.234 137.130 217.249 1.00 51.41  ? 3115 LEU A CB    1 
ATOM   13203 C  CG    . LEU A 1 3115 ? 168.611 137.247 215.856 1.00 47.10  ? 3115 LEU A CG    1 
ATOM   13204 C  CD1   . LEU A 1 3115 ? 169.008 138.561 215.208 1.00 47.96  ? 3115 LEU A CD1   1 
ATOM   13205 C  CD2   . LEU A 1 3115 ? 169.019 136.072 214.982 1.00 45.67  ? 3115 LEU A CD2   1 
ATOM   13206 N  N     . GLU A 1 3116 ? 170.109 134.696 219.905 1.00 61.11  ? 3116 GLU A N     1 
ATOM   13207 C  CA    . GLU A 1 3116 ? 171.029 134.516 221.020 1.00 67.31  ? 3116 GLU A CA    1 
ATOM   13208 C  C     . GLU A 1 3116 ? 171.732 133.173 220.889 1.00 69.49  ? 3116 GLU A C     1 
ATOM   13209 O  O     . GLU A 1 3116 ? 171.077 132.132 220.771 1.00 70.65  ? 3116 GLU A O     1 
ATOM   13210 C  CB    . GLU A 1 3116 ? 170.298 134.601 222.363 1.00 68.83  ? 3116 GLU A CB    1 
ATOM   13211 C  CG    . GLU A 1 3116 ? 169.784 135.992 222.711 1.00 67.44  ? 3116 GLU A CG    1 
ATOM   13212 C  CD    . GLU A 1 3116 ? 170.897 136.975 223.029 1.00 70.40  ? 3116 GLU A CD    1 
ATOM   13213 O  OE1   . GLU A 1 3116 ? 172.042 136.532 223.264 1.00 63.60  ? 3116 GLU A OE1   1 
ATOM   13214 O  OE2   . GLU A 1 3116 ? 170.627 138.194 223.041 1.00 68.67  ? 3116 GLU A OE2   1 
ATOM   13215 N  N     . LYS A 1 3117 ? 173.064 133.202 220.911 1.00 66.13  ? 3117 LYS A N     1 
ATOM   13216 C  CA    . LYS A 1 3117 ? 173.877 131.991 220.825 1.00 67.13  ? 3117 LYS A CA    1 
ATOM   13217 C  C     . LYS A 1 3117 ? 175.124 132.196 221.671 1.00 67.99  ? 3117 LYS A C     1 
ATOM   13218 O  O     . LYS A 1 3117 ? 176.122 132.763 221.209 1.00 66.80  ? 3117 LYS A O     1 
ATOM   13219 C  CB    . LYS A 1 3117 ? 174.236 131.664 219.375 1.00 62.30  ? 3117 LYS A CB    1 
ATOM   13220 C  CG    . LYS A 1 3117 ? 174.545 130.199 219.125 1.00 59.71  ? 3117 LYS A CG    1 
ATOM   13221 C  CD    . LYS A 1 3117 ? 174.564 129.885 217.638 1.00 58.34  ? 3117 LYS A CD    1 
ATOM   13222 C  CE    . LYS A 1 3117 ? 175.854 129.193 217.236 1.00 55.95  ? 3117 LYS A CE    1 
ATOM   13223 N  NZ    . LYS A 1 3117 ? 176.926 130.170 216.903 1.00 53.38  ? 3117 LYS A NZ    1 
ATOM   13224 N  N     . PRO A 1 3118 ? 175.097 131.757 222.932 1.00 70.26  ? 3118 PRO A N     1 
ATOM   13225 C  CA    . PRO A 1 3118 ? 176.272 131.948 223.799 1.00 67.95  ? 3118 PRO A CA    1 
ATOM   13226 C  C     . PRO A 1 3118 ? 177.517 131.234 223.303 1.00 64.86  ? 3118 PRO A C     1 
ATOM   13227 O  O     . PRO A 1 3118 ? 178.632 131.707 223.556 1.00 57.53  ? 3118 PRO A O     1 
ATOM   13228 C  CB    . PRO A 1 3118 ? 175.802 131.394 225.151 1.00 65.99  ? 3118 PRO A CB    1 
ATOM   13229 C  CG    . PRO A 1 3118 ? 174.706 130.440 224.809 1.00 61.55  ? 3118 PRO A CG    1 
ATOM   13230 C  CD    . PRO A 1 3118 ? 174.017 131.023 223.612 1.00 63.57  ? 3118 PRO A CD    1 
ATOM   13231 N  N     . ASN A 1 3119 ? 177.363 130.108 222.603 1.00 66.50  ? 3119 ASN A N     1 
ATOM   13232 C  CA    . ASN A 1 3119 ? 178.492 129.339 222.094 1.00 65.73  ? 3119 ASN A CA    1 
ATOM   13233 C  C     . ASN A 1 3119 ? 178.996 129.850 220.749 1.00 66.59  ? 3119 ASN A C     1 
ATOM   13234 O  O     . ASN A 1 3119 ? 179.742 129.141 220.060 1.00 65.53  ? 3119 ASN A O     1 
ATOM   13235 C  CB    . ASN A 1 3119 ? 178.117 127.859 221.994 1.00 64.17  ? 3119 ASN A CB    1 
ATOM   13236 C  CG    . ASN A 1 3119 ? 176.999 127.608 221.003 1.00 68.19  ? 3119 ASN A CG    1 
ATOM   13237 O  OD1   . ASN A 1 3119 ? 175.874 128.071 221.190 1.00 68.87  ? 3119 ASN A OD1   1 
ATOM   13238 N  ND2   . ASN A 1 3119 ? 177.303 126.872 219.941 1.00 64.21  ? 3119 ASN A ND2   1 
ATOM   13239 N  N     . TYR A 1 3120 ? 178.606 131.060 220.356 1.00 61.76  ? 3120 TYR A N     1 
ATOM   13240 C  CA    . TYR A 1 3120 ? 179.073 131.642 219.106 1.00 61.49  ? 3120 TYR A CA    1 
ATOM   13241 C  C     . TYR A 1 3120 ? 180.568 131.921 219.190 1.00 58.23  ? 3120 TYR A C     1 
ATOM   13242 O  O     . TYR A 1 3120 ? 181.041 132.540 220.149 1.00 60.17  ? 3120 TYR A O     1 
ATOM   13243 C  CB    . TYR A 1 3120 ? 178.307 132.929 218.801 1.00 60.02  ? 3120 TYR A CB    1 
ATOM   13244 C  CG    . TYR A 1 3120 ? 178.861 133.716 217.635 1.00 52.29  ? 3120 TYR A CG    1 
ATOM   13245 C  CD1   . TYR A 1 3120 ? 178.787 133.222 216.340 1.00 52.81  ? 3120 TYR A CD1   1 
ATOM   13246 C  CD2   . TYR A 1 3120 ? 179.454 134.956 217.830 1.00 48.50  ? 3120 TYR A CD2   1 
ATOM   13247 C  CE1   . TYR A 1 3120 ? 179.291 133.939 215.273 1.00 55.68  ? 3120 TYR A CE1   1 
ATOM   13248 C  CE2   . TYR A 1 3120 ? 179.961 135.680 216.768 1.00 49.69  ? 3120 TYR A CE2   1 
ATOM   13249 C  CZ    . TYR A 1 3120 ? 179.876 135.167 215.492 1.00 54.85  ? 3120 TYR A CZ    1 
ATOM   13250 O  OH    . TYR A 1 3120 ? 180.379 135.885 214.432 1.00 54.51  ? 3120 TYR A OH    1 
ATOM   13251 N  N     . ILE A 1 3121 ? 181.308 131.465 218.185 1.00 55.39  ? 3121 ILE A N     1 
ATOM   13252 C  CA    . ILE A 1 3121 ? 182.754 131.643 218.124 1.00 54.84  ? 3121 ILE A CA    1 
ATOM   13253 C  C     . ILE A 1 3121 ? 183.051 132.739 217.111 1.00 56.11  ? 3121 ILE A C     1 
ATOM   13254 O  O     . ILE A 1 3121 ? 182.705 132.615 215.930 1.00 59.99  ? 3121 ILE A O     1 
ATOM   13255 C  CB    . ILE A 1 3121 ? 183.468 130.334 217.754 1.00 58.77  ? 3121 ILE A CB    1 
ATOM   13256 C  CG1   . ILE A 1 3121 ? 183.533 129.396 218.963 1.00 61.86  ? 3121 ILE A CG1   1 
ATOM   13257 C  CG2   . ILE A 1 3121 ? 184.868 130.616 217.227 1.00 52.52  ? 3121 ILE A CG2   1 
ATOM   13258 C  CD1   . ILE A 1 3121 ? 183.870 130.092 220.266 1.00 58.22  ? 3121 ILE A CD1   1 
ATOM   13259 N  N     . VAL A 1 3122 ? 183.682 133.811 217.570 1.00 54.41  ? 3122 VAL A N     1 
ATOM   13260 C  CA    . VAL A 1 3122 ? 184.026 134.918 216.672 1.00 58.77  ? 3122 VAL A CA    1 
ATOM   13261 C  C     . VAL A 1 3122 ? 185.133 134.469 215.725 1.00 62.23  ? 3122 VAL A C     1 
ATOM   13262 O  O     . VAL A 1 3122 ? 186.173 133.967 216.187 1.00 61.99  ? 3122 VAL A O     1 
ATOM   13263 C  CB    . VAL A 1 3122 ? 184.455 136.144 217.479 1.00 60.40  ? 3122 VAL A CB    1 
ATOM   13264 C  CG1   . VAL A 1 3122 ? 184.950 137.244 216.550 1.00 53.41  ? 3122 VAL A CG1   1 
ATOM   13265 C  CG2   . VAL A 1 3122 ? 183.303 136.643 218.336 1.00 61.57  ? 3122 VAL A CG2   1 
ATOM   13266 N  N     . PRO A 1 3123 ? 184.952 134.574 214.386 1.00 63.18  ? 3123 PRO A N     1 
ATOM   13267 C  CA    . PRO A 1 3123 ? 185.954 134.082 213.450 1.00 66.22  ? 3123 PRO A CA    1 
ATOM   13268 C  C     . PRO A 1 3123 ? 187.238 134.895 213.509 1.00 73.65  ? 3123 PRO A C     1 
ATOM   13269 O  O     . PRO A 1 3123 ? 187.206 136.051 213.977 1.00 75.92  ? 3123 PRO A O     1 
ATOM   13270 C  CB    . PRO A 1 3123 ? 185.251 134.208 212.089 1.00 62.45  ? 3123 PRO A CB    1 
ATOM   13271 C  CG    . PRO A 1 3123 ? 184.283 135.349 212.287 1.00 62.57  ? 3123 PRO A CG    1 
ATOM   13272 C  CD    . PRO A 1 3123 ? 183.793 135.158 213.712 1.00 60.37  ? 3123 PRO A CD    1 
ATOM   13273 N  N     . ASP A 1 3124 ? 188.344 134.312 213.036 1.00 78.61  ? 3124 ASP A N     1 
ATOM   13274 C  CA    . ASP A 1 3124 ? 189.639 135.044 213.010 1.00 85.88  ? 3124 ASP A CA    1 
ATOM   13275 C  C     . ASP A 1 3124 ? 189.422 136.356 212.253 1.00 85.45  ? 3124 ASP A C     1 
ATOM   13276 O  O     . ASP A 1 3124 ? 189.821 137.416 212.780 1.00 86.62  ? 3124 ASP A O     1 
ATOM   13277 C  CB    . ASP A 1 3124 ? 190.746 134.194 212.407 1.00 92.02  ? 3124 ASP A CB    1 
ATOM   13278 C  CG    . ASP A 1 3124 ? 190.923 132.818 213.032 1.00 99.95  ? 3124 ASP A CG    1 
ATOM   13279 O  OD1   . ASP A 1 3124 ? 191.197 132.759 214.249 1.00 99.15  ? 3124 ASP A OD1   1 
ATOM   13280 O  OD2   . ASP A 1 3124 ? 190.781 131.818 212.297 1.00 100.99 ? 3124 ASP A OD2   1 
ATOM   13281 N  N     . TYR A 1 3125 ? 188.802 136.285 211.072 1.00 79.70  ? 3125 TYR A N     1 
ATOM   13282 C  CA    . TYR A 1 3125 ? 188.465 137.526 210.322 1.00 83.09  ? 3125 TYR A CA    1 
ATOM   13283 C  C     . TYR A 1 3125 ? 186.946 137.631 210.231 1.00 83.44  ? 3125 TYR A C     1 
ATOM   13284 O  O     . TYR A 1 3125 ? 186.292 136.665 209.780 1.00 76.84  ? 3125 TYR A O     1 
ATOM   13285 C  CB    . TYR A 1 3125 ? 189.059 137.577 208.911 1.00 81.85  ? 3125 TYR A CB    1 
ATOM   13286 C  CG    . TYR A 1 3125 ? 188.294 138.519 207.990 1.00 87.25  ? 3125 TYR A CG    1 
ATOM   13287 C  CD1   . TYR A 1 3125 ? 188.599 139.874 207.936 1.00 86.61  ? 3125 TYR A CD1   1 
ATOM   13288 C  CD2   . TYR A 1 3125 ? 187.258 138.056 207.188 1.00 90.68  ? 3125 TYR A CD2   1 
ATOM   13289 C  CE1   . TYR A 1 3125 ? 187.900 140.737 207.108 1.00 90.81  ? 3125 TYR A CE1   1 
ATOM   13290 C  CE2   . TYR A 1 3125 ? 186.552 138.909 206.357 1.00 93.38  ? 3125 TYR A CE2   1 
ATOM   13291 C  CZ    . TYR A 1 3125 ? 186.875 140.253 206.316 1.00 93.18  ? 3125 TYR A CZ    1 
ATOM   13292 O  OH    . TYR A 1 3125 ? 186.183 141.097 205.496 1.00 92.04  ? 3125 TYR A OH    1 
ATOM   13293 N  N     . MET A 1 3126 ? 186.395 138.772 210.648 1.00 83.34  ? 3126 MET A N     1 
ATOM   13294 C  CA    . MET A 1 3126 ? 184.930 138.985 210.537 1.00 76.86  ? 3126 MET A CA    1 
ATOM   13295 C  C     . MET A 1 3126 ? 184.651 139.790 209.262 1.00 71.21  ? 3126 MET A C     1 
ATOM   13296 O  O     . MET A 1 3126 ? 185.299 140.843 209.074 1.00 72.86  ? 3126 MET A O     1 
ATOM   13297 C  CB    . MET A 1 3126 ? 184.386 139.750 211.748 1.00 75.04  ? 3126 MET A CB    1 
ATOM   13298 C  CG    . MET A 1 3126 ? 182.911 140.087 211.645 1.00 73.82  ? 3126 MET A CG    1 
ATOM   13299 S  SD    . MET A 1 3126 ? 181.845 138.634 211.722 1.00 76.25  ? 3126 MET A SD    1 
ATOM   13300 C  CE    . MET A 1 3126 ? 182.178 138.113 213.409 1.00 57.57  ? 3126 MET A CE    1 
ATOM   13301 N  N     . PRO A 1 3127 ? 183.731 139.347 208.378 1.00 68.41  ? 3127 PRO A N     1 
ATOM   13302 C  CA    . PRO A 1 3127 ? 183.383 140.130 207.203 1.00 62.87  ? 3127 PRO A CA    1 
ATOM   13303 C  C     . PRO A 1 3127 ? 182.558 141.313 207.676 1.00 65.69  ? 3127 PRO A C     1 
ATOM   13304 O  O     . PRO A 1 3127 ? 181.365 141.411 207.323 1.00 62.74  ? 3127 PRO A O     1 
ATOM   13305 C  CB    . PRO A 1 3127 ? 182.586 139.143 206.348 1.00 54.70  ? 3127 PRO A CB    1 
ATOM   13306 C  CG    . PRO A 1 3127 ? 181.992 138.185 207.355 1.00 57.86  ? 3127 PRO A CG    1 
ATOM   13307 C  CD    . PRO A 1 3127 ? 183.016 138.086 208.474 1.00 65.61  ? 3127 PRO A CD    1 
ATOM   13308 N  N     . VAL A 1 3128 ? 183.178 142.196 208.466 1.00 67.59  ? 3128 VAL A N     1 
ATOM   13309 C  CA    . VAL A 1 3128 ? 182.453 143.374 209.029 1.00 66.87  ? 3128 VAL A CA    1 
ATOM   13310 C  C     . VAL A 1 3128 ? 182.018 144.295 207.880 1.00 63.60  ? 3128 VAL A C     1 
ATOM   13311 O  O     . VAL A 1 3128 ? 182.810 144.467 206.928 1.00 60.28  ? 3128 VAL A O     1 
ATOM   13312 C  CB    . VAL A 1 3128 ? 183.327 144.138 210.041 1.00 71.04  ? 3128 VAL A CB    1 
ATOM   13313 C  CG1   . VAL A 1 3128 ? 182.581 145.316 210.654 1.00 67.82  ? 3128 VAL A CG1   1 
ATOM   13314 C  CG2   . VAL A 1 3128 ? 183.869 143.223 211.131 1.00 67.47  ? 3128 VAL A CG2   1 
ATOM   13315 N  N     . VAL A 1 3129 ? 180.811 144.859 207.973 1.00 57.22  ? 3129 VAL A N     1 
ATOM   13316 C  CA    . VAL A 1 3129 ? 180.317 145.815 206.938 1.00 49.25  ? 3129 VAL A CA    1 
ATOM   13317 C  C     . VAL A 1 3129 ? 180.077 147.160 207.634 1.00 47.22  ? 3129 VAL A C     1 
ATOM   13318 O  O     . VAL A 1 3129 ? 180.167 148.206 206.956 1.00 45.54  ? 3129 VAL A O     1 
ATOM   13319 C  CB    . VAL A 1 3129 ? 179.032 145.274 206.286 1.00 46.92  ? 3129 VAL A CB    1 
ATOM   13320 C  CG1   . VAL A 1 3129 ? 178.506 146.201 205.197 1.00 37.51  ? 3129 VAL A CG1   1 
ATOM   13321 C  CG2   . VAL A 1 3129 ? 179.231 143.864 205.745 1.00 44.29  ? 3129 VAL A CG2   1 
ATOM   13322 N  N     . TYR A 1 3130 ? 179.798 147.125 208.940 1.00 49.60  ? 3130 TYR A N     1 
ATOM   13323 C  CA    . TYR A 1 3130 ? 179.552 148.343 209.698 1.00 50.67  ? 3130 TYR A CA    1 
ATOM   13324 C  C     . TYR A 1 3130 ? 180.836 148.744 210.415 1.00 59.67  ? 3130 TYR A C     1 
ATOM   13325 O  O     . TYR A 1 3130 ? 181.370 147.972 211.218 1.00 63.40  ? 3130 TYR A O     1 
ATOM   13326 C  CB    . TYR A 1 3130 ? 178.413 148.120 210.690 1.00 46.63  ? 3130 TYR A CB    1 
ATOM   13327 C  CG    . TYR A 1 3130 ? 178.084 149.314 211.554 1.00 47.54  ? 3130 TYR A CG    1 
ATOM   13328 C  CD1   . TYR A 1 3130 ? 178.141 150.605 211.046 1.00 46.79  ? 3130 TYR A CD1   1 
ATOM   13329 C  CD2   . TYR A 1 3130 ? 177.704 149.148 212.878 1.00 46.18  ? 3130 TYR A CD2   1 
ATOM   13330 C  CE1   . TYR A 1 3130 ? 177.838 151.695 211.836 1.00 47.99  ? 3130 TYR A CE1   1 
ATOM   13331 C  CE2   . TYR A 1 3130 ? 177.397 150.232 213.674 1.00 42.23  ? 3130 TYR A CE2   1 
ATOM   13332 C  CZ    . TYR A 1 3130 ? 177.465 151.502 213.149 1.00 45.90  ? 3130 TYR A CZ    1 
ATOM   13333 O  OH    . TYR A 1 3130 ? 177.159 152.582 213.942 1.00 51.86  ? 3130 TYR A OH    1 
ATOM   13334 N  N     . ASP A 1 3131 ? 181.331 149.949 210.122 1.00 61.05  ? 3131 ASP A N     1 
ATOM   13335 C  CA    . ASP A 1 3131 ? 182.629 150.365 210.645 1.00 61.62  ? 3131 ASP A CA    1 
ATOM   13336 C  C     . ASP A 1 3131 ? 182.625 150.435 212.167 1.00 64.32  ? 3131 ASP A C     1 
ATOM   13337 O  O     . ASP A 1 3131 ? 183.592 150.022 212.817 1.00 65.88  ? 3131 ASP A O     1 
ATOM   13338 C  CB    . ASP A 1 3131 ? 183.028 151.714 210.047 1.00 63.65  ? 3131 ASP A CB    1 
ATOM   13339 C  CG    . ASP A 1 3131 ? 183.022 151.703 208.532 1.00 74.20  ? 3131 ASP A CG    1 
ATOM   13340 O  OD1   . ASP A 1 3131 ? 183.011 150.601 207.944 1.00 75.76  ? 3131 ASP A OD1   1 
ATOM   13341 O  OD2   . ASP A 1 3131 ? 183.028 152.797 207.928 1.00 81.12  ? 3131 ASP A OD2   1 
ATOM   13342 N  N     . LYS A 1 3132 ? 181.546 150.950 212.755 1.00 59.10  ? 3132 LYS A N     1 
ATOM   13343 C  CA    . LYS A 1 3132 ? 181.444 151.093 214.200 1.00 54.31  ? 3132 LYS A CA    1 
ATOM   13344 C  C     . LYS A 1 3132 ? 180.942 149.827 214.884 1.00 57.06  ? 3132 LYS A C     1 
ATOM   13345 O  O     . LYS A 1 3132 ? 180.465 149.897 216.022 1.00 62.38  ? 3132 LYS A O     1 
ATOM   13346 C  CB    . LYS A 1 3132 ? 180.542 152.277 214.552 1.00 54.37  ? 3132 LYS A CB    1 
ATOM   13347 C  CG    . LYS A 1 3132 ? 181.279 153.603 214.639 1.00 55.35  ? 3132 LYS A CG    1 
ATOM   13348 C  CD    . LYS A 1 3132 ? 180.315 154.775 214.658 1.00 53.89  ? 3132 LYS A CD    1 
ATOM   13349 C  CE    . LYS A 1 3132 ? 179.446 154.794 213.414 1.00 54.14  ? 3132 LYS A CE    1 
ATOM   13350 N  NZ    . LYS A 1 3132 ? 178.235 155.638 213.601 1.00 48.36  ? 3132 LYS A NZ    1 
ATOM   13351 N  N     . LEU A 1 3133 ? 181.032 148.681 214.219 1.00 55.02  ? 3133 LEU A N     1 
ATOM   13352 C  CA    . LEU A 1 3133 ? 180.682 147.428 214.868 1.00 61.33  ? 3133 LEU A CA    1 
ATOM   13353 C  C     . LEU A 1 3133 ? 181.684 147.131 215.981 1.00 64.85  ? 3133 LEU A C     1 
ATOM   13354 O  O     . LEU A 1 3133 ? 182.897 147.260 215.775 1.00 67.10  ? 3133 LEU A O     1 
ATOM   13355 C  CB    . LEU A 1 3133 ? 180.660 146.283 213.855 1.00 58.74  ? 3133 LEU A CB    1 
ATOM   13356 C  CG    . LEU A 1 3133 ? 180.182 144.920 214.360 1.00 54.08  ? 3133 LEU A CG    1 
ATOM   13357 C  CD1   . LEU A 1 3133 ? 178.676 144.921 214.558 1.00 46.06  ? 3133 LEU A CD1   1 
ATOM   13358 C  CD2   . LEU A 1 3133 ? 180.596 143.816 213.401 1.00 56.90  ? 3133 LEU A CD2   1 
ATOM   13359 N  N     . PRO A 1 3134 ? 181.217 146.754 217.171 1.00 64.46  ? 3134 PRO A N     1 
ATOM   13360 C  CA    . PRO A 1 3134 ? 182.144 146.458 218.271 1.00 68.84  ? 3134 PRO A CA    1 
ATOM   13361 C  C     . PRO A 1 3134 ? 183.113 145.341 217.910 1.00 70.48  ? 3134 PRO A C     1 
ATOM   13362 O  O     . PRO A 1 3134 ? 182.765 144.391 217.206 1.00 69.70  ? 3134 PRO A O     1 
ATOM   13363 C  CB    . PRO A 1 3134 ? 181.211 146.051 219.415 1.00 64.77  ? 3134 PRO A CB    1 
ATOM   13364 C  CG    . PRO A 1 3134 ? 179.937 146.770 219.119 1.00 63.75  ? 3134 PRO A CG    1 
ATOM   13365 C  CD    . PRO A 1 3134 ? 179.816 146.787 217.620 1.00 59.05  ? 3134 PRO A CD    1 
ATOM   13366 N  N     . GLN A 1 3135 ? 184.345 145.477 218.401 1.00 75.73  ? 3135 GLN A N     1 
ATOM   13367 C  CA    . GLN A 1 3135 ? 185.399 144.532 218.044 1.00 76.13  ? 3135 GLN A CA    1 
ATOM   13368 C  C     . GLN A 1 3135 ? 185.091 143.085 218.421 1.00 77.64  ? 3135 GLN A C     1 
ATOM   13369 O  O     . GLN A 1 3135 ? 185.430 142.195 217.623 1.00 78.00  ? 3135 GLN A O     1 
ATOM   13370 C  CB    . GLN A 1 3135 ? 186.729 144.986 218.664 1.00 80.28  ? 3135 GLN A CB    1 
ATOM   13371 C  CG    . GLN A 1 3135 ? 187.024 146.469 218.487 1.00 83.42  ? 3135 GLN A CG    1 
ATOM   13372 C  CD    . GLN A 1 3135 ? 186.833 146.938 217.057 1.00 84.37  ? 3135 GLN A CD    1 
ATOM   13373 O  OE1   . GLN A 1 3135 ? 187.370 146.348 216.120 1.00 78.88  ? 3135 GLN A OE1   1 
ATOM   13374 N  NE2   . GLN A 1 3135 ? 186.062 148.006 216.884 1.00 78.13  ? 3135 GLN A NE2   1 
ATOM   13375 N  N     . PRO A 1 3136 ? 184.558 142.768 219.602 1.00 74.61  ? 3136 PRO A N     1 
ATOM   13376 C  CA    . PRO A 1 3136 ? 184.074 141.403 219.858 1.00 73.95  ? 3136 PRO A CA    1 
ATOM   13377 C  C     . PRO A 1 3136 ? 182.593 141.267 219.547 1.00 72.71  ? 3136 PRO A C     1 
ATOM   13378 O  O     . PRO A 1 3136 ? 181.760 141.335 220.464 1.00 72.17  ? 3136 PRO A O     1 
ATOM   13379 C  CB    . PRO A 1 3136 ? 184.349 141.210 221.356 1.00 74.02  ? 3136 PRO A CB    1 
ATOM   13380 C  CG    . PRO A 1 3136 ? 184.335 142.597 221.935 1.00 75.48  ? 3136 PRO A CG    1 
ATOM   13381 C  CD    . PRO A 1 3136 ? 184.444 143.604 220.812 1.00 71.85  ? 3136 PRO A CD    1 
ATOM   13382 N  N     . PRO A 1 3137 ? 182.212 141.084 218.282 1.00 68.86  ? 3137 PRO A N     1 
ATOM   13383 C  CA    . PRO A 1 3137 ? 180.782 141.034 217.958 1.00 63.13  ? 3137 PRO A CA    1 
ATOM   13384 C  C     . PRO A 1 3137 ? 180.129 139.785 218.530 1.00 55.63  ? 3137 PRO A C     1 
ATOM   13385 O  O     . PRO A 1 3137 ? 180.748 138.722 218.619 1.00 58.12  ? 3137 PRO A O     1 
ATOM   13386 C  CB    . PRO A 1 3137 ? 180.770 141.021 216.427 1.00 59.41  ? 3137 PRO A CB    1 
ATOM   13387 C  CG    . PRO A 1 3137 ? 182.024 140.309 216.069 1.00 63.00  ? 3137 PRO A CG    1 
ATOM   13388 C  CD    . PRO A 1 3137 ? 183.033 140.586 217.163 1.00 65.56  ? 3137 PRO A CD    1 
ATOM   13389 N  N     . SER A 1 3138 ? 178.865 139.923 218.922 1.00 46.96  ? 3138 SER A N     1 
ATOM   13390 C  CA    . SER A 1 3138 ? 178.091 138.790 219.401 1.00 45.49  ? 3138 SER A CA    1 
ATOM   13391 C  C     . SER A 1 3138 ? 177.317 138.168 218.241 1.00 48.94  ? 3138 SER A C     1 
ATOM   13392 O  O     . SER A 1 3138 ? 177.424 138.595 217.089 1.00 49.64  ? 3138 SER A O     1 
ATOM   13393 C  CB    . SER A 1 3138 ? 177.155 139.216 220.531 1.00 46.94  ? 3138 SER A CB    1 
ATOM   13394 O  OG    . SER A 1 3138 ? 176.181 140.135 220.074 1.00 39.36  ? 3138 SER A OG    1 
ATOM   13395 N  N     . HIS A 1 3139 ? 176.532 137.132 218.546 1.00 47.23  ? 3139 HIS A N     1 
ATOM   13396 C  CA    . HIS A 1 3139 ? 175.755 136.468 217.505 1.00 46.88  ? 3139 HIS A CA    1 
ATOM   13397 C  C     . HIS A 1 3139 ? 174.724 137.410 216.896 1.00 48.88  ? 3139 HIS A C     1 
ATOM   13398 O  O     . HIS A 1 3139 ? 174.553 137.446 215.672 1.00 47.06  ? 3139 HIS A O     1 
ATOM   13399 C  CB    . HIS A 1 3139 ? 175.074 135.221 218.067 1.00 50.35  ? 3139 HIS A CB    1 
ATOM   13400 C  CG    . HIS A 1 3139 ? 174.421 134.369 217.023 1.00 51.65  ? 3139 HIS A CG    1 
ATOM   13401 N  ND1   . HIS A 1 3139 ? 175.105 133.869 215.937 1.00 49.65  ? 3139 HIS A ND1   1 
ATOM   13402 C  CD2   . HIS A 1 3139 ? 173.145 133.933 216.898 1.00 49.57  ? 3139 HIS A CD2   1 
ATOM   13403 C  CE1   . HIS A 1 3139 ? 174.281 133.159 215.188 1.00 48.73  ? 3139 HIS A CE1   1 
ATOM   13404 N  NE2   . HIS A 1 3139 ? 173.085 133.182 215.749 1.00 54.31  ? 3139 HIS A NE2   1 
ATOM   13405 N  N     . ARG A 1 3140 ? 174.027 138.182 217.734 1.00 46.51  ? 3140 ARG A N     1 
ATOM   13406 C  CA    . ARG A 1 3140 ? 173.049 139.137 217.221 1.00 41.60  ? 3140 ARG A CA    1 
ATOM   13407 C  C     . ARG A 1 3140 ? 173.715 140.198 216.355 1.00 39.88  ? 3140 ARG A C     1 
ATOM   13408 O  O     . ARG A 1 3140 ? 173.196 140.559 215.293 1.00 41.01  ? 3140 ARG A O     1 
ATOM   13409 C  CB    . ARG A 1 3140 ? 172.297 139.794 218.378 1.00 39.57  ? 3140 ARG A CB    1 
ATOM   13410 C  CG    . ARG A 1 3140 ? 171.057 140.561 217.949 1.00 44.80  ? 3140 ARG A CG    1 
ATOM   13411 C  CD    . ARG A 1 3140 ? 170.400 141.259 219.127 1.00 37.07  ? 3140 ARG A CD    1 
ATOM   13412 N  NE    . ARG A 1 3140 ? 169.851 140.316 220.092 1.00 51.22  ? 3140 ARG A NE    1 
ATOM   13413 C  CZ    . ARG A 1 3140 ? 168.662 139.740 219.984 1.00 55.77  ? 3140 ARG A CZ    1 
ATOM   13414 N  NH1   . ARG A 1 3140 ? 167.868 139.983 218.953 1.00 50.78  ? 3140 ARG A NH1   1 
ATOM   13415 N  NH2   . ARG A 1 3140 ? 168.257 138.903 220.934 1.00 59.47  ? 3140 ARG A NH2   1 
ATOM   13416 N  N     . GLU A 1 3141 ? 174.864 140.711 216.797 1.00 37.17  ? 3141 GLU A N     1 
ATOM   13417 C  CA    . GLU A 1 3141 ? 175.564 141.739 216.035 1.00 38.28  ? 3141 GLU A CA    1 
ATOM   13418 C  C     . GLU A 1 3141 ? 176.049 141.204 214.694 1.00 37.22  ? 3141 GLU A C     1 
ATOM   13419 O  O     . GLU A 1 3141 ? 175.970 141.899 213.674 1.00 34.57  ? 3141 GLU A O     1 
ATOM   13420 C  CB    . GLU A 1 3141 ? 176.733 142.282 216.853 1.00 43.87  ? 3141 GLU A CB    1 
ATOM   13421 C  CG    . GLU A 1 3141 ? 176.348 142.681 218.265 1.00 50.83  ? 3141 GLU A CG    1 
ATOM   13422 C  CD    . GLU A 1 3141 ? 177.225 143.780 218.810 1.00 58.70  ? 3141 GLU A CD    1 
ATOM   13423 O  OE1   . GLU A 1 3141 ? 177.993 144.359 218.018 1.00 62.43  ? 3141 GLU A OE1   1 
ATOM   13424 O  OE2   . GLU A 1 3141 ? 177.151 144.063 220.024 1.00 65.69  ? 3141 GLU A OE2   1 
ATOM   13425 N  N     . ALA A 1 3142 ? 176.561 139.971 214.676 1.00 40.68  ? 3142 ALA A N     1 
ATOM   13426 C  CA    . ALA A 1 3142 ? 177.023 139.382 213.424 1.00 36.55  ? 3142 ALA A CA    1 
ATOM   13427 C  C     . ALA A 1 3142 ? 175.865 139.156 212.460 1.00 32.97  ? 3142 ALA A C     1 
ATOM   13428 O  O     . ALA A 1 3142 ? 176.029 139.279 211.241 1.00 29.94  ? 3142 ALA A O     1 
ATOM   13429 C  CB    . ALA A 1 3142 ? 177.759 138.072 213.699 1.00 42.57  ? 3142 ALA A CB    1 
ATOM   13430 N  N     . ILE A 1 3143 ? 174.687 138.815 212.988 1.00 36.25  ? 3143 ILE A N     1 
ATOM   13431 C  CA    . ILE A 1 3143 ? 173.519 138.615 212.133 1.00 30.49  ? 3143 ILE A CA    1 
ATOM   13432 C  C     . ILE A 1 3143 ? 173.116 139.927 211.471 1.00 28.92  ? 3143 ILE A C     1 
ATOM   13433 O  O     . ILE A 1 3143 ? 172.905 139.989 210.254 1.00 30.56  ? 3143 ILE A O     1 
ATOM   13434 C  CB    . ILE A 1 3143 ? 172.357 138.011 212.941 1.00 30.95  ? 3143 ILE A CB    1 
ATOM   13435 C  CG1   . ILE A 1 3143 ? 172.643 136.546 213.278 1.00 31.63  ? 3143 ILE A CG1   1 
ATOM   13436 C  CG2   . ILE A 1 3143 ? 171.053 138.144 212.175 1.00 29.80  ? 3143 ILE A CG2   1 
ATOM   13437 C  CD1   . ILE A 1 3143 ? 172.533 135.613 212.096 1.00 36.32  ? 3143 ILE A CD1   1 
ATOM   13438 N  N     . VAL A 1 3144 ? 173.015 140.998 212.262 1.00 25.86  ? 3144 VAL A N     1 
ATOM   13439 C  CA    . VAL A 1 3144 ? 172.637 142.295 211.709 1.00 22.94  ? 3144 VAL A CA    1 
ATOM   13440 C  C     . VAL A 1 3144 ? 173.697 142.788 210.734 1.00 25.89  ? 3144 VAL A C     1 
ATOM   13441 O  O     . VAL A 1 3144 ? 173.378 143.386 209.700 1.00 27.03  ? 3144 VAL A O     1 
ATOM   13442 C  CB    . VAL A 1 3144 ? 172.388 143.309 212.841 1.00 25.10  ? 3144 VAL A CB    1 
ATOM   13443 C  CG1   . VAL A 1 3144 ? 171.926 144.639 212.271 1.00 25.96  ? 3144 VAL A CG1   1 
ATOM   13444 C  CG2   . VAL A 1 3144 ? 171.361 142.769 213.820 1.00 28.28  ? 3144 VAL A CG2   1 
ATOM   13445 N  N     . ASN A 1 3145 ? 174.973 142.541 211.042 1.00 27.85  ? 3145 ASN A N     1 
ATOM   13446 C  CA    . ASN A 1 3145 ? 176.040 142.897 210.114 1.00 25.32  ? 3145 ASN A CA    1 
ATOM   13447 C  C     . ASN A 1 3145 ? 175.885 142.156 208.793 1.00 27.91  ? 3145 ASN A C     1 
ATOM   13448 O  O     . ASN A 1 3145 ? 176.099 142.731 207.719 1.00 29.78  ? 3145 ASN A O     1 
ATOM   13449 C  CB    . ASN A 1 3145 ? 177.402 142.601 210.743 1.00 27.12  ? 3145 ASN A CB    1 
ATOM   13450 C  CG    . ASN A 1 3145 ? 178.548 143.229 209.977 1.00 41.73  ? 3145 ASN A CG    1 
ATOM   13451 O  OD1   . ASN A 1 3145 ? 178.646 144.451 209.874 1.00 46.50  ? 3145 ASN A OD1   1 
ATOM   13452 N  ND2   . ASN A 1 3145 ? 179.424 142.393 209.435 1.00 41.60  ? 3145 ASN A ND2   1 
ATOM   13453 N  N     . SER A 1 3146 ? 175.517 140.875 208.854 1.00 28.32  ? 3146 SER A N     1 
ATOM   13454 C  CA    . SER A 1 3146 ? 175.269 140.116 207.634 1.00 26.17  ? 3146 SER A CA    1 
ATOM   13455 C  C     . SER A 1 3146 ? 174.055 140.654 206.886 1.00 25.35  ? 3146 SER A C     1 
ATOM   13456 O  O     . SER A 1 3146 ? 174.039 140.674 205.649 1.00 24.90  ? 3146 SER A O     1 
ATOM   13457 C  CB    . SER A 1 3146 ? 175.085 138.636 207.969 1.00 31.00  ? 3146 SER A CB    1 
ATOM   13458 O  OG    . SER A 1 3146 ? 176.219 138.121 208.643 1.00 35.32  ? 3146 SER A OG    1 
ATOM   13459 N  N     . CYS A 1 3147 ? 173.024 141.087 207.618 1.00 26.94  ? 3147 CYS A N     1 
ATOM   13460 C  CA    . CYS A 1 3147 ? 171.843 141.653 206.971 1.00 16.75  ? 3147 CYS A CA    1 
ATOM   13461 C  C     . CYS A 1 3147 ? 172.187 142.924 206.207 1.00 16.54  ? 3147 CYS A C     1 
ATOM   13462 O  O     . CYS A 1 3147 ? 171.688 143.142 205.096 1.00 21.49  ? 3147 CYS A O     1 
ATOM   13463 C  CB    . CYS A 1 3147 ? 170.750 141.930 208.004 1.00 15.41  ? 3147 CYS A CB    1 
ATOM   13464 S  SG    . CYS A 1 3147 ? 170.154 140.475 208.888 1.00 21.80  ? 3147 CYS A SG    1 
ATOM   13465 N  N     . VAL A 1 3148 ? 173.030 143.780 206.788 1.00 18.07  ? 3148 VAL A N     1 
ATOM   13466 C  CA    . VAL A 1 3148 ? 173.485 144.969 206.073 1.00 18.16  ? 3148 VAL A CA    1 
ATOM   13467 C  C     . VAL A 1 3148 ? 174.278 144.573 204.835 1.00 18.29  ? 3148 VAL A C     1 
ATOM   13468 O  O     . VAL A 1 3148 ? 174.121 145.169 203.763 1.00 18.35  ? 3148 VAL A O     1 
ATOM   13469 C  CB    . VAL A 1 3148 ? 174.307 145.879 207.004 1.00 20.02  ? 3148 VAL A CB    1 
ATOM   13470 C  CG1   . VAL A 1 3148 ? 174.718 147.144 206.274 1.00 23.43  ? 3148 VAL A CG1   1 
ATOM   13471 C  CG2   . VAL A 1 3148 ? 173.508 146.225 208.247 1.00 22.35  ? 3148 VAL A CG2   1 
ATOM   13472 N  N     . PHE A 1 3149 ? 175.133 143.556 204.962 1.00 22.84  ? 3149 PHE A N     1 
ATOM   13473 C  CA    . PHE A 1 3149 ? 175.953 143.120 203.835 1.00 21.28  ? 3149 PHE A CA    1 
ATOM   13474 C  C     . PHE A 1 3149 ? 175.087 142.659 202.670 1.00 19.67  ? 3149 PHE A C     1 
ATOM   13475 O  O     . PHE A 1 3149 ? 175.442 142.863 201.503 1.00 19.67  ? 3149 PHE A O     1 
ATOM   13476 C  CB    . PHE A 1 3149 ? 176.891 141.999 204.279 1.00 24.39  ? 3149 PHE A CB    1 
ATOM   13477 C  CG    . PHE A 1 3149 ? 177.663 141.370 203.155 1.00 25.08  ? 3149 PHE A CG    1 
ATOM   13478 C  CD1   . PHE A 1 3149 ? 178.797 141.985 202.652 1.00 25.62  ? 3149 PHE A CD1   1 
ATOM   13479 C  CD2   . PHE A 1 3149 ? 177.253 140.173 202.595 1.00 23.74  ? 3149 PHE A CD2   1 
ATOM   13480 C  CE1   . PHE A 1 3149 ? 179.512 141.415 201.619 1.00 24.73  ? 3149 PHE A CE1   1 
ATOM   13481 C  CE2   . PHE A 1 3149 ? 177.963 139.599 201.559 1.00 21.51  ? 3149 PHE A CE2   1 
ATOM   13482 C  CZ    . PHE A 1 3149 ? 179.098 140.216 201.077 1.00 22.24  ? 3149 PHE A CZ    1 
ATOM   13483 N  N     . VAL A 1 3150 ? 173.949 142.030 202.969 1.00 18.68  ? 3150 VAL A N     1 
ATOM   13484 C  CA    . VAL A 1 3150 ? 173.048 141.571 201.915 1.00 15.83  ? 3150 VAL A CA    1 
ATOM   13485 C  C     . VAL A 1 3150 ? 172.517 142.759 201.121 1.00 18.41  ? 3150 VAL A C     1 
ATOM   13486 O  O     . VAL A 1 3150 ? 172.411 142.712 199.890 1.00 22.86  ? 3150 VAL A O     1 
ATOM   13487 C  CB    . VAL A 1 3150 ? 171.906 140.732 202.516 1.00 14.73  ? 3150 VAL A CB    1 
ATOM   13488 C  CG1   . VAL A 1 3150 ? 170.814 140.496 201.489 1.00 12.47  ? 3150 VAL A CG1   1 
ATOM   13489 C  CG2   . VAL A 1 3150 ? 172.440 139.411 203.043 1.00 20.58  ? 3150 VAL A CG2   1 
ATOM   13490 N  N     . HIS A 1 3151 ? 172.185 143.849 201.817 1.00 16.63  ? 3151 HIS A N     1 
ATOM   13491 C  CA    . HIS A 1 3151 ? 171.693 145.044 201.139 1.00 12.64  ? 3151 HIS A CA    1 
ATOM   13492 C  C     . HIS A 1 3151 ? 172.761 145.644 200.232 1.00 17.76  ? 3151 HIS A C     1 
ATOM   13493 O  O     . HIS A 1 3151 ? 172.472 146.063 199.106 1.00 19.73  ? 3151 HIS A O     1 
ATOM   13494 C  CB    . HIS A 1 3151 ? 171.220 146.071 202.168 1.00 14.22  ? 3151 HIS A CB    1 
ATOM   13495 C  CG    . HIS A 1 3151 ? 170.320 147.123 201.600 1.00 12.29  ? 3151 HIS A CG    1 
ATOM   13496 N  ND1   . HIS A 1 3151 ? 169.017 146.870 201.230 1.00 14.29  ? 3151 HIS A ND1   1 
ATOM   13497 C  CD2   . HIS A 1 3151 ? 170.538 148.433 201.334 1.00 11.20  ? 3151 HIS A CD2   1 
ATOM   13498 C  CE1   . HIS A 1 3151 ? 168.471 147.978 200.763 1.00 14.66  ? 3151 HIS A CE1   1 
ATOM   13499 N  NE2   . HIS A 1 3151 ? 169.372 148.941 200.816 1.00 14.14  ? 3151 HIS A NE2   1 
ATOM   13500 N  N     . GLN A 1 3152 ? 174.009 145.696 200.710 1.00 19.69  ? 3152 GLN A N     1 
ATOM   13501 C  CA    . GLN A 1 3152 ? 175.079 146.303 199.924 1.00 19.70  ? 3152 GLN A CA    1 
ATOM   13502 C  C     . GLN A 1 3152 ? 175.398 145.495 198.672 1.00 20.86  ? 3152 GLN A C     1 
ATOM   13503 O  O     . GLN A 1 3152 ? 175.680 146.077 197.619 1.00 24.07  ? 3152 GLN A O     1 
ATOM   13504 C  CB    . GLN A 1 3152 ? 176.336 146.473 200.779 1.00 21.47  ? 3152 GLN A CB    1 
ATOM   13505 C  CG    . GLN A 1 3152 ? 176.071 146.986 202.185 1.00 28.40  ? 3152 GLN A CG    1 
ATOM   13506 C  CD    . GLN A 1 3152 ? 176.385 148.460 202.345 1.00 37.61  ? 3152 GLN A CD    1 
ATOM   13507 O  OE1   . GLN A 1 3152 ? 175.609 149.320 201.930 1.00 33.41  ? 3152 GLN A OE1   1 
ATOM   13508 N  NE2   . GLN A 1 3152 ? 177.523 148.760 202.959 1.00 33.94  ? 3152 GLN A NE2   1 
ATOM   13509 N  N     . THR A 1 3153 ? 175.363 144.163 198.761 1.00 18.84  ? 3153 THR A N     1 
ATOM   13510 C  CA    . THR A 1 3153 ? 175.645 143.337 197.591 1.00 18.71  ? 3153 THR A CA    1 
ATOM   13511 C  C     . THR A 1 3153 ? 174.584 143.489 196.513 1.00 19.81  ? 3153 THR A C     1 
ATOM   13512 O  O     . THR A 1 3153 ? 174.878 143.290 195.329 1.00 22.65  ? 3153 THR A O     1 
ATOM   13513 C  CB    . THR A 1 3153 ? 175.762 141.868 197.992 1.00 20.68  ? 3153 THR A CB    1 
ATOM   13514 O  OG1   . THR A 1 3153 ? 174.573 141.462 198.681 1.00 17.36  ? 3153 THR A OG1   1 
ATOM   13515 C  CG2   . THR A 1 3153 ? 176.960 141.671 198.890 1.00 25.56  ? 3153 THR A CG2   1 
ATOM   13516 N  N     . LEU A 1 3154 ? 173.354 143.830 196.898 1.00 22.45  ? 3154 LEU A N     1 
ATOM   13517 C  CA    . LEU A 1 3154 ? 172.330 144.121 195.903 1.00 20.85  ? 3154 LEU A CA    1 
ATOM   13518 C  C     . LEU A 1 3154 ? 172.701 145.355 195.094 1.00 20.38  ? 3154 LEU A C     1 
ATOM   13519 O  O     . LEU A 1 3154 ? 172.457 145.414 193.883 1.00 29.64  ? 3154 LEU A O     1 
ATOM   13520 C  CB    . LEU A 1 3154 ? 170.977 144.308 196.585 1.00 17.93  ? 3154 LEU A CB    1 
ATOM   13521 C  CG    . LEU A 1 3154 ? 169.993 143.150 196.432 1.00 12.71  ? 3154 LEU A CG    1 
ATOM   13522 C  CD1   . LEU A 1 3154 ? 169.645 142.931 194.978 1.00 11.24  ? 3154 LEU A CD1   1 
ATOM   13523 C  CD2   . LEU A 1 3154 ? 170.550 141.880 197.055 1.00 12.59  ? 3154 LEU A CD2   1 
ATOM   13524 N  N     . HIS A 1 3155 ? 173.282 146.359 195.754 1.00 22.41  ? 3155 HIS A N     1 
ATOM   13525 C  CA    . HIS A 1 3155 ? 173.782 147.527 195.038 1.00 23.71  ? 3155 HIS A CA    1 
ATOM   13526 C  C     . HIS A 1 3155 ? 174.915 147.145 194.095 1.00 26.94  ? 3155 HIS A C     1 
ATOM   13527 O  O     . HIS A 1 3155 ? 174.971 147.617 192.954 1.00 28.13  ? 3155 HIS A O     1 
ATOM   13528 C  CB    . HIS A 1 3155 ? 174.246 148.589 196.035 1.00 22.83  ? 3155 HIS A CB    1 
ATOM   13529 C  CG    . HIS A 1 3155 ? 173.127 149.366 196.657 1.00 24.72  ? 3155 HIS A CG    1 
ATOM   13530 N  ND1   . HIS A 1 3155 ? 172.349 150.253 195.945 1.00 25.52  ? 3155 HIS A ND1   1 
ATOM   13531 C  CD2   . HIS A 1 3155 ? 172.653 149.384 197.925 1.00 22.26  ? 3155 HIS A CD2   1 
ATOM   13532 C  CE1   . HIS A 1 3155 ? 171.447 150.787 196.748 1.00 26.08  ? 3155 HIS A CE1   1 
ATOM   13533 N  NE2   . HIS A 1 3155 ? 171.610 150.277 197.955 1.00 27.72  ? 3155 HIS A NE2   1 
ATOM   13534 N  N     . GLN A 1 3156 ? 175.831 146.289 194.559 1.00 30.95  ? 3156 GLN A N     1 
ATOM   13535 C  CA    . GLN A 1 3156 ? 176.925 145.832 193.708 1.00 29.44  ? 3156 GLN A CA    1 
ATOM   13536 C  C     . GLN A 1 3156 ? 176.410 144.999 192.540 1.00 28.75  ? 3156 GLN A C     1 
ATOM   13537 O  O     . GLN A 1 3156 ? 176.903 145.129 191.414 1.00 36.24  ? 3156 GLN A O     1 
ATOM   13538 C  CB    . GLN A 1 3156 ? 177.933 145.030 194.531 1.00 26.92  ? 3156 GLN A CB    1 
ATOM   13539 C  CG    . GLN A 1 3156 ? 178.757 145.865 195.497 1.00 27.34  ? 3156 GLN A CG    1 
ATOM   13540 C  CD    . GLN A 1 3156 ? 178.881 145.221 196.865 1.00 31.87  ? 3156 GLN A CD    1 
ATOM   13541 O  OE1   . GLN A 1 3156 ? 178.896 143.997 196.988 1.00 33.81  ? 3156 GLN A OE1   1 
ATOM   13542 N  NE2   . GLN A 1 3156 ? 178.973 146.047 197.901 1.00 28.35  ? 3156 GLN A NE2   1 
ATOM   13543 N  N     . ALA A 1 3157 ? 175.428 144.130 192.792 1.00 29.36  ? 3157 ALA A N     1 
ATOM   13544 C  CA    . ALA A 1 3157 ? 174.866 143.316 191.719 1.00 32.50  ? 3157 ALA A CA    1 
ATOM   13545 C  C     . ALA A 1 3157 ? 174.194 144.182 190.663 1.00 31.90  ? 3157 ALA A C     1 
ATOM   13546 O  O     . ALA A 1 3157 ? 174.320 143.916 189.462 1.00 36.09  ? 3157 ALA A O     1 
ATOM   13547 C  CB    . ALA A 1 3157 ? 173.878 142.300 192.291 1.00 29.86  ? 3157 ALA A CB    1 
ATOM   13548 N  N     . ASN A 1 3158 ? 173.468 145.217 191.092 1.00 28.54  ? 3158 ASN A N     1 
ATOM   13549 C  CA    . ASN A 1 3158 ? 172.853 146.137 190.142 1.00 34.36  ? 3158 ASN A CA    1 
ATOM   13550 C  C     . ASN A 1 3158 ? 173.910 146.872 189.326 1.00 39.76  ? 3158 ASN A C     1 
ATOM   13551 O  O     . ASN A 1 3158 ? 173.760 147.043 188.111 1.00 37.09  ? 3158 ASN A O     1 
ATOM   13552 C  CB    . ASN A 1 3158 ? 171.958 147.129 190.883 1.00 33.79  ? 3158 ASN A CB    1 
ATOM   13553 C  CG    . ASN A 1 3158 ? 170.487 146.916 190.593 1.00 36.57  ? 3158 ASN A CG    1 
ATOM   13554 O  OD1   . ASN A 1 3158 ? 170.030 145.783 190.443 1.00 36.93  ? 3158 ASN A OD1   1 
ATOM   13555 N  ND2   . ASN A 1 3158 ? 169.734 148.007 190.521 1.00 39.66  ? 3158 ASN A ND2   1 
ATOM   13556 N  N     . ALA A 1 3159 ? 174.986 147.315 189.980 1.00 44.00  ? 3159 ALA A N     1 
ATOM   13557 C  CA    . ALA A 1 3159 ? 176.063 147.991 189.264 1.00 43.50  ? 3159 ALA A CA    1 
ATOM   13558 C  C     . ALA A 1 3159 ? 176.745 147.052 188.277 1.00 44.51  ? 3159 ALA A C     1 
ATOM   13559 O  O     . ALA A 1 3159 ? 177.109 147.461 187.168 1.00 51.16  ? 3159 ALA A O     1 
ATOM   13560 C  CB    . ALA A 1 3159 ? 177.077 148.559 190.257 1.00 38.43  ? 3159 ALA A CB    1 
ATOM   13561 N  N     . ARG A 1 3160 ? 176.886 145.781 188.660 1.00 39.83  ? 3160 ARG A N     1 
ATOM   13562 C  CA    . ARG A 1 3160 ? 177.473 144.779 187.731 1.00 50.48  ? 3160 ARG A CA    1 
ATOM   13563 C  C     . ARG A 1 3160 ? 176.611 144.698 186.463 1.00 46.85  ? 3160 ARG A C     1 
ATOM   13564 O  O     . ARG A 1 3160 ? 177.161 144.883 185.356 1.00 50.82  ? 3160 ARG A O     1 
ATOM   13565 C  CB    . ARG A 1 3160 ? 177.545 143.405 188.404 1.00 51.98  ? 3160 ARG A CB    1 
ATOM   13566 C  CG    . ARG A 1 3160 ? 177.680 142.254 187.418 1.00 52.42  ? 3160 ARG A CG    1 
ATOM   13567 C  CD    . ARG A 1 3160 ? 177.437 140.911 188.087 1.00 55.91  ? 3160 ARG A CD    1 
ATOM   13568 N  NE    . ARG A 1 3160 ? 177.347 139.815 187.116 1.00 61.05  ? 3160 ARG A NE    1 
ATOM   13569 C  CZ    . ARG A 1 3160 ? 177.121 138.548 187.434 1.00 53.96  ? 3160 ARG A CZ    1 
ATOM   13570 N  NH1   . ARG A 1 3160 ? 177.051 138.188 188.703 1.00 47.98  ? 3160 ARG A NH1   1 
ATOM   13571 N  NH2   . ARG A 1 3160 ? 176.965 137.644 186.483 1.00 55.06  ? 3160 ARG A NH2   1 
ATOM   13572 N  N     . LEU A 1 3161 ? 175.311 144.435 186.623 1.00 48.76  ? 3161 LEU A N     1 
ATOM   13573 C  CA    . LEU A 1 3161 ? 174.400 144.296 185.456 1.00 48.41  ? 3161 LEU A CA    1 
ATOM   13574 C  C     . LEU A 1 3161 ? 174.388 145.607 184.655 1.00 47.93  ? 3161 LEU A C     1 
ATOM   13575 O  O     . LEU A 1 3161 ? 174.448 145.540 183.409 1.00 46.46  ? 3161 LEU A O     1 
ATOM   13576 C  CB    . LEU A 1 3161 ? 173.008 143.925 185.961 1.00 41.45  ? 3161 LEU A CB    1 
ATOM   13577 C  CG    . LEU A 1 3161 ? 171.961 143.626 184.884 1.00 46.55  ? 3161 LEU A CG    1 
ATOM   13578 C  CD1   . LEU A 1 3161 ? 172.410 142.464 184.017 1.00 46.01  ? 3161 LEU A CD1   1 
ATOM   13579 C  CD2   . LEU A 1 3161 ? 170.614 143.330 185.518 1.00 45.53  ? 3161 LEU A CD2   1 
ATOM   13580 N  N     . ALA A 1 3162 ? 174.323 146.748 185.347 1.00 49.32  ? 3162 ALA A N     1 
ATOM   13581 C  CA    . ALA A 1 3162 ? 174.326 148.062 184.662 1.00 48.37  ? 3162 ALA A CA    1 
ATOM   13582 C  C     . ALA A 1 3162 ? 175.612 148.200 183.848 1.00 54.66  ? 3162 ALA A C     1 
ATOM   13583 O  O     . ALA A 1 3162 ? 175.543 148.632 182.677 1.00 58.64  ? 3162 ALA A O     1 
ATOM   13584 C  CB    . ALA A 1 3162 ? 174.193 149.171 185.679 1.00 45.90  ? 3162 ALA A CB    1 
ATOM   13585 N  N     . LYS A 1 3163 ? 176.749 147.832 184.446 1.00 57.11  ? 3163 LYS A N     1 
ATOM   13586 C  CA    . LYS A 1 3163 ? 178.048 147.888 183.729 1.00 59.12  ? 3163 LYS A CA    1 
ATOM   13587 C  C     . LYS A 1 3163 ? 177.953 147.033 182.458 1.00 58.72  ? 3163 LYS A C     1 
ATOM   13588 O  O     . LYS A 1 3163 ? 178.535 147.434 181.427 1.00 61.07  ? 3163 LYS A O     1 
ATOM   13589 C  CB    . LYS A 1 3163 ? 179.158 147.368 184.648 1.00 57.86  ? 3163 LYS A CB    1 
ATOM   13590 C  CG    . LYS A 1 3163 ? 180.372 146.782 183.944 1.00 59.15  ? 3163 LYS A CG    1 
ATOM   13591 C  CD    . LYS A 1 3163 ? 181.139 145.815 184.837 1.00 62.11  ? 3163 LYS A CD    1 
ATOM   13592 C  CE    . LYS A 1 3163 ? 180.273 144.685 185.298 1.00 65.74  ? 3163 LYS A CE    1 
ATOM   13593 N  NZ    . LYS A 1 3163 ? 180.984 143.778 186.202 1.00 65.49  ? 3163 LYS A NZ    1 
ATOM   13594 N  N     . ARG A 1 3164 ? 177.239 145.906 182.532 1.00 54.61  ? 3164 ARG A N     1 
ATOM   13595 C  CA    . ARG A 1 3164 ? 177.117 144.994 181.365 1.00 55.70  ? 3164 ARG A CA    1 
ATOM   13596 C  C     . ARG A 1 3164 ? 175.907 145.415 180.515 1.00 58.67  ? 3164 ARG A C     1 
ATOM   13597 O  O     . ARG A 1 3164 ? 175.443 144.590 179.699 1.00 57.24  ? 3164 ARG A O     1 
ATOM   13598 C  CB    . ARG A 1 3164 ? 177.011 143.547 181.856 1.00 60.35  ? 3164 ARG A CB    1 
ATOM   13599 C  CG    . ARG A 1 3164 ? 178.186 143.149 182.739 1.00 65.27  ? 3164 ARG A CG    1 
ATOM   13600 C  CD    . ARG A 1 3164 ? 178.236 141.669 183.096 1.00 68.93  ? 3164 ARG A CD    1 
ATOM   13601 N  NE    . ARG A 1 3164 ? 177.339 141.270 184.186 1.00 74.71  ? 3164 ARG A NE    1 
ATOM   13602 C  CZ    . ARG A 1 3164 ? 176.013 141.287 184.152 1.00 71.39  ? 3164 ARG A CZ    1 
ATOM   13603 N  NH1   . ARG A 1 3164 ? 175.376 141.273 182.995 1.00 63.62  ? 3164 ARG A NH1   1 
ATOM   13604 N  NH2   . ARG A 1 3164 ? 175.327 141.294 185.280 1.00 67.26  ? 3164 ARG A NH2   1 
ATOM   13605 N  N     . GLY A 1 3165 ? 175.418 146.644 180.706 1.00 56.37  ? 3165 GLY A N     1 
ATOM   13606 C  CA    . GLY A 1 3165 ? 174.284 147.153 179.909 1.00 46.44  ? 3165 GLY A CA    1 
ATOM   13607 C  C     . GLY A 1 3165 ? 173.026 146.341 180.142 1.00 47.11  ? 3165 GLY A C     1 
ATOM   13608 O  O     . GLY A 1 3165 ? 172.232 146.200 179.189 1.00 46.41  ? 3165 GLY A O     1 
ATOM   13609 N  N     . GLY A 1 3166 ? 172.842 145.828 181.362 1.00 51.79  ? 3166 GLY A N     1 
ATOM   13610 C  CA    . GLY A 1 3166 ? 171.632 145.052 181.696 1.00 48.21  ? 3166 GLY A CA    1 
ATOM   13611 C  C     . GLY A 1 3166 ? 170.588 145.929 182.359 1.00 48.08  ? 3166 GLY A C     1 
ATOM   13612 O  O     . GLY A 1 3166 ? 170.974 146.962 182.945 1.00 47.85  ? 3166 GLY A O     1 
ATOM   13613 N  N     . ARG A 1 3167 ? 169.313 145.539 182.274 1.00 47.69  ? 3167 ARG A N     1 
ATOM   13614 C  CA    . ARG A 1 3167 ? 168.239 146.326 182.866 1.00 46.32  ? 3167 ARG A CA    1 
ATOM   13615 C  C     . ARG A 1 3167 ? 168.155 146.034 184.359 1.00 43.78  ? 3167 ARG A C     1 
ATOM   13616 O  O     . ARG A 1 3167 ? 168.001 144.877 184.764 1.00 41.91  ? 3167 ARG A O     1 
ATOM   13617 C  CB    . ARG A 1 3167 ? 166.905 146.018 182.183 1.00 42.44  ? 3167 ARG A CB    1 
ATOM   13618 C  CG    . ARG A 1 3167 ? 165.772 146.965 182.544 1.00 44.00  ? 3167 ARG A CG    1 
ATOM   13619 C  CD    . ARG A 1 3167 ? 164.669 146.894 181.496 1.00 48.26  ? 3167 ARG A CD    1 
ATOM   13620 N  NE    . ARG A 1 3167 ? 165.078 147.507 180.237 1.00 53.22  ? 3167 ARG A NE    1 
ATOM   13621 C  CZ    . ARG A 1 3167 ? 165.464 146.828 179.164 1.00 55.93  ? 3167 ARG A CZ    1 
ATOM   13622 N  NH1   . ARG A 1 3167 ? 165.509 145.506 179.163 1.00 47.86  ? 3167 ARG A NH1   1 
ATOM   13623 N  NH2   . ARG A 1 3167 ? 165.808 147.492 178.064 1.00 55.26  ? 3167 ARG A NH2   1 
ATOM   13624 N  N     . THR A 1 3168 ? 168.246 147.086 185.172 1.00 39.08  ? 3168 THR A N     1 
ATOM   13625 C  CA    . THR A 1 3168 ? 168.309 146.950 186.620 1.00 38.82  ? 3168 THR A CA    1 
ATOM   13626 C  C     . THR A 1 3168 ? 167.187 147.744 187.271 1.00 36.91  ? 3168 THR A C     1 
ATOM   13627 O  O     . THR A 1 3168 ? 166.731 148.760 186.739 1.00 43.14  ? 3168 THR A O     1 
ATOM   13628 C  CB    . THR A 1 3168 ? 169.655 147.438 187.178 1.00 40.94  ? 3168 THR A CB    1 
ATOM   13629 O  OG1   . THR A 1 3168 ? 169.674 148.871 187.193 1.00 41.27  ? 3168 THR A OG1   1 
ATOM   13630 C  CG2   . THR A 1 3168 ? 170.808 146.928 186.325 1.00 42.35  ? 3168 THR A CG2   1 
ATOM   13631 N  N     . MET A 1 3169 ? 166.748 147.272 188.435 1.00 31.83  ? 3169 MET A N     1 
ATOM   13632 C  CA    . MET A 1 3169 ? 165.745 147.955 189.239 1.00 32.59  ? 3169 MET A CA    1 
ATOM   13633 C  C     . MET A 1 3169 ? 166.401 148.542 190.480 1.00 33.69  ? 3169 MET A C     1 
ATOM   13634 O  O     . MET A 1 3169 ? 167.311 147.939 191.057 1.00 37.29  ? 3169 MET A O     1 
ATOM   13635 C  CB    . MET A 1 3169 ? 164.610 147.006 189.636 1.00 30.04  ? 3169 MET A CB    1 
ATOM   13636 C  CG    . MET A 1 3169 ? 163.879 146.406 188.449 1.00 30.52  ? 3169 MET A CG    1 
ATOM   13637 S  SD    . MET A 1 3169 ? 163.089 147.675 187.441 1.00 38.97  ? 3169 MET A SD    1 
ATOM   13638 C  CE    . MET A 1 3169 ? 162.247 146.671 186.224 1.00 33.21  ? 3169 MET A CE    1 
ATOM   13639 N  N     . ALA A 1 3170 ? 165.939 149.724 190.878 1.00 33.20  ? 3170 ALA A N     1 
ATOM   13640 C  CA    . ALA A 1 3170 ? 166.546 150.430 191.997 1.00 28.39  ? 3170 ALA A CA    1 
ATOM   13641 C  C     . ALA A 1 3170 ? 166.355 149.661 193.297 1.00 27.02  ? 3170 ALA A C     1 
ATOM   13642 O  O     . ALA A 1 3170 ? 165.276 149.128 193.573 1.00 29.70  ? 3170 ALA A O     1 
ATOM   13643 C  CB    . ALA A 1 3170 ? 165.950 151.831 192.126 1.00 26.69  ? 3170 ALA A CB    1 
ATOM   13644 N  N     . ILE A 1 3171 ? 167.414 149.607 194.099 1.00 24.07  ? 3171 ILE A N     1 
ATOM   13645 C  CA    . ILE A 1 3171 ? 167.379 148.989 195.418 1.00 18.51  ? 3171 ILE A CA    1 
ATOM   13646 C  C     . ILE A 1 3171 ? 167.137 150.092 196.438 1.00 21.90  ? 3171 ILE A C     1 
ATOM   13647 O  O     . ILE A 1 3171 ? 167.914 151.051 196.526 1.00 27.33  ? 3171 ILE A O     1 
ATOM   13648 C  CB    . ILE A 1 3171 ? 168.676 148.223 195.718 1.00 20.90  ? 3171 ILE A CB    1 
ATOM   13649 C  CG1   . ILE A 1 3171 ? 168.873 147.095 194.703 1.00 24.25  ? 3171 ILE A CG1   1 
ATOM   13650 C  CG2   . ILE A 1 3171 ? 168.653 147.669 197.133 1.00 22.28  ? 3171 ILE A CG2   1 
ATOM   13651 C  CD1   . ILE A 1 3171 ? 167.679 146.174 194.574 1.00 21.88  ? 3171 ILE A CD1   1 
ATOM   13652 N  N     . THR A 1 3172 ? 166.062 149.958 197.207 1.00 21.24  ? 3172 THR A N     1 
ATOM   13653 C  CA    . THR A 1 3172 ? 165.612 151.015 198.101 1.00 19.67  ? 3172 THR A CA    1 
ATOM   13654 C  C     . THR A 1 3172 ? 165.597 150.521 199.543 1.00 19.18  ? 3172 THR A C     1 
ATOM   13655 O  O     . THR A 1 3172 ? 165.656 149.308 199.782 1.00 17.70  ? 3172 THR A O     1 
ATOM   13656 C  CB    . THR A 1 3172 ? 164.221 151.501 197.689 1.00 21.77  ? 3172 THR A CB    1 
ATOM   13657 O  OG1   . THR A 1 3172 ? 163.285 150.421 197.794 1.00 21.68  ? 3172 THR A OG1   1 
ATOM   13658 C  CG2   . THR A 1 3172 ? 164.239 152.013 196.255 1.00 23.55  ? 3172 THR A CG2   1 
ATOM   13659 N  N     . PRO A 1 3173 ? 165.537 151.422 200.528 1.00 20.62  ? 3173 PRO A N     1 
ATOM   13660 C  CA    . PRO A 1 3173 ? 165.404 150.973 201.922 1.00 15.49  ? 3173 PRO A CA    1 
ATOM   13661 C  C     . PRO A 1 3173 ? 164.164 150.138 202.177 1.00 14.90  ? 3173 PRO A C     1 
ATOM   13662 O  O     . PRO A 1 3173 ? 164.136 149.382 203.155 1.00 16.48  ? 3173 PRO A O     1 
ATOM   13663 C  CB    . PRO A 1 3173 ? 165.362 152.289 202.707 1.00 15.92  ? 3173 PRO A CB    1 
ATOM   13664 C  CG    . PRO A 1 3173 ? 166.140 153.234 201.870 1.00 17.90  ? 3173 PRO A CG    1 
ATOM   13665 C  CD    . PRO A 1 3173 ? 165.836 152.863 200.445 1.00 19.50  ? 3173 PRO A CD    1 
ATOM   13666 N  N     . ARG A 1 3174 ? 163.135 150.250 201.334 1.00 15.81  ? 3174 ARG A N     1 
ATOM   13667 C  CA    . ARG A 1 3174 ? 161.960 149.401 201.491 1.00 14.16  ? 3174 ARG A CA    1 
ATOM   13668 C  C     . ARG A 1 3174 ? 162.291 147.939 201.220 1.00 13.97  ? 3174 ARG A C     1 
ATOM   13669 O  O     . ARG A 1 3174 ? 161.673 147.045 201.809 1.00 17.20  ? 3174 ARG A O     1 
ATOM   13670 C  CB    . ARG A 1 3174 ? 160.839 149.880 200.569 1.00 17.23  ? 3174 ARG A CB    1 
ATOM   13671 C  CG    . ARG A 1 3174 ? 160.460 151.337 200.777 1.00 21.97  ? 3174 ARG A CG    1 
ATOM   13672 C  CD    . ARG A 1 3174 ? 158.997 151.588 200.460 1.00 23.76  ? 3174 ARG A CD    1 
ATOM   13673 N  NE    . ARG A 1 3174 ? 158.117 150.655 201.153 1.00 21.76  ? 3174 ARG A NE    1 
ATOM   13674 C  CZ    . ARG A 1 3174 ? 156.840 150.469 200.852 1.00 25.05  ? 3174 ARG A CZ    1 
ATOM   13675 N  NH1   . ARG A 1 3174 ? 156.257 151.137 199.871 1.00 21.65  ? 3174 ARG A NH1   1 
ATOM   13676 N  NH2   . ARG A 1 3174 ? 156.130 149.590 201.554 1.00 23.13  ? 3174 ARG A NH2   1 
ATOM   13677 N  N     . HIS A 1 3175 ? 163.252 147.676 200.331 1.00 13.99  ? 3175 HIS A N     1 
ATOM   13678 C  CA    . HIS A 1 3175 ? 163.742 146.312 200.158 1.00 12.72  ? 3175 HIS A CA    1 
ATOM   13679 C  C     . HIS A 1 3175 ? 164.404 145.805 201.432 1.00 13.29  ? 3175 HIS A C     1 
ATOM   13680 O  O     . HIS A 1 3175 ? 164.230 144.641 201.812 1.00 14.31  ? 3175 HIS A O     1 
ATOM   13681 C  CB    . HIS A 1 3175 ? 164.720 146.241 198.987 1.00 16.34  ? 3175 HIS A CB    1 
ATOM   13682 C  CG    . HIS A 1 3175 ? 164.113 146.586 197.664 1.00 15.89  ? 3175 HIS A CG    1 
ATOM   13683 N  ND1   . HIS A 1 3175 ? 163.652 147.849 197.361 1.00 17.21  ? 3175 HIS A ND1   1 
ATOM   13684 C  CD2   . HIS A 1 3175 ? 163.896 145.832 196.561 1.00 16.54  ? 3175 HIS A CD2   1 
ATOM   13685 C  CE1   . HIS A 1 3175 ? 163.175 147.857 196.129 1.00 19.73  ? 3175 HIS A CE1   1 
ATOM   13686 N  NE2   . HIS A 1 3175 ? 163.310 146.645 195.622 1.00 25.90  ? 3175 HIS A NE2   1 
ATOM   13687 N  N     . TYR A 1 3176 ? 165.181 146.663 202.098 1.00 13.41  ? 3176 TYR A N     1 
ATOM   13688 C  CA    . TYR A 1 3176 ? 165.795 146.281 203.365 1.00 10.19  ? 3176 TYR A CA    1 
ATOM   13689 C  C     . TYR A 1 3176 ? 164.740 145.984 204.421 1.00 12.47  ? 3176 TYR A C     1 
ATOM   13690 O  O     . TYR A 1 3176 ? 164.843 144.991 205.151 1.00 15.66  ? 3176 TYR A O     1 
ATOM   13691 C  CB    . TYR A 1 3176 ? 166.734 147.386 203.848 1.00 11.34  ? 3176 TYR A CB    1 
ATOM   13692 C  CG    . TYR A 1 3176 ? 167.576 146.995 205.039 1.00 13.37  ? 3176 TYR A CG    1 
ATOM   13693 C  CD1   . TYR A 1 3176 ? 168.529 145.992 204.941 1.00 15.33  ? 3176 TYR A CD1   1 
ATOM   13694 C  CD2   . TYR A 1 3176 ? 167.409 147.620 206.266 1.00 14.72  ? 3176 TYR A CD2   1 
ATOM   13695 C  CE1   . TYR A 1 3176 ? 169.298 145.630 206.028 1.00 13.07  ? 3176 TYR A CE1   1 
ATOM   13696 C  CE2   . TYR A 1 3176 ? 168.174 147.264 207.357 1.00 17.38  ? 3176 TYR A CE2   1 
ATOM   13697 C  CZ    . TYR A 1 3176 ? 169.116 146.269 207.232 1.00 14.66  ? 3176 TYR A CZ    1 
ATOM   13698 O  OH    . TYR A 1 3176 ? 169.879 145.911 208.319 1.00 20.81  ? 3176 TYR A OH    1 
ATOM   13699 N  N     . LEU A 1 3177 ? 163.716 146.832 204.513 1.00 13.91  ? 3177 LEU A N     1 
ATOM   13700 C  CA    . LEU A 1 3177 ? 162.654 146.618 205.489 1.00 13.77  ? 3177 LEU A CA    1 
ATOM   13701 C  C     . LEU A 1 3177 ? 161.902 145.325 205.201 1.00 14.02  ? 3177 LEU A C     1 
ATOM   13702 O  O     . LEU A 1 3177 ? 161.501 144.606 206.123 1.00 19.44  ? 3177 LEU A O     1 
ATOM   13703 C  CB    . LEU A 1 3177 ? 161.702 147.812 205.489 1.00 11.84  ? 3177 LEU A CB    1 
ATOM   13704 C  CG    . LEU A 1 3177 ? 162.245 149.073 206.157 1.00 12.59  ? 3177 LEU A CG    1 
ATOM   13705 C  CD1   . LEU A 1 3177 ? 161.336 150.249 205.871 1.00 16.79  ? 3177 LEU A CD1   1 
ATOM   13706 C  CD2   . LEU A 1 3177 ? 162.393 148.859 207.652 1.00 12.74  ? 3177 LEU A CD2   1 
ATOM   13707 N  N     . ASP A 1 3178 ? 161.695 145.020 203.919 1.00 12.76  ? 3178 ASP A N     1 
ATOM   13708 C  CA    . ASP A 1 3178 ? 161.047 143.766 203.551 1.00 14.97  ? 3178 ASP A CA    1 
ATOM   13709 C  C     . ASP A 1 3178 ? 161.886 142.570 203.982 1.00 18.54  ? 3178 ASP A C     1 
ATOM   13710 O  O     . ASP A 1 3178 ? 161.350 141.569 204.472 1.00 20.68  ? 3178 ASP A O     1 
ATOM   13711 C  CB    . ASP A 1 3178 ? 160.799 143.731 202.044 1.00 16.56  ? 3178 ASP A CB    1 
ATOM   13712 C  CG    . ASP A 1 3178 ? 159.338 143.910 201.691 1.00 28.49  ? 3178 ASP A CG    1 
ATOM   13713 O  OD1   . ASP A 1 3178 ? 158.616 144.563 202.473 1.00 29.20  ? 3178 ASP A OD1   1 
ATOM   13714 O  OD2   . ASP A 1 3178 ? 158.911 143.399 200.635 1.00 38.55  ? 3178 ASP A OD2   1 
ATOM   13715 N  N     . PHE A 1 3179 ? 163.206 142.655 203.799 1.00 15.53  ? 3179 PHE A N     1 
ATOM   13716 C  CA    . PHE A 1 3179 ? 164.090 141.558 204.183 1.00 10.77  ? 3179 PHE A CA    1 
ATOM   13717 C  C     . PHE A 1 3179 ? 164.046 141.314 205.686 1.00 12.34  ? 3179 PHE A C     1 
ATOM   13718 O  O     . PHE A 1 3179 ? 163.905 140.170 206.133 1.00 16.44  ? 3179 PHE A O     1 
ATOM   13719 C  CB    . PHE A 1 3179 ? 165.515 141.866 203.714 1.00 11.77  ? 3179 PHE A CB    1 
ATOM   13720 C  CG    . PHE A 1 3179 ? 166.575 140.976 204.311 1.00 12.08  ? 3179 PHE A CG    1 
ATOM   13721 C  CD1   . PHE A 1 3179 ? 166.371 139.613 204.455 1.00 14.28  ? 3179 PHE A CD1   1 
ATOM   13722 C  CD2   . PHE A 1 3179 ? 167.784 141.509 204.719 1.00 9.95   ? 3179 PHE A CD2   1 
ATOM   13723 C  CE1   . PHE A 1 3179 ? 167.347 138.805 205.003 1.00 16.13  ? 3179 PHE A CE1   1 
ATOM   13724 C  CE2   . PHE A 1 3179 ? 168.764 140.707 205.265 1.00 13.00  ? 3179 PHE A CE2   1 
ATOM   13725 C  CZ    . PHE A 1 3179 ? 168.545 139.353 205.407 1.00 18.00  ? 3179 PHE A CZ    1 
ATOM   13726 N  N     . ILE A 1 3180 ? 164.153 142.378 206.483 1.00 15.46  ? 3180 ILE A N     1 
ATOM   13727 C  CA    . ILE A 1 3180 ? 164.167 142.211 207.932 1.00 15.12  ? 3180 ILE A CA    1 
ATOM   13728 C  C     . ILE A 1 3180 ? 162.810 141.723 208.426 1.00 17.93  ? 3180 ILE A C     1 
ATOM   13729 O  O     . ILE A 1 3180 ? 162.729 140.916 209.360 1.00 21.41  ? 3180 ILE A O     1 
ATOM   13730 C  CB    . ILE A 1 3180 ? 164.593 143.522 208.618 1.00 17.17  ? 3180 ILE A CB    1 
ATOM   13731 C  CG1   . ILE A 1 3180 ? 165.887 144.051 208.000 1.00 16.19  ? 3180 ILE A CG1   1 
ATOM   13732 C  CG2   . ILE A 1 3180 ? 164.821 143.294 210.097 1.00 28.24  ? 3180 ILE A CG2   1 
ATOM   13733 C  CD1   . ILE A 1 3180 ? 167.025 143.052 208.009 1.00 16.99  ? 3180 ILE A CD1   1 
ATOM   13734 N  N     . ASN A 1 3181 ? 161.725 142.202 207.812 1.00 18.01  ? 3181 ASN A N     1 
ATOM   13735 C  CA    . ASN A 1 3181 ? 160.396 141.713 208.170 1.00 21.23  ? 3181 ASN A CA    1 
ATOM   13736 C  C     . ASN A 1 3181 ? 160.240 140.236 207.823 1.00 24.84  ? 3181 ASN A C     1 
ATOM   13737 O  O     . ASN A 1 3181 ? 159.692 139.459 208.614 1.00 26.21  ? 3181 ASN A O     1 
ATOM   13738 C  CB    . ASN A 1 3181 ? 159.326 142.550 207.468 1.00 20.12  ? 3181 ASN A CB    1 
ATOM   13739 C  CG    . ASN A 1 3181 ? 157.980 142.501 208.174 1.00 32.91  ? 3181 ASN A CG    1 
ATOM   13740 O  OD1   . ASN A 1 3181 ? 157.706 141.576 208.939 1.00 35.89  ? 3181 ASN A OD1   1 
ATOM   13741 N  ND2   . ASN A 1 3181 ? 157.133 143.490 207.917 1.00 36.83  ? 3181 ASN A ND2   1 
ATOM   13742 N  N     . HIS A 1 3182 ? 160.711 139.831 206.640 1.00 19.35  ? 3182 HIS A N     1 
ATOM   13743 C  CA    . HIS A 1 3182 ? 160.673 138.418 206.274 1.00 18.90  ? 3182 HIS A CA    1 
ATOM   13744 C  C     . HIS A 1 3182 ? 161.551 137.589 207.202 1.00 24.20  ? 3182 HIS A C     1 
ATOM   13745 O  O     . HIS A 1 3182 ? 161.204 136.453 207.548 1.00 32.44  ? 3182 HIS A O     1 
ATOM   13746 C  CB    . HIS A 1 3182 ? 161.109 138.238 204.821 1.00 22.56  ? 3182 HIS A CB    1 
ATOM   13747 C  CG    . HIS A 1 3182 ? 160.030 138.520 203.824 1.00 21.49  ? 3182 HIS A CG    1 
ATOM   13748 N  ND1   . HIS A 1 3182 ? 160.216 139.350 202.740 1.00 21.63  ? 3182 HIS A ND1   1 
ATOM   13749 C  CD2   . HIS A 1 3182 ? 158.752 138.079 203.745 1.00 20.86  ? 3182 HIS A CD2   1 
ATOM   13750 C  CE1   . HIS A 1 3182 ? 159.099 139.410 202.037 1.00 23.20  ? 3182 HIS A CE1   1 
ATOM   13751 N  NE2   . HIS A 1 3182 ? 158.195 138.648 202.625 1.00 23.81  ? 3182 HIS A NE2   1 
ATOM   13752 N  N     . TYR A 1 3183 ? 162.699 138.139 207.604 1.00 21.65  ? 3183 TYR A N     1 
ATOM   13753 C  CA    . TYR A 1 3183 ? 163.587 137.443 208.530 1.00 21.51  ? 3183 TYR A CA    1 
ATOM   13754 C  C     . TYR A 1 3183 ? 162.900 137.186 209.865 1.00 27.53  ? 3183 TYR A C     1 
ATOM   13755 O  O     . TYR A 1 3183 ? 163.017 136.096 210.437 1.00 35.79  ? 3183 TYR A O     1 
ATOM   13756 C  CB    . TYR A 1 3183 ? 164.869 138.258 208.712 1.00 21.31  ? 3183 TYR A CB    1 
ATOM   13757 C  CG    . TYR A 1 3183 ? 165.967 137.561 209.481 1.00 23.13  ? 3183 TYR A CG    1 
ATOM   13758 C  CD1   . TYR A 1 3183 ? 166.352 136.268 209.166 1.00 24.72  ? 3183 TYR A CD1   1 
ATOM   13759 C  CD2   . TYR A 1 3183 ? 166.654 138.218 210.491 1.00 30.59  ? 3183 TYR A CD2   1 
ATOM   13760 C  CE1   . TYR A 1 3183 ? 167.361 135.634 209.866 1.00 30.82  ? 3183 TYR A CE1   1 
ATOM   13761 C  CE2   . TYR A 1 3183 ? 167.669 137.594 211.189 1.00 33.03  ? 3183 TYR A CE2   1 
ATOM   13762 C  CZ    . TYR A 1 3183 ? 168.018 136.303 210.871 1.00 31.75  ? 3183 TYR A CZ    1 
ATOM   13763 O  OH    . TYR A 1 3183 ? 169.027 135.675 211.563 1.00 36.72  ? 3183 TYR A OH    1 
ATOM   13764 N  N     . ALA A 1 3184 ? 162.172 138.179 210.377 1.00 28.25  ? 3184 ALA A N     1 
ATOM   13765 C  CA    . ALA A 1 3184 ? 161.435 137.992 211.622 1.00 31.27  ? 3184 ALA A CA    1 
ATOM   13766 C  C     . ALA A 1 3184 ? 160.330 136.953 211.460 1.00 33.39  ? 3184 ALA A C     1 
ATOM   13767 O  O     . ALA A 1 3184 ? 160.127 136.103 212.335 1.00 38.01  ? 3184 ALA A O     1 
ATOM   13768 C  CB    . ALA A 1 3184 ? 160.858 139.326 212.095 1.00 33.29  ? 3184 ALA A CB    1 
ATOM   13769 N  N     . ASN A 1 3185 ? 159.604 137.004 210.339 1.00 31.69  ? 3185 ASN A N     1 
ATOM   13770 C  CA    . ASN A 1 3185 ? 158.465 136.110 210.145 1.00 29.15  ? 3185 ASN A CA    1 
ATOM   13771 C  C     . ASN A 1 3185 ? 158.911 134.663 209.965 1.00 32.13  ? 3185 ASN A C     1 
ATOM   13772 O  O     . ASN A 1 3185 ? 158.353 133.749 210.583 1.00 38.26  ? 3185 ASN A O     1 
ATOM   13773 C  CB    . ASN A 1 3185 ? 157.634 136.574 208.947 1.00 25.40  ? 3185 ASN A CB    1 
ATOM   13774 C  CG    . ASN A 1 3185 ? 157.026 137.947 209.155 1.00 30.12  ? 3185 ASN A CG    1 
ATOM   13775 O  OD1   . ASN A 1 3185 ? 157.140 138.530 210.233 1.00 34.10  ? 3185 ASN A OD1   1 
ATOM   13776 N  ND2   . ASN A 1 3185 ? 156.382 138.473 208.120 1.00 28.50  ? 3185 ASN A ND2   1 
ATOM   13777 N  N     . LEU A 1 3186 ? 159.918 134.434 209.116 1.00 30.52  ? 3186 LEU A N     1 
ATOM   13778 C  CA    . LEU A 1 3186 ? 160.392 133.073 208.873 1.00 32.91  ? 3186 LEU A CA    1 
ATOM   13779 C  C     . LEU A 1 3186 ? 160.973 132.450 210.136 1.00 39.77  ? 3186 LEU A C     1 
ATOM   13780 O  O     . LEU A 1 3186 ? 160.755 131.264 210.407 1.00 41.46  ? 3186 LEU A O     1 
ATOM   13781 C  CB    . LEU A 1 3186 ? 161.431 133.070 207.752 1.00 27.50  ? 3186 LEU A CB    1 
ATOM   13782 C  CG    . LEU A 1 3186 ? 160.905 133.416 206.359 1.00 32.58  ? 3186 LEU A CG    1 
ATOM   13783 C  CD1   . LEU A 1 3186 ? 162.046 133.529 205.362 1.00 26.22  ? 3186 LEU A CD1   1 
ATOM   13784 C  CD2   . LEU A 1 3186 ? 159.886 132.383 205.902 1.00 32.20  ? 3186 LEU A CD2   1 
ATOM   13785 N  N     . PHE A 1 3187 ? 161.723 133.233 210.913 1.00 40.89  ? 3187 PHE A N     1 
ATOM   13786 C  CA    . PHE A 1 3187 ? 162.311 132.728 212.150 1.00 39.77  ? 3187 PHE A CA    1 
ATOM   13787 C  C     . PHE A 1 3187 ? 161.238 132.223 213.103 1.00 42.63  ? 3187 PHE A C     1 
ATOM   13788 O  O     . PHE A 1 3187 ? 161.345 131.122 213.653 1.00 52.29  ? 3187 PHE A O     1 
ATOM   13789 C  CB    . PHE A 1 3187 ? 163.120 133.838 212.812 1.00 41.13  ? 3187 PHE A CB    1 
ATOM   13790 C  CG    . PHE A 1 3187 ? 164.079 133.364 213.862 1.00 45.85  ? 3187 PHE A CG    1 
ATOM   13791 C  CD1   . PHE A 1 3187 ? 165.322 132.870 213.511 1.00 42.43  ? 3187 PHE A CD1   1 
ATOM   13792 C  CD2   . PHE A 1 3187 ? 163.741 133.427 215.204 1.00 45.23  ? 3187 PHE A CD2   1 
ATOM   13793 C  CE1   . PHE A 1 3187 ? 166.211 132.445 214.478 1.00 43.33  ? 3187 PHE A CE1   1 
ATOM   13794 C  CE2   . PHE A 1 3187 ? 164.624 133.000 216.174 1.00 50.57  ? 3187 PHE A CE2   1 
ATOM   13795 C  CZ    . PHE A 1 3187 ? 165.860 132.507 215.810 1.00 51.20  ? 3187 PHE A CZ    1 
ATOM   13796 N  N     . HIS A 1 3188 ? 160.196 133.027 213.319 1.00 40.68  ? 3188 HIS A N     1 
ATOM   13797 C  CA    . HIS A 1 3188 ? 159.121 132.619 214.215 1.00 44.54  ? 3188 HIS A CA    1 
ATOM   13798 C  C     . HIS A 1 3188 ? 158.384 131.407 213.664 1.00 48.07  ? 3188 HIS A C     1 
ATOM   13799 O  O     . HIS A 1 3188 ? 158.028 130.491 214.414 1.00 52.12  ? 3188 HIS A O     1 
ATOM   13800 C  CB    . HIS A 1 3188 ? 158.159 133.786 214.440 1.00 43.42  ? 3188 HIS A CB    1 
ATOM   13801 C  CG    . HIS A 1 3188 ? 157.050 133.486 215.400 1.00 54.96  ? 3188 HIS A CG    1 
ATOM   13802 N  ND1   . HIS A 1 3188 ? 155.894 134.234 215.461 1.00 51.66  ? 3188 HIS A ND1   1 
ATOM   13803 C  CD2   . HIS A 1 3188 ? 156.927 132.528 216.349 1.00 52.89  ? 3188 HIS A CD2   1 
ATOM   13804 C  CE1   . HIS A 1 3188 ? 155.104 133.744 216.399 1.00 59.51  ? 3188 HIS A CE1   1 
ATOM   13805 N  NE2   . HIS A 1 3188 ? 155.707 132.707 216.952 1.00 58.62  ? 3188 HIS A NE2   1 
ATOM   13806 N  N     . GLU A 1 3189 ? 158.155 131.380 212.350 1.00 46.17  ? 3189 GLU A N     1 
ATOM   13807 C  CA    . GLU A 1 3189 ? 157.451 130.256 211.742 1.00 45.62  ? 3189 GLU A CA    1 
ATOM   13808 C  C     . GLU A 1 3189 ? 158.296 128.988 211.786 1.00 48.80  ? 3189 GLU A C     1 
ATOM   13809 O  O     . GLU A 1 3189 ? 157.811 127.920 212.176 1.00 54.37  ? 3189 GLU A O     1 
ATOM   13810 C  CB    . GLU A 1 3189 ? 157.062 130.604 210.307 1.00 45.85  ? 3189 GLU A CB    1 
ATOM   13811 C  CG    . GLU A 1 3189 ? 156.440 129.457 209.533 1.00 51.33  ? 3189 GLU A CG    1 
ATOM   13812 C  CD    . GLU A 1 3189 ? 156.434 129.705 208.040 1.00 54.69  ? 3189 GLU A CD    1 
ATOM   13813 O  OE1   . GLU A 1 3189 ? 157.109 130.655 207.593 1.00 56.12  ? 3189 GLU A OE1   1 
ATOM   13814 O  OE2   . GLU A 1 3189 ? 155.748 128.954 207.315 1.00 54.52  ? 3189 GLU A OE2   1 
ATOM   13815 N  N     . LYS A 1 3190 ? 159.569 129.085 211.389 1.00 46.45  ? 3190 LYS A N     1 
ATOM   13816 C  CA    . LYS A 1 3190 ? 160.440 127.913 211.419 1.00 46.11  ? 3190 LYS A CA    1 
ATOM   13817 C  C     . LYS A 1 3190 ? 160.657 127.415 212.842 1.00 49.74  ? 3190 LYS A C     1 
ATOM   13818 O  O     . LYS A 1 3190 ? 160.664 126.203 213.088 1.00 58.59  ? 3190 LYS A O     1 
ATOM   13819 C  CB    . LYS A 1 3190 ? 161.781 128.226 210.753 1.00 48.54  ? 3190 LYS A CB    1 
ATOM   13820 C  CG    . LYS A 1 3190 ? 161.700 128.472 209.256 1.00 44.91  ? 3190 LYS A CG    1 
ATOM   13821 C  CD    . LYS A 1 3190 ? 161.079 127.285 208.542 1.00 46.79  ? 3190 LYS A CD    1 
ATOM   13822 C  CE    . LYS A 1 3190 ? 160.913 127.557 207.058 1.00 52.05  ? 3190 LYS A CE    1 
ATOM   13823 N  NZ    . LYS A 1 3190 ? 160.208 126.443 206.369 1.00 52.25  ? 3190 LYS A NZ    1 
ATOM   13824 N  N     . ARG A 1 3191 ? 160.847 128.332 213.792 1.00 50.85  ? 3191 ARG A N     1 
ATOM   13825 C  CA    . ARG A 1 3191 ? 161.059 127.927 215.178 1.00 53.11  ? 3191 ARG A CA    1 
ATOM   13826 C  C     . ARG A 1 3191 ? 159.816 127.254 215.747 1.00 53.43  ? 3191 ARG A C     1 
ATOM   13827 O  O     . ARG A 1 3191 ? 159.905 126.203 216.391 1.00 60.29  ? 3191 ARG A O     1 
ATOM   13828 C  CB    . ARG A 1 3191 ? 161.453 129.139 216.023 1.00 55.02  ? 3191 ARG A CB    1 
ATOM   13829 C  CG    . ARG A 1 3191 ? 162.669 128.923 216.909 1.00 60.76  ? 3191 ARG A CG    1 
ATOM   13830 C  CD    . ARG A 1 3191 ? 163.029 130.201 217.653 1.00 62.76  ? 3191 ARG A CD    1 
ATOM   13831 N  NE    . ARG A 1 3191 ? 163.754 129.939 218.890 1.00 64.76  ? 3191 ARG A NE    1 
ATOM   13832 C  CZ    . ARG A 1 3191 ? 165.055 129.687 218.957 1.00 69.40  ? 3191 ARG A CZ    1 
ATOM   13833 N  NH1   . ARG A 1 3191 ? 165.811 129.658 217.872 1.00 65.85  ? 3191 ARG A NH1   1 
ATOM   13834 N  NH2   . ARG A 1 3191 ? 165.611 129.460 220.144 1.00 68.05  ? 3191 ARG A NH2   1 
ATOM   13835 N  N     . SER A 1 3192 ? 158.640 127.843 215.508 1.00 49.68  ? 3192 SER A N     1 
ATOM   13836 C  CA    . SER A 1 3192 ? 157.405 127.275 216.043 1.00 56.31  ? 3192 SER A CA    1 
ATOM   13837 C  C     . SER A 1 3192 ? 157.111 125.910 215.435 1.00 63.14  ? 3192 SER A C     1 
ATOM   13838 O  O     . SER A 1 3192 ? 156.694 124.985 216.141 1.00 69.60  ? 3192 SER A O     1 
ATOM   13839 C  CB    . SER A 1 3192 ? 156.237 128.230 215.800 1.00 53.96  ? 3192 SER A CB    1 
ATOM   13840 O  OG    . SER A 1 3192 ? 156.544 129.533 216.260 1.00 56.84  ? 3192 SER A OG    1 
ATOM   13841 N  N     . GLU A 1 3193 ? 157.374 125.771 214.134 1.00 62.10  ? 3193 GLU A N     1 
ATOM   13842 C  CA    . GLU A 1 3193 ? 157.177 124.461 213.461 1.00 58.57  ? 3193 GLU A CA    1 
ATOM   13843 C  C     . GLU A 1 3193 ? 158.139 123.430 214.069 1.00 62.22  ? 3193 GLU A C     1 
ATOM   13844 O  O     . GLU A 1 3193 ? 157.659 122.362 214.510 1.00 72.11  ? 3193 GLU A O     1 
ATOM   13845 C  CB    . GLU A 1 3193 ? 157.433 124.596 211.960 1.00 55.20  ? 3193 GLU A CB    1 
ATOM   13846 C  CG    . GLU A 1 3193 ? 156.377 125.423 211.233 1.00 55.24  ? 3193 GLU A CG    1 
ATOM   13847 C  CD    . GLU A 1 3193 ? 156.791 125.826 209.830 1.00 63.74  ? 3193 GLU A CD    1 
ATOM   13848 O  OE1   . GLU A 1 3193 ? 157.933 125.509 209.437 1.00 59.65  ? 3193 GLU A OE1   1 
ATOM   13849 O  OE2   . GLU A 1 3193 ? 155.969 126.449 209.126 1.00 71.39  ? 3193 GLU A OE2   1 
ATOM   13850 N  N     . LEU A 1 3194 ? 159.438 123.744 214.102 1.00 58.13  ? 3194 LEU A N     1 
ATOM   13851 C  CA    . LEU A 1 3194 ? 160.447 122.774 214.607 1.00 64.53  ? 3194 LEU A CA    1 
ATOM   13852 C  C     . LEU A 1 3194 ? 160.103 122.366 216.048 1.00 69.88  ? 3194 LEU A C     1 
ATOM   13853 O  O     . LEU A 1 3194 ? 160.134 121.151 216.341 1.00 75.26  ? 3194 LEU A O     1 
ATOM   13854 C  CB    . LEU A 1 3194 ? 161.845 123.384 214.521 1.00 59.30  ? 3194 LEU A CB    1 
ATOM   13855 C  CG    . LEU A 1 3194 ? 162.986 122.508 215.049 1.00 67.83  ? 3194 LEU A CG    1 
ATOM   13856 C  CD1   . LEU A 1 3194 ? 162.990 121.155 214.359 1.00 67.50  ? 3194 LEU A CD1   1 
ATOM   13857 C  CD2   . LEU A 1 3194 ? 164.324 123.201 214.869 1.00 69.36  ? 3194 LEU A CD2   1 
ATOM   13858 N  N     . GLU A 1 3195 ? 159.788 123.339 216.906 1.00 72.22  ? 3195 GLU A N     1 
ATOM   13859 C  CA    . GLU A 1 3195 ? 159.507 123.030 218.333 1.00 72.36  ? 3195 GLU A CA    1 
ATOM   13860 C  C     . GLU A 1 3195 ? 158.335 122.040 218.414 1.00 70.20  ? 3195 GLU A C     1 
ATOM   13861 O  O     . GLU A 1 3195 ? 158.462 121.030 219.140 1.00 76.91  ? 3195 GLU A O     1 
ATOM   13862 C  CB    . GLU A 1 3195 ? 159.190 124.306 219.113 1.00 73.23  ? 3195 GLU A CB    1 
ATOM   13863 C  CG    . GLU A 1 3195 ? 160.360 125.283 219.186 1.00 74.43  ? 3195 GLU A CG    1 
ATOM   13864 C  CD    . GLU A 1 3195 ? 161.576 124.797 219.955 1.00 83.66  ? 3195 GLU A CD    1 
ATOM   13865 O  OE1   . GLU A 1 3195 ? 161.553 123.656 220.463 1.00 81.89  ? 3195 GLU A OE1   1 
ATOM   13866 O  OE2   . GLU A 1 3195 ? 162.550 125.572 220.050 1.00 87.51  ? 3195 GLU A OE2   1 
ATOM   13867 N  N     . GLU A 1 3196 ? 157.249 122.316 217.688 1.00 68.42  ? 3196 GLU A N     1 
ATOM   13868 C  CA    . GLU A 1 3196 ? 156.056 121.432 217.730 1.00 75.63  ? 3196 GLU A CA    1 
ATOM   13869 C  C     . GLU A 1 3196 ? 156.460 120.026 217.261 1.00 79.27  ? 3196 GLU A C     1 
ATOM   13870 O  O     . GLU A 1 3196 ? 156.041 119.041 217.907 1.00 83.56  ? 3196 GLU A O     1 
ATOM   13871 C  CB    . GLU A 1 3196 ? 154.942 122.002 216.852 1.00 75.07  ? 3196 GLU A CB    1 
ATOM   13872 C  CG    . GLU A 1 3196 ? 153.669 121.161 216.878 1.00 81.85  ? 3196 GLU A CG    1 
ATOM   13873 C  CD    . GLU A 1 3196 ? 152.582 121.648 215.938 1.00 89.87  ? 3196 GLU A CD    1 
ATOM   13874 O  OE1   . GLU A 1 3196 ? 152.810 122.662 215.246 1.00 90.55  ? 3196 GLU A OE1   1 
ATOM   13875 O  OE2   . GLU A 1 3196 ? 151.509 121.011 215.897 1.00 91.68  ? 3196 GLU A OE2   1 
ATOM   13876 N  N     . GLN A 1 3197 ? 157.254 119.946 216.190 1.00 77.98  ? 3197 GLN A N     1 
ATOM   13877 C  CA    . GLN A 1 3197 ? 157.697 118.632 215.658 1.00 76.80  ? 3197 GLN A CA    1 
ATOM   13878 C  C     . GLN A 1 3197 ? 158.465 117.875 216.750 1.00 81.74  ? 3197 GLN A C     1 
ATOM   13879 O  O     . GLN A 1 3197 ? 158.140 116.692 216.991 1.00 87.68  ? 3197 GLN A O     1 
ATOM   13880 C  CB    . GLN A 1 3197 ? 158.594 118.830 214.437 1.00 75.52  ? 3197 GLN A CB    1 
ATOM   13881 C  CG    . GLN A 1 3197 ? 159.194 117.538 213.896 1.00 80.63  ? 3197 GLN A CG    1 
ATOM   13882 C  CD    . GLN A 1 3197 ? 160.208 117.767 212.796 1.00 81.72  ? 3197 GLN A CD    1 
ATOM   13883 O  OE1   . GLN A 1 3197 ? 160.511 118.906 212.425 1.00 80.47  ? 3197 GLN A OE1   1 
ATOM   13884 N  NE2   . GLN A 1 3197 ? 160.747 116.679 212.266 1.00 77.09  ? 3197 GLN A NE2   1 
ATOM   13885 N  N     . GLN A 1 3198 ? 159.433 118.537 217.390 1.00 79.41  ? 3198 GLN A N     1 
ATOM   13886 C  CA    . GLN A 1 3198 ? 160.257 117.866 218.428 1.00 79.35  ? 3198 GLN A CA    1 
ATOM   13887 C  C     . GLN A 1 3198 ? 159.333 117.400 219.563 1.00 82.70  ? 3198 GLN A C     1 
ATOM   13888 O  O     . GLN A 1 3198 ? 159.503 116.255 220.035 1.00 85.93  ? 3198 GLN A O     1 
ATOM   13889 C  CB    . GLN A 1 3198 ? 161.348 118.802 218.947 1.00 76.00  ? 3198 GLN A CB    1 
ATOM   13890 C  CG    . GLN A 1 3198 ? 162.255 118.170 219.997 1.00 82.32  ? 3198 GLN A CG    1 
ATOM   13891 C  CD    . GLN A 1 3198 ? 163.056 116.997 219.475 1.00 87.72  ? 3198 GLN A CD    1 
ATOM   13892 O  OE1   . GLN A 1 3198 ? 162.976 116.629 218.298 1.00 88.11  ? 3198 GLN A OE1   1 
ATOM   13893 N  NE2   . GLN A 1 3198 ? 163.849 116.399 220.352 1.00 90.66  ? 3198 GLN A NE2   1 
ATOM   13894 N  N     . MET A 1 3199 ? 158.393 118.255 219.974 1.00 80.66  ? 3199 MET A N     1 
ATOM   13895 C  CA    . MET A 1 3199 ? 157.421 117.872 221.029 1.00 83.83  ? 3199 MET A CA    1 
ATOM   13896 C  C     . MET A 1 3199 ? 156.666 116.617 220.570 1.00 87.75  ? 3199 MET A C     1 
ATOM   13897 O  O     . MET A 1 3199 ? 156.662 115.617 221.320 1.00 93.06  ? 3199 MET A O     1 
ATOM   13898 C  CB    . MET A 1 3199 ? 156.419 119.003 221.278 1.00 81.91  ? 3199 MET A CB    1 
ATOM   13899 C  CG    . MET A 1 3199 ? 155.289 118.632 222.216 1.00 83.65  ? 3199 MET A CG    1 
ATOM   13900 S  SD    . MET A 1 3199 ? 154.085 119.966 222.373 1.00 98.34  ? 3199 MET A SD    1 
ATOM   13901 C  CE    . MET A 1 3199 ? 155.159 121.311 222.891 1.00 83.48  ? 3199 MET A CE    1 
ATOM   13902 N  N     . HIS A 1 3200 ? 156.059 116.672 219.381 1.00 84.45  ? 3200 HIS A N     1 
ATOM   13903 C  CA    . HIS A 1 3200 ? 155.311 115.530 218.866 1.00 86.55  ? 3200 HIS A CA    1 
ATOM   13904 C  C     . HIS A 1 3200 ? 156.183 114.281 218.814 1.00 88.22  ? 3200 HIS A C     1 
ATOM   13905 O  O     . HIS A 1 3200 ? 155.736 113.186 219.176 1.00 88.45  ? 3200 HIS A O     1 
ATOM   13906 C  CB    . HIS A 1 3200 ? 154.751 115.851 217.481 1.00 85.18  ? 3200 HIS A CB    1 
ATOM   13907 C  CG    . HIS A 1 3200 ? 153.663 116.879 217.492 1.00 84.58  ? 3200 HIS A CG    1 
ATOM   13908 N  ND1   . HIS A 1 3200 ? 152.972 117.219 218.634 1.00 84.67  ? 3200 HIS A ND1   1 
ATOM   13909 C  CD2   . HIS A 1 3200 ? 153.144 117.639 216.498 1.00 84.41  ? 3200 HIS A CD2   1 
ATOM   13910 C  CE1   . HIS A 1 3200 ? 152.076 118.146 218.345 1.00 87.08  ? 3200 HIS A CE1   1 
ATOM   13911 N  NE2   . HIS A 1 3200 ? 152.159 118.418 217.055 1.00 84.97  ? 3200 HIS A NE2   1 
ATOM   13912 N  N     . LEU A 1 3201 ? 157.432 114.426 218.364 1.00 88.38  ? 3201 LEU A N     1 
ATOM   13913 C  CA    . LEU A 1 3201 ? 158.335 113.281 218.306 1.00 88.67  ? 3201 LEU A CA    1 
ATOM   13914 C  C     . LEU A 1 3201 ? 158.699 112.794 219.703 1.00 92.07  ? 3201 LEU A C     1 
ATOM   13915 O  O     . LEU A 1 3201 ? 158.892 111.592 219.919 1.00 96.27  ? 3201 LEU A O     1 
ATOM   13916 C  CB    . LEU A 1 3201 ? 159.594 113.643 217.518 1.00 87.23  ? 3201 LEU A CB    1 
ATOM   13917 C  CG    . LEU A 1 3201 ? 159.421 113.832 216.010 1.00 92.68  ? 3201 LEU A CG    1 
ATOM   13918 C  CD1   . LEU A 1 3201 ? 160.772 114.004 215.334 1.00 90.09  ? 3201 LEU A CD1   1 
ATOM   13919 C  CD2   . LEU A 1 3201 ? 158.657 112.664 215.404 1.00 97.11  ? 3201 LEU A CD2   1 
ATOM   13920 N  N     . ASN A 1 3202 ? 158.808 113.715 220.663 1.00 89.16  ? 3202 ASN A N     1 
ATOM   13921 C  CA    . ASN A 1 3202 ? 159.099 113.319 222.037 1.00 90.00  ? 3202 ASN A CA    1 
ATOM   13922 C  C     . ASN A 1 3202 ? 157.968 112.483 222.619 1.00 92.22  ? 3202 ASN A C     1 
ATOM   13923 O  O     . ASN A 1 3202 ? 158.213 111.493 223.320 1.00 93.68  ? 3202 ASN A O     1 
ATOM   13924 C  CB    . ASN A 1 3202 ? 159.350 114.557 222.898 1.00 88.38  ? 3202 ASN A CB    1 
ATOM   13925 C  CG    . ASN A 1 3202 ? 160.819 114.917 222.987 1.00 89.90  ? 3202 ASN A CG    1 
ATOM   13926 O  OD1   . ASN A 1 3202 ? 161.224 116.016 222.606 1.00 92.17  ? 3202 ASN A OD1   1 
ATOM   13927 N  ND2   . ASN A 1 3202 ? 161.627 113.991 223.490 1.00 82.75  ? 3202 ASN A ND2   1 
ATOM   13928 N  N     . VAL A 1 3203 ? 156.720 112.868 222.344 1.00 90.61  ? 3203 VAL A N     1 
ATOM   13929 C  CA    . VAL A 1 3203 ? 155.575 112.126 222.867 1.00 92.02  ? 3203 VAL A CA    1 
ATOM   13930 C  C     . VAL A 1 3203 ? 155.529 110.729 222.259 1.00 95.17  ? 3203 VAL A C     1 
ATOM   13931 O  O     . VAL A 1 3203 ? 155.340 109.729 222.964 1.00 97.70  ? 3203 VAL A O     1 
ATOM   13932 C  CB    . VAL A 1 3203 ? 154.270 112.899 222.604 1.00 89.20  ? 3203 VAL A CB    1 
ATOM   13933 C  CG1   . VAL A 1 3203 ? 153.096 111.942 222.488 1.00 87.84  ? 3203 VAL A CG1   1 
ATOM   13934 C  CG2   . VAL A 1 3203 ? 154.027 113.931 223.693 1.00 86.62  ? 3203 VAL A CG2   1 
ATOM   13935 N  N     . GLY A 1 3204 ? 155.707 110.640 220.939 1.00 96.55  ? 3204 GLY A N     1 
ATOM   13936 C  CA    . GLY A 1 3204 ? 155.663 109.344 220.280 1.00 97.85  ? 3204 GLY A CA    1 
ATOM   13937 C  C     . GLY A 1 3204 ? 156.773 108.417 220.734 1.00 99.49  ? 3204 GLY A C     1 
ATOM   13938 O  O     . GLY A 1 3204 ? 156.560 107.215 220.905 1.00 102.02 ? 3204 GLY A O     1 
ATOM   13939 N  N     . LEU A 1 3205 ? 157.976 108.963 220.927 1.00 95.74  ? 3205 LEU A N     1 
ATOM   13940 C  CA    . LEU A 1 3205 ? 159.087 108.151 221.412 1.00 96.93  ? 3205 LEU A CA    1 
ATOM   13941 C  C     . LEU A 1 3205 ? 158.814 107.630 222.817 1.00 100.08 ? 3205 LEU A C     1 
ATOM   13942 O  O     . LEU A 1 3205 ? 159.137 106.480 223.135 1.00 101.79 ? 3205 LEU A O     1 
ATOM   13943 C  CB    . LEU A 1 3205 ? 160.382 108.965 221.372 1.00 93.18  ? 3205 LEU A CB    1 
ATOM   13944 C  CG    . LEU A 1 3205 ? 161.716 108.248 221.605 1.00 94.39  ? 3205 LEU A CG    1 
ATOM   13945 C  CD1   . LEU A 1 3205 ? 162.812 108.926 220.804 1.00 93.94  ? 3205 LEU A CD1   1 
ATOM   13946 C  CD2   . LEU A 1 3205 ? 162.088 108.222 223.081 1.00 90.06  ? 3205 LEU A CD2   1 
ATOM   13947 N  N     . ARG A 1 3206 ? 158.225 108.466 223.677 1.00 98.61  ? 3206 ARG A N     1 
ATOM   13948 C  CA    . ARG A 1 3206 ? 157.920 108.034 225.037 1.00 99.99  ? 3206 ARG A CA    1 
ATOM   13949 C  C     . ARG A 1 3206 ? 156.869 106.930 225.045 1.00 104.86 ? 3206 ARG A C     1 
ATOM   13950 O  O     . ARG A 1 3206 ? 157.000 105.943 225.779 1.00 107.66 ? 3206 ARG A O     1 
ATOM   13951 C  CB    . ARG A 1 3206 ? 157.456 109.225 225.877 1.00 101.75 ? 3206 ARG A CB    1 
ATOM   13952 C  CG    . ARG A 1 3206 ? 156.592 108.846 227.069 1.00 103.64 ? 3206 ARG A CG    1 
ATOM   13953 C  CD    . ARG A 1 3206 ? 156.412 110.010 228.031 1.00 102.70 ? 3206 ARG A CD    1 
ATOM   13954 N  NE    . ARG A 1 3206 ? 155.555 111.057 227.487 1.00 100.78 ? 3206 ARG A NE    1 
ATOM   13955 C  CZ    . ARG A 1 3206 ? 155.981 112.260 227.127 1.00 95.31  ? 3206 ARG A CZ    1 
ATOM   13956 N  NH1   . ARG A 1 3206 ? 157.256 112.599 227.220 1.00 94.33  ? 3206 ARG A NH1   1 
ATOM   13957 N  NH2   . ARG A 1 3206 ? 155.104 113.147 226.666 1.00 87.62  ? 3206 ARG A NH2   1 
ATOM   13958 N  N     . LYS A 1 3207 ? 155.819 107.079 224.233 1.00 105.68 ? 3207 LYS A N     1 
ATOM   13959 C  CA    . LYS A 1 3207 ? 154.766 106.069 224.189 1.00 106.32 ? 3207 LYS A CA    1 
ATOM   13960 C  C     . LYS A 1 3207 ? 155.300 104.733 223.687 1.00 105.98 ? 3207 LYS A C     1 
ATOM   13961 O  O     . LYS A 1 3207 ? 154.942 103.674 224.217 1.00 107.72 ? 3207 LYS A O     1 
ATOM   13962 C  CB    . LYS A 1 3207 ? 153.613 106.551 223.309 1.00 103.31 ? 3207 LYS A CB    1 
ATOM   13963 C  CG    . LYS A 1 3207 ? 152.746 107.621 223.952 1.00 103.05 ? 3207 LYS A CG    1 
ATOM   13964 C  CD    . LYS A 1 3207 ? 152.297 107.205 225.343 1.00 100.94 ? 3207 LYS A CD    1 
ATOM   13965 C  CE    . LYS A 1 3207 ? 151.580 108.339 226.057 1.00 100.50 ? 3207 LYS A CE    1 
ATOM   13966 N  NZ    . LYS A 1 3207 ? 150.390 108.809 225.293 1.00 102.89 ? 3207 LYS A NZ    1 
ATOM   13967 N  N     . ILE A 1 3208 ? 156.153 104.761 222.662 1.00 105.18 ? 3208 ILE A N     1 
ATOM   13968 C  CA    . ILE A 1 3208 ? 156.746 103.527 222.158 1.00 105.62 ? 3208 ILE A CA    1 
ATOM   13969 C  C     . ILE A 1 3208 ? 157.700 102.934 223.188 1.00 107.54 ? 3208 ILE A C     1 
ATOM   13970 O  O     . ILE A 1 3208 ? 157.719 101.716 223.409 1.00 109.33 ? 3208 ILE A O     1 
ATOM   13971 C  CB    . ILE A 1 3208 ? 157.443 103.785 220.810 1.00 101.68 ? 3208 ILE A CB    1 
ATOM   13972 C  CG1   . ILE A 1 3208 ? 156.400 104.022 219.715 1.00 100.41 ? 3208 ILE A CG1   1 
ATOM   13973 C  CG2   . ILE A 1 3208 ? 158.353 102.623 220.441 1.00 97.28  ? 3208 ILE A CG2   1 
ATOM   13974 C  CD1   . ILE A 1 3208 ? 156.980 104.121 218.322 1.00 96.49  ? 3208 ILE A CD1   1 
ATOM   13975 N  N     . LYS A 1 3209 ? 158.501 103.781 223.840 1.00 105.57 ? 3209 LYS A N     1 
ATOM   13976 C  CA    . LYS A 1 3209 ? 159.387 103.300 224.895 1.00 104.83 ? 3209 LYS A CA    1 
ATOM   13977 C  C     . LYS A 1 3209 ? 158.595 102.726 226.064 1.00 109.05 ? 3209 LYS A C     1 
ATOM   13978 O  O     . LYS A 1 3209 ? 158.978 101.699 226.636 1.00 109.53 ? 3209 LYS A O     1 
ATOM   13979 C  CB    . LYS A 1 3209 ? 160.303 104.428 225.370 1.00 100.83 ? 3209 LYS A CB    1 
ATOM   13980 C  CG    . LYS A 1 3209 ? 161.341 103.993 226.392 1.00 96.20  ? 3209 LYS A CG    1 
ATOM   13981 C  CD    . LYS A 1 3209 ? 162.541 103.347 225.721 1.00 93.01  ? 3209 LYS A CD    1 
ATOM   13982 C  CE    . LYS A 1 3209 ? 163.770 103.412 226.613 1.00 90.60  ? 3209 LYS A CE    1 
ATOM   13983 N  NZ    . LYS A 1 3209 ? 163.410 103.351 228.057 1.00 92.98  ? 3209 LYS A NZ    1 
ATOM   13984 N  N     . GLU A 1 3210 ? 157.491 103.380 226.436 1.00 109.42 ? 3210 GLU A N     1 
ATOM   13985 C  CA    . GLU A 1 3210 ? 156.639 102.847 227.493 1.00 110.30 ? 3210 GLU A CA    1 
ATOM   13986 C  C     . GLU A 1 3210 ? 156.044 101.504 227.089 1.00 113.38 ? 3210 GLU A C     1 
ATOM   13987 O  O     . GLU A 1 3210 ? 155.921 100.595 227.919 1.00 114.89 ? 3210 GLU A O     1 
ATOM   13988 C  CB    . GLU A 1 3210 ? 155.532 103.846 227.832 1.00 107.98 ? 3210 GLU A CB    1 
ATOM   13989 C  CG    . GLU A 1 3210 ? 155.084 103.809 229.284 1.00 108.75 ? 3210 GLU A CG    1 
ATOM   13990 C  CD    . GLU A 1 3210 ? 154.257 105.019 229.671 1.00 110.44 ? 3210 GLU A CD    1 
ATOM   13991 O  OE1   . GLU A 1 3210 ? 153.877 105.795 228.769 1.00 109.79 ? 3210 GLU A OE1   1 
ATOM   13992 O  OE2   . GLU A 1 3210 ? 153.987 105.195 230.878 1.00 105.00 ? 3210 GLU A OE2   1 
ATOM   13993 N  N     . THR A 1 3211 ? 155.665 101.365 225.817 1.00 113.56 ? 3211 THR A N     1 
ATOM   13994 C  CA    . THR A 1 3211 ? 155.161 100.086 225.326 1.00 114.44 ? 3211 THR A CA    1 
ATOM   13995 C  C     . THR A 1 3211 ? 156.228 99.002  225.417 1.00 115.56 ? 3211 THR A C     1 
ATOM   13996 O  O     . THR A 1 3211 ? 155.935 97.862  225.793 1.00 116.56 ? 3211 THR A O     1 
ATOM   13997 C  CB    . THR A 1 3211 ? 154.667 100.237 223.887 1.00 112.81 ? 3211 THR A CB    1 
ATOM   13998 O  OG1   . THR A 1 3211 ? 153.646 101.240 223.835 1.00 111.49 ? 3211 THR A OG1   1 
ATOM   13999 C  CG2   . THR A 1 3211 ? 154.104 98.920  223.370 1.00 110.69 ? 3211 THR A CG2   1 
ATOM   14000 N  N     . VAL A 1 3212 ? 157.476 99.343  225.083 1.00 113.78 ? 3212 VAL A N     1 
ATOM   14001 C  CA    . VAL A 1 3212 ? 158.565 98.372  225.157 1.00 112.15 ? 3212 VAL A CA    1 
ATOM   14002 C  C     . VAL A 1 3212 ? 158.740 97.876  226.587 1.00 113.57 ? 3212 VAL A C     1 
ATOM   14003 O  O     . VAL A 1 3212 ? 158.936 96.678  226.826 1.00 112.30 ? 3212 VAL A O     1 
ATOM   14004 C  CB    . VAL A 1 3212 ? 159.865 98.987  224.604 1.00 111.34 ? 3212 VAL A CB    1 
ATOM   14005 C  CG1   . VAL A 1 3212 ? 161.071 98.153  225.010 1.00 109.52 ? 3212 VAL A CG1   1 
ATOM   14006 C  CG2   . VAL A 1 3212 ? 159.787 99.120  223.091 1.00 109.92 ? 3212 VAL A CG2   1 
ATOM   14007 N  N     . ASP A 1 3213 ? 158.674 98.787  227.559 1.00 116.60 ? 3213 ASP A N     1 
ATOM   14008 C  CA    . ASP A 1 3213 ? 158.746 98.378  228.958 1.00 115.54 ? 3213 ASP A CA    1 
ATOM   14009 C  C     . ASP A 1 3213 ? 157.561 97.499  229.338 1.00 115.15 ? 3213 ASP A C     1 
ATOM   14010 O  O     . ASP A 1 3213 ? 157.712 96.535  230.098 1.00 113.89 ? 3213 ASP A O     1 
ATOM   14011 C  CB    . ASP A 1 3213 ? 158.815 99.609  229.862 1.00 114.53 ? 3213 ASP A CB    1 
ATOM   14012 C  CG    . ASP A 1 3213 ? 160.155 100.314 229.784 1.00 111.78 ? 3213 ASP A CG    1 
ATOM   14013 O  OD1   . ASP A 1 3213 ? 161.162 99.647  229.465 1.00 106.09 ? 3213 ASP A OD1   1 
ATOM   14014 O  OD2   . ASP A 1 3213 ? 160.201 101.535 230.043 1.00 111.23 ? 3213 ASP A OD2   1 
ATOM   14015 N  N     . GLN A 1 3214 ? 156.371 97.821  228.824 1.00 115.04 ? 3214 GLN A N     1 
ATOM   14016 C  CA    . GLN A 1 3214 ? 155.184 97.036  229.148 1.00 114.83 ? 3214 GLN A CA    1 
ATOM   14017 C  C     . GLN A 1 3214 ? 155.291 95.616  228.604 1.00 117.14 ? 3214 GLN A C     1 
ATOM   14018 O  O     . GLN A 1 3214 ? 155.036 94.644  229.323 1.00 117.74 ? 3214 GLN A O     1 
ATOM   14019 C  CB    . GLN A 1 3214 ? 153.933 97.728  228.605 1.00 110.52 ? 3214 GLN A CB    1 
ATOM   14020 C  CG    . GLN A 1 3214 ? 153.511 98.948  229.403 1.00 111.48 ? 3214 GLN A CG    1 
ATOM   14021 C  CD    . GLN A 1 3214 ? 153.199 98.614  230.848 1.00 112.40 ? 3214 GLN A CD    1 
ATOM   14022 O  OE1   . GLN A 1 3214 ? 152.402 97.721  231.132 1.00 112.43 ? 3214 GLN A OE1   1 
ATOM   14023 N  NE2   . GLN A 1 3214 ? 153.828 99.333  231.771 1.00 108.49 ? 3214 GLN A NE2   1 
ATOM   14024 N  N     . VAL A 1 3215 ? 155.668 95.475  227.331 1.00 118.02 ? 3215 VAL A N     1 
ATOM   14025 C  CA    . VAL A 1 3215 ? 155.763 94.141  226.743 1.00 116.78 ? 3215 VAL A CA    1 
ATOM   14026 C  C     . VAL A 1 3215 ? 156.877 93.338  227.404 1.00 118.37 ? 3215 VAL A C     1 
ATOM   14027 O  O     . VAL A 1 3215 ? 156.831 92.102  227.426 1.00 117.92 ? 3215 VAL A O     1 
ATOM   14028 C  CB    . VAL A 1 3215 ? 155.953 94.231  225.217 1.00 113.90 ? 3215 VAL A CB    1 
ATOM   14029 C  CG1   . VAL A 1 3215 ? 154.884 95.118  224.604 1.00 113.42 ? 3215 VAL A CG1   1 
ATOM   14030 C  CG2   . VAL A 1 3215 ? 157.340 94.743  224.870 1.00 112.04 ? 3215 VAL A CG2   1 
ATOM   14031 N  N     . GLU A 1 3216 ? 157.893 94.016  227.945 1.00 118.80 ? 3216 GLU A N     1 
ATOM   14032 C  CA    . GLU A 1 3216 ? 158.936 93.314  228.684 1.00 118.85 ? 3216 GLU A CA    1 
ATOM   14033 C  C     . GLU A 1 3216 ? 158.387 92.707  229.969 1.00 117.97 ? 3216 GLU A C     1 
ATOM   14034 O  O     . GLU A 1 3216 ? 158.736 91.575  230.326 1.00 115.94 ? 3216 GLU A O     1 
ATOM   14035 C  CB    . GLU A 1 3216 ? 160.094 94.265  228.986 1.00 118.30 ? 3216 GLU A CB    1 
ATOM   14036 C  CG    . GLU A 1 3216 ? 161.421 93.570  229.247 1.00 115.25 ? 3216 GLU A CG    1 
ATOM   14037 C  CD    . GLU A 1 3216 ? 161.595 93.168  230.698 1.00 114.15 ? 3216 GLU A CD    1 
ATOM   14038 O  OE1   . GLU A 1 3216 ? 161.029 93.850  231.577 1.00 112.50 ? 3216 GLU A OE1   1 
ATOM   14039 O  OE2   . GLU A 1 3216 ? 162.299 92.170  230.959 1.00 110.86 ? 3216 GLU A OE2   1 
ATOM   14040 N  N     . GLU A 1 3217 ? 157.526 93.442  230.678 1.00 118.46 ? 3217 GLU A N     1 
ATOM   14041 C  CA    . GLU A 1 3217 ? 156.962 92.921  231.918 1.00 120.59 ? 3217 GLU A CA    1 
ATOM   14042 C  C     . GLU A 1 3217 ? 155.867 91.896  231.653 1.00 122.86 ? 3217 GLU A C     1 
ATOM   14043 O  O     . GLU A 1 3217 ? 155.556 91.085  232.533 1.00 122.46 ? 3217 GLU A O     1 
ATOM   14044 C  CB    . GLU A 1 3217 ? 156.429 94.067  232.780 1.00 119.73 ? 3217 GLU A CB    1 
ATOM   14045 C  CG    . GLU A 1 3217 ? 154.987 94.453  232.498 1.00 121.97 ? 3217 GLU A CG    1 
ATOM   14046 C  CD    . GLU A 1 3217 ? 154.502 95.586  233.381 1.00 121.78 ? 3217 GLU A CD    1 
ATOM   14047 O  OE1   . GLU A 1 3217 ? 155.333 96.174  234.105 1.00 121.22 ? 3217 GLU A OE1   1 
ATOM   14048 O  OE2   . GLU A 1 3217 ? 153.291 95.888  233.351 1.00 120.76 ? 3217 GLU A OE2   1 
ATOM   14049 N  N     . LEU A 1 3218 ? 155.271 91.915  230.458 1.00 122.02 ? 3218 LEU A N     1 
ATOM   14050 C  CA    . LEU A 1 3218 ? 154.284 90.896  230.113 1.00 121.98 ? 3218 LEU A CA    1 
ATOM   14051 C  C     . LEU A 1 3218 ? 154.925 89.522  229.980 1.00 123.83 ? 3218 LEU A C     1 
ATOM   14052 O  O     . LEU A 1 3218 ? 154.293 88.509  230.302 1.00 124.35 ? 3218 LEU A O     1 
ATOM   14053 C  CB    . LEU A 1 3218 ? 153.558 91.274  228.822 1.00 120.25 ? 3218 LEU A CB    1 
ATOM   14054 C  CG    . LEU A 1 3218 ? 152.152 91.862  228.973 1.00 115.80 ? 3218 LEU A CG    1 
ATOM   14055 C  CD1   . LEU A 1 3218 ? 152.189 93.237  229.623 1.00 110.71 ? 3218 LEU A CD1   1 
ATOM   14056 C  CD2   . LEU A 1 3218 ? 151.448 91.922  227.625 1.00 112.38 ? 3218 LEU A CD2   1 
ATOM   14057 N  N     . ARG A 1 3219 ? 156.171 89.464  229.502 1.00 123.02 ? 3219 ARG A N     1 
ATOM   14058 C  CA    . ARG A 1 3219 ? 156.876 88.189  229.427 1.00 122.66 ? 3219 ARG A CA    1 
ATOM   14059 C  C     . ARG A 1 3219 ? 157.087 87.596  230.815 1.00 124.57 ? 3219 ARG A C     1 
ATOM   14060 O  O     . ARG A 1 3219 ? 156.918 86.387  231.012 1.00 124.93 ? 3219 ARG A O     1 
ATOM   14061 C  CB    . ARG A 1 3219 ? 158.212 88.369  228.709 1.00 116.85 ? 3219 ARG A CB    1 
ATOM   14062 C  CG    . ARG A 1 3219 ? 158.118 88.282  227.195 1.00 115.14 ? 3219 ARG A CG    1 
ATOM   14063 C  CD    . ARG A 1 3219 ? 159.497 88.246  226.558 1.00 116.06 ? 3219 ARG A CD    1 
ATOM   14064 N  NE    . ARG A 1 3219 ? 160.296 89.410  226.922 1.00 118.78 ? 3219 ARG A NE    1 
ATOM   14065 C  CZ    . ARG A 1 3219 ? 160.628 90.382  226.083 1.00 116.00 ? 3219 ARG A CZ    1 
ATOM   14066 N  NH1   . ARG A 1 3219 ? 160.246 90.363  224.816 1.00 106.53 ? 3219 ARG A NH1   1 
ATOM   14067 N  NH2   . ARG A 1 3219 ? 161.361 91.399  226.527 1.00 116.08 ? 3219 ARG A NH2   1 
ATOM   14068 N  N     . ARG A 1 3220 ? 157.465 88.431  231.787 1.00 124.08 ? 3220 ARG A N     1 
ATOM   14069 C  CA    . ARG A 1 3220 ? 157.585 87.958  233.162 1.00 124.44 ? 3220 ARG A CA    1 
ATOM   14070 C  C     . ARG A 1 3220 ? 156.235 87.510  233.705 1.00 125.83 ? 3220 ARG A C     1 
ATOM   14071 O  O     . ARG A 1 3220 ? 156.140 86.478  234.381 1.00 124.84 ? 3220 ARG A O     1 
ATOM   14072 C  CB    . ARG A 1 3220 ? 158.187 89.055  234.042 1.00 123.26 ? 3220 ARG A CB    1 
ATOM   14073 C  CG    . ARG A 1 3220 ? 157.928 88.879  235.530 1.00 120.84 ? 3220 ARG A CG    1 
ATOM   14074 C  CD    . ARG A 1 3220 ? 157.720 90.220  236.217 1.00 119.12 ? 3220 ARG A CD    1 
ATOM   14075 N  NE    . ARG A 1 3220 ? 156.633 90.983  235.616 1.00 125.54 ? 3220 ARG A NE    1 
ATOM   14076 C  CZ    . ARG A 1 3220 ? 155.346 90.772  235.855 1.00 124.73 ? 3220 ARG A CZ    1 
ATOM   14077 N  NH1   . ARG A 1 3220 ? 154.943 89.825  236.686 1.00 122.26 ? 3220 ARG A NH1   1 
ATOM   14078 N  NH2   . ARG A 1 3220 ? 154.440 91.531  235.245 1.00 120.07 ? 3220 ARG A NH2   1 
ATOM   14079 N  N     . ASP A 1 3221 ? 155.177 88.271  233.415 1.00 125.90 ? 3221 ASP A N     1 
ATOM   14080 C  CA    . ASP A 1 3221 ? 153.835 87.861  233.817 1.00 126.20 ? 3221 ASP A CA    1 
ATOM   14081 C  C     . ASP A 1 3221 ? 153.429 86.566  233.126 1.00 128.88 ? 3221 ASP A C     1 
ATOM   14082 O  O     . ASP A 1 3221 ? 152.775 85.709  233.731 1.00 127.65 ? 3221 ASP A O     1 
ATOM   14083 C  CB    . ASP A 1 3221 ? 152.833 88.974  233.510 1.00 123.37 ? 3221 ASP A CB    1 
ATOM   14084 C  CG    . ASP A 1 3221 ? 151.427 88.638  233.971 1.00 121.36 ? 3221 ASP A CG    1 
ATOM   14085 O  OD1   . ASP A 1 3221 ? 150.703 87.946  233.225 1.00 118.92 ? 3221 ASP A OD1   1 
ATOM   14086 O  OD2   . ASP A 1 3221 ? 151.047 89.066  235.081 1.00 119.55 ? 3221 ASP A OD2   1 
ATOM   14087 N  N     . LEU A 1 3222 ? 153.801 86.411  231.853 1.00 130.11 ? 3222 LEU A N     1 
ATOM   14088 C  CA    . LEU A 1 3222 ? 153.505 85.173  231.139 1.00 130.34 ? 3222 LEU A CA    1 
ATOM   14089 C  C     . LEU A 1 3222 ? 154.210 83.984  231.779 1.00 129.55 ? 3222 LEU A C     1 
ATOM   14090 O  O     . LEU A 1 3222 ? 153.620 82.906  231.921 1.00 128.18 ? 3222 LEU A O     1 
ATOM   14091 C  CB    . LEU A 1 3222 ? 153.906 85.310  229.670 1.00 130.32 ? 3222 LEU A CB    1 
ATOM   14092 C  CG    . LEU A 1 3222 ? 153.721 84.073  228.789 1.00 128.13 ? 3222 LEU A CG    1 
ATOM   14093 C  CD1   . LEU A 1 3222 ? 152.276 83.951  228.337 1.00 125.14 ? 3222 LEU A CD1   1 
ATOM   14094 C  CD2   . LEU A 1 3222 ? 154.659 84.121  227.592 1.00 117.78 ? 3222 LEU A CD2   1 
ATOM   14095 N  N     . ARG A 1 3223 ? 155.476 84.158  232.167 1.00 128.80 ? 3223 ARG A N     1 
ATOM   14096 C  CA    . ARG A 1 3223 ? 156.206 83.072  232.814 1.00 126.57 ? 3223 ARG A CA    1 
ATOM   14097 C  C     . ARG A 1 3223 ? 155.608 82.740  234.176 1.00 127.39 ? 3223 ARG A C     1 
ATOM   14098 O  O     . ARG A 1 3223 ? 155.505 81.564  234.546 1.00 127.28 ? 3223 ARG A O     1 
ATOM   14099 C  CB    . ARG A 1 3223 ? 157.684 83.438  232.947 1.00 122.39 ? 3223 ARG A CB    1 
ATOM   14100 C  CG    . ARG A 1 3223 ? 158.541 82.337  233.554 1.00 117.69 ? 3223 ARG A CG    1 
ATOM   14101 C  CD    . ARG A 1 3223 ? 159.828 82.891  234.146 1.00 116.37 ? 3223 ARG A CD    1 
ATOM   14102 N  NE    . ARG A 1 3223 ? 159.617 84.148  234.854 1.00 120.34 ? 3223 ARG A NE    1 
ATOM   14103 C  CZ    . ARG A 1 3223 ? 159.132 84.244  236.084 1.00 121.25 ? 3223 ARG A CZ    1 
ATOM   14104 N  NH1   . ARG A 1 3223 ? 158.791 83.171  236.779 1.00 117.43 ? 3223 ARG A NH1   1 
ATOM   14105 N  NH2   . ARG A 1 3223 ? 158.988 85.447  236.632 1.00 120.55 ? 3223 ARG A NH2   1 
ATOM   14106 N  N     . ILE A 1 3224 ? 155.215 83.763  234.939 1.00 127.26 ? 3224 ILE A N     1 
ATOM   14107 C  CA    . ILE A 1 3224 ? 154.576 83.526  236.231 1.00 128.35 ? 3224 ILE A CA    1 
ATOM   14108 C  C     . ILE A 1 3224 ? 153.252 82.798  236.044 1.00 130.00 ? 3224 ILE A C     1 
ATOM   14109 O  O     . ILE A 1 3224 ? 152.933 81.857  236.781 1.00 129.01 ? 3224 ILE A O     1 
ATOM   14110 C  CB    . ILE A 1 3224 ? 154.391 84.856  236.988 1.00 124.49 ? 3224 ILE A CB    1 
ATOM   14111 C  CG1   . ILE A 1 3224 ? 155.747 85.421  237.413 1.00 122.14 ? 3224 ILE A CG1   1 
ATOM   14112 C  CG2   . ILE A 1 3224 ? 153.490 84.665  238.199 1.00 116.94 ? 3224 ILE A CG2   1 
ATOM   14113 C  CD1   . ILE A 1 3224 ? 155.654 86.727  238.171 1.00 115.80 ? 3224 ILE A CD1   1 
ATOM   14114 N  N     . LYS A 1 3225 ? 152.461 83.220  235.054 1.00 129.47 ? 3225 LYS A N     1 
ATOM   14115 C  CA    . LYS A 1 3225 ? 151.190 82.556  234.785 1.00 129.48 ? 3225 LYS A CA    1 
ATOM   14116 C  C     . LYS A 1 3225 ? 151.402 81.110  234.351 1.00 131.33 ? 3225 LYS A C     1 
ATOM   14117 O  O     . LYS A 1 3225 ? 150.638 80.219  234.741 1.00 131.67 ? 3225 LYS A O     1 
ATOM   14118 C  CB    . LYS A 1 3225 ? 150.410 83.328  233.722 1.00 128.83 ? 3225 LYS A CB    1 
ATOM   14119 C  CG    . LYS A 1 3225 ? 149.689 84.560  234.250 1.00 126.31 ? 3225 LYS A CG    1 
ATOM   14120 C  CD    . LYS A 1 3225 ? 148.541 84.185  235.179 1.00 123.01 ? 3225 LYS A CD    1 
ATOM   14121 C  CE    . LYS A 1 3225 ? 147.579 83.203  234.524 1.00 126.19 ? 3225 LYS A CE    1 
ATOM   14122 N  NZ    . LYS A 1 3225 ? 147.264 83.573  233.115 1.00 126.21 ? 3225 LYS A NZ    1 
ATOM   14123 N  N     . SER A 1 3226 ? 152.429 80.860  233.534 1.00 132.12 ? 3226 SER A N     1 
ATOM   14124 C  CA    . SER A 1 3226 ? 152.728 79.493  233.119 1.00 130.48 ? 3226 SER A CA    1 
ATOM   14125 C  C     . SER A 1 3226 ? 153.114 78.628  234.312 1.00 131.19 ? 3226 SER A C     1 
ATOM   14126 O  O     . SER A 1 3226 ? 152.692 77.470  234.411 1.00 128.90 ? 3226 SER A O     1 
ATOM   14127 C  CB    . SER A 1 3226 ? 153.841 79.493  232.072 1.00 123.87 ? 3226 SER A CB    1 
ATOM   14128 O  OG    . SER A 1 3226 ? 155.041 80.025  232.605 1.00 122.24 ? 3226 SER A OG    1 
ATOM   14129 N  N     . GLN A 1 3227 ? 153.924 79.171  235.225 1.00 131.24 ? 3227 GLN A N     1 
ATOM   14130 C  CA    . GLN A 1 3227 ? 154.284 78.432  236.430 1.00 129.49 ? 3227 GLN A CA    1 
ATOM   14131 C  C     . GLN A 1 3227 ? 153.059 78.160  237.294 1.00 131.08 ? 3227 GLN A C     1 
ATOM   14132 O  O     . GLN A 1 3227 ? 152.920 77.072  237.865 1.00 129.16 ? 3227 GLN A O     1 
ATOM   14133 C  CB    . GLN A 1 3227 ? 155.343 79.201  237.221 1.00 127.21 ? 3227 GLN A CB    1 
ATOM   14134 C  CG    . GLN A 1 3227 ? 155.772 78.530  238.518 1.00 127.98 ? 3227 GLN A CG    1 
ATOM   14135 C  CD    . GLN A 1 3227 ? 155.007 79.041  239.725 1.00 130.69 ? 3227 GLN A CD    1 
ATOM   14136 O  OE1   . GLN A 1 3227 ? 154.203 79.966  239.618 1.00 132.85 ? 3227 GLN A OE1   1 
ATOM   14137 N  NE2   . GLN A 1 3227 ? 155.255 78.437  240.882 1.00 125.24 ? 3227 GLN A NE2   1 
ATOM   14138 N  N     . GLU A 1 3228 ? 152.161 79.143  237.406 1.00 132.74 ? 3228 GLU A N     1 
ATOM   14139 C  CA    . GLU A 1 3228 ? 150.939 78.947  238.179 1.00 132.36 ? 3228 GLU A CA    1 
ATOM   14140 C  C     . GLU A 1 3228 ? 150.072 77.851  237.571 1.00 134.26 ? 3228 GLU A C     1 
ATOM   14141 O  O     . GLU A 1 3228 ? 149.488 77.037  238.296 1.00 135.24 ? 3228 GLU A O     1 
ATOM   14142 C  CB    . GLU A 1 3228 ? 150.162 80.261  238.271 1.00 130.00 ? 3228 GLU A CB    1 
ATOM   14143 C  CG    . GLU A 1 3228 ? 148.799 80.136  238.933 1.00 130.39 ? 3228 GLU A CG    1 
ATOM   14144 C  CD    . GLU A 1 3228 ? 147.946 81.376  238.750 1.00 132.46 ? 3228 GLU A CD    1 
ATOM   14145 O  OE1   . GLU A 1 3228 ? 148.392 82.307  238.046 1.00 132.88 ? 3228 GLU A OE1   1 
ATOM   14146 O  OE2   . GLU A 1 3228 ? 146.831 81.420  239.310 1.00 130.51 ? 3228 GLU A OE2   1 
ATOM   14147 N  N     . LEU A 1 3229 ? 149.974 77.817  236.240 1.00 134.59 ? 3229 LEU A N     1 
ATOM   14148 C  CA    . LEU A 1 3229 ? 149.183 76.781  235.581 1.00 132.43 ? 3229 LEU A CA    1 
ATOM   14149 C  C     . LEU A 1 3229 ? 149.758 75.395  235.846 1.00 132.14 ? 3229 LEU A C     1 
ATOM   14150 O  O     . LEU A 1 3229 ? 149.010 74.442  236.096 1.00 131.11 ? 3229 LEU A O     1 
ATOM   14151 C  CB    . LEU A 1 3229 ? 149.111 77.051  234.079 1.00 130.19 ? 3229 LEU A CB    1 
ATOM   14152 C  CG    . LEU A 1 3229 ? 148.347 76.017  233.250 1.00 127.97 ? 3229 LEU A CG    1 
ATOM   14153 C  CD1   . LEU A 1 3229 ? 146.979 75.749  233.860 1.00 127.84 ? 3229 LEU A CD1   1 
ATOM   14154 C  CD2   . LEU A 1 3229 ? 148.216 76.470  231.806 1.00 123.30 ? 3229 LEU A CD2   1 
ATOM   14155 N  N     . GLU A 1 3230 ? 151.085 75.262  235.789 1.00 131.61 ? 3230 GLU A N     1 
ATOM   14156 C  CA    . GLU A 1 3230 ? 151.710 73.967  236.038 1.00 129.46 ? 3230 GLU A CA    1 
ATOM   14157 C  C     . GLU A 1 3230 ? 151.451 73.493  237.462 1.00 132.32 ? 3230 GLU A C     1 
ATOM   14158 O  O     . GLU A 1 3230 ? 151.186 72.307  237.690 1.00 131.45 ? 3230 GLU A O     1 
ATOM   14159 C  CB    . GLU A 1 3230 ? 153.212 74.048  235.764 1.00 126.09 ? 3230 GLU A CB    1 
ATOM   14160 C  CG    . GLU A 1 3230 ? 153.564 74.310  234.309 1.00 127.38 ? 3230 GLU A CG    1 
ATOM   14161 C  CD    . GLU A 1 3230 ? 154.981 74.822  234.135 1.00 125.35 ? 3230 GLU A CD    1 
ATOM   14162 O  OE1   . GLU A 1 3230 ? 155.682 74.991  235.155 1.00 124.59 ? 3230 GLU A OE1   1 
ATOM   14163 O  OE2   . GLU A 1 3230 ? 155.393 75.055  232.980 1.00 121.99 ? 3230 GLU A OE2   1 
ATOM   14164 N  N     . VAL A 1 3231 ? 151.527 74.405  238.434 1.00 133.95 ? 3231 VAL A N     1 
ATOM   14165 C  CA    . VAL A 1 3231 ? 151.275 74.036  239.825 1.00 131.13 ? 3231 VAL A CA    1 
ATOM   14166 C  C     . VAL A 1 3231 ? 149.824 73.604  240.006 1.00 131.75 ? 3231 VAL A C     1 
ATOM   14167 O  O     . VAL A 1 3231 ? 149.534 72.591  240.653 1.00 130.69 ? 3231 VAL A O     1 
ATOM   14168 C  CB    . VAL A 1 3231 ? 151.639 75.202  240.763 1.00 125.94 ? 3231 VAL A CB    1 
ATOM   14169 C  CG1   . VAL A 1 3231 ? 151.108 74.948  242.166 1.00 119.69 ? 3231 VAL A CG1   1 
ATOM   14170 C  CG2   . VAL A 1 3231 ? 153.146 75.411  240.787 1.00 121.93 ? 3231 VAL A CG2   1 
ATOM   14171 N  N     . LYS A 1 3232 ? 148.890 74.369  239.434 1.00 133.00 ? 3232 LYS A N     1 
ATOM   14172 C  CA    . LYS A 1 3232 ? 147.474 74.037  239.564 1.00 133.34 ? 3232 LYS A CA    1 
ATOM   14173 C  C     . LYS A 1 3232 ? 147.155 72.705  238.896 1.00 135.91 ? 3232 LYS A C     1 
ATOM   14174 O  O     . LYS A 1 3232 ? 146.413 71.883  239.446 1.00 135.70 ? 3232 LYS A O     1 
ATOM   14175 C  CB    . LYS A 1 3232 ? 146.617 75.156  238.971 1.00 130.22 ? 3232 LYS A CB    1 
ATOM   14176 C  CG    . LYS A 1 3232 ? 146.655 76.456  239.758 1.00 128.91 ? 3232 LYS A CG    1 
ATOM   14177 C  CD    . LYS A 1 3232 ? 145.862 76.344  241.049 1.00 124.56 ? 3232 LYS A CD    1 
ATOM   14178 C  CE    . LYS A 1 3232 ? 145.677 77.704  241.701 1.00 119.38 ? 3232 LYS A CE    1 
ATOM   14179 N  NZ    . LYS A 1 3232 ? 144.742 77.643  242.858 1.00 117.55 ? 3232 LYS A NZ    1 
ATOM   14180 N  N     . ASN A 1 3233 ? 147.706 72.475  237.701 1.00 136.66 ? 3233 ASN A N     1 
ATOM   14181 C  CA    . ASN A 1 3233 ? 147.424 71.234  236.987 1.00 133.91 ? 3233 ASN A CA    1 
ATOM   14182 C  C     . ASN A 1 3233 ? 148.055 70.035  237.686 1.00 134.49 ? 3233 ASN A C     1 
ATOM   14183 O  O     . ASN A 1 3233 ? 147.415 68.985  237.824 1.00 133.18 ? 3233 ASN A O     1 
ATOM   14184 C  CB    . ASN A 1 3233 ? 147.915 71.336  235.543 1.00 128.88 ? 3233 ASN A CB    1 
ATOM   14185 C  CG    . ASN A 1 3233 ? 147.394 70.211  234.668 1.00 125.55 ? 3233 ASN A CG    1 
ATOM   14186 O  OD1   . ASN A 1 3233 ? 147.786 69.054  234.822 1.00 126.11 ? 3233 ASN A OD1   1 
ATOM   14187 N  ND2   . ASN A 1 3233 ? 146.504 70.548  233.742 1.00 122.63 ? 3233 ASN A ND2   1 
ATOM   14188 N  N     . ALA A 1 3234 ? 149.308 70.168  238.128 1.00 135.33 ? 3234 ALA A N     1 
ATOM   14189 C  CA    . ALA A 1 3234 ? 149.977 69.056  238.797 1.00 131.68 ? 3234 ALA A CA    1 
ATOM   14190 C  C     . ALA A 1 3234 ? 149.296 68.710  240.114 1.00 133.81 ? 3234 ALA A C     1 
ATOM   14191 O  O     . ALA A 1 3234 ? 149.114 67.529  240.435 1.00 133.04 ? 3234 ALA A O     1 
ATOM   14192 C  CB    . ALA A 1 3234 ? 151.451 69.389  239.026 1.00 124.57 ? 3234 ALA A CB    1 
ATOM   14193 N  N     . ALA A 1 3235 ? 148.917 69.725  240.894 1.00 134.64 ? 3235 ALA A N     1 
ATOM   14194 C  CA    . ALA A 1 3235 ? 148.243 69.470  242.163 1.00 131.69 ? 3235 ALA A CA    1 
ATOM   14195 C  C     . ALA A 1 3235 ? 146.886 68.812  241.946 1.00 133.36 ? 3235 ALA A C     1 
ATOM   14196 O  O     . ALA A 1 3235 ? 146.506 67.898  242.687 1.00 131.51 ? 3235 ALA A O     1 
ATOM   14197 C  CB    . ALA A 1 3235 ? 148.089 70.772  242.949 1.00 124.01 ? 3235 ALA A CB    1 
ATOM   14198 N  N     . ALA A 1 3236 ? 146.138 69.269  240.938 1.00 134.43 ? 3236 ALA A N     1 
ATOM   14199 C  CA    . ALA A 1 3236 ? 144.827 68.688  240.667 1.00 132.47 ? 3236 ALA A CA    1 
ATOM   14200 C  C     . ALA A 1 3236 ? 144.943 67.231  240.235 1.00 134.70 ? 3236 ALA A C     1 
ATOM   14201 O  O     . ALA A 1 3236 ? 144.182 66.376  240.702 1.00 133.08 ? 3236 ALA A O     1 
ATOM   14202 C  CB    . ALA A 1 3236 ? 144.100 69.509  239.603 1.00 128.33 ? 3236 ALA A CB    1 
ATOM   14203 N  N     . ASN A 1 3237 ? 145.887 66.930  239.340 1.00 135.58 ? 3237 ASN A N     1 
ATOM   14204 C  CA    . ASN A 1 3237 ? 146.062 65.553  238.887 1.00 132.05 ? 3237 ASN A CA    1 
ATOM   14205 C  C     . ASN A 1 3237 ? 146.548 64.653  240.017 1.00 131.40 ? 3237 ASN A C     1 
ATOM   14206 O  O     . ASN A 1 3237 ? 146.072 63.521  240.164 1.00 129.58 ? 3237 ASN A O     1 
ATOM   14207 C  CB    . ASN A 1 3237 ? 147.032 65.506  237.706 1.00 127.65 ? 3237 ASN A CB    1 
ATOM   14208 C  CG    . ASN A 1 3237 ? 146.563 66.344  236.534 1.00 127.33 ? 3237 ASN A CG    1 
ATOM   14209 O  OD1   . ASN A 1 3237 ? 145.533 67.015  236.607 1.00 127.72 ? 3237 ASN A OD1   1 
ATOM   14210 N  ND2   . ASN A 1 3237 ? 147.318 66.309  235.442 1.00 122.79 ? 3237 ASN A ND2   1 
ATOM   14211 N  N     . ASP A 1 3238 ? 147.499 65.134  240.822 1.00 132.96 ? 3238 ASP A N     1 
ATOM   14212 C  CA    . ASP A 1 3238 ? 147.980 64.345  241.951 1.00 131.41 ? 3238 ASP A CA    1 
ATOM   14213 C  C     . ASP A 1 3238 ? 146.887 64.120  242.987 1.00 132.04 ? 3238 ASP A C     1 
ATOM   14214 O  O     . ASP A 1 3238 ? 146.774 63.018  243.537 1.00 129.06 ? 3238 ASP A O     1 
ATOM   14215 C  CB    . ASP A 1 3238 ? 149.190 65.025  242.593 1.00 130.24 ? 3238 ASP A CB    1 
ATOM   14216 C  CG    . ASP A 1 3238 ? 150.406 65.024  241.689 1.00 130.65 ? 3238 ASP A CG    1 
ATOM   14217 O  OD1   . ASP A 1 3238 ? 150.326 64.450  240.583 1.00 129.74 ? 3238 ASP A OD1   1 
ATOM   14218 O  OD2   . ASP A 1 3238 ? 151.443 65.597  242.084 1.00 129.38 ? 3238 ASP A OD2   1 
ATOM   14219 N  N     . LYS A 1 3239 ? 146.078 65.144  243.269 1.00 134.86 ? 3239 LYS A N     1 
ATOM   14220 C  CA    . LYS A 1 3239 ? 144.971 64.972  244.203 1.00 134.48 ? 3239 LYS A CA    1 
ATOM   14221 C  C     . LYS A 1 3239 ? 143.891 64.064  243.630 1.00 133.27 ? 3239 LYS A C     1 
ATOM   14222 O  O     . LYS A 1 3239 ? 143.217 63.353  244.385 1.00 130.58 ? 3239 LYS A O     1 
ATOM   14223 C  CB    . LYS A 1 3239 ? 144.385 66.332  244.580 1.00 132.36 ? 3239 LYS A CB    1 
ATOM   14224 C  CG    . LYS A 1 3239 ? 145.197 67.088  245.620 1.00 130.34 ? 3239 LYS A CG    1 
ATOM   14225 C  CD    . LYS A 1 3239 ? 144.384 68.204  246.255 1.00 127.80 ? 3239 LYS A CD    1 
ATOM   14226 C  CE    . LYS A 1 3239 ? 145.208 68.972  247.277 1.00 121.43 ? 3239 LYS A CE    1 
ATOM   14227 N  NZ    . LYS A 1 3239 ? 144.432 70.082  247.896 1.00 114.30 ? 3239 LYS A NZ    1 
ATOM   14228 N  N     . LEU A 1 3240 ? 143.706 64.076  242.307 1.00 133.86 ? 3240 LEU A N     1 
ATOM   14229 C  CA    . LEU A 1 3240 ? 142.777 63.141  241.682 1.00 133.33 ? 3240 LEU A CA    1 
ATOM   14230 C  C     . LEU A 1 3240 ? 143.253 61.701  241.824 1.00 131.48 ? 3240 LEU A C     1 
ATOM   14231 O  O     . LEU A 1 3240 ? 142.431 60.777  241.849 1.00 129.04 ? 3240 LEU A O     1 
ATOM   14232 C  CB    . LEU A 1 3240 ? 142.586 63.491  240.206 1.00 131.16 ? 3240 LEU A CB    1 
ATOM   14233 C  CG    . LEU A 1 3240 ? 141.559 64.576  239.879 1.00 127.95 ? 3240 LEU A CG    1 
ATOM   14234 C  CD1   . LEU A 1 3240 ? 141.619 64.942  238.404 1.00 121.93 ? 3240 LEU A CD1   1 
ATOM   14235 C  CD2   . LEU A 1 3240 ? 140.160 64.120  240.262 1.00 122.93 ? 3240 LEU A CD2   1 
ATOM   14236 N  N     . LYS A 1 3241 ? 144.568 61.490  241.915 1.00 132.84 ? 3241 LYS A N     1 
ATOM   14237 C  CA    . LYS A 1 3241 ? 145.104 60.144  242.082 1.00 131.24 ? 3241 LYS A CA    1 
ATOM   14238 C  C     . LYS A 1 3241 ? 144.755 59.547  243.439 1.00 131.02 ? 3241 LYS A C     1 
ATOM   14239 O  O     . LYS A 1 3241 ? 144.863 58.329  243.613 1.00 127.82 ? 3241 LYS A O     1 
ATOM   14240 C  CB    . LYS A 1 3241 ? 146.622 60.159  241.895 1.00 127.51 ? 3241 LYS A CB    1 
ATOM   14241 C  CG    . LYS A 1 3241 ? 147.070 60.335  240.453 1.00 123.45 ? 3241 LYS A CG    1 
ATOM   14242 C  CD    . LYS A 1 3241 ? 148.496 60.858  240.380 1.00 121.83 ? 3241 LYS A CD    1 
ATOM   14243 C  CE    . LYS A 1 3241 ? 148.785 61.488  239.027 1.00 119.43 ? 3241 LYS A CE    1 
ATOM   14244 N  NZ    . LYS A 1 3241 ? 150.112 62.162  239.000 1.00 113.94 ? 3241 LYS A NZ    1 
ATOM   14245 N  N     . LYS A 1 3242 ? 144.345 60.371  244.398 1.00 132.05 ? 3242 LYS A N     1 
ATOM   14246 C  CA    . LYS A 1 3242 ? 143.987 59.892  245.728 1.00 127.37 ? 3242 LYS A CA    1 
ATOM   14247 C  C     . LYS A 1 3242 ? 142.731 59.027  245.682 1.00 122.02 ? 3242 LYS A C     1 
ATOM   14248 O  O     . LYS A 1 3242 ? 141.938 59.110  244.744 0.00 124.03 ? 3242 LYS A O     1 
ATOM   14249 C  CB    . LYS A 1 3242 ? 143.778 61.069  246.683 1.00 125.76 ? 3242 LYS A CB    1 
ATOM   14250 C  CG    . LYS A 1 3242 ? 145.062 61.763  247.109 1.00 124.26 ? 3242 LYS A CG    1 
ATOM   14251 C  CD    . LYS A 1 3242 ? 144.768 63.048  247.865 1.00 124.12 ? 3242 LYS A CD    1 
ATOM   14252 C  CE    . LYS A 1 3242 ? 146.048 63.777  248.236 1.00 118.72 ? 3242 LYS A CE    1 
ATOM   14253 N  NZ    . LYS A 1 3242 ? 145.780 65.165  248.705 1.00 115.27 ? 3242 LYS A NZ    1 
ATOM   14254 N  N     . GLU A 1 3449 ? 134.720 65.978  243.656 1.00 124.29 ? 3449 GLU A N     1 
ATOM   14255 C  CA    . GLU A 1 3449 ? 133.957 67.191  243.923 1.00 128.23 ? 3449 GLU A CA    1 
ATOM   14256 C  C     . GLU A 1 3449 ? 134.879 68.401  244.028 1.00 130.12 ? 3449 GLU A C     1 
ATOM   14257 O  O     . GLU A 1 3449 ? 134.914 69.245  243.132 1.00 130.05 ? 3449 GLU A O     1 
ATOM   14258 C  CB    . GLU A 1 3449 ? 133.136 67.038  245.204 1.00 125.98 ? 3449 GLU A CB    1 
ATOM   14259 C  CG    . GLU A 1 3449 ? 132.296 65.773  245.250 1.00 124.39 ? 3449 GLU A CG    1 
ATOM   14260 C  CD    . GLU A 1 3449 ? 131.495 65.652  246.531 1.00 123.06 ? 3449 GLU A CD    1 
ATOM   14261 O  OE1   . GLU A 1 3449 ? 131.583 66.566  247.377 1.00 120.76 ? 3449 GLU A OE1   1 
ATOM   14262 O  OE2   . GLU A 1 3449 ? 130.779 64.642  246.692 1.00 123.31 ? 3449 GLU A OE2   1 
ATOM   14263 N  N     . GLU A 1 3450 ? 135.622 68.483  245.134 1.00 128.01 ? 3450 GLU A N     1 
ATOM   14264 C  CA    . GLU A 1 3450 ? 136.579 69.573  245.301 1.00 129.14 ? 3450 GLU A CA    1 
ATOM   14265 C  C     . GLU A 1 3450 ? 137.694 69.488  244.266 1.00 133.87 ? 3450 GLU A C     1 
ATOM   14266 O  O     . GLU A 1 3450 ? 138.154 70.515  243.755 1.00 133.65 ? 3450 GLU A O     1 
ATOM   14267 C  CB    . GLU A 1 3450 ? 137.154 69.557  246.717 1.00 126.23 ? 3450 GLU A CB    1 
ATOM   14268 C  CG    . GLU A 1 3450 ? 138.181 70.648  246.980 1.00 124.69 ? 3450 GLU A CG    1 
ATOM   14269 C  CD    . GLU A 1 3450 ? 138.659 70.667  248.419 1.00 118.60 ? 3450 GLU A CD    1 
ATOM   14270 O  OE1   . GLU A 1 3450 ? 138.356 69.708  249.160 1.00 114.19 ? 3450 GLU A OE1   1 
ATOM   14271 O  OE2   . GLU A 1 3450 ? 139.337 71.640  248.808 1.00 112.87 ? 3450 GLU A OE2   1 
ATOM   14272 N  N     . TYR A 1 3451 ? 138.144 68.271  243.949 1.00 135.22 ? 3451 TYR A N     1 
ATOM   14273 C  CA    . TYR A 1 3451 ? 139.163 68.105  242.919 1.00 133.78 ? 3451 TYR A CA    1 
ATOM   14274 C  C     . TYR A 1 3451 ? 138.647 68.523  241.548 1.00 135.23 ? 3451 TYR A C     1 
ATOM   14275 O  O     . TYR A 1 3451 ? 139.429 68.979  240.706 1.00 132.67 ? 3451 TYR A O     1 
ATOM   14276 C  CB    . TYR A 1 3451 ? 139.649 66.657  242.891 1.00 130.31 ? 3451 TYR A CB    1 
ATOM   14277 C  CG    . TYR A 1 3451 ? 139.936 66.090  244.263 1.00 129.56 ? 3451 TYR A CG    1 
ATOM   14278 C  CD1   . TYR A 1 3451 ? 140.940 66.623  245.059 1.00 128.64 ? 3451 TYR A CD1   1 
ATOM   14279 C  CD2   . TYR A 1 3451 ? 139.202 65.022  244.762 1.00 127.48 ? 3451 TYR A CD2   1 
ATOM   14280 C  CE1   . TYR A 1 3451 ? 141.207 66.110  246.314 1.00 128.03 ? 3451 TYR A CE1   1 
ATOM   14281 C  CE2   . TYR A 1 3451 ? 139.461 64.501  246.016 1.00 126.11 ? 3451 TYR A CE2   1 
ATOM   14282 C  CZ    . TYR A 1 3451 ? 140.465 65.049  246.787 1.00 127.52 ? 3451 TYR A CZ    1 
ATOM   14283 O  OH    . TYR A 1 3451 ? 140.727 64.535  248.036 1.00 123.29 ? 3451 TYR A OH    1 
ATOM   14284 N  N     . ALA A 1 3452 ? 137.343 68.372  241.304 1.00 136.36 ? 3452 ALA A N     1 
ATOM   14285 C  CA    . ALA A 1 3452 ? 136.762 68.871  240.062 1.00 133.34 ? 3452 ALA A CA    1 
ATOM   14286 C  C     . ALA A 1 3452 ? 136.848 70.390  239.991 1.00 133.51 ? 3452 ALA A C     1 
ATOM   14287 O  O     . ALA A 1 3452 ? 136.979 70.963  238.904 1.00 131.18 ? 3452 ALA A O     1 
ATOM   14288 C  CB    . ALA A 1 3452 ? 135.312 68.405  239.934 1.00 125.49 ? 3452 ALA A CB    1 
ATOM   14289 N  N     . VAL A 1 3453 ? 136.761 71.060  241.142 1.00 135.41 ? 3453 VAL A N     1 
ATOM   14290 C  CA    . VAL A 1 3453 ? 136.974 72.504  241.175 1.00 132.97 ? 3453 VAL A CA    1 
ATOM   14291 C  C     . VAL A 1 3453 ? 138.429 72.830  240.860 1.00 133.87 ? 3453 VAL A C     1 
ATOM   14292 O  O     . VAL A 1 3453 ? 138.728 73.836  240.204 1.00 134.03 ? 3453 VAL A O     1 
ATOM   14293 C  CB    . VAL A 1 3453 ? 136.544 73.078  242.538 1.00 126.49 ? 3453 VAL A CB    1 
ATOM   14294 C  CG1   . VAL A 1 3453 ? 136.588 74.599  242.514 1.00 118.07 ? 3453 VAL A CG1   1 
ATOM   14295 C  CG2   . VAL A 1 3453 ? 135.153 72.584  242.906 1.00 121.86 ? 3453 VAL A CG2   1 
ATOM   14296 N  N     . LEU A 1 3454 ? 139.354 71.988  241.325 1.00 134.25 ? 3454 LEU A N     1 
ATOM   14297 C  CA    . LEU A 1 3454 ? 140.772 72.215  241.064 1.00 133.19 ? 3454 LEU A CA    1 
ATOM   14298 C  C     . LEU A 1 3454 ? 141.079 72.134  239.573 1.00 133.73 ? 3454 LEU A C     1 
ATOM   14299 O  O     . LEU A 1 3454 ? 141.858 72.936  239.043 1.00 132.24 ? 3454 LEU A O     1 
ATOM   14300 C  CB    . LEU A 1 3454 ? 141.617 71.207  241.844 1.00 129.39 ? 3454 LEU A CB    1 
ATOM   14301 C  CG    . LEU A 1 3454 ? 142.223 71.695  243.161 1.00 124.96 ? 3454 LEU A CG    1 
ATOM   14302 C  CD1   . LEU A 1 3454 ? 141.138 71.960  244.194 1.00 119.31 ? 3454 LEU A CD1   1 
ATOM   14303 C  CD2   . LEU A 1 3454 ? 143.238 70.693  243.689 1.00 122.85 ? 3454 LEU A CD2   1 
ATOM   14304 N  N     . ILE A 1 3455 ? 140.482 71.164  238.877 1.00 134.65 ? 3455 ILE A N     1 
ATOM   14305 C  CA    . ILE A 1 3455 ? 140.717 71.056  237.441 1.00 133.98 ? 3455 ILE A CA    1 
ATOM   14306 C  C     . ILE A 1 3455 ? 139.945 72.130  236.685 1.00 134.68 ? 3455 ILE A C     1 
ATOM   14307 O  O     . ILE A 1 3455 ? 140.326 72.507  235.570 1.00 132.24 ? 3455 ILE A O     1 
ATOM   14308 C  CB    . ILE A 1 3455 ? 140.370 69.641  236.936 1.00 130.99 ? 3455 ILE A CB    1 
ATOM   14309 C  CG1   . ILE A 1 3455 ? 138.856 69.434  236.883 1.00 127.45 ? 3455 ILE A CG1   1 
ATOM   14310 C  CG2   . ILE A 1 3455 ? 141.021 68.586  237.815 1.00 127.35 ? 3455 ILE A CG2   1 
ATOM   14311 C  CD1   . ILE A 1 3455 ? 138.440 68.139  236.222 1.00 118.22 ? 3455 ILE A CD1   1 
ATOM   14312 N  N     . SER A 1 3456 ? 138.854 72.638  237.265 1.00 135.61 ? 3456 SER A N     1 
ATOM   14313 C  CA    . SER A 1 3456 ? 138.109 73.710  236.613 1.00 132.94 ? 3456 SER A CA    1 
ATOM   14314 C  C     . SER A 1 3456 ? 138.872 75.028  236.676 1.00 134.34 ? 3456 SER A C     1 
ATOM   14315 O  O     . SER A 1 3456 ? 138.959 75.749  235.676 1.00 131.79 ? 3456 SER A O     1 
ATOM   14316 C  CB    . SER A 1 3456 ? 136.729 73.860  237.250 1.00 127.35 ? 3456 SER A CB    1 
ATOM   14317 O  OG    . SER A 1 3456 ? 136.829 74.359  238.571 1.00 128.40 ? 3456 SER A OG    1 
ATOM   14318 N  N     . GLU A 1 3457 ? 139.428 75.360  237.844 1.00 135.13 ? 3457 GLU A N     1 
ATOM   14319 C  CA    . GLU A 1 3457 ? 140.239 76.568  237.951 1.00 133.51 ? 3457 GLU A CA    1 
ATOM   14320 C  C     . GLU A 1 3457 ? 141.537 76.437  237.166 1.00 137.34 ? 3457 GLU A C     1 
ATOM   14321 O  O     . GLU A 1 3457 ? 142.075 77.443  236.690 1.00 137.00 ? 3457 GLU A O     1 
ATOM   14322 C  CB    . GLU A 1 3457 ? 140.522 76.891  239.420 1.00 129.58 ? 3457 GLU A CB    1 
ATOM   14323 C  CG    . GLU A 1 3457 ? 141.452 75.913  240.120 1.00 130.04 ? 3457 GLU A CG    1 
ATOM   14324 C  CD    . GLU A 1 3457 ? 141.613 76.217  241.597 1.00 126.45 ? 3457 GLU A CD    1 
ATOM   14325 O  OE1   . GLU A 1 3457 ? 140.973 77.174  242.082 1.00 119.93 ? 3457 GLU A OE1   1 
ATOM   14326 O  OE2   . GLU A 1 3457 ? 142.379 75.499  242.273 1.00 124.46 ? 3457 GLU A OE2   1 
ATOM   14327 N  N     . ALA A 1 3458 ? 142.054 75.214  237.023 1.00 137.84 ? 3458 ALA A N     1 
ATOM   14328 C  CA    . ALA A 1 3458 ? 143.210 74.997  236.159 1.00 136.66 ? 3458 ALA A CA    1 
ATOM   14329 C  C     . ALA A 1 3458 ? 142.873 75.315  234.709 1.00 137.21 ? 3458 ALA A C     1 
ATOM   14330 O  O     . ALA A 1 3458 ? 143.684 75.911  233.990 1.00 136.64 ? 3458 ALA A O     1 
ATOM   14331 C  CB    . ALA A 1 3458 ? 143.707 73.558  236.296 1.00 130.27 ? 3458 ALA A CB    1 
ATOM   14332 N  N     . GLN A 1 3459 ? 141.678 74.922  234.261 1.00 136.25 ? 3459 GLN A N     1 
ATOM   14333 C  CA    . GLN A 1 3459 ? 141.241 75.265  232.911 1.00 134.34 ? 3459 GLN A CA    1 
ATOM   14334 C  C     . GLN A 1 3459 ? 141.067 76.771  232.758 1.00 135.26 ? 3459 GLN A C     1 
ATOM   14335 O  O     . GLN A 1 3459 ? 141.323 77.328  231.684 1.00 132.49 ? 3459 GLN A O     1 
ATOM   14336 C  CB    . GLN A 1 3459 ? 139.939 74.536  232.580 1.00 131.24 ? 3459 GLN A CB    1 
ATOM   14337 C  CG    . GLN A 1 3459 ? 139.544 74.603  231.114 1.00 126.35 ? 3459 GLN A CG    1 
ATOM   14338 C  CD    . GLN A 1 3459 ? 138.334 73.748  230.798 1.00 123.85 ? 3459 GLN A CD    1 
ATOM   14339 O  OE1   . GLN A 1 3459 ? 138.329 72.542  231.045 1.00 125.77 ? 3459 GLN A OE1   1 
ATOM   14340 N  NE2   . GLN A 1 3459 ? 137.297 74.369  230.248 1.00 119.89 ? 3459 GLN A NE2   1 
ATOM   14341 N  N     . ALA A 1 3460 ? 140.623 77.446  233.821 1.00 136.30 ? 3460 ALA A N     1 
ATOM   14342 C  CA    . ALA A 1 3460 ? 140.505 78.900  233.779 1.00 134.12 ? 3460 ALA A CA    1 
ATOM   14343 C  C     . ALA A 1 3460 ? 141.866 79.556  233.586 1.00 134.99 ? 3460 ALA A C     1 
ATOM   14344 O  O     . ALA A 1 3460 ? 141.993 80.535  232.841 1.00 132.18 ? 3460 ALA A O     1 
ATOM   14345 C  CB    . ALA A 1 3460 ? 139.837 79.411  235.056 1.00 127.98 ? 3460 ALA A CB    1 
ATOM   14346 N  N     . ILE A 1 3461 ? 142.896 79.035  234.257 1.00 136.53 ? 3461 ILE A N     1 
ATOM   14347 C  CA    . ILE A 1 3461 ? 144.247 79.555  234.069 1.00 135.76 ? 3461 ILE A CA    1 
ATOM   14348 C  C     . ILE A 1 3461 ? 144.728 79.280  232.648 1.00 135.29 ? 3461 ILE A C     1 
ATOM   14349 O  O     . ILE A 1 3461 ? 145.459 80.085  232.058 1.00 135.09 ? 3461 ILE A O     1 
ATOM   14350 C  CB    . ILE A 1 3461 ? 145.202 78.960  235.121 1.00 133.49 ? 3461 ILE A CB    1 
ATOM   14351 C  CG1   . ILE A 1 3461 ? 144.702 79.275  236.532 1.00 130.05 ? 3461 ILE A CG1   1 
ATOM   14352 C  CG2   . ILE A 1 3461 ? 146.607 79.509  234.942 1.00 129.61 ? 3461 ILE A CG2   1 
ATOM   14353 C  CD1   . ILE A 1 3461 ? 144.510 80.752  236.797 1.00 126.67 ? 3461 ILE A CD1   1 
ATOM   14354 N  N     . LYS A 1 3462 ? 144.325 78.141  232.078 1.00 134.45 ? 3462 LYS A N     1 
ATOM   14355 C  CA    . LYS A 1 3462 ? 144.698 77.824  230.702 1.00 132.36 ? 3462 LYS A CA    1 
ATOM   14356 C  C     . LYS A 1 3462 ? 144.181 78.884  229.738 1.00 131.96 ? 3462 LYS A C     1 
ATOM   14357 O  O     . LYS A 1 3462 ? 144.905 79.334  228.843 1.00 129.00 ? 3462 LYS A O     1 
ATOM   14358 C  CB    . LYS A 1 3462 ? 144.160 76.444  230.315 1.00 131.14 ? 3462 LYS A CB    1 
ATOM   14359 C  CG    . LYS A 1 3462 ? 144.851 75.280  231.002 1.00 129.99 ? 3462 LYS A CG    1 
ATOM   14360 C  CD    . LYS A 1 3462 ? 144.081 73.984  230.798 1.00 128.12 ? 3462 LYS A CD    1 
ATOM   14361 C  CE    . LYS A 1 3462 ? 144.738 72.828  231.535 1.00 126.96 ? 3462 LYS A CE    1 
ATOM   14362 N  NZ    . LYS A 1 3462 ? 144.782 73.060  233.005 1.00 126.58 ? 3462 LYS A NZ    1 
ATOM   14363 N  N     . ALA A 1 3463 ? 142.920 79.292  229.904 1.00 132.91 ? 3463 ALA A N     1 
ATOM   14364 C  CA    . ALA A 1 3463 ? 142.372 80.354  229.067 1.00 130.29 ? 3463 ALA A CA    1 
ATOM   14365 C  C     . ALA A 1 3463 ? 143.079 81.678  229.323 1.00 130.15 ? 3463 ALA A C     1 
ATOM   14366 O  O     . ALA A 1 3463 ? 143.377 82.424  228.382 1.00 127.00 ? 3463 ALA A O     1 
ATOM   14367 C  CB    . ALA A 1 3463 ? 140.869 80.491  229.311 1.00 125.62 ? 3463 ALA A CB    1 
ATOM   14368 N  N     . ASP A 1 3464 ? 143.351 81.991  230.592 1.00 132.57 ? 3464 ASP A N     1 
ATOM   14369 C  CA    . ASP A 1 3464 ? 144.035 83.238  230.918 1.00 132.11 ? 3464 ASP A CA    1 
ATOM   14370 C  C     . ASP A 1 3464 ? 145.457 83.251  230.368 1.00 132.16 ? 3464 ASP A C     1 
ATOM   14371 O  O     . ASP A 1 3464 ? 145.917 84.272  229.844 1.00 132.26 ? 3464 ASP A O     1 
ATOM   14372 C  CB    . ASP A 1 3464 ? 144.041 83.452  232.432 1.00 129.90 ? 3464 ASP A CB    1 
ATOM   14373 C  CG    . ASP A 1 3464 ? 144.364 84.883  232.818 1.00 126.42 ? 3464 ASP A CG    1 
ATOM   14374 O  OD1   . ASP A 1 3464 ? 144.443 85.742  231.915 1.00 123.64 ? 3464 ASP A OD1   1 
ATOM   14375 O  OD2   . ASP A 1 3464 ? 144.540 85.149  234.025 1.00 124.63 ? 3464 ASP A OD2   1 
ATOM   14376 N  N     . LEU A 1 3465 ? 146.170 82.127  230.482 1.00 133.25 ? 3465 LEU A N     1 
ATOM   14377 C  CA    . LEU A 1 3465 ? 147.524 82.056  229.942 1.00 132.61 ? 3465 LEU A CA    1 
ATOM   14378 C  C     . LEU A 1 3465 ? 147.520 82.186  228.424 1.00 130.82 ? 3465 LEU A C     1 
ATOM   14379 O  O     . LEU A 1 3465 ? 148.383 82.859  227.848 1.00 128.70 ? 3465 LEU A O     1 
ATOM   14380 C  CB    . LEU A 1 3465 ? 148.194 80.749  230.366 1.00 131.17 ? 3465 LEU A CB    1 
ATOM   14381 C  CG    . LEU A 1 3465 ? 149.620 80.533  229.853 1.00 126.95 ? 3465 LEU A CG    1 
ATOM   14382 C  CD1   . LEU A 1 3465 ? 150.586 81.490  230.534 1.00 126.40 ? 3465 LEU A CD1   1 
ATOM   14383 C  CD2   . LEU A 1 3465 ? 150.060 79.092  230.053 1.00 121.63 ? 3465 LEU A CD2   1 
ATOM   14384 N  N     . ALA A 1 3466 ? 146.559 81.541  227.758 1.00 129.62 ? 3466 ALA A N     1 
ATOM   14385 C  CA    . ALA A 1 3466 ? 146.460 81.653  226.306 1.00 128.12 ? 3466 ALA A CA    1 
ATOM   14386 C  C     . ALA A 1 3466 ? 146.140 83.080  225.883 1.00 129.27 ? 3466 ALA A C     1 
ATOM   14387 O  O     . ALA A 1 3466 ? 146.683 83.578  224.889 1.00 127.16 ? 3466 ALA A O     1 
ATOM   14388 C  CB    . ALA A 1 3466 ? 145.404 80.684  225.776 1.00 123.46 ? 3466 ALA A CB    1 
ATOM   14389 N  N     . ALA A 1 3467 ? 145.253 83.752  226.620 1.00 130.67 ? 3467 ALA A N     1 
ATOM   14390 C  CA    . ALA A 1 3467 ? 144.919 85.136  226.298 1.00 127.96 ? 3467 ALA A CA    1 
ATOM   14391 C  C     . ALA A 1 3467 ? 146.124 86.051  226.476 1.00 128.85 ? 3467 ALA A C     1 
ATOM   14392 O  O     . ALA A 1 3467 ? 146.340 86.969  225.676 1.00 124.22 ? 3467 ALA A O     1 
ATOM   14393 C  CB    . ALA A 1 3467 ? 143.751 85.610  227.163 1.00 118.15 ? 3467 ALA A CB    1 
ATOM   14394 N  N     . VAL A 1 3468 ? 146.917 85.822  227.526 1.00 132.04 ? 3468 VAL A N     1 
ATOM   14395 C  CA    . VAL A 1 3468 ? 148.098 86.648  227.763 1.00 131.00 ? 3468 VAL A CA    1 
ATOM   14396 C  C     . VAL A 1 3468 ? 149.117 86.460  226.645 1.00 130.18 ? 3468 VAL A C     1 
ATOM   14397 O  O     . VAL A 1 3468 ? 149.688 87.433  226.137 1.00 127.60 ? 3468 VAL A O     1 
ATOM   14398 C  CB    . VAL A 1 3468 ? 148.704 86.329  229.144 1.00 126.62 ? 3468 VAL A CB    1 
ATOM   14399 C  CG1   . VAL A 1 3468 ? 150.110 86.899  229.257 1.00 123.12 ? 3468 VAL A CG1   1 
ATOM   14400 C  CG2   . VAL A 1 3468 ? 147.815 86.878  230.249 1.00 121.01 ? 3468 VAL A CG2   1 
ATOM   14401 N  N     . GLU A 1 3469 ? 149.356 85.210  226.240 1.00 130.26 ? 3469 GLU A N     1 
ATOM   14402 C  CA    . GLU A 1 3469 ? 150.339 84.952  225.191 1.00 128.11 ? 3469 GLU A CA    1 
ATOM   14403 C  C     . GLU A 1 3469 ? 149.878 85.509  223.849 1.00 127.90 ? 3469 GLU A C     1 
ATOM   14404 O  O     . GLU A 1 3469 ? 150.706 85.879  223.008 1.00 123.42 ? 3469 GLU A O     1 
ATOM   14405 C  CB    . GLU A 1 3469 ? 150.627 83.451  225.095 1.00 123.41 ? 3469 GLU A CB    1 
ATOM   14406 C  CG    . GLU A 1 3469 ? 149.727 82.680  224.143 1.00 123.93 ? 3469 GLU A CG    1 
ATOM   14407 C  CD    . GLU A 1 3469 ? 150.120 81.221  224.023 1.00 124.18 ? 3469 GLU A CD    1 
ATOM   14408 O  OE1   . GLU A 1 3469 ? 151.274 80.945  223.634 1.00 122.43 ? 3469 GLU A OE1   1 
ATOM   14409 O  OE2   . GLU A 1 3469 ? 149.275 80.349  224.319 1.00 123.06 ? 3469 GLU A OE2   1 
ATOM   14410 N  N     . ALA A 1 3470 ? 148.562 85.573  223.626 1.00 128.85 ? 3470 ALA A N     1 
ATOM   14411 C  CA    . ALA A 1 3470 ? 148.053 86.195  222.409 1.00 124.04 ? 3470 ALA A CA    1 
ATOM   14412 C  C     . ALA A 1 3470 ? 148.331 87.692  222.402 1.00 121.34 ? 3470 ALA A C     1 
ATOM   14413 O  O     . ALA A 1 3470 ? 148.719 88.256  221.372 1.00 117.23 ? 3470 ALA A O     1 
ATOM   14414 C  CB    . ALA A 1 3470 ? 146.555 85.924  222.265 1.00 120.88 ? 3470 ALA A CB    1 
ATOM   14415 N  N     . LYS A 1 3471 ? 148.134 88.353  223.546 1.00 121.50 ? 3471 LYS A N     1 
ATOM   14416 C  CA    . LYS A 1 3471 ? 148.439 89.776  223.645 1.00 117.81 ? 3471 LYS A CA    1 
ATOM   14417 C  C     . LYS A 1 3471 ? 149.935 90.027  223.506 1.00 117.38 ? 3471 LYS A C     1 
ATOM   14418 O  O     . LYS A 1 3471 ? 150.353 91.034  222.921 1.00 114.81 ? 3471 LYS A O     1 
ATOM   14419 C  CB    . LYS A 1 3471 ? 147.916 90.328  224.972 1.00 114.58 ? 3471 LYS A CB    1 
ATOM   14420 C  CG    . LYS A 1 3471 ? 148.234 91.793  225.217 1.00 111.41 ? 3471 LYS A CG    1 
ATOM   14421 C  CD    . LYS A 1 3471 ? 147.575 92.288  226.496 1.00 106.91 ? 3471 LYS A CD    1 
ATOM   14422 C  CE    . LYS A 1 3471 ? 146.070 92.417  226.328 1.00 105.11 ? 3471 LYS A CE    1 
ATOM   14423 N  NZ    . LYS A 1 3471 ? 145.435 93.086  227.498 1.00 94.60  ? 3471 LYS A NZ    1 
ATOM   14424 N  N     . VAL A 1 3472 ? 150.758 89.122  224.043 1.00 119.54 ? 3472 VAL A N     1 
ATOM   14425 C  CA    . VAL A 1 3472 ? 152.206 89.263  223.923 1.00 119.09 ? 3472 VAL A CA    1 
ATOM   14426 C  C     . VAL A 1 3472 ? 152.633 89.177  222.463 1.00 117.93 ? 3472 VAL A C     1 
ATOM   14427 O  O     . VAL A 1 3472 ? 153.443 89.983  221.988 1.00 116.38 ? 3472 VAL A O     1 
ATOM   14428 C  CB    . VAL A 1 3472 ? 152.917 88.204  224.787 1.00 119.54 ? 3472 VAL A CB    1 
ATOM   14429 C  CG1   . VAL A 1 3472 ? 154.366 88.039  224.351 1.00 113.74 ? 3472 VAL A CG1   1 
ATOM   14430 C  CG2   . VAL A 1 3472 ? 152.837 88.580  226.259 1.00 120.47 ? 3472 VAL A CG2   1 
ATOM   14431 N  N     . ASN A 1 3473 ? 152.092 88.202  221.727 1.00 119.20 ? 3473 ASN A N     1 
ATOM   14432 C  CA    . ASN A 1 3473 ? 152.448 88.053  220.319 1.00 118.31 ? 3473 ASN A CA    1 
ATOM   14433 C  C     . ASN A 1 3473 ? 151.989 89.253  219.500 1.00 116.44 ? 3473 ASN A C     1 
ATOM   14434 O  O     . ASN A 1 3473 ? 152.718 89.729  218.621 1.00 113.27 ? 3473 ASN A O     1 
ATOM   14435 C  CB    . ASN A 1 3473 ? 151.850 86.761  219.761 1.00 118.60 ? 3473 ASN A CB    1 
ATOM   14436 C  CG    . ASN A 1 3473 ? 152.460 85.521  220.383 1.00 116.74 ? 3473 ASN A CG    1 
ATOM   14437 O  OD1   . ASN A 1 3473 ? 153.347 85.611  221.233 1.00 117.51 ? 3473 ASN A OD1   1 
ATOM   14438 N  ND2   . ASN A 1 3473 ? 151.988 84.354  219.961 1.00 109.56 ? 3473 ASN A ND2   1 
ATOM   14439 N  N     . ARG A 1 3474 ? 150.780 89.752  219.768 1.00 117.53 ? 3474 ARG A N     1 
ATOM   14440 C  CA    . ARG A 1 3474 ? 150.298 90.939  219.069 1.00 113.96 ? 3474 ARG A CA    1 
ATOM   14441 C  C     . ARG A 1 3474 ? 151.168 92.150  219.378 1.00 111.77 ? 3474 ARG A C     1 
ATOM   14442 O  O     . ARG A 1 3474 ? 151.500 92.933  218.480 1.00 108.94 ? 3474 ARG A O     1 
ATOM   14443 C  CB    . ARG A 1 3474 ? 148.844 91.217  219.448 1.00 109.16 ? 3474 ARG A CB    1 
ATOM   14444 C  CG    . ARG A 1 3474 ? 148.320 92.557  218.957 1.00 105.55 ? 3474 ARG A CG    1 
ATOM   14445 C  CD    . ARG A 1 3474 ? 146.926 92.836  219.492 1.00 106.40 ? 3474 ARG A CD    1 
ATOM   14446 N  NE    . ARG A 1 3474 ? 146.845 92.623  220.932 1.00 113.23 ? 3474 ARG A NE    1 
ATOM   14447 C  CZ    . ARG A 1 3474 ? 145.754 92.822  221.659 1.00 110.09 ? 3474 ARG A CZ    1 
ATOM   14448 N  NH1   . ARG A 1 3474 ? 144.625 93.240  221.110 1.00 107.25 ? 3474 ARG A NH1   1 
ATOM   14449 N  NH2   . ARG A 1 3474 ? 145.797 92.597  222.969 1.00 106.05 ? 3474 ARG A NH2   1 
ATOM   14450 N  N     . SER A 1 3475 ? 151.547 92.318  220.646 1.00 113.82 ? 3475 SER A N     1 
ATOM   14451 C  CA    . SER A 1 3475 ? 152.379 93.453  221.031 1.00 113.11 ? 3475 SER A CA    1 
ATOM   14452 C  C     . SER A 1 3475 ? 153.772 93.353  220.422 1.00 112.63 ? 3475 SER A C     1 
ATOM   14453 O  O     . SER A 1 3475 ? 154.364 94.370  220.044 1.00 110.19 ? 3475 SER A O     1 
ATOM   14454 C  CB    . SER A 1 3475 ? 152.459 93.544  222.553 1.00 112.64 ? 3475 SER A CB    1 
ATOM   14455 O  OG    . SER A 1 3475 ? 151.163 93.576  223.126 1.00 113.68 ? 3475 SER A OG    1 
ATOM   14456 N  N     . THR A 1 3476 ? 154.315 92.136  220.330 1.00 112.61 ? 3476 THR A N     1 
ATOM   14457 C  CA    . THR A 1 3476 ? 155.608 91.953  219.679 1.00 111.43 ? 3476 THR A CA    1 
ATOM   14458 C  C     . THR A 1 3476 ? 155.537 92.333  218.205 1.00 113.32 ? 3476 THR A C     1 
ATOM   14459 O  O     . THR A 1 3476 ? 156.479 92.920  217.660 1.00 111.16 ? 3476 THR A O     1 
ATOM   14460 C  CB    . THR A 1 3476 ? 156.081 90.508  219.839 1.00 109.83 ? 3476 THR A CB    1 
ATOM   14461 O  OG1   . THR A 1 3476 ? 155.890 90.089  221.196 1.00 110.59 ? 3476 THR A OG1   1 
ATOM   14462 C  CG2   . THR A 1 3476 ? 157.555 90.387  219.480 1.00 103.92 ? 3476 THR A CG2   1 
ATOM   14463 N  N     . ALA A 1 3477 ? 154.402 92.040  217.567 1.00 114.80 ? 3477 ALA A N     1 
ATOM   14464 C  CA    . ALA A 1 3477 ? 154.219 92.455  216.156 1.00 113.49 ? 3477 ALA A CA    1 
ATOM   14465 C  C     . ALA A 1 3477 ? 154.204 93.984  216.081 1.00 111.24 ? 3477 ALA A C     1 
ATOM   14466 O  O     . ALA A 1 3477 ? 154.842 94.550  215.166 1.00 112.02 ? 3477 ALA A O     1 
ATOM   14467 C  CB    . ALA A 1 3477 ? 152.943 91.860  215.606 1.00 109.12 ? 3477 ALA A CB    1 
ATOM   14468 N  N     . LEU A 1 3478 ? 153.511 94.633  217.022 1.00 110.35 ? 3478 LEU A N     1 
ATOM   14469 C  CA    . LEU A 1 3478 ? 153.406 96.116  217.021 1.00 107.96 ? 3478 LEU A CA    1 
ATOM   14470 C  C     . LEU A 1 3478 ? 154.811 96.728  217.120 1.00 108.49 ? 3478 LEU A C     1 
ATOM   14471 O  O     . LEU A 1 3478 ? 155.082 97.711  216.397 1.00 106.68 ? 3478 LEU A O     1 
ATOM   14472 C  CB    . LEU A 1 3478 ? 152.527 96.565  218.186 1.00 106.06 ? 3478 LEU A CB    1 
ATOM   14473 C  CG    . LEU A 1 3478 ? 151.125 95.951  218.244 1.00 111.12 ? 3478 LEU A CG    1 
ATOM   14474 C  CD1   . LEU A 1 3478 ? 150.402 96.383  219.507 1.00 109.08 ? 3478 LEU A CD1   1 
ATOM   14475 C  CD2   . LEU A 1 3478 ? 150.321 96.322  217.011 1.00 106.98 ? 3478 LEU A CD2   1 
ATOM   14476 N  N     . LEU A 1 3479 ? 155.663 96.167  217.983 1.00 110.88 ? 3479 LEU A N     1 
ATOM   14477 C  CA    . LEU A 1 3479 ? 157.027 96.721  218.180 1.00 108.99 ? 3479 LEU A CA    1 
ATOM   14478 C  C     . LEU A 1 3479 ? 157.766 96.718  216.834 1.00 109.63 ? 3479 LEU A C     1 
ATOM   14479 O  O     . LEU A 1 3479 ? 158.352 97.763  216.476 1.00 107.93 ? 3479 LEU A O     1 
ATOM   14480 C  CB    . LEU A 1 3479 ? 157.761 95.881  219.223 1.00 107.42 ? 3479 LEU A CB    1 
ATOM   14481 C  CG    . LEU A 1 3479 ? 157.025 95.669  220.549 1.00 106.80 ? 3479 LEU A CG    1 
ATOM   14482 C  CD1   . LEU A 1 3479 ? 157.791 94.711  221.443 1.00 104.09 ? 3479 LEU A CD1   1 
ATOM   14483 C  CD2   . LEU A 1 3479 ? 156.778 96.989  221.260 1.00 102.93 ? 3479 LEU A CD2   1 
ATOM   14484 N  N     . LYS A 1 3480 ? 157.726 95.590  216.120 1.00 111.22 ? 3480 LYS A N     1 
ATOM   14485 C  CA    . LYS A 1 3480 ? 158.411 95.485  214.806 1.00 109.72 ? 3480 LYS A CA    1 
ATOM   14486 C  C     . LYS A 1 3480 ? 157.767 96.475  213.826 1.00 112.60 ? 3480 LYS A C     1 
ATOM   14487 O  O     . LYS A 1 3480 ? 158.513 97.130  213.066 1.00 110.29 ? 3480 LYS A O     1 
ATOM   14488 C  CB    . LYS A 1 3480 ? 158.288 94.053  214.276 1.00 108.55 ? 3480 LYS A CB    1 
ATOM   14489 C  CG    . LYS A 1 3480 ? 158.639 92.962  215.277 1.00 112.30 ? 3480 LYS A CG    1 
ATOM   14490 C  CD    . LYS A 1 3480 ? 158.365 91.560  214.745 1.00 110.74 ? 3480 LYS A CD    1 
ATOM   14491 C  CE    . LYS A 1 3480 ? 158.695 90.496  215.742 1.00 108.15 ? 3480 LYS A CE    1 
ATOM   14492 N  NZ    . LYS A 1 3480 ? 157.922 90.655  216.976 1.00 105.19 ? 3480 LYS A NZ    1 
ATOM   14493 N  N     . SER A 1 3481 ? 156.436 96.581  213.854 1.00 112.05 ? 3481 SER A N     1 
ATOM   14494 C  CA    . SER A 1 3481 ? 155.713 97.476  212.913 1.00 107.70 ? 3481 SER A CA    1 
ATOM   14495 C  C     . SER A 1 3481 ? 156.149 98.932  213.129 1.00 108.86 ? 3481 SER A C     1 
ATOM   14496 O  O     . SER A 1 3481 ? 156.268 99.666  212.125 1.00 107.93 ? 3481 SER A O     1 
ATOM   14497 C  CB    . SER A 1 3481 ? 154.224 97.319  213.074 1.00 104.80 ? 3481 SER A CB    1 
ATOM   14498 O  OG    . SER A 1 3481 ? 153.539 97.723  211.898 1.00 105.59 ? 3481 SER A OG    1 
ATOM   14499 N  N     . LEU A 1 3482 ? 156.379 99.330  214.384 1.00 109.34 ? 3482 LEU A N     1 
ATOM   14500 C  CA    . LEU A 1 3482 ? 156.750 100.737 214.691 1.00 105.11 ? 3482 LEU A CA    1 
ATOM   14501 C  C     . LEU A 1 3482 ? 158.280 100.881 214.734 1.00 104.13 ? 3482 LEU A C     1 
ATOM   14502 O  O     . LEU A 1 3482 ? 158.759 102.027 214.864 1.00 103.37 ? 3482 LEU A O     1 
ATOM   14503 C  CB    . LEU A 1 3482 ? 156.109 101.134 216.019 1.00 99.26  ? 3482 LEU A CB    1 
ATOM   14504 C  CG    . LEU A 1 3482 ? 154.583 101.020 216.084 1.00 98.76  ? 3482 LEU A CG    1 
ATOM   14505 C  CD1   . LEU A 1 3482 ? 154.068 101.406 217.459 1.00 90.12  ? 3482 LEU A CD1   1 
ATOM   14506 C  CD2   . LEU A 1 3482 ? 153.932 101.873 215.008 1.00 101.20 ? 3482 LEU A CD2   1 
ATOM   14507 N  N     . SER A 1 3483 ? 159.011 99.767  214.629 1.00 104.63 ? 3483 SER A N     1 
ATOM   14508 C  CA    . SER A 1 3483 ? 160.496 99.807  214.718 1.00 104.62 ? 3483 SER A CA    1 
ATOM   14509 C  C     . SER A 1 3483 ? 161.057 100.908 213.808 1.00 104.42 ? 3483 SER A C     1 
ATOM   14510 O  O     . SER A 1 3483 ? 161.645 101.874 214.343 1.00 103.30 ? 3483 SER A O     1 
ATOM   14511 C  CB    . SER A 1 3483 ? 161.094 98.466  214.380 1.00 102.80 ? 3483 SER A CB    1 
ATOM   14512 O  OG    . SER A 1 3483 ? 162.514 98.523  214.418 1.00 94.60  ? 3483 SER A OG    1 
ATOM   14513 N  N     . ALA A 1 3484 ? 160.893 100.763 212.490 1.00 104.89 ? 3484 ALA A N     1 
ATOM   14514 C  CA    . ALA A 1 3484 ? 161.426 101.745 211.551 1.00 104.08 ? 3484 ALA A CA    1 
ATOM   14515 C  C     . ALA A 1 3484 ? 161.025 103.161 211.945 1.00 106.08 ? 3484 ALA A C     1 
ATOM   14516 O  O     . ALA A 1 3484 ? 161.832 104.093 211.847 1.00 105.30 ? 3484 ALA A O     1 
ATOM   14517 C  CB    . ALA A 1 3484 ? 160.954 101.427 210.132 1.00 96.45  ? 3484 ALA A CB    1 
ATOM   14518 N  N     . GLU A 1 3485 ? 159.778 103.343 212.385 1.00 106.31 ? 3485 GLU A N     1 
ATOM   14519 C  CA    . GLU A 1 3485 ? 159.335 104.659 212.834 1.00 104.17 ? 3485 GLU A CA    1 
ATOM   14520 C  C     . GLU A 1 3485 ? 160.131 105.123 214.047 1.00 104.14 ? 3485 GLU A C     1 
ATOM   14521 O  O     . GLU A 1 3485 ? 160.503 106.298 214.142 1.00 104.97 ? 3485 GLU A O     1 
ATOM   14522 C  CB    . GLU A 1 3485 ? 157.840 104.630 213.150 1.00 104.67 ? 3485 GLU A CB    1 
ATOM   14523 C  CG    . GLU A 1 3485 ? 156.942 104.782 211.932 1.00 106.16 ? 3485 GLU A CG    1 
ATOM   14524 C  CD    . GLU A 1 3485 ? 156.853 103.513 211.106 1.00 108.69 ? 3485 GLU A CD    1 
ATOM   14525 O  OE1   . GLU A 1 3485 ? 157.325 102.457 211.577 1.00 111.00 ? 3485 GLU A OE1   1 
ATOM   14526 O  OE2   . GLU A 1 3485 ? 156.309 103.571 209.983 1.00 102.93 ? 3485 GLU A OE2   1 
ATOM   14527 N  N     . ARG A 1 3486 ? 160.398 104.213 214.986 1.00 106.34 ? 3486 ARG A N     1 
ATOM   14528 C  CA    . ARG A 1 3486 ? 161.182 104.572 216.163 1.00 105.24 ? 3486 ARG A CA    1 
ATOM   14529 C  C     . ARG A 1 3486 ? 162.600 104.980 215.782 1.00 105.36 ? 3486 ARG A C     1 
ATOM   14530 O  O     . ARG A 1 3486 ? 163.140 105.952 216.323 1.00 107.10 ? 3486 ARG A O     1 
ATOM   14531 C  CB    . ARG A 1 3486 ? 161.203 103.406 217.152 1.00 102.09 ? 3486 ARG A CB    1 
ATOM   14532 C  CG    . ARG A 1 3486 ? 162.010 103.670 218.413 1.00 100.82 ? 3486 ARG A CG    1 
ATOM   14533 C  CD    . ARG A 1 3486 ? 161.929 102.495 219.376 1.00 100.04 ? 3486 ARG A CD    1 
ATOM   14534 N  NE    . ARG A 1 3486 ? 162.127 101.218 218.701 1.00 103.09 ? 3486 ARG A NE    1 
ATOM   14535 C  CZ    . ARG A 1 3486 ? 163.305 100.741 218.324 1.00 100.42 ? 3486 ARG A CZ    1 
ATOM   14536 N  NH1   . ARG A 1 3486 ? 164.425 101.409 218.547 1.00 101.01 ? 3486 ARG A NH1   1 
ATOM   14537 N  NH2   . ARG A 1 3486 ? 163.362 99.563  217.708 1.00 93.05  ? 3486 ARG A NH2   1 
ATOM   14538 N  N     . GLU A 1 3487 ? 163.220 104.248 214.854 1.00 106.83 ? 3487 GLU A N     1 
ATOM   14539 C  CA    . GLU A 1 3487 ? 164.581 104.573 214.437 1.00 106.33 ? 3487 GLU A CA    1 
ATOM   14540 C  C     . GLU A 1 3487 ? 164.637 105.931 213.746 1.00 104.15 ? 3487 GLU A C     1 
ATOM   14541 O  O     . GLU A 1 3487 ? 165.533 106.740 214.014 1.00 103.63 ? 3487 GLU A O     1 
ATOM   14542 C  CB    . GLU A 1 3487 ? 165.125 103.478 213.520 1.00 105.46 ? 3487 GLU A CB    1 
ATOM   14543 C  CG    . GLU A 1 3487 ? 165.313 102.131 214.201 1.00 103.04 ? 3487 GLU A CG    1 
ATOM   14544 C  CD    . GLU A 1 3487 ? 166.121 102.230 215.480 1.00 102.06 ? 3487 GLU A CD    1 
ATOM   14545 O  OE1   . GLU A 1 3487 ? 167.179 102.896 215.468 1.00 100.64 ? 3487 GLU A OE1   1 
ATOM   14546 O  OE2   . GLU A 1 3487 ? 165.700 101.642 216.497 1.00 103.03 ? 3487 GLU A OE2   1 
ATOM   14547 N  N     . ARG A 1 3488 ? 163.687 106.196 212.845 1.00 103.49 ? 3488 ARG A N     1 
ATOM   14548 C  CA    . ARG A 1 3488 ? 163.667 107.481 212.151 1.00 102.71 ? 3488 ARG A CA    1 
ATOM   14549 C  C     . ARG A 1 3488 ? 163.405 108.627 213.120 1.00 101.19 ? 3488 ARG A C     1 
ATOM   14550 O  O     . ARG A 1 3488 ? 164.050 109.680 213.039 1.00 99.00  ? 3488 ARG A O     1 
ATOM   14551 C  CB    . ARG A 1 3488 ? 162.615 107.466 211.042 1.00 99.54  ? 3488 ARG A CB    1 
ATOM   14552 C  CG    . ARG A 1 3488 ? 162.329 108.838 210.450 1.00 95.70  ? 3488 ARG A CG    1 
ATOM   14553 C  CD    . ARG A 1 3488 ? 161.044 108.854 209.635 1.00 97.15  ? 3488 ARG A CD    1 
ATOM   14554 N  NE    . ARG A 1 3488 ? 160.988 107.765 208.668 1.00 100.69 ? 3488 ARG A NE    1 
ATOM   14555 C  CZ    . ARG A 1 3488 ? 159.985 106.903 208.567 1.00 97.45  ? 3488 ARG A CZ    1 
ATOM   14556 N  NH1   . ARG A 1 3488 ? 158.927 106.978 209.358 1.00 96.56  ? 3488 ARG A NH1   1 
ATOM   14557 N  NH2   . ARG A 1 3488 ? 160.043 105.945 207.647 1.00 88.30  ? 3488 ARG A NH2   1 
ATOM   14558 N  N     . TRP A 1 3489 ? 162.463 108.440 214.047 1.00 99.28  ? 3489 TRP A N     1 
ATOM   14559 C  CA    . TRP A 1 3489 ? 162.124 109.502 214.989 1.00 99.42  ? 3489 TRP A CA    1 
ATOM   14560 C  C     . TRP A 1 3489 ? 163.291 109.811 215.919 1.00 101.22 ? 3489 TRP A C     1 
ATOM   14561 O  O     . TRP A 1 3489 ? 163.495 110.969 216.302 1.00 101.15 ? 3489 TRP A O     1 
ATOM   14562 C  CB    . TRP A 1 3489 ? 160.881 109.113 215.786 1.00 99.04  ? 3489 TRP A CB    1 
ATOM   14563 C  CG    . TRP A 1 3489 ? 159.638 109.073 214.953 1.00 100.51 ? 3489 TRP A CG    1 
ATOM   14564 C  CD1   . TRP A 1 3489 ? 159.518 109.442 213.644 1.00 99.61  ? 3489 TRP A CD1   1 
ATOM   14565 C  CD2   . TRP A 1 3489 ? 158.342 108.622 215.362 1.00 99.72  ? 3489 TRP A CD2   1 
ATOM   14566 N  NE1   . TRP A 1 3489 ? 158.226 109.259 213.217 1.00 101.76 ? 3489 TRP A NE1   1 
ATOM   14567 C  CE2   . TRP A 1 3489 ? 157.484 108.755 214.252 1.00 101.84 ? 3489 TRP A CE2   1 
ATOM   14568 C  CE3   . TRP A 1 3489 ? 157.823 108.123 216.560 1.00 99.15  ? 3489 TRP A CE3   1 
ATOM   14569 C  CZ2   . TRP A 1 3489 ? 156.137 108.407 214.305 1.00 99.85  ? 3489 TRP A CZ2   1 
ATOM   14570 C  CZ3   . TRP A 1 3489 ? 156.486 107.778 216.610 1.00 98.46  ? 3489 TRP A CZ3   1 
ATOM   14571 C  CH2   . TRP A 1 3489 ? 155.658 107.922 215.490 1.00 99.10  ? 3489 TRP A CH2   1 
ATOM   14572 N  N     . GLU A 1 3490 ? 164.061 108.790 216.301 1.00 103.40 ? 3490 GLU A N     1 
ATOM   14573 C  CA    . GLU A 1 3490 ? 165.243 109.026 217.123 1.00 100.96 ? 3490 GLU A CA    1 
ATOM   14574 C  C     . GLU A 1 3490 ? 166.270 109.875 216.382 1.00 96.98  ? 3490 GLU A C     1 
ATOM   14575 O  O     . GLU A 1 3490 ? 166.884 110.773 216.970 1.00 96.50  ? 3490 GLU A O     1 
ATOM   14576 C  CB    . GLU A 1 3490 ? 165.862 107.697 217.556 1.00 103.26 ? 3490 GLU A CB    1 
ATOM   14577 C  CG    . GLU A 1 3490 ? 165.190 107.058 218.761 1.00 106.70 ? 3490 GLU A CG    1 
ATOM   14578 C  CD    . GLU A 1 3490 ? 165.165 105.544 218.683 1.00 111.79 ? 3490 GLU A CD    1 
ATOM   14579 O  OE1   . GLU A 1 3490 ? 165.542 104.994 217.627 1.00 111.97 ? 3490 GLU A OE1   1 
ATOM   14580 O  OE2   . GLU A 1 3490 ? 164.771 104.904 219.680 1.00 108.41 ? 3490 GLU A OE2   1 
ATOM   14581 N  N     . LYS A 1 3491 ? 166.474 109.600 215.091 1.00 97.09  ? 3491 LYS A N     1 
ATOM   14582 C  CA    . LYS A 1 3491 ? 167.440 110.373 214.315 1.00 96.97  ? 3491 LYS A CA    1 
ATOM   14583 C  C     . LYS A 1 3491 ? 167.008 111.828 214.184 1.00 98.47  ? 3491 LYS A C     1 
ATOM   14584 O  O     . LYS A 1 3491 ? 167.822 112.742 214.357 1.00 96.63  ? 3491 LYS A O     1 
ATOM   14585 C  CB    . LYS A 1 3491 ? 167.628 109.744 212.935 1.00 96.57  ? 3491 LYS A CB    1 
ATOM   14586 C  CG    . LYS A 1 3491 ? 168.176 108.327 212.965 1.00 98.59  ? 3491 LYS A CG    1 
ATOM   14587 C  CD    . LYS A 1 3491 ? 169.454 108.244 213.782 1.00 98.33  ? 3491 LYS A CD    1 
ATOM   14588 C  CE    . LYS A 1 3491 ? 169.951 106.811 213.878 1.00 97.00  ? 3491 LYS A CE    1 
ATOM   14589 N  NZ    . LYS A 1 3491 ? 168.922 105.907 214.464 1.00 97.78  ? 3491 LYS A NZ    1 
ATOM   14590 N  N     . THR A 1 3492 ? 165.729 112.063 213.878 1.00 99.84  ? 3492 THR A N     1 
ATOM   14591 C  CA    . THR A 1 3492 ? 165.240 113.432 213.756 1.00 92.80  ? 3492 THR A CA    1 
ATOM   14592 C  C     . THR A 1 3492 ? 165.298 114.160 215.093 1.00 90.39  ? 3492 THR A C     1 
ATOM   14593 O  O     . THR A 1 3492 ? 165.640 115.347 215.146 1.00 92.07  ? 3492 THR A O     1 
ATOM   14594 C  CB    . THR A 1 3492 ? 163.815 113.436 213.203 1.00 92.97  ? 3492 THR A CB    1 
ATOM   14595 O  OG1   . THR A 1 3492 ? 163.724 112.513 212.111 1.00 95.62  ? 3492 THR A OG1   1 
ATOM   14596 C  CG2   . THR A 1 3492 ? 163.439 114.827 212.714 1.00 82.42  ? 3492 THR A CG2   1 
ATOM   14597 N  N     . SER A 1 3493 ? 164.965 113.465 216.184 1.00 88.50  ? 3493 SER A N     1 
ATOM   14598 C  CA    . SER A 1 3493 ? 165.093 114.066 217.507 1.00 89.05  ? 3493 SER A CA    1 
ATOM   14599 C  C     . SER A 1 3493 ? 166.549 114.352 217.852 1.00 91.68  ? 3493 SER A C     1 
ATOM   14600 O  O     . SER A 1 3493 ? 166.835 115.314 218.574 1.00 91.46  ? 3493 SER A O     1 
ATOM   14601 C  CB    . SER A 1 3493 ? 164.465 113.155 218.562 1.00 91.43  ? 3493 SER A CB    1 
ATOM   14602 O  OG    . SER A 1 3493 ? 164.623 113.696 219.862 1.00 90.93  ? 3493 SER A OG    1 
ATOM   14603 N  N     . GLU A 1 3494 ? 167.476 113.531 217.356 1.00 92.06  ? 3494 GLU A N     1 
ATOM   14604 C  CA    . GLU A 1 3494 ? 168.893 113.801 217.575 1.00 92.88  ? 3494 GLU A CA    1 
ATOM   14605 C  C     . GLU A 1 3494 ? 169.358 114.997 216.754 1.00 94.44  ? 3494 GLU A C     1 
ATOM   14606 O  O     . GLU A 1 3494 ? 170.084 115.861 217.260 1.00 92.86  ? 3494 GLU A O     1 
ATOM   14607 C  CB    . GLU A 1 3494 ? 169.723 112.562 217.240 1.00 93.89  ? 3494 GLU A CB    1 
ATOM   14608 C  CG    . GLU A 1 3494 ? 171.162 112.629 217.727 1.00 96.39  ? 3494 GLU A CG    1 
ATOM   14609 C  CD    . GLU A 1 3494 ? 172.111 113.170 216.674 1.00 96.44  ? 3494 GLU A CD    1 
ATOM   14610 O  OE1   . GLU A 1 3494 ? 171.679 113.345 215.516 1.00 93.30  ? 3494 GLU A OE1   1 
ATOM   14611 O  OE2   . GLU A 1 3494 ? 173.289 113.421 217.006 1.00 93.96  ? 3494 GLU A OE2   1 
ATOM   14612 N  N     . THR A 1 3495 ? 168.948 115.068 215.487 1.00 96.06  ? 3495 THR A N     1 
ATOM   14613 C  CA    . THR A 1 3495 ? 169.289 116.198 214.634 1.00 95.80  ? 3495 THR A CA    1 
ATOM   14614 C  C     . THR A 1 3495 ? 168.466 117.441 214.946 1.00 95.99  ? 3495 THR A C     1 
ATOM   14615 O  O     . THR A 1 3495 ? 168.690 118.482 214.320 1.00 94.54  ? 3495 THR A O     1 
ATOM   14616 C  CB    . THR A 1 3495 ? 169.112 115.827 213.159 1.00 94.46  ? 3495 THR A CB    1 
ATOM   14617 O  OG1   . THR A 1 3495 ? 167.732 115.543 212.895 1.00 92.56  ? 3495 THR A OG1   1 
ATOM   14618 C  CG2   . THR A 1 3495 ? 169.956 114.611 212.809 1.00 90.68  ? 3495 THR A CG2   1 
ATOM   14619 N  N     . PHE A 1 3496 ? 167.525 117.351 215.890 1.00 94.81  ? 3496 PHE A N     1 
ATOM   14620 C  CA    . PHE A 1 3496 ? 166.705 118.503 216.252 1.00 90.08  ? 3496 PHE A CA    1 
ATOM   14621 C  C     . PHE A 1 3496 ? 167.560 119.662 216.747 1.00 88.04  ? 3496 PHE A C     1 
ATOM   14622 O  O     . PHE A 1 3496 ? 167.304 120.824 216.407 1.00 87.42  ? 3496 PHE A O     1 
ATOM   14623 C  CB    . PHE A 1 3496 ? 165.686 118.095 217.318 1.00 87.48  ? 3496 PHE A CB    1 
ATOM   14624 C  CG    . PHE A 1 3496 ? 165.255 119.222 218.211 1.00 85.17  ? 3496 PHE A CG    1 
ATOM   14625 C  CD1   . PHE A 1 3496 ? 164.424 120.222 217.736 1.00 83.55  ? 3496 PHE A CD1   1 
ATOM   14626 C  CD2   . PHE A 1 3496 ? 165.686 119.283 219.526 1.00 84.94  ? 3496 PHE A CD2   1 
ATOM   14627 C  CE1   . PHE A 1 3496 ? 164.025 121.256 218.558 1.00 82.77  ? 3496 PHE A CE1   1 
ATOM   14628 C  CE2   . PHE A 1 3496 ? 165.294 120.318 220.352 1.00 84.75  ? 3496 PHE A CE2   1 
ATOM   14629 C  CZ    . PHE A 1 3496 ? 164.462 121.307 219.866 1.00 84.62  ? 3496 PHE A CZ    1 
ATOM   14630 N  N     . LYS A 1 3497 ? 168.579 119.367 217.558 1.00 84.76  ? 3497 LYS A N     1 
ATOM   14631 C  CA    . LYS A 1 3497 ? 169.459 120.419 218.055 1.00 86.73  ? 3497 LYS A CA    1 
ATOM   14632 C  C     . LYS A 1 3497 ? 170.208 121.097 216.914 1.00 86.44  ? 3497 LYS A C     1 
ATOM   14633 O  O     . LYS A 1 3497 ? 170.604 122.263 217.027 1.00 82.72  ? 3497 LYS A O     1 
ATOM   14634 C  CB    . LYS A 1 3497 ? 170.442 119.841 219.073 1.00 87.34  ? 3497 LYS A CB    1 
ATOM   14635 C  CG    . LYS A 1 3497 ? 169.783 119.244 220.306 1.00 90.94  ? 3497 LYS A CG    1 
ATOM   14636 C  CD    . LYS A 1 3497 ? 170.803 118.963 221.397 1.00 89.38  ? 3497 LYS A CD    1 
ATOM   14637 C  CE    . LYS A 1 3497 ? 171.114 120.217 222.197 1.00 87.29  ? 3497 LYS A CE    1 
ATOM   14638 N  NZ    . LYS A 1 3497 ? 169.944 120.660 223.005 1.00 83.15  ? 3497 LYS A NZ    1 
ATOM   14639 N  N     . ASN A 1 3498 ? 170.415 120.380 215.807 1.00 87.07  ? 3498 ASN A N     1 
ATOM   14640 C  CA    . ASN A 1 3498 ? 171.125 120.960 214.673 1.00 83.93  ? 3498 ASN A CA    1 
ATOM   14641 C  C     . ASN A 1 3498 ? 170.277 122.004 213.955 1.00 77.65  ? 3498 ASN A C     1 
ATOM   14642 O  O     . ASN A 1 3498 ? 170.789 123.054 213.549 1.00 76.24  ? 3498 ASN A O     1 
ATOM   14643 C  CB    . ASN A 1 3498 ? 171.553 119.858 213.703 1.00 86.68  ? 3498 ASN A CB    1 
ATOM   14644 C  CG    . ASN A 1 3498 ? 172.585 120.333 212.700 1.00 84.80  ? 3498 ASN A CG    1 
ATOM   14645 O  OD1   . ASN A 1 3498 ? 172.260 120.627 211.550 1.00 82.57  ? 3498 ASN A OD1   1 
ATOM   14646 N  ND2   . ASN A 1 3498 ? 173.837 120.412 213.133 1.00 77.08  ? 3498 ASN A ND2   1 
ATOM   14647 N  N     . GLN A 1 3499 ? 168.980 121.732 213.780 1.00 76.05  ? 3499 GLN A N     1 
ATOM   14648 C  CA    . GLN A 1 3499 ? 168.133 122.659 213.034 1.00 79.14  ? 3499 GLN A CA    1 
ATOM   14649 C  C     . GLN A 1 3499 ? 168.000 124.000 213.749 1.00 71.69  ? 3499 GLN A C     1 
ATOM   14650 O  O     . GLN A 1 3499 ? 168.042 125.055 213.107 1.00 65.68  ? 3499 GLN A O     1 
ATOM   14651 C  CB    . GLN A 1 3499 ? 166.757 122.043 212.776 1.00 76.62  ? 3499 GLN A CB    1 
ATOM   14652 C  CG    . GLN A 1 3499 ? 166.754 120.887 211.787 1.00 74.54  ? 3499 GLN A CG    1 
ATOM   14653 C  CD    . GLN A 1 3499 ? 166.599 119.538 212.456 1.00 84.34  ? 3499 GLN A CD    1 
ATOM   14654 O  OE1   . GLN A 1 3499 ? 165.705 119.340 213.278 1.00 83.74  ? 3499 GLN A OE1   1 
ATOM   14655 N  NE2   . GLN A 1 3499 ? 167.467 118.599 212.102 1.00 86.66  ? 3499 GLN A NE2   1 
ATOM   14656 N  N     . MET A 1 3500 ? 167.843 123.985 215.078 1.00 71.65  ? 3500 MET A N     1 
ATOM   14657 C  CA    . MET A 1 3500 ? 167.817 125.242 215.823 1.00 67.47  ? 3500 MET A CA    1 
ATOM   14658 C  C     . MET A 1 3500 ? 169.111 126.026 215.651 1.00 64.67  ? 3500 MET A C     1 
ATOM   14659 O  O     . MET A 1 3500 ? 169.083 127.259 215.572 1.00 65.87  ? 3500 MET A O     1 
ATOM   14660 C  CB    . MET A 1 3500 ? 167.558 124.991 217.310 1.00 62.94  ? 3500 MET A CB    1 
ATOM   14661 C  CG    . MET A 1 3500 ? 166.935 126.186 218.033 1.00 64.21  ? 3500 MET A CG    1 
ATOM   14662 S  SD    . MET A 1 3500 ? 165.136 126.299 218.012 1.00 77.48  ? 3500 MET A SD    1 
ATOM   14663 C  CE    . MET A 1 3500 ? 164.686 124.574 217.943 1.00 75.80  ? 3500 MET A CE    1 
ATOM   14664 N  N     . SER A 1 3501 ? 170.250 125.333 215.596 1.00 64.80  ? 3501 SER A N     1 
ATOM   14665 C  CA    . SER A 1 3501 ? 171.524 126.019 215.419 1.00 66.85  ? 3501 SER A CA    1 
ATOM   14666 C  C     . SER A 1 3501 ? 171.599 126.720 214.068 1.00 64.87  ? 3501 SER A C     1 
ATOM   14667 O  O     . SER A 1 3501 ? 172.226 127.779 213.947 1.00 67.69  ? 3501 SER A O     1 
ATOM   14668 C  CB    . SER A 1 3501 ? 172.676 125.026 215.574 1.00 69.62  ? 3501 SER A CB    1 
ATOM   14669 O  OG    . SER A 1 3501 ? 172.725 124.128 214.479 1.00 73.67  ? 3501 SER A OG    1 
ATOM   14670 N  N     . THR A 1 3502 ? 170.968 126.151 213.044 1.00 61.08  ? 3502 THR A N     1 
ATOM   14671 C  CA    . THR A 1 3502 ? 171.060 126.677 211.688 1.00 56.97  ? 3502 THR A CA    1 
ATOM   14672 C  C     . THR A 1 3502 ? 169.842 127.491 211.263 1.00 50.26  ? 3502 THR A C     1 
ATOM   14673 O  O     . THR A 1 3502 ? 169.827 128.001 210.139 1.00 49.41  ? 3502 THR A O     1 
ATOM   14674 C  CB    . THR A 1 3502 ? 171.271 125.531 210.692 1.00 60.19  ? 3502 THR A CB    1 
ATOM   14675 O  OG1   . THR A 1 3502 ? 170.351 124.471 210.978 1.00 63.95  ? 3502 THR A OG1   1 
ATOM   14676 C  CG2   . THR A 1 3502 ? 172.693 125.000 210.783 1.00 55.43  ? 3502 THR A CG2   1 
ATOM   14677 N  N     . ILE A 1 3503 ? 168.828 127.630 212.122 1.00 49.47  ? 3503 ILE A N     1 
ATOM   14678 C  CA    . ILE A 1 3503 ? 167.615 128.345 211.727 1.00 47.14  ? 3503 ILE A CA    1 
ATOM   14679 C  C     . ILE A 1 3503 ? 167.923 129.809 211.435 1.00 41.10  ? 3503 ILE A C     1 
ATOM   14680 O  O     . ILE A 1 3503 ? 167.425 130.379 210.456 1.00 39.31  ? 3503 ILE A O     1 
ATOM   14681 C  CB    . ILE A 1 3503 ? 166.523 128.193 212.804 1.00 52.10  ? 3503 ILE A CB    1 
ATOM   14682 C  CG1   . ILE A 1 3503 ? 165.659 126.965 212.519 1.00 52.99  ? 3503 ILE A CG1   1 
ATOM   14683 C  CG2   . ILE A 1 3503 ? 165.637 129.420 212.857 1.00 45.69  ? 3503 ILE A CG2   1 
ATOM   14684 C  CD1   . ILE A 1 3503 ? 164.785 126.555 213.681 1.00 53.60  ? 3503 ILE A CD1   1 
ATOM   14685 N  N     . ALA A 1 3504 ? 168.748 130.440 212.274 1.00 40.78  ? 3504 ALA A N     1 
ATOM   14686 C  CA    . ALA A 1 3504 ? 169.062 131.854 212.085 1.00 37.25  ? 3504 ALA A CA    1 
ATOM   14687 C  C     . ALA A 1 3504 ? 169.745 132.094 210.744 1.00 35.21  ? 3504 ALA A C     1 
ATOM   14688 O  O     . ALA A 1 3504 ? 169.404 133.035 210.019 1.00 33.07  ? 3504 ALA A O     1 
ATOM   14689 C  CB    . ALA A 1 3504 ? 169.937 132.353 213.235 1.00 31.01  ? 3504 ALA A CB    1 
ATOM   14690 N  N     . GLY A 1 3505 ? 170.720 131.251 210.399 1.00 32.21  ? 3505 GLY A N     1 
ATOM   14691 C  CA    . GLY A 1 3505 ? 171.384 131.393 209.113 1.00 32.74  ? 3505 GLY A CA    1 
ATOM   14692 C  C     . GLY A 1 3505 ? 170.482 131.057 207.939 1.00 31.74  ? 3505 GLY A C     1 
ATOM   14693 O  O     . GLY A 1 3505 ? 170.505 131.741 206.913 1.00 28.75  ? 3505 GLY A O     1 
ATOM   14694 N  N     . ASP A 1 3506 ? 169.682 129.995 208.071 1.00 34.62  ? 3506 ASP A N     1 
ATOM   14695 C  CA    . ASP A 1 3506 ? 168.804 129.584 206.978 1.00 29.15  ? 3506 ASP A CA    1 
ATOM   14696 C  C     . ASP A 1 3506 ? 167.739 130.634 206.689 1.00 31.80  ? 3506 ASP A C     1 
ATOM   14697 O  O     . ASP A 1 3506 ? 167.459 130.940 205.525 1.00 29.72  ? 3506 ASP A O     1 
ATOM   14698 C  CB    . ASP A 1 3506 ? 168.150 128.242 207.304 1.00 38.28  ? 3506 ASP A CB    1 
ATOM   14699 C  CG    . ASP A 1 3506 ? 169.141 127.099 207.319 1.00 48.46  ? 3506 ASP A CG    1 
ATOM   14700 O  OD1   . ASP A 1 3506 ? 170.208 127.231 206.686 1.00 49.41  ? 3506 ASP A OD1   1 
ATOM   14701 O  OD2   . ASP A 1 3506 ? 168.854 126.070 207.965 1.00 52.84  ? 3506 ASP A OD2   1 
ATOM   14702 N  N     . CYS A 1 3507 ? 167.130 131.193 207.737 1.00 31.94  ? 3507 CYS A N     1 
ATOM   14703 C  CA    . CYS A 1 3507 ? 166.065 132.168 207.530 1.00 27.30  ? 3507 CYS A CA    1 
ATOM   14704 C  C     . CYS A 1 3507 ? 166.600 133.470 206.948 1.00 26.07  ? 3507 CYS A C     1 
ATOM   14705 O  O     . CYS A 1 3507 ? 165.873 134.167 206.231 1.00 26.05  ? 3507 CYS A O     1 
ATOM   14706 C  CB    . CYS A 1 3507 ? 165.332 132.433 208.844 1.00 32.93  ? 3507 CYS A CB    1 
ATOM   14707 S  SG    . CYS A 1 3507 ? 164.361 131.033 209.444 1.00 45.87  ? 3507 CYS A SG    1 
ATOM   14708 N  N     . LEU A 1 3508 ? 167.854 133.816 207.245 1.00 23.07  ? 3508 LEU A N     1 
ATOM   14709 C  CA    . LEU A 1 3508 ? 168.452 135.008 206.651 1.00 18.43  ? 3508 LEU A CA    1 
ATOM   14710 C  C     . LEU A 1 3508 ? 168.614 134.839 205.147 1.00 22.93  ? 3508 LEU A C     1 
ATOM   14711 O  O     . LEU A 1 3508 ? 168.306 135.750 204.370 1.00 20.70  ? 3508 LEU A O     1 
ATOM   14712 C  CB    . LEU A 1 3508 ? 169.795 135.305 207.324 1.00 20.20  ? 3508 LEU A CB    1 
ATOM   14713 C  CG    . LEU A 1 3508 ? 170.519 136.621 207.019 1.00 21.31  ? 3508 LEU A CG    1 
ATOM   14714 C  CD1   . LEU A 1 3508 ? 171.363 137.034 208.212 1.00 25.11  ? 3508 LEU A CD1   1 
ATOM   14715 C  CD2   . LEU A 1 3508 ? 171.395 136.504 205.784 1.00 25.12  ? 3508 LEU A CD2   1 
ATOM   14716 N  N     . LEU A 1 3509 ? 169.102 133.673 204.718 1.00 27.32  ? 3509 LEU A N     1 
ATOM   14717 C  CA    . LEU A 1 3509 ? 169.237 133.406 203.290 1.00 20.83  ? 3509 LEU A CA    1 
ATOM   14718 C  C     . LEU A 1 3509 ? 167.880 133.384 202.602 1.00 21.15  ? 3509 LEU A C     1 
ATOM   14719 O  O     . LEU A 1 3509 ? 167.721 133.936 201.506 1.00 27.06  ? 3509 LEU A O     1 
ATOM   14720 C  CB    . LEU A 1 3509 ? 169.968 132.083 203.071 1.00 19.93  ? 3509 LEU A CB    1 
ATOM   14721 C  CG    . LEU A 1 3509 ? 171.443 132.056 203.461 1.00 21.84  ? 3509 LEU A CG    1 
ATOM   14722 C  CD1   . LEU A 1 3509 ? 172.071 130.724 203.095 1.00 27.16  ? 3509 LEU A CD1   1 
ATOM   14723 C  CD2   . LEU A 1 3509 ? 172.175 133.195 202.781 1.00 23.79  ? 3509 LEU A CD2   1 
ATOM   14724 N  N     . SER A 1 3510 ? 166.889 132.746 203.227 1.00 17.74  ? 3510 SER A N     1 
ATOM   14725 C  CA    . SER A 1 3510 ? 165.566 132.658 202.617 1.00 16.06  ? 3510 SER A CA    1 
ATOM   14726 C  C     . SER A 1 3510 ? 164.898 134.024 202.541 1.00 17.53  ? 3510 SER A C     1 
ATOM   14727 O  O     . SER A 1 3510 ? 164.347 134.395 201.499 1.00 18.19  ? 3510 SER A O     1 
ATOM   14728 C  CB    . SER A 1 3510 ? 164.697 131.676 203.400 1.00 23.44  ? 3510 SER A CB    1 
ATOM   14729 O  OG    . SER A 1 3510 ? 165.359 130.436 203.564 1.00 30.38  ? 3510 SER A OG    1 
ATOM   14730 N  N     . ALA A 1 3511 ? 164.945 134.792 203.633 1.00 19.67  ? 3511 ALA A N     1 
ATOM   14731 C  CA    . ALA A 1 3511 ? 164.312 136.107 203.644 1.00 17.08  ? 3511 ALA A CA    1 
ATOM   14732 C  C     . ALA A 1 3511 ? 164.960 137.041 202.632 1.00 16.68  ? 3511 ALA A C     1 
ATOM   14733 O  O     . ALA A 1 3511 ? 164.269 137.814 201.958 1.00 21.17  ? 3511 ALA A O     1 
ATOM   14734 C  CB    . ALA A 1 3511 ? 164.376 136.710 205.046 1.00 19.19  ? 3511 ALA A CB    1 
ATOM   14735 N  N     . ALA A 1 3512 ? 166.289 136.993 202.519 1.00 16.60  ? 3512 ALA A N     1 
ATOM   14736 C  CA    . ALA A 1 3512 ? 166.976 137.806 201.523 1.00 11.61  ? 3512 ALA A CA    1 
ATOM   14737 C  C     . ALA A 1 3512 ? 166.578 137.398 200.112 1.00 15.75  ? 3512 ALA A C     1 
ATOM   14738 O  O     . ALA A 1 3512 ? 166.494 138.242 199.213 1.00 20.20  ? 3512 ALA A O     1 
ATOM   14739 C  CB    . ALA A 1 3512 ? 168.489 137.697 201.708 1.00 13.02  ? 3512 ALA A CB    1 
ATOM   14740 N  N     . PHE A 1 3513 ? 166.333 136.104 199.897 1.00 15.96  ? 3513 PHE A N     1 
ATOM   14741 C  CA    . PHE A 1 3513 ? 165.942 135.636 198.573 1.00 15.71  ? 3513 PHE A CA    1 
ATOM   14742 C  C     . PHE A 1 3513 ? 164.569 136.168 198.177 1.00 19.91  ? 3513 PHE A C     1 
ATOM   14743 O  O     . PHE A 1 3513 ? 164.363 136.579 197.029 1.00 25.40  ? 3513 PHE A O     1 
ATOM   14744 C  CB    . PHE A 1 3513 ? 165.961 134.109 198.531 1.00 16.98  ? 3513 PHE A CB    1 
ATOM   14745 C  CG    . PHE A 1 3513 ? 165.908 133.542 197.144 1.00 19.63  ? 3513 PHE A CG    1 
ATOM   14746 C  CD1   . PHE A 1 3513 ? 167.055 133.462 196.373 1.00 21.21  ? 3513 PHE A CD1   1 
ATOM   14747 C  CD2   . PHE A 1 3513 ? 164.714 133.087 196.610 1.00 21.18  ? 3513 PHE A CD2   1 
ATOM   14748 C  CE1   . PHE A 1 3513 ? 167.013 132.945 195.095 1.00 21.37  ? 3513 PHE A CE1   1 
ATOM   14749 C  CE2   . PHE A 1 3513 ? 164.666 132.567 195.331 1.00 24.41  ? 3513 PHE A CE2   1 
ATOM   14750 C  CZ    . PHE A 1 3513 ? 165.818 132.496 194.573 1.00 24.43  ? 3513 PHE A CZ    1 
ATOM   14751 N  N     . ILE A 1 3514 ? 163.617 136.173 199.113 1.00 17.56  ? 3514 ILE A N     1 
ATOM   14752 C  CA    . ILE A 1 3514 ? 162.268 136.634 198.797 1.00 15.17  ? 3514 ILE A CA    1 
ATOM   14753 C  C     . ILE A 1 3514 ? 162.257 138.140 198.565 1.00 20.21  ? 3514 ILE A C     1 
ATOM   14754 O  O     . ILE A 1 3514 ? 161.617 138.637 197.631 1.00 27.38  ? 3514 ILE A O     1 
ATOM   14755 C  CB    . ILE A 1 3514 ? 161.283 136.236 199.911 1.00 13.14  ? 3514 ILE A CB    1 
ATOM   14756 C  CG1   . ILE A 1 3514 ? 161.477 134.775 200.312 1.00 16.45  ? 3514 ILE A CG1   1 
ATOM   14757 C  CG2   . ILE A 1 3514 ? 159.850 136.474 199.464 1.00 19.45  ? 3514 ILE A CG2   1 
ATOM   14758 C  CD1   . ILE A 1 3514 ? 161.103 134.490 201.749 1.00 20.38  ? 3514 ILE A CD1   1 
ATOM   14759 N  N     . ALA A 1 3515 ? 162.962 138.888 199.413 1.00 16.43  ? 3515 ALA A N     1 
ATOM   14760 C  CA    . ALA A 1 3515 ? 162.885 140.343 199.371 1.00 11.27  ? 3515 ALA A CA    1 
ATOM   14761 C  C     . ALA A 1 3515 ? 163.658 140.946 198.206 1.00 11.56  ? 3515 ALA A C     1 
ATOM   14762 O  O     . ALA A 1 3515 ? 163.331 142.053 197.765 1.00 14.91  ? 3515 ALA A O     1 
ATOM   14763 C  CB    . ALA A 1 3515 ? 163.398 140.931 200.685 1.00 13.58  ? 3515 ALA A CB    1 
ATOM   14764 N  N     . TYR A 1 3516 ? 164.676 140.255 197.696 1.00 13.70  ? 3516 TYR A N     1 
ATOM   14765 C  CA    . TYR A 1 3516 ? 165.628 140.861 196.774 1.00 9.30   ? 3516 TYR A CA    1 
ATOM   14766 C  C     . TYR A 1 3516 ? 165.674 140.192 195.409 1.00 11.73  ? 3516 TYR A C     1 
ATOM   14767 O  O     . TYR A 1 3516 ? 165.733 140.882 194.387 1.00 15.56  ? 3516 TYR A O     1 
ATOM   14768 C  CB    . TYR A 1 3516 ? 167.032 140.835 197.393 1.00 9.59   ? 3516 TYR A CB    1 
ATOM   14769 C  CG    . TYR A 1 3516 ? 167.232 141.782 198.553 1.00 9.68   ? 3516 TYR A CG    1 
ATOM   14770 C  CD1   . TYR A 1 3516 ? 167.192 143.155 198.371 1.00 7.84   ? 3516 TYR A CD1   1 
ATOM   14771 C  CD2   . TYR A 1 3516 ? 167.481 141.299 199.829 1.00 11.97  ? 3516 TYR A CD2   1 
ATOM   14772 C  CE1   . TYR A 1 3516 ? 167.388 144.019 199.428 1.00 8.46   ? 3516 TYR A CE1   1 
ATOM   14773 C  CE2   . TYR A 1 3516 ? 167.675 142.156 200.891 1.00 10.04  ? 3516 TYR A CE2   1 
ATOM   14774 C  CZ    . TYR A 1 3516 ? 167.626 143.514 200.685 1.00 9.62   ? 3516 TYR A CZ    1 
ATOM   14775 O  OH    . TYR A 1 3516 ? 167.820 144.371 201.742 1.00 11.65  ? 3516 TYR A OH    1 
ATOM   14776 N  N     . ALA A 1 3517 ? 165.642 138.863 195.360 1.00 12.43  ? 3517 ALA A N     1 
ATOM   14777 C  CA    . ALA A 1 3517 ? 166.004 138.116 194.160 1.00 14.25  ? 3517 ALA A CA    1 
ATOM   14778 C  C     . ALA A 1 3517 ? 164.854 137.937 193.176 1.00 11.18  ? 3517 ALA A C     1 
ATOM   14779 O  O     . ALA A 1 3517 ? 164.993 137.154 192.231 1.00 12.87  ? 3517 ALA A O     1 
ATOM   14780 C  CB    . ALA A 1 3517 ? 166.563 136.746 194.550 1.00 17.28  ? 3517 ALA A CB    1 
ATOM   14781 N  N     . GLY A 1 3518 ? 163.731 138.629 193.367 1.00 13.12  ? 3518 GLY A N     1 
ATOM   14782 C  CA    . GLY A 1 3518 ? 162.586 138.408 192.498 1.00 11.90  ? 3518 GLY A CA    1 
ATOM   14783 C  C     . GLY A 1 3518 ? 162.815 138.850 191.064 1.00 11.74  ? 3518 GLY A C     1 
ATOM   14784 O  O     . GLY A 1 3518 ? 162.389 138.174 190.123 1.00 13.45  ? 3518 GLY A O     1 
ATOM   14785 N  N     . TYR A 1 3519 ? 163.485 139.988 190.874 1.00 13.40  ? 3519 TYR A N     1 
ATOM   14786 C  CA    . TYR A 1 3519 ? 163.631 140.551 189.535 1.00 11.32  ? 3519 TYR A CA    1 
ATOM   14787 C  C     . TYR A 1 3519 ? 164.669 139.821 188.692 1.00 12.59  ? 3519 TYR A C     1 
ATOM   14788 O  O     . TYR A 1 3519 ? 164.533 139.767 187.465 1.00 20.73  ? 3519 TYR A O     1 
ATOM   14789 C  CB    . TYR A 1 3519 ? 163.993 142.035 189.622 1.00 15.81  ? 3519 TYR A CB    1 
ATOM   14790 C  CG    . TYR A 1 3519 ? 164.245 142.674 188.276 1.00 19.08  ? 3519 TYR A CG    1 
ATOM   14791 C  CD1   . TYR A 1 3519 ? 163.219 142.829 187.354 1.00 21.47  ? 3519 TYR A CD1   1 
ATOM   14792 C  CD2   . TYR A 1 3519 ? 165.511 143.125 187.927 1.00 20.91  ? 3519 TYR A CD2   1 
ATOM   14793 C  CE1   . TYR A 1 3519 ? 163.448 143.408 186.123 1.00 25.85  ? 3519 TYR A CE1   1 
ATOM   14794 C  CE2   . TYR A 1 3519 ? 165.748 143.709 186.699 1.00 30.14  ? 3519 TYR A CE2   1 
ATOM   14795 C  CZ    . TYR A 1 3519 ? 164.713 143.849 185.801 1.00 29.89  ? 3519 TYR A CZ    1 
ATOM   14796 O  OH    . TYR A 1 3519 ? 164.944 144.431 184.576 1.00 36.56  ? 3519 TYR A OH    1 
ATOM   14797 N  N     . PHE A 1 3520 ? 165.696 139.255 189.315 1.00 12.59  ? 3520 PHE A N     1 
ATOM   14798 C  CA    . PHE A 1 3520 ? 166.808 138.702 188.561 1.00 14.60  ? 3520 PHE A CA    1 
ATOM   14799 C  C     . PHE A 1 3520 ? 166.481 137.312 188.024 1.00 16.40  ? 3520 PHE A C     1 
ATOM   14800 O  O     . PHE A 1 3520 ? 165.542 136.645 188.465 1.00 18.85  ? 3520 PHE A O     1 
ATOM   14801 C  CB    . PHE A 1 3520 ? 168.069 138.660 189.424 1.00 17.17  ? 3520 PHE A CB    1 
ATOM   14802 C  CG    . PHE A 1 3520 ? 168.275 139.899 190.243 1.00 15.28  ? 3520 PHE A CG    1 
ATOM   14803 C  CD1   . PHE A 1 3520 ? 168.938 140.989 189.710 1.00 14.83  ? 3520 PHE A CD1   1 
ATOM   14804 C  CD2   . PHE A 1 3520 ? 167.804 139.976 191.541 1.00 16.12  ? 3520 PHE A CD2   1 
ATOM   14805 C  CE1   . PHE A 1 3520 ? 169.128 142.132 190.454 1.00 16.47  ? 3520 PHE A CE1   1 
ATOM   14806 C  CE2   . PHE A 1 3520 ? 167.992 141.117 192.289 1.00 20.66  ? 3520 PHE A CE2   1 
ATOM   14807 C  CZ    . PHE A 1 3520 ? 168.654 142.197 191.744 1.00 21.95  ? 3520 PHE A CZ    1 
ATOM   14808 N  N     . ASP A 1 3521 ? 167.277 136.887 187.047 1.00 20.50  ? 3521 ASP A N     1 
ATOM   14809 C  CA    . ASP A 1 3521 ? 167.086 135.609 186.377 1.00 20.63  ? 3521 ASP A CA    1 
ATOM   14810 C  C     . ASP A 1 3521 ? 167.725 134.494 187.202 1.00 20.53  ? 3521 ASP A C     1 
ATOM   14811 O  O     . ASP A 1 3521 ? 168.195 134.706 188.323 1.00 22.12  ? 3521 ASP A O     1 
ATOM   14812 C  CB    . ASP A 1 3521 ? 167.653 135.668 184.962 1.00 20.61  ? 3521 ASP A CB    1 
ATOM   14813 C  CG    . ASP A 1 3521 ? 168.960 136.429 184.893 1.00 34.71  ? 3521 ASP A CG    1 
ATOM   14814 O  OD1   . ASP A 1 3521 ? 169.590 136.432 183.816 1.00 40.85  ? 3521 ASP A OD1   1 
ATOM   14815 O  OD2   . ASP A 1 3521 ? 169.358 137.022 185.917 1.00 33.21  ? 3521 ASP A OD2   1 
ATOM   14816 N  N     . GLN A 1 3522 ? 167.749 133.284 186.641 1.00 20.51  ? 3522 GLN A N     1 
ATOM   14817 C  CA    . GLN A 1 3522 ? 168.253 132.126 187.374 1.00 18.55  ? 3522 GLN A CA    1 
ATOM   14818 C  C     . GLN A 1 3522 ? 169.728 132.285 187.723 1.00 23.45  ? 3522 GLN A C     1 
ATOM   14819 O  O     . GLN A 1 3522 ? 170.148 131.980 188.846 1.00 23.96  ? 3522 GLN A O     1 
ATOM   14820 C  CB    . GLN A 1 3522 ? 168.026 130.856 186.552 1.00 18.24  ? 3522 GLN A CB    1 
ATOM   14821 C  CG    . GLN A 1 3522 ? 168.873 129.673 186.984 1.00 18.96  ? 3522 GLN A CG    1 
ATOM   14822 C  CD    . GLN A 1 3522 ? 168.109 128.367 186.940 1.00 25.16  ? 3522 GLN A CD    1 
ATOM   14823 O  OE1   . GLN A 1 3522 ? 166.879 128.354 186.969 1.00 28.15  ? 3522 GLN A OE1   1 
ATOM   14824 N  NE2   . GLN A 1 3522 ? 168.836 127.258 186.872 1.00 29.72  ? 3522 GLN A NE2   1 
ATOM   14825 N  N     . GLN A 1 3523 ? 170.532 132.761 186.770 1.00 24.09  ? 3523 GLN A N     1 
ATOM   14826 C  CA    . GLN A 1 3523 ? 171.972 132.845 186.996 1.00 23.88  ? 3523 GLN A CA    1 
ATOM   14827 C  C     . GLN A 1 3523 ? 172.312 133.851 188.089 1.00 24.72  ? 3523 GLN A C     1 
ATOM   14828 O  O     . GLN A 1 3523 ? 173.141 133.569 188.961 1.00 25.16  ? 3523 GLN A O     1 
ATOM   14829 C  CB    . GLN A 1 3523 ? 172.689 133.206 185.695 1.00 24.32  ? 3523 GLN A CB    1 
ATOM   14830 C  CG    . GLN A 1 3523 ? 174.163 132.834 185.684 1.00 33.61  ? 3523 GLN A CG    1 
ATOM   14831 C  CD    . GLN A 1 3523 ? 175.056 133.986 185.269 1.00 40.74  ? 3523 GLN A CD    1 
ATOM   14832 O  OE1   . GLN A 1 3523 ? 174.733 135.152 185.499 1.00 31.94  ? 3523 GLN A OE1   1 
ATOM   14833 N  NE2   . GLN A 1 3523 ? 176.188 133.665 184.655 1.00 45.61  ? 3523 GLN A NE2   1 
ATOM   14834 N  N     . MET A 1 3524 ? 171.683 135.029 188.063 1.00 23.44  ? 3524 MET A N     1 
ATOM   14835 C  CA    . MET A 1 3524 ? 171.993 136.041 189.067 1.00 25.86  ? 3524 MET A CA    1 
ATOM   14836 C  C     . MET A 1 3524 ? 171.467 135.659 190.444 1.00 24.82  ? 3524 MET A C     1 
ATOM   14837 O  O     . MET A 1 3524 ? 172.102 135.980 191.454 1.00 25.98  ? 3524 MET A O     1 
ATOM   14838 C  CB    . MET A 1 3524 ? 171.441 137.402 188.642 1.00 26.40  ? 3524 MET A CB    1 
ATOM   14839 C  CG    . MET A 1 3524 ? 172.147 138.574 189.307 1.00 31.89  ? 3524 MET A CG    1 
ATOM   14840 S  SD    . MET A 1 3524 ? 173.875 138.730 188.815 1.00 57.78  ? 3524 MET A SD    1 
ATOM   14841 C  CE    . MET A 1 3524 ? 173.842 140.283 187.927 1.00 46.05  ? 3524 MET A CE    1 
ATOM   14842 N  N     . ARG A 1 3525 ? 170.321 134.975 190.508 1.00 20.33  ? 3525 ARG A N     1 
ATOM   14843 C  CA    . ARG A 1 3525 ? 169.801 134.532 191.799 1.00 18.60  ? 3525 ARG A CA    1 
ATOM   14844 C  C     . ARG A 1 3525 ? 170.778 133.591 192.490 1.00 21.43  ? 3525 ARG A C     1 
ATOM   14845 O  O     . ARG A 1 3525 ? 170.947 133.647 193.713 1.00 27.22  ? 3525 ARG A O     1 
ATOM   14846 C  CB    . ARG A 1 3525 ? 168.442 133.855 191.620 1.00 18.42  ? 3525 ARG A CB    1 
ATOM   14847 C  CG    . ARG A 1 3525 ? 167.299 134.810 191.329 1.00 15.61  ? 3525 ARG A CG    1 
ATOM   14848 C  CD    . ARG A 1 3525 ? 165.978 134.069 191.229 1.00 13.28  ? 3525 ARG A CD    1 
ATOM   14849 N  NE    . ARG A 1 3525 ? 164.971 134.851 190.523 1.00 12.21  ? 3525 ARG A NE    1 
ATOM   14850 C  CZ    . ARG A 1 3525 ? 163.672 134.588 190.536 1.00 9.99   ? 3525 ARG A CZ    1 
ATOM   14851 N  NH1   . ARG A 1 3525 ? 163.182 133.561 191.211 1.00 12.25  ? 3525 ARG A NH1   1 
ATOM   14852 N  NH2   . ARG A 1 3525 ? 162.843 135.374 189.855 1.00 12.78  ? 3525 ARG A NH2   1 
ATOM   14853 N  N     . GLN A 1 3526 ? 171.426 132.713 191.722 1.00 24.58  ? 3526 GLN A N     1 
ATOM   14854 C  CA    . GLN A 1 3526 ? 172.439 131.838 192.302 1.00 23.44  ? 3526 GLN A CA    1 
ATOM   14855 C  C     . GLN A 1 3526 ? 173.661 132.631 192.747 1.00 22.05  ? 3526 GLN A C     1 
ATOM   14856 O  O     . GLN A 1 3526 ? 174.286 132.304 193.762 1.00 25.61  ? 3526 GLN A O     1 
ATOM   14857 C  CB    . GLN A 1 3526 ? 172.835 130.756 191.299 1.00 22.47  ? 3526 GLN A CB    1 
ATOM   14858 C  CG    . GLN A 1 3526 ? 173.440 129.517 191.936 1.00 21.71  ? 3526 GLN A CG    1 
ATOM   14859 C  CD    . GLN A 1 3526 ? 172.662 129.051 193.151 1.00 30.30  ? 3526 GLN A CD    1 
ATOM   14860 O  OE1   . GLN A 1 3526 ? 171.473 128.748 193.062 1.00 31.23  ? 3526 GLN A OE1   1 
ATOM   14861 N  NE2   . GLN A 1 3526 ? 173.332 128.994 194.296 1.00 30.48  ? 3526 GLN A NE2   1 
ATOM   14862 N  N     . ASN A 1 3527 ? 174.023 133.674 191.994 1.00 20.49  ? 3527 ASN A N     1 
ATOM   14863 C  CA    . ASN A 1 3527 ? 175.176 134.488 192.365 1.00 21.25  ? 3527 ASN A CA    1 
ATOM   14864 C  C     . ASN A 1 3527 ? 174.957 135.185 193.701 1.00 24.54  ? 3527 ASN A C     1 
ATOM   14865 O  O     . ASN A 1 3527 ? 175.856 135.207 194.551 1.00 29.07  ? 3527 ASN A O     1 
ATOM   14866 C  CB    . ASN A 1 3527 ? 175.475 135.514 191.271 1.00 24.70  ? 3527 ASN A CB    1 
ATOM   14867 C  CG    . ASN A 1 3527 ? 175.797 134.870 189.939 1.00 32.55  ? 3527 ASN A CG    1 
ATOM   14868 O  OD1   . ASN A 1 3527 ? 176.333 133.763 189.883 1.00 36.61  ? 3527 ASN A OD1   1 
ATOM   14869 N  ND2   . ASN A 1 3527 ? 175.476 135.565 188.854 1.00 35.05  ? 3527 ASN A ND2   1 
ATOM   14870 N  N     . LEU A 1 3528 ? 173.773 135.768 193.905 1.00 22.97  ? 3528 LEU A N     1 
ATOM   14871 C  CA    . LEU A 1 3528 ? 173.496 136.440 195.171 1.00 16.93  ? 3528 LEU A CA    1 
ATOM   14872 C  C     . LEU A 1 3528 ? 173.463 135.450 196.329 1.00 17.09  ? 3528 LEU A C     1 
ATOM   14873 O  O     . LEU A 1 3528 ? 174.009 135.723 197.403 1.00 23.31  ? 3528 LEU A O     1 
ATOM   14874 C  CB    . LEU A 1 3528 ? 172.181 137.214 195.089 1.00 14.72  ? 3528 LEU A CB    1 
ATOM   14875 C  CG    . LEU A 1 3528 ? 172.096 138.322 194.038 1.00 18.01  ? 3528 LEU A CG    1 
ATOM   14876 C  CD1   . LEU A 1 3528 ? 170.807 138.218 193.237 1.00 22.13  ? 3528 LEU A CD1   1 
ATOM   14877 C  CD2   . LEU A 1 3528 ? 172.224 139.688 194.687 1.00 16.05  ? 3528 LEU A CD2   1 
ATOM   14878 N  N     . PHE A 1 3529 ? 172.828 134.292 196.128 1.00 14.40  ? 3529 PHE A N     1 
ATOM   14879 C  CA    . PHE A 1 3529 ? 172.765 133.292 197.190 1.00 20.21  ? 3529 PHE A CA    1 
ATOM   14880 C  C     . PHE A 1 3529 ? 174.154 132.775 197.543 1.00 26.65  ? 3529 PHE A C     1 
ATOM   14881 O  O     . PHE A 1 3529 ? 174.471 132.583 198.723 1.00 28.40  ? 3529 PHE A O     1 
ATOM   14882 C  CB    . PHE A 1 3529 ? 171.853 132.140 196.774 1.00 23.67  ? 3529 PHE A CB    1 
ATOM   14883 C  CG    . PHE A 1 3529 ? 171.236 131.410 197.931 1.00 25.35  ? 3529 PHE A CG    1 
ATOM   14884 C  CD1   . PHE A 1 3529 ? 170.137 131.934 198.590 1.00 24.70  ? 3529 PHE A CD1   1 
ATOM   14885 C  CD2   . PHE A 1 3529 ? 171.757 130.202 198.362 1.00 22.88  ? 3529 PHE A CD2   1 
ATOM   14886 C  CE1   . PHE A 1 3529 ? 169.568 131.265 199.656 1.00 22.50  ? 3529 PHE A CE1   1 
ATOM   14887 C  CE2   . PHE A 1 3529 ? 171.192 129.529 199.428 1.00 23.68  ? 3529 PHE A CE2   1 
ATOM   14888 C  CZ    . PHE A 1 3529 ? 170.097 130.061 200.075 1.00 22.59  ? 3529 PHE A CZ    1 
ATOM   14889 N  N     . THR A 1 3530 ? 174.993 132.536 196.533 1.00 24.47  ? 3530 THR A N     1 
ATOM   14890 C  CA    . THR A 1 3530 ? 176.367 132.120 196.798 1.00 24.34  ? 3530 THR A CA    1 
ATOM   14891 C  C     . THR A 1 3530 ? 177.142 133.220 197.512 1.00 26.85  ? 3530 THR A C     1 
ATOM   14892 O  O     . THR A 1 3530 ? 177.923 132.945 198.431 1.00 29.12  ? 3530 THR A O     1 
ATOM   14893 C  CB    . THR A 1 3530 ? 177.055 131.730 195.488 1.00 27.10  ? 3530 THR A CB    1 
ATOM   14894 O  OG1   . THR A 1 3530 ? 176.453 130.538 194.970 1.00 23.76  ? 3530 THR A OG1   1 
ATOM   14895 C  CG2   . THR A 1 3530 ? 178.539 131.479 195.710 1.00 34.60  ? 3530 THR A CG2   1 
ATOM   14896 N  N     . THR A 1 3531 ? 176.932 134.476 197.109 1.00 23.28  ? 3531 THR A N     1 
ATOM   14897 C  CA    . THR A 1 3531 ? 177.603 135.593 197.767 1.00 22.85  ? 3531 THR A CA    1 
ATOM   14898 C  C     . THR A 1 3531 ? 177.181 135.707 199.227 1.00 24.05  ? 3531 THR A C     1 
ATOM   14899 O  O     . THR A 1 3531 ? 178.017 135.914 200.113 1.00 30.29  ? 3531 THR A O     1 
ATOM   14900 C  CB    . THR A 1 3531 ? 177.309 136.894 197.018 1.00 20.59  ? 3531 THR A CB    1 
ATOM   14901 O  OG1   . THR A 1 3531 ? 177.676 136.748 195.640 1.00 21.23  ? 3531 THR A OG1   1 
ATOM   14902 C  CG2   . THR A 1 3531 ? 178.091 138.049 197.625 1.00 18.19  ? 3531 THR A CG2   1 
ATOM   14903 N  N     . TRP A 1 3532 ? 175.879 135.579 199.497 1.00 19.42  ? 3532 TRP A N     1 
ATOM   14904 C  CA    . TRP A 1 3532 ? 175.404 135.631 200.877 1.00 22.96  ? 3532 TRP A CA    1 
ATOM   14905 C  C     . TRP A 1 3532 ? 175.898 134.434 201.679 1.00 26.31  ? 3532 TRP A C     1 
ATOM   14906 O  O     . TRP A 1 3532 ? 176.297 134.578 202.841 1.00 27.30  ? 3532 TRP A O     1 
ATOM   14907 C  CB    . TRP A 1 3532 ? 173.877 135.698 200.912 1.00 23.59  ? 3532 TRP A CB    1 
ATOM   14908 C  CG    . TRP A 1 3532 ? 173.279 136.797 200.092 1.00 18.43  ? 3532 TRP A CG    1 
ATOM   14909 C  CD1   . TRP A 1 3532 ? 173.849 137.995 199.781 1.00 16.35  ? 3532 TRP A CD1   1 
ATOM   14910 C  CD2   . TRP A 1 3532 ? 171.987 136.796 199.477 1.00 14.34  ? 3532 TRP A CD2   1 
ATOM   14911 N  NE1   . TRP A 1 3532 ? 172.992 138.742 199.010 1.00 14.70  ? 3532 TRP A NE1   1 
ATOM   14912 C  CE2   . TRP A 1 3532 ? 171.841 138.027 198.808 1.00 12.66  ? 3532 TRP A CE2   1 
ATOM   14913 C  CE3   . TRP A 1 3532 ? 170.939 135.872 199.426 1.00 14.01  ? 3532 TRP A CE3   1 
ATOM   14914 C  CZ2   . TRP A 1 3532 ? 170.690 138.359 198.098 1.00 14.04  ? 3532 TRP A CZ2   1 
ATOM   14915 C  CZ3   . TRP A 1 3532 ? 169.799 136.202 198.721 1.00 11.30  ? 3532 TRP A CZ3   1 
ATOM   14916 C  CH2   . TRP A 1 3532 ? 169.683 137.435 198.066 1.00 13.55  ? 3532 TRP A CH2   1 
ATOM   14917 N  N     . SER A 1 3533 ? 175.873 133.241 201.078 1.00 32.17  ? 3533 SER A N     1 
ATOM   14918 C  CA    . SER A 1 3533 ? 176.302 132.041 201.791 1.00 32.70  ? 3533 SER A CA    1 
ATOM   14919 C  C     . SER A 1 3533 ? 177.785 132.101 202.134 1.00 35.08  ? 3533 SER A C     1 
ATOM   14920 O  O     . SER A 1 3533 ? 178.203 131.640 203.203 1.00 35.69  ? 3533 SER A O     1 
ATOM   14921 C  CB    . SER A 1 3533 ? 175.992 130.797 200.959 1.00 30.59  ? 3533 SER A CB    1 
ATOM   14922 O  OG    . SER A 1 3533 ? 174.648 130.806 200.510 1.00 37.14  ? 3533 SER A OG    1 
ATOM   14923 N  N     . HIS A 1 3534 ? 178.598 132.658 201.233 1.00 28.74  ? 3534 HIS A N     1 
ATOM   14924 C  CA    . HIS A 1 3534 ? 180.019 132.820 201.521 1.00 33.63  ? 3534 HIS A CA    1 
ATOM   14925 C  C     . HIS A 1 3534 ? 180.235 133.747 202.710 1.00 34.93  ? 3534 HIS A C     1 
ATOM   14926 O  O     . HIS A 1 3534 ? 181.108 133.499 203.551 1.00 42.35  ? 3534 HIS A O     1 
ATOM   14927 C  CB    . HIS A 1 3534 ? 180.747 133.354 200.287 1.00 38.04  ? 3534 HIS A CB    1 
ATOM   14928 C  CG    . HIS A 1 3534 ? 181.152 132.290 199.316 1.00 46.50  ? 3534 HIS A CG    1 
ATOM   14929 N  ND1   . HIS A 1 3534 ? 181.396 132.552 197.985 1.00 49.62  ? 3534 HIS A ND1   1 
ATOM   14930 C  CD2   . HIS A 1 3534 ? 181.355 130.961 199.481 1.00 45.76  ? 3534 HIS A CD2   1 
ATOM   14931 C  CE1   . HIS A 1 3534 ? 181.732 131.431 197.372 1.00 52.63  ? 3534 HIS A CE1   1 
ATOM   14932 N  NE2   . HIS A 1 3534 ? 181.715 130.451 198.258 1.00 50.72  ? 3534 HIS A NE2   1 
ATOM   14933 N  N     . HIS A 1 3535 ? 179.454 134.826 202.791 1.00 32.41  ? 3535 HIS A N     1 
ATOM   14934 C  CA    . HIS A 1 3535 ? 179.590 135.762 203.901 1.00 31.47  ? 3535 HIS A CA    1 
ATOM   14935 C  C     . HIS A 1 3535 ? 179.226 135.109 205.229 1.00 33.25  ? 3535 HIS A C     1 
ATOM   14936 O  O     . HIS A 1 3535 ? 179.917 135.306 206.235 1.00 42.26  ? 3535 HIS A O     1 
ATOM   14937 C  CB    . HIS A 1 3535 ? 178.722 136.993 203.650 1.00 26.09  ? 3535 HIS A CB    1 
ATOM   14938 C  CG    . HIS A 1 3535 ? 178.920 138.089 204.650 1.00 28.34  ? 3535 HIS A CG    1 
ATOM   14939 N  ND1   . HIS A 1 3535 ? 178.230 138.144 205.841 1.00 26.76  ? 3535 HIS A ND1   1 
ATOM   14940 C  CD2   . HIS A 1 3535 ? 179.729 139.175 204.633 1.00 27.64  ? 3535 HIS A CD2   1 
ATOM   14941 C  CE1   . HIS A 1 3535 ? 178.605 139.216 206.516 1.00 30.69  ? 3535 HIS A CE1   1 
ATOM   14942 N  NE2   . HIS A 1 3535 ? 179.514 139.859 205.805 1.00 34.78  ? 3535 HIS A NE2   1 
ATOM   14943 N  N     . LEU A 1 3536 ? 178.142 134.329 205.255 1.00 28.11  ? 3536 LEU A N     1 
ATOM   14944 C  CA    . LEU A 1 3536 ? 177.726 133.692 206.500 1.00 33.56  ? 3536 LEU A CA    1 
ATOM   14945 C  C     . LEU A 1 3536 ? 178.718 132.621 206.936 1.00 43.13  ? 3536 LEU A C     1 
ATOM   14946 O  O     . LEU A 1 3536 ? 178.985 132.467 208.133 1.00 45.94  ? 3536 LEU A O     1 
ATOM   14947 C  CB    . LEU A 1 3536 ? 176.328 133.094 206.349 1.00 35.04  ? 3536 LEU A CB    1 
ATOM   14948 C  CG    . LEU A 1 3536 ? 175.178 134.080 206.143 1.00 30.76  ? 3536 LEU A CG    1 
ATOM   14949 C  CD1   . LEU A 1 3536 ? 173.878 133.331 205.930 1.00 31.84  ? 3536 LEU A CD1   1 
ATOM   14950 C  CD2   . LEU A 1 3536 ? 175.062 135.034 207.314 1.00 31.66  ? 3536 LEU A CD2   1 
ATOM   14951 N  N     . GLN A 1 3537 ? 179.263 131.862 205.981 1.00 43.62  ? 3537 GLN A N     1 
ATOM   14952 C  CA    . GLN A 1 3537 ? 180.279 130.869 206.319 1.00 41.41  ? 3537 GLN A CA    1 
ATOM   14953 C  C     . GLN A 1 3537 ? 181.521 131.530 206.900 1.00 44.77  ? 3537 GLN A C     1 
ATOM   14954 O  O     . GLN A 1 3537 ? 182.067 131.069 207.909 1.00 52.88  ? 3537 GLN A O     1 
ATOM   14955 C  CB    . GLN A 1 3537 ? 180.646 130.048 205.084 1.00 42.74  ? 3537 GLN A CB    1 
ATOM   14956 C  CG    . GLN A 1 3537 ? 179.768 128.833 204.853 1.00 49.51  ? 3537 GLN A CG    1 
ATOM   14957 C  CD    . GLN A 1 3537 ? 180.078 128.136 203.543 1.00 50.81  ? 3537 GLN A CD    1 
ATOM   14958 O  OE1   . GLN A 1 3537 ? 181.063 128.452 202.876 1.00 51.87  ? 3537 GLN A OE1   1 
ATOM   14959 N  NE2   . GLN A 1 3537 ? 179.235 127.183 203.167 1.00 47.75  ? 3537 GLN A NE2   1 
ATOM   14960 N  N     . GLN A 1 3538 ? 181.978 132.618 206.278 1.00 39.59  ? 3538 GLN A N     1 
ATOM   14961 C  CA    . GLN A 1 3538 ? 183.167 133.309 206.756 1.00 46.32  ? 3538 GLN A CA    1 
ATOM   14962 C  C     . GLN A 1 3538 ? 182.906 134.056 208.060 1.00 47.97  ? 3538 GLN A C     1 
ATOM   14963 O  O     . GLN A 1 3538 ? 183.851 134.322 208.811 1.00 52.92  ? 3538 GLN A O     1 
ATOM   14964 C  CB    . GLN A 1 3538 ? 183.680 134.244 205.652 1.00 41.87  ? 3538 GLN A CB    1 
ATOM   14965 C  CG    . GLN A 1 3538 ? 184.236 135.578 206.104 1.00 53.40  ? 3538 GLN A CG    1 
ATOM   14966 C  CD    . GLN A 1 3538 ? 184.785 136.401 204.955 1.00 60.11  ? 3538 GLN A CD    1 
ATOM   14967 O  OE1   . GLN A 1 3538 ? 184.047 137.128 204.289 1.00 54.50  ? 3538 GLN A OE1   1 
ATOM   14968 N  NE2   . GLN A 1 3538 ? 186.086 136.292 204.717 1.00 66.72  ? 3538 GLN A NE2   1 
ATOM   14969 N  N     . ALA A 1 3539 ? 181.644 134.352 208.369 1.00 44.19  ? 3539 ALA A N     1 
ATOM   14970 C  CA    . ALA A 1 3539 ? 181.268 135.004 209.616 1.00 47.14  ? 3539 ALA A CA    1 
ATOM   14971 C  C     . ALA A 1 3539 ? 180.855 134.012 210.696 1.00 43.19  ? 3539 ALA A C     1 
ATOM   14972 O  O     . ALA A 1 3539 ? 180.329 134.426 211.734 1.00 43.55  ? 3539 ALA A O     1 
ATOM   14973 C  CB    . ALA A 1 3539 ? 180.139 136.008 209.371 1.00 45.09  ? 3539 ALA A CB    1 
ATOM   14974 N  N     . ASN A 1 3540 ? 181.076 132.715 210.468 1.00 44.69  ? 3540 ASN A N     1 
ATOM   14975 C  CA    . ASN A 1 3540 ? 180.797 131.668 211.455 1.00 46.54  ? 3540 ASN A CA    1 
ATOM   14976 C  C     . ASN A 1 3540 ? 179.324 131.650 211.862 1.00 45.67  ? 3540 ASN A C     1 
ATOM   14977 O  O     . ASN A 1 3540 ? 178.988 131.500 213.038 1.00 46.47  ? 3540 ASN A O     1 
ATOM   14978 C  CB    . ASN A 1 3540 ? 181.696 131.815 212.685 1.00 51.40  ? 3540 ASN A CB    1 
ATOM   14979 C  CG    . ASN A 1 3540 ? 183.135 131.427 212.405 1.00 52.41  ? 3540 ASN A CG    1 
ATOM   14980 O  OD1   . ASN A 1 3540 ? 183.505 131.151 211.264 1.00 51.99  ? 3540 ASN A OD1   1 
ATOM   14981 N  ND2   . ASN A 1 3540 ? 183.956 131.408 213.448 1.00 55.62  ? 3540 ASN A ND2   1 
ATOM   14982 N  N     . ILE A 1 3541 ? 178.438 131.802 210.883 1.00 46.52  ? 3541 ILE A N     1 
ATOM   14983 C  CA    . ILE A 1 3541 ? 176.997 131.716 211.097 1.00 43.55  ? 3541 ILE A CA    1 
ATOM   14984 C  C     . ILE A 1 3541 ? 176.510 130.425 210.453 1.00 49.27  ? 3541 ILE A C     1 
ATOM   14985 O  O     . ILE A 1 3541 ? 176.687 130.218 209.245 1.00 44.77  ? 3541 ILE A O     1 
ATOM   14986 C  CB    . ILE A 1 3541 ? 176.262 132.939 210.530 1.00 36.60  ? 3541 ILE A CB    1 
ATOM   14987 C  CG1   . ILE A 1 3541 ? 176.708 134.204 211.267 1.00 38.37  ? 3541 ILE A CG1   1 
ATOM   14988 C  CG2   . ILE A 1 3541 ? 174.757 132.755 210.642 1.00 34.93  ? 3541 ILE A CG2   1 
ATOM   14989 C  CD1   . ILE A 1 3541 ? 176.050 135.470 210.773 1.00 32.99  ? 3541 ILE A CD1   1 
ATOM   14990 N  N     . GLN A 1 3542 ? 175.900 129.559 211.258 1.00 48.88  ? 3542 GLN A N     1 
ATOM   14991 C  CA    . GLN A 1 3542 ? 175.532 128.225 210.807 1.00 48.33  ? 3542 GLN A CA    1 
ATOM   14992 C  C     . GLN A 1 3542 ? 174.291 128.271 209.925 1.00 50.12  ? 3542 GLN A C     1 
ATOM   14993 O  O     . GLN A 1 3542 ? 173.297 128.921 210.265 1.00 47.90  ? 3542 GLN A O     1 
ATOM   14994 C  CB    . GLN A 1 3542 ? 175.290 127.310 212.009 1.00 50.41  ? 3542 GLN A CB    1 
ATOM   14995 C  CG    . GLN A 1 3542 ? 176.541 126.815 212.751 1.00 53.19  ? 3542 GLN A CG    1 
ATOM   14996 C  CD    . GLN A 1 3542 ? 177.777 126.657 211.873 1.00 61.59  ? 3542 GLN A CD    1 
ATOM   14997 O  OE1   . GLN A 1 3542 ? 178.400 127.636 211.456 1.00 55.43  ? 3542 GLN A OE1   1 
ATOM   14998 N  NE2   . GLN A 1 3542 ? 178.135 125.410 211.588 1.00 60.16  ? 3542 GLN A NE2   1 
ATOM   14999 N  N     . PHE A 1 3543 ? 174.355 127.579 208.789 1.00 48.80  ? 3543 PHE A N     1 
ATOM   15000 C  CA    . PHE A 1 3543 ? 173.216 127.428 207.896 1.00 44.43  ? 3543 PHE A CA    1 
ATOM   15001 C  C     . PHE A 1 3543 ? 173.393 126.140 207.107 1.00 50.71  ? 3543 PHE A C     1 
ATOM   15002 O  O     . PHE A 1 3543 ? 174.517 125.777 206.750 1.00 51.79  ? 3543 PHE A O     1 
ATOM   15003 C  CB    . PHE A 1 3543 ? 173.074 128.625 206.946 1.00 39.25  ? 3543 PHE A CB    1 
ATOM   15004 C  CG    . PHE A 1 3543 ? 174.200 128.759 205.960 1.00 37.54  ? 3543 PHE A CG    1 
ATOM   15005 C  CD1   . PHE A 1 3543 ? 175.354 129.445 206.297 1.00 37.68  ? 3543 PHE A CD1   1 
ATOM   15006 C  CD2   . PHE A 1 3543 ? 174.102 128.205 204.694 1.00 43.73  ? 3543 PHE A CD2   1 
ATOM   15007 C  CE1   . PHE A 1 3543 ? 176.388 129.572 205.394 1.00 37.12  ? 3543 PHE A CE1   1 
ATOM   15008 C  CE2   . PHE A 1 3543 ? 175.135 128.328 203.787 1.00 40.37  ? 3543 PHE A CE2   1 
ATOM   15009 C  CZ    . PHE A 1 3543 ? 176.279 129.013 204.137 1.00 37.36  ? 3543 PHE A CZ    1 
ATOM   15010 N  N     . ARG A 1 3544 ? 172.287 125.452 206.842 1.00 53.53  ? 3544 ARG A N     1 
ATOM   15011 C  CA    . ARG A 1 3544 ? 172.352 124.219 206.076 1.00 53.83  ? 3544 ARG A CA    1 
ATOM   15012 C  C     . ARG A 1 3544 ? 172.586 124.512 204.599 1.00 60.80  ? 3544 ARG A C     1 
ATOM   15013 O  O     . ARG A 1 3544 ? 172.123 125.521 204.059 1.00 61.36  ? 3544 ARG A O     1 
ATOM   15014 C  CB    . ARG A 1 3544 ? 171.072 123.398 206.240 1.00 57.10  ? 3544 ARG A CB    1 
ATOM   15015 C  CG    . ARG A 1 3544 ? 170.845 122.857 207.640 1.00 63.15  ? 3544 ARG A CG    1 
ATOM   15016 C  CD    . ARG A 1 3544 ? 169.564 122.043 207.706 1.00 69.52  ? 3544 ARG A CD    1 
ATOM   15017 N  NE    . ARG A 1 3544 ? 168.371 122.857 207.511 1.00 65.67  ? 3544 ARG A NE    1 
ATOM   15018 C  CZ    . ARG A 1 3544 ? 167.146 122.366 207.391 1.00 64.85  ? 3544 ARG A CZ    1 
ATOM   15019 N  NH1   . ARG A 1 3544 ? 166.916 121.064 207.438 1.00 63.44  ? 3544 ARG A NH1   1 
ATOM   15020 N  NH2   . ARG A 1 3544 ? 166.126 123.201 207.218 1.00 64.95  ? 3544 ARG A NH2   1 
ATOM   15021 N  N     . THR A 1 3545 ? 173.316 123.610 203.946 1.00 66.77  ? 3545 THR A N     1 
ATOM   15022 C  CA    . THR A 1 3545 ? 173.604 123.710 202.522 1.00 69.73  ? 3545 THR A CA    1 
ATOM   15023 C  C     . THR A 1 3545 ? 172.899 122.645 201.696 1.00 69.86  ? 3545 THR A C     1 
ATOM   15024 O  O     . THR A 1 3545 ? 172.569 122.896 200.534 1.00 69.43  ? 3545 THR A O     1 
ATOM   15025 C  CB    . THR A 1 3545 ? 175.120 123.619 202.285 1.00 71.38  ? 3545 THR A CB    1 
ATOM   15026 O  OG1   . THR A 1 3545 ? 175.777 124.675 202.996 1.00 66.94  ? 3545 THR A OG1   1 
ATOM   15027 C  CG2   . THR A 1 3545 ? 175.459 123.748 200.806 1.00 67.06  ? 3545 THR A CG2   1 
ATOM   15028 N  N     . ASP A 1 3546 ? 172.630 121.477 202.285 1.00 70.74  ? 3546 ASP A N     1 
ATOM   15029 C  CA    . ASP A 1 3546 ? 172.008 120.385 201.543 1.00 71.81  ? 3546 ASP A CA    1 
ATOM   15030 C  C     . ASP A 1 3546 ? 170.608 120.753 201.066 1.00 74.82  ? 3546 ASP A C     1 
ATOM   15031 O  O     . ASP A 1 3546 ? 170.227 120.435 199.933 1.00 75.73  ? 3546 ASP A O     1 
ATOM   15032 C  CB    . ASP A 1 3546 ? 171.962 119.129 202.413 1.00 70.87  ? 3546 ASP A CB    1 
ATOM   15033 C  CG    . ASP A 1 3546 ? 171.451 119.409 203.815 1.00 72.42  ? 3546 ASP A CG    1 
ATOM   15034 O  OD1   . ASP A 1 3546 ? 171.125 120.579 204.109 1.00 71.11  ? 3546 ASP A OD1   1 
ATOM   15035 O  OD2   . ASP A 1 3546 ? 171.373 118.459 204.622 1.00 70.22  ? 3546 ASP A OD2   1 
ATOM   15036 N  N     . ILE A 1 3547 ? 169.828 121.418 201.912 1.00 74.27  ? 3547 ILE A N     1 
ATOM   15037 C  CA    . ILE A 1 3547 ? 168.431 121.701 201.602 1.00 72.51  ? 3547 ILE A CA    1 
ATOM   15038 C  C     . ILE A 1 3547 ? 168.351 122.833 200.586 1.00 65.97  ? 3547 ILE A C     1 
ATOM   15039 O  O     . ILE A 1 3547 ? 169.057 123.842 200.698 1.00 59.46  ? 3547 ILE A O     1 
ATOM   15040 C  CB    . ILE A 1 3547 ? 167.647 122.038 202.882 1.00 68.95  ? 3547 ILE A CB    1 
ATOM   15041 C  CG1   . ILE A 1 3547 ? 166.194 122.385 202.548 1.00 61.54  ? 3547 ILE A CG1   1 
ATOM   15042 C  CG2   . ILE A 1 3547 ? 168.323 123.166 203.655 1.00 65.40  ? 3547 ILE A CG2   1 
ATOM   15043 C  CD1   . ILE A 1 3547 ? 165.266 122.342 203.741 1.00 59.00  ? 3547 ILE A CD1   1 
ATOM   15044 N  N     . ALA A 1 3548 ? 167.502 122.656 199.577 1.00 61.10  ? 3548 ALA A N     1 
ATOM   15045 C  CA    . ALA A 1 3548 ? 167.249 123.702 198.599 1.00 58.10  ? 3548 ALA A CA    1 
ATOM   15046 C  C     . ALA A 1 3548 ? 166.222 124.692 199.136 1.00 53.43  ? 3548 ALA A C     1 
ATOM   15047 O  O     . ALA A 1 3548 ? 165.351 124.343 199.937 1.00 52.76  ? 3548 ALA A O     1 
ATOM   15048 C  CB    . ALA A 1 3548 ? 166.758 123.100 197.282 1.00 56.12  ? 3548 ALA A CB    1 
ATOM   15049 N  N     . ARG A 1 3549 ? 166.336 125.944 198.683 1.00 43.33  ? 3549 ARG A N     1 
ATOM   15050 C  CA    . ARG A 1 3549 ? 165.445 126.990 199.176 1.00 39.96  ? 3549 ARG A CA    1 
ATOM   15051 C  C     . ARG A 1 3549 ? 163.996 126.740 198.780 1.00 41.94  ? 3549 ARG A C     1 
ATOM   15052 O  O     . ARG A 1 3549 ? 163.080 127.230 199.451 1.00 45.13  ? 3549 ARG A O     1 
ATOM   15053 C  CB    . ARG A 1 3549 ? 165.901 128.356 198.666 1.00 33.22  ? 3549 ARG A CB    1 
ATOM   15054 C  CG    . ARG A 1 3549 ? 166.304 128.376 197.204 1.00 31.33  ? 3549 ARG A CG    1 
ATOM   15055 C  CD    . ARG A 1 3549 ? 166.966 129.693 196.843 1.00 25.98  ? 3549 ARG A CD    1 
ATOM   15056 N  NE    . ARG A 1 3549 ? 167.409 129.720 195.455 1.00 28.23  ? 3549 ARG A NE    1 
ATOM   15057 C  CZ    . ARG A 1 3549 ? 168.649 129.463 195.061 1.00 35.66  ? 3549 ARG A CZ    1 
ATOM   15058 N  NH1   . ARG A 1 3549 ? 169.597 129.147 195.927 1.00 34.09  ? 3549 ARG A NH1   1 
ATOM   15059 N  NH2   . ARG A 1 3549 ? 168.944 129.525 193.766 1.00 34.62  ? 3549 ARG A NH2   1 
ATOM   15060 N  N     . THR A 1 3550 ? 163.766 125.996 197.695 1.00 41.65  ? 3550 THR A N     1 
ATOM   15061 C  CA    . THR A 1 3550 ? 162.399 125.695 197.282 1.00 39.16  ? 3550 THR A CA    1 
ATOM   15062 C  C     . THR A 1 3550 ? 161.671 124.865 198.334 1.00 41.83  ? 3550 THR A C     1 
ATOM   15063 O  O     . THR A 1 3550 ? 160.526 125.167 198.691 1.00 40.17  ? 3550 THR A O     1 
ATOM   15064 C  CB    . THR A 1 3550 ? 162.411 124.969 195.934 1.00 37.14  ? 3550 THR A CB    1 
ATOM   15065 O  OG1   . THR A 1 3550 ? 162.529 125.927 194.875 1.00 33.85  ? 3550 THR A OG1   1 
ATOM   15066 C  CG2   . THR A 1 3550 ? 161.140 124.155 195.741 1.00 35.33  ? 3550 THR A CG2   1 
ATOM   15067 N  N     . GLU A 1 3551 ? 162.324 123.825 198.853 1.00 44.99  ? 3551 GLU A N     1 
ATOM   15068 C  CA    . GLU A 1 3551 ? 161.697 122.965 199.848 1.00 44.78  ? 3551 GLU A CA    1 
ATOM   15069 C  C     . GLU A 1 3551 ? 161.714 123.570 201.245 1.00 47.85  ? 3551 GLU A C     1 
ATOM   15070 O  O     . GLU A 1 3551 ? 160.919 123.154 202.094 1.00 49.68  ? 3551 GLU A O     1 
ATOM   15071 C  CB    . GLU A 1 3551 ? 162.386 121.599 199.863 1.00 49.53  ? 3551 GLU A CB    1 
ATOM   15072 C  CG    . GLU A 1 3551 ? 162.223 120.818 198.568 1.00 58.03  ? 3551 GLU A CG    1 
ATOM   15073 C  CD    . GLU A 1 3551 ? 162.478 119.334 198.742 1.00 74.11  ? 3551 GLU A CD    1 
ATOM   15074 O  OE1   . GLU A 1 3551 ? 161.502 118.555 198.722 1.00 73.58  ? 3551 GLU A OE1   1 
ATOM   15075 O  OE2   . GLU A 1 3551 ? 163.655 118.947 198.896 1.00 79.01  ? 3551 GLU A OE2   1 
ATOM   15076 N  N     . TYR A 1 3552 ? 162.603 124.531 201.504 1.00 46.11  ? 3552 TYR A N     1 
ATOM   15077 C  CA    . TYR A 1 3552 ? 162.629 125.182 202.809 1.00 39.05  ? 3552 TYR A CA    1 
ATOM   15078 C  C     . TYR A 1 3552 ? 161.476 126.166 202.965 1.00 41.92  ? 3552 TYR A C     1 
ATOM   15079 O  O     . TYR A 1 3552 ? 160.848 126.231 204.028 1.00 46.05  ? 3552 TYR A O     1 
ATOM   15080 C  CB    . TYR A 1 3552 ? 163.968 125.890 203.012 1.00 42.01  ? 3552 TYR A CB    1 
ATOM   15081 C  CG    . TYR A 1 3552 ? 164.208 126.362 204.427 1.00 41.69  ? 3552 TYR A CG    1 
ATOM   15082 C  CD1   . TYR A 1 3552 ? 164.279 125.461 205.479 1.00 43.39  ? 3552 TYR A CD1   1 
ATOM   15083 C  CD2   . TYR A 1 3552 ? 164.367 127.711 204.710 1.00 40.65  ? 3552 TYR A CD2   1 
ATOM   15084 C  CE1   . TYR A 1 3552 ? 164.500 125.891 206.773 1.00 47.09  ? 3552 TYR A CE1   1 
ATOM   15085 C  CE2   . TYR A 1 3552 ? 164.590 128.150 206.000 1.00 41.50  ? 3552 TYR A CE2   1 
ATOM   15086 C  CZ    . TYR A 1 3552 ? 164.655 127.236 207.027 1.00 46.89  ? 3552 TYR A CZ    1 
ATOM   15087 O  OH    . TYR A 1 3552 ? 164.876 127.669 208.314 1.00 47.67  ? 3552 TYR A OH    1 
ATOM   15088 N  N     . LEU A 1 3553 ? 161.180 126.933 201.919 1.00 39.69  ? 3553 LEU A N     1 
ATOM   15089 C  CA    . LEU A 1 3553 ? 160.176 127.987 201.981 1.00 33.34  ? 3553 LEU A CA    1 
ATOM   15090 C  C     . LEU A 1 3553 ? 158.790 127.527 201.551 1.00 36.11  ? 3553 LEU A C     1 
ATOM   15091 O  O     . LEU A 1 3553 ? 157.873 128.352 201.493 1.00 37.47  ? 3553 LEU A O     1 
ATOM   15092 C  CB    . LEU A 1 3553 ? 160.610 129.174 201.118 1.00 29.97  ? 3553 LEU A CB    1 
ATOM   15093 C  CG    . LEU A 1 3553 ? 161.731 130.038 201.694 1.00 30.91  ? 3553 LEU A CG    1 
ATOM   15094 C  CD1   . LEU A 1 3553 ? 162.287 130.977 200.637 1.00 25.57  ? 3553 LEU A CD1   1 
ATOM   15095 C  CD2   . LEU A 1 3553 ? 161.219 130.817 202.890 1.00 24.59  ? 3553 LEU A CD2   1 
ATOM   15096 N  N     . SER A 1 3554 ? 158.614 126.244 201.247 1.00 35.84  ? 3554 SER A N     1 
ATOM   15097 C  CA    . SER A 1 3554 ? 157.312 125.733 200.846 1.00 36.86  ? 3554 SER A CA    1 
ATOM   15098 C  C     . SER A 1 3554 ? 157.221 124.262 201.217 1.00 43.04  ? 3554 SER A C     1 
ATOM   15099 O  O     . SER A 1 3554 ? 158.234 123.577 201.381 1.00 48.48  ? 3554 SER A O     1 
ATOM   15100 C  CB    . SER A 1 3554 ? 157.069 125.925 199.345 1.00 36.98  ? 3554 SER A CB    1 
ATOM   15101 O  OG    . SER A 1 3554 ? 155.725 125.633 199.005 1.00 42.87  ? 3554 SER A OG    1 
ATOM   15102 N  N     . ASN A 1 3555 ? 155.990 123.781 201.346 1.00 39.20  ? 3555 ASN A N     1 
ATOM   15103 C  CA    . ASN A 1 3555 ? 155.730 122.387 201.663 1.00 39.80  ? 3555 ASN A CA    1 
ATOM   15104 C  C     . ASN A 1 3555 ? 155.214 121.655 200.429 1.00 43.18  ? 3555 ASN A C     1 
ATOM   15105 O  O     . ASN A 1 3555 ? 154.776 122.262 199.449 1.00 41.98  ? 3555 ASN A O     1 
ATOM   15106 C  CB    . ASN A 1 3555 ? 154.735 122.271 202.822 1.00 37.83  ? 3555 ASN A CB    1 
ATOM   15107 C  CG    . ASN A 1 3555 ? 153.493 123.112 202.612 1.00 45.07  ? 3555 ASN A CG    1 
ATOM   15108 O  OD1   . ASN A 1 3555 ? 152.677 122.825 201.737 1.00 46.02  ? 3555 ASN A OD1   1 
ATOM   15109 N  ND2   . ASN A 1 3555 ? 153.341 124.156 203.418 1.00 46.39  ? 3555 ASN A ND2   1 
ATOM   15110 N  N     . ALA A 1 3556 ? 155.280 120.322 200.488 1.00 46.23  ? 3556 ALA A N     1 
ATOM   15111 C  CA    . ALA A 1 3556 ? 154.884 119.508 199.343 1.00 45.17  ? 3556 ALA A CA    1 
ATOM   15112 C  C     . ALA A 1 3556 ? 153.405 119.682 199.022 1.00 48.58  ? 3556 ALA A C     1 
ATOM   15113 O  O     . ALA A 1 3556 ? 153.008 119.633 197.851 1.00 47.41  ? 3556 ALA A O     1 
ATOM   15114 C  CB    . ALA A 1 3556 ? 155.210 118.039 199.607 1.00 43.92  ? 3556 ALA A CB    1 
ATOM   15115 N  N     . ASP A 1 3557 ? 152.572 119.876 200.047 1.00 44.20  ? 3557 ASP A N     1 
ATOM   15116 C  CA    . ASP A 1 3557 ? 151.147 120.086 199.811 1.00 43.65  ? 3557 ASP A CA    1 
ATOM   15117 C  C     . ASP A 1 3557 ? 150.899 121.362 199.018 1.00 44.31  ? 3557 ASP A C     1 
ATOM   15118 O  O     . ASP A 1 3557 ? 150.057 121.386 198.113 1.00 44.19  ? 3557 ASP A O     1 
ATOM   15119 C  CB    . ASP A 1 3557 ? 150.394 120.124 201.141 1.00 51.04  ? 3557 ASP A CB    1 
ATOM   15120 C  CG    . ASP A 1 3557 ? 149.768 118.790 201.493 1.00 62.52  ? 3557 ASP A CG    1 
ATOM   15121 O  OD1   . ASP A 1 3557 ? 149.269 118.106 200.575 1.00 64.21  ? 3557 ASP A OD1   1 
ATOM   15122 O  OD2   . ASP A 1 3557 ? 149.775 118.425 202.688 1.00 57.87  ? 3557 ASP A OD2   1 
ATOM   15123 N  N     . GLU A 1 3558 ? 151.619 122.438 199.346 1.00 46.48  ? 3558 GLU A N     1 
ATOM   15124 C  CA    . GLU A 1 3558 ? 151.461 123.685 198.604 1.00 42.85  ? 3558 GLU A CA    1 
ATOM   15125 C  C     . GLU A 1 3558 ? 151.991 123.555 197.182 1.00 40.83  ? 3558 GLU A C     1 
ATOM   15126 O  O     . GLU A 1 3558 ? 151.390 124.083 196.239 1.00 41.20  ? 3558 GLU A O     1 
ATOM   15127 C  CB    . GLU A 1 3558 ? 152.166 124.825 199.336 1.00 41.49  ? 3558 GLU A CB    1 
ATOM   15128 C  CG    . GLU A 1 3558 ? 151.567 126.191 199.066 1.00 46.84  ? 3558 GLU A CG    1 
ATOM   15129 C  CD    . GLU A 1 3558 ? 152.030 127.234 200.060 1.00 51.45  ? 3558 GLU A CD    1 
ATOM   15130 O  OE1   . GLU A 1 3558 ? 153.013 126.974 200.785 1.00 42.85  ? 3558 GLU A OE1   1 
ATOM   15131 O  OE2   . GLU A 1 3558 ? 151.406 128.314 200.117 1.00 52.77  ? 3558 GLU A OE2   1 
ATOM   15132 N  N     . ARG A 1 3559 ? 153.120 122.862 197.010 1.00 41.30  ? 3559 ARG A N     1 
ATOM   15133 C  CA    . ARG A 1 3559 ? 153.685 122.686 195.676 1.00 41.40  ? 3559 ARG A CA    1 
ATOM   15134 C  C     . ARG A 1 3559 ? 152.762 121.860 194.789 1.00 42.62  ? 3559 ARG A C     1 
ATOM   15135 O  O     . ARG A 1 3559 ? 152.624 122.141 193.593 1.00 43.25  ? 3559 ARG A O     1 
ATOM   15136 C  CB    . ARG A 1 3559 ? 155.066 122.039 195.775 1.00 36.46  ? 3559 ARG A CB    1 
ATOM   15137 C  CG    . ARG A 1 3559 ? 156.132 122.964 196.337 1.00 37.83  ? 3559 ARG A CG    1 
ATOM   15138 C  CD    . ARG A 1 3559 ? 157.519 122.357 196.224 1.00 40.03  ? 3559 ARG A CD    1 
ATOM   15139 N  NE    . ARG A 1 3559 ? 157.644 121.133 197.003 1.00 49.41  ? 3559 ARG A NE    1 
ATOM   15140 C  CZ    . ARG A 1 3559 ? 158.154 121.074 198.225 1.00 47.77  ? 3559 ARG A CZ    1 
ATOM   15141 N  NH1   . ARG A 1 3559 ? 158.580 122.160 198.849 1.00 46.22  ? 3559 ARG A NH1   1 
ATOM   15142 N  NH2   . ARG A 1 3559 ? 158.236 119.896 198.839 1.00 45.39  ? 3559 ARG A NH2   1 
ATOM   15143 N  N     . LEU A 1 3560 ? 152.131 120.829 195.355 1.00 43.10  ? 3560 LEU A N     1 
ATOM   15144 C  CA    . LEU A 1 3560 ? 151.166 120.045 194.591 1.00 42.42  ? 3560 LEU A CA    1 
ATOM   15145 C  C     . LEU A 1 3560 ? 149.975 120.898 194.174 1.00 40.70  ? 3560 LEU A C     1 
ATOM   15146 O  O     . LEU A 1 3560 ? 149.499 120.799 193.037 1.00 39.18  ? 3560 LEU A O     1 
ATOM   15147 C  CB    . LEU A 1 3560 ? 150.710 118.836 195.409 1.00 44.72  ? 3560 LEU A CB    1 
ATOM   15148 C  CG    . LEU A 1 3560 ? 150.434 117.531 194.655 1.00 43.87  ? 3560 LEU A CG    1 
ATOM   15149 C  CD1   . LEU A 1 3560 ? 150.384 116.361 195.623 1.00 46.50  ? 3560 LEU A CD1   1 
ATOM   15150 C  CD2   . LEU A 1 3560 ? 149.143 117.613 193.855 1.00 43.57  ? 3560 LEU A CD2   1 
ATOM   15151 N  N     . ARG A 1 3561 ? 149.478 121.741 195.083 1.00 40.14  ? 3561 ARG A N     1 
ATOM   15152 C  CA    . ARG A 1 3561 ? 148.375 122.634 194.740 1.00 41.22  ? 3561 ARG A CA    1 
ATOM   15153 C  C     . ARG A 1 3561 ? 148.787 123.629 193.663 1.00 40.66  ? 3561 ARG A C     1 
ATOM   15154 O  O     . ARG A 1 3561 ? 147.987 123.970 192.783 1.00 38.58  ? 3561 ARG A O     1 
ATOM   15155 C  CB    . ARG A 1 3561 ? 147.883 123.367 195.987 1.00 44.07  ? 3561 ARG A CB    1 
ATOM   15156 C  CG    . ARG A 1 3561 ? 146.492 123.959 195.845 1.00 44.98  ? 3561 ARG A CG    1 
ATOM   15157 C  CD    . ARG A 1 3561 ? 146.433 125.370 196.405 1.00 46.46  ? 3561 ARG A CD    1 
ATOM   15158 N  NE    . ARG A 1 3561 ? 146.557 125.384 197.858 1.00 55.23  ? 3561 ARG A NE    1 
ATOM   15159 C  CZ    . ARG A 1 3561 ? 145.536 125.509 198.694 1.00 57.71  ? 3561 ARG A CZ    1 
ATOM   15160 N  NH1   . ARG A 1 3561 ? 144.294 125.635 198.256 1.00 57.86  ? 3561 ARG A NH1   1 
ATOM   15161 N  NH2   . ARG A 1 3561 ? 145.766 125.506 200.004 1.00 53.05  ? 3561 ARG A NH2   1 
ATOM   15162 N  N     . TRP A 1 3562 ? 150.028 124.117 193.724 1.00 41.91  ? 3562 TRP A N     1 
ATOM   15163 C  CA    . TRP A 1 3562 ? 150.521 125.017 192.687 1.00 38.63  ? 3562 TRP A CA    1 
ATOM   15164 C  C     . TRP A 1 3562 ? 150.559 124.323 191.330 1.00 39.91  ? 3562 TRP A C     1 
ATOM   15165 O  O     . TRP A 1 3562 ? 150.211 124.925 190.308 1.00 41.31  ? 3562 TRP A O     1 
ATOM   15166 C  CB    . TRP A 1 3562 ? 151.904 125.545 193.064 1.00 37.62  ? 3562 TRP A CB    1 
ATOM   15167 C  CG    . TRP A 1 3562 ? 151.880 126.551 194.174 1.00 34.60  ? 3562 TRP A CG    1 
ATOM   15168 C  CD1   . TRP A 1 3562 ? 150.830 127.338 194.543 1.00 32.29  ? 3562 TRP A CD1   1 
ATOM   15169 C  CD2   . TRP A 1 3562 ? 152.959 126.882 195.057 1.00 35.06  ? 3562 TRP A CD2   1 
ATOM   15170 N  NE1   . TRP A 1 3562 ? 151.186 128.137 195.602 1.00 34.79  ? 3562 TRP A NE1   1 
ATOM   15171 C  CE2   . TRP A 1 3562 ? 152.488 127.876 195.937 1.00 31.49  ? 3562 TRP A CE2   1 
ATOM   15172 C  CE3   . TRP A 1 3562 ? 154.276 126.432 195.189 1.00 30.25  ? 3562 TRP A CE3   1 
ATOM   15173 C  CZ2   . TRP A 1 3562 ? 153.288 128.430 196.934 1.00 25.46  ? 3562 TRP A CZ2   1 
ATOM   15174 C  CZ3   . TRP A 1 3562 ? 155.067 126.982 196.180 1.00 29.02  ? 3562 TRP A CZ3   1 
ATOM   15175 C  CH2   . TRP A 1 3562 ? 154.571 127.970 197.040 1.00 27.29  ? 3562 TRP A CH2   1 
ATOM   15176 N  N     . GLN A 1 3563 ? 150.978 123.055 191.302 1.00 37.71  ? 3563 GLN A N     1 
ATOM   15177 C  CA    . GLN A 1 3563 ? 150.954 122.297 190.054 1.00 38.24  ? 3563 GLN A CA    1 
ATOM   15178 C  C     . GLN A 1 3563 ? 149.533 122.159 189.523 1.00 41.48  ? 3563 GLN A C     1 
ATOM   15179 O  O     . GLN A 1 3563 ? 149.302 122.259 188.312 1.00 42.37  ? 3563 GLN A O     1 
ATOM   15180 C  CB    . GLN A 1 3563 ? 151.587 120.921 190.262 1.00 37.44  ? 3563 GLN A CB    1 
ATOM   15181 C  CG    . GLN A 1 3563 ? 152.919 120.727 189.551 1.00 38.43  ? 3563 GLN A CG    1 
ATOM   15182 C  CD    . GLN A 1 3563 ? 153.930 121.805 189.889 1.00 46.00  ? 3563 GLN A CD    1 
ATOM   15183 O  OE1   . GLN A 1 3563 ? 154.582 121.756 190.932 1.00 47.74  ? 3563 GLN A OE1   1 
ATOM   15184 N  NE2   . GLN A 1 3563 ? 154.073 122.782 189.000 1.00 41.45  ? 3563 GLN A NE2   1 
ATOM   15185 N  N     . ALA A 1 3564 ? 148.566 121.927 190.414 1.00 43.26  ? 3564 ALA A N     1 
ATOM   15186 C  CA    . ALA A 1 3564 ? 147.173 121.819 189.998 1.00 42.26  ? 3564 ALA A CA    1 
ATOM   15187 C  C     . ALA A 1 3564 ? 146.621 123.133 189.463 1.00 42.58  ? 3564 ALA A C     1 
ATOM   15188 O  O     . ALA A 1 3564 ? 145.624 123.120 188.733 1.00 45.36  ? 3564 ALA A O     1 
ATOM   15189 C  CB    . ALA A 1 3564 ? 146.312 121.329 191.164 1.00 41.06  ? 3564 ALA A CB    1 
ATOM   15190 N  N     . SER A 1 3565 ? 147.241 124.263 189.806 1.00 40.59  ? 3565 SER A N     1 
ATOM   15191 C  CA    . SER A 1 3565 ? 146.827 125.573 189.317 1.00 40.26  ? 3565 SER A CA    1 
ATOM   15192 C  C     . SER A 1 3565 ? 147.604 125.996 188.075 1.00 43.49  ? 3565 SER A C     1 
ATOM   15193 O  O     . SER A 1 3565 ? 147.757 127.195 187.818 1.00 46.39  ? 3565 SER A O     1 
ATOM   15194 C  CB    . SER A 1 3565 ? 146.972 126.621 190.419 1.00 42.73  ? 3565 SER A CB    1 
ATOM   15195 O  OG    . SER A 1 3565 ? 146.078 126.363 191.487 1.00 45.61  ? 3565 SER A OG    1 
ATOM   15196 N  N     . SER A 1 3566 ? 148.104 125.025 187.306 1.00 42.15  ? 3566 SER A N     1 
ATOM   15197 C  CA    . SER A 1 3566 ? 148.814 125.278 186.050 1.00 40.38  ? 3566 SER A CA    1 
ATOM   15198 C  C     . SER A 1 3566 ? 150.066 126.126 186.265 1.00 39.39  ? 3566 SER A C     1 
ATOM   15199 O  O     . SER A 1 3566 ? 150.365 127.033 185.486 1.00 44.66  ? 3566 SER A O     1 
ATOM   15200 C  CB    . SER A 1 3566 ? 147.893 125.925 185.013 1.00 49.01  ? 3566 SER A CB    1 
ATOM   15201 O  OG    . SER A 1 3566 ? 147.707 127.303 185.284 1.00 51.27  ? 3566 SER A OG    1 
ATOM   15202 N  N     . LEU A 1 3567 ? 150.806 125.831 187.333 1.00 37.95  ? 3567 LEU A N     1 
ATOM   15203 C  CA    . LEU A 1 3567 ? 152.112 126.461 187.502 1.00 35.52  ? 3567 LEU A CA    1 
ATOM   15204 C  C     . LEU A 1 3567 ? 153.192 125.562 186.916 1.00 37.37  ? 3567 LEU A C     1 
ATOM   15205 O  O     . LEU A 1 3567 ? 153.287 124.391 187.301 1.00 36.40  ? 3567 LEU A O     1 
ATOM   15206 C  CB    . LEU A 1 3567 ? 152.410 126.729 188.970 1.00 36.06  ? 3567 LEU A CB    1 
ATOM   15207 C  CG    . LEU A 1 3567 ? 153.803 127.293 189.263 1.00 32.04  ? 3567 LEU A CG    1 
ATOM   15208 C  CD1   . LEU A 1 3567 ? 153.826 128.800 189.062 1.00 30.44  ? 3567 LEU A CD1   1 
ATOM   15209 C  CD2   . LEU A 1 3567 ? 154.258 126.928 190.666 1.00 29.60  ? 3567 LEU A CD2   1 
ATOM   15210 N  N     . PRO A 1 3568 ? 154.007 126.063 185.988 1.00 37.58  ? 3568 PRO A N     1 
ATOM   15211 C  CA    . PRO A 1 3568 ? 155.033 125.212 185.372 1.00 33.76  ? 3568 PRO A CA    1 
ATOM   15212 C  C     . PRO A 1 3568 ? 156.011 124.676 186.406 1.00 35.02  ? 3568 PRO A C     1 
ATOM   15213 O  O     . PRO A 1 3568 ? 156.355 125.353 187.377 1.00 38.31  ? 3568 PRO A O     1 
ATOM   15214 C  CB    . PRO A 1 3568 ? 155.722 126.149 184.373 1.00 34.44  ? 3568 PRO A CB    1 
ATOM   15215 C  CG    . PRO A 1 3568 ? 155.361 127.531 184.811 1.00 36.84  ? 3568 PRO A CG    1 
ATOM   15216 C  CD    . PRO A 1 3568 ? 154.014 127.431 185.446 1.00 36.46  ? 3568 PRO A CD    1 
ATOM   15217 N  N     . ALA A 1 3569 ? 156.456 123.440 186.187 1.00 35.91  ? 3569 ALA A N     1 
ATOM   15218 C  CA    . ALA A 1 3569 ? 157.356 122.753 187.112 1.00 32.77  ? 3569 ALA A CA    1 
ATOM   15219 C  C     . ALA A 1 3569 ? 158.777 123.236 186.857 1.00 33.27  ? 3569 ALA A C     1 
ATOM   15220 O  O     . ALA A 1 3569 ? 159.524 122.662 186.063 1.00 38.71  ? 3569 ALA A O     1 
ATOM   15221 C  CB    . ALA A 1 3569 ? 157.243 121.243 186.954 1.00 32.31  ? 3569 ALA A CB    1 
ATOM   15222 N  N     . ASP A 1 3570 ? 159.155 124.311 187.544 1.00 33.77  ? 3570 ASP A N     1 
ATOM   15223 C  CA    . ASP A 1 3570 ? 160.491 124.871 187.427 1.00 31.39  ? 3570 ASP A CA    1 
ATOM   15224 C  C     . ASP A 1 3570 ? 160.914 125.412 188.785 1.00 26.21  ? 3570 ASP A C     1 
ATOM   15225 O  O     . ASP A 1 3570 ? 160.093 125.940 189.539 1.00 27.32  ? 3570 ASP A O     1 
ATOM   15226 C  CB    . ASP A 1 3570 ? 160.548 125.977 186.366 1.00 26.24  ? 3570 ASP A CB    1 
ATOM   15227 C  CG    . ASP A 1 3570 ? 161.932 126.580 186.225 1.00 31.76  ? 3570 ASP A CG    1 
ATOM   15228 O  OD1   . ASP A 1 3570 ? 162.924 125.836 186.368 1.00 34.90  ? 3570 ASP A OD1   1 
ATOM   15229 O  OD2   . ASP A 1 3570 ? 162.026 127.798 185.969 1.00 27.05  ? 3570 ASP A OD2   1 
ATOM   15230 N  N     . ASP A 1 3571 ? 162.205 125.265 189.091 1.00 25.73  ? 3571 ASP A N     1 
ATOM   15231 C  CA    . ASP A 1 3571 ? 162.719 125.760 190.364 1.00 26.66  ? 3571 ASP A CA    1 
ATOM   15232 C  C     . ASP A 1 3571 ? 162.568 127.272 190.469 1.00 25.68  ? 3571 ASP A C     1 
ATOM   15233 O  O     . ASP A 1 3571 ? 162.186 127.793 191.523 1.00 29.44  ? 3571 ASP A O     1 
ATOM   15234 C  CB    . ASP A 1 3571 ? 164.181 125.350 190.536 1.00 24.96  ? 3571 ASP A CB    1 
ATOM   15235 C  CG    . ASP A 1 3571 ? 164.332 124.035 191.272 1.00 33.96  ? 3571 ASP A CG    1 
ATOM   15236 O  OD1   . ASP A 1 3571 ? 163.317 123.522 191.788 1.00 34.25  ? 3571 ASP A OD1   1 
ATOM   15237 O  OD2   . ASP A 1 3571 ? 165.465 123.515 191.337 1.00 37.84  ? 3571 ASP A OD2   1 
ATOM   15238 N  N     . LEU A 1 3572 ? 162.866 127.994 189.386 1.00 22.62  ? 3572 LEU A N     1 
ATOM   15239 C  CA    . LEU A 1 3572 ? 162.649 129.437 189.380 1.00 21.15  ? 3572 LEU A CA    1 
ATOM   15240 C  C     . LEU A 1 3572 ? 161.171 129.771 189.527 1.00 21.65  ? 3572 LEU A C     1 
ATOM   15241 O  O     . LEU A 1 3572 ? 160.806 130.702 190.255 1.00 22.49  ? 3572 LEU A O     1 
ATOM   15242 C  CB    . LEU A 1 3572 ? 163.213 130.048 188.097 1.00 18.38  ? 3572 LEU A CB    1 
ATOM   15243 C  CG    . LEU A 1 3572 ? 163.268 131.576 188.033 1.00 15.81  ? 3572 LEU A CG    1 
ATOM   15244 C  CD1   . LEU A 1 3572 ? 164.597 132.037 187.470 1.00 14.18  ? 3572 LEU A CD1   1 
ATOM   15245 C  CD2   . LEU A 1 3572 ? 162.120 132.126 187.203 1.00 18.62  ? 3572 LEU A CD2   1 
ATOM   15246 N  N     . CYS A 1 3573 ? 160.306 129.023 188.840 1.00 22.35  ? 3573 CYS A N     1 
ATOM   15247 C  CA    . CYS A 1 3573 ? 158.872 129.280 188.924 1.00 20.99  ? 3573 CYS A CA    1 
ATOM   15248 C  C     . CYS A 1 3573 ? 158.335 128.978 190.318 1.00 20.58  ? 3573 CYS A C     1 
ATOM   15249 O  O     . CYS A 1 3573 ? 157.473 129.704 190.827 1.00 21.15  ? 3573 CYS A O     1 
ATOM   15250 C  CB    . CYS A 1 3573 ? 158.132 128.461 187.870 1.00 22.58  ? 3573 CYS A CB    1 
ATOM   15251 S  SG    . CYS A 1 3573 ? 158.098 129.233 186.237 1.00 52.97  ? 3573 CYS A SG    1 
ATOM   15252 N  N     . THR A 1 3574 ? 158.825 127.906 190.947 1.00 22.86  ? 3574 THR A N     1 
ATOM   15253 C  CA    . THR A 1 3574 ? 158.394 127.591 192.305 1.00 19.16  ? 3574 THR A CA    1 
ATOM   15254 C  C     . THR A 1 3574 ? 158.826 128.677 193.282 1.00 20.79  ? 3574 THR A C     1 
ATOM   15255 O  O     . THR A 1 3574 ? 158.078 129.029 194.202 1.00 23.63  ? 3574 THR A O     1 
ATOM   15256 C  CB    . THR A 1 3574 ? 158.945 126.230 192.733 1.00 19.32  ? 3574 THR A CB    1 
ATOM   15257 O  OG1   . THR A 1 3574 ? 158.519 125.228 191.802 1.00 27.09  ? 3574 THR A OG1   1 
ATOM   15258 C  CG2   . THR A 1 3574 ? 158.433 125.864 194.117 1.00 21.01  ? 3574 THR A CG2   1 
ATOM   15259 N  N     . GLU A 1 3575 ? 160.033 129.220 193.099 1.00 18.84  ? 3575 GLU A N     1 
ATOM   15260 C  CA    . GLU A 1 3575 ? 160.465 130.351 193.914 1.00 17.88  ? 3575 GLU A CA    1 
ATOM   15261 C  C     . GLU A 1 3575 ? 159.548 131.548 193.709 1.00 16.96  ? 3575 GLU A C     1 
ATOM   15262 O  O     . GLU A 1 3575 ? 159.238 132.275 194.660 1.00 17.08  ? 3575 GLU A O     1 
ATOM   15263 C  CB    . GLU A 1 3575 ? 161.908 130.724 193.577 1.00 21.87  ? 3575 GLU A CB    1 
ATOM   15264 C  CG    . GLU A 1 3575 ? 162.940 129.684 193.975 1.00 25.89  ? 3575 GLU A CG    1 
ATOM   15265 C  CD    . GLU A 1 3575 ? 164.253 129.860 193.236 1.00 30.28  ? 3575 GLU A CD    1 
ATOM   15266 O  OE1   . GLU A 1 3575 ? 164.240 130.437 192.128 1.00 24.05  ? 3575 GLU A OE1   1 
ATOM   15267 O  OE2   . GLU A 1 3575 ? 165.297 129.421 193.762 1.00 35.94  ? 3575 GLU A OE2   1 
ATOM   15268 N  N     . ASN A 1 3576 ? 159.111 131.771 192.468 1.00 17.25  ? 3576 ASN A N     1 
ATOM   15269 C  CA    . ASN A 1 3576 ? 158.178 132.855 192.186 1.00 14.23  ? 3576 ASN A CA    1 
ATOM   15270 C  C     . ASN A 1 3576 ? 156.850 132.639 192.901 1.00 16.16  ? 3576 ASN A C     1 
ATOM   15271 O  O     . ASN A 1 3576 ? 156.261 133.588 193.432 1.00 15.37  ? 3576 ASN A O     1 
ATOM   15272 C  CB    . ASN A 1 3576 ? 157.967 132.976 190.679 1.00 13.65  ? 3576 ASN A CB    1 
ATOM   15273 C  CG    . ASN A 1 3576 ? 159.153 133.597 189.973 1.00 16.01  ? 3576 ASN A CG    1 
ATOM   15274 O  OD1   . ASN A 1 3576 ? 160.068 134.116 190.612 1.00 21.88  ? 3576 ASN A OD1   1 
ATOM   15275 N  ND2   . ASN A 1 3576 ? 159.146 133.547 188.646 1.00 16.25  ? 3576 ASN A ND2   1 
ATOM   15276 N  N     . ALA A 1 3577 ? 156.362 131.397 192.920 1.00 18.34  ? 3577 ALA A N     1 
ATOM   15277 C  CA    . ALA A 1 3577 ? 155.140 131.092 193.657 1.00 15.98  ? 3577 ALA A CA    1 
ATOM   15278 C  C     . ALA A 1 3577 ? 155.333 131.298 195.153 1.00 17.40  ? 3577 ALA A C     1 
ATOM   15279 O  O     . ALA A 1 3577 ? 154.406 131.724 195.852 1.00 23.34  ? 3577 ALA A O     1 
ATOM   15280 C  CB    . ALA A 1 3577 ? 154.691 129.661 193.363 1.00 20.65  ? 3577 ALA A CB    1 
ATOM   15281 N  N     . ILE A 1 3578 ? 156.535 130.992 195.648 1.00 17.69  ? 3578 ILE A N     1 
ATOM   15282 C  CA    . ILE A 1 3578 ? 156.835 131.200 197.098 1.00 14.26  ? 3578 ILE A CA    1 
ATOM   15283 C  C     . ILE A 1 3578 ? 156.787 132.708 197.386 1.00 16.06  ? 3578 ILE A C     1 
ATOM   15284 O  O     . ILE A 1 3578 ? 156.236 133.091 198.439 1.00 23.62  ? 3578 ILE A O     1 
ATOM   15285 C  CB    . ILE A 1 3578 ? 158.194 130.586 197.478 1.00 15.13  ? 3578 ILE A CB    1 
ATOM   15286 C  CG1   . ILE A 1 3578 ? 158.203 129.072 197.274 1.00 21.52  ? 3578 ILE A CG1   1 
ATOM   15287 C  CG2   . ILE A 1 3578 ? 158.581 130.963 198.907 1.00 19.68  ? 3578 ILE A CG2   1 
ATOM   15288 C  CD1   . ILE A 1 3578 ? 159.540 128.416 197.567 1.00 22.78  ? 3578 ILE A CD1   1 
ATOM   15289 N  N     . MET A 1 3579 ? 157.339 133.521 196.482 1.00 15.72  ? 3579 MET A N     1 
ATOM   15290 C  CA    . MET A 1 3579 ? 157.326 134.996 196.657 1.00 14.51  ? 3579 MET A CA    1 
ATOM   15291 C  C     . MET A 1 3579 ? 155.877 135.501 196.581 1.00 16.76  ? 3579 MET A C     1 
ATOM   15292 O  O     . MET A 1 3579 ? 155.517 136.388 197.385 1.00 19.40  ? 3579 MET A O     1 
ATOM   15293 C  CB    . MET A 1 3579 ? 158.170 135.675 195.573 1.00 13.13  ? 3579 MET A CB    1 
ATOM   15294 C  CG    . MET A 1 3579 ? 159.631 135.267 195.588 1.00 14.29  ? 3579 MET A CG    1 
ATOM   15295 S  SD    . MET A 1 3579 ? 160.580 135.974 194.227 1.00 21.88  ? 3579 MET A SD    1 
ATOM   15296 C  CE    . MET A 1 3579 ? 162.207 135.279 194.545 1.00 21.73  ? 3579 MET A CE    1 
ATOM   15297 N  N     . LEU A 1 3580 ? 155.082 134.949 195.660 1.00 18.52  ? 3580 LEU A N     1 
ATOM   15298 C  CA    . LEU A 1 3580 ? 153.671 135.388 195.487 1.00 17.57  ? 3580 LEU A CA    1 
ATOM   15299 C  C     . LEU A 1 3580 ? 152.838 134.924 196.693 1.00 23.45  ? 3580 LEU A C     1 
ATOM   15300 O  O     . LEU A 1 3580 ? 151.671 135.357 196.806 1.00 28.89  ? 3580 LEU A O     1 
ATOM   15301 C  CB    . LEU A 1 3580 ? 153.117 134.839 194.174 1.00 15.81  ? 3580 LEU A CB    1 
ATOM   15302 C  CG    . LEU A 1 3580 ? 153.789 135.351 192.896 1.00 16.19  ? 3580 LEU A CG    1 
ATOM   15303 C  CD1   . LEU A 1 3580 ? 153.224 134.656 191.670 1.00 17.60  ? 3580 LEU A CD1   1 
ATOM   15304 C  CD2   . LEU A 1 3580 ? 153.633 136.856 192.777 1.00 18.54  ? 3580 LEU A CD2   1 
ATOM   15305 N  N     . LYS A 1 3581 ? 153.409 134.070 197.546 1.00 18.96  ? 3581 LYS A N     1 
ATOM   15306 C  CA    . LYS A 1 3581 ? 152.690 133.574 198.748 1.00 18.96  ? 3581 LYS A CA    1 
ATOM   15307 C  C     . LYS A 1 3581 ? 153.284 134.227 200.005 1.00 24.69  ? 3581 LYS A C     1 
ATOM   15308 O  O     . LYS A 1 3581 ? 152.578 134.276 201.035 1.00 29.23  ? 3581 LYS A O     1 
ATOM   15309 C  CB    . LYS A 1 3581 ? 152.782 132.044 198.786 1.00 21.03  ? 3581 LYS A CB    1 
ATOM   15310 C  CG    . LYS A 1 3581 ? 152.402 131.374 200.098 1.00 26.34  ? 3581 LYS A CG    1 
ATOM   15311 C  CD    . LYS A 1 3581 ? 153.613 130.821 200.840 1.00 30.74  ? 3581 LYS A CD    1 
ATOM   15312 C  CE    . LYS A 1 3581 ? 154.446 129.941 199.963 1.00 35.48  ? 3581 LYS A CE    1 
ATOM   15313 N  NZ    . LYS A 1 3581 ? 155.555 129.325 200.695 1.00 35.41  ? 3581 LYS A NZ    1 
ATOM   15314 N  N     . ARG A 1 3582 ? 154.524 134.718 199.919 1.00 22.01  ? 3582 ARG A N     1 
ATOM   15315 C  CA    . ARG A 1 3582 ? 155.200 135.329 201.093 1.00 19.92  ? 3582 ARG A CA    1 
ATOM   15316 C  C     . ARG A 1 3582 ? 155.727 136.719 200.711 1.00 23.88  ? 3582 ARG A C     1 
ATOM   15317 O  O     . ARG A 1 3582 ? 156.960 136.859 200.570 1.00 29.76  ? 3582 ARG A O     1 
ATOM   15318 C  CB    . ARG A 1 3582 ? 156.388 134.471 201.535 1.00 21.37  ? 3582 ARG A CB    1 
ATOM   15319 C  CG    . ARG A 1 3582 ? 156.114 133.014 201.876 1.00 25.88  ? 3582 ARG A CG    1 
ATOM   15320 C  CD    . ARG A 1 3582 ? 157.429 132.278 202.092 1.00 26.65  ? 3582 ARG A CD    1 
ATOM   15321 N  NE    . ARG A 1 3582 ? 157.267 130.897 202.561 1.00 31.93  ? 3582 ARG A NE    1 
ATOM   15322 C  CZ    . ARG A 1 3582 ? 156.715 130.545 203.715 1.00 38.63  ? 3582 ARG A CZ    1 
ATOM   15323 N  NH1   . ARG A 1 3582 ? 156.362 131.467 204.592 1.00 40.19  ? 3582 ARG A NH1   1 
ATOM   15324 N  NH2   . ARG A 1 3582 ? 156.526 129.267 203.992 1.00 34.25  ? 3582 ARG A NH2   1 
ATOM   15325 N  N     . PHE A 1 3583 ? 154.837 137.702 200.548 1.00 23.34  ? 3583 PHE A N     1 
ATOM   15326 C  CA    . PHE A 1 3583 ? 155.286 139.047 200.094 1.00 21.09  ? 3583 PHE A CA    1 
ATOM   15327 C  C     . PHE A 1 3583 ? 154.780 140.119 201.054 1.00 21.86  ? 3583 PHE A C     1 
ATOM   15328 O  O     . PHE A 1 3583 ? 153.572 140.125 201.374 1.00 26.54  ? 3583 PHE A O     1 
ATOM   15329 C  CB    . PHE A 1 3583 ? 154.810 139.321 198.664 1.00 23.17  ? 3583 PHE A CB    1 
ATOM   15330 C  CG    . PHE A 1 3583 ? 153.301 139.300 198.458 1.00 27.56  ? 3583 PHE A CG    1 
ATOM   15331 C  CD1   . PHE A 1 3583 ? 152.647 138.129 198.094 1.00 25.22  ? 3583 PHE A CD1   1 
ATOM   15332 C  CD2   . PHE A 1 3583 ? 152.541 140.452 198.624 1.00 24.70  ? 3583 PHE A CD2   1 
ATOM   15333 C  CE1   . PHE A 1 3583 ? 151.274 138.115 197.905 1.00 22.88  ? 3583 PHE A CE1   1 
ATOM   15334 C  CE2   . PHE A 1 3583 ? 151.169 140.431 198.436 1.00 23.45  ? 3583 PHE A CE2   1 
ATOM   15335 C  CZ    . PHE A 1 3583 ? 150.539 139.264 198.076 1.00 26.57  ? 3583 PHE A CZ    1 
ATOM   15336 N  N     . ASN A 1 3584 ? 155.676 140.998 201.514 1.00 24.99  ? 3584 ASN A N     1 
ATOM   15337 C  CA    . ASN A 1 3584 ? 155.233 142.137 202.365 1.00 23.82  ? 3584 ASN A CA    1 
ATOM   15338 C  C     . ASN A 1 3584 ? 154.644 143.192 201.429 1.00 26.80  ? 3584 ASN A C     1 
ATOM   15339 O  O     . ASN A 1 3584 ? 153.467 143.566 201.625 1.00 36.93  ? 3584 ASN A O     1 
ATOM   15340 C  CB    . ASN A 1 3584 ? 156.366 142.695 203.218 1.00 26.28  ? 3584 ASN A CB    1 
ATOM   15341 C  CG    . ASN A 1 3584 ? 157.021 141.641 204.078 1.00 31.40  ? 3584 ASN A CG    1 
ATOM   15342 O  OD1   . ASN A 1 3584 ? 156.343 140.960 204.855 1.00 33.01  ? 3584 ASN A OD1   1 
ATOM   15343 N  ND2   . ASN A 1 3584 ? 158.332 141.489 203.954 1.00 29.32  ? 3584 ASN A ND2   1 
ATOM   15344 N  N     . ARG A 1 3585 ? 155.427 143.645 200.447 1.00 23.22  ? 3585 ARG A N     1 
ATOM   15345 C  CA    . ARG A 1 3585 ? 154.910 144.579 199.461 1.00 19.78  ? 3585 ARG A CA    1 
ATOM   15346 C  C     . ARG A 1 3585 ? 154.140 143.819 198.390 1.00 21.62  ? 3585 ARG A C     1 
ATOM   15347 O  O     . ARG A 1 3585 ? 154.396 142.639 198.134 1.00 25.54  ? 3585 ARG A O     1 
ATOM   15348 C  CB    . ARG A 1 3585 ? 156.046 145.378 198.822 1.00 17.06  ? 3585 ARG A CB    1 
ATOM   15349 C  CG    . ARG A 1 3585 ? 156.657 146.428 199.730 1.00 18.24  ? 3585 ARG A CG    1 
ATOM   15350 C  CD    . ARG A 1 3585 ? 157.935 146.991 199.132 1.00 20.85  ? 3585 ARG A CD    1 
ATOM   15351 N  NE    . ARG A 1 3585 ? 158.922 145.950 198.873 1.00 17.90  ? 3585 ARG A NE    1 
ATOM   15352 C  CZ    . ARG A 1 3585 ? 159.974 146.096 198.080 1.00 13.68  ? 3585 ARG A CZ    1 
ATOM   15353 N  NH1   . ARG A 1 3585 ? 160.206 147.232 197.443 1.00 15.50  ? 3585 ARG A NH1   1 
ATOM   15354 N  NH2   . ARG A 1 3585 ? 160.814 145.077 197.922 1.00 13.03  ? 3585 ARG A NH2   1 
ATOM   15355 N  N     . TYR A 1 3586 ? 153.188 144.501 197.767 1.00 20.12  ? 3586 TYR A N     1 
ATOM   15356 C  CA    . TYR A 1 3586 ? 152.352 143.849 196.772 1.00 17.40  ? 3586 TYR A CA    1 
ATOM   15357 C  C     . TYR A 1 3586 ? 153.186 143.464 195.551 1.00 18.40  ? 3586 TYR A C     1 
ATOM   15358 O  O     . TYR A 1 3586 ? 154.074 144.217 195.139 1.00 20.77  ? 3586 TYR A O     1 
ATOM   15359 C  CB    . TYR A 1 3586 ? 151.194 144.758 196.370 1.00 19.91  ? 3586 TYR A CB    1 
ATOM   15360 C  CG    . TYR A 1 3586 ? 150.179 144.930 197.476 1.00 26.88  ? 3586 TYR A CG    1 
ATOM   15361 C  CD1   . TYR A 1 3586 ? 149.493 143.837 197.987 1.00 24.60  ? 3586 TYR A CD1   1 
ATOM   15362 C  CD2   . TYR A 1 3586 ? 149.913 146.180 198.017 1.00 27.09  ? 3586 TYR A CD2   1 
ATOM   15363 C  CE1   . TYR A 1 3586 ? 148.567 143.983 198.999 1.00 26.64  ? 3586 TYR A CE1   1 
ATOM   15364 C  CE2   . TYR A 1 3586 ? 148.988 146.336 199.030 1.00 29.64  ? 3586 TYR A CE2   1 
ATOM   15365 C  CZ    . TYR A 1 3586 ? 148.319 145.235 199.518 1.00 31.25  ? 3586 TYR A CZ    1 
ATOM   15366 O  OH    . TYR A 1 3586 ? 147.397 145.385 200.528 1.00 36.74  ? 3586 TYR A OH    1 
ATOM   15367 N  N     . PRO A 1 3587 ? 152.932 142.300 194.961 1.00 14.95  ? 3587 PRO A N     1 
ATOM   15368 C  CA    . PRO A 1 3587 ? 153.817 141.792 193.909 1.00 12.48  ? 3587 PRO A CA    1 
ATOM   15369 C  C     . PRO A 1 3587 ? 153.616 142.487 192.574 1.00 16.57  ? 3587 PRO A C     1 
ATOM   15370 O  O     . PRO A 1 3587 ? 152.518 142.923 192.222 1.00 17.12  ? 3587 PRO A O     1 
ATOM   15371 C  CB    . PRO A 1 3587 ? 153.437 140.307 193.808 1.00 15.14  ? 3587 PRO A CB    1 
ATOM   15372 C  CG    . PRO A 1 3587 ? 152.474 140.040 194.935 1.00 19.72  ? 3587 PRO A CG    1 
ATOM   15373 C  CD    . PRO A 1 3587 ? 151.860 141.349 195.284 1.00 19.66  ? 3587 PRO A CD    1 
ATOM   15374 N  N     . LEU A 1 3588 ? 154.713 142.581 191.828 1.00 18.28  ? 3588 LEU A N     1 
ATOM   15375 C  CA    . LEU A 1 3588 ? 154.696 143.010 190.435 1.00 15.97  ? 3588 LEU A CA    1 
ATOM   15376 C  C     . LEU A 1 3588 ? 155.265 141.869 189.600 1.00 16.98  ? 3588 LEU A C     1 
ATOM   15377 O  O     . LEU A 1 3588 ? 156.431 141.494 189.763 1.00 18.41  ? 3588 LEU A O     1 
ATOM   15378 C  CB    . LEU A 1 3588 ? 155.487 144.299 190.236 1.00 13.53  ? 3588 LEU A CB    1 
ATOM   15379 C  CG    . LEU A 1 3588 ? 155.539 144.752 188.780 1.00 13.85  ? 3588 LEU A CG    1 
ATOM   15380 C  CD1   . LEU A 1 3588 ? 154.216 145.354 188.416 1.00 16.91  ? 3588 LEU A CD1   1 
ATOM   15381 C  CD2   . LEU A 1 3588 ? 156.628 145.771 188.570 1.00 18.20  ? 3588 LEU A CD2   1 
ATOM   15382 N  N     . ILE A 1 3589 ? 154.444 141.322 188.709 1.00 15.80  ? 3589 ILE A N     1 
ATOM   15383 C  CA    . ILE A 1 3589 ? 154.767 140.104 187.977 1.00 13.16  ? 3589 ILE A CA    1 
ATOM   15384 C  C     . ILE A 1 3589 ? 155.185 140.469 186.561 1.00 18.16  ? 3589 ILE A C     1 
ATOM   15385 O  O     . ILE A 1 3589 ? 154.509 141.257 185.888 1.00 23.28  ? 3589 ILE A O     1 
ATOM   15386 C  CB    . ILE A 1 3589 ? 153.574 139.135 187.962 1.00 14.30  ? 3589 ILE A CB    1 
ATOM   15387 C  CG1   . ILE A 1 3589 ? 153.215 138.709 189.385 1.00 19.03  ? 3589 ILE A CG1   1 
ATOM   15388 C  CG2   . ILE A 1 3589 ? 153.887 137.917 187.112 1.00 19.15  ? 3589 ILE A CG2   1 
ATOM   15389 C  CD1   . ILE A 1 3589 ? 151.964 137.866 189.468 1.00 29.11  ? 3589 ILE A CD1   1 
ATOM   15390 N  N     . ILE A 1 3590 ? 156.298 139.900 186.108 1.00 18.18  ? 3590 ILE A N     1 
ATOM   15391 C  CA    . ILE A 1 3590 ? 156.750 140.025 184.728 1.00 19.23  ? 3590 ILE A CA    1 
ATOM   15392 C  C     . ILE A 1 3590 ? 156.693 138.636 184.107 1.00 24.97  ? 3590 ILE A C     1 
ATOM   15393 O  O     . ILE A 1 3590 ? 157.469 137.749 184.484 1.00 23.85  ? 3590 ILE A O     1 
ATOM   15394 C  CB    . ILE A 1 3590 ? 158.163 140.614 184.632 1.00 17.00  ? 3590 ILE A CB    1 
ATOM   15395 C  CG1   . ILE A 1 3590 ? 158.282 141.868 185.500 1.00 22.53  ? 3590 ILE A CG1   1 
ATOM   15396 C  CG2   . ILE A 1 3590 ? 158.508 140.934 183.188 1.00 23.50  ? 3590 ILE A CG2   1 
ATOM   15397 C  CD1   . ILE A 1 3590 ? 159.703 142.345 185.685 1.00 24.41  ? 3590 ILE A CD1   1 
ATOM   15398 N  N     . ASP A 1 3591 ? 155.777 138.443 183.159 1.00 24.59  ? 3591 ASP A N     1 
ATOM   15399 C  CA    . ASP A 1 3591 ? 155.656 137.175 182.439 1.00 26.10  ? 3591 ASP A CA    1 
ATOM   15400 C  C     . ASP A 1 3591 ? 155.218 137.464 181.013 1.00 31.04  ? 3591 ASP A C     1 
ATOM   15401 O  O     . ASP A 1 3591 ? 154.017 137.619 180.740 1.00 32.65  ? 3591 ASP A O     1 
ATOM   15402 C  CB    . ASP A 1 3591 ? 154.680 136.217 183.117 1.00 30.57  ? 3591 ASP A CB    1 
ATOM   15403 C  CG    . ASP A 1 3591 ? 154.943 134.770 182.748 1.00 38.52  ? 3591 ASP A CG    1 
ATOM   15404 O  OD1   . ASP A 1 3591 ? 155.909 134.514 182.000 1.00 39.80  ? 3591 ASP A OD1   1 
ATOM   15405 O  OD2   . ASP A 1 3591 ? 154.182 133.887 183.194 1.00 39.55  ? 3591 ASP A OD2   1 
ATOM   15406 N  N     . PRO A 1 3592 ? 156.159 137.551 180.073 1.00 33.76  ? 3592 PRO A N     1 
ATOM   15407 C  CA    . PRO A 1 3592 ? 155.765 137.628 178.658 1.00 33.63  ? 3592 PRO A CA    1 
ATOM   15408 C  C     . PRO A 1 3592 ? 154.989 136.410 178.191 1.00 31.95  ? 3592 PRO A C     1 
ATOM   15409 O  O     . PRO A 1 3592 ? 154.117 136.536 177.323 1.00 35.58  ? 3592 PRO A O     1 
ATOM   15410 C  CB    . PRO A 1 3592 ? 157.108 137.762 177.925 1.00 30.03  ? 3592 PRO A CB    1 
ATOM   15411 C  CG    . PRO A 1 3592 ? 158.130 137.251 178.887 1.00 31.75  ? 3592 PRO A CG    1 
ATOM   15412 C  CD    . PRO A 1 3592 ? 157.620 137.588 180.250 1.00 29.46  ? 3592 PRO A CD    1 
ATOM   15413 N  N     . SER A 1 3593 ? 155.282 135.230 178.744 1.00 31.37  ? 3593 SER A N     1 
ATOM   15414 C  CA    . SER A 1 3593 ? 154.627 134.005 178.302 1.00 34.64  ? 3593 SER A CA    1 
ATOM   15415 C  C     . SER A 1 3593 ? 153.191 133.891 178.802 1.00 34.61  ? 3593 SER A C     1 
ATOM   15416 O  O     . SER A 1 3593 ? 152.344 133.347 178.086 1.00 36.87  ? 3593 SER A O     1 
ATOM   15417 C  CB    . SER A 1 3593 ? 155.443 132.794 178.753 1.00 38.89  ? 3593 SER A CB    1 
ATOM   15418 O  OG    . SER A 1 3593 ? 156.737 132.806 178.175 1.00 33.80  ? 3593 SER A OG    1 
ATOM   15419 N  N     . GLY A 1 3594 ? 152.897 134.384 180.004 1.00 33.57  ? 3594 GLY A N     1 
ATOM   15420 C  CA    . GLY A 1 3594 ? 151.528 134.498 180.463 1.00 31.84  ? 3594 GLY A CA    1 
ATOM   15421 C  C     . GLY A 1 3594 ? 151.037 133.436 181.425 1.00 39.27  ? 3594 GLY A C     1 
ATOM   15422 O  O     . GLY A 1 3594 ? 149.896 133.541 181.893 1.00 38.76  ? 3594 GLY A O     1 
ATOM   15423 N  N     . GLN A 1 3595 ? 151.841 132.416 181.741 1.00 39.41  ? 3595 GLN A N     1 
ATOM   15424 C  CA    . GLN A 1 3595 ? 151.380 131.410 182.696 1.00 38.30  ? 3595 GLN A CA    1 
ATOM   15425 C  C     . GLN A 1 3595 ? 151.223 131.980 184.100 1.00 42.71  ? 3595 GLN A C     1 
ATOM   15426 O  O     . GLN A 1 3595 ? 150.390 131.492 184.871 1.00 44.86  ? 3595 GLN A O     1 
ATOM   15427 C  CB    . GLN A 1 3595 ? 152.324 130.206 182.724 1.00 41.03  ? 3595 GLN A CB    1 
ATOM   15428 C  CG    . GLN A 1 3595 ? 152.358 129.391 181.442 1.00 49.25  ? 3595 GLN A CG    1 
ATOM   15429 C  CD    . GLN A 1 3595 ? 153.668 129.515 180.700 1.00 50.73  ? 3595 GLN A CD    1 
ATOM   15430 O  OE1   . GLN A 1 3595 ? 153.893 130.481 179.976 1.00 41.80  ? 3595 GLN A OE1   1 
ATOM   15431 N  NE2   . GLN A 1 3595 ? 154.544 128.533 180.875 1.00 50.21  ? 3595 GLN A NE2   1 
ATOM   15432 N  N     . ALA A 1 3596 ? 152.011 132.998 184.454 1.00 39.05  ? 3596 ALA A N     1 
ATOM   15433 C  CA    . ALA A 1 3596 ? 151.902 133.584 185.788 1.00 33.85  ? 3596 ALA A CA    1 
ATOM   15434 C  C     . ALA A 1 3596 ? 150.544 134.239 186.001 1.00 35.91  ? 3596 ALA A C     1 
ATOM   15435 O  O     . ALA A 1 3596 ? 149.932 134.078 187.063 1.00 40.06  ? 3596 ALA A O     1 
ATOM   15436 C  CB    . ALA A 1 3596 ? 153.020 134.597 186.011 1.00 29.21  ? 3596 ALA A CB    1 
ATOM   15437 N  N     . THR A 1 3597 ? 150.062 134.990 185.008 1.00 36.40  ? 3597 THR A N     1 
ATOM   15438 C  CA    . THR A 1 3597 ? 148.754 135.625 185.131 1.00 40.84  ? 3597 THR A CA    1 
ATOM   15439 C  C     . THR A 1 3597 ? 147.651 134.582 185.258 1.00 40.28  ? 3597 THR A C     1 
ATOM   15440 O  O     . THR A 1 3597 ? 146.743 134.723 186.087 1.00 37.73  ? 3597 THR A O     1 
ATOM   15441 C  CB    . THR A 1 3597 ? 148.503 136.541 183.931 1.00 38.48  ? 3597 THR A CB    1 
ATOM   15442 O  OG1   . THR A 1 3597 ? 149.157 137.798 184.145 1.00 25.77  ? 3597 THR A OG1   1 
ATOM   15443 C  CG2   . THR A 1 3597 ? 147.012 136.782 183.731 1.00 39.83  ? 3597 THR A CG2   1 
ATOM   15444 N  N     . GLU A 1 3598 ? 147.721 133.520 184.453 1.00 40.96  ? 3598 GLU A N     1 
ATOM   15445 C  CA    . GLU A 1 3598 ? 146.758 132.431 184.580 1.00 41.80  ? 3598 GLU A CA    1 
ATOM   15446 C  C     . GLU A 1 3598 ? 146.879 131.743 185.934 1.00 42.18  ? 3598 GLU A C     1 
ATOM   15447 O  O     . GLU A 1 3598 ? 145.867 131.434 186.573 1.00 40.84  ? 3598 GLU A O     1 
ATOM   15448 C  CB    . GLU A 1 3598 ? 146.952 131.428 183.444 1.00 43.81  ? 3598 GLU A CB    1 
ATOM   15449 C  CG    . GLU A 1 3598 ? 146.023 130.228 183.506 1.00 53.21  ? 3598 GLU A CG    1 
ATOM   15450 C  CD    . GLU A 1 3598 ? 146.451 129.111 182.575 1.00 66.01  ? 3598 GLU A CD    1 
ATOM   15451 O  OE1   . GLU A 1 3598 ? 145.593 128.282 182.205 1.00 64.17  ? 3598 GLU A OE1   1 
ATOM   15452 O  OE2   . GLU A 1 3598 ? 147.645 129.064 182.211 1.00 63.15  ? 3598 GLU A OE2   1 
ATOM   15453 N  N     . PHE A 1 3599 ? 148.112 131.511 186.395 1.00 43.21  ? 3599 PHE A N     1 
ATOM   15454 C  CA    . PHE A 1 3599 ? 148.318 130.835 187.673 1.00 36.18  ? 3599 PHE A CA    1 
ATOM   15455 C  C     . PHE A 1 3599 ? 147.703 131.622 188.823 1.00 37.00  ? 3599 PHE A C     1 
ATOM   15456 O  O     . PHE A 1 3599 ? 147.085 131.042 189.722 1.00 38.13  ? 3599 PHE A O     1 
ATOM   15457 C  CB    . PHE A 1 3599 ? 149.812 130.615 187.914 1.00 33.40  ? 3599 PHE A CB    1 
ATOM   15458 C  CG    . PHE A 1 3599 ? 150.169 130.397 189.357 1.00 34.26  ? 3599 PHE A CG    1 
ATOM   15459 C  CD1   . PHE A 1 3599 ? 149.868 129.202 189.988 1.00 34.38  ? 3599 PHE A CD1   1 
ATOM   15460 C  CD2   . PHE A 1 3599 ? 150.804 131.391 190.083 1.00 31.90  ? 3599 PHE A CD2   1 
ATOM   15461 C  CE1   . PHE A 1 3599 ? 150.195 129.002 191.315 1.00 32.92  ? 3599 PHE A CE1   1 
ATOM   15462 C  CE2   . PHE A 1 3599 ? 151.133 131.197 191.409 1.00 27.41  ? 3599 PHE A CE2   1 
ATOM   15463 C  CZ    . PHE A 1 3599 ? 150.828 130.001 192.026 1.00 31.55  ? 3599 PHE A CZ    1 
ATOM   15464 N  N     . ILE A 1 3600 ? 147.868 132.946 188.813 1.00 38.16  ? 3600 ILE A N     1 
ATOM   15465 C  CA    . ILE A 1 3600 ? 147.270 133.779 189.851 1.00 37.98  ? 3600 ILE A CA    1 
ATOM   15466 C  C     . ILE A 1 3600 ? 145.749 133.709 189.780 1.00 38.44  ? 3600 ILE A C     1 
ATOM   15467 O  O     . ILE A 1 3600 ? 145.068 133.644 190.811 1.00 39.20  ? 3600 ILE A O     1 
ATOM   15468 C  CB    . ILE A 1 3600 ? 147.786 135.225 189.731 1.00 34.70  ? 3600 ILE A CB    1 
ATOM   15469 C  CG1   . ILE A 1 3600 ? 149.189 135.340 190.329 1.00 31.54  ? 3600 ILE A CG1   1 
ATOM   15470 C  CG2   . ILE A 1 3600 ? 146.845 136.200 190.416 1.00 32.89  ? 3600 ILE A CG2   1 
ATOM   15471 C  CD1   . ILE A 1 3600 ? 149.240 135.083 191.819 1.00 27.38  ? 3600 ILE A CD1   1 
ATOM   15472 N  N     . MET A 1 3601 ? 145.191 133.712 188.566 1.00 40.39  ? 3601 MET A N     1 
ATOM   15473 C  CA    . MET A 1 3601 ? 143.739 133.689 188.414 1.00 38.16  ? 3601 MET A CA    1 
ATOM   15474 C  C     . MET A 1 3601 ? 143.137 132.397 188.956 1.00 45.51  ? 3601 MET A C     1 
ATOM   15475 O  O     . MET A 1 3601 ? 142.107 132.425 189.639 1.00 51.74  ? 3601 MET A O     1 
ATOM   15476 C  CB    . MET A 1 3601 ? 143.365 133.882 186.944 1.00 36.62  ? 3601 MET A CB    1 
ATOM   15477 C  CG    . MET A 1 3601 ? 143.506 135.314 186.453 1.00 40.23  ? 3601 MET A CG    1 
ATOM   15478 S  SD    . MET A 1 3601 ? 142.295 136.433 187.183 1.00 60.89  ? 3601 MET A SD    1 
ATOM   15479 C  CE    . MET A 1 3601 ? 140.787 135.852 186.412 1.00 47.04  ? 3601 MET A CE    1 
ATOM   15480 N  N     . ASN A 1 3602 ? 143.760 131.252 188.660 1.00 39.33  ? 3602 ASN A N     1 
ATOM   15481 C  CA    . ASN A 1 3602 ? 143.243 129.989 189.182 1.00 37.70  ? 3602 ASN A CA    1 
ATOM   15482 C  C     . ASN A 1 3602 ? 143.487 129.865 190.680 1.00 41.28  ? 3602 ASN A C     1 
ATOM   15483 O  O     . ASN A 1 3602 ? 142.668 129.283 191.401 1.00 46.66  ? 3602 ASN A O     1 
ATOM   15484 C  CB    . ASN A 1 3602 ? 143.865 128.803 188.443 1.00 36.26  ? 3602 ASN A CB    1 
ATOM   15485 C  CG    . ASN A 1 3602 ? 143.825 128.961 186.936 1.00 45.59  ? 3602 ASN A CG    1 
ATOM   15486 O  OD1   . ASN A 1 3602 ? 144.861 128.957 186.272 1.00 48.70  ? 3602 ASN A OD1   1 
ATOM   15487 N  ND2   . ASN A 1 3602 ? 142.624 129.101 186.387 1.00 49.61  ? 3602 ASN A ND2   1 
ATOM   15488 N  N     . GLU A 1 3603 ? 144.611 130.397 191.167 1.00 41.76  ? 3603 GLU A N     1 
ATOM   15489 C  CA    . GLU A 1 3603 ? 144.940 130.267 192.583 1.00 40.96  ? 3603 GLU A CA    1 
ATOM   15490 C  C     . GLU A 1 3603 ? 143.942 131.017 193.457 1.00 44.87  ? 3603 GLU A C     1 
ATOM   15491 O  O     . GLU A 1 3603 ? 143.563 130.534 194.530 1.00 46.08  ? 3603 GLU A O     1 
ATOM   15492 C  CB    . GLU A 1 3603 ? 146.361 130.768 192.840 1.00 39.91  ? 3603 GLU A CB    1 
ATOM   15493 C  CG    . GLU A 1 3603 ? 146.906 130.411 194.210 1.00 41.36  ? 3603 GLU A CG    1 
ATOM   15494 C  CD    . GLU A 1 3603 ? 147.456 129.000 194.264 1.00 41.93  ? 3603 GLU A CD    1 
ATOM   15495 O  OE1   . GLU A 1 3603 ? 147.558 128.360 193.196 1.00 43.08  ? 3603 GLU A OE1   1 
ATOM   15496 O  OE2   . GLU A 1 3603 ? 147.785 128.530 195.373 1.00 45.57  ? 3603 GLU A OE2   1 
ATOM   15497 N  N     . TYR A 1 3604 ? 143.508 132.198 193.018 1.00 45.55  ? 3604 TYR A N     1 
ATOM   15498 C  CA    . TYR A 1 3604 ? 142.567 133.020 193.766 1.00 47.73  ? 3604 TYR A CA    1 
ATOM   15499 C  C     . TYR A 1 3604 ? 141.152 132.946 193.202 1.00 51.81  ? 3604 TYR A C     1 
ATOM   15500 O  O     . TYR A 1 3604 ? 140.358 133.869 193.414 1.00 56.50  ? 3604 TYR A O     1 
ATOM   15501 C  CB    . TYR A 1 3604 ? 143.045 134.472 193.799 1.00 46.50  ? 3604 TYR A CB    1 
ATOM   15502 C  CG    . TYR A 1 3604 ? 144.223 134.715 194.714 1.00 45.67  ? 3604 TYR A CG    1 
ATOM   15503 C  CD1   . TYR A 1 3604 ? 145.518 134.429 194.302 1.00 41.59  ? 3604 TYR A CD1   1 
ATOM   15504 C  CD2   . TYR A 1 3604 ? 144.042 135.231 195.990 1.00 45.47  ? 3604 TYR A CD2   1 
ATOM   15505 C  CE1   . TYR A 1 3604 ? 146.597 134.649 195.134 1.00 38.15  ? 3604 TYR A CE1   1 
ATOM   15506 C  CE2   . TYR A 1 3604 ? 145.116 135.455 196.828 1.00 44.27  ? 3604 TYR A CE2   1 
ATOM   15507 C  CZ    . TYR A 1 3604 ? 146.391 135.163 196.395 1.00 38.88  ? 3604 TYR A CZ    1 
ATOM   15508 O  OH    . TYR A 1 3604 ? 147.462 135.385 197.229 1.00 39.84  ? 3604 TYR A OH    1 
ATOM   15509 N  N     . LYS A 1 3605 ? 140.848 131.864 192.481 1.00 53.00  ? 3605 LYS A N     1 
ATOM   15510 C  CA    . LYS A 1 3605 ? 139.507 131.712 191.856 1.00 54.26  ? 3605 LYS A CA    1 
ATOM   15511 C  C     . LYS A 1 3605 ? 138.440 131.624 192.957 1.00 58.90  ? 3605 LYS A C     1 
ATOM   15512 O  O     . LYS A 1 3605 ? 137.385 132.279 192.814 1.00 55.82  ? 3605 LYS A O     1 
ATOM   15513 C  CB    . LYS A 1 3605 ? 139.481 130.462 190.971 1.00 50.20  ? 3605 LYS A CB    1 
ATOM   15514 C  CG    . LYS A 1 3605 ? 138.270 130.346 190.058 1.00 58.78  ? 3605 LYS A CG    1 
ATOM   15515 C  CD    . LYS A 1 3605 ? 138.179 131.488 189.054 1.00 63.54  ? 3605 LYS A CD    1 
ATOM   15516 C  CE    . LYS A 1 3605 ? 139.419 131.621 188.228 1.00 66.82  ? 3605 LYS A CE    1 
ATOM   15517 N  NZ    . LYS A 1 3605 ? 139.743 130.377 187.525 1.00 68.54  ? 3605 LYS A NZ    1 
ATOM   15518 N  N     . ASP A 1 3606 ? 138.709 130.846 194.009 1.00 61.66  ? 3606 ASP A N     1 
ATOM   15519 C  CA    . ASP A 1 3606 ? 137.738 130.686 195.127 1.00 60.09  ? 3606 ASP A CA    1 
ATOM   15520 C  C     . ASP A 1 3606 ? 137.483 132.051 195.773 1.00 61.00  ? 3606 ASP A C     1 
ATOM   15521 O  O     . ASP A 1 3606 ? 136.390 132.240 196.347 1.00 62.12  ? 3606 ASP A O     1 
ATOM   15522 C  CB    . ASP A 1 3606 ? 138.228 129.658 196.132 1.00 62.16  ? 3606 ASP A CB    1 
ATOM   15523 C  CG    . ASP A 1 3606 ? 139.678 129.819 196.565 1.00 64.99  ? 3606 ASP A CG    1 
ATOM   15524 O  OD1   . ASP A 1 3606 ? 140.012 130.892 197.109 1.00 62.32  ? 3606 ASP A OD1   1 
ATOM   15525 O  OD2   . ASP A 1 3606 ? 140.462 128.870 196.352 1.00 67.09  ? 3606 ASP A OD2   1 
ATOM   15526 N  N     . ARG A 1 3607 ? 138.460 132.957 195.696 1.00 59.20  ? 3607 ARG A N     1 
ATOM   15527 C  CA    . ARG A 1 3607 ? 138.296 134.321 196.264 1.00 56.86  ? 3607 ARG A CA    1 
ATOM   15528 C  C     . ARG A 1 3607 ? 137.738 135.249 195.176 1.00 54.22  ? 3607 ARG A C     1 
ATOM   15529 O  O     . ARG A 1 3607 ? 137.628 136.467 195.436 1.00 57.29  ? 3607 ARG A O     1 
ATOM   15530 C  CB    . ARG A 1 3607 ? 139.638 134.838 196.790 1.00 56.14  ? 3607 ARG A CB    1 
ATOM   15531 C  CG    . ARG A 1 3607 ? 140.253 133.991 197.894 1.00 57.09  ? 3607 ARG A CG    1 
ATOM   15532 C  CD    . ARG A 1 3607 ? 141.552 134.619 198.365 1.00 58.83  ? 3607 ARG A CD    1 
ATOM   15533 N  NE    . ARG A 1 3607 ? 141.362 136.053 198.605 1.00 64.69  ? 3607 ARG A NE    1 
ATOM   15534 C  CZ    . ARG A 1 3607 ? 142.306 136.891 199.008 1.00 66.30  ? 3607 ARG A CZ    1 
ATOM   15535 N  NH1   . ARG A 1 3607 ? 143.483 136.429 199.392 1.00 67.58  ? 3607 ARG A NH1   1 
ATOM   15536 N  NH2   . ARG A 1 3607 ? 142.066 138.189 199.028 1.00 63.38  ? 3607 ARG A NH2   1 
ATOM   15537 N  N     . LYS A 1 3608 ? 137.407 134.692 194.008 1.00 53.99  ? 3608 LYS A N     1 
ATOM   15538 C  CA    . LYS A 1 3608 ? 136.850 135.502 192.892 1.00 55.42  ? 3608 LYS A CA    1 
ATOM   15539 C  C     . LYS A 1 3608 ? 137.784 136.688 192.603 1.00 50.97  ? 3608 LYS A C     1 
ATOM   15540 O  O     . LYS A 1 3608 ? 137.308 137.843 192.658 1.00 49.09  ? 3608 LYS A O     1 
ATOM   15541 C  CB    . LYS A 1 3608 ? 135.432 135.984 193.222 1.00 54.84  ? 3608 LYS A CB    1 
ATOM   15542 C  CG    . LYS A 1 3608 ? 134.314 135.091 192.703 1.00 58.08  ? 3608 LYS A CG    1 
ATOM   15543 C  CD    . LYS A 1 3608 ? 134.341 133.674 193.262 1.00 64.75  ? 3608 LYS A CD    1 
ATOM   15544 C  CE    . LYS A 1 3608 ? 134.089 133.641 194.735 1.00 62.54  ? 3608 LYS A CE    1 
ATOM   15545 N  NZ    . LYS A 1 3608 ? 134.018 132.266 195.234 1.00 60.10  ? 3608 LYS A NZ    1 
ATOM   15546 N  N     . ILE A 1 3609 ? 139.058 136.411 192.309 1.00 46.48  ? 3609 ILE A N     1 
ATOM   15547 C  CA    . ILE A 1 3609 ? 140.003 137.508 191.941 1.00 42.26  ? 3609 ILE A CA    1 
ATOM   15548 C  C     . ILE A 1 3609 ? 139.466 138.197 190.677 1.00 40.79  ? 3609 ILE A C     1 
ATOM   15549 O  O     . ILE A 1 3609 ? 139.022 137.479 189.755 1.00 37.93  ? 3609 ILE A O     1 
ATOM   15550 C  CB    . ILE A 1 3609 ? 141.433 136.971 191.741 1.00 40.09  ? 3609 ILE A CB    1 
ATOM   15551 C  CG1   . ILE A 1 3609 ? 142.400 138.092 191.362 1.00 32.54  ? 3609 ILE A CG1   1 
ATOM   15552 C  CG2   . ILE A 1 3609 ? 141.457 135.831 190.722 1.00 42.49  ? 3609 ILE A CG2   1 
ATOM   15553 C  CD1   . ILE A 1 3609 ? 143.851 137.655 191.277 1.00 34.71  ? 3609 ILE A CD1   1 
ATOM   15554 N  N     . THR A 1 3610 ? 139.499 139.531 190.645 1.00 38.89  ? 3610 THR A N     1 
ATOM   15555 C  CA    . THR A 1 3610 ? 138.964 140.280 189.487 1.00 36.69  ? 3610 THR A CA    1 
ATOM   15556 C  C     . THR A 1 3610 ? 140.111 140.699 188.595 1.00 38.74  ? 3610 THR A C     1 
ATOM   15557 O  O     . THR A 1 3610 ? 141.122 141.206 189.129 1.00 40.04  ? 3610 THR A O     1 
ATOM   15558 C  CB    . THR A 1 3610 ? 138.165 141.483 189.981 1.00 41.71  ? 3610 THR A CB    1 
ATOM   15559 O  OG1   . THR A 1 3610 ? 137.074 140.925 190.707 1.00 39.12  ? 3610 THR A OG1   1 
ATOM   15560 C  CG2   . THR A 1 3610 ? 137.652 142.347 188.844 1.00 43.48  ? 3610 THR A CG2   1 
ATOM   15561 N  N     . ARG A 1 3611 ? 139.966 140.498 187.282 1.00 39.15  ? 3611 ARG A N     1 
ATOM   15562 C  CA    . ARG A 1 3611 ? 141.024 140.905 186.320 1.00 37.79  ? 3611 ARG A CA    1 
ATOM   15563 C  C     . ARG A 1 3611 ? 140.671 142.277 185.728 1.00 40.30  ? 3611 ARG A C     1 
ATOM   15564 O  O     . ARG A 1 3611 ? 139.471 142.520 185.472 1.00 41.02  ? 3611 ARG A O     1 
ATOM   15565 C  CB    . ARG A 1 3611 ? 141.204 139.853 185.219 1.00 38.70  ? 3611 ARG A CB    1 
ATOM   15566 C  CG    . ARG A 1 3611 ? 142.273 140.231 184.205 1.00 41.64  ? 3611 ARG A CG    1 
ATOM   15567 C  CD    . ARG A 1 3611 ? 142.433 139.181 183.120 1.00 46.86  ? 3611 ARG A CD    1 
ATOM   15568 N  NE    . ARG A 1 3611 ? 142.973 137.917 183.632 1.00 49.94  ? 3611 ARG A NE    1 
ATOM   15569 C  CZ    . ARG A 1 3611 ? 143.211 136.852 182.878 1.00 58.36  ? 3611 ARG A CZ    1 
ATOM   15570 N  NH1   . ARG A 1 3611 ? 142.862 136.854 181.604 1.00 63.79  ? 3611 ARG A NH1   1 
ATOM   15571 N  NH2   . ARG A 1 3611 ? 143.797 135.788 183.398 1.00 54.95  ? 3611 ARG A NH2   1 
ATOM   15572 N  N     . THR A 1 3612 ? 141.674 143.133 185.522 1.00 38.45  ? 3612 THR A N     1 
ATOM   15573 C  CA    . THR A 1 3612 ? 141.459 144.463 184.970 1.00 37.44  ? 3612 THR A CA    1 
ATOM   15574 C  C     . THR A 1 3612 ? 142.796 145.030 184.513 1.00 31.59  ? 3612 THR A C     1 
ATOM   15575 O  O     . THR A 1 3612 ? 143.844 144.398 184.666 1.00 33.58  ? 3612 THR A O     1 
ATOM   15576 C  CB    . THR A 1 3612 ? 140.790 145.400 185.985 1.00 44.04  ? 3612 THR A CB    1 
ATOM   15577 O  OG1   . THR A 1 3612 ? 140.386 146.609 185.330 1.00 48.61  ? 3612 THR A OG1   1 
ATOM   15578 C  CG2   . THR A 1 3612 ? 141.746 145.737 187.116 1.00 39.76  ? 3612 THR A CG2   1 
ATOM   15579 N  N     . SER A 1 3613 ? 142.747 146.231 183.940 1.00 30.38  ? 3613 SER A N     1 
ATOM   15580 C  CA    . SER A 1 3613 ? 143.929 146.885 183.401 1.00 34.52  ? 3613 SER A CA    1 
ATOM   15581 C  C     . SER A 1 3613 ? 143.913 148.367 183.749 1.00 39.85  ? 3613 SER A C     1 
ATOM   15582 O  O     . SER A 1 3613 ? 142.853 148.959 183.971 1.00 48.15  ? 3613 SER A O     1 
ATOM   15583 C  CB    . SER A 1 3613 ? 144.019 146.711 181.878 1.00 38.20  ? 3613 SER A CB    1 
ATOM   15584 O  OG    . SER A 1 3613 ? 144.965 147.603 181.318 1.00 45.13  ? 3613 SER A OG    1 
ATOM   15585 N  N     . PHE A 1 3614 ? 145.110 148.957 183.800 1.00 41.04  ? 3614 PHE A N     1 
ATOM   15586 C  CA    . PHE A 1 3614 ? 145.229 150.384 184.084 1.00 40.85  ? 3614 PHE A CA    1 
ATOM   15587 C  C     . PHE A 1 3614 ? 144.596 151.233 182.991 1.00 44.69  ? 3614 PHE A C     1 
ATOM   15588 O  O     . PHE A 1 3614 ? 143.961 152.252 183.286 1.00 53.41  ? 3614 PHE A O     1 
ATOM   15589 C  CB    . PHE A 1 3614 ? 146.700 150.764 184.258 1.00 41.23  ? 3614 PHE A CB    1 
ATOM   15590 C  CG    . PHE A 1 3614 ? 147.268 150.402 185.599 1.00 38.98  ? 3614 PHE A CG    1 
ATOM   15591 C  CD1   . PHE A 1 3614 ? 146.724 150.922 186.760 1.00 37.33  ? 3614 PHE A CD1   1 
ATOM   15592 C  CD2   . PHE A 1 3614 ? 148.348 149.541 185.699 1.00 36.04  ? 3614 PHE A CD2   1 
ATOM   15593 C  CE1   . PHE A 1 3614 ? 147.247 150.592 187.995 1.00 34.63  ? 3614 PHE A CE1   1 
ATOM   15594 C  CE2   . PHE A 1 3614 ? 148.875 149.206 186.931 1.00 32.84  ? 3614 PHE A CE2   1 
ATOM   15595 C  CZ    . PHE A 1 3614 ? 148.323 149.733 188.081 1.00 31.27  ? 3614 PHE A CZ    1 
ATOM   15596 N  N     . LEU A 1 3615 ? 144.762 150.838 181.726 1.00 42.99  ? 3615 LEU A N     1 
ATOM   15597 C  CA    . LEU A 1 3615 ? 144.209 151.610 180.619 1.00 47.94  ? 3615 LEU A CA    1 
ATOM   15598 C  C     . LEU A 1 3615 ? 142.687 151.614 180.613 1.00 49.37  ? 3615 LEU A C     1 
ATOM   15599 O  O     . LEU A 1 3615 ? 142.086 152.516 180.021 1.00 52.13  ? 3615 LEU A O     1 
ATOM   15600 C  CB    . LEU A 1 3615 ? 144.727 151.064 179.290 1.00 51.61  ? 3615 LEU A CB    1 
ATOM   15601 C  CG    . LEU A 1 3615 ? 146.240 150.891 179.175 1.00 44.57  ? 3615 LEU A CG    1 
ATOM   15602 C  CD1   . LEU A 1 3615 ? 146.567 149.867 178.107 1.00 43.21  ? 3615 LEU A CD1   1 
ATOM   15603 C  CD2   . LEU A 1 3615 ? 146.908 152.219 178.868 1.00 40.17  ? 3615 LEU A CD2   1 
ATOM   15604 N  N     . ASP A 1 3616 ? 142.055 150.631 181.248 1.00 47.54  ? 3616 ASP A N     1 
ATOM   15605 C  CA    . ASP A 1 3616 ? 140.602 150.579 181.288 1.00 50.84  ? 3616 ASP A CA    1 
ATOM   15606 C  C     . ASP A 1 3616 ? 140.049 151.697 182.164 1.00 53.58  ? 3616 ASP A C     1 
ATOM   15607 O  O     . ASP A 1 3616 ? 140.621 152.037 183.203 1.00 52.03  ? 3616 ASP A O     1 
ATOM   15608 C  CB    . ASP A 1 3616 ? 140.135 149.220 181.807 1.00 48.78  ? 3616 ASP A CB    1 
ATOM   15609 C  CG    . ASP A 1 3616 ? 138.716 148.895 181.392 1.00 63.60  ? 3616 ASP A CG    1 
ATOM   15610 O  OD1   . ASP A 1 3616 ? 137.829 148.868 182.270 1.00 65.92  ? 3616 ASP A OD1   1 
ATOM   15611 O  OD2   . ASP A 1 3616 ? 138.487 148.668 180.186 1.00 70.66  ? 3616 ASP A OD2   1 
ATOM   15612 N  N     . ASP A 1 3617 ? 138.925 152.275 181.732 1.00 60.34  ? 3617 ASP A N     1 
ATOM   15613 C  CA    . ASP A 1 3617 ? 138.288 153.328 182.515 1.00 63.16  ? 3617 ASP A CA    1 
ATOM   15614 C  C     . ASP A 1 3617 ? 137.643 152.778 183.780 1.00 58.60  ? 3617 ASP A C     1 
ATOM   15615 O  O     . ASP A 1 3617 ? 137.614 153.465 184.807 1.00 60.01  ? 3617 ASP A O     1 
ATOM   15616 C  CB    . ASP A 1 3617 ? 137.250 154.060 181.666 1.00 60.51  ? 3617 ASP A CB    1 
ATOM   15617 C  CG    . ASP A 1 3617 ? 137.878 154.871 180.550 1.00 68.77  ? 3617 ASP A CG    1 
ATOM   15618 O  OD1   . ASP A 1 3617 ? 139.030 155.324 180.718 1.00 66.77  ? 3617 ASP A OD1   1 
ATOM   15619 O  OD2   . ASP A 1 3617 ? 137.219 155.056 179.505 1.00 71.06  ? 3617 ASP A OD2   1 
ATOM   15620 N  N     . ALA A 1 3618 ? 137.126 151.549 183.729 1.00 53.66  ? 3618 ALA A N     1 
ATOM   15621 C  CA    . ALA A 1 3618 ? 136.486 150.947 184.892 1.00 56.37  ? 3618 ALA A CA    1 
ATOM   15622 C  C     . ALA A 1 3618 ? 137.483 150.466 185.937 1.00 60.19  ? 3618 ALA A C     1 
ATOM   15623 O  O     . ALA A 1 3618 ? 137.072 149.804 186.896 1.00 58.64  ? 3618 ALA A O     1 
ATOM   15624 C  CB    . ALA A 1 3618 ? 135.596 149.782 184.456 1.00 52.38  ? 3618 ALA A CB    1 
ATOM   15625 N  N     . PHE A 1 3619 ? 138.771 150.773 185.777 1.00 58.69  ? 3619 PHE A N     1 
ATOM   15626 C  CA    . PHE A 1 3619 ? 139.772 150.352 186.750 1.00 53.05  ? 3619 PHE A CA    1 
ATOM   15627 C  C     . PHE A 1 3619 ? 139.529 151.007 188.105 1.00 52.91  ? 3619 PHE A C     1 
ATOM   15628 O  O     . PHE A 1 3619 ? 139.656 150.366 189.154 1.00 53.39  ? 3619 PHE A O     1 
ATOM   15629 C  CB    . PHE A 1 3619 ? 141.174 150.681 186.232 1.00 48.32  ? 3619 PHE A CB    1 
ATOM   15630 C  CG    . PHE A 1 3619 ? 142.214 150.772 187.313 1.00 49.42  ? 3619 PHE A CG    1 
ATOM   15631 C  CD1   . PHE A 1 3619 ? 142.553 149.657 188.064 1.00 45.66  ? 3619 PHE A CD1   1 
ATOM   15632 C  CD2   . PHE A 1 3619 ? 142.850 151.973 187.581 1.00 41.75  ? 3619 PHE A CD2   1 
ATOM   15633 C  CE1   . PHE A 1 3619 ? 143.506 149.739 189.060 1.00 39.37  ? 3619 PHE A CE1   1 
ATOM   15634 C  CE2   . PHE A 1 3619 ? 143.804 152.060 188.576 1.00 43.73  ? 3619 PHE A CE2   1 
ATOM   15635 C  CZ    . PHE A 1 3619 ? 144.131 150.942 189.317 1.00 41.74  ? 3619 PHE A CZ    1 
ATOM   15636 N  N     . ARG A 1 3620 ? 139.182 152.296 188.099 1.00 52.25  ? 3620 ARG A N     1 
ATOM   15637 C  CA    . ARG A 1 3620 ? 138.945 153.021 189.342 1.00 53.96  ? 3620 ARG A CA    1 
ATOM   15638 C  C     . ARG A 1 3620 ? 137.765 152.439 190.113 1.00 53.44  ? 3620 ARG A C     1 
ATOM   15639 O  O     . ARG A 1 3620 ? 137.825 152.272 191.336 1.00 54.60  ? 3620 ARG A O     1 
ATOM   15640 C  CB    . ARG A 1 3620 ? 138.714 154.504 189.042 1.00 54.40  ? 3620 ARG A CB    1 
ATOM   15641 C  CG    . ARG A 1 3620 ? 139.990 155.307 188.878 1.00 49.63  ? 3620 ARG A CG    1 
ATOM   15642 C  CD    . ARG A 1 3620 ? 140.621 155.611 190.224 1.00 54.21  ? 3620 ARG A CD    1 
ATOM   15643 N  NE    . ARG A 1 3620 ? 139.656 156.159 191.170 1.00 57.01  ? 3620 ARG A NE    1 
ATOM   15644 C  CZ    . ARG A 1 3620 ? 139.754 157.358 191.729 1.00 58.74  ? 3620 ARG A CZ    1 
ATOM   15645 N  NH1   . ARG A 1 3620 ? 140.762 158.169 191.453 1.00 53.13  ? 3620 ARG A NH1   1 
ATOM   15646 N  NH2   . ARG A 1 3620 ? 138.817 157.752 192.586 1.00 53.89  ? 3620 ARG A NH2   1 
ATOM   15647 N  N     . LYS A 1 3621 ? 136.678 152.131 189.404 1.00 54.39  ? 3621 LYS A N     1 
ATOM   15648 C  CA    . LYS A 1 3621 ? 135.538 151.479 190.041 1.00 55.84  ? 3621 LYS A CA    1 
ATOM   15649 C  C     . LYS A 1 3621 ? 135.907 150.076 190.506 1.00 51.76  ? 3621 LYS A C     1 
ATOM   15650 O  O     . LYS A 1 3621 ? 135.536 149.652 191.606 1.00 52.55  ? 3621 LYS A O     1 
ATOM   15651 C  CB    . LYS A 1 3621 ? 134.352 151.436 189.075 1.00 58.04  ? 3621 LYS A CB    1 
ATOM   15652 C  CG    . LYS A 1 3621 ? 133.768 152.797 188.688 1.00 63.19  ? 3621 LYS A CG    1 
ATOM   15653 C  CD    . LYS A 1 3621 ? 133.842 153.819 189.819 1.00 64.59  ? 3621 LYS A CD    1 
ATOM   15654 C  CE    . LYS A 1 3621 ? 134.861 154.915 189.529 1.00 65.90  ? 3621 LYS A CE    1 
ATOM   15655 N  NZ    . LYS A 1 3621 ? 135.338 155.573 190.777 1.00 60.79  ? 3621 LYS A NZ    1 
ATOM   15656 N  N     . ASN A 1 3622 ? 136.641 149.339 189.669 1.00 52.06  ? 3622 ASN A N     1 
ATOM   15657 C  CA    . ASN A 1 3622 ? 137.034 147.977 190.014 1.00 51.67  ? 3622 ASN A CA    1 
ATOM   15658 C  C     . ASN A 1 3622 ? 137.964 147.963 191.221 1.00 48.38  ? 3622 ASN A C     1 
ATOM   15659 O  O     . ASN A 1 3622 ? 137.839 147.112 192.109 1.00 47.07  ? 3622 ASN A O     1 
ATOM   15660 C  CB    . ASN A 1 3622 ? 137.700 147.310 188.810 1.00 53.56  ? 3622 ASN A CB    1 
ATOM   15661 C  CG    . ASN A 1 3622 ? 136.722 146.508 187.979 1.00 60.92  ? 3622 ASN A CG    1 
ATOM   15662 O  OD1   . ASN A 1 3622 ? 136.573 145.301 188.168 1.00 61.57  ? 3622 ASN A OD1   1 
ATOM   15663 N  ND2   . ASN A 1 3622 ? 136.062 147.170 187.041 1.00 61.47  ? 3622 ASN A ND2   1 
ATOM   15664 N  N     . LEU A 1 3623 ? 138.917 148.897 191.263 1.00 46.88  ? 3623 LEU A N     1 
ATOM   15665 C  CA    . LEU A 1 3623 ? 139.785 149.017 192.430 1.00 46.68  ? 3623 LEU A CA    1 
ATOM   15666 C  C     . LEU A 1 3623 ? 138.987 149.422 193.664 1.00 48.85  ? 3623 LEU A C     1 
ATOM   15667 O  O     . LEU A 1 3623 ? 139.226 148.909 194.763 1.00 47.19  ? 3623 LEU A O     1 
ATOM   15668 C  CB    . LEU A 1 3623 ? 140.900 150.026 192.152 1.00 47.88  ? 3623 LEU A CB    1 
ATOM   15669 C  CG    . LEU A 1 3623 ? 141.706 150.536 193.349 1.00 45.07  ? 3623 LEU A CG    1 
ATOM   15670 C  CD1   . LEU A 1 3623 ? 142.485 149.404 193.999 1.00 43.47  ? 3623 LEU A CD1   1 
ATOM   15671 C  CD2   . LEU A 1 3623 ? 142.635 151.662 192.928 1.00 38.30  ? 3623 LEU A CD2   1 
ATOM   15672 N  N     . GLU A 1 3624 ? 138.032 150.340 193.497 1.00 51.51  ? 3624 GLU A N     1 
ATOM   15673 C  CA    . GLU A 1 3624 ? 137.199 150.766 194.616 1.00 50.67  ? 3624 GLU A CA    1 
ATOM   15674 C  C     . GLU A 1 3624 ? 136.396 149.603 195.183 1.00 51.76  ? 3624 GLU A C     1 
ATOM   15675 O  O     . GLU A 1 3624 ? 136.259 149.471 196.405 1.00 49.39  ? 3624 GLU A O     1 
ATOM   15676 C  CB    . GLU A 1 3624 ? 136.269 151.896 194.172 1.00 56.78  ? 3624 GLU A CB    1 
ATOM   15677 C  CG    . GLU A 1 3624 ? 135.349 152.417 195.259 1.00 64.94  ? 3624 GLU A CG    1 
ATOM   15678 C  CD    . GLU A 1 3624 ? 134.077 153.023 194.704 1.00 73.67  ? 3624 GLU A CD    1 
ATOM   15679 O  OE1   . GLU A 1 3624 ? 133.941 153.090 193.464 1.00 67.55  ? 3624 GLU A OE1   1 
ATOM   15680 O  OE2   . GLU A 1 3624 ? 133.214 153.435 195.507 1.00 75.31  ? 3624 GLU A OE2   1 
ATOM   15681 N  N     . SER A 1 3625 ? 135.849 148.754 194.311 1.00 52.39  ? 3625 SER A N     1 
ATOM   15682 C  CA    . SER A 1 3625 ? 135.113 147.583 194.775 1.00 48.36  ? 3625 SER A CA    1 
ATOM   15683 C  C     . SER A 1 3625 ? 136.023 146.632 195.544 1.00 50.00  ? 3625 SER A C     1 
ATOM   15684 O  O     . SER A 1 3625 ? 135.641 146.100 196.592 1.00 50.96  ? 3625 SER A O     1 
ATOM   15685 C  CB    . SER A 1 3625 ? 134.464 146.870 193.588 1.00 50.76  ? 3625 SER A CB    1 
ATOM   15686 O  OG    . SER A 1 3625 ? 134.039 147.800 192.608 1.00 59.27  ? 3625 SER A OG    1 
ATOM   15687 N  N     . ALA A 1 3626 ? 137.234 146.404 195.030 1.00 52.12  ? 3626 ALA A N     1 
ATOM   15688 C  CA    . ALA A 1 3626 ? 138.173 145.516 195.708 1.00 48.86  ? 3626 ALA A CA    1 
ATOM   15689 C  C     . ALA A 1 3626 ? 138.597 146.068 197.062 1.00 46.48  ? 3626 ALA A C     1 
ATOM   15690 O  O     . ALA A 1 3626 ? 138.675 145.317 198.041 1.00 45.97  ? 3626 ALA A O     1 
ATOM   15691 C  CB    . ALA A 1 3626 ? 139.397 145.274 194.825 1.00 43.59  ? 3626 ALA A CB    1 
ATOM   15692 N  N     . LEU A 1 3627 ? 138.875 147.372 197.140 1.00 44.54  ? 3627 LEU A N     1 
ATOM   15693 C  CA    . LEU A 1 3627 ? 139.252 147.993 198.404 1.00 41.54  ? 3627 LEU A CA    1 
ATOM   15694 C  C     . LEU A 1 3627 ? 138.140 147.935 199.441 1.00 53.98  ? 3627 LEU A C     1 
ATOM   15695 O  O     . LEU A 1 3627 ? 138.431 147.932 200.642 1.00 54.28  ? 3627 LEU A O     1 
ATOM   15696 C  CB    . LEU A 1 3627 ? 139.657 149.452 198.177 1.00 42.74  ? 3627 LEU A CB    1 
ATOM   15697 C  CG    . LEU A 1 3627 ? 140.926 149.724 197.367 1.00 46.10  ? 3627 LEU A CG    1 
ATOM   15698 C  CD1   . LEU A 1 3627 ? 141.123 151.218 197.173 1.00 50.46  ? 3627 LEU A CD1   1 
ATOM   15699 C  CD2   . LEU A 1 3627 ? 142.137 149.108 198.040 1.00 41.56  ? 3627 LEU A CD2   1 
ATOM   15700 N  N     . ARG A 1 3628 ? 136.881 147.888 199.009 1.00 57.45  ? 3628 ARG A N     1 
ATOM   15701 C  CA    . ARG A 1 3628 ? 135.736 147.887 199.912 1.00 52.19  ? 3628 ARG A CA    1 
ATOM   15702 C  C     . ARG A 1 3628 ? 135.321 146.483 200.333 1.00 48.51  ? 3628 ARG A C     1 
ATOM   15703 O  O     . ARG A 1 3628 ? 135.150 146.219 201.526 1.00 45.35  ? 3628 ARG A O     1 
ATOM   15704 C  CB    . ARG A 1 3628 ? 134.554 148.605 199.251 1.00 51.40  ? 3628 ARG A CB    1 
ATOM   15705 C  CG    . ARG A 1 3628 ? 134.466 150.084 199.582 1.00 54.74  ? 3628 ARG A CG    1 
ATOM   15706 C  CD    . ARG A 1 3628 ? 133.347 150.762 198.804 1.00 61.33  ? 3628 ARG A CD    1 
ATOM   15707 N  NE    . ARG A 1 3628 ? 133.519 152.209 198.736 1.00 68.19  ? 3628 ARG A NE    1 
ATOM   15708 C  CZ    . ARG A 1 3628 ? 133.381 153.034 199.766 1.00 67.97  ? 3628 ARG A CZ    1 
ATOM   15709 N  NH1   . ARG A 1 3628 ? 133.044 152.593 200.967 1.00 59.08  ? 3628 ARG A NH1   1 
ATOM   15710 N  NH2   . ARG A 1 3628 ? 133.580 154.336 199.584 1.00 69.90  ? 3628 ARG A NH2   1 
ATOM   15711 N  N     . PHE A 1 3629 ? 135.152 145.574 199.374 1.00 46.58  ? 3629 PHE A N     1 
ATOM   15712 C  CA    . PHE A 1 3629 ? 134.687 144.225 199.665 1.00 51.59  ? 3629 PHE A CA    1 
ATOM   15713 C  C     . PHE A 1 3629 ? 135.819 143.244 199.943 1.00 52.72  ? 3629 PHE A C     1 
ATOM   15714 O  O     . PHE A 1 3629 ? 135.546 142.105 200.335 1.00 54.28  ? 3629 PHE A O     1 
ATOM   15715 C  CB    . PHE A 1 3629 ? 133.828 143.703 198.507 1.00 57.45  ? 3629 PHE A CB    1 
ATOM   15716 C  CG    . PHE A 1 3629 ? 132.795 144.683 198.022 1.00 61.84  ? 3629 PHE A CG    1 
ATOM   15717 C  CD1   . PHE A 1 3629 ? 132.093 145.475 198.916 1.00 53.89  ? 3629 PHE A CD1   1 
ATOM   15718 C  CD2   . PHE A 1 3629 ? 132.529 144.813 196.669 1.00 59.79  ? 3629 PHE A CD2   1 
ATOM   15719 C  CE1   . PHE A 1 3629 ? 131.146 146.377 198.470 1.00 53.11  ? 3629 PHE A CE1   1 
ATOM   15720 C  CE2   . PHE A 1 3629 ? 131.582 145.712 196.217 1.00 54.27  ? 3629 PHE A CE2   1 
ATOM   15721 C  CZ    . PHE A 1 3629 ? 130.890 146.495 197.119 1.00 54.84  ? 3629 PHE A CZ    1 
ATOM   15722 N  N     . GLY A 1 3630 ? 137.073 143.651 199.753 1.00 53.33  ? 3630 GLY A N     1 
ATOM   15723 C  CA    . GLY A 1 3630 ? 138.198 142.803 200.093 1.00 48.74  ? 3630 GLY A CA    1 
ATOM   15724 C  C     . GLY A 1 3630 ? 138.497 141.681 199.127 1.00 46.77  ? 3630 GLY A C     1 
ATOM   15725 O  O     . GLY A 1 3630 ? 139.187 140.728 199.502 1.00 49.44  ? 3630 GLY A O     1 
ATOM   15726 N  N     . ASN A 1 3631 ? 138.000 141.753 197.895 1.00 48.23  ? 3631 ASN A N     1 
ATOM   15727 C  CA    . ASN A 1 3631 ? 138.312 140.708 196.935 1.00 48.00  ? 3631 ASN A CA    1 
ATOM   15728 C  C     . ASN A 1 3631 ? 139.696 140.926 196.324 1.00 47.17  ? 3631 ASN A C     1 
ATOM   15729 O  O     . ASN A 1 3631 ? 140.155 142.065 196.198 1.00 45.86  ? 3631 ASN A O     1 
ATOM   15730 C  CB    . ASN A 1 3631 ? 137.265 140.666 195.827 1.00 44.50  ? 3631 ASN A CB    1 
ATOM   15731 C  CG    . ASN A 1 3631 ? 135.861 140.492 196.362 1.00 51.87  ? 3631 ASN A CG    1 
ATOM   15732 O  OD1   . ASN A 1 3631 ? 135.318 141.382 197.012 1.00 56.00  ? 3631 ASN A OD1   1 
ATOM   15733 N  ND2   . ASN A 1 3631 ? 135.263 139.338 196.089 1.00 50.23  ? 3631 ASN A ND2   1 
ATOM   15734 N  N     . PRO A 1 3632 ? 140.382 139.847 195.950 1.00 41.54  ? 3632 PRO A N     1 
ATOM   15735 C  CA    . PRO A 1 3632 ? 141.665 139.997 195.254 1.00 33.80  ? 3632 PRO A CA    1 
ATOM   15736 C  C     . PRO A 1 3632 ? 141.486 140.664 193.899 1.00 34.03  ? 3632 PRO A C     1 
ATOM   15737 O  O     . PRO A 1 3632 ? 140.461 140.508 193.233 1.00 40.25  ? 3632 PRO A O     1 
ATOM   15738 C  CB    . PRO A 1 3632 ? 142.164 138.554 195.106 1.00 38.31  ? 3632 PRO A CB    1 
ATOM   15739 C  CG    . PRO A 1 3632 ? 140.956 137.697 195.308 1.00 46.38  ? 3632 PRO A CG    1 
ATOM   15740 C  CD    . PRO A 1 3632 ? 140.083 138.441 196.263 1.00 45.87  ? 3632 PRO A CD    1 
ATOM   15741 N  N     . LEU A 1 3633 ? 142.507 141.414 193.495 1.00 29.59  ? 3633 LEU A N     1 
ATOM   15742 C  CA    . LEU A 1 3633 ? 142.490 142.141 192.236 1.00 27.86  ? 3633 LEU A CA    1 
ATOM   15743 C  C     . LEU A 1 3633 ? 143.805 141.931 191.500 1.00 30.42  ? 3633 LEU A C     1 
ATOM   15744 O  O     . LEU A 1 3633 ? 144.879 141.903 192.107 1.00 30.41  ? 3633 LEU A O     1 
ATOM   15745 C  CB    . LEU A 1 3633 ? 142.247 143.640 192.463 1.00 29.10  ? 3633 LEU A CB    1 
ATOM   15746 C  CG    . LEU A 1 3633 ? 142.054 144.516 191.225 1.00 30.62  ? 3633 LEU A CG    1 
ATOM   15747 C  CD1   . LEU A 1 3633 ? 140.712 144.233 190.575 1.00 33.21  ? 3633 LEU A CD1   1 
ATOM   15748 C  CD2   . LEU A 1 3633 ? 142.172 145.985 191.593 1.00 31.33  ? 3633 LEU A CD2   1 
ATOM   15749 N  N     . LEU A 1 3634 ? 143.708 141.779 190.180 1.00 29.50  ? 3634 LEU A N     1 
ATOM   15750 C  CA    . LEU A 1 3634 ? 144.873 141.666 189.308 1.00 21.02  ? 3634 LEU A CA    1 
ATOM   15751 C  C     . LEU A 1 3634 ? 144.766 142.745 188.240 1.00 27.68  ? 3634 LEU A C     1 
ATOM   15752 O  O     . LEU A 1 3634 ? 143.785 142.785 187.490 1.00 39.03  ? 3634 LEU A O     1 
ATOM   15753 C  CB    . LEU A 1 3634 ? 144.965 140.276 188.677 1.00 24.87  ? 3634 LEU A CB    1 
ATOM   15754 C  CG    . LEU A 1 3634 ? 145.953 140.125 187.519 1.00 25.77  ? 3634 LEU A CG    1 
ATOM   15755 C  CD1   . LEU A 1 3634 ? 147.387 140.190 188.020 1.00 19.98  ? 3634 LEU A CD1   1 
ATOM   15756 C  CD2   . LEU A 1 3634 ? 145.704 138.828 186.766 1.00 31.13  ? 3634 LEU A CD2   1 
ATOM   15757 N  N     . VAL A 1 3635 ? 145.770 143.615 188.171 1.00 23.64  ? 3635 VAL A N     1 
ATOM   15758 C  CA    . VAL A 1 3635 ? 145.796 144.728 187.230 1.00 24.09  ? 3635 VAL A CA    1 
ATOM   15759 C  C     . VAL A 1 3635 ? 146.984 144.537 186.300 1.00 23.65  ? 3635 VAL A C     1 
ATOM   15760 O  O     . VAL A 1 3635 ? 148.118 144.363 186.760 1.00 24.26  ? 3635 VAL A O     1 
ATOM   15761 C  CB    . VAL A 1 3635 ? 145.886 146.082 187.956 1.00 24.49  ? 3635 VAL A CB    1 
ATOM   15762 C  CG1   . VAL A 1 3635 ? 145.821 147.229 186.959 1.00 28.61  ? 3635 VAL A CG1   1 
ATOM   15763 C  CG2   . VAL A 1 3635 ? 144.792 146.206 189.003 1.00 29.26  ? 3635 VAL A CG2   1 
ATOM   15764 N  N     . GLN A 1 3636 ? 146.726 144.572 184.997 1.00 27.12  ? 3636 GLN A N     1 
ATOM   15765 C  CA    . GLN A 1 3636 ? 147.773 144.451 183.999 1.00 27.08  ? 3636 GLN A CA    1 
ATOM   15766 C  C     . GLN A 1 3636 ? 148.124 145.827 183.441 1.00 31.48  ? 3636 GLN A C     1 
ATOM   15767 O  O     . GLN A 1 3636 ? 147.553 146.851 183.825 1.00 28.68  ? 3636 GLN A O     1 
ATOM   15768 C  CB    . GLN A 1 3636 ? 147.354 143.500 182.877 1.00 30.09  ? 3636 GLN A CB    1 
ATOM   15769 C  CG    . GLN A 1 3636 ? 146.576 142.280 183.326 1.00 33.26  ? 3636 GLN A CG    1 
ATOM   15770 C  CD    . GLN A 1 3636 ? 145.870 141.600 182.171 1.00 38.58  ? 3636 GLN A CD    1 
ATOM   15771 O  OE1   . GLN A 1 3636 ? 145.892 142.088 181.041 1.00 34.99  ? 3636 GLN A OE1   1 
ATOM   15772 N  NE2   . GLN A 1 3636 ? 145.256 140.457 182.445 1.00 40.78  ? 3636 GLN A NE2   1 
ATOM   15773 N  N     . ASP A 1 3637 ? 149.090 145.838 182.521 1.00 34.15  ? 3637 ASP A N     1 
ATOM   15774 C  CA    . ASP A 1 3637 ? 149.557 147.056 181.860 1.00 39.98  ? 3637 ASP A CA    1 
ATOM   15775 C  C     . ASP A 1 3637 ? 150.119 148.049 182.878 1.00 40.30  ? 3637 ASP A C     1 
ATOM   15776 O  O     . ASP A 1 3637 ? 149.726 149.215 182.930 1.00 46.30  ? 3637 ASP A O     1 
ATOM   15777 C  CB    . ASP A 1 3637 ? 148.445 147.690 181.020 1.00 42.48  ? 3637 ASP A CB    1 
ATOM   15778 C  CG    . ASP A 1 3637 ? 148.060 146.838 179.827 1.00 46.57  ? 3637 ASP A CG    1 
ATOM   15779 O  OD1   . ASP A 1 3637 ? 148.927 146.586 178.966 1.00 50.52  ? 3637 ASP A OD1   1 
ATOM   15780 O  OD2   . ASP A 1 3637 ? 146.885 146.424 179.747 1.00 45.35  ? 3637 ASP A OD2   1 
ATOM   15781 N  N     . VAL A 1 3638 ? 151.066 147.569 183.690 1.00 34.32  ? 3638 VAL A N     1 
ATOM   15782 C  CA    . VAL A 1 3638 ? 151.676 148.409 184.713 1.00 33.67  ? 3638 VAL A CA    1 
ATOM   15783 C  C     . VAL A 1 3638 ? 152.699 149.366 184.106 1.00 34.18  ? 3638 VAL A C     1 
ATOM   15784 O  O     . VAL A 1 3638 ? 153.076 150.355 184.744 1.00 38.61  ? 3638 VAL A O     1 
ATOM   15785 C  CB    . VAL A 1 3638 ? 152.293 147.511 185.804 1.00 29.81  ? 3638 VAL A CB    1 
ATOM   15786 C  CG1   . VAL A 1 3638 ? 153.212 146.476 185.182 1.00 27.50  ? 3638 VAL A CG1   1 
ATOM   15787 C  CG2   . VAL A 1 3638 ? 152.991 148.329 186.897 1.00 26.30  ? 3638 VAL A CG2   1 
ATOM   15788 N  N     . GLU A 1 3639 ? 153.141 149.120 182.869 1.00 34.22  ? 3639 GLU A N     1 
ATOM   15789 C  CA    . GLU A 1 3639 ? 153.922 150.130 182.163 1.00 34.79  ? 3639 GLU A CA    1 
ATOM   15790 C  C     . GLU A 1 3639 ? 153.123 151.409 181.958 1.00 36.68  ? 3639 GLU A C     1 
ATOM   15791 O  O     . GLU A 1 3639 ? 153.711 152.459 181.677 1.00 38.00  ? 3639 GLU A O     1 
ATOM   15792 C  CB    . GLU A 1 3639 ? 154.427 149.614 180.805 1.00 34.78  ? 3639 GLU A CB    1 
ATOM   15793 C  CG    . GLU A 1 3639 ? 153.400 149.000 179.836 1.00 38.28  ? 3639 GLU A CG    1 
ATOM   15794 C  CD    . GLU A 1 3639 ? 152.804 147.670 180.291 1.00 47.81  ? 3639 GLU A CD    1 
ATOM   15795 O  OE1   . GLU A 1 3639 ? 152.478 146.843 179.414 1.00 49.67  ? 3639 GLU A OE1   1 
ATOM   15796 O  OE2   . GLU A 1 3639 ? 152.695 147.423 181.508 1.00 46.75  ? 3639 GLU A OE2   1 
ATOM   15797 N  N     . SER A 1 3640 ? 151.800 151.337 182.083 1.00 33.86  ? 3640 SER A N     1 
ATOM   15798 C  CA    . SER A 1 3640 ? 150.919 152.497 182.126 1.00 36.02  ? 3640 SER A CA    1 
ATOM   15799 C  C     . SER A 1 3640 ? 150.353 152.685 183.532 1.00 40.70  ? 3640 SER A C     1 
ATOM   15800 O  O     . SER A 1 3640 ? 149.167 152.969 183.711 1.00 39.45  ? 3640 SER A O     1 
ATOM   15801 C  CB    . SER A 1 3640 ? 149.793 152.362 181.106 1.00 38.78  ? 3640 SER A CB    1 
ATOM   15802 O  OG    . SER A 1 3640 ? 150.308 152.232 179.794 1.00 38.00  ? 3640 SER A OG    1 
ATOM   15803 N  N     . TYR A 1 3641 ? 151.205 152.497 184.540 1.00 37.11  ? 3641 TYR A N     1 
ATOM   15804 C  CA    . TYR A 1 3641 ? 150.774 152.524 185.933 1.00 33.04  ? 3641 TYR A CA    1 
ATOM   15805 C  C     . TYR A 1 3641 ? 150.088 153.842 186.265 1.00 33.85  ? 3641 TYR A C     1 
ATOM   15806 O  O     . TYR A 1 3641 ? 150.560 154.918 185.889 1.00 36.46  ? 3641 TYR A O     1 
ATOM   15807 C  CB    . TYR A 1 3641 ? 151.978 152.306 186.849 1.00 30.07  ? 3641 TYR A CB    1 
ATOM   15808 C  CG    . TYR A 1 3641 ? 151.755 152.660 188.299 1.00 28.05  ? 3641 TYR A CG    1 
ATOM   15809 C  CD1   . TYR A 1 3641 ? 151.053 151.809 189.141 1.00 28.17  ? 3641 TYR A CD1   1 
ATOM   15810 C  CD2   . TYR A 1 3641 ? 152.263 153.836 188.831 1.00 24.43  ? 3641 TYR A CD2   1 
ATOM   15811 C  CE1   . TYR A 1 3641 ? 150.854 152.125 190.470 1.00 29.35  ? 3641 TYR A CE1   1 
ATOM   15812 C  CE2   . TYR A 1 3641 ? 152.068 154.161 190.158 1.00 27.48  ? 3641 TYR A CE2   1 
ATOM   15813 C  CZ    . TYR A 1 3641 ? 151.364 153.302 190.972 1.00 29.43  ? 3641 TYR A CZ    1 
ATOM   15814 O  OH    . TYR A 1 3641 ? 151.169 153.621 192.294 1.00 30.87  ? 3641 TYR A OH    1 
ATOM   15815 N  N     . ASP A 1 3642 ? 148.965 153.748 186.976 1.00 33.72  ? 3642 ASP A N     1 
ATOM   15816 C  CA    . ASP A 1 3642 ? 148.164 154.912 187.308 1.00 34.53  ? 3642 ASP A CA    1 
ATOM   15817 C  C     . ASP A 1 3642 ? 148.396 155.280 188.765 1.00 38.11  ? 3642 ASP A C     1 
ATOM   15818 O  O     . ASP A 1 3642 ? 148.184 154.436 189.650 1.00 36.77  ? 3642 ASP A O     1 
ATOM   15819 C  CB    . ASP A 1 3642 ? 146.689 154.630 187.043 1.00 38.02  ? 3642 ASP A CB    1 
ATOM   15820 C  CG    . ASP A 1 3642 ? 145.772 155.572 187.775 1.00 44.68  ? 3642 ASP A CG    1 
ATOM   15821 O  OD1   . ASP A 1 3642 ? 145.475 155.301 188.951 1.00 42.25  ? 3642 ASP A OD1   1 
ATOM   15822 O  OD2   . ASP A 1 3642 ? 145.344 156.579 187.174 1.00 47.04  ? 3642 ASP A OD2   1 
ATOM   15823 N  N     . PRO A 1 3643 ? 148.824 156.511 189.060 1.00 36.68  ? 3643 PRO A N     1 
ATOM   15824 C  CA    . PRO A 1 3643 ? 149.395 156.804 190.386 1.00 33.35  ? 3643 PRO A CA    1 
ATOM   15825 C  C     . PRO A 1 3643 ? 148.393 156.874 191.532 1.00 35.39  ? 3643 PRO A C     1 
ATOM   15826 O  O     . PRO A 1 3643 ? 148.818 157.147 192.662 1.00 34.69  ? 3643 PRO A O     1 
ATOM   15827 C  CB    . PRO A 1 3643 ? 150.076 158.165 190.180 1.00 37.96  ? 3643 PRO A CB    1 
ATOM   15828 C  CG    . PRO A 1 3643 ? 150.255 158.295 188.699 1.00 39.11  ? 3643 PRO A CG    1 
ATOM   15829 C  CD    . PRO A 1 3643 ? 149.078 157.595 188.099 1.00 41.09  ? 3643 PRO A CD    1 
ATOM   15830 N  N     . VAL A 1 3644 ? 147.096 156.648 191.305 1.00 37.59  ? 3644 VAL A N     1 
ATOM   15831 C  CA    . VAL A 1 3644 ? 146.160 156.713 192.426 1.00 38.90  ? 3644 VAL A CA    1 
ATOM   15832 C  C     . VAL A 1 3644 ? 146.339 155.523 193.357 1.00 39.12  ? 3644 VAL A C     1 
ATOM   15833 O  O     . VAL A 1 3644 ? 145.776 155.506 194.456 1.00 43.31  ? 3644 VAL A O     1 
ATOM   15834 C  CB    . VAL A 1 3644 ? 144.695 156.803 191.945 1.00 40.84  ? 3644 VAL A CB    1 
ATOM   15835 C  CG1   . VAL A 1 3644 ? 144.566 157.768 190.772 1.00 43.74  ? 3644 VAL A CG1   1 
ATOM   15836 C  CG2   . VAL A 1 3644 ? 144.136 155.424 191.627 1.00 37.70  ? 3644 VAL A CG2   1 
ATOM   15837 N  N     . LEU A 1 3645 ? 147.116 154.525 192.941 1.00 34.55  ? 3645 LEU A N     1 
ATOM   15838 C  CA    . LEU A 1 3645 ? 147.399 153.351 193.753 1.00 30.45  ? 3645 LEU A CA    1 
ATOM   15839 C  C     . LEU A 1 3645 ? 148.530 153.576 194.748 1.00 27.67  ? 3645 LEU A C     1 
ATOM   15840 O  O     . LEU A 1 3645 ? 148.845 152.661 195.516 1.00 28.77  ? 3645 LEU A O     1 
ATOM   15841 C  CB    . LEU A 1 3645 ? 147.745 152.165 192.849 1.00 30.83  ? 3645 LEU A CB    1 
ATOM   15842 C  CG    . LEU A 1 3645 ? 146.620 151.192 192.495 1.00 31.48  ? 3645 LEU A CG    1 
ATOM   15843 C  CD1   . LEU A 1 3645 ? 147.123 150.140 191.522 1.00 35.45  ? 3645 LEU A CD1   1 
ATOM   15844 C  CD2   . LEU A 1 3645 ? 146.054 150.542 193.743 1.00 28.48  ? 3645 LEU A CD2   1 
ATOM   15845 N  N     . ASN A 1 3646 ? 149.151 154.757 194.742 1.00 27.19  ? 3646 ASN A N     1 
ATOM   15846 C  CA    . ASN A 1 3646 ? 150.280 155.012 195.635 1.00 29.83  ? 3646 ASN A CA    1 
ATOM   15847 C  C     . ASN A 1 3646 ? 149.928 154.835 197.107 1.00 33.02  ? 3646 ASN A C     1 
ATOM   15848 O  O     . ASN A 1 3646 ? 150.683 154.147 197.816 1.00 32.19  ? 3646 ASN A O     1 
ATOM   15849 C  CB    . ASN A 1 3646 ? 150.851 156.407 195.357 1.00 30.94  ? 3646 ASN A CB    1 
ATOM   15850 C  CG    . ASN A 1 3646 ? 151.650 156.465 194.071 1.00 32.10  ? 3646 ASN A CG    1 
ATOM   15851 O  OD1   . ASN A 1 3646 ? 151.775 155.469 193.360 1.00 29.08  ? 3646 ASN A OD1   1 
ATOM   15852 N  ND2   . ASN A 1 3646 ? 152.197 157.636 193.766 1.00 32.86  ? 3646 ASN A ND2   1 
ATOM   15853 N  N     . PRO A 1 3647 ? 148.842 155.411 197.638 1.00 35.51  ? 3647 PRO A N     1 
ATOM   15854 C  CA    . PRO A 1 3647 ? 148.489 155.112 199.036 1.00 32.29  ? 3647 PRO A CA    1 
ATOM   15855 C  C     . PRO A 1 3647 ? 148.183 153.646 199.279 1.00 29.68  ? 3647 PRO A C     1 
ATOM   15856 O  O     . PRO A 1 3647 ? 148.467 153.134 200.369 1.00 32.72  ? 3647 PRO A O     1 
ATOM   15857 C  CB    . PRO A 1 3647 ? 147.259 155.998 199.283 1.00 36.58  ? 3647 PRO A CB    1 
ATOM   15858 C  CG    . PRO A 1 3647 ? 146.698 156.243 197.928 1.00 32.38  ? 3647 PRO A CG    1 
ATOM   15859 C  CD    . PRO A 1 3647 ? 147.899 156.380 197.050 1.00 31.38  ? 3647 PRO A CD    1 
ATOM   15860 N  N     . VAL A 1 3648 ? 147.610 152.954 198.293 1.00 31.71  ? 3648 VAL A N     1 
ATOM   15861 C  CA    . VAL A 1 3648 ? 147.256 151.549 198.472 1.00 29.61  ? 3648 VAL A CA    1 
ATOM   15862 C  C     . VAL A 1 3648 ? 148.510 150.689 198.571 1.00 30.23  ? 3648 VAL A C     1 
ATOM   15863 O  O     . VAL A 1 3648 ? 148.627 149.831 199.454 1.00 29.98  ? 3648 VAL A O     1 
ATOM   15864 C  CB    . VAL A 1 3648 ? 146.339 151.081 197.328 1.00 29.60  ? 3648 VAL A CB    1 
ATOM   15865 C  CG1   . VAL A 1 3648 ? 145.916 149.641 197.544 1.00 31.36  ? 3648 VAL A CG1   1 
ATOM   15866 C  CG2   . VAL A 1 3648 ? 145.125 151.990 197.214 1.00 36.78  ? 3648 VAL A CG2   1 
ATOM   15867 N  N     . LEU A 1 3649 ? 149.466 150.902 197.663 1.00 29.36  ? 3649 LEU A N     1 
ATOM   15868 C  CA    . LEU A 1 3649 ? 150.698 150.121 197.689 1.00 28.11  ? 3649 LEU A CA    1 
ATOM   15869 C  C     . LEU A 1 3649 ? 151.533 150.444 198.920 1.00 27.75  ? 3649 LEU A C     1 
ATOM   15870 O  O     . LEU A 1 3649 ? 152.121 149.545 199.533 1.00 30.86  ? 3649 LEU A O     1 
ATOM   15871 C  CB    . LEU A 1 3649 ? 151.502 150.364 196.413 1.00 27.14  ? 3649 LEU A CB    1 
ATOM   15872 C  CG    . LEU A 1 3649 ? 150.852 149.890 195.113 1.00 23.59  ? 3649 LEU A CG    1 
ATOM   15873 C  CD1   . LEU A 1 3649 ? 151.802 150.073 193.941 1.00 24.07  ? 3649 LEU A CD1   1 
ATOM   15874 C  CD2   . LEU A 1 3649 ? 150.416 148.440 195.231 1.00 29.37  ? 3649 LEU A CD2   1 
ATOM   15875 N  N     . ASN A 1 3650 ? 151.600 151.721 199.299 1.00 31.41  ? 3650 ASN A N     1 
ATOM   15876 C  CA    . ASN A 1 3650 ? 152.325 152.116 200.499 1.00 30.48  ? 3650 ASN A CA    1 
ATOM   15877 C  C     . ASN A 1 3650 ? 151.617 151.693 201.778 1.00 29.87  ? 3650 ASN A C     1 
ATOM   15878 O  O     . ASN A 1 3650 ? 152.209 151.811 202.857 1.00 30.75  ? 3650 ASN A O     1 
ATOM   15879 C  CB    . ASN A 1 3650 ? 152.541 153.630 200.511 1.00 27.88  ? 3650 ASN A CB    1 
ATOM   15880 C  CG    . ASN A 1 3650 ? 153.754 154.052 199.709 1.00 30.90  ? 3650 ASN A CG    1 
ATOM   15881 O  OD1   . ASN A 1 3650 ? 154.782 153.375 199.712 1.00 38.13  ? 3650 ASN A OD1   1 
ATOM   15882 N  ND2   . ASN A 1 3650 ? 153.642 155.180 199.018 1.00 31.26  ? 3650 ASN A ND2   1 
ATOM   15883 N  N     . ARG A 1 3651 ? 150.376 151.210 201.681 1.00 30.43  ? 3651 ARG A N     1 
ATOM   15884 C  CA    . ARG A 1 3651 ? 149.584 150.801 202.842 1.00 30.33  ? 3651 ARG A CA    1 
ATOM   15885 C  C     . ARG A 1 3651 ? 149.448 151.943 203.845 1.00 33.48  ? 3651 ARG A C     1 
ATOM   15886 O  O     . ARG A 1 3651 ? 149.591 151.757 205.055 1.00 38.17  ? 3651 ARG A O     1 
ATOM   15887 C  CB    . ARG A 1 3651 ? 150.173 149.552 203.500 1.00 31.29  ? 3651 ARG A CB    1 
ATOM   15888 C  CG    . ARG A 1 3651 ? 149.578 148.256 202.974 1.00 32.26  ? 3651 ARG A CG    1 
ATOM   15889 C  CD    . ARG A 1 3651 ? 149.892 147.078 203.878 1.00 36.77  ? 3651 ARG A CD    1 
ATOM   15890 N  NE    . ARG A 1 3651 ? 149.820 145.814 203.155 1.00 36.28  ? 3651 ARG A NE    1 
ATOM   15891 C  CZ    . ARG A 1 3651 ? 150.768 145.355 202.351 1.00 37.13  ? 3651 ARG A CZ    1 
ATOM   15892 N  NH1   . ARG A 1 3651 ? 151.887 146.030 202.145 1.00 33.85  ? 3651 ARG A NH1   1 
ATOM   15893 N  NH2   . ARG A 1 3651 ? 150.589 144.189 201.737 1.00 33.94  ? 3651 ARG A NH2   1 
ATOM   15894 N  N     . GLU A 1 3652 ? 149.168 153.138 203.330 1.00 34.28  ? 3652 GLU A N     1 
ATOM   15895 C  CA    . GLU A 1 3652 ? 148.986 154.336 204.147 1.00 35.17  ? 3652 GLU A CA    1 
ATOM   15896 C  C     . GLU A 1 3652 ? 147.532 154.388 204.595 1.00 36.58  ? 3652 GLU A C     1 
ATOM   15897 O  O     . GLU A 1 3652 ? 146.664 154.934 203.912 1.00 44.74  ? 3652 GLU A O     1 
ATOM   15898 C  CB    . GLU A 1 3652 ? 149.377 155.582 203.362 1.00 35.32  ? 3652 GLU A CB    1 
ATOM   15899 C  CG    . GLU A 1 3652 ? 150.847 155.641 202.984 1.00 33.03  ? 3652 GLU A CG    1 
ATOM   15900 C  CD    . GLU A 1 3652 ? 151.143 156.721 201.962 1.00 44.46  ? 3652 GLU A CD    1 
ATOM   15901 O  OE1   . GLU A 1 3652 ? 150.193 157.402 201.522 1.00 39.65  ? 3652 GLU A OE1   1 
ATOM   15902 O  OE2   . GLU A 1 3652 ? 152.325 156.886 201.595 1.00 50.69  ? 3652 GLU A OE2   1 
ATOM   15903 N  N     . VAL A 1 3653 ? 147.261 153.814 205.765 1.00 41.34  ? 3653 VAL A N     1 
ATOM   15904 C  CA    . VAL A 1 3653 ? 145.905 153.703 206.282 1.00 46.18  ? 3653 VAL A CA    1 
ATOM   15905 C  C     . VAL A 1 3653 ? 145.823 154.403 207.632 1.00 49.01  ? 3653 VAL A C     1 
ATOM   15906 O  O     . VAL A 1 3653 ? 146.818 154.562 208.344 1.00 49.69  ? 3653 VAL A O     1 
ATOM   15907 C  CB    . VAL A 1 3653 ? 145.449 152.235 206.405 1.00 45.60  ? 3653 VAL A CB    1 
ATOM   15908 C  CG1   . VAL A 1 3653 ? 145.406 151.575 205.036 1.00 43.73  ? 3653 VAL A CG1   1 
ATOM   15909 C  CG2   . VAL A 1 3653 ? 146.369 151.470 207.343 1.00 43.65  ? 3653 VAL A CG2   1 
ATOM   15910 N  N     . ARG A 1 3654 ? 144.610 154.829 207.976 1.00 53.20  ? 3654 ARG A N     1 
ATOM   15911 C  CA    . ARG A 1 3654 ? 144.316 155.443 209.264 1.00 56.08  ? 3654 ARG A CA    1 
ATOM   15912 C  C     . ARG A 1 3654 ? 143.251 154.605 209.956 1.00 61.22  ? 3654 ARG A C     1 
ATOM   15913 O  O     . ARG A 1 3654 ? 142.142 154.452 209.434 1.00 66.24  ? 3654 ARG A O     1 
ATOM   15914 C  CB    . ARG A 1 3654 ? 143.847 156.891 209.095 1.00 58.76  ? 3654 ARG A CB    1 
ATOM   15915 C  CG    . ARG A 1 3654 ? 142.901 157.378 210.185 1.00 60.85  ? 3654 ARG A CG    1 
ATOM   15916 C  CD    . ARG A 1 3654 ? 142.229 158.687 209.801 1.00 62.96  ? 3654 ARG A CD    1 
ATOM   15917 N  NE    . ARG A 1 3654 ? 143.022 159.450 208.845 1.00 69.29  ? 3654 ARG A NE    1 
ATOM   15918 C  CZ    . ARG A 1 3654 ? 142.546 159.967 207.721 1.00 78.43  ? 3654 ARG A CZ    1 
ATOM   15919 N  NH1   . ARG A 1 3654 ? 141.278 159.818 207.374 1.00 76.29  ? 3654 ARG A NH1   1 
ATOM   15920 N  NH2   . ARG A 1 3654 ? 143.363 160.651 206.924 1.00 69.94  ? 3654 ARG A NH2   1 
ATOM   15921 N  N     . ARG A 1 3655 ? 143.593 154.054 211.118 1.00 60.91  ? 3655 ARG A N     1 
ATOM   15922 C  CA    . ARG A 1 3655 ? 142.685 153.207 211.888 1.00 63.98  ? 3655 ARG A CA    1 
ATOM   15923 C  C     . ARG A 1 3655 ? 142.047 154.059 212.979 1.00 70.43  ? 3655 ARG A C     1 
ATOM   15924 O  O     . ARG A 1 3655 ? 142.636 154.273 214.041 1.00 68.30  ? 3655 ARG A O     1 
ATOM   15925 C  CB    . ARG A 1 3655 ? 143.424 152.006 212.468 1.00 63.04  ? 3655 ARG A CB    1 
ATOM   15926 C  CG    . ARG A 1 3655 ? 143.890 151.006 211.423 1.00 68.15  ? 3655 ARG A CG    1 
ATOM   15927 C  CD    . ARG A 1 3655 ? 144.619 149.835 212.058 1.00 64.55  ? 3655 ARG A CD    1 
ATOM   15928 N  NE    . ARG A 1 3655 ? 145.043 148.854 211.066 1.00 66.78  ? 3655 ARG A NE    1 
ATOM   15929 C  CZ    . ARG A 1 3655 ? 146.213 148.872 210.443 1.00 67.89  ? 3655 ARG A CZ    1 
ATOM   15930 N  NH1   . ARG A 1 3655 ? 147.110 149.814 210.683 1.00 64.49  ? 3655 ARG A NH1   1 
ATOM   15931 N  NH2   . ARG A 1 3655 ? 146.491 147.919 209.557 1.00 72.75  ? 3655 ARG A NH2   1 
ATOM   15932 N  N     . THR A 1 3656 ? 140.836 154.545 212.712 1.00 76.12  ? 3656 THR A N     1 
ATOM   15933 C  CA    . THR A 1 3656 ? 140.108 155.400 213.640 1.00 79.22  ? 3656 THR A CA    1 
ATOM   15934 C  C     . THR A 1 3656 ? 138.710 154.841 213.851 1.00 80.81  ? 3656 THR A C     1 
ATOM   15935 O  O     . THR A 1 3656 ? 137.946 154.692 212.892 1.00 80.33  ? 3656 THR A O     1 
ATOM   15936 C  CB    . THR A 1 3656 ? 140.028 156.840 213.120 1.00 73.78  ? 3656 THR A CB    1 
ATOM   15937 O  OG1   . THR A 1 3656 ? 141.338 157.421 213.109 1.00 60.52  ? 3656 THR A OG1   1 
ATOM   15938 C  CG2   . THR A 1 3656 ? 139.114 157.678 214.002 1.00 67.90  ? 3656 THR A CG2   1 
ATOM   15939 N  N     . GLY A 1 3657 ? 138.379 154.538 215.103 1.00 81.69  ? 3657 GLY A N     1 
ATOM   15940 C  CA    . GLY A 1 3657 ? 137.048 154.055 215.438 1.00 80.01  ? 3657 GLY A CA    1 
ATOM   15941 C  C     . GLY A 1 3657 ? 136.680 152.738 214.792 1.00 82.35  ? 3657 GLY A C     1 
ATOM   15942 O  O     . GLY A 1 3657 ? 135.546 152.573 214.325 1.00 84.67  ? 3657 GLY A O     1 
ATOM   15943 N  N     . GLY A 1 3658 ? 137.616 151.792 214.752 1.00 81.29  ? 3658 GLY A N     1 
ATOM   15944 C  CA    . GLY A 1 3658 ? 137.348 150.503 214.148 1.00 79.36  ? 3658 GLY A CA    1 
ATOM   15945 C  C     . GLY A 1 3658 ? 137.261 150.509 212.640 1.00 85.12  ? 3658 GLY A C     1 
ATOM   15946 O  O     . GLY A 1 3658 ? 136.888 149.489 212.052 1.00 80.83  ? 3658 GLY A O     1 
ATOM   15947 N  N     . ARG A 1 3659 ? 137.593 151.624 211.995 1.00 85.34  ? 3659 ARG A N     1 
ATOM   15948 C  CA    . ARG A 1 3659 ? 137.530 151.755 210.547 1.00 75.95  ? 3659 ARG A CA    1 
ATOM   15949 C  C     . ARG A 1 3659 ? 138.939 151.921 209.997 1.00 75.89  ? 3659 ARG A C     1 
ATOM   15950 O  O     . ARG A 1 3659 ? 139.664 152.835 210.402 1.00 76.53  ? 3659 ARG A O     1 
ATOM   15951 C  CB    . ARG A 1 3659 ? 136.658 152.948 210.145 1.00 72.64  ? 3659 ARG A CB    1 
ATOM   15952 C  CG    . ARG A 1 3659 ? 135.166 152.715 210.322 1.00 73.84  ? 3659 ARG A CG    1 
ATOM   15953 C  CD    . ARG A 1 3659 ? 134.378 154.010 210.176 1.00 78.93  ? 3659 ARG A CD    1 
ATOM   15954 N  NE    . ARG A 1 3659 ? 134.632 154.685 208.908 1.00 80.00  ? 3659 ARG A NE    1 
ATOM   15955 C  CZ    . ARG A 1 3659 ? 134.111 155.856 208.568 1.00 78.22  ? 3659 ARG A CZ    1 
ATOM   15956 N  NH1   . ARG A 1 3659 ? 133.306 156.518 209.384 1.00 75.05  ? 3659 ARG A NH1   1 
ATOM   15957 N  NH2   . ARG A 1 3659 ? 134.407 156.379 207.382 1.00 74.11  ? 3659 ARG A NH2   1 
ATOM   15958 N  N     . VAL A 1 3660 ? 139.322 151.040 209.078 1.00 70.85  ? 3660 VAL A N     1 
ATOM   15959 C  CA    . VAL A 1 3660 ? 140.607 151.120 208.394 1.00 65.75  ? 3660 VAL A CA    1 
ATOM   15960 C  C     . VAL A 1 3660 ? 140.361 151.901 207.109 1.00 63.78  ? 3660 VAL A C     1 
ATOM   15961 O  O     . VAL A 1 3660 ? 139.927 151.342 206.098 1.00 69.11  ? 3660 VAL A O     1 
ATOM   15962 C  CB    . VAL A 1 3660 ? 141.194 149.733 208.118 1.00 59.60  ? 3660 VAL A CB    1 
ATOM   15963 C  CG1   . VAL A 1 3660 ? 142.484 149.849 207.319 1.00 59.81  ? 3660 VAL A CG1   1 
ATOM   15964 C  CG2   . VAL A 1 3660 ? 141.433 148.989 209.423 1.00 57.96  ? 3660 VAL A CG2   1 
ATOM   15965 N  N     . LEU A 1 3661 ? 140.634 153.201 207.144 1.00 60.41  ? 3661 LEU A N     1 
ATOM   15966 C  CA    . LEU A 1 3661 ? 140.321 154.089 206.035 1.00 64.52  ? 3661 LEU A CA    1 
ATOM   15967 C  C     . LEU A 1 3661 ? 141.570 154.388 205.218 1.00 62.06  ? 3661 LEU A C     1 
ATOM   15968 O  O     . LEU A 1 3661 ? 142.623 154.724 205.767 1.00 61.88  ? 3661 LEU A O     1 
ATOM   15969 C  CB    . LEU A 1 3661 ? 139.706 155.396 206.540 1.00 66.83  ? 3661 LEU A CB    1 
ATOM   15970 C  CG    . LEU A 1 3661 ? 138.498 155.248 207.466 1.00 70.61  ? 3661 LEU A CG    1 
ATOM   15971 C  CD1   . LEU A 1 3661 ? 138.251 156.534 208.242 1.00 69.35  ? 3661 LEU A CD1   1 
ATOM   15972 C  CD2   . LEU A 1 3661 ? 137.263 154.838 206.680 1.00 70.77  ? 3661 LEU A CD2   1 
ATOM   15973 N  N     . ILE A 1 3662 ? 141.442 154.261 203.900 1.00 58.35  ? 3662 ILE A N     1 
ATOM   15974 C  CA    . ILE A 1 3662 ? 142.505 154.593 202.962 1.00 50.17  ? 3662 ILE A CA    1 
ATOM   15975 C  C     . ILE A 1 3662 ? 141.958 155.601 201.961 1.00 53.80  ? 3662 ILE A C     1 
ATOM   15976 O  O     . ILE A 1 3662 ? 140.852 155.434 201.435 1.00 59.75  ? 3662 ILE A O     1 
ATOM   15977 C  CB    . ILE A 1 3662 ? 143.064 153.336 202.256 1.00 52.26  ? 3662 ILE A CB    1 
ATOM   15978 C  CG1   . ILE A 1 3662 ? 144.239 153.705 201.350 1.00 46.73  ? 3662 ILE A CG1   1 
ATOM   15979 C  CG2   . ILE A 1 3662 ? 141.972 152.592 201.492 1.00 57.36  ? 3662 ILE A CG2   1 
ATOM   15980 C  CD1   . ILE A 1 3662 ? 145.343 152.676 201.348 1.00 38.02  ? 3662 ILE A CD1   1 
ATOM   15981 N  N     . THR A 1 3663 ? 142.720 156.664 201.721 1.00 52.54  ? 3663 THR A N     1 
ATOM   15982 C  CA    . THR A 1 3663 ? 142.267 157.773 200.884 1.00 60.01  ? 3663 THR A CA    1 
ATOM   15983 C  C     . THR A 1 3663 ? 142.669 157.494 199.441 1.00 55.90  ? 3663 THR A C     1 
ATOM   15984 O  O     . THR A 1 3663 ? 143.784 157.810 199.020 1.00 53.31  ? 3663 THR A O     1 
ATOM   15985 C  CB    . THR A 1 3663 ? 142.846 159.094 201.378 1.00 62.34  ? 3663 THR A CB    1 
ATOM   15986 O  OG1   . THR A 1 3663 ? 142.486 159.291 202.751 1.00 61.67  ? 3663 THR A OG1   1 
ATOM   15987 C  CG2   . THR A 1 3663 ? 142.305 160.253 200.552 1.00 60.72  ? 3663 THR A CG2   1 
ATOM   15988 N  N     . LEU A 1 3664 ? 141.757 156.896 198.680 1.00 59.97  ? 3664 LEU A N     1 
ATOM   15989 C  CA    . LEU A 1 3664 ? 141.963 156.666 197.257 1.00 58.05  ? 3664 LEU A CA    1 
ATOM   15990 C  C     . LEU A 1 3664 ? 141.555 157.926 196.502 1.00 64.65  ? 3664 LEU A C     1 
ATOM   15991 O  O     . LEU A 1 3664 ? 140.379 158.307 196.508 1.00 66.83  ? 3664 LEU A O     1 
ATOM   15992 C  CB    . LEU A 1 3664 ? 141.163 155.452 196.783 1.00 57.64  ? 3664 LEU A CB    1 
ATOM   15993 C  CG    . LEU A 1 3664 ? 140.675 155.403 195.331 1.00 57.84  ? 3664 LEU A CG    1 
ATOM   15994 C  CD1   . LEU A 1 3664 ? 141.846 155.322 194.370 1.00 51.44  ? 3664 LEU A CD1   1 
ATOM   15995 C  CD2   . LEU A 1 3664 ? 139.730 154.233 195.119 1.00 55.65  ? 3664 LEU A CD2   1 
ATOM   15996 N  N     . GLY A 1 3665 ? 142.524 158.572 195.866 1.00 62.13  ? 3665 GLY A N     1 
ATOM   15997 C  CA    . GLY A 1 3665 ? 142.245 159.821 195.179 1.00 61.76  ? 3665 GLY A CA    1 
ATOM   15998 C  C     . GLY A 1 3665 ? 141.816 160.888 196.168 1.00 70.94  ? 3665 GLY A C     1 
ATOM   15999 O  O     . GLY A 1 3665 ? 142.524 161.197 197.133 1.00 70.14  ? 3665 GLY A O     1 
ATOM   16000 N  N     . ASP A 1 3666 ? 140.639 161.465 195.932 1.00 75.42  ? 3666 ASP A N     1 
ATOM   16001 C  CA    . ASP A 1 3666 ? 140.068 162.477 196.810 1.00 76.98  ? 3666 ASP A CA    1 
ATOM   16002 C  C     . ASP A 1 3666 ? 138.976 161.919 197.713 1.00 74.41  ? 3666 ASP A C     1 
ATOM   16003 O  O     . ASP A 1 3666 ? 138.318 162.688 198.423 1.00 73.76  ? 3666 ASP A O     1 
ATOM   16004 C  CB    . ASP A 1 3666 ? 139.519 163.641 195.982 1.00 85.17  ? 3666 ASP A CB    1 
ATOM   16005 C  CG    . ASP A 1 3666 ? 138.522 163.188 194.933 1.00 84.74  ? 3666 ASP A CG    1 
ATOM   16006 O  OD1   . ASP A 1 3666 ? 138.871 162.303 194.123 1.00 78.19  ? 3666 ASP A OD1   1 
ATOM   16007 O  OD2   . ASP A 1 3666 ? 137.390 163.717 194.917 1.00 87.41  ? 3666 ASP A OD2   1 
ATOM   16008 N  N     . GLN A 1 3667 ? 138.768 160.605 197.708 1.00 74.49  ? 3667 GLN A N     1 
ATOM   16009 C  CA    . GLN A 1 3667 ? 137.690 159.969 198.452 1.00 75.57  ? 3667 GLN A CA    1 
ATOM   16010 C  C     . GLN A 1 3667 ? 138.276 159.085 199.543 1.00 72.20  ? 3667 GLN A C     1 
ATOM   16011 O  O     . GLN A 1 3667 ? 139.305 158.434 199.334 1.00 71.94  ? 3667 GLN A O     1 
ATOM   16012 C  CB    . GLN A 1 3667 ? 136.796 159.146 197.517 1.00 76.75  ? 3667 GLN A CB    1 
ATOM   16013 C  CG    . GLN A 1 3667 ? 135.628 158.454 198.201 1.00 78.05  ? 3667 GLN A CG    1 
ATOM   16014 C  CD    . GLN A 1 3667 ? 135.023 157.356 197.348 1.00 85.11  ? 3667 GLN A CD    1 
ATOM   16015 O  OE1   . GLN A 1 3667 ? 135.542 157.024 196.282 1.00 88.69  ? 3667 GLN A OE1   1 
ATOM   16016 N  NE2   . GLN A 1 3667 ? 133.917 156.788 197.812 1.00 80.90  ? 3667 GLN A NE2   1 
ATOM   16017 N  N     . ASP A 1 3668 ? 137.622 159.067 200.702 1.00 68.88  ? 3668 ASP A N     1 
ATOM   16018 C  CA    . ASP A 1 3668 ? 138.032 158.229 201.822 1.00 67.70  ? 3668 ASP A CA    1 
ATOM   16019 C  C     . ASP A 1 3668 ? 137.252 156.920 201.769 1.00 69.79  ? 3668 ASP A C     1 
ATOM   16020 O  O     . ASP A 1 3668 ? 136.021 156.930 201.660 1.00 71.24  ? 3668 ASP A O     1 
ATOM   16021 C  CB    . ASP A 1 3668 ? 137.796 158.951 203.147 1.00 72.31  ? 3668 ASP A CB    1 
ATOM   16022 C  CG    . ASP A 1 3668 ? 138.483 158.272 204.313 1.00 75.54  ? 3668 ASP A CG    1 
ATOM   16023 O  OD1   . ASP A 1 3668 ? 139.728 158.333 204.390 1.00 71.62  ? 3668 ASP A OD1   1 
ATOM   16024 O  OD2   . ASP A 1 3668 ? 137.777 157.682 205.155 1.00 74.76  ? 3668 ASP A OD2   1 
ATOM   16025 N  N     . ILE A 1 3669 ? 137.966 155.798 201.843 1.00 67.36  ? 3669 ILE A N     1 
ATOM   16026 C  CA    . ILE A 1 3669 ? 137.387 154.478 201.621 1.00 63.50  ? 3669 ILE A CA    1 
ATOM   16027 C  C     . ILE A 1 3669 ? 137.781 153.565 202.773 1.00 64.13  ? 3669 ILE A C     1 
ATOM   16028 O  O     . ILE A 1 3669 ? 138.948 153.542 203.180 1.00 67.07  ? 3669 ILE A O     1 
ATOM   16029 C  CB    . ILE A 1 3669 ? 137.850 153.882 200.278 1.00 62.22  ? 3669 ILE A CB    1 
ATOM   16030 C  CG1   . ILE A 1 3669 ? 137.257 154.679 199.116 1.00 68.39  ? 3669 ILE A CG1   1 
ATOM   16031 C  CG2   . ILE A 1 3669 ? 137.461 152.414 200.176 1.00 56.79  ? 3669 ILE A CG2   1 
ATOM   16032 C  CD1   . ILE A 1 3669 ? 137.261 153.941 197.805 1.00 65.78  ? 3669 ILE A CD1   1 
ATOM   16033 N  N     . ASP A 1 3670 ? 136.813 152.811 203.291 1.00 60.27  ? 3670 ASP A N     1 
ATOM   16034 C  CA    . ASP A 1 3670 ? 137.110 151.795 204.290 1.00 60.99  ? 3670 ASP A CA    1 
ATOM   16035 C  C     . ASP A 1 3670 ? 137.762 150.586 203.630 1.00 60.29  ? 3670 ASP A C     1 
ATOM   16036 O  O     . ASP A 1 3670 ? 137.249 150.041 202.649 1.00 57.86  ? 3670 ASP A O     1 
ATOM   16037 C  CB    . ASP A 1 3670 ? 135.833 151.375 205.017 1.00 62.31  ? 3670 ASP A CB    1 
ATOM   16038 C  CG    . ASP A 1 3670 ? 136.112 150.644 206.315 1.00 66.49  ? 3670 ASP A CG    1 
ATOM   16039 O  OD1   . ASP A 1 3670 ? 135.160 150.089 206.902 1.00 66.94  ? 3670 ASP A OD1   1 
ATOM   16040 O  OD2   . ASP A 1 3670 ? 137.282 150.625 206.750 1.00 68.25  ? 3670 ASP A OD2   1 
ATOM   16041 N  N     . LEU A 1 3671 ? 138.900 150.166 204.176 1.00 63.91  ? 3671 LEU A N     1 
ATOM   16042 C  CA    . LEU A 1 3671 ? 139.701 149.089 203.610 1.00 58.39  ? 3671 LEU A CA    1 
ATOM   16043 C  C     . LEU A 1 3671 ? 139.433 147.793 204.361 1.00 53.40  ? 3671 LEU A C     1 
ATOM   16044 O  O     . LEU A 1 3671 ? 139.483 147.763 205.595 1.00 56.20  ? 3671 LEU A O     1 
ATOM   16045 C  CB    . LEU A 1 3671 ? 141.192 149.431 203.664 1.00 58.19  ? 3671 LEU A CB    1 
ATOM   16046 C  CG    . LEU A 1 3671 ? 142.149 148.352 203.155 1.00 53.01  ? 3671 LEU A CG    1 
ATOM   16047 C  CD1   . LEU A 1 3671 ? 142.253 148.398 201.641 1.00 46.68  ? 3671 LEU A CD1   1 
ATOM   16048 C  CD2   . LEU A 1 3671 ? 143.521 148.504 203.795 1.00 43.13  ? 3671 LEU A CD2   1 
ATOM   16049 N  N     . SER A 1 3672 ? 139.152 146.728 203.614 1.00 50.72  ? 3672 SER A N     1 
ATOM   16050 C  CA    . SER A 1 3672 ? 138.904 145.388 204.131 1.00 51.81  ? 3672 SER A CA    1 
ATOM   16051 C  C     . SER A 1 3672 ? 140.218 144.619 204.262 1.00 51.40  ? 3672 SER A C     1 
ATOM   16052 O  O     . SER A 1 3672 ? 141.095 144.740 203.401 1.00 54.89  ? 3672 SER A O     1 
ATOM   16053 C  CB    . SER A 1 3672 ? 137.951 144.625 203.217 1.00 48.82  ? 3672 SER A CB    1 
ATOM   16054 O  OG    . SER A 1 3672 ? 137.858 143.263 203.594 1.00 53.44  ? 3672 SER A OG    1 
ATOM   16055 N  N     . PRO A 1 3673 ? 140.377 143.832 205.331 1.00 49.02  ? 3673 PRO A N     1 
ATOM   16056 C  CA    . PRO A 1 3673 ? 141.654 143.130 205.543 1.00 49.86  ? 3673 PRO A CA    1 
ATOM   16057 C  C     . PRO A 1 3673 ? 141.975 142.088 204.485 1.00 49.92  ? 3673 PRO A C     1 
ATOM   16058 O  O     . PRO A 1 3673 ? 143.151 141.736 204.329 1.00 48.77  ? 3673 PRO A O     1 
ATOM   16059 C  CB    . PRO A 1 3673 ? 141.473 142.482 206.922 1.00 48.58  ? 3673 PRO A CB    1 
ATOM   16060 C  CG    . PRO A 1 3673 ? 139.995 142.335 207.074 1.00 54.41  ? 3673 PRO A CG    1 
ATOM   16061 C  CD    . PRO A 1 3673 ? 139.396 143.528 206.387 1.00 52.61  ? 3673 PRO A CD    1 
ATOM   16062 N  N     . SER A 1 3674 ? 140.982 141.585 203.758 1.00 51.56  ? 3674 SER A N     1 
ATOM   16063 C  CA    . SER A 1 3674 ? 141.191 140.524 202.782 1.00 46.67  ? 3674 SER A CA    1 
ATOM   16064 C  C     . SER A 1 3674 ? 141.646 141.042 201.424 1.00 50.37  ? 3674 SER A C     1 
ATOM   16065 O  O     . SER A 1 3674 ? 141.861 140.236 200.512 1.00 53.41  ? 3674 SER A O     1 
ATOM   16066 C  CB    . SER A 1 3674 ? 139.908 139.705 202.615 1.00 44.47  ? 3674 SER A CB    1 
ATOM   16067 O  OG    . SER A 1 3674 ? 138.772 140.549 202.554 1.00 48.28  ? 3674 SER A OG    1 
ATOM   16068 N  N     . PHE A 1 3675 ? 141.792 142.354 201.265 1.00 46.50  ? 3675 PHE A N     1 
ATOM   16069 C  CA    . PHE A 1 3675 ? 142.201 142.913 199.985 1.00 37.25  ? 3675 PHE A CA    1 
ATOM   16070 C  C     . PHE A 1 3675 ? 143.635 142.519 199.652 1.00 39.00  ? 3675 PHE A C     1 
ATOM   16071 O  O     . PHE A 1 3675 ? 144.511 142.494 200.521 1.00 42.06  ? 3675 PHE A O     1 
ATOM   16072 C  CB    . PHE A 1 3675 ? 142.071 144.435 200.003 1.00 33.17  ? 3675 PHE A CB    1 
ATOM   16073 C  CG    . PHE A 1 3675 ? 142.710 145.109 198.824 1.00 30.87  ? 3675 PHE A CG    1 
ATOM   16074 C  CD1   . PHE A 1 3675 ? 142.134 145.029 197.567 1.00 37.07  ? 3675 PHE A CD1   1 
ATOM   16075 C  CD2   . PHE A 1 3675 ? 143.893 145.813 198.970 1.00 30.92  ? 3675 PHE A CD2   1 
ATOM   16076 C  CE1   . PHE A 1 3675 ? 142.721 145.646 196.480 1.00 35.34  ? 3675 PHE A CE1   1 
ATOM   16077 C  CE2   . PHE A 1 3675 ? 144.486 146.429 197.886 1.00 34.10  ? 3675 PHE A CE2   1 
ATOM   16078 C  CZ    . PHE A 1 3675 ? 143.899 146.346 196.640 1.00 33.01  ? 3675 PHE A CZ    1 
ATOM   16079 N  N     . VAL A 1 3676 ? 143.866 142.208 198.381 1.00 37.54  ? 3676 VAL A N     1 
ATOM   16080 C  CA    . VAL A 1 3676 ? 145.205 141.934 197.871 1.00 30.02  ? 3676 VAL A CA    1 
ATOM   16081 C  C     . VAL A 1 3676 ? 145.209 142.282 196.389 1.00 29.50  ? 3676 VAL A C     1 
ATOM   16082 O  O     . VAL A 1 3676 ? 144.241 142.015 195.673 1.00 33.45  ? 3676 VAL A O     1 
ATOM   16083 C  CB    . VAL A 1 3676 ? 145.618 140.464 198.130 1.00 28.91  ? 3676 VAL A CB    1 
ATOM   16084 C  CG1   . VAL A 1 3676 ? 144.575 139.506 197.584 1.00 36.00  ? 3676 VAL A CG1   1 
ATOM   16085 C  CG2   . VAL A 1 3676 ? 146.982 140.173 197.527 1.00 25.30  ? 3676 VAL A CG2   1 
ATOM   16086 N  N     . ILE A 1 3677 ? 146.300 142.895 195.936 1.00 27.50  ? 3677 ILE A N     1 
ATOM   16087 C  CA    . ILE A 1 3677 ? 146.407 143.385 194.568 1.00 19.67  ? 3677 ILE A CA    1 
ATOM   16088 C  C     . ILE A 1 3677 ? 147.662 142.811 193.925 1.00 24.18  ? 3677 ILE A C     1 
ATOM   16089 O  O     . ILE A 1 3677 ? 148.713 142.703 194.568 1.00 28.13  ? 3677 ILE A O     1 
ATOM   16090 C  CB    . ILE A 1 3677 ? 146.410 144.930 194.517 1.00 22.62  ? 3677 ILE A CB    1 
ATOM   16091 C  CG1   . ILE A 1 3677 ? 146.377 145.423 193.070 1.00 27.19  ? 3677 ILE A CG1   1 
ATOM   16092 C  CG2   . ILE A 1 3677 ? 147.601 145.507 195.263 1.00 24.53  ? 3677 ILE A CG2   1 
ATOM   16093 C  CD1   . ILE A 1 3677 ? 146.185 146.912 192.945 1.00 29.42  ? 3677 ILE A CD1   1 
ATOM   16094 N  N     . PHE A 1 3678 ? 147.538 142.412 192.662 1.00 25.72  ? 3678 PHE A N     1 
ATOM   16095 C  CA    . PHE A 1 3678 ? 148.653 141.916 191.865 1.00 16.10  ? 3678 PHE A CA    1 
ATOM   16096 C  C     . PHE A 1 3678 ? 148.769 142.774 190.615 1.00 17.35  ? 3678 PHE A C     1 
ATOM   16097 O  O     . PHE A 1 3678 ? 147.774 142.996 189.917 1.00 24.18  ? 3678 PHE A O     1 
ATOM   16098 C  CB    . PHE A 1 3678 ? 148.454 140.446 191.489 1.00 16.59  ? 3678 PHE A CB    1 
ATOM   16099 C  CG    . PHE A 1 3678 ? 148.340 139.524 192.668 1.00 19.25  ? 3678 PHE A CG    1 
ATOM   16100 C  CD1   . PHE A 1 3678 ? 149.472 138.992 193.260 1.00 21.82  ? 3678 PHE A CD1   1 
ATOM   16101 C  CD2   . PHE A 1 3678 ? 147.100 139.184 193.181 1.00 24.83  ? 3678 PHE A CD2   1 
ATOM   16102 C  CE1   . PHE A 1 3678 ? 149.371 138.141 194.342 1.00 22.39  ? 3678 PHE A CE1   1 
ATOM   16103 C  CE2   . PHE A 1 3678 ? 146.992 138.334 194.262 1.00 26.34  ? 3678 PHE A CE2   1 
ATOM   16104 C  CZ    . PHE A 1 3678 ? 148.130 137.811 194.843 1.00 23.14  ? 3678 PHE A CZ    1 
ATOM   16105 N  N     . LEU A 1 3679 ? 149.975 143.258 190.337 1.00 19.59  ? 3679 LEU A N     1 
ATOM   16106 C  CA    . LEU A 1 3679 ? 150.238 144.031 189.132 1.00 18.06  ? 3679 LEU A CA    1 
ATOM   16107 C  C     . LEU A 1 3679 ? 151.134 143.220 188.205 1.00 16.10  ? 3679 LEU A C     1 
ATOM   16108 O  O     . LEU A 1 3679 ? 152.124 142.632 188.649 1.00 18.83  ? 3679 LEU A O     1 
ATOM   16109 C  CB    . LEU A 1 3679 ? 150.889 145.371 189.476 1.00 17.01  ? 3679 LEU A CB    1 
ATOM   16110 C  CG    . LEU A 1 3679 ? 150.220 146.226 190.553 1.00 17.00  ? 3679 LEU A CG    1 
ATOM   16111 C  CD1   . LEU A 1 3679 ? 150.890 147.587 190.641 1.00 20.39  ? 3679 LEU A CD1   1 
ATOM   16112 C  CD2   . LEU A 1 3679 ? 148.736 146.379 190.275 1.00 20.56  ? 3679 LEU A CD2   1 
ATOM   16113 N  N     . SER A 1 3680 ? 150.783 143.182 186.921 1.00 18.62  ? 3680 SER A N     1 
ATOM   16114 C  CA    . SER A 1 3680 ? 151.461 142.310 185.974 1.00 17.53  ? 3680 SER A CA    1 
ATOM   16115 C  C     . SER A 1 3680 ? 151.773 143.061 184.689 1.00 21.15  ? 3680 SER A C     1 
ATOM   16116 O  O     . SER A 1 3680 ? 151.095 144.027 184.331 1.00 26.80  ? 3680 SER A O     1 
ATOM   16117 C  CB    . SER A 1 3680 ? 150.618 141.068 185.657 1.00 21.56  ? 3680 SER A CB    1 
ATOM   16118 O  OG    . SER A 1 3680 ? 149.395 141.426 185.038 1.00 25.92  ? 3680 SER A OG    1 
ATOM   16119 N  N     . THR A 1 3681 ? 152.817 142.601 184.001 1.00 20.08  ? 3681 THR A N     1 
ATOM   16120 C  CA    . THR A 1 3681 ? 153.187 143.115 182.691 1.00 22.28  ? 3681 THR A CA    1 
ATOM   16121 C  C     . THR A 1 3681 ? 153.621 141.956 181.807 1.00 24.64  ? 3681 THR A C     1 
ATOM   16122 O  O     . THR A 1 3681 ? 154.062 140.912 182.296 1.00 29.97  ? 3681 THR A O     1 
ATOM   16123 C  CB    . THR A 1 3681 ? 154.317 144.154 182.771 1.00 21.98  ? 3681 THR A CB    1 
ATOM   16124 O  OG1   . THR A 1 3681 ? 154.550 144.716 181.473 1.00 24.27  ? 3681 THR A OG1   1 
ATOM   16125 C  CG2   . THR A 1 3681 ? 155.601 143.519 183.283 1.00 23.69  ? 3681 THR A CG2   1 
ATOM   16126 N  N     . ARG A 1 3682 ? 153.482 142.147 180.498 1.00 21.16  ? 3682 ARG A N     1 
ATOM   16127 C  CA    . ARG A 1 3682 ? 153.943 141.178 179.515 1.00 19.50  ? 3682 ARG A CA    1 
ATOM   16128 C  C     . ARG A 1 3682 ? 155.249 141.592 178.852 1.00 25.68  ? 3682 ARG A C     1 
ATOM   16129 O  O     . ARG A 1 3682 ? 155.701 140.911 177.926 1.00 34.64  ? 3682 ARG A O     1 
ATOM   16130 C  CB    . ARG A 1 3682 ? 152.872 140.959 178.442 1.00 20.75  ? 3682 ARG A CB    1 
ATOM   16131 C  CG    . ARG A 1 3682 ? 151.621 140.257 178.942 1.00 20.55  ? 3682 ARG A CG    1 
ATOM   16132 C  CD    . ARG A 1 3682 ? 150.613 140.061 177.819 1.00 22.01  ? 3682 ARG A CD    1 
ATOM   16133 N  NE    . ARG A 1 3682 ? 150.212 141.326 177.214 1.00 25.83  ? 3682 ARG A NE    1 
ATOM   16134 C  CZ    . ARG A 1 3682 ? 150.588 141.731 176.009 1.00 30.08  ? 3682 ARG A CZ    1 
ATOM   16135 N  NH1   . ARG A 1 3682 ? 151.378 140.993 175.246 1.00 29.49  ? 3682 ARG A NH1   1 
ATOM   16136 N  NH2   . ARG A 1 3682 ? 150.161 142.908 175.558 1.00 31.75  ? 3682 ARG A NH2   1 
ATOM   16137 N  N     . ASP A 1 3683 ? 155.862 142.684 179.300 1.00 21.78  ? 3683 ASP A N     1 
ATOM   16138 C  CA    . ASP A 1 3683 ? 157.081 143.200 178.689 1.00 24.06  ? 3683 ASP A CA    1 
ATOM   16139 C  C     . ASP A 1 3683 ? 158.272 142.926 179.595 1.00 30.12  ? 3683 ASP A C     1 
ATOM   16140 O  O     . ASP A 1 3683 ? 158.404 143.573 180.645 1.00 34.01  ? 3683 ASP A O     1 
ATOM   16141 C  CB    . ASP A 1 3683 ? 156.951 144.700 178.422 1.00 26.91  ? 3683 ASP A CB    1 
ATOM   16142 C  CG    . ASP A 1 3683 ? 157.922 145.191 177.368 1.00 35.87  ? 3683 ASP A CG    1 
ATOM   16143 O  OD1   . ASP A 1 3683 ? 158.587 144.349 176.729 1.00 35.41  ? 3683 ASP A OD1   1 
ATOM   16144 O  OD2   . ASP A 1 3683 ? 158.022 146.422 177.180 1.00 32.37  ? 3683 ASP A OD2   1 
ATOM   16145 N  N     . PRO A 1 3684 ? 159.154 141.985 179.249 1.00 37.29  ? 3684 PRO A N     1 
ATOM   16146 C  CA    . PRO A 1 3684 ? 160.349 141.764 180.079 1.00 36.42  ? 3684 PRO A CA    1 
ATOM   16147 C  C     . PRO A 1 3684 ? 161.347 142.906 180.024 1.00 38.45  ? 3684 PRO A C     1 
ATOM   16148 O  O     . PRO A 1 3684 ? 162.192 143.008 180.922 1.00 44.66  ? 3684 PRO A O     1 
ATOM   16149 C  CB    . PRO A 1 3684 ? 160.945 140.475 179.501 1.00 32.36  ? 3684 PRO A CB    1 
ATOM   16150 C  CG    . PRO A 1 3684 ? 160.467 140.444 178.089 1.00 31.90  ? 3684 PRO A CG    1 
ATOM   16151 C  CD    . PRO A 1 3684 ? 159.103 141.076 178.091 1.00 35.53  ? 3684 PRO A CD    1 
ATOM   16152 N  N     . THR A 1 3685 ? 161.281 143.765 179.008 1.00 38.31  ? 3685 THR A N     1 
ATOM   16153 C  CA    . THR A 1 3685 ? 162.239 144.847 178.825 1.00 41.06  ? 3685 THR A CA    1 
ATOM   16154 C  C     . THR A 1 3685 ? 161.720 146.190 179.320 1.00 38.22  ? 3685 THR A C     1 
ATOM   16155 O  O     . THR A 1 3685 ? 162.367 147.216 179.084 1.00 41.53  ? 3685 THR A O     1 
ATOM   16156 C  CB    . THR A 1 3685 ? 162.631 144.961 177.350 1.00 43.11  ? 3685 THR A CB    1 
ATOM   16157 O  OG1   . THR A 1 3685 ? 161.563 145.574 176.617 1.00 39.87  ? 3685 THR A OG1   1 
ATOM   16158 C  CG2   . THR A 1 3685 ? 162.913 143.585 176.767 1.00 39.23  ? 3685 THR A CG2   1 
ATOM   16159 N  N     . VAL A 1 3686 ? 160.569 146.213 179.991 1.00 35.67  ? 3686 VAL A N     1 
ATOM   16160 C  CA    . VAL A 1 3686 ? 159.989 147.475 180.431 1.00 34.33  ? 3686 VAL A CA    1 
ATOM   16161 C  C     . VAL A 1 3686 ? 160.830 148.071 181.553 1.00 34.23  ? 3686 VAL A C     1 
ATOM   16162 O  O     . VAL A 1 3686 ? 161.354 147.356 182.419 1.00 35.88  ? 3686 VAL A O     1 
ATOM   16163 C  CB    . VAL A 1 3686 ? 158.526 147.275 180.864 1.00 29.84  ? 3686 VAL A CB    1 
ATOM   16164 C  CG1   . VAL A 1 3686 ? 158.437 146.417 182.114 1.00 33.43  ? 3686 VAL A CG1   1 
ATOM   16165 C  CG2   . VAL A 1 3686 ? 157.854 148.618 181.087 1.00 30.43  ? 3686 VAL A CG2   1 
ATOM   16166 N  N     . GLU A 1 3687 ? 160.988 149.390 181.522 1.00 38.08  ? 3687 GLU A N     1 
ATOM   16167 C  CA    . GLU A 1 3687 ? 161.691 150.127 182.561 1.00 36.77  ? 3687 GLU A CA    1 
ATOM   16168 C  C     . GLU A 1 3687 ? 160.683 150.698 183.548 1.00 35.87  ? 3687 GLU A C     1 
ATOM   16169 O  O     . GLU A 1 3687 ? 159.575 151.084 183.165 1.00 32.29  ? 3687 GLU A O     1 
ATOM   16170 C  CB    . GLU A 1 3687 ? 162.534 151.252 181.958 1.00 37.56  ? 3687 GLU A CB    1 
ATOM   16171 C  CG    . GLU A 1 3687 ? 163.635 151.768 182.870 1.00 42.07  ? 3687 GLU A CG    1 
ATOM   16172 C  CD    . GLU A 1 3687 ? 164.651 150.699 183.219 1.00 52.77  ? 3687 GLU A CD    1 
ATOM   16173 O  OE1   . GLU A 1 3687 ? 165.353 150.223 182.302 1.00 53.86  ? 3687 GLU A OE1   1 
ATOM   16174 O  OE2   . GLU A 1 3687 ? 164.749 150.335 184.410 1.00 50.03  ? 3687 GLU A OE2   1 
ATOM   16175 N  N     . PHE A 1 3688 ? 161.071 150.747 184.819 1.00 33.10  ? 3688 PHE A N     1 
ATOM   16176 C  CA    . PHE A 1 3688 ? 160.189 151.268 185.847 1.00 32.00  ? 3688 PHE A CA    1 
ATOM   16177 C  C     . PHE A 1 3688 ? 160.882 152.374 186.634 1.00 35.93  ? 3688 PHE A C     1 
ATOM   16178 O  O     . PHE A 1 3688 ? 162.090 152.306 186.880 1.00 41.37  ? 3688 PHE A O     1 
ATOM   16179 C  CB    . PHE A 1 3688 ? 159.740 150.163 186.811 1.00 32.44  ? 3688 PHE A CB    1 
ATOM   16180 C  CG    . PHE A 1 3688 ? 158.708 149.237 186.235 1.00 28.69  ? 3688 PHE A CG    1 
ATOM   16181 C  CD1   . PHE A 1 3688 ? 157.465 149.713 185.856 1.00 28.51  ? 3688 PHE A CD1   1 
ATOM   16182 C  CD2   . PHE A 1 3688 ? 158.980 147.889 186.075 1.00 28.85  ? 3688 PHE A CD2   1 
ATOM   16183 C  CE1   . PHE A 1 3688 ? 156.512 148.864 185.328 1.00 33.60  ? 3688 PHE A CE1   1 
ATOM   16184 C  CE2   . PHE A 1 3688 ? 158.032 147.034 185.547 1.00 29.28  ? 3688 PHE A CE2   1 
ATOM   16185 C  CZ    . PHE A 1 3688 ? 156.797 147.522 185.173 1.00 30.98  ? 3688 PHE A CZ    1 
ATOM   16186 N  N     . PRO A 1 3689 ? 160.141 153.409 187.036 1.00 37.24  ? 3689 PRO A N     1 
ATOM   16187 C  CA    . PRO A 1 3689 ? 160.752 154.477 187.822 1.00 33.35  ? 3689 PRO A CA    1 
ATOM   16188 C  C     . PRO A 1 3689 ? 161.129 153.977 189.204 1.00 31.57  ? 3689 PRO A C     1 
ATOM   16189 O  O     . PRO A 1 3689 ? 160.548 153.000 189.707 1.00 32.39  ? 3689 PRO A O     1 
ATOM   16190 C  CB    . PRO A 1 3689 ? 159.644 155.543 187.891 1.00 33.62  ? 3689 PRO A CB    1 
ATOM   16191 C  CG    . PRO A 1 3689 ? 158.381 154.786 187.683 1.00 35.03  ? 3689 PRO A CG    1 
ATOM   16192 C  CD    . PRO A 1 3689 ? 158.725 153.677 186.735 1.00 35.62  ? 3689 PRO A CD    1 
ATOM   16193 N  N     . PRO A 1 3690 ? 162.109 154.609 189.856 1.00 32.84  ? 3690 PRO A N     1 
ATOM   16194 C  CA    . PRO A 1 3690 ? 162.558 154.112 191.167 1.00 29.96  ? 3690 PRO A CA    1 
ATOM   16195 C  C     . PRO A 1 3690 ? 161.466 154.071 192.222 1.00 27.75  ? 3690 PRO A C     1 
ATOM   16196 O  O     . PRO A 1 3690 ? 161.474 153.168 193.068 1.00 28.24  ? 3690 PRO A O     1 
ATOM   16197 C  CB    . PRO A 1 3690 ? 163.672 155.097 191.551 1.00 30.55  ? 3690 PRO A CB    1 
ATOM   16198 C  CG    . PRO A 1 3690 ? 164.127 155.684 190.258 1.00 30.18  ? 3690 PRO A CG    1 
ATOM   16199 C  CD    . PRO A 1 3690 ? 162.906 155.759 189.396 1.00 31.22  ? 3690 PRO A CD    1 
ATOM   16200 N  N     . ASP A 1 3691 ? 160.527 155.021 192.207 1.00 29.63  ? 3691 ASP A N     1 
ATOM   16201 C  CA    . ASP A 1 3691 ? 159.474 155.025 193.218 1.00 32.09  ? 3691 ASP A CA    1 
ATOM   16202 C  C     . ASP A 1 3691 ? 158.543 153.829 193.057 1.00 30.62  ? 3691 ASP A C     1 
ATOM   16203 O  O     . ASP A 1 3691 ? 158.113 153.234 194.052 1.00 30.56  ? 3691 ASP A O     1 
ATOM   16204 C  CB    . ASP A 1 3691 ? 158.689 156.335 193.160 1.00 30.87  ? 3691 ASP A CB    1 
ATOM   16205 C  CG    . ASP A 1 3691 ? 158.279 156.705 191.753 1.00 36.77  ? 3691 ASP A CG    1 
ATOM   16206 O  OD1   . ASP A 1 3691 ? 157.189 157.290 191.582 1.00 42.96  ? 3691 ASP A OD1   1 
ATOM   16207 O  OD2   . ASP A 1 3691 ? 159.051 156.417 190.818 1.00 35.22  ? 3691 ASP A OD2   1 
ATOM   16208 N  N     . LEU A 1 3692 ? 158.216 153.464 191.816 1.00 28.97  ? 3692 LEU A N     1 
ATOM   16209 C  CA    . LEU A 1 3692 ? 157.388 152.284 191.595 1.00 27.10  ? 3692 LEU A CA    1 
ATOM   16210 C  C     . LEU A 1 3692 ? 158.126 151.013 191.998 1.00 22.31  ? 3692 LEU A C     1 
ATOM   16211 O  O     . LEU A 1 3692 ? 157.522 150.089 192.555 1.00 21.83  ? 3692 LEU A O     1 
ATOM   16212 C  CB    . LEU A 1 3692 ? 156.947 152.214 190.134 1.00 32.15  ? 3692 LEU A CB    1 
ATOM   16213 C  CG    . LEU A 1 3692 ? 155.970 151.091 189.778 1.00 24.53  ? 3692 LEU A CG    1 
ATOM   16214 C  CD1   . LEU A 1 3692 ? 154.815 151.059 190.764 1.00 21.13  ? 3692 LEU A CD1   1 
ATOM   16215 C  CD2   . LEU A 1 3692 ? 155.457 151.256 188.360 1.00 24.11  ? 3692 LEU A CD2   1 
ATOM   16216 N  N     . CYS A 1 3693 ? 159.431 150.948 191.720 1.00 26.88  ? 3693 CYS A N     1 
ATOM   16217 C  CA    . CYS A 1 3693 ? 160.220 149.791 192.130 1.00 23.72  ? 3693 CYS A CA    1 
ATOM   16218 C  C     . CYS A 1 3693 ? 160.248 149.641 193.644 1.00 22.15  ? 3693 CYS A C     1 
ATOM   16219 O  O     . CYS A 1 3693 ? 160.294 148.518 194.157 1.00 25.52  ? 3693 CYS A O     1 
ATOM   16220 C  CB    . CYS A 1 3693 ? 161.645 149.906 191.586 1.00 22.57  ? 3693 CYS A CB    1 
ATOM   16221 S  SG    . CYS A 1 3693 ? 161.755 150.026 189.789 1.00 38.35  ? 3693 CYS A SG    1 
ATOM   16222 N  N     . SER A 1 3694 ? 160.227 150.758 194.373 1.00 21.80  ? 3694 SER A N     1 
ATOM   16223 C  CA    . SER A 1 3694 ? 160.242 150.695 195.829 1.00 21.17  ? 3694 SER A CA    1 
ATOM   16224 C  C     . SER A 1 3694 ? 158.901 150.247 196.394 1.00 20.64  ? 3694 SER A C     1 
ATOM   16225 O  O     . SER A 1 3694 ? 158.855 149.659 197.480 1.00 25.45  ? 3694 SER A O     1 
ATOM   16226 C  CB    . SER A 1 3694 ? 160.626 152.056 196.407 1.00 25.66  ? 3694 SER A CB    1 
ATOM   16227 O  OG    . SER A 1 3694 ? 159.583 152.998 196.227 1.00 24.71  ? 3694 SER A OG    1 
ATOM   16228 N  N     . ARG A 1 3695 ? 157.805 150.515 195.683 1.00 19.90  ? 3695 ARG A N     1 
ATOM   16229 C  CA    . ARG A 1 3695 ? 156.476 150.264 196.225 1.00 19.05  ? 3695 ARG A CA    1 
ATOM   16230 C  C     . ARG A 1 3695 ? 156.006 148.829 196.028 1.00 16.97  ? 3695 ARG A C     1 
ATOM   16231 O  O     . ARG A 1 3695 ? 154.980 148.447 196.601 1.00 25.89  ? 3695 ARG A O     1 
ATOM   16232 C  CB    . ARG A 1 3695 ? 155.462 151.217 195.590 1.00 23.60  ? 3695 ARG A CB    1 
ATOM   16233 C  CG    . ARG A 1 3695 ? 155.236 152.498 196.373 1.00 29.09  ? 3695 ARG A CG    1 
ATOM   16234 C  CD    . ARG A 1 3695 ? 154.170 153.359 195.718 1.00 28.58  ? 3695 ARG A CD    1 
ATOM   16235 N  NE    . ARG A 1 3695 ? 154.741 154.367 194.833 1.00 26.76  ? 3695 ARG A NE    1 
ATOM   16236 C  CZ    . ARG A 1 3695 ? 155.112 155.579 195.220 1.00 30.53  ? 3695 ARG A CZ    1 
ATOM   16237 N  NH1   . ARG A 1 3695 ? 155.001 155.967 196.479 1.00 27.28  ? 3695 ARG A NH1   1 
ATOM   16238 N  NH2   . ARG A 1 3695 ? 155.606 156.424 194.321 1.00 29.84  ? 3695 ARG A NH2   1 
ATOM   16239 N  N     . VAL A 1 3696 ? 156.718 148.029 195.236 1.00 16.55  ? 3696 VAL A N     1 
ATOM   16240 C  CA    . VAL A 1 3696 ? 156.300 146.669 194.926 1.00 15.43  ? 3696 VAL A CA    1 
ATOM   16241 C  C     . VAL A 1 3696 ? 157.492 145.734 195.062 1.00 17.34  ? 3696 VAL A C     1 
ATOM   16242 O  O     . VAL A 1 3696 ? 158.648 146.160 195.108 1.00 22.84  ? 3696 VAL A O     1 
ATOM   16243 C  CB    . VAL A 1 3696 ? 155.696 146.550 193.508 1.00 17.66  ? 3696 VAL A CB    1 
ATOM   16244 C  CG1   . VAL A 1 3696 ? 154.434 147.388 193.385 1.00 20.63  ? 3696 VAL A CG1   1 
ATOM   16245 C  CG2   . VAL A 1 3696 ? 156.721 146.954 192.460 1.00 15.07  ? 3696 VAL A CG2   1 
ATOM   16246 N  N     . THR A 1 3697 ? 157.193 144.440 195.131 1.00 15.96  ? 3697 THR A N     1 
ATOM   16247 C  CA    . THR A 1 3697 ? 158.207 143.400 195.032 1.00 14.89  ? 3697 THR A CA    1 
ATOM   16248 C  C     . THR A 1 3697 ? 158.133 142.773 193.645 1.00 16.98  ? 3697 THR A C     1 
ATOM   16249 O  O     . THR A 1 3697 ? 157.044 142.461 193.152 1.00 18.11  ? 3697 THR A O     1 
ATOM   16250 C  CB    . THR A 1 3697 ? 158.038 142.337 196.124 1.00 18.77  ? 3697 THR A CB    1 
ATOM   16251 O  OG1   . THR A 1 3697 ? 159.019 141.308 195.948 1.00 24.63  ? 3697 THR A OG1   1 
ATOM   16252 C  CG2   . THR A 1 3697 ? 156.654 141.718 196.090 1.00 18.68  ? 3697 THR A CG2   1 
ATOM   16253 N  N     . PHE A 1 3698 ? 159.290 142.619 193.011 1.00 16.93  ? 3698 PHE A N     1 
ATOM   16254 C  CA    . PHE A 1 3698 ? 159.348 142.112 191.651 1.00 11.52  ? 3698 PHE A CA    1 
ATOM   16255 C  C     . PHE A 1 3698 ? 159.293 140.592 191.650 1.00 12.58  ? 3698 PHE A C     1 
ATOM   16256 O  O     . PHE A 1 3698 ? 159.890 139.934 192.506 1.00 16.95  ? 3698 PHE A O     1 
ATOM   16257 C  CB    . PHE A 1 3698 ? 160.626 142.591 190.965 1.00 14.81  ? 3698 PHE A CB    1 
ATOM   16258 C  CG    . PHE A 1 3698 ? 160.584 144.030 190.543 1.00 18.62  ? 3698 PHE A CG    1 
ATOM   16259 C  CD1   . PHE A 1 3698 ? 160.004 144.402 189.344 1.00 21.69  ? 3698 PHE A CD1   1 
ATOM   16260 C  CD2   . PHE A 1 3698 ? 161.112 145.016 191.358 1.00 23.19  ? 3698 PHE A CD2   1 
ATOM   16261 C  CE1   . PHE A 1 3698 ? 159.970 145.726 188.958 1.00 21.46  ? 3698 PHE A CE1   1 
ATOM   16262 C  CE2   . PHE A 1 3698 ? 161.075 146.342 190.979 1.00 23.65  ? 3698 PHE A CE2   1 
ATOM   16263 C  CZ    . PHE A 1 3698 ? 160.501 146.697 189.778 1.00 23.42  ? 3698 PHE A CZ    1 
ATOM   16264 N  N     . VAL A 1 3699 ? 158.550 140.035 190.698 1.00 15.29  ? 3699 VAL A N     1 
ATOM   16265 C  CA    . VAL A 1 3699 ? 158.462 138.592 190.496 1.00 12.54  ? 3699 VAL A CA    1 
ATOM   16266 C  C     . VAL A 1 3699 ? 158.618 138.359 188.999 1.00 15.06  ? 3699 VAL A C     1 
ATOM   16267 O  O     . VAL A 1 3699 ? 157.645 138.458 188.243 1.00 17.01  ? 3699 VAL A O     1 
ATOM   16268 C  CB    . VAL A 1 3699 ? 157.147 138.000 191.016 1.00 10.89  ? 3699 VAL A CB    1 
ATOM   16269 C  CG1   . VAL A 1 3699 ? 157.154 136.492 190.865 1.00 11.83  ? 3699 VAL A CG1   1 
ATOM   16270 C  CG2   . VAL A 1 3699 ? 156.921 138.381 192.470 1.00 16.42  ? 3699 VAL A CG2   1 
ATOM   16271 N  N     . ASN A 1 3700 ? 159.837 138.048 188.565 1.00 13.13  ? 3700 ASN A N     1 
ATOM   16272 C  CA    . ASN A 1 3700 ? 160.159 137.902 187.151 1.00 14.26  ? 3700 ASN A CA    1 
ATOM   16273 C  C     . ASN A 1 3700 ? 160.026 136.440 186.743 1.00 18.10  ? 3700 ASN A C     1 
ATOM   16274 O  O     . ASN A 1 3700 ? 160.752 135.580 187.254 1.00 19.30  ? 3700 ASN A O     1 
ATOM   16275 C  CB    . ASN A 1 3700 ? 161.570 138.415 186.864 1.00 14.24  ? 3700 ASN A CB    1 
ATOM   16276 C  CG    . ASN A 1 3700 ? 161.746 138.864 185.429 1.00 15.45  ? 3700 ASN A CG    1 
ATOM   16277 O  OD1   . ASN A 1 3700 ? 160.922 138.563 184.567 1.00 20.39  ? 3700 ASN A OD1   1 
ATOM   16278 N  ND2   . ASN A 1 3700 ? 162.824 139.592 185.165 1.00 13.82  ? 3700 ASN A ND2   1 
ATOM   16279 N  N     . PHE A 1 3701 ? 159.103 136.164 185.822 1.00 17.71  ? 3701 PHE A N     1 
ATOM   16280 C  CA    . PHE A 1 3701 ? 158.913 134.823 185.273 1.00 16.91  ? 3701 PHE A CA    1 
ATOM   16281 C  C     . PHE A 1 3701 ? 159.710 134.722 183.976 1.00 19.58  ? 3701 PHE A C     1 
ATOM   16282 O  O     . PHE A 1 3701 ? 159.207 134.959 182.879 1.00 30.87  ? 3701 PHE A O     1 
ATOM   16283 C  CB    . PHE A 1 3701 ? 157.432 134.538 185.047 1.00 18.39  ? 3701 PHE A CB    1 
ATOM   16284 C  CG    . PHE A 1 3701 ? 156.696 134.116 186.282 1.00 16.22  ? 3701 PHE A CG    1 
ATOM   16285 C  CD1   . PHE A 1 3701 ? 156.276 135.051 187.212 1.00 16.20  ? 3701 PHE A CD1   1 
ATOM   16286 C  CD2   . PHE A 1 3701 ? 156.403 132.781 186.502 1.00 16.83  ? 3701 PHE A CD2   1 
ATOM   16287 C  CE1   . PHE A 1 3701 ? 155.591 134.659 188.345 1.00 16.68  ? 3701 PHE A CE1   1 
ATOM   16288 C  CE2   . PHE A 1 3701 ? 155.718 132.385 187.631 1.00 17.90  ? 3701 PHE A CE2   1 
ATOM   16289 C  CZ    . PHE A 1 3701 ? 155.309 133.325 188.552 1.00 16.60  ? 3701 PHE A CZ    1 
ATOM   16290 N  N     . THR A 1 3702 ? 160.980 134.362 184.115 1.00 19.45  ? 3702 THR A N     1 
ATOM   16291 C  CA    . THR A 1 3702 ? 161.871 134.201 182.978 1.00 14.72  ? 3702 THR A CA    1 
ATOM   16292 C  C     . THR A 1 3702 ? 161.958 132.734 182.576 1.00 14.90  ? 3702 THR A C     1 
ATOM   16293 O  O     . THR A 1 3702 ? 161.666 131.830 183.362 1.00 17.72  ? 3702 THR A O     1 
ATOM   16294 C  CB    . THR A 1 3702 ? 163.267 134.742 183.298 1.00 14.13  ? 3702 THR A CB    1 
ATOM   16295 O  OG1   . THR A 1 3702 ? 163.585 134.465 184.667 1.00 21.56  ? 3702 THR A OG1   1 
ATOM   16296 C  CG2   . THR A 1 3702 ? 163.319 136.243 183.065 1.00 11.60  ? 3702 THR A CG2   1 
ATOM   16297 N  N     . VAL A 1 3703 ? 162.362 132.510 181.331 1.00 19.65  ? 3703 VAL A N     1 
ATOM   16298 C  CA    . VAL A 1 3703 ? 162.501 131.164 180.789 1.00 17.73  ? 3703 VAL A CA    1 
ATOM   16299 C  C     . VAL A 1 3703 ? 163.910 130.668 181.082 1.00 16.97  ? 3703 VAL A C     1 
ATOM   16300 O  O     . VAL A 1 3703 ? 164.895 131.336 180.748 1.00 20.71  ? 3703 VAL A O     1 
ATOM   16301 C  CB    . VAL A 1 3703 ? 162.210 131.137 179.281 1.00 20.26  ? 3703 VAL A CB    1 
ATOM   16302 C  CG1   . VAL A 1 3703 ? 162.334 129.721 178.742 1.00 21.34  ? 3703 VAL A CG1   1 
ATOM   16303 C  CG2   . VAL A 1 3703 ? 160.826 131.698 179.000 1.00 24.55  ? 3703 VAL A CG2   1 
ATOM   16304 N  N     . THR A 1 3704 ? 164.006 129.501 181.708 1.00 18.75  ? 3704 THR A N     1 
ATOM   16305 C  CA    . THR A 1 3704 ? 165.284 128.884 182.026 1.00 20.13  ? 3704 THR A CA    1 
ATOM   16306 C  C     . THR A 1 3704 ? 165.562 127.729 181.071 1.00 20.50  ? 3704 THR A C     1 
ATOM   16307 O  O     . THR A 1 3704 ? 164.651 127.151 180.473 1.00 21.41  ? 3704 THR A O     1 
ATOM   16308 C  CB    . THR A 1 3704 ? 165.305 128.386 183.474 1.00 19.07  ? 3704 THR A CB    1 
ATOM   16309 O  OG1   . THR A 1 3704 ? 164.315 127.364 183.644 1.00 20.46  ? 3704 THR A OG1   1 
ATOM   16310 C  CG2   . THR A 1 3704 ? 165.013 129.530 184.433 1.00 16.35  ? 3704 THR A CG2   1 
ATOM   16311 N  N     . ARG A 1 3705 ? 166.849 127.405 180.928 1.00 19.84  ? 3705 ARG A N     1 
ATOM   16312 C  CA    . ARG A 1 3705 ? 167.248 126.350 180.002 1.00 18.44  ? 3705 ARG A CA    1 
ATOM   16313 C  C     . ARG A 1 3705 ? 166.689 124.998 180.426 1.00 21.77  ? 3705 ARG A C     1 
ATOM   16314 O  O     . ARG A 1 3705 ? 166.242 124.212 179.583 1.00 26.05  ? 3705 ARG A O     1 
ATOM   16315 C  CB    . ARG A 1 3705 ? 168.772 126.294 179.896 1.00 16.66  ? 3705 ARG A CB    1 
ATOM   16316 C  CG    . ARG A 1 3705 ? 169.371 127.457 179.127 1.00 18.78  ? 3705 ARG A CG    1 
ATOM   16317 C  CD    . ARG A 1 3705 ? 170.885 127.385 179.074 1.00 21.69  ? 3705 ARG A CD    1 
ATOM   16318 N  NE    . ARG A 1 3705 ? 171.427 128.238 178.023 1.00 24.57  ? 3705 ARG A NE    1 
ATOM   16319 C  CZ    . ARG A 1 3705 ? 171.546 127.878 176.752 1.00 26.31  ? 3705 ARG A CZ    1 
ATOM   16320 N  NH1   . ARG A 1 3705 ? 171.170 126.681 176.335 1.00 24.34  ? 3705 ARG A NH1   1 
ATOM   16321 N  NH2   . ARG A 1 3705 ? 172.054 128.742 175.878 1.00 24.16  ? 3705 ARG A NH2   1 
ATOM   16322 N  N     . SER A 1 3706 ? 166.711 124.707 181.729 1.00 20.52  ? 3706 SER A N     1 
ATOM   16323 C  CA    . SER A 1 3706 ? 166.202 123.425 182.208 1.00 22.54  ? 3706 SER A CA    1 
ATOM   16324 C  C     . SER A 1 3706 ? 164.704 123.291 181.959 1.00 19.76  ? 3706 SER A C     1 
ATOM   16325 O  O     . SER A 1 3706 ? 164.234 122.230 181.532 1.00 22.46  ? 3706 SER A O     1 
ATOM   16326 C  CB    . SER A 1 3706 ? 166.514 123.262 183.695 1.00 27.37  ? 3706 SER A CB    1 
ATOM   16327 O  OG    . SER A 1 3706 ? 167.761 123.849 184.021 1.00 24.08  ? 3706 SER A OG    1 
ATOM   16328 N  N     . SER A 1 3707 ? 163.939 124.351 182.228 1.00 19.23  ? 3707 SER A N     1 
ATOM   16329 C  CA    . SER A 1 3707 ? 162.495 124.292 182.023 1.00 21.43  ? 3707 SER A CA    1 
ATOM   16330 C  C     . SER A 1 3707 ? 162.148 124.143 180.547 1.00 21.51  ? 3707 SER A C     1 
ATOM   16331 O  O     . SER A 1 3707 ? 161.259 123.363 180.186 1.00 19.02  ? 3707 SER A O     1 
ATOM   16332 C  CB    . SER A 1 3707 ? 161.830 125.538 182.607 1.00 19.13  ? 3707 SER A CB    1 
ATOM   16333 O  OG    . SER A 1 3707 ? 162.244 126.706 181.920 1.00 21.89  ? 3707 SER A OG    1 
ATOM   16334 N  N     . LEU A 1 3708 ? 162.838 124.886 179.678 1.00 20.56  ? 3708 LEU A N     1 
ATOM   16335 C  CA    . LEU A 1 3708 ? 162.556 124.802 178.249 1.00 16.55  ? 3708 LEU A CA    1 
ATOM   16336 C  C     . LEU A 1 3708 ? 162.934 123.436 177.689 1.00 18.85  ? 3708 LEU A C     1 
ATOM   16337 O  O     . LEU A 1 3708 ? 162.244 122.910 176.807 1.00 23.26  ? 3708 LEU A O     1 
ATOM   16338 C  CB    . LEU A 1 3708 ? 163.289 125.915 177.503 1.00 17.71  ? 3708 LEU A CB    1 
ATOM   16339 C  CG    . LEU A 1 3708 ? 162.990 126.031 176.009 1.00 16.23  ? 3708 LEU A CG    1 
ATOM   16340 C  CD1   . LEU A 1 3708 ? 161.515 126.301 175.778 1.00 15.17  ? 3708 LEU A CD1   1 
ATOM   16341 C  CD2   . LEU A 1 3708 ? 163.835 127.124 175.387 1.00 18.28  ? 3708 LEU A CD2   1 
ATOM   16342 N  N     . GLN A 1 3709 ? 164.028 122.850 178.182 1.00 15.95  ? 3709 GLN A N     1 
ATOM   16343 C  CA    . GLN A 1 3709 ? 164.396 121.503 177.758 1.00 16.40  ? 3709 GLN A CA    1 
ATOM   16344 C  C     . GLN A 1 3709 ? 163.317 120.496 178.133 1.00 20.14  ? 3709 GLN A C     1 
ATOM   16345 O  O     . GLN A 1 3709 ? 162.971 119.618 177.335 1.00 26.74  ? 3709 GLN A O     1 
ATOM   16346 C  CB    . GLN A 1 3709 ? 165.736 121.102 178.374 1.00 18.53  ? 3709 GLN A CB    1 
ATOM   16347 C  CG    . GLN A 1 3709 ? 166.949 121.618 177.625 1.00 22.32  ? 3709 GLN A CG    1 
ATOM   16348 C  CD    . GLN A 1 3709 ? 168.238 121.390 178.387 1.00 28.70  ? 3709 GLN A CD    1 
ATOM   16349 O  OE1   . GLN A 1 3709 ? 168.333 120.478 179.209 1.00 30.90  ? 3709 GLN A OE1   1 
ATOM   16350 N  NE2   . GLN A 1 3709 ? 169.241 122.217 178.116 1.00 34.26  ? 3709 GLN A NE2   1 
ATOM   16351 N  N     . SER A 1 3710 ? 162.776 120.607 179.348 1.00 19.76  ? 3710 SER A N     1 
ATOM   16352 C  CA    . SER A 1 3710 ? 161.703 119.710 179.764 1.00 22.04  ? 3710 SER A CA    1 
ATOM   16353 C  C     . SER A 1 3710 ? 160.442 119.941 178.941 1.00 21.59  ? 3710 SER A C     1 
ATOM   16354 O  O     . SER A 1 3710 ? 159.736 118.987 178.592 1.00 22.27  ? 3710 SER A O     1 
ATOM   16355 C  CB    . SER A 1 3710 ? 161.416 119.892 181.254 1.00 23.19  ? 3710 SER A CB    1 
ATOM   16356 O  OG    . SER A 1 3710 ? 160.397 119.009 181.690 1.00 26.18  ? 3710 SER A OG    1 
ATOM   16357 N  N     . GLN A 1 3711 ? 160.137 121.203 178.632 1.00 19.39  ? 3711 GLN A N     1 
ATOM   16358 C  CA    . GLN A 1 3711 ? 158.966 121.509 177.815 1.00 19.76  ? 3711 GLN A CA    1 
ATOM   16359 C  C     . GLN A 1 3711 ? 159.102 120.918 176.418 1.00 23.01  ? 3711 GLN A C     1 
ATOM   16360 O  O     . GLN A 1 3711 ? 158.150 120.345 175.877 1.00 22.99  ? 3711 GLN A O     1 
ATOM   16361 C  CB    . GLN A 1 3711 ? 158.765 123.023 177.735 1.00 20.88  ? 3711 GLN A CB    1 
ATOM   16362 C  CG    . GLN A 1 3711 ? 158.204 123.653 178.995 1.00 22.55  ? 3711 GLN A CG    1 
ATOM   16363 C  CD    . GLN A 1 3711 ? 158.086 125.159 178.881 1.00 25.47  ? 3711 GLN A CD    1 
ATOM   16364 O  OE1   . GLN A 1 3711 ? 158.498 125.896 179.776 1.00 26.49  ? 3711 GLN A OE1   1 
ATOM   16365 N  NE2   . GLN A 1 3711 ? 157.526 125.626 177.771 1.00 22.32  ? 3711 GLN A NE2   1 
ATOM   16366 N  N     . CYS A 1 3712 ? 160.285 121.053 175.816 1.00 23.09  ? 3712 CYS A N     1 
ATOM   16367 C  CA    . CYS A 1 3712 ? 160.488 120.543 174.464 1.00 18.87  ? 3712 CYS A CA    1 
ATOM   16368 C  C     . CYS A 1 3712 ? 160.597 119.024 174.454 1.00 20.98  ? 3712 CYS A C     1 
ATOM   16369 O  O     . CYS A 1 3712 ? 160.138 118.371 173.510 1.00 26.34  ? 3712 CYS A O     1 
ATOM   16370 C  CB    . CYS A 1 3712 ? 161.730 121.183 173.846 1.00 19.13  ? 3712 CYS A CB    1 
ATOM   16371 S  SG    . CYS A 1 3712 ? 161.608 122.976 173.654 1.00 29.00  ? 3712 CYS A SG    1 
ATOM   16372 N  N     . LEU A 1 3713 ? 161.207 118.443 175.490 1.00 21.22  ? 3713 LEU A N     1 
ATOM   16373 C  CA    . LEU A 1 3713 ? 161.232 116.989 175.605 1.00 24.64  ? 3713 LEU A CA    1 
ATOM   16374 C  C     . LEU A 1 3713 ? 159.826 116.432 175.778 1.00 23.87  ? 3713 LEU A C     1 
ATOM   16375 O  O     . LEU A 1 3713 ? 159.490 115.381 175.221 1.00 26.02  ? 3713 LEU A O     1 
ATOM   16376 C  CB    . LEU A 1 3713 ? 162.127 116.569 176.771 1.00 21.33  ? 3713 LEU A CB    1 
ATOM   16377 C  CG    . LEU A 1 3713 ? 162.195 115.074 177.090 1.00 21.90  ? 3713 LEU A CG    1 
ATOM   16378 C  CD1   . LEU A 1 3713 ? 162.912 114.319 175.984 1.00 26.96  ? 3713 LEU A CD1   1 
ATOM   16379 C  CD2   . LEU A 1 3713 ? 162.878 114.843 178.427 1.00 26.51  ? 3713 LEU A CD2   1 
ATOM   16380 N  N     . ASN A 1 3714 ? 158.991 117.125 176.555 1.00 25.51  ? 3714 ASN A N     1 
ATOM   16381 C  CA    . ASN A 1 3714 ? 157.610 116.692 176.733 1.00 27.88  ? 3714 ASN A CA    1 
ATOM   16382 C  C     . ASN A 1 3714 ? 156.828 116.793 175.430 1.00 28.41  ? 3714 ASN A C     1 
ATOM   16383 O  O     . ASN A 1 3714 ? 156.034 115.903 175.103 1.00 31.73  ? 3714 ASN A O     1 
ATOM   16384 C  CB    . ASN A 1 3714 ? 156.942 117.529 177.822 1.00 29.64  ? 3714 ASN A CB    1 
ATOM   16385 C  CG    . ASN A 1 3714 ? 157.276 117.040 179.212 1.00 35.39  ? 3714 ASN A CG    1 
ATOM   16386 O  OD1   . ASN A 1 3714 ? 156.798 115.995 179.642 1.00 43.83  ? 3714 ASN A OD1   1 
ATOM   16387 N  ND2   . ASN A 1 3714 ? 158.104 117.795 179.924 1.00 31.82  ? 3714 ASN A ND2   1 
ATOM   16388 N  N     . GLU A 1 3715 ? 157.037 117.875 174.675 1.00 28.73  ? 3715 GLU A N     1 
ATOM   16389 C  CA    . GLU A 1 3715 ? 156.288 118.073 173.439 1.00 25.82  ? 3715 GLU A CA    1 
ATOM   16390 C  C     . GLU A 1 3715 ? 156.641 117.014 172.401 1.00 30.71  ? 3715 GLU A C     1 
ATOM   16391 O  O     . GLU A 1 3715 ? 155.759 116.497 171.706 1.00 36.50  ? 3715 GLU A O     1 
ATOM   16392 C  CB    . GLU A 1 3715 ? 156.548 119.476 172.890 1.00 27.01  ? 3715 GLU A CB    1 
ATOM   16393 C  CG    . GLU A 1 3715 ? 155.615 119.888 171.764 1.00 38.28  ? 3715 GLU A CG    1 
ATOM   16394 C  CD    . GLU A 1 3715 ? 154.154 119.809 172.159 1.00 45.16  ? 3715 GLU A CD    1 
ATOM   16395 O  OE1   . GLU A 1 3715 ? 153.800 120.332 173.237 1.00 43.03  ? 3715 GLU A OE1   1 
ATOM   16396 O  OE2   . GLU A 1 3715 ? 153.358 119.226 171.393 1.00 51.40  ? 3715 GLU A OE2   1 
ATOM   16397 N  N     . VAL A 1 3716 ? 157.929 116.682 172.277 1.00 28.79  ? 3716 VAL A N     1 
ATOM   16398 C  CA    . VAL A 1 3716 ? 158.330 115.638 171.340 1.00 27.65  ? 3716 VAL A CA    1 
ATOM   16399 C  C     . VAL A 1 3716 ? 157.827 114.274 171.799 1.00 32.38  ? 3716 VAL A C     1 
ATOM   16400 O  O     . VAL A 1 3716 ? 157.485 113.423 170.969 1.00 34.89  ? 3716 VAL A O     1 
ATOM   16401 C  CB    . VAL A 1 3716 ? 159.858 115.655 171.125 1.00 26.82  ? 3716 VAL A CB    1 
ATOM   16402 C  CG1   . VAL A 1 3716 ? 160.587 114.843 172.186 1.00 29.43  ? 3716 VAL A CG1   1 
ATOM   16403 C  CG2   . VAL A 1 3716 ? 160.198 115.129 169.743 1.00 23.33  ? 3716 VAL A CG2   1 
ATOM   16404 N  N     . LEU A 1 3717 ? 157.775 114.037 173.113 1.00 33.75  ? 3717 LEU A N     1 
ATOM   16405 C  CA    . LEU A 1 3717 ? 157.253 112.769 173.610 1.00 34.55  ? 3717 LEU A CA    1 
ATOM   16406 C  C     . LEU A 1 3717 ? 155.771 112.623 173.291 1.00 35.68  ? 3717 LEU A C     1 
ATOM   16407 O  O     . LEU A 1 3717 ? 155.323 111.549 172.878 1.00 41.40  ? 3717 LEU A O     1 
ATOM   16408 C  CB    . LEU A 1 3717 ? 157.496 112.652 175.114 1.00 39.43  ? 3717 LEU A CB    1 
ATOM   16409 C  CG    . LEU A 1 3717 ? 158.422 111.519 175.562 1.00 40.78  ? 3717 LEU A CG    1 
ATOM   16410 C  CD1   . LEU A 1 3717 ? 158.270 111.259 177.053 1.00 40.72  ? 3717 LEU A CD1   1 
ATOM   16411 C  CD2   . LEU A 1 3717 ? 158.156 110.250 174.763 1.00 33.29  ? 3717 LEU A CD2   1 
ATOM   16412 N  N     . LYS A 1 3718 ? 154.998 113.696 173.472 1.00 37.55  ? 3718 LYS A N     1 
ATOM   16413 C  CA    . LYS A 1 3718 ? 153.580 113.652 173.133 1.00 38.07  ? 3718 LYS A CA    1 
ATOM   16414 C  C     . LYS A 1 3718 ? 153.381 113.473 171.634 1.00 39.03  ? 3718 LYS A C     1 
ATOM   16415 O  O     . LYS A 1 3718 ? 152.418 112.831 171.198 1.00 39.99  ? 3718 LYS A O     1 
ATOM   16416 C  CB    . LYS A 1 3718 ? 152.889 114.925 173.621 1.00 36.50  ? 3718 LYS A CB    1 
ATOM   16417 C  CG    . LYS A 1 3718 ? 151.397 114.775 173.867 1.00 43.58  ? 3718 LYS A CG    1 
ATOM   16418 C  CD    . LYS A 1 3718 ? 150.708 116.129 173.908 1.00 48.92  ? 3718 LYS A CD    1 
ATOM   16419 C  CE    . LYS A 1 3718 ? 150.513 116.609 175.339 1.00 55.23  ? 3718 LYS A CE    1 
ATOM   16420 N  NZ    . LYS A 1 3718 ? 149.740 115.635 176.158 1.00 54.61  ? 3718 LYS A NZ    1 
ATOM   16421 N  N     . ALA A 1 3719 ? 154.284 114.033 170.829 1.00 41.14  ? 3719 ALA A N     1 
ATOM   16422 C  CA    . ALA A 1 3719 ? 154.147 113.958 169.379 1.00 37.94  ? 3719 ALA A CA    1 
ATOM   16423 C  C     . ALA A 1 3719 ? 154.585 112.598 168.849 1.00 40.20  ? 3719 ALA A C     1 
ATOM   16424 O  O     . ALA A 1 3719 ? 153.798 111.873 168.231 1.00 40.78  ? 3719 ALA A O     1 
ATOM   16425 C  CB    . ALA A 1 3719 ? 154.960 115.076 168.724 1.00 37.33  ? 3719 ALA A CB    1 
ATOM   16426 N  N     . GLU A 1 3720 ? 155.849 112.237 169.081 1.00 40.31  ? 3720 GLU A N     1 
ATOM   16427 C  CA    . GLU A 1 3720 ? 156.408 111.048 168.447 1.00 38.10  ? 3720 GLU A CA    1 
ATOM   16428 C  C     . GLU A 1 3720 ? 155.880 109.767 169.081 1.00 39.52  ? 3720 GLU A C     1 
ATOM   16429 O  O     . GLU A 1 3720 ? 155.545 108.811 168.372 1.00 50.49  ? 3720 GLU A O     1 
ATOM   16430 C  CB    . GLU A 1 3720 ? 157.934 111.090 168.517 1.00 39.38  ? 3720 GLU A CB    1 
ATOM   16431 C  CG    . GLU A 1 3720 ? 158.579 111.950 167.445 1.00 38.92  ? 3720 GLU A CG    1 
ATOM   16432 C  CD    . GLU A 1 3720 ? 158.067 111.628 166.056 1.00 43.61  ? 3720 GLU A CD    1 
ATOM   16433 O  OE1   . GLU A 1 3720 ? 158.316 110.503 165.575 1.00 45.68  ? 3720 GLU A OE1   1 
ATOM   16434 O  OE2   . GLU A 1 3720 ? 157.412 112.500 165.447 1.00 45.07  ? 3720 GLU A OE2   1 
ATOM   16435 N  N     . ARG A 1 3721 ? 155.798 109.723 170.408 1.00 38.68  ? 3721 ARG A N     1 
ATOM   16436 C  CA    . ARG A 1 3721 ? 155.454 108.507 171.145 1.00 45.25  ? 3721 ARG A CA    1 
ATOM   16437 C  C     . ARG A 1 3721 ? 154.347 108.817 172.144 1.00 43.90  ? 3721 ARG A C     1 
ATOM   16438 O  O     . ARG A 1 3721 ? 154.582 108.872 173.357 1.00 44.58  ? 3721 ARG A O     1 
ATOM   16439 C  CB    . ARG A 1 3721 ? 156.690 107.937 171.842 1.00 40.09  ? 3721 ARG A CB    1 
ATOM   16440 C  CG    . ARG A 1 3721 ? 157.763 107.449 170.879 1.00 37.84  ? 3721 ARG A CG    1 
ATOM   16441 C  CD    . ARG A 1 3721 ? 158.995 106.950 171.615 1.00 43.15  ? 3721 ARG A CD    1 
ATOM   16442 N  NE    . ARG A 1 3721 ? 158.718 105.768 172.421 1.00 54.60  ? 3721 ARG A NE    1 
ATOM   16443 C  CZ    . ARG A 1 3721 ? 158.787 104.523 171.971 1.00 47.67  ? 3721 ARG A CZ    1 
ATOM   16444 N  NH1   . ARG A 1 3721 ? 159.131 104.259 170.722 1.00 40.97  ? 3721 ARG A NH1   1 
ATOM   16445 N  NH2   . ARG A 1 3721 ? 158.508 103.518 172.796 1.00 50.02  ? 3721 ARG A NH2   1 
ATOM   16446 N  N     . PRO A 1 3722 ? 153.118 109.027 171.662 1.00 47.48  ? 3722 PRO A N     1 
ATOM   16447 C  CA    . PRO A 1 3722 ? 152.038 109.455 172.568 1.00 48.97  ? 3722 PRO A CA    1 
ATOM   16448 C  C     . PRO A 1 3722 ? 151.731 108.466 173.679 1.00 50.58  ? 3722 PRO A C     1 
ATOM   16449 O  O     . PRO A 1 3722 ? 151.364 108.889 174.783 1.00 51.85  ? 3722 PRO A O     1 
ATOM   16450 C  CB    . PRO A 1 3722 ? 150.841 109.631 171.623 1.00 45.71  ? 3722 PRO A CB    1 
ATOM   16451 C  CG    . PRO A 1 3722 ? 151.151 108.765 170.449 1.00 41.61  ? 3722 PRO A CG    1 
ATOM   16452 C  CD    . PRO A 1 3722 ? 152.639 108.811 170.286 1.00 43.86  ? 3722 PRO A CD    1 
ATOM   16453 N  N     . ASP A 1 3723 ? 151.861 107.161 173.424 1.00 51.87  ? 3723 ASP A N     1 
ATOM   16454 C  CA    . ASP A 1 3723 ? 151.584 106.177 174.466 1.00 48.88  ? 3723 ASP A CA    1 
ATOM   16455 C  C     . ASP A 1 3723 ? 152.579 106.292 175.615 1.00 54.56  ? 3723 ASP A C     1 
ATOM   16456 O  O     . ASP A 1 3723 ? 152.201 106.176 176.786 1.00 58.37  ? 3723 ASP A O     1 
ATOM   16457 C  CB    . ASP A 1 3723 ? 151.601 104.766 173.876 1.00 50.85  ? 3723 ASP A CB    1 
ATOM   16458 C  CG    . ASP A 1 3723 ? 152.883 104.462 173.130 1.00 54.27  ? 3723 ASP A CG    1 
ATOM   16459 O  OD1   . ASP A 1 3723 ? 153.071 105.008 172.023 1.00 57.15  ? 3723 ASP A OD1   1 
ATOM   16460 O  OD2   . ASP A 1 3723 ? 153.705 103.680 173.652 1.00 55.11  ? 3723 ASP A OD2   1 
ATOM   16461 N  N     . VAL A 1 3724 ? 153.857 106.510 175.299 1.00 55.19  ? 3724 VAL A N     1 
ATOM   16462 C  CA    . VAL A 1 3724 ? 154.862 106.682 176.343 1.00 51.15  ? 3724 VAL A CA    1 
ATOM   16463 C  C     . VAL A 1 3724 ? 154.585 107.947 177.147 1.00 52.33  ? 3724 VAL A C     1 
ATOM   16464 O  O     . VAL A 1 3724 ? 154.687 107.950 178.380 1.00 60.71  ? 3724 VAL A O     1 
ATOM   16465 C  CB    . VAL A 1 3724 ? 156.274 106.696 175.730 1.00 50.24  ? 3724 VAL A CB    1 
ATOM   16466 C  CG1   . VAL A 1 3724 ? 157.320 106.915 176.810 1.00 53.93  ? 3724 VAL A CG1   1 
ATOM   16467 C  CG2   . VAL A 1 3724 ? 156.538 105.400 174.982 1.00 46.46  ? 3724 VAL A CG2   1 
ATOM   16468 N  N     . ASP A 1 3725 ? 154.234 109.040 176.465 1.00 50.16  ? 3725 ASP A N     1 
ATOM   16469 C  CA    . ASP A 1 3725 ? 153.895 110.274 177.166 1.00 51.13  ? 3725 ASP A CA    1 
ATOM   16470 C  C     . ASP A 1 3725 ? 152.655 110.093 178.034 1.00 58.31  ? 3725 ASP A C     1 
ATOM   16471 O  O     . ASP A 1 3725 ? 152.599 110.602 179.159 1.00 61.22  ? 3725 ASP A O     1 
ATOM   16472 C  CB    . ASP A 1 3725 ? 153.687 111.409 176.165 1.00 49.75  ? 3725 ASP A CB    1 
ATOM   16473 C  CG    . ASP A 1 3725 ? 153.234 112.694 176.829 1.00 53.36  ? 3725 ASP A CG    1 
ATOM   16474 O  OD1   . ASP A 1 3725 ? 154.035 113.293 177.577 1.00 53.42  ? 3725 ASP A OD1   1 
ATOM   16475 O  OD2   . ASP A 1 3725 ? 152.076 113.104 176.605 1.00 50.39  ? 3725 ASP A OD2   1 
ATOM   16476 N  N     . GLU A 1 3726 ? 151.649 109.377 177.524 1.00 58.04  ? 3726 GLU A N     1 
ATOM   16477 C  CA    . GLU A 1 3726 ? 150.458 109.104 178.321 1.00 56.78  ? 3726 GLU A CA    1 
ATOM   16478 C  C     . GLU A 1 3726 ? 150.799 108.270 179.548 1.00 61.37  ? 3726 GLU A C     1 
ATOM   16479 O  O     . GLU A 1 3726 ? 150.281 108.520 180.643 1.00 67.50  ? 3726 GLU A O     1 
ATOM   16480 C  CB    . GLU A 1 3726 ? 149.406 108.398 177.467 1.00 56.64  ? 3726 GLU A CB    1 
ATOM   16481 C  CG    . GLU A 1 3726 ? 148.126 108.059 178.213 1.00 62.83  ? 3726 GLU A CG    1 
ATOM   16482 C  CD    . GLU A 1 3726 ? 147.094 107.394 177.324 1.00 71.08  ? 3726 GLU A CD    1 
ATOM   16483 O  OE1   . GLU A 1 3726 ? 147.392 107.169 176.133 1.00 71.38  ? 3726 GLU A OE1   1 
ATOM   16484 O  OE2   . GLU A 1 3726 ? 145.985 107.098 177.817 1.00 71.65  ? 3726 GLU A OE2   1 
ATOM   16485 N  N     . LYS A 1 3727 ? 151.666 107.268 179.383 1.00 58.73  ? 3727 LYS A N     1 
ATOM   16486 C  CA    . LYS A 1 3727 ? 152.108 106.479 180.528 1.00 58.74  ? 3727 LYS A CA    1 
ATOM   16487 C  C     . LYS A 1 3727 ? 152.876 107.338 181.524 1.00 61.73  ? 3727 LYS A C     1 
ATOM   16488 O  O     . LYS A 1 3727 ? 152.682 107.217 182.738 1.00 67.42  ? 3727 LYS A O     1 
ATOM   16489 C  CB    . LYS A 1 3727 ? 152.968 105.306 180.056 1.00 60.58  ? 3727 LYS A CB    1 
ATOM   16490 C  CG    . LYS A 1 3727 ? 153.473 104.415 181.180 1.00 62.08  ? 3727 LYS A CG    1 
ATOM   16491 C  CD    . LYS A 1 3727 ? 154.589 103.496 180.706 1.00 59.72  ? 3727 LYS A CD    1 
ATOM   16492 C  CE    . LYS A 1 3727 ? 154.213 102.783 179.418 1.00 59.72  ? 3727 LYS A CE    1 
ATOM   16493 N  NZ    . LYS A 1 3727 ? 152.981 101.962 179.579 1.00 60.15  ? 3727 LYS A NZ    1 
ATOM   16494 N  N     . ARG A 1 3728 ? 153.751 108.216 181.027 1.00 58.99  ? 3728 ARG A N     1 
ATOM   16495 C  CA    . ARG A 1 3728 ? 154.535 109.062 181.921 1.00 62.02  ? 3728 ARG A CA    1 
ATOM   16496 C  C     . ARG A 1 3728 ? 153.646 110.029 182.692 1.00 64.03  ? 3728 ARG A C     1 
ATOM   16497 O  O     . ARG A 1 3728 ? 153.847 110.244 183.894 1.00 67.46  ? 3728 ARG A O     1 
ATOM   16498 C  CB    . ARG A 1 3728 ? 155.586 109.833 181.126 1.00 60.31  ? 3728 ARG A CB    1 
ATOM   16499 C  CG    . ARG A 1 3728 ? 156.560 110.611 181.993 1.00 61.32  ? 3728 ARG A CG    1 
ATOM   16500 C  CD    . ARG A 1 3728 ? 157.388 111.562 181.154 1.00 54.93  ? 3728 ARG A CD    1 
ATOM   16501 N  NE    . ARG A 1 3728 ? 156.540 112.579 180.548 1.00 54.18  ? 3728 ARG A NE    1 
ATOM   16502 C  CZ    . ARG A 1 3728 ? 156.069 113.637 181.192 1.00 53.95  ? 3728 ARG A CZ    1 
ATOM   16503 N  NH1   . ARG A 1 3728 ? 156.387 113.876 182.453 1.00 53.03  ? 3728 ARG A NH1   1 
ATOM   16504 N  NH2   . ARG A 1 3728 ? 155.265 114.482 180.551 1.00 52.57  ? 3728 ARG A NH2   1 
ATOM   16505 N  N     . SER A 1 3729 ? 152.663 110.628 182.016 1.00 62.82  ? 3729 SER A N     1 
ATOM   16506 C  CA    . SER A 1 3729 ? 151.778 111.579 182.682 1.00 61.47  ? 3729 SER A CA    1 
ATOM   16507 C  C     . SER A 1 3729 ? 150.947 110.897 183.761 1.00 65.73  ? 3729 SER A C     1 
ATOM   16508 O  O     . SER A 1 3729 ? 150.670 111.490 184.810 1.00 70.73  ? 3729 SER A O     1 
ATOM   16509 C  CB    . SER A 1 3729 ? 150.873 112.262 181.657 1.00 62.01  ? 3729 SER A CB    1 
ATOM   16510 O  OG    . SER A 1 3729 ? 151.628 113.063 180.764 1.00 60.03  ? 3729 SER A OG    1 
ATOM   16511 N  N     . ASP A 1 3730 ? 150.531 109.652 183.516 1.00 65.62  ? 3730 ASP A N     1 
ATOM   16512 C  CA    . ASP A 1 3730 ? 149.798 108.905 184.533 1.00 65.93  ? 3730 ASP A CA    1 
ATOM   16513 C  C     . ASP A 1 3730 ? 150.669 108.635 185.753 1.00 65.28  ? 3730 ASP A C     1 
ATOM   16514 O  O     . ASP A 1 3730 ? 150.197 108.719 186.893 1.00 66.50  ? 3730 ASP A O     1 
ATOM   16515 C  CB    . ASP A 1 3730 ? 149.275 107.596 183.944 1.00 67.97  ? 3730 ASP A CB    1 
ATOM   16516 C  CG    . ASP A 1 3730 ? 148.211 107.816 182.889 1.00 72.32  ? 3730 ASP A CG    1 
ATOM   16517 O  OD1   . ASP A 1 3730 ? 148.085 106.965 181.983 1.00 73.01  ? 3730 ASP A OD1   1 
ATOM   16518 O  OD2   . ASP A 1 3730 ? 147.501 108.841 182.964 1.00 74.34  ? 3730 ASP A OD2   1 
ATOM   16519 N  N     . LEU A 1 3731 ? 151.945 108.308 185.534 1.00 63.93  ? 3731 LEU A N     1 
ATOM   16520 C  CA    . LEU A 1 3731 ? 152.843 108.049 186.655 1.00 65.27  ? 3731 LEU A CA    1 
ATOM   16521 C  C     . LEU A 1 3731 ? 153.146 109.323 187.433 1.00 68.64  ? 3731 LEU A C     1 
ATOM   16522 O  O     . LEU A 1 3731 ? 153.463 109.263 188.627 1.00 70.65  ? 3731 LEU A O     1 
ATOM   16523 C  CB    . LEU A 1 3731 ? 154.135 107.391 186.164 1.00 63.58  ? 3731 LEU A CB    1 
ATOM   16524 C  CG    . LEU A 1 3731 ? 154.161 105.865 186.002 1.00 69.30  ? 3731 LEU A CG    1 
ATOM   16525 C  CD1   . LEU A 1 3731 ? 152.959 105.322 185.237 1.00 64.36  ? 3731 LEU A CD1   1 
ATOM   16526 C  CD2   . LEU A 1 3731 ? 155.457 105.425 185.336 1.00 68.41  ? 3731 LEU A CD2   1 
ATOM   16527 N  N     . LEU A 1 3732 ? 153.065 110.485 186.779 1.00 65.29  ? 3732 LEU A N     1 
ATOM   16528 C  CA    . LEU A 1 3732 ? 153.152 111.744 187.513 1.00 68.60  ? 3732 LEU A CA    1 
ATOM   16529 C  C     . LEU A 1 3732 ? 152.014 111.860 188.518 1.00 69.04  ? 3732 LEU A C     1 
ATOM   16530 O  O     . LEU A 1 3732 ? 152.225 112.230 189.679 1.00 67.33  ? 3732 LEU A O     1 
ATOM   16531 C  CB    . LEU A 1 3732 ? 153.126 112.933 186.550 1.00 71.27  ? 3732 LEU A CB    1 
ATOM   16532 C  CG    . LEU A 1 3732 ? 154.433 113.534 186.026 1.00 71.77  ? 3732 LEU A CG    1 
ATOM   16533 C  CD1   . LEU A 1 3732 ? 155.468 112.467 185.729 1.00 63.65  ? 3732 LEU A CD1   1 
ATOM   16534 C  CD2   . LEU A 1 3732 ? 154.166 114.393 184.799 1.00 68.36  ? 3732 LEU A CD2   1 
ATOM   16535 N  N     . LYS A 1 3733 ? 150.793 111.543 188.083 1.00 67.50  ? 3733 LYS A N     1 
ATOM   16536 C  CA    . LYS A 1 3733 ? 149.639 111.640 188.969 1.00 66.97  ? 3733 LYS A CA    1 
ATOM   16537 C  C     . LYS A 1 3733 ? 149.686 110.572 190.054 1.00 68.27  ? 3733 LYS A C     1 
ATOM   16538 O  O     . LYS A 1 3733 ? 149.385 110.849 191.221 1.00 69.22  ? 3733 LYS A O     1 
ATOM   16539 C  CB    . LYS A 1 3733 ? 148.351 111.528 188.154 1.00 67.11  ? 3733 LYS A CB    1 
ATOM   16540 C  CG    . LYS A 1 3733 ? 147.077 111.697 188.965 1.00 70.23  ? 3733 LYS A CG    1 
ATOM   16541 C  CD    . LYS A 1 3733 ? 145.952 112.287 188.121 1.00 71.50  ? 3733 LYS A CD    1 
ATOM   16542 C  CE    . LYS A 1 3733 ? 146.275 113.685 187.595 1.00 76.38  ? 3733 LYS A CE    1 
ATOM   16543 N  NZ    . LYS A 1 3733 ? 147.228 114.449 188.451 1.00 69.46  ? 3733 LYS A NZ    1 
ATOM   16544 N  N     . LEU A 1 3734 ? 150.057 109.343 189.687 1.00 66.58  ? 3734 LEU A N     1 
ATOM   16545 C  CA    . LEU A 1 3734 ? 150.093 108.256 190.661 1.00 69.10  ? 3734 LEU A CA    1 
ATOM   16546 C  C     . LEU A 1 3734 ? 151.149 108.497 191.732 1.00 68.44  ? 3734 LEU A C     1 
ATOM   16547 O  O     . LEU A 1 3734 ? 150.897 108.278 192.922 1.00 69.17  ? 3734 LEU A O     1 
ATOM   16548 C  CB    . LEU A 1 3734 ? 150.345 106.925 189.951 1.00 67.06  ? 3734 LEU A CB    1 
ATOM   16549 C  CG    . LEU A 1 3734 ? 149.127 106.042 189.666 1.00 63.59  ? 3734 LEU A CG    1 
ATOM   16550 C  CD1   . LEU A 1 3734 ? 148.051 106.815 188.920 1.00 62.82  ? 3734 LEU A CD1   1 
ATOM   16551 C  CD2   . LEU A 1 3734 ? 149.541 104.805 188.884 1.00 66.10  ? 3734 LEU A CD2   1 
ATOM   16552 N  N     . GLN A 1 3735 ? 152.342 108.945 191.330 1.00 68.23  ? 3735 GLN A N     1 
ATOM   16553 C  CA    . GLN A 1 3735 ? 153.411 109.167 192.299 1.00 66.45  ? 3735 GLN A CA    1 
ATOM   16554 C  C     . GLN A 1 3735 ? 153.072 110.309 193.249 1.00 63.39  ? 3735 GLN A C     1 
ATOM   16555 O  O     . GLN A 1 3735 ? 153.344 110.222 194.452 1.00 62.67  ? 3735 GLN A O     1 
ATOM   16556 C  CB    . GLN A 1 3735 ? 154.729 109.445 191.578 1.00 68.30  ? 3735 GLN A CB    1 
ATOM   16557 C  CG    . GLN A 1 3735 ? 155.675 108.258 191.536 1.00 68.79  ? 3735 GLN A CG    1 
ATOM   16558 C  CD    . GLN A 1 3735 ? 156.397 108.143 190.210 1.00 73.02  ? 3735 GLN A CD    1 
ATOM   16559 O  OE1   . GLN A 1 3735 ? 156.598 109.137 189.513 1.00 69.88  ? 3735 GLN A OE1   1 
ATOM   16560 N  NE2   . GLN A 1 3735 ? 156.790 106.926 189.852 1.00 74.46  ? 3735 GLN A NE2   1 
ATOM   16561 N  N     . GLY A 1 3736 ? 152.487 111.389 192.727 1.00 65.86  ? 3736 GLY A N     1 
ATOM   16562 C  CA    . GLY A 1 3736 ? 152.121 112.504 193.586 1.00 62.02  ? 3736 GLY A CA    1 
ATOM   16563 C  C     . GLY A 1 3736 ? 151.080 112.120 194.620 1.00 65.33  ? 3736 GLY A C     1 
ATOM   16564 O  O     . GLY A 1 3736 ? 151.161 112.522 195.783 1.00 66.43  ? 3736 GLY A O     1 
ATOM   16565 N  N     . GLU A 1 3737 ? 150.084 111.334 194.205 1.00 70.64  ? 3737 GLU A N     1 
ATOM   16566 C  CA    . GLU A 1 3737 ? 149.078 110.854 195.147 1.00 66.10  ? 3737 GLU A CA    1 
ATOM   16567 C  C     . GLU A 1 3737 ? 149.693 109.925 196.185 1.00 68.55  ? 3737 GLU A C     1 
ATOM   16568 O  O     . GLU A 1 3737 ? 149.338 109.982 197.368 1.00 75.51  ? 3737 GLU A O     1 
ATOM   16569 C  CB    . GLU A 1 3737 ? 147.950 110.150 194.393 1.00 68.33  ? 3737 GLU A CB    1 
ATOM   16570 C  CG    . GLU A 1 3737 ? 147.104 111.079 193.538 1.00 73.09  ? 3737 GLU A CG    1 
ATOM   16571 C  CD    . GLU A 1 3737 ? 146.236 110.330 192.547 1.00 85.56  ? 3737 GLU A CD    1 
ATOM   16572 O  OE1   . GLU A 1 3737 ? 146.319 109.085 192.504 1.00 85.13  ? 3737 GLU A OE1   1 
ATOM   16573 O  OE2   . GLU A 1 3737 ? 145.472 110.987 191.808 1.00 87.90  ? 3737 GLU A OE2   1 
ATOM   16574 N  N     . PHE A 1 3738 ? 150.612 109.054 195.759 1.00 65.15  ? 3738 PHE A N     1 
ATOM   16575 C  CA    . PHE A 1 3738 ? 151.260 108.142 196.697 1.00 63.89  ? 3738 PHE A CA    1 
ATOM   16576 C  C     . PHE A 1 3738 ? 152.106 108.900 197.712 1.00 68.67  ? 3738 PHE A C     1 
ATOM   16577 O  O     . PHE A 1 3738 ? 152.104 108.564 198.903 1.00 74.64  ? 3738 PHE A O     1 
ATOM   16578 C  CB    . PHE A 1 3738 ? 152.113 107.127 195.937 1.00 67.64  ? 3738 PHE A CB    1 
ATOM   16579 C  CG    . PHE A 1 3738 ? 151.314 106.156 195.114 1.00 74.67  ? 3738 PHE A CG    1 
ATOM   16580 C  CD1   . PHE A 1 3738 ? 149.959 105.977 195.347 1.00 73.96  ? 3738 PHE A CD1   1 
ATOM   16581 C  CD2   . PHE A 1 3738 ? 151.917 105.424 194.105 1.00 76.43  ? 3738 PHE A CD2   1 
ATOM   16582 C  CE1   . PHE A 1 3738 ? 149.223 105.086 194.590 1.00 71.41  ? 3738 PHE A CE1   1 
ATOM   16583 C  CE2   . PHE A 1 3738 ? 151.186 104.532 193.345 1.00 77.14  ? 3738 PHE A CE2   1 
ATOM   16584 C  CZ    . PHE A 1 3738 ? 149.837 104.362 193.588 1.00 76.06  ? 3738 PHE A CZ    1 
ATOM   16585 N  N     . GLN A 1 3739 ? 152.843 109.918 197.262 1.00 69.72  ? 3739 GLN A N     1 
ATOM   16586 C  CA    . GLN A 1 3739 ? 153.617 110.735 198.191 1.00 69.30  ? 3739 GLN A CA    1 
ATOM   16587 C  C     . GLN A 1 3739 ? 152.703 111.505 199.135 1.00 64.65  ? 3739 GLN A C     1 
ATOM   16588 O  O     . GLN A 1 3739 ? 153.004 111.646 200.326 1.00 65.02  ? 3739 GLN A O     1 
ATOM   16589 C  CB    . GLN A 1 3739 ? 154.526 111.692 197.419 1.00 66.38  ? 3739 GLN A CB    1 
ATOM   16590 C  CG    . GLN A 1 3739 ? 155.617 110.998 196.621 1.00 62.49  ? 3739 GLN A CG    1 
ATOM   16591 C  CD    . GLN A 1 3739 ? 156.416 110.018 197.457 1.00 70.37  ? 3739 GLN A CD    1 
ATOM   16592 O  OE1   . GLN A 1 3739 ? 157.101 110.406 198.404 1.00 73.13  ? 3739 GLN A OE1   1 
ATOM   16593 N  NE2   . GLN A 1 3739 ? 156.330 108.739 197.113 1.00 73.25  ? 3739 GLN A NE2   1 
ATOM   16594 N  N     . LEU A 1 3740 ? 151.586 112.021 198.617 1.00 66.42  ? 3740 LEU A N     1 
ATOM   16595 C  CA    . LEU A 1 3740 ? 150.612 112.691 199.473 1.00 65.93  ? 3740 LEU A CA    1 
ATOM   16596 C  C     . LEU A 1 3740 ? 150.011 111.723 200.483 1.00 67.97  ? 3740 LEU A C     1 
ATOM   16597 O  O     . LEU A 1 3740 ? 149.843 112.064 201.660 1.00 72.18  ? 3740 LEU A O     1 
ATOM   16598 C  CB    . LEU A 1 3740 ? 149.516 113.327 198.619 1.00 62.95  ? 3740 LEU A CB    1 
ATOM   16599 C  CG    . LEU A 1 3740 ? 148.257 113.808 199.343 1.00 65.46  ? 3740 LEU A CG    1 
ATOM   16600 C  CD1   . LEU A 1 3740 ? 148.598 114.875 200.371 1.00 64.77  ? 3740 LEU A CD1   1 
ATOM   16601 C  CD2   . LEU A 1 3740 ? 147.229 114.326 198.348 1.00 61.24  ? 3740 LEU A CD2   1 
ATOM   16602 N  N     . ARG A 1 3741 ? 149.678 110.509 200.039 1.00 67.77  ? 3741 ARG A N     1 
ATOM   16603 C  CA    . ARG A 1 3741 ? 149.117 109.512 200.946 1.00 72.34  ? 3741 ARG A CA    1 
ATOM   16604 C  C     . ARG A 1 3741 ? 150.133 109.125 202.017 1.00 71.64  ? 3741 ARG A C     1 
ATOM   16605 O  O     . ARG A 1 3741 ? 149.783 109.001 203.197 1.00 76.08  ? 3741 ARG A O     1 
ATOM   16606 C  CB    . ARG A 1 3741 ? 148.661 108.291 200.141 1.00 73.34  ? 3741 ARG A CB    1 
ATOM   16607 C  CG    . ARG A 1 3741 ? 148.309 107.024 200.926 1.00 77.77  ? 3741 ARG A CG    1 
ATOM   16608 C  CD    . ARG A 1 3741 ? 147.454 107.287 202.162 1.00 79.87  ? 3741 ARG A CD    1 
ATOM   16609 N  NE    . ARG A 1 3741 ? 146.280 108.100 201.870 1.00 80.12  ? 3741 ARG A NE    1 
ATOM   16610 C  CZ    . ARG A 1 3741 ? 145.207 108.169 202.646 1.00 81.85  ? 3741 ARG A CZ    1 
ATOM   16611 N  NH1   . ARG A 1 3741 ? 145.124 107.480 203.772 1.00 80.52  ? 3741 ARG A NH1   1 
ATOM   16612 N  NH2   . ARG A 1 3741 ? 144.193 108.950 202.284 1.00 81.13  ? 3741 ARG A NH2   1 
ATOM   16613 N  N     . LEU A 1 3742 ? 151.399 108.953 201.627 1.00 68.18  ? 3742 LEU A N     1 
ATOM   16614 C  CA    . LEU A 1 3742 ? 152.435 108.617 202.599 1.00 69.41  ? 3742 LEU A CA    1 
ATOM   16615 C  C     . LEU A 1 3742 ? 152.596 109.716 203.641 1.00 75.89  ? 3742 LEU A C     1 
ATOM   16616 O  O     . LEU A 1 3742 ? 152.772 109.433 204.831 1.00 80.69  ? 3742 LEU A O     1 
ATOM   16617 C  CB    . LEU A 1 3742 ? 153.762 108.358 201.884 1.00 68.11  ? 3742 LEU A CB    1 
ATOM   16618 C  CG    . LEU A 1 3742 ? 154.060 106.915 201.473 1.00 71.97  ? 3742 LEU A CG    1 
ATOM   16619 C  CD1   . LEU A 1 3742 ? 155.507 106.776 201.031 1.00 70.80  ? 3742 LEU A CD1   1 
ATOM   16620 C  CD2   . LEU A 1 3742 ? 153.752 105.956 202.612 1.00 75.45  ? 3742 LEU A CD2   1 
ATOM   16621 N  N     . ARG A 1 3743 ? 152.549 110.979 203.210 1.00 74.35  ? 3743 ARG A N     1 
ATOM   16622 C  CA    . ARG A 1 3743 ? 152.643 112.087 204.155 1.00 70.96  ? 3743 ARG A CA    1 
ATOM   16623 C  C     . ARG A 1 3743 ? 151.449 112.108 205.101 1.00 75.14  ? 3743 ARG A C     1 
ATOM   16624 O  O     . ARG A 1 3743 ? 151.602 112.371 206.300 1.00 76.88  ? 3743 ARG A O     1 
ATOM   16625 C  CB    . ARG A 1 3743 ? 152.757 113.410 203.401 1.00 65.43  ? 3743 ARG A CB    1 
ATOM   16626 C  CG    . ARG A 1 3743 ? 154.138 113.672 202.822 1.00 62.03  ? 3743 ARG A CG    1 
ATOM   16627 C  CD    . ARG A 1 3743 ? 154.250 115.087 202.284 1.00 55.86  ? 3743 ARG A CD    1 
ATOM   16628 N  NE    . ARG A 1 3743 ? 153.861 115.164 200.881 1.00 57.61  ? 3743 ARG A NE    1 
ATOM   16629 C  CZ    . ARG A 1 3743 ? 152.734 115.712 200.446 1.00 57.02  ? 3743 ARG A CZ    1 
ATOM   16630 N  NH1   . ARG A 1 3743 ? 151.855 116.241 201.281 1.00 52.88  ? 3743 ARG A NH1   1 
ATOM   16631 N  NH2   . ARG A 1 3743 ? 152.483 115.728 199.140 1.00 54.61  ? 3743 ARG A NH2   1 
ATOM   16632 N  N     . GLN A 1 3744 ? 150.249 111.840 204.579 1.00 76.01  ? 3744 GLN A N     1 
ATOM   16633 C  CA    . GLN A 1 3744 ? 149.064 111.798 205.431 1.00 73.96  ? 3744 GLN A CA    1 
ATOM   16634 C  C     . GLN A 1 3744 ? 149.162 110.678 206.458 1.00 77.68  ? 3744 GLN A C     1 
ATOM   16635 O  O     . GLN A 1 3744 ? 148.795 110.861 207.625 1.00 78.66  ? 3744 GLN A O     1 
ATOM   16636 C  CB    . GLN A 1 3744 ? 147.808 111.630 204.575 1.00 71.76  ? 3744 GLN A CB    1 
ATOM   16637 C  CG    . GLN A 1 3744 ? 147.340 112.905 203.895 1.00 73.44  ? 3744 GLN A CG    1 
ATOM   16638 C  CD    . GLN A 1 3744 ? 146.286 112.645 202.837 1.00 74.43  ? 3744 GLN A CD    1 
ATOM   16639 O  OE1   . GLN A 1 3744 ? 146.301 111.611 202.170 1.00 80.31  ? 3744 GLN A OE1   1 
ATOM   16640 N  NE2   . GLN A 1 3744 ? 145.362 113.586 202.679 1.00 66.83  ? 3744 GLN A NE2   1 
ATOM   16641 N  N     . LEU A 1 3745 ? 149.650 109.507 206.042 1.00 79.81  ? 3745 LEU A N     1 
ATOM   16642 C  CA    . LEU A 1 3745 ? 149.776 108.385 206.966 1.00 81.02  ? 3745 LEU A CA    1 
ATOM   16643 C  C     . LEU A 1 3745 ? 150.793 108.678 208.061 1.00 81.36  ? 3745 LEU A C     1 
ATOM   16644 O  O     . LEU A 1 3745 ? 150.582 108.320 209.226 1.00 85.32  ? 3745 LEU A O     1 
ATOM   16645 C  CB    . LEU A 1 3745 ? 150.158 107.117 206.203 1.00 81.23  ? 3745 LEU A CB    1 
ATOM   16646 C  CG    . LEU A 1 3745 ? 149.084 106.542 205.279 1.00 81.12  ? 3745 LEU A CG    1 
ATOM   16647 C  CD1   . LEU A 1 3745 ? 149.476 105.160 204.791 1.00 85.87  ? 3745 LEU A CD1   1 
ATOM   16648 C  CD2   . LEU A 1 3745 ? 147.731 106.504 205.974 1.00 79.83  ? 3745 LEU A CD2   1 
ATOM   16649 N  N     . GLU A 1 3746 ? 151.909 109.320 207.706 1.00 80.55  ? 3746 GLU A N     1 
ATOM   16650 C  CA    . GLU A 1 3746 ? 152.921 109.655 208.702 1.00 81.74  ? 3746 GLU A CA    1 
ATOM   16651 C  C     . GLU A 1 3746 ? 152.369 110.627 209.738 1.00 85.61  ? 3746 GLU A C     1 
ATOM   16652 O  O     . GLU A 1 3746 ? 152.607 110.473 210.941 1.00 89.45  ? 3746 GLU A O     1 
ATOM   16653 C  CB    . GLU A 1 3746 ? 154.156 110.239 208.016 1.00 83.30  ? 3746 GLU A CB    1 
ATOM   16654 C  CG    . GLU A 1 3746 ? 155.266 110.648 208.972 1.00 87.72  ? 3746 GLU A CG    1 
ATOM   16655 C  CD    . GLU A 1 3746 ? 155.927 109.460 209.642 1.00 95.99  ? 3746 GLU A CD    1 
ATOM   16656 O  OE1   . GLU A 1 3746 ? 155.967 108.374 209.025 1.00 94.26  ? 3746 GLU A OE1   1 
ATOM   16657 O  OE2   . GLU A 1 3746 ? 156.408 109.611 210.785 1.00 101.99 ? 3746 GLU A OE2   1 
ATOM   16658 N  N     . LYS A 1 3747 ? 151.630 111.642 209.284 1.00 85.24  ? 3747 LYS A N     1 
ATOM   16659 C  CA    . LYS A 1 3747 ? 151.015 112.582 210.216 1.00 82.45  ? 3747 LYS A CA    1 
ATOM   16660 C  C     . LYS A 1 3747 ? 149.958 111.897 211.072 1.00 86.23  ? 3747 LYS A C     1 
ATOM   16661 O  O     . LYS A 1 3747 ? 149.881 112.133 212.284 1.00 91.64  ? 3747 LYS A O     1 
ATOM   16662 C  CB    . LYS A 1 3747 ? 150.411 113.758 209.448 1.00 75.36  ? 3747 LYS A CB    1 
ATOM   16663 C  CG    . LYS A 1 3747 ? 149.516 114.660 210.280 1.00 74.40  ? 3747 LYS A CG    1 
ATOM   16664 C  CD    . LYS A 1 3747 ? 148.973 115.811 209.449 1.00 76.51  ? 3747 LYS A CD    1 
ATOM   16665 C  CE    . LYS A 1 3747 ? 150.098 116.673 208.899 1.00 78.06  ? 3747 LYS A CE    1 
ATOM   16666 N  NZ    . LYS A 1 3747 ? 149.582 117.848 208.142 1.00 75.33  ? 3747 LYS A NZ    1 
ATOM   16667 N  N     . SER A 1 3748 ? 149.132 111.045 210.459 1.00 84.58  ? 3748 SER A N     1 
ATOM   16668 C  CA    . SER A 1 3748 ? 148.108 110.330 211.214 1.00 85.05  ? 3748 SER A CA    1 
ATOM   16669 C  C     . SER A 1 3748 ? 148.729 109.369 212.219 1.00 88.84  ? 3748 SER A C     1 
ATOM   16670 O  O     . SER A 1 3748 ? 148.248 109.252 213.353 1.00 88.41  ? 3748 SER A O     1 
ATOM   16671 C  CB    . SER A 1 3748 ? 147.178 109.582 210.258 1.00 82.01  ? 3748 SER A CB    1 
ATOM   16672 O  OG    . SER A 1 3748 ? 147.791 108.401 209.771 1.00 84.08  ? 3748 SER A OG    1 
ATOM   16673 N  N     . LEU A 1 3749 ? 149.792 108.665 211.821 1.00 88.89  ? 3749 LEU A N     1 
ATOM   16674 C  CA    . LEU A 1 3749 ? 150.469 107.759 212.744 1.00 89.21  ? 3749 LEU A CA    1 
ATOM   16675 C  C     . LEU A 1 3749 ? 151.074 108.521 213.915 1.00 93.78  ? 3749 LEU A C     1 
ATOM   16676 O  O     . LEU A 1 3749 ? 150.991 108.075 215.066 1.00 96.71  ? 3749 LEU A O     1 
ATOM   16677 C  CB    . LEU A 1 3749 ? 151.543 106.962 212.001 1.00 86.62  ? 3749 LEU A CB    1 
ATOM   16678 C  CG    . LEU A 1 3749 ? 152.105 105.710 212.679 1.00 92.18  ? 3749 LEU A CG    1 
ATOM   16679 C  CD1   . LEU A 1 3749 ? 152.405 104.639 211.643 1.00 91.42  ? 3749 LEU A CD1   1 
ATOM   16680 C  CD2   . LEU A 1 3749 ? 153.358 106.039 213.476 1.00 93.94  ? 3749 LEU A CD2   1 
ATOM   16681 N  N     . LEU A 1 3750 ? 151.695 109.670 213.641 1.00 94.27  ? 3750 LEU A N     1 
ATOM   16682 C  CA    . LEU A 1 3750 ? 152.232 110.497 214.717 1.00 94.05  ? 3750 LEU A CA    1 
ATOM   16683 C  C     . LEU A 1 3750 ? 151.117 111.044 215.600 1.00 92.42  ? 3750 LEU A C     1 
ATOM   16684 O  O     . LEU A 1 3750 ? 151.241 111.060 216.830 1.00 93.10  ? 3750 LEU A O     1 
ATOM   16685 C  CB    . LEU A 1 3750 ? 153.065 111.637 214.133 1.00 90.92  ? 3750 LEU A CB    1 
ATOM   16686 C  CG    . LEU A 1 3750 ? 153.992 112.378 215.098 1.00 91.68  ? 3750 LEU A CG    1 
ATOM   16687 C  CD1   . LEU A 1 3750 ? 154.797 111.397 215.933 1.00 90.29  ? 3750 LEU A CD1   1 
ATOM   16688 C  CD2   . LEU A 1 3750 ? 154.911 113.324 214.338 1.00 90.12  ? 3750 LEU A CD2   1 
ATOM   16689 N  N     . GLN A 1 3751 ? 150.018 111.494 214.988 1.00 91.61  ? 3751 GLN A N     1 
ATOM   16690 C  CA    . GLN A 1 3751 ? 148.925 112.084 215.755 1.00 91.90  ? 3751 GLN A CA    1 
ATOM   16691 C  C     . GLN A 1 3751 ? 148.280 111.062 216.683 1.00 94.45  ? 3751 GLN A C     1 
ATOM   16692 O  O     . GLN A 1 3751 ? 147.924 111.386 217.822 1.00 97.68  ? 3751 GLN A O     1 
ATOM   16693 C  CB    . GLN A 1 3751 ? 147.886 112.683 214.806 1.00 89.38  ? 3751 GLN A CB    1 
ATOM   16694 C  CG    . GLN A 1 3751 ? 146.535 112.958 215.447 1.00 90.77  ? 3751 GLN A CG    1 
ATOM   16695 C  CD    . GLN A 1 3751 ? 145.405 112.991 214.437 1.00 93.20  ? 3751 GLN A CD    1 
ATOM   16696 O  OE1   . GLN A 1 3751 ? 145.404 113.809 213.517 1.00 94.25  ? 3751 GLN A OE1   1 
ATOM   16697 N  NE2   . GLN A 1 3751 ? 144.435 112.100 214.605 1.00 91.70  ? 3751 GLN A NE2   1 
ATOM   16698 N  N     . ALA A 1 3752 ? 148.118 109.823 216.212 1.00 95.92  ? 3752 ALA A N     1 
ATOM   16699 C  CA    . ALA A 1 3752 ? 147.507 108.789 217.042 1.00 96.00  ? 3752 ALA A CA    1 
ATOM   16700 C  C     . ALA A 1 3752 ? 148.329 108.532 218.298 1.00 98.49  ? 3752 ALA A C     1 
ATOM   16701 O  O     . ALA A 1 3752 ? 147.775 108.393 219.395 1.00 102.37 ? 3752 ALA A O     1 
ATOM   16702 C  CB    . ALA A 1 3752 ? 147.335 107.502 216.237 1.00 93.17  ? 3752 ALA A CB    1 
ATOM   16703 N  N     . LEU A 1 3753 ? 149.655 108.465 218.158 1.00 94.58  ? 3753 LEU A N     1 
ATOM   16704 C  CA    . LEU A 1 3753 ? 150.515 108.302 219.323 1.00 96.72  ? 3753 LEU A CA    1 
ATOM   16705 C  C     . LEU A 1 3753 ? 150.579 109.562 220.175 1.00 100.09 ? 3753 LEU A C     1 
ATOM   16706 O  O     . LEU A 1 3753 ? 150.940 109.481 221.353 1.00 102.50 ? 3753 LEU A O     1 
ATOM   16707 C  CB    . LEU A 1 3753 ? 151.922 107.892 218.888 1.00 97.66  ? 3753 LEU A CB    1 
ATOM   16708 C  CG    . LEU A 1 3753 ? 152.032 106.504 218.254 1.00 98.25  ? 3753 LEU A CG    1 
ATOM   16709 C  CD1   . LEU A 1 3753 ? 153.439 106.252 217.739 1.00 98.26  ? 3753 LEU A CD1   1 
ATOM   16710 C  CD2   . LEU A 1 3753 ? 151.625 105.432 219.251 1.00 100.26 ? 3753 LEU A CD2   1 
ATOM   16711 N  N     . ASN A 1 3754 ? 150.249 110.723 219.606 1.00 100.06 ? 3754 ASN A N     1 
ATOM   16712 C  CA    . ASN A 1 3754 ? 150.218 111.950 220.395 1.00 98.74  ? 3754 ASN A CA    1 
ATOM   16713 C  C     . ASN A 1 3754 ? 148.964 112.034 221.257 1.00 97.91  ? 3754 ASN A C     1 
ATOM   16714 O  O     . ASN A 1 3754 ? 149.011 112.562 222.373 1.00 98.61  ? 3754 ASN A O     1 
ATOM   16715 C  CB    . ASN A 1 3754 ? 150.319 113.170 219.479 1.00 99.23  ? 3754 ASN A CB    1 
ATOM   16716 C  CG    . ASN A 1 3754 ? 151.677 113.290 218.816 1.00 100.45 ? 3754 ASN A CG    1 
ATOM   16717 O  OD1   . ASN A 1 3754 ? 152.686 112.835 219.355 1.00 97.63  ? 3754 ASN A OD1   1 
ATOM   16718 N  ND2   . ASN A 1 3754 ? 151.709 113.906 217.640 1.00 96.99  ? 3754 ASN A ND2   1 
ATOM   16719 N  N     . GLU A 1 3755 ? 147.840 111.522 220.761 1.00 99.40  ? 3755 GLU A N     1 
ATOM   16720 C  CA    . GLU A 1 3755 ? 146.565 111.625 221.458 1.00 100.12 ? 3755 GLU A CA    1 
ATOM   16721 C  C     . GLU A 1 3755 ? 146.197 110.369 222.237 1.00 99.86  ? 3755 GLU A C     1 
ATOM   16722 O  O     . GLU A 1 3755 ? 145.135 110.343 222.869 1.00 95.56  ? 3755 GLU A O     1 
ATOM   16723 C  CB    . GLU A 1 3755 ? 145.449 111.956 220.462 1.00 98.13  ? 3755 GLU A CB    1 
ATOM   16724 C  CG    . GLU A 1 3755 ? 145.726 113.182 219.607 1.00 97.18  ? 3755 GLU A CG    1 
ATOM   16725 C  CD    . GLU A 1 3755 ? 146.321 114.327 220.405 1.00 99.91  ? 3755 GLU A CD    1 
ATOM   16726 O  OE1   . GLU A 1 3755 ? 145.655 114.808 221.345 1.00 100.89 ? 3755 GLU A OE1   1 
ATOM   16727 O  OE2   . GLU A 1 3755 ? 147.456 114.744 220.093 1.00 95.97  ? 3755 GLU A OE2   1 
ATOM   16728 N  N     . VAL A 1 3756 ? 147.034 109.330 222.213 1.00 104.12 ? 3756 VAL A N     1 
ATOM   16729 C  CA    . VAL A 1 3756 ? 146.737 108.125 222.977 1.00 105.49 ? 3756 VAL A CA    1 
ATOM   16730 C  C     . VAL A 1 3756 ? 147.003 108.383 224.454 1.00 106.14 ? 3756 VAL A C     1 
ATOM   16731 O  O     . VAL A 1 3756 ? 148.017 108.988 224.831 1.00 104.47 ? 3756 VAL A O     1 
ATOM   16732 C  CB    . VAL A 1 3756 ? 147.552 106.930 222.450 1.00 109.02 ? 3756 VAL A CB    1 
ATOM   16733 C  CG1   . VAL A 1 3756 ? 149.046 107.200 222.541 1.00 105.83 ? 3756 VAL A CG1   1 
ATOM   16734 C  CG2   . VAL A 1 3756 ? 147.186 105.659 223.206 1.00 107.87 ? 3756 VAL A CG2   1 
ATOM   16735 N  N     . LYS A 1 3757 ? 146.076 107.944 225.301 1.00 108.92 ? 3757 LYS A N     1 
ATOM   16736 C  CA    . LYS A 1 3757 ? 146.159 108.165 226.738 1.00 106.30 ? 3757 LYS A CA    1 
ATOM   16737 C  C     . LYS A 1 3757 ? 146.567 106.872 227.430 1.00 106.39 ? 3757 LYS A C     1 
ATOM   16738 O  O     . LYS A 1 3757 ? 145.960 105.820 227.202 1.00 107.89 ? 3757 LYS A O     1 
ATOM   16739 C  CB    . LYS A 1 3757 ? 144.822 108.663 227.289 1.00 100.63 ? 3757 LYS A CB    1 
ATOM   16740 C  CG    . LYS A 1 3757 ? 144.172 109.754 226.452 1.00 98.36  ? 3757 LYS A CG    1 
ATOM   16741 C  CD    . LYS A 1 3757 ? 145.087 110.959 226.297 1.00 101.39 ? 3757 LYS A CD    1 
ATOM   16742 C  CE    . LYS A 1 3757 ? 145.327 111.652 227.628 1.00 97.33  ? 3757 LYS A CE    1 
ATOM   16743 N  NZ    . LYS A 1 3757 ? 146.223 112.832 227.481 1.00 87.88  ? 3757 LYS A NZ    1 
ATOM   16744 N  N     . GLY A 1 3758 ? 147.592 106.955 228.273 1.00 107.40 ? 3758 GLY A N     1 
ATOM   16745 C  CA    . GLY A 1 3758 ? 148.082 105.790 228.982 1.00 111.48 ? 3758 GLY A CA    1 
ATOM   16746 C  C     . GLY A 1 3758 ? 149.084 104.985 228.182 1.00 112.71 ? 3758 GLY A C     1 
ATOM   16747 O  O     . GLY A 1 3758 ? 150.178 105.468 227.875 1.00 110.17 ? 3758 GLY A O     1 
ATOM   16748 N  N     . ARG A 1 3759 ? 148.721 103.752 227.836 1.00 116.97 ? 3759 ARG A N     1 
ATOM   16749 C  CA    . ARG A 1 3759 ? 149.586 102.862 227.078 1.00 119.80 ? 3759 ARG A CA    1 
ATOM   16750 C  C     . ARG A 1 3759 ? 148.825 102.312 225.879 1.00 120.01 ? 3759 ARG A C     1 
ATOM   16751 O  O     . ARG A 1 3759 ? 147.592 102.274 225.862 1.00 119.14 ? 3759 ARG A O     1 
ATOM   16752 C  CB    . ARG A 1 3759 ? 150.115 101.710 227.946 1.00 118.61 ? 3759 ARG A CB    1 
ATOM   16753 C  CG    . ARG A 1 3759 ? 150.594 102.143 229.325 1.00 114.50 ? 3759 ARG A CG    1 
ATOM   16754 C  CD    . ARG A 1 3759 ? 150.647 100.973 230.294 1.00 115.02 ? 3759 ARG A CD    1 
ATOM   16755 N  NE    . ARG A 1 3759 ? 149.350 100.330 230.462 1.00 118.47 ? 3759 ARG A NE    1 
ATOM   16756 C  CZ    . ARG A 1 3759 ? 149.114 99.329  231.299 1.00 114.21 ? 3759 ARG A CZ    1 
ATOM   16757 N  NH1   . ARG A 1 3759 ? 150.070 98.829  232.065 1.00 109.77 ? 3759 ARG A NH1   1 
ATOM   16758 N  NH2   . ARG A 1 3759 ? 147.889 98.817  231.370 1.00 110.99 ? 3759 ARG A NH2   1 
ATOM   16759 N  N     . ILE A 1 3760 ? 149.585 101.892 224.865 1.00 118.45 ? 3760 ILE A N     1 
ATOM   16760 C  CA    . ILE A 1 3760 ? 148.978 101.385 223.638 1.00 118.94 ? 3760 ILE A CA    1 
ATOM   16761 C  C     . ILE A 1 3760 ? 148.234 100.082 223.904 1.00 121.13 ? 3760 ILE A C     1 
ATOM   16762 O  O     . ILE A 1 3760 ? 147.168 99.832  223.328 1.00 120.46 ? 3760 ILE A O     1 
ATOM   16763 C  CB    . ILE A 1 3760 ? 150.048 101.215 222.545 1.00 116.05 ? 3760 ILE A CB    1 
ATOM   16764 C  CG1   . ILE A 1 3760 ? 150.861 102.502 222.391 1.00 113.50 ? 3760 ILE A CG1   1 
ATOM   16765 C  CG2   . ILE A 1 3760 ? 149.405 100.833 221.222 1.00 115.52 ? 3760 ILE A CG2   1 
ATOM   16766 C  CD1   . ILE A 1 3760 ? 151.935 102.420 221.329 1.00 106.69 ? 3760 ILE A CD1   1 
ATOM   16767 N  N     . LEU A 1 3761 ? 148.780 99.231  224.776 1.00 119.95 ? 3761 LEU A N     1 
ATOM   16768 C  CA    . LEU A 1 3761 ? 148.134 97.958  225.080 1.00 117.93 ? 3761 LEU A CA    1 
ATOM   16769 C  C     . LEU A 1 3761 ? 146.795 98.152  225.781 1.00 118.20 ? 3761 LEU A C     1 
ATOM   16770 O  O     . LEU A 1 3761 ? 145.933 97.268  225.717 1.00 115.45 ? 3761 LEU A O     1 
ATOM   16771 C  CB    . LEU A 1 3761 ? 149.054 97.090  225.940 1.00 117.57 ? 3761 LEU A CB    1 
ATOM   16772 C  CG    . LEU A 1 3761 ? 150.376 96.618  225.332 1.00 115.31 ? 3761 LEU A CG    1 
ATOM   16773 C  CD1   . LEU A 1 3761 ? 151.494 97.607  225.619 1.00 112.40 ? 3761 LEU A CD1   1 
ATOM   16774 C  CD2   . LEU A 1 3761 ? 150.733 95.239  225.861 1.00 112.32 ? 3761 LEU A CD2   1 
ATOM   16775 N  N     . ASP A 1 3762 ? 146.606 99.287  226.459 1.00 120.22 ? 3762 ASP A N     1 
ATOM   16776 C  CA    . ASP A 1 3762 ? 145.367 99.514  227.197 1.00 117.75 ? 3762 ASP A CA    1 
ATOM   16777 C  C     . ASP A 1 3762 ? 144.162 99.568  226.266 1.00 116.89 ? 3762 ASP A C     1 
ATOM   16778 O  O     . ASP A 1 3762 ? 143.106 99.001  226.573 1.00 114.69 ? 3762 ASP A O     1 
ATOM   16779 C  CB    . ASP A 1 3762 ? 145.470 100.803 228.012 1.00 116.41 ? 3762 ASP A CB    1 
ATOM   16780 C  CG    . ASP A 1 3762 ? 146.353 100.652 229.233 1.00 117.69 ? 3762 ASP A CG    1 
ATOM   16781 O  OD1   . ASP A 1 3762 ? 146.155 99.683  229.995 1.00 117.66 ? 3762 ASP A OD1   1 
ATOM   16782 O  OD2   . ASP A 1 3762 ? 147.243 101.505 229.433 1.00 117.10 ? 3762 ASP A OD2   1 
ATOM   16783 N  N     . ASP A 1 3763 ? 144.297 100.241 225.128 1.00 117.56 ? 3763 ASP A N     1 
ATOM   16784 C  CA    . ASP A 1 3763 ? 143.200 100.426 224.186 1.00 119.37 ? 3763 ASP A CA    1 
ATOM   16785 C  C     . ASP A 1 3763 ? 143.461 99.584  222.944 1.00 118.97 ? 3763 ASP A C     1 
ATOM   16786 O  O     . ASP A 1 3763 ? 144.490 99.752  222.281 1.00 117.81 ? 3763 ASP A O     1 
ATOM   16787 C  CB    . ASP A 1 3763 ? 143.043 101.901 223.816 1.00 118.20 ? 3763 ASP A CB    1 
ATOM   16788 C  CG    . ASP A 1 3763 ? 141.778 102.172 223.027 1.00 116.07 ? 3763 ASP A CG    1 
ATOM   16789 O  OD1   . ASP A 1 3763 ? 140.679 101.898 223.552 1.00 114.68 ? 3763 ASP A OD1   1 
ATOM   16790 O  OD2   . ASP A 1 3763 ? 141.884 102.661 221.883 1.00 113.28 ? 3763 ASP A OD2   1 
ATOM   16791 N  N     . ASP A 1 3764 ? 142.526 98.683  222.633 1.00 117.94 ? 3764 ASP A N     1 
ATOM   16792 C  CA    . ASP A 1 3764 ? 142.675 97.847  221.446 1.00 117.61 ? 3764 ASP A CA    1 
ATOM   16793 C  C     . ASP A 1 3764 ? 142.396 98.627  220.168 1.00 115.30 ? 3764 ASP A C     1 
ATOM   16794 O  O     . ASP A 1 3764 ? 142.930 98.284  219.107 1.00 114.41 ? 3764 ASP A O     1 
ATOM   16795 C  CB    . ASP A 1 3764 ? 141.752 96.632  221.539 1.00 116.85 ? 3764 ASP A CB    1 
ATOM   16796 C  CG    . ASP A 1 3764 ? 142.224 95.621  222.565 1.00 115.69 ? 3764 ASP A CG    1 
ATOM   16797 O  OD1   . ASP A 1 3764 ? 143.302 95.832  223.159 1.00 117.69 ? 3764 ASP A OD1   1 
ATOM   16798 O  OD2   . ASP A 1 3764 ? 141.517 94.613  222.777 1.00 109.74 ? 3764 ASP A OD2   1 
ATOM   16799 N  N     . THR A 1 3765 ? 141.563 99.669  220.246 1.00 115.38 ? 3765 THR A N     1 
ATOM   16800 C  CA    . THR A 1 3765 ? 141.278 100.479 219.065 1.00 118.36 ? 3765 THR A CA    1 
ATOM   16801 C  C     . THR A 1 3765 ? 142.535 101.182 218.564 1.00 116.87 ? 3765 THR A C     1 
ATOM   16802 O  O     . THR A 1 3765 ? 142.765 101.270 217.352 1.00 114.72 ? 3765 THR A O     1 
ATOM   16803 C  CB    . THR A 1 3765 ? 140.179 101.496 219.376 1.00 112.31 ? 3765 THR A CB    1 
ATOM   16804 O  OG1   . THR A 1 3765 ? 139.038 100.818 219.916 1.00 106.08 ? 3765 THR A OG1   1 
ATOM   16805 C  CG2   . THR A 1 3765 ? 139.766 102.238 218.113 1.00 106.21 ? 3765 THR A CG2   1 
ATOM   16806 N  N     . ILE A 1 3766 ? 143.358 101.688 219.484 1.00 115.20 ? 3766 ILE A N     1 
ATOM   16807 C  CA    . ILE A 1 3766 ? 144.618 102.319 219.098 1.00 115.84 ? 3766 ILE A CA    1 
ATOM   16808 C  C     . ILE A 1 3766 ? 145.526 101.313 218.403 1.00 117.05 ? 3766 ILE A C     1 
ATOM   16809 O  O     . ILE A 1 3766 ? 146.189 101.634 217.409 1.00 117.66 ? 3766 ILE A O     1 
ATOM   16810 C  CB    . ILE A 1 3766 ? 145.298 102.947 220.330 1.00 115.82 ? 3766 ILE A CB    1 
ATOM   16811 C  CG1   . ILE A 1 3766 ? 144.555 104.213 220.762 1.00 112.59 ? 3766 ILE A CG1   1 
ATOM   16812 C  CG2   . ILE A 1 3766 ? 146.760 103.257 220.046 1.00 114.45 ? 3766 ILE A CG2   1 
ATOM   16813 C  CD1   . ILE A 1 3766 ? 144.636 105.341 219.758 1.00 108.41 ? 3766 ILE A CD1   1 
ATOM   16814 N  N     . ILE A 1 3767 ? 145.566 100.079 218.911 1.00 115.05 ? 3767 ILE A N     1 
ATOM   16815 C  CA    . ILE A 1 3767 ? 146.396 99.041  218.302 1.00 113.80 ? 3767 ILE A CA    1 
ATOM   16816 C  C     . ILE A 1 3767 ? 145.934 98.757  216.878 1.00 112.79 ? 3767 ILE A C     1 
ATOM   16817 O  O     . ILE A 1 3767 ? 146.747 98.634  215.954 1.00 111.03 ? 3767 ILE A O     1 
ATOM   16818 C  CB    . ILE A 1 3767 ? 146.380 97.767  219.166 1.00 112.69 ? 3767 ILE A CB    1 
ATOM   16819 C  CG1   . ILE A 1 3767 ? 147.137 98.000  220.475 1.00 112.76 ? 3767 ILE A CG1   1 
ATOM   16820 C  CG2   . ILE A 1 3767 ? 146.969 96.590  218.403 1.00 111.41 ? 3767 ILE A CG2   1 
ATOM   16821 C  CD1   . ILE A 1 3767 ? 147.177 96.789  221.381 1.00 111.39 ? 3767 ILE A CD1   1 
ATOM   16822 N  N     . THR A 1 3768 ? 144.617 98.650  216.681 1.00 114.47 ? 3768 THR A N     1 
ATOM   16823 C  CA    . THR A 1 3768 ? 144.087 98.370  215.349 1.00 114.72 ? 3768 THR A CA    1 
ATOM   16824 C  C     . THR A 1 3768 ? 144.417 99.494  214.374 1.00 110.17 ? 3768 THR A C     1 
ATOM   16825 O  O     . THR A 1 3768 ? 144.765 99.237  213.215 1.00 107.52 ? 3768 THR A O     1 
ATOM   16826 C  CB    . THR A 1 3768 ? 142.576 98.150  215.417 1.00 114.02 ? 3768 THR A CB    1 
ATOM   16827 O  OG1   . THR A 1 3768 ? 141.957 99.266  216.068 1.00 113.39 ? 3768 THR A OG1   1 
ATOM   16828 C  CG2   . THR A 1 3768 ? 142.258 96.877  216.188 1.00 108.78 ? 3768 THR A CG2   1 
ATOM   16829 N  N     . THR A 1 3769 ? 144.308 100.747 214.823 1.00 110.62 ? 3769 THR A N     1 
ATOM   16830 C  CA    . THR A 1 3769 ? 144.649 101.872 213.957 1.00 108.95 ? 3769 THR A CA    1 
ATOM   16831 C  C     . THR A 1 3769 ? 146.123 101.845 213.573 1.00 108.95 ? 3769 THR A C     1 
ATOM   16832 O  O     . THR A 1 3769 ? 146.475 102.099 212.416 1.00 108.07 ? 3769 THR A O     1 
ATOM   16833 C  CB    . THR A 1 3769 ? 144.299 103.193 214.642 1.00 107.91 ? 3769 THR A CB    1 
ATOM   16834 O  OG1   . THR A 1 3769 ? 144.901 103.235 215.942 1.00 110.85 ? 3769 THR A OG1   1 
ATOM   16835 C  CG2   . THR A 1 3769 ? 142.791 103.338 214.780 1.00 100.20 ? 3769 THR A CG2   1 
ATOM   16836 N  N     . LEU A 1 3770 ? 147.001 101.540 214.533 1.00 109.12 ? 3770 LEU A N     1 
ATOM   16837 C  CA    . LEU A 1 3770 ? 148.428 101.463 214.232 1.00 107.80 ? 3770 LEU A CA    1 
ATOM   16838 C  C     . LEU A 1 3770 ? 148.722 100.353 213.231 1.00 107.27 ? 3770 LEU A C     1 
ATOM   16839 O  O     . LEU A 1 3770 ? 149.544 100.526 212.323 1.00 107.26 ? 3770 LEU A O     1 
ATOM   16840 C  CB    . LEU A 1 3770 ? 149.226 101.253 215.518 1.00 106.25 ? 3770 LEU A CB    1 
ATOM   16841 C  CG    . LEU A 1 3770 ? 149.268 102.419 216.509 1.00 105.42 ? 3770 LEU A CG    1 
ATOM   16842 C  CD1   . LEU A 1 3770 ? 150.391 102.227 217.517 1.00 100.60 ? 3770 LEU A CD1   1 
ATOM   16843 C  CD2   . LEU A 1 3770 ? 149.415 103.748 215.784 1.00 101.62 ? 3770 LEU A CD2   1 
ATOM   16844 N  N     . GLU A 1 3771 ? 148.067 99.200  213.387 1.00 107.27 ? 3771 GLU A N     1 
ATOM   16845 C  CA    . GLU A 1 3771 ? 148.268 98.102  212.446 1.00 106.25 ? 3771 GLU A CA    1 
ATOM   16846 C  C     . GLU A 1 3771 ? 147.764 98.465  211.055 1.00 104.30 ? 3771 GLU A C     1 
ATOM   16847 O  O     . GLU A 1 3771 ? 148.407 98.140  210.049 1.00 102.88 ? 3771 GLU A O     1 
ATOM   16848 C  CB    . GLU A 1 3771 ? 147.572 96.840  212.957 1.00 107.70 ? 3771 GLU A CB    1 
ATOM   16849 C  CG    . GLU A 1 3771 ? 148.226 96.225  214.183 1.00 108.56 ? 3771 GLU A CG    1 
ATOM   16850 C  CD    . GLU A 1 3771 ? 147.323 95.234  214.890 1.00 111.63 ? 3771 GLU A CD    1 
ATOM   16851 O  OE1   . GLU A 1 3771 ? 146.199 95.621  215.274 1.00 112.27 ? 3771 GLU A OE1   1 
ATOM   16852 O  OE2   . GLU A 1 3771 ? 147.737 94.068  215.064 1.00 110.40 ? 3771 GLU A OE2   1 
ATOM   16853 N  N     . ASN A 1 3772 ? 146.609 99.131  210.976 1.00 105.49 ? 3772 ASN A N     1 
ATOM   16854 C  CA    . ASN A 1 3772 ? 146.068 99.518  209.677 1.00 103.76 ? 3772 ASN A CA    1 
ATOM   16855 C  C     . ASN A 1 3772 ? 146.937 100.574 209.005 1.00 100.97 ? 3772 ASN A C     1 
ATOM   16856 O  O     . ASN A 1 3772 ? 147.170 100.516 207.792 1.00 100.74 ? 3772 ASN A O     1 
ATOM   16857 C  CB    . ASN A 1 3772 ? 144.635 100.026 209.834 1.00 98.17  ? 3772 ASN A CB    1 
ATOM   16858 C  CG    . ASN A 1 3772 ? 143.694 98.959  210.354 1.00 99.71  ? 3772 ASN A CG    1 
ATOM   16859 O  OD1   . ASN A 1 3772 ? 144.105 97.830  210.620 1.00 99.48  ? 3772 ASN A OD1   1 
ATOM   16860 N  ND2   . ASN A 1 3772 ? 142.422 99.312  210.501 1.00 96.25  ? 3772 ASN A ND2   1 
ATOM   16861 N  N     . LEU A 1 3773 ? 147.420 101.552 209.776 1.00 100.05 ? 3773 LEU A N     1 
ATOM   16862 C  CA    . LEU A 1 3773 ? 148.253 102.601 209.198 1.00 99.69  ? 3773 LEU A CA    1 
ATOM   16863 C  C     . LEU A 1 3773 ? 149.556 102.033 208.649 1.00 101.15 ? 3773 LEU A C     1 
ATOM   16864 O  O     . LEU A 1 3773 ? 150.005 102.425 207.566 1.00 100.37 ? 3773 LEU A O     1 
ATOM   16865 C  CB    . LEU A 1 3773 ? 148.532 103.685 210.239 1.00 95.02  ? 3773 LEU A CB    1 
ATOM   16866 C  CG    . LEU A 1 3773 ? 147.339 104.576 210.591 1.00 92.60  ? 3773 LEU A CG    1 
ATOM   16867 C  CD1   . LEU A 1 3773 ? 147.721 105.606 211.642 1.00 87.24  ? 3773 LEU A CD1   1 
ATOM   16868 C  CD2   . LEU A 1 3773 ? 146.788 105.252 209.346 1.00 87.46  ? 3773 LEU A CD2   1 
ATOM   16869 N  N     . LYS A 1 3774 ? 150.179 101.108 209.383 1.00 100.73 ? 3774 LYS A N     1 
ATOM   16870 C  CA    . LYS A 1 3774 ? 151.397 100.476 208.885 1.00 99.01  ? 3774 LYS A CA    1 
ATOM   16871 C  C     . LYS A 1 3774 ? 151.113 99.605  207.668 1.00 99.57  ? 3774 LYS A C     1 
ATOM   16872 O  O     . LYS A 1 3774 ? 151.903 99.588  206.716 1.00 101.78 ? 3774 LYS A O     1 
ATOM   16873 C  CB    . LYS A 1 3774 ? 152.060 99.656  209.991 1.00 97.34  ? 3774 LYS A CB    1 
ATOM   16874 C  CG    . LYS A 1 3774 ? 152.962 100.470 210.905 1.00 101.07 ? 3774 LYS A CG    1 
ATOM   16875 C  CD    . LYS A 1 3774 ? 154.170 101.015 210.150 1.00 100.65 ? 3774 LYS A CD    1 
ATOM   16876 C  CE    . LYS A 1 3774 ? 154.887 99.924  209.367 1.00 96.97  ? 3774 LYS A CE    1 
ATOM   16877 N  NZ    . LYS A 1 3774 ? 156.168 100.407 208.783 1.00 98.13  ? 3774 LYS A NZ    1 
ATOM   16878 N  N     . ARG A 1 3775 ? 149.999 98.869  207.681 1.00 97.99  ? 3775 ARG A N     1 
ATOM   16879 C  CA    . ARG A 1 3775 ? 149.644 98.056  206.522 1.00 97.53  ? 3775 ARG A CA    1 
ATOM   16880 C  C     . ARG A 1 3775 ? 149.397 98.926  205.297 1.00 95.38  ? 3775 ARG A C     1 
ATOM   16881 O  O     . ARG A 1 3775 ? 149.843 98.597  204.191 1.00 95.98  ? 3775 ARG A O     1 
ATOM   16882 C  CB    . ARG A 1 3775 ? 148.413 97.201  206.827 1.00 99.41  ? 3775 ARG A CB    1 
ATOM   16883 C  CG    . ARG A 1 3775 ? 148.031 96.261  205.692 1.00 100.58 ? 3775 ARG A CG    1 
ATOM   16884 C  CD    . ARG A 1 3775 ? 146.747 95.502  205.987 1.00 101.22 ? 3775 ARG A CD    1 
ATOM   16885 N  NE    . ARG A 1 3775 ? 146.745 94.915  207.320 1.00 107.38 ? 3775 ARG A NE    1 
ATOM   16886 C  CZ    . ARG A 1 3775 ? 145.873 95.220  208.271 1.00 104.75 ? 3775 ARG A CZ    1 
ATOM   16887 N  NH1   . ARG A 1 3775 ? 144.912 96.107  208.069 1.00 102.11 ? 3775 ARG A NH1   1 
ATOM   16888 N  NH2   . ARG A 1 3775 ? 145.966 94.620  209.454 1.00 99.24  ? 3775 ARG A NH2   1 
ATOM   16889 N  N     . GLU A 1 3776 ? 148.686 100.042 205.474 1.00 92.16  ? 3776 GLU A N     1 
ATOM   16890 C  CA    . GLU A 1 3776 ? 148.493 100.975 204.369 1.00 90.18  ? 3776 GLU A CA    1 
ATOM   16891 C  C     . GLU A 1 3776 ? 149.814 101.601 203.944 1.00 91.45  ? 3776 GLU A C     1 
ATOM   16892 O  O     . GLU A 1 3776 ? 150.071 101.771 202.747 1.00 93.86  ? 3776 GLU A O     1 
ATOM   16893 C  CB    . GLU A 1 3776 ? 147.486 102.055 204.761 1.00 90.90  ? 3776 GLU A CB    1 
ATOM   16894 C  CG    . GLU A 1 3776 ? 146.727 102.648 203.585 1.00 90.40  ? 3776 GLU A CG    1 
ATOM   16895 C  CD    . GLU A 1 3776 ? 145.550 103.498 204.019 1.00 91.17  ? 3776 GLU A CD    1 
ATOM   16896 O  OE1   . GLU A 1 3776 ? 145.350 103.657 205.241 1.00 94.37  ? 3776 GLU A OE1   1 
ATOM   16897 O  OE2   . GLU A 1 3776 ? 144.825 104.006 203.138 1.00 86.85  ? 3776 GLU A OE2   1 
ATOM   16898 N  N     . ALA A 1 3777 ? 150.666 101.949 204.911 1.00 94.99  ? 3777 ALA A N     1 
ATOM   16899 C  CA    . ALA A 1 3777 ? 151.970 102.511 204.578 1.00 93.41  ? 3777 ALA A CA    1 
ATOM   16900 C  C     . ALA A 1 3777 ? 152.823 101.509 203.812 1.00 92.87  ? 3777 ALA A C     1 
ATOM   16901 O  O     . ALA A 1 3777 ? 153.496 101.871 202.841 1.00 96.60  ? 3777 ALA A O     1 
ATOM   16902 C  CB    . ALA A 1 3777 ? 152.688 102.969 205.847 1.00 93.44  ? 3777 ALA A CB    1 
ATOM   16903 N  N     . ALA A 1 3778 ? 152.808 100.243 204.236 1.00 93.31  ? 3778 ALA A N     1 
ATOM   16904 C  CA    . ALA A 1 3778 ? 153.563 99.218  203.524 1.00 94.05  ? 3778 ALA A CA    1 
ATOM   16905 C  C     . ALA A 1 3778 ? 153.012 98.999  202.121 1.00 93.46  ? 3778 ALA A C     1 
ATOM   16906 O  O     . ALA A 1 3778 ? 153.777 98.819  201.167 1.00 88.41  ? 3778 ALA A O     1 
ATOM   16907 C  CB    . ALA A 1 3778 ? 153.551 97.910  204.316 1.00 91.79  ? 3778 ALA A CB    1 
ATOM   16908 N  N     . GLU A 1 3779 ? 151.684 99.007  201.976 1.00 93.57  ? 3779 GLU A N     1 
ATOM   16909 C  CA    . GLU A 1 3779 ? 151.084 98.801  200.662 1.00 93.00  ? 3779 GLU A CA    1 
ATOM   16910 C  C     . GLU A 1 3779 ? 151.352 99.982  199.738 1.00 91.76  ? 3779 GLU A C     1 
ATOM   16911 O  O     . GLU A 1 3779 ? 151.701 99.794  198.566 1.00 90.54  ? 3779 GLU A O     1 
ATOM   16912 C  CB    . GLU A 1 3779 ? 149.582 98.557  200.803 1.00 91.94  ? 3779 GLU A CB    1 
ATOM   16913 C  CG    . GLU A 1 3779 ? 149.212 97.094  200.976 1.00 97.76  ? 3779 GLU A CG    1 
ATOM   16914 C  CD    . GLU A 1 3779 ? 149.851 96.206  199.926 1.00 101.03 ? 3779 GLU A CD    1 
ATOM   16915 O  OE1   . GLU A 1 3779 ? 149.494 96.338  198.736 1.00 104.24 ? 3779 GLU A OE1   1 
ATOM   16916 O  OE2   . GLU A 1 3779 ? 150.711 95.377  200.290 1.00 95.09  ? 3779 GLU A OE2   1 
ATOM   16917 N  N     . VAL A 1 3780 ? 151.192 101.207 200.244 1.00 89.55  ? 3780 VAL A N     1 
ATOM   16918 C  CA    . VAL A 1 3780 ? 151.472 102.387 199.430 1.00 88.10  ? 3780 VAL A CA    1 
ATOM   16919 C  C     . VAL A 1 3780 ? 152.953 102.449 199.082 1.00 88.52  ? 3780 VAL A C     1 
ATOM   16920 O  O     . VAL A 1 3780 ? 153.331 102.860 197.977 1.00 89.68  ? 3780 VAL A O     1 
ATOM   16921 C  CB    . VAL A 1 3780 ? 150.998 103.663 200.152 1.00 84.57  ? 3780 VAL A CB    1 
ATOM   16922 C  CG1   . VAL A 1 3780 ? 151.450 104.906 199.402 1.00 75.95  ? 3780 VAL A CG1   1 
ATOM   16923 C  CG2   . VAL A 1 3780 ? 149.486 103.657 200.285 1.00 87.39  ? 3780 VAL A CG2   1 
ATOM   16924 N  N     . THR A 1 3781 ? 153.814 102.033 200.013 1.00 87.92  ? 3781 THR A N     1 
ATOM   16925 C  CA    . THR A 1 3781 ? 155.241 101.956 199.716 1.00 85.53  ? 3781 THR A CA    1 
ATOM   16926 C  C     . THR A 1 3781 ? 155.504 100.992 198.568 1.00 88.21  ? 3781 THR A C     1 
ATOM   16927 O  O     . THR A 1 3781 ? 156.265 101.303 197.647 1.00 92.53  ? 3781 THR A O     1 
ATOM   16928 C  CB    . THR A 1 3781 ? 156.022 101.531 200.960 1.00 84.62  ? 3781 THR A CB    1 
ATOM   16929 O  OG1   . THR A 1 3781 ? 155.653 102.363 202.066 1.00 86.50  ? 3781 THR A OG1   1 
ATOM   16930 C  CG2   . THR A 1 3781 ? 157.519 101.650 200.716 1.00 79.87  ? 3781 THR A CG2   1 
ATOM   16931 N  N     . ARG A 1 3782 ? 154.864 99.819  198.599 1.00 90.18  ? 3782 ARG A N     1 
ATOM   16932 C  CA    . ARG A 1 3782 ? 155.066 98.825  197.549 1.00 89.08  ? 3782 ARG A CA    1 
ATOM   16933 C  C     . ARG A 1 3782 ? 154.703 99.384  196.179 1.00 91.98  ? 3782 ARG A C     1 
ATOM   16934 O  O     . ARG A 1 3782 ? 155.366 99.081  195.179 1.00 90.82  ? 3782 ARG A O     1 
ATOM   16935 C  CB    . ARG A 1 3782 ? 154.246 97.571  197.856 1.00 89.00  ? 3782 ARG A CB    1 
ATOM   16936 C  CG    . ARG A 1 3782 ? 154.095 96.606  196.690 1.00 88.61  ? 3782 ARG A CG    1 
ATOM   16937 C  CD    . ARG A 1 3782 ? 152.853 95.736  196.853 1.00 88.12  ? 3782 ARG A CD    1 
ATOM   16938 N  NE    . ARG A 1 3782 ? 151.641 96.369  196.342 1.00 93.53  ? 3782 ARG A NE    1 
ATOM   16939 C  CZ    . ARG A 1 3782 ? 151.425 96.680  195.070 1.00 93.93  ? 3782 ARG A CZ    1 
ATOM   16940 N  NH1   . ARG A 1 3782 ? 152.301 96.384  194.125 1.00 94.60  ? 3782 ARG A NH1   1 
ATOM   16941 N  NH2   . ARG A 1 3782 ? 150.292 97.292  194.737 1.00 90.27  ? 3782 ARG A NH2   1 
ATOM   16942 N  N     . LYS A 1 3783 ? 153.657 100.210 196.114 1.00 91.38  ? 3783 LYS A N     1 
ATOM   16943 C  CA    . LYS A 1 3783 ? 153.273 100.818 194.845 1.00 88.13  ? 3783 LYS A CA    1 
ATOM   16944 C  C     . LYS A 1 3783 ? 154.328 101.806 194.360 1.00 87.57  ? 3783 LYS A C     1 
ATOM   16945 O  O     . LYS A 1 3783 ? 154.403 102.105 193.163 1.00 90.78  ? 3783 LYS A O     1 
ATOM   16946 C  CB    . LYS A 1 3783 ? 151.917 101.509 194.986 1.00 83.16  ? 3783 LYS A CB    1 
ATOM   16947 C  CG    . LYS A 1 3783 ? 150.802 100.604 195.480 1.00 85.65  ? 3783 LYS A CG    1 
ATOM   16948 C  CD    . LYS A 1 3783 ? 149.693 101.409 196.138 1.00 86.29  ? 3783 LYS A CD    1 
ATOM   16949 C  CE    . LYS A 1 3783 ? 148.884 100.552 197.098 1.00 90.41  ? 3783 LYS A CE    1 
ATOM   16950 N  NZ    . LYS A 1 3783 ? 148.194 101.373 198.130 1.00 86.74  ? 3783 LYS A NZ    1 
ATOM   16951 N  N     . VAL A 1 3784 ? 155.146 102.331 195.276 1.00 88.28  ? 3784 VAL A N     1 
ATOM   16952 C  CA    . VAL A 1 3784 ? 156.129 103.343 194.898 1.00 86.13  ? 3784 VAL A CA    1 
ATOM   16953 C  C     . VAL A 1 3784 ? 157.222 102.734 194.025 1.00 89.37  ? 3784 VAL A C     1 
ATOM   16954 O  O     . VAL A 1 3784 ? 157.587 103.293 192.984 1.00 92.53  ? 3784 VAL A O     1 
ATOM   16955 C  CB    . VAL A 1 3784 ? 156.713 104.024 196.149 1.00 85.01  ? 3784 VAL A CB    1 
ATOM   16956 C  CG1   . VAL A 1 3784 ? 157.953 104.827 195.789 1.00 82.84  ? 3784 VAL A CG1   1 
ATOM   16957 C  CG2   . VAL A 1 3784 ? 155.668 104.918 196.799 1.00 79.25  ? 3784 VAL A CG2   1 
ATOM   16958 N  N     . GLU A 1 3785 ? 157.765 101.580 194.433 1.00 86.34  ? 3785 GLU A N     1 
ATOM   16959 C  CA    . GLU A 1 3785 ? 158.834 100.975 193.643 1.00 88.57  ? 3785 GLU A CA    1 
ATOM   16960 C  C     . GLU A 1 3785 ? 158.335 100.547 192.269 1.00 87.52  ? 3785 GLU A C     1 
ATOM   16961 O  O     . GLU A 1 3785 ? 159.028 100.747 191.265 1.00 87.99  ? 3785 GLU A O     1 
ATOM   16962 C  CB    . GLU A 1 3785 ? 159.460 99.780  194.367 1.00 88.51  ? 3785 GLU A CB    1 
ATOM   16963 C  CG    . GLU A 1 3785 ? 160.246 100.129 195.619 1.00 85.98  ? 3785 GLU A CG    1 
ATOM   16964 C  CD    . GLU A 1 3785 ? 159.372 100.182 196.845 1.00 91.44  ? 3785 GLU A CD    1 
ATOM   16965 O  OE1   . GLU A 1 3785 ? 158.182 99.836  196.722 1.00 92.54  ? 3785 GLU A OE1   1 
ATOM   16966 O  OE2   . GLU A 1 3785 ? 159.868 100.567 197.924 1.00 92.83  ? 3785 GLU A OE2   1 
ATOM   16967 N  N     . GLU A 1 3786 ? 157.138 99.959  192.200 1.00 88.09  ? 3786 GLU A N     1 
ATOM   16968 C  CA    . GLU A 1 3786 ? 156.619 99.524  190.908 1.00 85.25  ? 3786 GLU A CA    1 
ATOM   16969 C  C     . GLU A 1 3786 ? 156.384 100.712 189.983 1.00 86.73  ? 3786 GLU A C     1 
ATOM   16970 O  O     . GLU A 1 3786 ? 156.619 100.615 188.774 1.00 85.46  ? 3786 GLU A O     1 
ATOM   16971 C  CB    . GLU A 1 3786 ? 155.341 98.700  191.091 1.00 84.72  ? 3786 GLU A CB    1 
ATOM   16972 C  CG    . GLU A 1 3786 ? 154.065 99.497  191.310 1.00 88.60  ? 3786 GLU A CG    1 
ATOM   16973 C  CD    . GLU A 1 3786 ? 152.985 98.685  191.992 1.00 95.27  ? 3786 GLU A CD    1 
ATOM   16974 O  OE1   . GLU A 1 3786 ? 153.287 97.562  192.447 1.00 94.94  ? 3786 GLU A OE1   1 
ATOM   16975 O  OE2   . GLU A 1 3786 ? 151.835 99.166  192.068 1.00 96.85  ? 3786 GLU A OE2   1 
ATOM   16976 N  N     . THR A 1 3787 ? 155.933 101.844 190.528 1.00 84.11  ? 3787 THR A N     1 
ATOM   16977 C  CA    . THR A 1 3787 ? 155.829 103.049 189.714 1.00 82.50  ? 3787 THR A CA    1 
ATOM   16978 C  C     . THR A 1 3787 ? 157.205 103.600 189.366 1.00 81.16  ? 3787 THR A C     1 
ATOM   16979 O  O     . THR A 1 3787 ? 157.370 104.244 188.324 1.00 81.53  ? 3787 THR A O     1 
ATOM   16980 C  CB    . THR A 1 3787 ? 154.998 104.111 190.436 1.00 86.09  ? 3787 THR A CB    1 
ATOM   16981 O  OG1   . THR A 1 3787 ? 155.492 104.287 191.769 1.00 87.49  ? 3787 THR A OG1   1 
ATOM   16982 C  CG2   . THR A 1 3787 ? 153.532 103.700 190.485 1.00 81.24  ? 3787 THR A CG2   1 
ATOM   16983 N  N     . ASP A 1 3788 ? 158.180 103.366 190.248 1.00 81.71  ? 3788 ASP A N     1 
ATOM   16984 C  CA    . ASP A 1 3788 ? 159.557 103.879 190.010 1.00 82.87  ? 3788 ASP A CA    1 
ATOM   16985 C  C     . ASP A 1 3788 ? 160.167 103.140 188.816 1.00 78.93  ? 3788 ASP A C     1 
ATOM   16986 O  O     . ASP A 1 3788 ? 160.738 103.814 187.933 1.00 76.83  ? 3788 ASP A O     1 
ATOM   16987 C  CB    . ASP A 1 3788 ? 160.412 103.777 191.264 1.00 87.32  ? 3788 ASP A CB    1 
ATOM   16988 C  CG    . ASP A 1 3788 ? 160.012 104.705 192.401 1.00 95.91  ? 3788 ASP A CG    1 
ATOM   16989 O  OD1   . ASP A 1 3788 ? 159.055 105.485 192.211 1.00 95.05  ? 3788 ASP A OD1   1 
ATOM   16990 O  OD2   . ASP A 1 3788 ? 160.657 104.636 193.468 1.00 103.42 ? 3788 ASP A OD2   1 
ATOM   16991 N  N     . ILE A 1 3789 ? 160.044 101.810 188.790 1.00 77.87  ? 3789 ILE A N     1 
ATOM   16992 C  CA    . ILE A 1 3789 ? 160.648 100.996 187.691 1.00 75.97  ? 3789 ILE A CA    1 
ATOM   16993 C  C     . ILE A 1 3789 ? 159.982 101.375 186.357 1.00 72.83  ? 3789 ILE A C     1 
ATOM   16994 O  O     . ILE A 1 3789 ? 160.711 101.506 185.349 1.00 71.61  ? 3789 ILE A O     1 
ATOM   16995 C  CB    . ILE A 1 3789 ? 160.520 99.492  187.994 1.00 77.23  ? 3789 ILE A CB    1 
ATOM   16996 C  CG1   . ILE A 1 3789 ? 159.061 99.047  188.053 1.00 77.47  ? 3789 ILE A CG1   1 
ATOM   16997 C  CG2   . ILE A 1 3789 ? 161.270 99.132  189.277 1.00 72.47  ? 3789 ILE A CG2   1 
ATOM   16998 C  CD1   . ILE A 1 3789 ? 158.870 97.600  188.466 1.00 73.70  ? 3789 ILE A CD1   1 
ATOM   16999 N  N     . VAL A 1 3790 ? 158.656 101.541 186.355 1.00 74.02  ? 3790 VAL A N     1 
ATOM   17000 C  CA    . VAL A 1 3790 ? 157.925 101.919 185.107 1.00 72.09  ? 3790 VAL A CA    1 
ATOM   17001 C  C     . VAL A 1 3790 ? 158.382 103.326 184.688 1.00 68.76  ? 3790 VAL A C     1 
ATOM   17002 O  O     . VAL A 1 3790 ? 158.618 103.539 183.481 1.00 70.68  ? 3790 VAL A O     1 
ATOM   17003 C  CB    . VAL A 1 3790 ? 156.396 101.854 185.281 1.00 71.78  ? 3790 VAL A CB    1 
ATOM   17004 C  CG1   . VAL A 1 3790 ? 155.668 102.244 184.000 1.00 66.51  ? 3790 VAL A CG1   1 
ATOM   17005 C  CG2   . VAL A 1 3790 ? 155.942 100.479 185.753 1.00 69.27  ? 3790 VAL A CG2   1 
ATOM   17006 N  N     . MET A 1 3791 ? 158.513 104.241 185.651 1.00 70.46  ? 3791 MET A N     1 
ATOM   17007 C  CA    . MET A 1 3791 ? 159.008 105.605 185.336 1.00 69.27  ? 3791 MET A CA    1 
ATOM   17008 C  C     . MET A 1 3791 ? 160.433 105.485 184.777 1.00 68.33  ? 3791 MET A C     1 
ATOM   17009 O  O     . MET A 1 3791 ? 160.783 106.270 183.870 1.00 67.42  ? 3791 MET A O     1 
ATOM   17010 C  CB    . MET A 1 3791 ? 159.017 106.489 186.588 1.00 71.18  ? 3791 MET A CB    1 
ATOM   17011 C  CG    . MET A 1 3791 ? 159.192 107.964 186.293 1.00 73.12  ? 3791 MET A CG    1 
ATOM   17012 S  SD    . MET A 1 3791 ? 157.855 108.608 185.268 1.00 80.59  ? 3791 MET A SD    1 
ATOM   17013 C  CE    . MET A 1 3791 ? 158.375 110.319 185.082 1.00 73.44  ? 3791 MET A CE    1 
ATOM   17014 N  N     . GLN A 1 3792 ? 161.215 104.537 185.301 1.00 67.94  ? 3792 GLN A N     1 
ATOM   17015 C  CA    . GLN A 1 3792 ? 162.611 104.334 184.835 1.00 65.39  ? 3792 GLN A CA    1 
ATOM   17016 C  C     . GLN A 1 3792 ? 162.603 103.921 183.354 1.00 65.76  ? 3792 GLN A C     1 
ATOM   17017 O  O     . GLN A 1 3792 ? 163.394 104.496 182.574 1.00 66.27  ? 3792 GLN A O     1 
ATOM   17018 C  CB    . GLN A 1 3792 ? 163.289 103.273 185.699 1.00 67.42  ? 3792 GLN A CB    1 
ATOM   17019 C  CG    . GLN A 1 3792 ? 164.620 102.777 185.145 1.00 69.72  ? 3792 GLN A CG    1 
ATOM   17020 C  CD    . GLN A 1 3792 ? 165.224 101.660 185.967 1.00 76.91  ? 3792 GLN A CD    1 
ATOM   17021 O  OE1   . GLN A 1 3792 ? 166.338 101.772 186.489 1.00 83.05  ? 3792 GLN A OE1   1 
ATOM   17022 N  NE2   . GLN A 1 3792 ? 164.488 100.565 186.089 1.00 74.24  ? 3792 GLN A NE2   1 
ATOM   17023 N  N     . GLU A 1 3793 ? 161.737 102.972 182.987 1.00 63.20  ? 3793 GLU A N     1 
ATOM   17024 C  CA    . GLU A 1 3793 ? 161.642 102.531 181.571 1.00 65.27  ? 3793 GLU A CA    1 
ATOM   17025 C  C     . GLU A 1 3793 ? 161.246 103.744 180.717 1.00 64.38  ? 3793 GLU A C     1 
ATOM   17026 O  O     . GLU A 1 3793 ? 161.680 103.820 179.548 1.00 65.86  ? 3793 GLU A O     1 
ATOM   17027 C  CB    . GLU A 1 3793 ? 160.640 101.387 181.409 1.00 68.04  ? 3793 GLU A CB    1 
ATOM   17028 C  CG    . GLU A 1 3793 ? 159.198 101.860 181.246 1.00 72.48  ? 3793 GLU A CG    1 
ATOM   17029 C  CD    . GLU A 1 3793 ? 158.157 100.759 181.327 1.00 79.73  ? 3793 GLU A CD    1 
ATOM   17030 O  OE1   . GLU A 1 3793 ? 158.093 100.084 182.375 1.00 78.22  ? 3793 GLU A OE1   1 
ATOM   17031 O  OE2   . GLU A 1 3793 ? 157.408 100.580 180.344 1.00 81.27  ? 3793 GLU A OE2   1 
ATOM   17032 N  N     . VAL A 1 3794 ? 160.452 104.654 181.288 1.00 61.95  ? 3794 VAL A N     1 
ATOM   17033 C  CA    . VAL A 1 3794 ? 160.046 105.887 180.553 1.00 58.94  ? 3794 VAL A CA    1 
ATOM   17034 C  C     . VAL A 1 3794 ? 161.299 106.732 180.279 1.00 59.68  ? 3794 VAL A C     1 
ATOM   17035 O  O     . VAL A 1 3794 ? 161.422 107.250 179.148 1.00 60.17  ? 3794 VAL A O     1 
ATOM   17036 C  CB    . VAL A 1 3794 ? 158.993 106.693 181.338 1.00 61.00  ? 3794 VAL A CB    1 
ATOM   17037 C  CG1   . VAL A 1 3794 ? 158.733 108.054 180.704 1.00 60.37  ? 3794 VAL A CG1   1 
ATOM   17038 C  CG2   . VAL A 1 3794 ? 157.693 105.917 181.506 1.00 59.45  ? 3794 VAL A CG2   1 
ATOM   17039 N  N     . GLU A 1 3795 ? 162.195 106.859 181.264 1.00 61.60  ? 3795 GLU A N     1 
ATOM   17040 C  CA    . GLU A 1 3795 ? 163.358 107.724 181.079 1.00 60.30  ? 3795 GLU A CA    1 
ATOM   17041 C  C     . GLU A 1 3795 ? 164.303 107.174 180.018 1.00 56.54  ? 3795 GLU A C     1 
ATOM   17042 O  O     . GLU A 1 3795 ? 164.900 107.945 179.257 1.00 56.00  ? 3795 GLU A O     1 
ATOM   17043 C  CB    . GLU A 1 3795 ? 164.095 107.916 182.404 1.00 61.36  ? 3795 GLU A CB    1 
ATOM   17044 C  CG    . GLU A 1 3795 ? 163.187 108.084 183.607 1.00 66.44  ? 3795 GLU A CG    1 
ATOM   17045 C  CD    . GLU A 1 3795 ? 162.533 109.450 183.656 1.00 76.06  ? 3795 GLU A CD    1 
ATOM   17046 O  OE1   . GLU A 1 3795 ? 163.217 110.449 183.353 1.00 78.03  ? 3795 GLU A OE1   1 
ATOM   17047 O  OE2   . GLU A 1 3795 ? 161.333 109.524 183.994 1.00 77.77  ? 3795 GLU A OE2   1 
ATOM   17048 N  N     . THR A 1 3796 ? 164.461 105.850 179.954 1.00 56.16  ? 3796 THR A N     1 
ATOM   17049 C  CA    . THR A 1 3796 ? 165.343 105.272 178.944 1.00 55.56  ? 3796 THR A CA    1 
ATOM   17050 C  C     . THR A 1 3796 ? 164.808 105.530 177.538 1.00 57.09  ? 3796 THR A C     1 
ATOM   17051 O  O     . THR A 1 3796 ? 165.585 105.639 176.582 1.00 57.65  ? 3796 THR A O     1 
ATOM   17052 C  CB    . THR A 1 3796 ? 165.544 103.774 179.203 1.00 59.82  ? 3796 THR A CB    1 
ATOM   17053 O  OG1   . THR A 1 3796 ? 166.794 103.354 178.640 1.00 65.86  ? 3796 THR A OG1   1 
ATOM   17054 C  CG2   . THR A 1 3796 ? 164.419 102.939 178.602 1.00 57.30  ? 3796 THR A CG2   1 
ATOM   17055 N  N     . VAL A 1 3797 ? 163.484 105.634 177.393 1.00 53.46  ? 3797 VAL A N     1 
ATOM   17056 C  CA    . VAL A 1 3797 ? 162.912 106.086 176.129 1.00 49.47  ? 3797 VAL A CA    1 
ATOM   17057 C  C     . VAL A 1 3797 ? 163.169 107.575 175.938 1.00 46.59  ? 3797 VAL A C     1 
ATOM   17058 O  O     . VAL A 1 3797 ? 163.520 108.025 174.840 1.00 45.11  ? 3797 VAL A O     1 
ATOM   17059 C  CB    . VAL A 1 3797 ? 161.410 105.750 176.074 1.00 50.36  ? 3797 VAL A CB    1 
ATOM   17060 C  CG1   . VAL A 1 3797 ? 160.664 106.740 175.191 1.00 46.26  ? 3797 VAL A CG1   1 
ATOM   17061 C  CG2   . VAL A 1 3797 ? 161.204 104.328 175.576 1.00 50.57  ? 3797 VAL A CG2   1 
ATOM   17062 N  N     . SER A 1 3798 ? 163.014 108.362 177.006 1.00 48.90  ? 3798 SER A N     1 
ATOM   17063 C  CA    . SER A 1 3798 ? 163.247 109.799 176.929 1.00 45.79  ? 3798 SER A CA    1 
ATOM   17064 C  C     . SER A 1 3798 ? 164.712 110.140 176.690 1.00 42.22  ? 3798 SER A C     1 
ATOM   17065 O  O     . SER A 1 3798 ? 165.011 111.264 176.272 1.00 40.45  ? 3798 SER A O     1 
ATOM   17066 C  CB    . SER A 1 3798 ? 162.759 110.479 178.209 1.00 42.43  ? 3798 SER A CB    1 
ATOM   17067 O  OG    . SER A 1 3798 ? 161.370 110.275 178.399 1.00 45.51  ? 3798 SER A OG    1 
ATOM   17068 N  N     . GLN A 1 3799 ? 165.628 109.203 176.949 1.00 40.19  ? 3799 GLN A N     1 
ATOM   17069 C  CA    . GLN A 1 3799 ? 167.041 109.462 176.699 1.00 43.84  ? 3799 GLN A CA    1 
ATOM   17070 C  C     . GLN A 1 3799 ? 167.322 109.639 175.213 1.00 40.91  ? 3799 GLN A C     1 
ATOM   17071 O  O     . GLN A 1 3799 ? 168.189 110.435 174.835 1.00 38.31  ? 3799 GLN A O     1 
ATOM   17072 C  CB    . GLN A 1 3799 ? 167.893 108.327 177.267 1.00 45.38  ? 3799 GLN A CB    1 
ATOM   17073 C  CG    . GLN A 1 3799 ? 168.150 108.427 178.762 1.00 47.09  ? 3799 GLN A CG    1 
ATOM   17074 C  CD    . GLN A 1 3799 ? 168.751 109.760 179.165 1.00 52.03  ? 3799 GLN A CD    1 
ATOM   17075 O  OE1   . GLN A 1 3799 ? 168.056 110.638 179.677 1.00 49.88  ? 3799 GLN A OE1   1 
ATOM   17076 N  NE2   . GLN A 1 3799 ? 170.049 109.917 178.935 1.00 49.91  ? 3799 GLN A NE2   1 
ATOM   17077 N  N     . GLN A 1 3800 ? 166.606 108.903 174.359 1.00 39.26  ? 3800 GLN A N     1 
ATOM   17078 C  CA    . GLN A 1 3800 ? 166.798 109.034 172.918 1.00 35.06  ? 3800 GLN A CA    1 
ATOM   17079 C  C     . GLN A 1 3800 ? 166.428 110.430 172.431 1.00 35.44  ? 3800 GLN A C     1 
ATOM   17080 O  O     . GLN A 1 3800 ? 167.134 111.011 171.599 1.00 32.73  ? 3800 GLN A O     1 
ATOM   17081 C  CB    . GLN A 1 3800 ? 165.979 107.970 172.186 1.00 35.67  ? 3800 GLN A CB    1 
ATOM   17082 C  CG    . GLN A 1 3800 ? 165.555 108.362 170.782 1.00 39.09  ? 3800 GLN A CG    1 
ATOM   17083 C  CD    . GLN A 1 3800 ? 165.500 107.182 169.832 1.00 48.88  ? 3800 GLN A CD    1 
ATOM   17084 O  OE1   . GLN A 1 3800 ? 166.393 106.994 169.006 1.00 40.03  ? 3800 GLN A OE1   1 
ATOM   17085 N  NE2   . GLN A 1 3800 ? 164.446 106.382 169.941 1.00 47.93  ? 3800 GLN A NE2   1 
ATOM   17086 N  N     . TYR A 1 3801 ? 165.332 110.988 172.942 1.00 38.17  ? 3801 TYR A N     1 
ATOM   17087 C  CA    . TYR A 1 3801 ? 164.870 112.304 172.524 1.00 32.19  ? 3801 TYR A CA    1 
ATOM   17088 C  C     . TYR A 1 3801 ? 165.482 113.438 173.334 1.00 28.55  ? 3801 TYR A C     1 
ATOM   17089 O  O     . TYR A 1 3801 ? 165.181 114.605 173.060 1.00 30.13  ? 3801 TYR A O     1 
ATOM   17090 C  CB    . TYR A 1 3801 ? 163.342 112.382 172.616 1.00 27.82  ? 3801 TYR A CB    1 
ATOM   17091 C  CG    . TYR A 1 3801 ? 162.621 111.435 171.684 1.00 28.55  ? 3801 TYR A CG    1 
ATOM   17092 C  CD1   . TYR A 1 3801 ? 162.424 110.106 172.029 1.00 33.88  ? 3801 TYR A CD1   1 
ATOM   17093 C  CD2   . TYR A 1 3801 ? 162.142 111.870 170.456 1.00 33.97  ? 3801 TYR A CD2   1 
ATOM   17094 C  CE1   . TYR A 1 3801 ? 161.768 109.237 171.179 1.00 39.76  ? 3801 TYR A CE1   1 
ATOM   17095 C  CE2   . TYR A 1 3801 ? 161.485 111.008 169.600 1.00 34.22  ? 3801 TYR A CE2   1 
ATOM   17096 C  CZ    . TYR A 1 3801 ? 161.301 109.693 169.966 1.00 37.46  ? 3801 TYR A CZ    1 
ATOM   17097 O  OH    . TYR A 1 3801 ? 160.646 108.832 169.117 1.00 39.85  ? 3801 TYR A OH    1 
ATOM   17098 N  N     . LEU A 1 3802 ? 166.320 113.127 174.322 1.00 27.84  ? 3802 LEU A N     1 
ATOM   17099 C  CA    . LEU A 1 3802 ? 166.969 114.165 175.122 1.00 29.92  ? 3802 LEU A CA    1 
ATOM   17100 C  C     . LEU A 1 3802 ? 167.861 115.099 174.311 1.00 26.48  ? 3802 LEU A C     1 
ATOM   17101 O  O     . LEU A 1 3802 ? 167.786 116.319 174.529 1.00 25.88  ? 3802 LEU A O     1 
ATOM   17102 C  CB    . LEU A 1 3802 ? 167.756 113.508 176.265 1.00 33.04  ? 3802 LEU A CB    1 
ATOM   17103 C  CG    . LEU A 1 3802 ? 168.085 114.413 177.453 1.00 27.22  ? 3802 LEU A CG    1 
ATOM   17104 C  CD1   . LEU A 1 3802 ? 167.004 114.315 178.517 1.00 32.25  ? 3802 LEU A CD1   1 
ATOM   17105 C  CD2   . LEU A 1 3802 ? 169.447 114.071 178.033 1.00 26.64  ? 3802 LEU A CD2   1 
ATOM   17106 N  N     . PRO A 1 3803 ? 168.722 114.624 173.400 1.00 25.23  ? 3803 PRO A N     1 
ATOM   17107 C  CA    . PRO A 1 3803 ? 169.550 115.573 172.633 1.00 20.90  ? 3803 PRO A CA    1 
ATOM   17108 C  C     . PRO A 1 3803 ? 168.745 116.578 171.829 1.00 17.35  ? 3803 PRO A C     1 
ATOM   17109 O  O     . PRO A 1 3803 ? 169.183 117.725 171.678 1.00 16.72  ? 3803 PRO A O     1 
ATOM   17110 C  CB    . PRO A 1 3803 ? 170.377 114.657 171.722 1.00 16.76  ? 3803 PRO A CB    1 
ATOM   17111 C  CG    . PRO A 1 3803 ? 170.433 113.370 172.442 1.00 20.53  ? 3803 PRO A CG    1 
ATOM   17112 C  CD    . PRO A 1 3803 ? 169.098 113.230 173.103 1.00 24.83  ? 3803 PRO A CD    1 
ATOM   17113 N  N     . LEU A 1 3804 ? 167.585 116.183 171.300 1.00 17.82  ? 3804 LEU A N     1 
ATOM   17114 C  CA    . LEU A 1 3804 ? 166.769 117.122 170.538 1.00 17.34  ? 3804 LEU A CA    1 
ATOM   17115 C  C     . LEU A 1 3804 ? 166.260 118.254 171.421 1.00 19.23  ? 3804 LEU A C     1 
ATOM   17116 O  O     . LEU A 1 3804 ? 166.281 119.423 171.018 1.00 18.81  ? 3804 LEU A O     1 
ATOM   17117 C  CB    . LEU A 1 3804 ? 165.601 116.389 169.881 1.00 15.48  ? 3804 LEU A CB    1 
ATOM   17118 C  CG    . LEU A 1 3804 ? 164.563 117.280 169.199 1.00 19.78  ? 3804 LEU A CG    1 
ATOM   17119 C  CD1   . LEU A 1 3804 ? 165.195 118.068 168.062 1.00 22.43  ? 3804 LEU A CD1   1 
ATOM   17120 C  CD2   . LEU A 1 3804 ? 163.399 116.456 168.699 1.00 20.80  ? 3804 LEU A CD2   1 
ATOM   17121 N  N     . SER A 1 3805 ? 165.798 117.926 172.631 1.00 21.33  ? 3805 SER A N     1 
ATOM   17122 C  CA    . SER A 1 3805 ? 165.321 118.958 173.545 1.00 16.99  ? 3805 SER A CA    1 
ATOM   17123 C  C     . SER A 1 3805 ? 166.455 119.877 173.976 1.00 16.21  ? 3805 SER A C     1 
ATOM   17124 O  O     . SER A 1 3805 ? 166.245 121.077 174.188 1.00 19.68  ? 3805 SER A O     1 
ATOM   17125 C  CB    . SER A 1 3805 ? 164.658 118.315 174.763 1.00 20.38  ? 3805 SER A CB    1 
ATOM   17126 O  OG    . SER A 1 3805 ? 165.539 118.299 175.872 1.00 30.56  ? 3805 SER A OG    1 
ATOM   17127 N  N     . THR A 1 3806 ? 167.663 119.329 174.121 1.00 16.54  ? 3806 THR A N     1 
ATOM   17128 C  CA    . THR A 1 3806 ? 168.822 120.165 174.414 1.00 19.58  ? 3806 THR A CA    1 
ATOM   17129 C  C     . THR A 1 3806 ? 169.095 121.136 173.274 1.00 15.70  ? 3806 THR A C     1 
ATOM   17130 O  O     . THR A 1 3806 ? 169.429 122.304 173.507 1.00 14.87  ? 3806 THR A O     1 
ATOM   17131 C  CB    . THR A 1 3806 ? 170.048 119.292 174.679 1.00 24.42  ? 3806 THR A CB    1 
ATOM   17132 O  OG1   . THR A 1 3806 ? 169.698 118.232 175.579 1.00 19.75  ? 3806 THR A OG1   1 
ATOM   17133 C  CG2   . THR A 1 3806 ? 171.168 120.119 175.292 1.00 19.35  ? 3806 THR A CG2   1 
ATOM   17134 N  N     . ALA A 1 3807 ? 168.962 120.667 172.030 1.00 16.56  ? 3807 ALA A N     1 
ATOM   17135 C  CA    . ALA A 1 3807 ? 169.135 121.550 170.882 1.00 15.25  ? 3807 ALA A CA    1 
ATOM   17136 C  C     . ALA A 1 3807 ? 168.074 122.642 170.861 1.00 15.37  ? 3807 ALA A C     1 
ATOM   17137 O  O     . ALA A 1 3807 ? 168.367 123.795 170.528 1.00 15.63  ? 3807 ALA A O     1 
ATOM   17138 C  CB    . ALA A 1 3807 ? 169.098 120.740 169.587 1.00 10.93  ? 3807 ALA A CB    1 
ATOM   17139 N  N     . CYS A 1 3808 ? 166.835 122.297 171.223 1.00 12.84  ? 3808 CYS A N     1 
ATOM   17140 C  CA    . CYS A 1 3808 ? 165.744 123.266 171.175 1.00 14.05  ? 3808 CYS A CA    1 
ATOM   17141 C  C     . CYS A 1 3808 ? 166.012 124.448 172.100 1.00 15.64  ? 3808 CYS A C     1 
ATOM   17142 O  O     . CYS A 1 3808 ? 165.787 125.605 171.728 1.00 16.47  ? 3808 CYS A O     1 
ATOM   17143 C  CB    . CYS A 1 3808 ? 164.426 122.585 171.542 1.00 15.28  ? 3808 CYS A CB    1 
ATOM   17144 S  SG    . CYS A 1 3808 ? 163.833 121.393 170.326 1.00 28.07  ? 3808 CYS A SG    1 
ATOM   17145 N  N     . SER A 1 3809 ? 166.494 124.174 173.314 1.00 16.41  ? 3809 SER A N     1 
ATOM   17146 C  CA    . SER A 1 3809 ? 166.815 125.254 174.240 1.00 16.51  ? 3809 SER A CA    1 
ATOM   17147 C  C     . SER A 1 3809 ? 167.960 126.110 173.714 1.00 15.58  ? 3809 SER A C     1 
ATOM   17148 O  O     . SER A 1 3809 ? 167.961 127.335 173.886 1.00 16.44  ? 3809 SER A O     1 
ATOM   17149 C  CB    . SER A 1 3809 ? 167.159 124.684 175.615 1.00 19.21  ? 3809 SER A CB    1 
ATOM   17150 O  OG    . SER A 1 3809 ? 168.562 124.634 175.810 1.00 22.11  ? 3809 SER A OG    1 
ATOM   17151 N  N     . SER A 1 3810 ? 168.950 125.479 173.077 1.00 14.30  ? 3810 SER A N     1 
ATOM   17152 C  CA    . SER A 1 3810 ? 170.089 126.221 172.549 1.00 11.31  ? 3810 SER A CA    1 
ATOM   17153 C  C     . SER A 1 3810 ? 169.666 127.182 171.444 1.00 12.59  ? 3810 SER A C     1 
ATOM   17154 O  O     . SER A 1 3810 ? 170.189 128.299 171.352 1.00 12.48  ? 3810 SER A O     1 
ATOM   17155 C  CB    . SER A 1 3810 ? 171.153 125.251 172.038 1.00 11.08  ? 3810 SER A CB    1 
ATOM   17156 O  OG    . SER A 1 3810 ? 171.645 124.438 173.088 1.00 13.46  ? 3810 SER A OG    1 
ATOM   17157 N  N     . ILE A 1 3811 ? 168.734 126.760 170.586 1.00 12.91  ? 3811 ILE A N     1 
ATOM   17158 C  CA    . ILE A 1 3811 ? 168.284 127.626 169.499 1.00 9.89   ? 3811 ILE A CA    1 
ATOM   17159 C  C     . ILE A 1 3811 ? 167.551 128.843 170.045 1.00 10.95  ? 3811 ILE A C     1 
ATOM   17160 O  O     . ILE A 1 3811 ? 167.811 129.977 169.629 1.00 12.10  ? 3811 ILE A O     1 
ATOM   17161 C  CB    . ILE A 1 3811 ? 167.407 126.837 168.508 1.00 10.17  ? 3811 ILE A CB    1 
ATOM   17162 C  CG1   . ILE A 1 3811 ? 168.141 125.586 168.021 1.00 10.82  ? 3811 ILE A CG1   1 
ATOM   17163 C  CG2   . ILE A 1 3811 ? 167.000 127.721 167.337 1.00 17.08  ? 3811 ILE A CG2   1 
ATOM   17164 C  CD1   . ILE A 1 3811 ? 167.542 124.960 166.782 1.00 15.78  ? 3811 ILE A CD1   1 
ATOM   17165 N  N     . TYR A 1 3812 ? 166.632 128.631 170.992 1.00 10.60  ? 3812 TYR A N     1 
ATOM   17166 C  CA    . TYR A 1 3812 ? 165.831 129.740 171.504 1.00 9.85   ? 3812 TYR A CA    1 
ATOM   17167 C  C     . TYR A 1 3812 ? 166.695 130.787 172.194 1.00 10.73  ? 3812 TYR A C     1 
ATOM   17168 O  O     . TYR A 1 3812 ? 166.502 131.991 171.992 1.00 12.98  ? 3812 TYR A O     1 
ATOM   17169 C  CB    . TYR A 1 3812 ? 164.755 129.223 172.460 1.00 11.76  ? 3812 TYR A CB    1 
ATOM   17170 C  CG    . TYR A 1 3812 ? 164.162 130.304 173.339 1.00 15.20  ? 3812 TYR A CG    1 
ATOM   17171 C  CD1   . TYR A 1 3812 ? 163.101 131.080 172.896 1.00 17.84  ? 3812 TYR A CD1   1 
ATOM   17172 C  CD2   . TYR A 1 3812 ? 164.649 130.532 174.620 1.00 13.12  ? 3812 TYR A CD2   1 
ATOM   17173 C  CE1   . TYR A 1 3812 ? 162.560 132.068 173.693 1.00 19.28  ? 3812 TYR A CE1   1 
ATOM   17174 C  CE2   . TYR A 1 3812 ? 164.111 131.514 175.423 1.00 16.52  ? 3812 TYR A CE2   1 
ATOM   17175 C  CZ    . TYR A 1 3812 ? 163.065 132.277 174.956 1.00 22.35  ? 3812 TYR A CZ    1 
ATOM   17176 O  OH    . TYR A 1 3812 ? 162.524 133.257 175.756 1.00 27.75  ? 3812 TYR A OH    1 
ATOM   17177 N  N     . PHE A 1 3813 ? 167.649 130.351 173.018 1.00 9.78   ? 3813 PHE A N     1 
ATOM   17178 C  CA    . PHE A 1 3813 ? 168.480 131.311 173.734 1.00 9.84   ? 3813 PHE A CA    1 
ATOM   17179 C  C     . PHE A 1 3813 ? 169.458 132.008 172.799 1.00 11.32  ? 3813 PHE A C     1 
ATOM   17180 O  O     . PHE A 1 3813 ? 169.875 133.139 173.071 1.00 13.98  ? 3813 PHE A O     1 
ATOM   17181 C  CB    . PHE A 1 3813 ? 169.212 130.615 174.879 1.00 12.37  ? 3813 PHE A CB    1 
ATOM   17182 C  CG    . PHE A 1 3813 ? 168.382 130.472 176.121 1.00 12.19  ? 3813 PHE A CG    1 
ATOM   17183 C  CD1   . PHE A 1 3813 ? 168.316 131.495 177.051 1.00 15.44  ? 3813 PHE A CD1   1 
ATOM   17184 C  CD2   . PHE A 1 3813 ? 167.647 129.322 176.345 1.00 14.14  ? 3813 PHE A CD2   1 
ATOM   17185 C  CE1   . PHE A 1 3813 ? 167.543 131.366 178.190 1.00 17.55  ? 3813 PHE A CE1   1 
ATOM   17186 C  CE2   . PHE A 1 3813 ? 166.872 129.187 177.479 1.00 17.98  ? 3813 PHE A CE2   1 
ATOM   17187 C  CZ    . PHE A 1 3813 ? 166.822 130.208 178.404 1.00 17.56  ? 3813 PHE A CZ    1 
ATOM   17188 N  N     . THR A 1 3814 ? 169.836 131.353 171.698 1.00 9.62   ? 3814 THR A N     1 
ATOM   17189 C  CA    . THR A 1 3814 ? 170.583 132.045 170.655 1.00 9.95   ? 3814 THR A CA    1 
ATOM   17190 C  C     . THR A 1 3814 ? 169.731 133.130 170.004 1.00 11.23  ? 3814 THR A C     1 
ATOM   17191 O  O     . THR A 1 3814 ? 170.207 134.246 169.765 1.00 14.01  ? 3814 THR A O     1 
ATOM   17192 C  CB    . THR A 1 3814 ? 171.079 131.040 169.613 1.00 10.78  ? 3814 THR A CB    1 
ATOM   17193 O  OG1   . THR A 1 3814 ? 172.181 130.301 170.152 1.00 17.05  ? 3814 THR A OG1   1 
ATOM   17194 C  CG2   . THR A 1 3814 ? 171.530 131.750 168.344 1.00 13.51  ? 3814 THR A CG2   1 
ATOM   17195 N  N     . MET A 1 3815 ? 168.462 132.822 169.724 1.00 9.35   ? 3815 MET A N     1 
ATOM   17196 C  CA    . MET A 1 3815 ? 167.552 133.833 169.195 1.00 9.82   ? 3815 MET A CA    1 
ATOM   17197 C  C     . MET A 1 3815 ? 167.321 134.947 170.206 1.00 11.87  ? 3815 MET A C     1 
ATOM   17198 O  O     . MET A 1 3815 ? 167.234 136.124 169.836 1.00 15.95  ? 3815 MET A O     1 
ATOM   17199 C  CB    . MET A 1 3815 ? 166.224 133.191 168.801 1.00 11.43  ? 3815 MET A CB    1 
ATOM   17200 C  CG    . MET A 1 3815 ? 166.352 132.034 167.835 1.00 8.53   ? 3815 MET A CG    1 
ATOM   17201 S  SD    . MET A 1 3815 ? 164.774 131.620 167.085 1.00 21.02  ? 3815 MET A SD    1 
ATOM   17202 C  CE    . MET A 1 3815 ? 163.982 130.787 168.446 1.00 11.25  ? 3815 MET A CE    1 
ATOM   17203 N  N     . GLU A 1 3816 ? 167.202 134.593 171.487 1.00 13.73  ? 3816 GLU A N     1 
ATOM   17204 C  CA    . GLU A 1 3816 ? 167.030 135.602 172.527 1.00 13.24  ? 3816 GLU A CA    1 
ATOM   17205 C  C     . GLU A 1 3816 ? 168.207 136.565 172.560 1.00 15.29  ? 3816 GLU A C     1 
ATOM   17206 O  O     . GLU A 1 3816 ? 168.022 137.777 172.720 1.00 19.26  ? 3816 GLU A O     1 
ATOM   17207 C  CB    . GLU A 1 3816 ? 166.849 134.930 173.886 1.00 13.34  ? 3816 GLU A CB    1 
ATOM   17208 C  CG    . GLU A 1 3816 ? 165.405 134.733 174.293 1.00 23.80  ? 3816 GLU A CG    1 
ATOM   17209 C  CD    . GLU A 1 3816 ? 164.891 135.864 175.162 1.00 39.48  ? 3816 GLU A CD    1 
ATOM   17210 O  OE1   . GLU A 1 3816 ? 164.702 136.984 174.641 1.00 32.63  ? 3816 GLU A OE1   1 
ATOM   17211 O  OE2   . GLU A 1 3816 ? 164.679 135.633 176.371 1.00 35.23  ? 3816 GLU A OE2   1 
ATOM   17212 N  N     . SER A 1 3817 ? 169.425 136.046 172.412 1.00 14.94  ? 3817 SER A N     1 
ATOM   17213 C  CA    . SER A 1 3817 ? 170.608 136.894 172.398 1.00 16.49  ? 3817 SER A CA    1 
ATOM   17214 C  C     . SER A 1 3817 ? 170.835 137.570 171.053 1.00 14.05  ? 3817 SER A C     1 
ATOM   17215 O  O     . SER A 1 3817 ? 171.710 138.436 170.960 1.00 18.12  ? 3817 SER A O     1 
ATOM   17216 C  CB    . SER A 1 3817 ? 171.839 136.073 172.783 1.00 22.18  ? 3817 SER A CB    1 
ATOM   17217 O  OG    . SER A 1 3817 ? 172.258 135.256 171.705 1.00 24.92  ? 3817 SER A OG    1 
ATOM   17218 N  N     . LEU A 1 3818 ? 170.072 137.207 170.018 1.00 13.51  ? 3818 LEU A N     1 
ATOM   17219 C  CA    . LEU A 1 3818 ? 170.211 137.867 168.724 1.00 11.88  ? 3818 LEU A CA    1 
ATOM   17220 C  C     . LEU A 1 3818 ? 169.878 139.349 168.794 1.00 12.90  ? 3818 LEU A C     1 
ATOM   17221 O  O     . LEU A 1 3818 ? 170.344 140.118 167.948 1.00 13.32  ? 3818 LEU A O     1 
ATOM   17222 C  CB    . LEU A 1 3818 ? 169.320 137.191 167.681 1.00 8.50   ? 3818 LEU A CB    1 
ATOM   17223 C  CG    . LEU A 1 3818 ? 169.928 136.045 166.873 1.00 9.52   ? 3818 LEU A CG    1 
ATOM   17224 C  CD1   . LEU A 1 3818 ? 168.902 135.471 165.913 1.00 10.74  ? 3818 LEU A CD1   1 
ATOM   17225 C  CD2   . LEU A 1 3818 ? 171.159 136.520 166.121 1.00 14.37  ? 3818 LEU A CD2   1 
ATOM   17226 N  N     . LYS A 1 3819 ? 169.082 139.767 169.780 1.00 13.87  ? 3819 LYS A N     1 
ATOM   17227 C  CA    . LYS A 1 3819 ? 168.755 141.175 169.953 1.00 12.91  ? 3819 LYS A CA    1 
ATOM   17228 C  C     . LYS A 1 3819 ? 169.963 142.023 170.326 1.00 14.79  ? 3819 LYS A C     1 
ATOM   17229 O  O     . LYS A 1 3819 ? 169.898 143.251 170.196 1.00 18.21  ? 3819 LYS A O     1 
ATOM   17230 C  CB    . LYS A 1 3819 ? 167.667 141.325 171.017 1.00 14.95  ? 3819 LYS A CB    1 
ATOM   17231 C  CG    . LYS A 1 3819 ? 168.132 140.999 172.425 1.00 13.19  ? 3819 LYS A CG    1 
ATOM   17232 C  CD    . LYS A 1 3819 ? 167.190 141.573 173.466 1.00 14.80  ? 3819 LYS A CD    1 
ATOM   17233 C  CE    . LYS A 1 3819 ? 166.001 140.653 173.694 1.00 17.67  ? 3819 LYS A CE    1 
ATOM   17234 N  NZ    . LYS A 1 3819 ? 166.366 139.465 174.514 1.00 19.16  ? 3819 LYS A NZ    1 
ATOM   17235 N  N     . GLN A 1 3820 ? 171.057 141.408 170.782 1.00 16.35  ? 3820 GLN A N     1 
ATOM   17236 C  CA    . GLN A 1 3820 ? 172.248 142.171 171.131 1.00 19.65  ? 3820 GLN A CA    1 
ATOM   17237 C  C     . GLN A 1 3820 ? 172.945 142.753 169.909 1.00 18.66  ? 3820 GLN A C     1 
ATOM   17238 O  O     . GLN A 1 3820 ? 173.688 143.730 170.044 1.00 24.49  ? 3820 GLN A O     1 
ATOM   17239 C  CB    . GLN A 1 3820 ? 173.228 141.296 171.915 1.00 25.61  ? 3820 GLN A CB    1 
ATOM   17240 C  CG    . GLN A 1 3820 ? 172.612 140.567 173.098 1.00 23.17  ? 3820 GLN A CG    1 
ATOM   17241 C  CD    . GLN A 1 3820 ? 172.224 141.501 174.222 1.00 30.49  ? 3820 GLN A CD    1 
ATOM   17242 O  OE1   . GLN A 1 3820 ? 173.057 142.241 174.746 1.00 34.07  ? 3820 GLN A OE1   1 
ATOM   17243 N  NE2   . GLN A 1 3820 ? 170.952 141.473 174.601 1.00 31.52  ? 3820 GLN A NE2   1 
ATOM   17244 N  N     . ILE A 1 3821 ? 172.726 142.180 168.723 1.00 16.57  ? 3821 ILE A N     1 
ATOM   17245 C  CA    . ILE A 1 3821 ? 173.362 142.677 167.507 1.00 15.48  ? 3821 ILE A CA    1 
ATOM   17246 C  C     . ILE A 1 3821 ? 172.439 143.558 166.677 1.00 18.92  ? 3821 ILE A C     1 
ATOM   17247 O  O     . ILE A 1 3821 ? 172.922 144.248 165.764 1.00 21.83  ? 3821 ILE A O     1 
ATOM   17248 C  CB    . ILE A 1 3821 ? 173.896 141.516 166.641 1.00 18.63  ? 3821 ILE A CB    1 
ATOM   17249 C  CG1   . ILE A 1 3821 ? 172.755 140.842 165.880 1.00 19.55  ? 3821 ILE A CG1   1 
ATOM   17250 C  CG2   . ILE A 1 3821 ? 174.628 140.504 167.502 1.00 19.55  ? 3821 ILE A CG2   1 
ATOM   17251 C  CD1   . ILE A 1 3821 ? 173.198 139.664 165.047 1.00 24.26  ? 3821 ILE A CD1   1 
ATOM   17252 N  N     . HIS A 1 3822 ? 171.138 143.562 166.960 1.00 19.57  ? 3822 HIS A N     1 
ATOM   17253 C  CA    . HIS A 1 3822 ? 170.202 144.431 166.262 1.00 15.05  ? 3822 HIS A CA    1 
ATOM   17254 C  C     . HIS A 1 3822 ? 168.924 144.536 167.081 1.00 15.01  ? 3822 HIS A C     1 
ATOM   17255 O  O     . HIS A 1 3822 ? 168.434 143.533 167.606 1.00 14.53  ? 3822 HIS A O     1 
ATOM   17256 C  CB    . HIS A 1 3822 ? 169.888 143.910 164.855 1.00 15.04  ? 3822 HIS A CB    1 
ATOM   17257 C  CG    . HIS A 1 3822 ? 169.455 144.979 163.901 1.00 13.57  ? 3822 HIS A CG    1 
ATOM   17258 N  ND1   . HIS A 1 3822 ? 168.190 145.523 163.918 1.00 12.84  ? 3822 HIS A ND1   1 
ATOM   17259 C  CD2   . HIS A 1 3822 ? 170.122 145.609 162.906 1.00 16.12  ? 3822 HIS A CD2   1 
ATOM   17260 C  CE1   . HIS A 1 3822 ? 168.095 146.441 162.973 1.00 15.98  ? 3822 HIS A CE1   1 
ATOM   17261 N  NE2   . HIS A 1 3822 ? 169.253 146.512 162.344 1.00 17.70  ? 3822 HIS A NE2   1 
ATOM   17262 N  N     . PHE A 1 3823 ? 168.393 145.757 167.183 1.00 14.38  ? 3823 PHE A N     1 
ATOM   17263 C  CA    . PHE A 1 3823 ? 167.184 145.988 167.964 1.00 9.90   ? 3823 PHE A CA    1 
ATOM   17264 C  C     . PHE A 1 3823 ? 165.955 145.329 167.353 1.00 11.48  ? 3823 PHE A C     1 
ATOM   17265 O  O     . PHE A 1 3823 ? 164.992 145.052 168.077 1.00 16.16  ? 3823 PHE A O     1 
ATOM   17266 C  CB    . PHE A 1 3823 ? 166.944 147.491 168.124 1.00 9.56   ? 3823 PHE A CB    1 
ATOM   17267 C  CG    . PHE A 1 3823 ? 166.820 148.231 166.820 1.00 14.08  ? 3823 PHE A CG    1 
ATOM   17268 C  CD1   . PHE A 1 3823 ? 165.600 148.324 166.171 1.00 15.77  ? 3823 PHE A CD1   1 
ATOM   17269 C  CD2   . PHE A 1 3823 ? 167.925 148.836 166.246 1.00 17.72  ? 3823 PHE A CD2   1 
ATOM   17270 C  CE1   . PHE A 1 3823 ? 165.485 149.002 164.974 1.00 17.36  ? 3823 PHE A CE1   1 
ATOM   17271 C  CE2   . PHE A 1 3823 ? 167.816 149.517 165.050 1.00 19.03  ? 3823 PHE A CE2   1 
ATOM   17272 C  CZ    . PHE A 1 3823 ? 166.594 149.600 164.414 1.00 18.50  ? 3823 PHE A CZ    1 
ATOM   17273 N  N     . LEU A 1 3824 ? 165.963 145.072 166.046 1.00 12.63  ? 3824 LEU A N     1 
ATOM   17274 C  CA    . LEU A 1 3824 ? 164.814 144.481 165.375 1.00 10.71  ? 3824 LEU A CA    1 
ATOM   17275 C  C     . LEU A 1 3824 ? 164.669 142.990 165.641 1.00 10.71  ? 3824 LEU A C     1 
ATOM   17276 O  O     . LEU A 1 3824 ? 163.592 142.437 165.399 1.00 15.64  ? 3824 LEU A O     1 
ATOM   17277 C  CB    . LEU A 1 3824 ? 164.910 144.725 163.866 1.00 9.77   ? 3824 LEU A CB    1 
ATOM   17278 C  CG    . LEU A 1 3824 ? 163.612 144.693 163.058 1.00 12.24  ? 3824 LEU A CG    1 
ATOM   17279 C  CD1   . LEU A 1 3824 ? 162.872 146.013 163.172 1.00 14.26  ? 3824 LEU A CD1   1 
ATOM   17280 C  CD2   . LEU A 1 3824 ? 163.900 144.362 161.605 1.00 11.93  ? 3824 LEU A CD2   1 
ATOM   17281 N  N     . TYR A 1 3825 ? 165.712 142.332 166.142 1.00 10.66  ? 3825 TYR A N     1 
ATOM   17282 C  CA    . TYR A 1 3825 ? 165.710 140.876 166.294 1.00 10.72  ? 3825 TYR A CA    1 
ATOM   17283 C  C     . TYR A 1 3825 ? 165.074 140.502 167.634 1.00 12.63  ? 3825 TYR A C     1 
ATOM   17284 O  O     . TYR A 1 3825 ? 165.724 140.034 168.570 1.00 15.12  ? 3825 TYR A O     1 
ATOM   17285 C  CB    . TYR A 1 3825 ? 167.126 140.321 166.164 1.00 11.71  ? 3825 TYR A CB    1 
ATOM   17286 C  CG    . TYR A 1 3825 ? 167.828 140.599 164.841 1.00 10.97  ? 3825 TYR A CG    1 
ATOM   17287 C  CD1   . TYR A 1 3825 ? 167.260 141.416 163.871 1.00 11.32  ? 3825 TYR A CD1   1 
ATOM   17288 C  CD2   . TYR A 1 3825 ? 169.075 140.050 164.574 1.00 12.72  ? 3825 TYR A CD2   1 
ATOM   17289 C  CE1   . TYR A 1 3825 ? 167.903 141.667 162.679 1.00 13.32  ? 3825 TYR A CE1   1 
ATOM   17290 C  CE2   . TYR A 1 3825 ? 169.727 140.301 163.382 1.00 17.49  ? 3825 TYR A CE2   1 
ATOM   17291 C  CZ    . TYR A 1 3825 ? 169.134 141.109 162.439 1.00 15.96  ? 3825 TYR A CZ    1 
ATOM   17292 O  OH    . TYR A 1 3825 ? 169.774 141.363 161.248 1.00 15.12  ? 3825 TYR A OH    1 
ATOM   17293 N  N     . GLN A 1 3826 ? 163.763 140.722 167.707 1.00 13.86  ? 3826 GLN A N     1 
ATOM   17294 C  CA    . GLN A 1 3826 ? 162.973 140.418 168.895 1.00 11.14  ? 3826 GLN A CA    1 
ATOM   17295 C  C     . GLN A 1 3826 ? 162.111 139.197 168.597 1.00 14.21  ? 3826 GLN A C     1 
ATOM   17296 O  O     . GLN A 1 3826 ? 161.205 139.259 167.760 1.00 16.09  ? 3826 GLN A O     1 
ATOM   17297 C  CB    . GLN A 1 3826 ? 162.113 141.615 169.293 1.00 10.99  ? 3826 GLN A CB    1 
ATOM   17298 C  CG    . GLN A 1 3826 ? 162.885 142.917 169.432 1.00 11.83  ? 3826 GLN A CG    1 
ATOM   17299 C  CD    . GLN A 1 3826 ? 163.842 142.906 170.606 1.00 15.73  ? 3826 GLN A CD    1 
ATOM   17300 O  OE1   . GLN A 1 3826 ? 163.553 142.326 171.651 1.00 18.07  ? 3826 GLN A OE1   1 
ATOM   17301 N  NE2   . GLN A 1 3826 ? 164.990 143.554 170.440 1.00 11.78  ? 3826 GLN A NE2   1 
ATOM   17302 N  N     . TYR A 1 3827 ? 162.392 138.090 169.280 1.00 14.85  ? 3827 TYR A N     1 
ATOM   17303 C  CA    . TYR A 1 3827 ? 161.714 136.825 169.034 1.00 13.33  ? 3827 TYR A CA    1 
ATOM   17304 C  C     . TYR A 1 3827 ? 161.179 136.291 170.353 1.00 18.13  ? 3827 TYR A C     1 
ATOM   17305 O  O     . TYR A 1 3827 ? 161.949 136.068 171.292 1.00 20.92  ? 3827 TYR A O     1 
ATOM   17306 C  CB    . TYR A 1 3827 ? 162.665 135.817 168.384 1.00 16.02  ? 3827 TYR A CB    1 
ATOM   17307 C  CG    . TYR A 1 3827 ? 163.106 136.223 166.998 1.00 16.30  ? 3827 TYR A CG    1 
ATOM   17308 C  CD1   . TYR A 1 3827 ? 162.306 135.978 165.894 1.00 17.62  ? 3827 TYR A CD1   1 
ATOM   17309 C  CD2   . TYR A 1 3827 ? 164.322 136.861 166.795 1.00 13.88  ? 3827 TYR A CD2   1 
ATOM   17310 C  CE1   . TYR A 1 3827 ? 162.705 136.352 164.624 1.00 20.01  ? 3827 TYR A CE1   1 
ATOM   17311 C  CE2   . TYR A 1 3827 ? 164.729 137.239 165.532 1.00 14.81  ? 3827 TYR A CE2   1 
ATOM   17312 C  CZ    . TYR A 1 3827 ? 163.917 136.983 164.450 1.00 21.11  ? 3827 TYR A CZ    1 
ATOM   17313 O  OH    . TYR A 1 3827 ? 164.319 137.357 163.189 1.00 23.21  ? 3827 TYR A OH    1 
ATOM   17314 N  N     . SER A 1 3828 ? 159.866 136.088 170.420 1.00 21.32  ? 3828 SER A N     1 
ATOM   17315 C  CA    . SER A 1 3828 ? 159.227 135.597 171.629 1.00 17.46  ? 3828 SER A CA    1 
ATOM   17316 C  C     . SER A 1 3828 ? 159.393 134.083 171.753 1.00 20.64  ? 3828 SER A C     1 
ATOM   17317 O  O     . SER A 1 3828 ? 159.788 133.389 170.813 1.00 27.52  ? 3828 SER A O     1 
ATOM   17318 C  CB    . SER A 1 3828 ? 157.746 135.968 171.638 1.00 19.65  ? 3828 SER A CB    1 
ATOM   17319 O  OG    . SER A 1 3828 ? 157.044 135.283 170.615 1.00 19.13  ? 3828 SER A OG    1 
ATOM   17320 N  N     . LEU A 1 3829 ? 159.085 133.573 172.949 1.00 15.74  ? 3829 LEU A N     1 
ATOM   17321 C  CA    . LEU A 1 3829 ? 159.081 132.130 173.161 1.00 13.76  ? 3829 LEU A CA    1 
ATOM   17322 C  C     . LEU A 1 3829 ? 158.018 131.443 172.315 1.00 16.28  ? 3829 LEU A C     1 
ATOM   17323 O  O     . LEU A 1 3829 ? 158.215 130.305 171.877 1.00 22.76  ? 3829 LEU A O     1 
ATOM   17324 C  CB    . LEU A 1 3829 ? 158.867 131.815 174.642 1.00 19.54  ? 3829 LEU A CB    1 
ATOM   17325 C  CG    . LEU A 1 3829 ? 158.879 130.341 175.056 1.00 16.83  ? 3829 LEU A CG    1 
ATOM   17326 C  CD1   . LEU A 1 3829 ? 160.272 129.748 174.940 1.00 17.46  ? 3829 LEU A CD1   1 
ATOM   17327 C  CD2   . LEU A 1 3829 ? 158.342 130.178 176.466 1.00 22.83  ? 3829 LEU A CD2   1 
ATOM   17328 N  N     . GLN A 1 3830 ? 156.889 132.114 172.078 1.00 19.00  ? 3830 GLN A N     1 
ATOM   17329 C  CA    . GLN A 1 3830 ? 155.836 131.529 171.257 1.00 19.04  ? 3830 GLN A CA    1 
ATOM   17330 C  C     . GLN A 1 3830 ? 156.289 131.325 169.817 1.00 21.97  ? 3830 GLN A C     1 
ATOM   17331 O  O     . GLN A 1 3830 ? 155.872 130.358 169.170 1.00 28.71  ? 3830 GLN A O     1 
ATOM   17332 C  CB    . GLN A 1 3830 ? 154.587 132.410 171.298 1.00 20.86  ? 3830 GLN A CB    1 
ATOM   17333 C  CG    . GLN A 1 3830 ? 153.335 131.739 170.762 1.00 27.10  ? 3830 GLN A CG    1 
ATOM   17334 C  CD    . GLN A 1 3830 ? 153.246 130.276 171.145 1.00 32.58  ? 3830 GLN A CD    1 
ATOM   17335 O  OE1   . GLN A 1 3830 ? 153.197 129.933 172.326 1.00 31.18  ? 3830 GLN A OE1   1 
ATOM   17336 N  NE2   . GLN A 1 3830 ? 153.225 129.403 170.145 1.00 31.48  ? 3830 GLN A NE2   1 
ATOM   17337 N  N     . PHE A 1 3831 ? 157.129 132.223 169.297 1.00 17.72  ? 3831 PHE A N     1 
ATOM   17338 C  CA    . PHE A 1 3831 ? 157.606 132.081 167.926 1.00 14.71  ? 3831 PHE A CA    1 
ATOM   17339 C  C     . PHE A 1 3831 ? 158.427 130.807 167.761 1.00 19.21  ? 3831 PHE A C     1 
ATOM   17340 O  O     . PHE A 1 3831 ? 158.289 130.090 166.763 1.00 20.70  ? 3831 PHE A O     1 
ATOM   17341 C  CB    . PHE A 1 3831 ? 158.425 133.306 167.524 1.00 14.51  ? 3831 PHE A CB    1 
ATOM   17342 C  CG    . PHE A 1 3831 ? 158.924 133.260 166.109 1.00 16.33  ? 3831 PHE A CG    1 
ATOM   17343 C  CD1   . PHE A 1 3831 ? 158.035 133.166 165.051 1.00 21.24  ? 3831 PHE A CD1   1 
ATOM   17344 C  CD2   . PHE A 1 3831 ? 160.279 133.293 165.837 1.00 15.88  ? 3831 PHE A CD2   1 
ATOM   17345 C  CE1   . PHE A 1 3831 ? 158.490 133.119 163.749 1.00 20.92  ? 3831 PHE A CE1   1 
ATOM   17346 C  CE2   . PHE A 1 3831 ? 160.740 133.246 164.536 1.00 18.09  ? 3831 PHE A CE2   1 
ATOM   17347 C  CZ    . PHE A 1 3831 ? 159.844 133.160 163.491 1.00 18.52  ? 3831 PHE A CZ    1 
ATOM   17348 N  N     . PHE A 1 3832 ? 159.297 130.513 168.732 1.00 15.74  ? 3832 PHE A N     1 
ATOM   17349 C  CA    . PHE A 1 3832 ? 160.055 129.268 168.684 1.00 15.05  ? 3832 PHE A CA    1 
ATOM   17350 C  C     . PHE A 1 3832 ? 159.141 128.059 168.815 1.00 17.43  ? 3832 PHE A C     1 
ATOM   17351 O  O     . PHE A 1 3832 ? 159.332 127.050 168.124 1.00 20.17  ? 3832 PHE A O     1 
ATOM   17352 C  CB    . PHE A 1 3832 ? 161.115 129.244 169.783 1.00 15.05  ? 3832 PHE A CB    1 
ATOM   17353 C  CG    . PHE A 1 3832 ? 161.831 127.931 169.896 1.00 15.42  ? 3832 PHE A CG    1 
ATOM   17354 C  CD1   . PHE A 1 3832 ? 162.783 127.564 168.961 1.00 17.13  ? 3832 PHE A CD1   1 
ATOM   17355 C  CD2   . PHE A 1 3832 ? 161.542 127.058 170.928 1.00 18.58  ? 3832 PHE A CD2   1 
ATOM   17356 C  CE1   . PHE A 1 3832 ? 163.438 126.356 169.058 1.00 18.87  ? 3832 PHE A CE1   1 
ATOM   17357 C  CE2   . PHE A 1 3832 ? 162.193 125.848 171.030 1.00 17.59  ? 3832 PHE A CE2   1 
ATOM   17358 C  CZ    . PHE A 1 3832 ? 163.142 125.497 170.092 1.00 19.07  ? 3832 PHE A CZ    1 
ATOM   17359 N  N     . LEU A 1 3833 ? 158.149 128.138 169.703 1.00 15.17  ? 3833 LEU A N     1 
ATOM   17360 C  CA    . LEU A 1 3833 ? 157.212 127.032 169.863 1.00 17.05  ? 3833 LEU A CA    1 
ATOM   17361 C  C     . LEU A 1 3833 ? 156.429 126.790 168.580 1.00 20.07  ? 3833 LEU A C     1 
ATOM   17362 O  O     . LEU A 1 3833 ? 156.092 125.645 168.260 1.00 22.90  ? 3833 LEU A O     1 
ATOM   17363 C  CB    . LEU A 1 3833 ? 156.270 127.309 171.034 1.00 19.86  ? 3833 LEU A CB    1 
ATOM   17364 C  CG    . LEU A 1 3833 ? 156.905 127.266 172.426 1.00 16.33  ? 3833 LEU A CG    1 
ATOM   17365 C  CD1   . LEU A 1 3833 ? 155.846 127.430 173.501 1.00 20.35  ? 3833 LEU A CD1   1 
ATOM   17366 C  CD2   . LEU A 1 3833 ? 157.678 125.972 172.627 1.00 14.76  ? 3833 LEU A CD2   1 
ATOM   17367 N  N     . ASP A 1 3834 ? 156.135 127.856 167.830 1.00 21.67  ? 3834 ASP A N     1 
ATOM   17368 C  CA    . ASP A 1 3834 ? 155.512 127.691 166.521 1.00 21.87  ? 3834 ASP A CA    1 
ATOM   17369 C  C     . ASP A 1 3834 ? 156.440 126.957 165.560 1.00 22.48  ? 3834 ASP A C     1 
ATOM   17370 O  O     . ASP A 1 3834 ? 155.995 126.099 164.789 1.00 26.45  ? 3834 ASP A O     1 
ATOM   17371 C  CB    . ASP A 1 3834 ? 155.118 129.054 165.951 1.00 25.04  ? 3834 ASP A CB    1 
ATOM   17372 C  CG    . ASP A 1 3834 ? 153.975 129.696 166.713 1.00 37.53  ? 3834 ASP A CG    1 
ATOM   17373 O  OD1   . ASP A 1 3834 ? 153.788 130.924 166.580 1.00 33.65  ? 3834 ASP A OD1   1 
ATOM   17374 O  OD2   . ASP A 1 3834 ? 153.265 128.974 167.444 1.00 39.45  ? 3834 ASP A OD2   1 
ATOM   17375 N  N     . ILE A 1 3835 ? 157.733 127.288 165.586 1.00 17.91  ? 3835 ILE A N     1 
ATOM   17376 C  CA    . ILE A 1 3835 ? 158.706 126.577 164.759 1.00 16.28  ? 3835 ILE A CA    1 
ATOM   17377 C  C     . ILE A 1 3835 ? 158.799 125.120 165.194 1.00 21.11  ? 3835 ILE A C     1 
ATOM   17378 O  O     . ILE A 1 3835 ? 158.812 124.202 164.365 1.00 27.29  ? 3835 ILE A O     1 
ATOM   17379 C  CB    . ILE A 1 3835 ? 160.077 127.275 164.825 1.00 16.42  ? 3835 ILE A CB    1 
ATOM   17380 C  CG1   . ILE A 1 3835 ? 160.026 128.627 164.114 1.00 19.04  ? 3835 ILE A CG1   1 
ATOM   17381 C  CG2   . ILE A 1 3835 ? 161.159 126.398 164.216 1.00 14.87  ? 3835 ILE A CG2   1 
ATOM   17382 C  CD1   . ILE A 1 3835 ? 161.236 129.493 164.374 1.00 17.67  ? 3835 ILE A CD1   1 
ATOM   17383 N  N     . TYR A 1 3836 ? 158.866 124.889 166.507 1.00 21.10  ? 3836 TYR A N     1 
ATOM   17384 C  CA    . TYR A 1 3836 ? 158.902 123.526 167.026 1.00 16.79  ? 3836 TYR A CA    1 
ATOM   17385 C  C     . TYR A 1 3836 ? 157.608 122.786 166.711 1.00 19.21  ? 3836 TYR A C     1 
ATOM   17386 O  O     . TYR A 1 3836 ? 157.626 121.592 166.390 1.00 24.67  ? 3836 TYR A O     1 
ATOM   17387 C  CB    . TYR A 1 3836 ? 159.159 123.557 168.533 1.00 17.17  ? 3836 TYR A CB    1 
ATOM   17388 C  CG    . TYR A 1 3836 ? 159.638 122.247 169.110 1.00 19.39  ? 3836 TYR A CG    1 
ATOM   17389 C  CD1   . TYR A 1 3836 ? 160.453 121.399 168.375 1.00 21.32  ? 3836 TYR A CD1   1 
ATOM   17390 C  CD2   . TYR A 1 3836 ? 159.284 121.862 170.394 1.00 19.72  ? 3836 TYR A CD2   1 
ATOM   17391 C  CE1   . TYR A 1 3836 ? 160.896 120.203 168.901 1.00 22.35  ? 3836 TYR A CE1   1 
ATOM   17392 C  CE2   . TYR A 1 3836 ? 159.723 120.668 170.928 1.00 18.77  ? 3836 TYR A CE2   1 
ATOM   17393 C  CZ    . TYR A 1 3836 ? 160.529 119.844 170.177 1.00 22.02  ? 3836 TYR A CZ    1 
ATOM   17394 O  OH    . TYR A 1 3836 ? 160.968 118.654 170.706 1.00 27.12  ? 3836 TYR A OH    1 
ATOM   17395 N  N     . HIS A 1 3837 ? 156.472 123.482 166.806 1.00 21.92  ? 3837 HIS A N     1 
ATOM   17396 C  CA    . HIS A 1 3837 ? 155.187 122.882 166.459 1.00 25.75  ? 3837 HIS A CA    1 
ATOM   17397 C  C     . HIS A 1 3837 ? 155.140 122.492 164.986 1.00 32.66  ? 3837 HIS A C     1 
ATOM   17398 O  O     . HIS A 1 3837 ? 154.608 121.433 164.632 1.00 37.89  ? 3837 HIS A O     1 
ATOM   17399 C  CB    . HIS A 1 3837 ? 154.059 123.859 166.793 1.00 28.88  ? 3837 HIS A CB    1 
ATOM   17400 C  CG    . HIS A 1 3837 ? 152.685 123.326 166.532 1.00 40.13  ? 3837 HIS A CG    1 
ATOM   17401 N  ND1   . HIS A 1 3837 ? 152.138 122.287 167.254 1.00 41.18  ? 3837 HIS A ND1   1 
ATOM   17402 C  CD2   . HIS A 1 3837 ? 151.742 123.698 165.635 1.00 44.81  ? 3837 HIS A CD2   1 
ATOM   17403 C  CE1   . HIS A 1 3837 ? 150.917 122.042 166.811 1.00 45.30  ? 3837 HIS A CE1   1 
ATOM   17404 N  NE2   . HIS A 1 3837 ? 150.654 122.882 165.827 1.00 48.05  ? 3837 HIS A NE2   1 
ATOM   17405 N  N     . ASN A 1 3838 ? 155.682 123.345 164.113 1.00 28.26  ? 3838 ASN A N     1 
ATOM   17406 C  CA    . ASN A 1 3838 ? 155.662 123.063 162.681 1.00 24.99  ? 3838 ASN A CA    1 
ATOM   17407 C  C     . ASN A 1 3838 ? 156.472 121.817 162.345 1.00 25.65  ? 3838 ASN A C     1 
ATOM   17408 O  O     . ASN A 1 3838 ? 156.041 120.986 161.538 1.00 35.68  ? 3838 ASN A O     1 
ATOM   17409 C  CB    . ASN A 1 3838 ? 156.192 124.270 161.906 1.00 26.55  ? 3838 ASN A CB    1 
ATOM   17410 C  CG    . ASN A 1 3838 ? 156.422 123.967 160.438 1.00 27.73  ? 3838 ASN A CG    1 
ATOM   17411 O  OD1   . ASN A 1 3838 ? 157.560 123.799 159.998 1.00 30.01  ? 3838 ASN A OD1   1 
ATOM   17412 N  ND2   . ASN A 1 3838 ? 155.341 123.900 159.672 1.00 23.77  ? 3838 ASN A ND2   1 
ATOM   17413 N  N     . VAL A 1 3839 ? 157.650 121.671 162.953 1.00 26.36  ? 3839 VAL A N     1 
ATOM   17414 C  CA    . VAL A 1 3839 ? 158.517 120.541 162.636 1.00 23.10  ? 3839 VAL A CA    1 
ATOM   17415 C  C     . VAL A 1 3839 ? 157.900 119.236 163.128 1.00 31.20  ? 3839 VAL A C     1 
ATOM   17416 O  O     . VAL A 1 3839 ? 158.015 118.193 162.474 1.00 37.36  ? 3839 VAL A O     1 
ATOM   17417 C  CB    . VAL A 1 3839 ? 159.921 120.770 163.226 1.00 21.92  ? 3839 VAL A CB    1 
ATOM   17418 C  CG1   . VAL A 1 3839 ? 160.763 119.508 163.134 1.00 27.49  ? 3839 VAL A CG1   1 
ATOM   17419 C  CG2   . VAL A 1 3839 ? 160.609 121.926 162.519 1.00 19.41  ? 3839 VAL A CG2   1 
ATOM   17420 N  N     . LEU A 1 3840 ? 157.237 119.270 164.284 1.00 29.42  ? 3840 LEU A N     1 
ATOM   17421 C  CA    . LEU A 1 3840 ? 156.708 118.044 164.871 1.00 30.04  ? 3840 LEU A CA    1 
ATOM   17422 C  C     . LEU A 1 3840 ? 155.470 117.542 164.135 1.00 37.10  ? 3840 LEU A C     1 
ATOM   17423 O  O     . LEU A 1 3840 ? 155.335 116.339 163.885 1.00 42.28  ? 3840 LEU A O     1 
ATOM   17424 C  CB    . LEU A 1 3840 ? 156.395 118.269 166.351 1.00 32.51  ? 3840 LEU A CB    1 
ATOM   17425 C  CG    . LEU A 1 3840 ? 157.593 118.150 167.292 1.00 27.37  ? 3840 LEU A CG    1 
ATOM   17426 C  CD1   . LEU A 1 3840 ? 157.212 118.539 168.711 1.00 26.97  ? 3840 LEU A CD1   1 
ATOM   17427 C  CD2   . LEU A 1 3840 ? 158.150 116.741 167.249 1.00 30.64  ? 3840 LEU A CD2   1 
ATOM   17428 N  N     . TYR A 1 3841 ? 154.557 118.445 163.776 1.00 36.45  ? 3841 TYR A N     1 
ATOM   17429 C  CA    . TYR A 1 3841 ? 153.254 118.055 163.249 1.00 35.22  ? 3841 TYR A CA    1 
ATOM   17430 C  C     . TYR A 1 3841 ? 153.013 118.440 161.798 1.00 38.42  ? 3841 TYR A C     1 
ATOM   17431 O  O     . TYR A 1 3841 ? 152.303 117.716 161.099 1.00 43.37  ? 3841 TYR A O     1 
ATOM   17432 C  CB    . TYR A 1 3841 ? 152.138 118.655 164.113 1.00 35.24  ? 3841 TYR A CB    1 
ATOM   17433 C  CG    . TYR A 1 3841 ? 152.223 118.251 165.566 1.00 42.18  ? 3841 TYR A CG    1 
ATOM   17434 C  CD1   . TYR A 1 3841 ? 152.143 116.918 165.940 1.00 43.09  ? 3841 TYR A CD1   1 
ATOM   17435 C  CD2   . TYR A 1 3841 ? 152.412 119.198 166.560 1.00 42.12  ? 3841 TYR A CD2   1 
ATOM   17436 C  CE1   . TYR A 1 3841 ? 152.221 116.543 167.264 1.00 41.10  ? 3841 TYR A CE1   1 
ATOM   17437 C  CE2   . TYR A 1 3841 ? 152.495 118.833 167.889 1.00 42.46  ? 3841 TYR A CE2   1 
ATOM   17438 C  CZ    . TYR A 1 3841 ? 152.402 117.504 168.235 1.00 45.03  ? 3841 TYR A CZ    1 
ATOM   17439 O  OH    . TYR A 1 3841 ? 152.487 117.136 169.558 1.00 50.54  ? 3841 TYR A OH    1 
ATOM   17440 N  N     . GLU A 1 3842 ? 153.573 119.550 161.324 1.00 34.51  ? 3842 GLU A N     1 
ATOM   17441 C  CA    . GLU A 1 3842 ? 153.391 119.982 159.939 1.00 34.10  ? 3842 GLU A CA    1 
ATOM   17442 C  C     . GLU A 1 3842 ? 154.623 119.696 159.092 1.00 39.54  ? 3842 GLU A C     1 
ATOM   17443 O  O     . GLU A 1 3842 ? 154.990 120.493 158.224 1.00 41.87  ? 3842 GLU A O     1 
ATOM   17444 C  CB    . GLU A 1 3842 ? 153.029 121.463 159.880 1.00 33.64  ? 3842 GLU A CB    1 
ATOM   17445 C  CG    . GLU A 1 3842 ? 152.167 121.949 161.033 1.00 39.43  ? 3842 GLU A CG    1 
ATOM   17446 C  CD    . GLU A 1 3842 ? 152.374 123.422 161.333 1.00 42.30  ? 3842 GLU A CD    1 
ATOM   17447 O  OE1   . GLU A 1 3842 ? 153.208 124.057 160.654 1.00 36.83  ? 3842 GLU A OE1   1 
ATOM   17448 O  OE2   . GLU A 1 3842 ? 151.703 123.945 162.247 1.00 41.91  ? 3842 GLU A OE2   1 
ATOM   17449 N  N     . ASN A 1 3843 ? 155.280 118.560 159.327 1.00 41.40  ? 3843 ASN A N     1 
ATOM   17450 C  CA    . ASN A 1 3843 ? 156.507 118.224 158.619 1.00 42.26  ? 3843 ASN A CA    1 
ATOM   17451 C  C     . ASN A 1 3843 ? 156.170 117.428 157.366 1.00 47.74  ? 3843 ASN A C     1 
ATOM   17452 O  O     . ASN A 1 3843 ? 155.645 116.309 157.481 1.00 53.06  ? 3843 ASN A O     1 
ATOM   17453 C  CB    . ASN A 1 3843 ? 157.438 117.423 159.516 1.00 41.30  ? 3843 ASN A CB    1 
ATOM   17454 C  CG    . ASN A 1 3843 ? 158.882 117.843 159.372 1.00 42.28  ? 3843 ASN A CG    1 
ATOM   17455 O  OD1   . ASN A 1 3843 ? 159.220 118.645 158.504 1.00 46.02  ? 3843 ASN A OD1   1 
ATOM   17456 N  ND2   . ASN A 1 3843 ? 159.746 117.302 160.223 1.00 41.15  ? 3843 ASN A ND2   1 
ATOM   17457 N  N     . PRO A 1 3844 ? 156.441 117.948 156.166 1.00 49.02  ? 3844 PRO A N     1 
ATOM   17458 C  CA    . PRO A 1 3844 ? 156.209 117.147 154.953 1.00 50.44  ? 3844 PRO A CA    1 
ATOM   17459 C  C     . PRO A 1 3844 ? 157.133 115.949 154.830 1.00 51.89  ? 3844 PRO A C     1 
ATOM   17460 O  O     . PRO A 1 3844 ? 156.815 115.020 154.077 1.00 51.88  ? 3844 PRO A O     1 
ATOM   17461 C  CB    . PRO A 1 3844 ? 156.444 118.151 153.813 1.00 49.45  ? 3844 PRO A CB    1 
ATOM   17462 C  CG    . PRO A 1 3844 ? 156.422 119.506 154.462 1.00 48.38  ? 3844 PRO A CG    1 
ATOM   17463 C  CD    . PRO A 1 3844 ? 156.925 119.300 155.850 1.00 46.96  ? 3844 PRO A CD    1 
ATOM   17464 N  N     . ASN A 1 3845 ? 158.259 115.935 155.540 1.00 48.88  ? 3845 ASN A N     1 
ATOM   17465 C  CA    . ASN A 1 3845 ? 159.218 114.842 155.450 1.00 48.25  ? 3845 ASN A CA    1 
ATOM   17466 C  C     . ASN A 1 3845 ? 158.862 113.659 156.340 1.00 49.26  ? 3845 ASN A C     1 
ATOM   17467 O  O     . ASN A 1 3845 ? 159.559 112.640 156.293 1.00 50.41  ? 3845 ASN A O     1 
ATOM   17468 C  CB    . ASN A 1 3845 ? 160.620 115.348 155.799 1.00 47.23  ? 3845 ASN A CB    1 
ATOM   17469 C  CG    . ASN A 1 3845 ? 161.038 116.533 154.953 1.00 51.11  ? 3845 ASN A CG    1 
ATOM   17470 O  OD1   . ASN A 1 3845 ? 160.928 116.506 153.728 1.00 58.36  ? 3845 ASN A OD1   1 
ATOM   17471 N  ND2   . ASN A 1 3845 ? 161.522 117.584 155.605 1.00 42.84  ? 3845 ASN A ND2   1 
ATOM   17472 N  N     . LEU A 1 3846 ? 157.805 113.766 157.146 1.00 49.89  ? 3846 LEU A N     1 
ATOM   17473 C  CA    . LEU A 1 3846 ? 157.344 112.677 157.997 1.00 52.33  ? 3846 LEU A CA    1 
ATOM   17474 C  C     . LEU A 1 3846 ? 156.075 112.026 157.457 1.00 62.06  ? 3846 LEU A C     1 
ATOM   17475 O  O     . LEU A 1 3846 ? 155.329 111.395 158.214 1.00 63.79  ? 3846 LEU A O     1 
ATOM   17476 C  CB    . LEU A 1 3846 ? 157.118 113.179 159.423 1.00 43.60  ? 3846 LEU A CB    1 
ATOM   17477 C  CG    . LEU A 1 3846 ? 158.359 113.659 160.176 1.00 41.76  ? 3846 LEU A CG    1 
ATOM   17478 C  CD1   . LEU A 1 3846 ? 157.988 114.175 161.558 1.00 39.82  ? 3846 LEU A CD1   1 
ATOM   17479 C  CD2   . LEU A 1 3846 ? 159.390 112.547 160.272 1.00 42.76  ? 3846 LEU A CD2   1 
ATOM   17480 N  N     . LYS A 1 3847 ? 155.816 112.177 156.156 1.00 62.52  ? 3847 LYS A N     1 
ATOM   17481 C  CA    . LYS A 1 3847 ? 154.575 111.677 155.573 1.00 64.15  ? 3847 LYS A CA    1 
ATOM   17482 C  C     . LYS A 1 3847 ? 154.483 110.158 155.667 1.00 69.47  ? 3847 LYS A C     1 
ATOM   17483 O  O     . LYS A 1 3847 ? 153.431 109.611 156.017 1.00 71.15  ? 3847 LYS A O     1 
ATOM   17484 C  CB    . LYS A 1 3847 ? 154.465 112.133 154.117 1.00 68.31  ? 3847 LYS A CB    1 
ATOM   17485 C  CG    . LYS A 1 3847 ? 153.881 113.526 153.945 1.00 74.05  ? 3847 LYS A CG    1 
ATOM   17486 C  CD    . LYS A 1 3847 ? 152.413 113.564 154.331 1.00 73.40  ? 3847 LYS A CD    1 
ATOM   17487 C  CE    . LYS A 1 3847 ? 151.648 114.562 153.478 1.00 74.85  ? 3847 LYS A CE    1 
ATOM   17488 N  NZ    . LYS A 1 3847 ? 151.676 114.195 152.036 1.00 73.10  ? 3847 LYS A NZ    1 
ATOM   17489 N  N     . GLY A 1 3848 ? 155.575 109.460 155.364 1.00 66.69  ? 3848 GLY A N     1 
ATOM   17490 C  CA    . GLY A 1 3848 ? 155.541 108.011 155.323 1.00 64.01  ? 3848 GLY A CA    1 
ATOM   17491 C  C     . GLY A 1 3848 ? 156.602 107.328 156.161 1.00 62.25  ? 3848 GLY A C     1 
ATOM   17492 O  O     . GLY A 1 3848 ? 156.739 106.102 156.113 1.00 66.95  ? 3848 GLY A O     1 
ATOM   17493 N  N     . VAL A 1 3849 ? 157.360 108.102 156.929 1.00 65.11  ? 3849 VAL A N     1 
ATOM   17494 C  CA    . VAL A 1 3849 ? 158.417 107.544 157.765 1.00 66.03  ? 3849 VAL A CA    1 
ATOM   17495 C  C     . VAL A 1 3849 ? 157.800 106.987 159.040 1.00 59.12  ? 3849 VAL A C     1 
ATOM   17496 O  O     . VAL A 1 3849 ? 156.997 107.656 159.701 1.00 57.73  ? 3849 VAL A O     1 
ATOM   17497 C  CB    . VAL A 1 3849 ? 159.483 108.605 158.078 1.00 58.23  ? 3849 VAL A CB    1 
ATOM   17498 C  CG1   . VAL A 1 3849 ? 160.700 107.958 158.720 1.00 51.19  ? 3849 VAL A CG1   1 
ATOM   17499 C  CG2   . VAL A 1 3849 ? 159.874 109.350 156.813 1.00 55.82  ? 3849 VAL A CG2   1 
ATOM   17500 N  N     . THR A 1 3850 ? 158.174 105.754 159.389 1.00 57.63  ? 3850 THR A N     1 
ATOM   17501 C  CA    . THR A 1 3850 ? 157.656 105.093 160.577 1.00 59.03  ? 3850 THR A CA    1 
ATOM   17502 C  C     . THR A 1 3850 ? 158.712 104.783 161.627 1.00 61.69  ? 3850 THR A C     1 
ATOM   17503 O  O     . THR A 1 3850 ? 158.356 104.636 162.802 1.00 60.64  ? 3850 THR A O     1 
ATOM   17504 C  CB    . THR A 1 3850 ? 156.942 103.784 160.202 1.00 60.43  ? 3850 THR A CB    1 
ATOM   17505 O  OG1   . THR A 1 3850 ? 156.401 103.177 161.382 1.00 58.12  ? 3850 THR A OG1   1 
ATOM   17506 C  CG2   . THR A 1 3850 ? 157.909 102.815 159.532 1.00 52.64  ? 3850 THR A CG2   1 
ATOM   17507 N  N     . ASP A 1 3851 ? 159.982 104.668 161.247 1.00 57.20  ? 3851 ASP A N     1 
ATOM   17508 C  CA    . ASP A 1 3851 ? 161.034 104.389 162.215 1.00 56.55  ? 3851 ASP A CA    1 
ATOM   17509 C  C     . ASP A 1 3851 ? 161.150 105.533 163.214 1.00 56.89  ? 3851 ASP A C     1 
ATOM   17510 O  O     . ASP A 1 3851 ? 161.159 106.707 162.832 1.00 59.85  ? 3851 ASP A O     1 
ATOM   17511 C  CB    . ASP A 1 3851 ? 162.367 104.171 161.502 1.00 54.70  ? 3851 ASP A CB    1 
ATOM   17512 C  CG    . ASP A 1 3851 ? 163.443 103.633 162.426 1.00 58.42  ? 3851 ASP A CG    1 
ATOM   17513 O  OD1   . ASP A 1 3851 ? 163.111 103.227 163.560 1.00 58.62  ? 3851 ASP A OD1   1 
ATOM   17514 O  OD2   . ASP A 1 3851 ? 164.624 103.621 162.020 1.00 56.86  ? 3851 ASP A OD2   1 
ATOM   17515 N  N     . HIS A 1 3852 ? 161.235 105.187 164.500 1.00 52.24  ? 3852 HIS A N     1 
ATOM   17516 C  CA    . HIS A 1 3852 ? 161.368 106.208 165.534 1.00 49.42  ? 3852 HIS A CA    1 
ATOM   17517 C  C     . HIS A 1 3852 ? 162.683 106.966 165.397 1.00 47.41  ? 3852 HIS A C     1 
ATOM   17518 O  O     . HIS A 1 3852 ? 162.714 108.195 165.535 1.00 51.34  ? 3852 HIS A O     1 
ATOM   17519 C  CB    . HIS A 1 3852 ? 161.253 105.569 166.917 1.00 49.75  ? 3852 HIS A CB    1 
ATOM   17520 C  CG    . HIS A 1 3852 ? 159.889 105.035 167.222 1.00 47.23  ? 3852 HIS A CG    1 
ATOM   17521 N  ND1   . HIS A 1 3852 ? 158.746 105.793 167.089 1.00 56.01  ? 3852 HIS A ND1   1 
ATOM   17522 C  CD2   . HIS A 1 3852 ? 159.484 103.814 167.644 1.00 46.20  ? 3852 HIS A CD2   1 
ATOM   17523 C  CE1   . HIS A 1 3852 ? 157.696 105.064 167.421 1.00 51.59  ? 3852 HIS A CE1   1 
ATOM   17524 N  NE2   . HIS A 1 3852 ? 158.116 103.859 167.762 1.00 55.41  ? 3852 HIS A NE2   1 
ATOM   17525 N  N     . THR A 1 3853 ? 163.778 106.251 165.132 1.00 43.08  ? 3853 THR A N     1 
ATOM   17526 C  CA    . THR A 1 3853 ? 165.069 106.911 164.959 1.00 43.41  ? 3853 THR A CA    1 
ATOM   17527 C  C     . THR A 1 3853 ? 165.094 107.761 163.694 1.00 45.51  ? 3853 THR A C     1 
ATOM   17528 O  O     . THR A 1 3853 ? 165.618 108.881 163.703 1.00 43.19  ? 3853 THR A O     1 
ATOM   17529 C  CB    . THR A 1 3853 ? 166.191 105.873 164.928 1.00 40.13  ? 3853 THR A CB    1 
ATOM   17530 O  OG1   . THR A 1 3853 ? 166.008 104.938 165.998 1.00 43.70  ? 3853 THR A OG1   1 
ATOM   17531 C  CG2   . THR A 1 3853 ? 167.544 106.549 165.082 1.00 40.18  ? 3853 THR A CG2   1 
ATOM   17532 N  N     . GLN A 1 3854 ? 164.538 107.242 162.596 1.00 44.88  ? 3854 GLN A N     1 
ATOM   17533 C  CA    . GLN A 1 3854 ? 164.529 107.991 161.342 1.00 46.11  ? 3854 GLN A CA    1 
ATOM   17534 C  C     . GLN A 1 3854 ? 163.690 109.257 161.459 1.00 44.30  ? 3854 GLN A C     1 
ATOM   17535 O  O     . GLN A 1 3854 ? 164.079 110.317 160.955 1.00 42.79  ? 3854 GLN A O     1 
ATOM   17536 C  CB    . GLN A 1 3854 ? 164.010 107.107 160.209 1.00 48.44  ? 3854 GLN A CB    1 
ATOM   17537 C  CG    . GLN A 1 3854 ? 164.569 107.456 158.841 1.00 52.84  ? 3854 GLN A CG    1 
ATOM   17538 C  CD    . GLN A 1 3854 ? 163.917 106.662 157.727 1.00 60.55  ? 3854 GLN A CD    1 
ATOM   17539 O  OE1   . GLN A 1 3854 ? 163.676 105.462 157.864 1.00 59.27  ? 3854 GLN A OE1   1 
ATOM   17540 N  NE2   . GLN A 1 3854 ? 163.624 107.329 156.617 1.00 59.72  ? 3854 GLN A NE2   1 
ATOM   17541 N  N     . ARG A 1 3855 ? 162.530 109.164 162.113 1.00 44.03  ? 3855 ARG A N     1 
ATOM   17542 C  CA    . ARG A 1 3855 ? 161.699 110.346 162.314 1.00 41.15  ? 3855 ARG A CA    1 
ATOM   17543 C  C     . ARG A 1 3855 ? 162.406 111.372 163.190 1.00 38.56  ? 3855 ARG A C     1 
ATOM   17544 O  O     . ARG A 1 3855 ? 162.307 112.580 162.948 1.00 38.96  ? 3855 ARG A O     1 
ATOM   17545 C  CB    . ARG A 1 3855 ? 160.357 109.945 162.927 1.00 38.29  ? 3855 ARG A CB    1 
ATOM   17546 C  CG    . ARG A 1 3855 ? 159.417 109.254 161.952 1.00 42.06  ? 3855 ARG A CG    1 
ATOM   17547 C  CD    . ARG A 1 3855 ? 158.044 109.022 162.561 1.00 42.41  ? 3855 ARG A CD    1 
ATOM   17548 N  NE    . ARG A 1 3855 ? 157.393 110.268 162.950 1.00 35.60  ? 3855 ARG A NE    1 
ATOM   17549 C  CZ    . ARG A 1 3855 ? 156.326 110.773 162.346 1.00 41.76  ? 3855 ARG A CZ    1 
ATOM   17550 N  NH1   . ARG A 1 3855 ? 155.768 110.171 161.309 1.00 45.70  ? 3855 ARG A NH1   1 
ATOM   17551 N  NH2   . ARG A 1 3855 ? 155.806 111.912 162.795 1.00 46.96  ? 3855 ARG A NH2   1 
ATOM   17552 N  N     . LEU A 1 3856 ? 163.121 110.908 164.218 1.00 36.59  ? 3856 LEU A N     1 
ATOM   17553 C  CA    . LEU A 1 3856 ? 163.860 111.824 165.082 1.00 37.05  ? 3856 LEU A CA    1 
ATOM   17554 C  C     . LEU A 1 3856 ? 164.957 112.550 164.313 1.00 33.59  ? 3856 LEU A C     1 
ATOM   17555 O  O     . LEU A 1 3856 ? 165.160 113.756 164.498 1.00 34.07  ? 3856 LEU A O     1 
ATOM   17556 C  CB    . LEU A 1 3856 ? 164.452 111.064 166.267 1.00 38.25  ? 3856 LEU A CB    1 
ATOM   17557 C  CG    . LEU A 1 3856 ? 165.198 111.920 167.290 1.00 33.96  ? 3856 LEU A CG    1 
ATOM   17558 C  CD1   . LEU A 1 3856 ? 164.301 113.029 167.809 1.00 34.52  ? 3856 LEU A CD1   1 
ATOM   17559 C  CD2   . LEU A 1 3856 ? 165.716 111.067 168.431 1.00 30.14  ? 3856 LEU A CD2   1 
ATOM   17560 N  N     . SER A 1 3857 ? 165.680 111.831 163.451 1.00 34.56  ? 3857 SER A N     1 
ATOM   17561 C  CA    . SER A 1 3857 ? 166.738 112.460 162.666 1.00 33.70  ? 3857 SER A CA    1 
ATOM   17562 C  C     . SER A 1 3857 ? 166.171 113.506 161.715 1.00 30.57  ? 3857 SER A C     1 
ATOM   17563 O  O     . SER A 1 3857 ? 166.763 114.576 161.532 1.00 28.67  ? 3857 SER A O     1 
ATOM   17564 C  CB    . SER A 1 3857 ? 167.520 111.398 161.894 1.00 33.09  ? 3857 SER A CB    1 
ATOM   17565 O  OG    . SER A 1 3857 ? 166.711 110.789 160.904 1.00 32.31  ? 3857 SER A OG    1 
ATOM   17566 N  N     . ILE A 1 3858 ? 165.028 113.208 161.093 1.00 32.82  ? 3858 ILE A N     1 
ATOM   17567 C  CA    . ILE A 1 3858 ? 164.376 114.179 160.219 1.00 33.12  ? 3858 ILE A CA    1 
ATOM   17568 C  C     . ILE A 1 3858 ? 163.948 115.406 161.014 1.00 32.64  ? 3858 ILE A C     1 
ATOM   17569 O  O     . ILE A 1 3858 ? 164.119 116.546 160.566 1.00 35.09  ? 3858 ILE A O     1 
ATOM   17570 C  CB    . ILE A 1 3858 ? 163.185 113.524 159.496 1.00 33.63  ? 3858 ILE A CB    1 
ATOM   17571 C  CG1   . ILE A 1 3858 ? 163.680 112.582 158.398 1.00 32.04  ? 3858 ILE A CG1   1 
ATOM   17572 C  CG2   . ILE A 1 3858 ? 162.261 114.581 158.916 1.00 35.26  ? 3858 ILE A CG2   1 
ATOM   17573 C  CD1   . ILE A 1 3858 ? 162.578 111.794 157.729 1.00 41.86  ? 3858 ILE A CD1   1 
ATOM   17574 N  N     . ILE A 1 3859 ? 163.387 115.191 162.207 1.00 29.06  ? 3859 ILE A N     1 
ATOM   17575 C  CA    . ILE A 1 3859 ? 162.928 116.305 163.032 1.00 26.83  ? 3859 ILE A CA    1 
ATOM   17576 C  C     . ILE A 1 3859 ? 164.098 117.197 163.429 1.00 26.21  ? 3859 ILE A C     1 
ATOM   17577 O  O     . ILE A 1 3859 ? 164.016 118.428 163.344 1.00 27.13  ? 3859 ILE A O     1 
ATOM   17578 C  CB    . ILE A 1 3859 ? 162.176 115.775 164.267 1.00 29.53  ? 3859 ILE A CB    1 
ATOM   17579 C  CG1   . ILE A 1 3859 ? 160.761 115.340 163.885 1.00 30.79  ? 3859 ILE A CG1   1 
ATOM   17580 C  CG2   . ILE A 1 3859 ? 162.121 116.830 165.355 1.00 28.36  ? 3859 ILE A CG2   1 
ATOM   17581 C  CD1   . ILE A 1 3859 ? 160.056 114.553 164.963 1.00 28.13  ? 3859 ILE A CD1   1 
ATOM   17582 N  N     . THR A 1 3860 ? 165.204 116.592 163.868 1.00 24.74  ? 3860 THR A N     1 
ATOM   17583 C  CA    . THR A 1 3860 ? 166.370 117.374 164.271 1.00 22.92  ? 3860 THR A CA    1 
ATOM   17584 C  C     . THR A 1 3860 ? 166.943 118.151 163.092 1.00 28.20  ? 3860 THR A C     1 
ATOM   17585 O  O     . THR A 1 3860 ? 167.304 119.326 163.223 1.00 28.48  ? 3860 THR A O     1 
ATOM   17586 C  CB    . THR A 1 3860 ? 167.432 116.458 164.879 1.00 21.98  ? 3860 THR A CB    1 
ATOM   17587 O  OG1   . THR A 1 3860 ? 166.869 115.731 165.978 1.00 27.44  ? 3860 THR A OG1   1 
ATOM   17588 C  CG2   . THR A 1 3860 ? 168.618 117.272 165.375 1.00 19.45  ? 3860 THR A CG2   1 
ATOM   17589 N  N     . LYS A 1 3861 ? 167.035 117.505 161.928 1.00 25.30  ? 3861 LYS A N     1 
ATOM   17590 C  CA    . LYS A 1 3861 ? 167.521 118.188 160.733 1.00 24.50  ? 3861 LYS A CA    1 
ATOM   17591 C  C     . LYS A 1 3861 ? 166.596 119.334 160.343 1.00 25.56  ? 3861 LYS A C     1 
ATOM   17592 O  O     . LYS A 1 3861 ? 167.054 120.428 159.992 1.00 26.84  ? 3861 LYS A O     1 
ATOM   17593 C  CB    . LYS A 1 3861 ? 167.653 117.192 159.581 1.00 26.82  ? 3861 LYS A CB    1 
ATOM   17594 C  CG    . LYS A 1 3861 ? 168.210 117.792 158.301 1.00 27.62  ? 3861 LYS A CG    1 
ATOM   17595 C  CD    . LYS A 1 3861 ? 168.366 116.736 157.222 1.00 32.50  ? 3861 LYS A CD    1 
ATOM   17596 C  CE    . LYS A 1 3861 ? 169.135 117.275 156.029 1.00 32.27  ? 3861 LYS A CE    1 
ATOM   17597 N  NZ    . LYS A 1 3861 ? 169.346 116.229 154.991 1.00 29.89  ? 3861 LYS A NZ    1 
ATOM   17598 N  N     . ASP A 1 3862 ? 165.285 119.098 160.401 1.00 27.92  ? 3862 ASP A N     1 
ATOM   17599 C  CA    . ASP A 1 3862 ? 164.330 120.115 159.977 1.00 26.13  ? 3862 ASP A CA    1 
ATOM   17600 C  C     . ASP A 1 3862 ? 164.180 121.222 161.013 1.00 21.76  ? 3862 ASP A C     1 
ATOM   17601 O  O     . ASP A 1 3862 ? 163.802 122.345 160.663 1.00 22.01  ? 3862 ASP A O     1 
ATOM   17602 C  CB    . ASP A 1 3862 ? 162.980 119.466 159.680 1.00 28.53  ? 3862 ASP A CB    1 
ATOM   17603 C  CG    . ASP A 1 3862 ? 162.899 118.925 158.267 1.00 46.95  ? 3862 ASP A CG    1 
ATOM   17604 O  OD1   . ASP A 1 3862 ? 163.898 119.047 157.527 1.00 45.40  ? 3862 ASP A OD1   1 
ATOM   17605 O  OD2   . ASP A 1 3862 ? 161.846 118.368 157.898 1.00 55.95  ? 3862 ASP A OD2   1 
ATOM   17606 N  N     . LEU A 1 3863 ? 164.459 120.928 162.285 1.00 22.58  ? 3863 LEU A N     1 
ATOM   17607 C  CA    . LEU A 1 3863 ? 164.368 121.956 163.317 1.00 18.79  ? 3863 LEU A CA    1 
ATOM   17608 C  C     . LEU A 1 3863 ? 165.351 123.088 163.050 1.00 14.48  ? 3863 LEU A C     1 
ATOM   17609 O  O     . LEU A 1 3863 ? 165.001 124.269 163.152 1.00 17.89  ? 3863 LEU A O     1 
ATOM   17610 C  CB    . LEU A 1 3863 ? 164.617 121.341 164.694 1.00 21.09  ? 3863 LEU A CB    1 
ATOM   17611 C  CG    . LEU A 1 3863 ? 164.765 122.329 165.853 1.00 20.20  ? 3863 LEU A CG    1 
ATOM   17612 C  CD1   . LEU A 1 3863 ? 163.421 122.935 166.222 1.00 21.17  ? 3863 LEU A CD1   1 
ATOM   17613 C  CD2   . LEU A 1 3863 ? 165.402 121.658 167.056 1.00 21.83  ? 3863 LEU A CD2   1 
ATOM   17614 N  N     . PHE A 1 3864 ? 166.591 122.742 162.700 1.00 15.65  ? 3864 PHE A N     1 
ATOM   17615 C  CA    . PHE A 1 3864 ? 167.591 123.761 162.396 1.00 13.89  ? 3864 PHE A CA    1 
ATOM   17616 C  C     . PHE A 1 3864 ? 167.222 124.532 161.135 1.00 13.55  ? 3864 PHE A C     1 
ATOM   17617 O  O     . PHE A 1 3864 ? 167.410 125.751 161.060 1.00 12.75  ? 3864 PHE A O     1 
ATOM   17618 C  CB    . PHE A 1 3864 ? 168.966 123.111 162.249 1.00 13.56  ? 3864 PHE A CB    1 
ATOM   17619 C  CG    . PHE A 1 3864 ? 169.626 122.784 163.557 1.00 14.06  ? 3864 PHE A CG    1 
ATOM   17620 C  CD1   . PHE A 1 3864 ? 170.229 123.776 164.310 1.00 16.90  ? 3864 PHE A CD1   1 
ATOM   17621 C  CD2   . PHE A 1 3864 ? 169.640 121.485 164.034 1.00 14.77  ? 3864 PHE A CD2   1 
ATOM   17622 C  CE1   . PHE A 1 3864 ? 170.837 123.477 165.514 1.00 20.12  ? 3864 PHE A CE1   1 
ATOM   17623 C  CE2   . PHE A 1 3864 ? 170.246 121.180 165.237 1.00 15.53  ? 3864 PHE A CE2   1 
ATOM   17624 C  CZ    . PHE A 1 3864 ? 170.845 122.177 165.977 1.00 16.17  ? 3864 PHE A CZ    1 
ATOM   17625 N  N     . GLN A 1 3865 ? 166.694 123.832 160.129 1.00 13.17  ? 3865 GLN A N     1 
ATOM   17626 C  CA    . GLN A 1 3865 ? 166.373 124.479 158.860 1.00 10.84  ? 3865 GLN A CA    1 
ATOM   17627 C  C     . GLN A 1 3865 ? 165.200 125.440 159.009 1.00 12.05  ? 3865 GLN A C     1 
ATOM   17628 O  O     . GLN A 1 3865 ? 165.251 126.579 158.529 1.00 13.26  ? 3865 GLN A O     1 
ATOM   17629 C  CB    . GLN A 1 3865 ? 166.072 123.422 157.798 1.00 15.87  ? 3865 GLN A CB    1 
ATOM   17630 C  CG    . GLN A 1 3865 ? 165.853 123.991 156.407 1.00 13.22  ? 3865 GLN A CG    1 
ATOM   17631 C  CD    . GLN A 1 3865 ? 167.108 124.614 155.829 1.00 14.10  ? 3865 GLN A CD    1 
ATOM   17632 O  OE1   . GLN A 1 3865 ? 168.037 123.911 155.432 1.00 16.41  ? 3865 GLN A OE1   1 
ATOM   17633 N  NE2   . GLN A 1 3865 ? 167.142 125.940 155.779 1.00 14.18  ? 3865 GLN A NE2   1 
ATOM   17634 N  N     . VAL A 1 3866 ? 164.130 124.998 159.671 1.00 10.96  ? 3866 VAL A N     1 
ATOM   17635 C  CA    . VAL A 1 3866 ? 162.944 125.838 159.804 1.00 8.95   ? 3866 VAL A CA    1 
ATOM   17636 C  C     . VAL A 1 3866 ? 163.233 127.031 160.706 1.00 9.80   ? 3866 VAL A C     1 
ATOM   17637 O  O     . VAL A 1 3866 ? 162.760 128.146 160.455 1.00 12.12  ? 3866 VAL A O     1 
ATOM   17638 C  CB    . VAL A 1 3866 ? 161.755 125.004 160.317 1.00 10.23  ? 3866 VAL A CB    1 
ATOM   17639 C  CG1   . VAL A 1 3866 ? 160.579 125.902 160.668 1.00 15.78  ? 3866 VAL A CG1   1 
ATOM   17640 C  CG2   . VAL A 1 3866 ? 161.348 123.974 159.280 1.00 11.61  ? 3866 VAL A CG2   1 
ATOM   17641 N  N     . ALA A 1 3867 ? 164.019 126.822 161.764 1.00 10.55  ? 3867 ALA A N     1 
ATOM   17642 C  CA    . ALA A 1 3867 ? 164.388 127.928 162.642 1.00 9.93   ? 3867 ALA A CA    1 
ATOM   17643 C  C     . ALA A 1 3867 ? 165.199 128.976 161.891 1.00 11.22  ? 3867 ALA A C     1 
ATOM   17644 O  O     . ALA A 1 3867 ? 164.998 130.181 162.073 1.00 12.66  ? 3867 ALA A O     1 
ATOM   17645 C  CB    . ALA A 1 3867 ? 165.167 127.405 163.848 1.00 11.91  ? 3867 ALA A CB    1 
ATOM   17646 N  N     . PHE A 1 3868 ? 166.128 128.531 161.042 1.00 11.14  ? 3868 PHE A N     1 
ATOM   17647 C  CA    . PHE A 1 3868 ? 166.921 129.469 160.255 1.00 8.17   ? 3868 PHE A CA    1 
ATOM   17648 C  C     . PHE A 1 3868 ? 166.050 130.239 159.270 1.00 10.31  ? 3868 PHE A C     1 
ATOM   17649 O  O     . PHE A 1 3868 ? 166.161 131.464 159.153 1.00 10.44  ? 3868 PHE A O     1 
ATOM   17650 C  CB    . PHE A 1 3868 ? 168.032 128.726 159.514 1.00 8.46   ? 3868 PHE A CB    1 
ATOM   17651 C  CG    . PHE A 1 3868 ? 168.790 129.588 158.543 1.00 10.27  ? 3868 PHE A CG    1 
ATOM   17652 C  CD1   . PHE A 1 3868 ? 169.734 130.494 158.993 1.00 11.43  ? 3868 PHE A CD1   1 
ATOM   17653 C  CD2   . PHE A 1 3868 ? 168.550 129.498 157.183 1.00 9.54   ? 3868 PHE A CD2   1 
ATOM   17654 C  CE1   . PHE A 1 3868 ? 170.428 131.289 158.104 1.00 12.05  ? 3868 PHE A CE1   1 
ATOM   17655 C  CE2   . PHE A 1 3868 ? 169.240 130.291 156.289 1.00 10.90  ? 3868 PHE A CE2   1 
ATOM   17656 C  CZ    . PHE A 1 3868 ? 170.180 131.189 156.751 1.00 11.55  ? 3868 PHE A CZ    1 
ATOM   17657 N  N     . ASN A 1 3869 ? 165.171 129.533 158.555 1.00 11.49  ? 3869 ASN A N     1 
ATOM   17658 C  CA    . ASN A 1 3869 ? 164.375 130.171 157.511 1.00 9.59   ? 3869 ASN A CA    1 
ATOM   17659 C  C     . ASN A 1 3869 ? 163.475 131.255 158.088 1.00 13.11  ? 3869 ASN A C     1 
ATOM   17660 O  O     . ASN A 1 3869 ? 163.366 132.352 157.528 1.00 16.97  ? 3869 ASN A O     1 
ATOM   17661 C  CB    . ASN A 1 3869 ? 163.543 129.121 156.775 1.00 9.77   ? 3869 ASN A CB    1 
ATOM   17662 C  CG    . ASN A 1 3869 ? 164.395 128.170 155.964 1.00 16.17  ? 3869 ASN A CG    1 
ATOM   17663 O  OD1   . ASN A 1 3869 ? 165.619 128.291 155.931 1.00 24.46  ? 3869 ASN A OD1   1 
ATOM   17664 N  ND2   . ASN A 1 3869 ? 163.752 127.215 155.303 1.00 15.36  ? 3869 ASN A ND2   1 
ATOM   17665 N  N     . ARG A 1 3870 ? 162.821 130.965 159.212 1.00 11.87  ? 3870 ARG A N     1 
ATOM   17666 C  CA    . ARG A 1 3870 ? 161.883 131.923 159.786 1.00 8.67   ? 3870 ARG A CA    1 
ATOM   17667 C  C     . ARG A 1 3870 ? 162.610 133.119 160.390 1.00 9.97   ? 3870 ARG A C     1 
ATOM   17668 O  O     . ARG A 1 3870 ? 162.153 134.260 160.261 1.00 15.83  ? 3870 ARG A O     1 
ATOM   17669 C  CB    . ARG A 1 3870 ? 161.012 131.226 160.829 1.00 10.04  ? 3870 ARG A CB    1 
ATOM   17670 C  CG    . ARG A 1 3870 ? 160.126 130.141 160.241 1.00 15.86  ? 3870 ARG A CG    1 
ATOM   17671 C  CD    . ARG A 1 3870 ? 158.814 130.007 160.986 1.00 21.51  ? 3870 ARG A CD    1 
ATOM   17672 N  NE    . ARG A 1 3870 ? 158.072 128.833 160.545 1.00 22.26  ? 3870 ARG A NE    1 
ATOM   17673 C  CZ    . ARG A 1 3870 ? 156.868 128.497 160.986 1.00 28.58  ? 3870 ARG A CZ    1 
ATOM   17674 N  NH1   . ARG A 1 3870 ? 156.235 129.225 161.890 1.00 27.75  ? 3870 ARG A NH1   1 
ATOM   17675 N  NH2   . ARG A 1 3870 ? 156.285 127.402 160.506 1.00 32.32  ? 3870 ARG A NH2   1 
ATOM   17676 N  N     . VAL A 1 3871 ? 163.740 132.878 161.057 1.00 9.10   ? 3871 VAL A N     1 
ATOM   17677 C  CA    . VAL A 1 3871 ? 164.491 133.971 161.667 1.00 8.97   ? 3871 VAL A CA    1 
ATOM   17678 C  C     . VAL A 1 3871 ? 165.179 134.819 160.603 1.00 12.65  ? 3871 VAL A C     1 
ATOM   17679 O  O     . VAL A 1 3871 ? 165.124 136.054 160.647 1.00 16.25  ? 3871 VAL A O     1 
ATOM   17680 C  CB    . VAL A 1 3871 ? 165.498 133.417 162.689 1.00 9.54   ? 3871 VAL A CB    1 
ATOM   17681 C  CG1   . VAL A 1 3871 ? 166.445 134.509 163.150 1.00 10.41  ? 3871 VAL A CG1   1 
ATOM   17682 C  CG2   . VAL A 1 3871 ? 164.762 132.826 163.868 1.00 10.27  ? 3871 VAL A CG2   1 
ATOM   17683 N  N     . ALA A 1 3872 ? 165.832 134.177 159.631 1.00 12.76  ? 3872 ALA A N     1 
ATOM   17684 C  CA    . ALA A 1 3872 ? 166.587 134.921 158.629 1.00 8.45   ? 3872 ALA A CA    1 
ATOM   17685 C  C     . ALA A 1 3872 ? 165.689 135.739 157.714 1.00 12.38  ? 3872 ALA A C     1 
ATOM   17686 O  O     . ALA A 1 3872 ? 166.166 136.698 157.098 1.00 13.23  ? 3872 ALA A O     1 
ATOM   17687 C  CB    . ALA A 1 3872 ? 167.450 133.971 157.798 1.00 9.76   ? 3872 ALA A CB    1 
ATOM   17688 N  N     . ARG A 1 3873 ? 164.406 135.385 157.609 1.00 13.68  ? 3873 ARG A N     1 
ATOM   17689 C  CA    . ARG A 1 3873 ? 163.476 136.194 156.832 1.00 11.42  ? 3873 ARG A CA    1 
ATOM   17690 C  C     . ARG A 1 3873 ? 163.250 137.557 157.468 1.00 10.16  ? 3873 ARG A C     1 
ATOM   17691 O  O     . ARG A 1 3873 ? 162.908 138.512 156.762 1.00 11.77  ? 3873 ARG A O     1 
ATOM   17692 C  CB    . ARG A 1 3873 ? 162.142 135.464 156.680 1.00 14.73  ? 3873 ARG A CB    1 
ATOM   17693 C  CG    . ARG A 1 3873 ? 162.087 134.503 155.505 1.00 20.67  ? 3873 ARG A CG    1 
ATOM   17694 C  CD    . ARG A 1 3873 ? 162.569 135.146 154.219 1.00 21.15  ? 3873 ARG A CD    1 
ATOM   17695 N  NE    . ARG A 1 3873 ? 162.528 134.205 153.106 1.00 26.83  ? 3873 ARG A NE    1 
ATOM   17696 C  CZ    . ARG A 1 3873 ? 163.061 134.428 151.913 1.00 30.46  ? 3873 ARG A CZ    1 
ATOM   17697 N  NH1   . ARG A 1 3873 ? 163.687 135.560 151.636 1.00 31.47  ? 3873 ARG A NH1   1 
ATOM   17698 N  NH2   . ARG A 1 3873 ? 162.964 133.491 150.974 1.00 28.52  ? 3873 ARG A NH2   1 
ATOM   17699 N  N     . GLY A 1 3874 ? 163.430 137.667 158.781 1.00 8.91   ? 3874 GLY A N     1 
ATOM   17700 C  CA    . GLY A 1 3874 ? 163.302 138.933 159.471 1.00 9.04   ? 3874 GLY A CA    1 
ATOM   17701 C  C     . GLY A 1 3874 ? 164.632 139.444 159.978 1.00 12.49  ? 3874 GLY A C     1 
ATOM   17702 O  O     . GLY A 1 3874 ? 164.708 140.065 161.042 1.00 17.88  ? 3874 GLY A O     1 
ATOM   17703 N  N     . MET A 1 3875 ? 165.691 139.186 159.217 1.00 12.66  ? 3875 MET A N     1 
ATOM   17704 C  CA    . MET A 1 3875 ? 167.034 139.623 159.557 1.00 10.17  ? 3875 MET A CA    1 
ATOM   17705 C  C     . MET A 1 3875 ? 167.692 140.232 158.330 1.00 14.58  ? 3875 MET A C     1 
ATOM   17706 O  O     . MET A 1 3875 ? 167.355 139.891 157.193 1.00 17.13  ? 3875 MET A O     1 
ATOM   17707 C  CB    . MET A 1 3875 ? 167.886 138.459 160.077 1.00 15.40  ? 3875 MET A CB    1 
ATOM   17708 C  CG    . MET A 1 3875 ? 167.569 138.035 161.500 1.00 16.21  ? 3875 MET A CG    1 
ATOM   17709 S  SD    . MET A 1 3875 ? 168.925 137.135 162.276 1.00 24.53  ? 3875 MET A SD    1 
ATOM   17710 C  CE    . MET A 1 3875 ? 169.720 136.416 160.844 1.00 12.60  ? 3875 MET A CE    1 
ATOM   17711 N  N     . LEU A 1 3876 ? 168.630 141.144 158.570 1.00 17.52  ? 3876 LEU A N     1 
ATOM   17712 C  CA    . LEU A 1 3876 ? 169.437 141.680 157.486 1.00 12.72  ? 3876 LEU A CA    1 
ATOM   17713 C  C     . LEU A 1 3876 ? 170.342 140.592 156.920 1.00 15.10  ? 3876 LEU A C     1 
ATOM   17714 O  O     . LEU A 1 3876 ? 170.837 139.726 157.647 1.00 17.83  ? 3876 LEU A O     1 
ATOM   17715 C  CB    . LEU A 1 3876 ? 170.276 142.861 157.971 1.00 14.82  ? 3876 LEU A CB    1 
ATOM   17716 C  CG    . LEU A 1 3876 ? 169.502 144.090 158.447 1.00 13.22  ? 3876 LEU A CG    1 
ATOM   17717 C  CD1   . LEU A 1 3876 ? 170.441 145.099 159.084 1.00 12.77  ? 3876 LEU A CD1   1 
ATOM   17718 C  CD2   . LEU A 1 3876 ? 168.740 144.720 157.294 1.00 10.77  ? 3876 LEU A CD2   1 
ATOM   17719 N  N     . HIS A 1 3877 ? 170.555 140.645 155.602 1.00 14.99  ? 3877 HIS A N     1 
ATOM   17720 C  CA    . HIS A 1 3877 ? 171.303 139.586 154.930 1.00 11.81  ? 3877 HIS A CA    1 
ATOM   17721 C  C     . HIS A 1 3877 ? 172.720 139.455 155.471 1.00 13.04  ? 3877 HIS A C     1 
ATOM   17722 O  O     . HIS A 1 3877 ? 173.261 138.345 155.523 1.00 13.65  ? 3877 HIS A O     1 
ATOM   17723 C  CB    . HIS A 1 3877 ? 171.335 139.831 153.423 1.00 11.85  ? 3877 HIS A CB    1 
ATOM   17724 C  CG    . HIS A 1 3877 ? 171.707 138.619 152.628 1.00 13.97  ? 3877 HIS A CG    1 
ATOM   17725 N  ND1   . HIS A 1 3877 ? 170.783 137.677 152.231 1.00 13.91  ? 3877 HIS A ND1   1 
ATOM   17726 C  CD2   . HIS A 1 3877 ? 172.904 138.191 152.165 1.00 11.35  ? 3877 HIS A CD2   1 
ATOM   17727 C  CE1   . HIS A 1 3877 ? 171.395 136.723 151.553 1.00 13.19  ? 3877 HIS A CE1   1 
ATOM   17728 N  NE2   . HIS A 1 3877 ? 172.683 137.010 151.500 1.00 14.82  ? 3877 HIS A NE2   1 
ATOM   17729 N  N     . GLN A 1 3878 ? 173.335 140.565 155.877 1.00 12.57  ? 3878 GLN A N     1 
ATOM   17730 C  CA    . GLN A 1 3878 ? 174.675 140.519 156.445 1.00 13.10  ? 3878 GLN A CA    1 
ATOM   17731 C  C     . GLN A 1 3878 ? 174.730 139.780 157.776 1.00 16.64  ? 3878 GLN A C     1 
ATOM   17732 O  O     . GLN A 1 3878 ? 175.827 139.434 158.226 1.00 19.33  ? 3878 GLN A O     1 
ATOM   17733 C  CB    . GLN A 1 3878 ? 175.223 141.937 156.622 1.00 15.57  ? 3878 GLN A CB    1 
ATOM   17734 C  CG    . GLN A 1 3878 ? 174.793 142.615 157.910 1.00 18.45  ? 3878 GLN A CG    1 
ATOM   17735 C  CD    . GLN A 1 3878 ? 174.423 144.069 157.706 1.00 23.91  ? 3878 GLN A CD    1 
ATOM   17736 O  OE1   . GLN A 1 3878 ? 173.412 144.380 157.077 1.00 24.87  ? 3878 GLN A OE1   1 
ATOM   17737 N  NE2   . GLN A 1 3878 ? 175.241 144.968 158.239 1.00 22.33  ? 3878 GLN A NE2   1 
ATOM   17738 N  N     . ASP A 1 3879 ? 173.585 139.533 158.412 1.00 19.62  ? 3879 ASP A N     1 
ATOM   17739 C  CA    . ASP A 1 3879 ? 173.532 138.796 159.666 1.00 15.35  ? 3879 ASP A CA    1 
ATOM   17740 C  C     . ASP A 1 3879 ? 173.056 137.359 159.499 1.00 12.48  ? 3879 ASP A C     1 
ATOM   17741 O  O     . ASP A 1 3879 ? 173.008 136.624 160.490 1.00 18.53  ? 3879 ASP A O     1 
ATOM   17742 C  CB    . ASP A 1 3879 ? 172.624 139.521 160.665 1.00 15.97  ? 3879 ASP A CB    1 
ATOM   17743 C  CG    . ASP A 1 3879 ? 173.016 140.973 160.860 1.00 22.52  ? 3879 ASP A CG    1 
ATOM   17744 O  OD1   . ASP A 1 3879 ? 174.212 141.238 161.091 1.00 26.08  ? 3879 ASP A OD1   1 
ATOM   17745 O  OD2   . ASP A 1 3879 ? 172.129 141.848 160.784 1.00 23.64  ? 3879 ASP A OD2   1 
ATOM   17746 N  N     . HIS A 1 3880 ? 172.703 136.944 158.279 1.00 12.52  ? 3880 HIS A N     1 
ATOM   17747 C  CA    . HIS A 1 3880 ? 172.300 135.558 158.055 1.00 13.70  ? 3880 HIS A CA    1 
ATOM   17748 C  C     . HIS A 1 3880 ? 173.446 134.598 158.342 1.00 12.57  ? 3880 HIS A C     1 
ATOM   17749 O  O     . HIS A 1 3880 ? 173.235 133.520 158.910 1.00 15.69  ? 3880 HIS A O     1 
ATOM   17750 C  CB    . HIS A 1 3880 ? 171.803 135.370 156.622 1.00 15.57  ? 3880 HIS A CB    1 
ATOM   17751 C  CG    . HIS A 1 3880 ? 170.509 136.064 156.331 1.00 9.32   ? 3880 HIS A CG    1 
ATOM   17752 N  ND1   . HIS A 1 3880 ? 169.786 135.834 155.181 1.00 9.70   ? 3880 HIS A ND1   1 
ATOM   17753 C  CD2   . HIS A 1 3880 ? 169.804 136.973 157.043 1.00 10.91  ? 3880 HIS A CD2   1 
ATOM   17754 C  CE1   . HIS A 1 3880 ? 168.694 136.577 155.194 1.00 14.70  ? 3880 HIS A CE1   1 
ATOM   17755 N  NE2   . HIS A 1 3880 ? 168.681 137.278 156.313 1.00 17.13  ? 3880 HIS A NE2   1 
ATOM   17756 N  N     . ILE A 1 3881 ? 174.665 134.966 157.943 1.00 15.47  ? 3881 ILE A N     1 
ATOM   17757 C  CA    . ILE A 1 3881 ? 175.813 134.095 158.169 1.00 13.75  ? 3881 ILE A CA    1 
ATOM   17758 C  C     . ILE A 1 3881 ? 176.061 133.919 159.662 1.00 14.87  ? 3881 ILE A C     1 
ATOM   17759 O  O     . ILE A 1 3881 ? 176.471 132.843 160.112 1.00 17.30  ? 3881 ILE A O     1 
ATOM   17760 C  CB    . ILE A 1 3881 ? 177.054 134.642 157.437 1.00 13.60  ? 3881 ILE A CB    1 
ATOM   17761 C  CG1   . ILE A 1 3881 ? 178.243 133.691 157.599 1.00 17.72  ? 3881 ILE A CG1   1 
ATOM   17762 C  CG2   . ILE A 1 3881 ? 177.406 136.043 157.921 1.00 14.45  ? 3881 ILE A CG2   1 
ATOM   17763 C  CD1   . ILE A 1 3881 ? 177.936 132.258 157.224 1.00 17.15  ? 3881 ILE A CD1   1 
ATOM   17764 N  N     . THR A 1 3882 ? 175.809 134.964 160.453 1.00 13.86  ? 3882 THR A N     1 
ATOM   17765 C  CA    . THR A 1 3882 ? 176.021 134.871 161.894 1.00 13.11  ? 3882 THR A CA    1 
ATOM   17766 C  C     . THR A 1 3882 ? 175.084 133.847 162.522 1.00 13.78  ? 3882 THR A C     1 
ATOM   17767 O  O     . THR A 1 3882 ? 175.505 133.027 163.345 1.00 15.33  ? 3882 THR A O     1 
ATOM   17768 C  CB    . THR A 1 3882 ? 175.828 136.243 162.541 1.00 15.70  ? 3882 THR A CB    1 
ATOM   17769 O  OG1   . THR A 1 3882 ? 176.642 137.209 161.866 1.00 20.89  ? 3882 THR A OG1   1 
ATOM   17770 C  CG2   . THR A 1 3882 ? 176.221 136.197 164.010 1.00 20.44  ? 3882 THR A CG2   1 
ATOM   17771 N  N     . PHE A 1 3883 ? 173.806 133.875 162.139 1.00 10.89  ? 3883 PHE A N     1 
ATOM   17772 C  CA    . PHE A 1 3883 ? 172.839 132.960 162.736 1.00 8.98   ? 3883 PHE A CA    1 
ATOM   17773 C  C     . PHE A 1 3883 ? 173.105 131.515 162.329 1.00 10.03  ? 3883 PHE A C     1 
ATOM   17774 O  O     . PHE A 1 3883 ? 173.054 130.611 163.171 1.00 11.05  ? 3883 PHE A O     1 
ATOM   17775 C  CB    . PHE A 1 3883 ? 171.420 133.367 162.349 1.00 9.66   ? 3883 PHE A CB    1 
ATOM   17776 C  CG    . PHE A 1 3883 ? 170.354 132.609 163.085 1.00 10.82  ? 3883 PHE A CG    1 
ATOM   17777 C  CD1   . PHE A 1 3883 ? 170.400 132.487 164.464 1.00 9.15   ? 3883 PHE A CD1   1 
ATOM   17778 C  CD2   . PHE A 1 3883 ? 169.313 132.009 162.399 1.00 8.34   ? 3883 PHE A CD2   1 
ATOM   17779 C  CE1   . PHE A 1 3883 ? 169.422 131.790 165.144 1.00 7.81   ? 3883 PHE A CE1   1 
ATOM   17780 C  CE2   . PHE A 1 3883 ? 168.335 131.310 163.072 1.00 7.41   ? 3883 PHE A CE2   1 
ATOM   17781 C  CZ    . PHE A 1 3883 ? 168.389 131.201 164.447 1.00 7.00   ? 3883 PHE A CZ    1 
ATOM   17782 N  N     . ALA A 1 3884 ? 173.380 131.275 161.044 1.00 10.68  ? 3884 ALA A N     1 
ATOM   17783 C  CA    . ALA A 1 3884 ? 173.643 129.913 160.588 1.00 11.69  ? 3884 ALA A CA    1 
ATOM   17784 C  C     . ALA A 1 3884 ? 174.946 129.377 161.170 1.00 10.94  ? 3884 ALA A C     1 
ATOM   17785 O  O     . ALA A 1 3884 ? 175.055 128.181 161.464 1.00 13.21  ? 3884 ALA A O     1 
ATOM   17786 C  CB    . ALA A 1 3884 ? 173.675 129.864 159.061 1.00 13.06  ? 3884 ALA A CB    1 
ATOM   17787 N  N     . MET A 1 3885 ? 175.944 130.248 161.335 1.00 12.15  ? 3885 MET A N     1 
ATOM   17788 C  CA    . MET A 1 3885 ? 177.204 129.848 161.951 1.00 13.91  ? 3885 MET A CA    1 
ATOM   17789 C  C     . MET A 1 3885 ? 176.978 129.367 163.379 1.00 13.38  ? 3885 MET A C     1 
ATOM   17790 O  O     . MET A 1 3885 ? 177.542 128.351 163.801 1.00 15.96  ? 3885 MET A O     1 
ATOM   17791 C  CB    . MET A 1 3885 ? 178.173 131.028 161.940 1.00 19.21  ? 3885 MET A CB    1 
ATOM   17792 C  CG    . MET A 1 3885 ? 179.640 130.718 162.153 1.00 20.68  ? 3885 MET A CG    1 
ATOM   17793 S  SD    . MET A 1 3885 ? 180.574 130.499 160.633 1.00 30.68  ? 3885 MET A SD    1 
ATOM   17794 C  CE    . MET A 1 3885 ? 181.392 128.958 160.972 1.00 25.50  ? 3885 MET A CE    1 
ATOM   17795 N  N     . LEU A 1 3886 ? 176.144 130.087 164.132 1.00 14.84  ? 3886 LEU A N     1 
ATOM   17796 C  CA    . LEU A 1 3886 ? 175.842 129.702 165.506 1.00 12.13  ? 3886 LEU A CA    1 
ATOM   17797 C  C     . LEU A 1 3886 ? 174.981 128.447 165.554 1.00 9.74   ? 3886 LEU A C     1 
ATOM   17798 O  O     . LEU A 1 3886 ? 175.138 127.611 166.452 1.00 13.02  ? 3886 LEU A O     1 
ATOM   17799 C  CB    . LEU A 1 3886 ? 175.146 130.859 166.215 1.00 9.05   ? 3886 LEU A CB    1 
ATOM   17800 C  CG    . LEU A 1 3886 ? 175.981 132.129 166.355 1.00 13.15  ? 3886 LEU A CG    1 
ATOM   17801 C  CD1   . LEU A 1 3886 ? 175.083 133.295 166.677 1.00 11.92  ? 3886 LEU A CD1   1 
ATOM   17802 C  CD2   . LEU A 1 3886 ? 177.036 131.953 167.430 1.00 12.80  ? 3886 LEU A CD2   1 
ATOM   17803 N  N     . LEU A 1 3887 ? 174.051 128.306 164.608 1.00 6.88   ? 3887 LEU A N     1 
ATOM   17804 C  CA    . LEU A 1 3887 ? 173.270 127.078 164.527 1.00 9.23   ? 3887 LEU A CA    1 
ATOM   17805 C  C     . LEU A 1 3887 ? 174.163 125.888 164.202 1.00 11.72  ? 3887 LEU A C     1 
ATOM   17806 O  O     . LEU A 1 3887 ? 173.923 124.773 164.679 1.00 12.81  ? 3887 LEU A O     1 
ATOM   17807 C  CB    . LEU A 1 3887 ? 172.160 127.220 163.485 1.00 16.10  ? 3887 LEU A CB    1 
ATOM   17808 C  CG    . LEU A 1 3887 ? 170.978 128.123 163.843 1.00 10.00  ? 3887 LEU A CG    1 
ATOM   17809 C  CD1   . LEU A 1 3887 ? 169.844 127.932 162.850 1.00 8.43   ? 3887 LEU A CD1   1 
ATOM   17810 C  CD2   . LEU A 1 3887 ? 170.502 127.849 165.259 1.00 11.23  ? 3887 LEU A CD2   1 
ATOM   17811 N  N     . ALA A 1 3888 ? 175.196 126.107 163.386 1.00 15.65  ? 3888 ALA A N     1 
ATOM   17812 C  CA    . ALA A 1 3888 ? 176.148 125.041 163.097 1.00 15.49  ? 3888 ALA A CA    1 
ATOM   17813 C  C     . ALA A 1 3888 ? 176.925 124.643 164.345 1.00 15.24  ? 3888 ALA A C     1 
ATOM   17814 O  O     . ALA A 1 3888 ? 177.202 123.458 164.561 1.00 20.69  ? 3888 ALA A O     1 
ATOM   17815 C  CB    . ALA A 1 3888 ? 177.098 125.474 161.982 1.00 11.93  ? 3888 ALA A CB    1 
ATOM   17816 N  N     . ARG A 1 3889 ? 177.292 125.622 165.177 1.00 11.99  ? 3889 ARG A N     1 
ATOM   17817 C  CA    . ARG A 1 3889 ? 177.969 125.309 166.432 1.00 18.47  ? 3889 ARG A CA    1 
ATOM   17818 C  C     . ARG A 1 3889 ? 177.057 124.524 167.367 1.00 24.24  ? 3889 ARG A C     1 
ATOM   17819 O  O     . ARG A 1 3889 ? 177.515 123.624 168.082 1.00 28.97  ? 3889 ARG A O     1 
ATOM   17820 C  CB    . ARG A 1 3889 ? 178.454 126.592 167.106 1.00 17.19  ? 3889 ARG A CB    1 
ATOM   17821 C  CG    . ARG A 1 3889 ? 179.600 127.280 166.385 1.00 27.16  ? 3889 ARG A CG    1 
ATOM   17822 C  CD    . ARG A 1 3889 ? 180.375 128.194 167.321 1.00 29.00  ? 3889 ARG A CD    1 
ATOM   17823 N  NE    . ARG A 1 3889 ? 181.069 127.444 168.362 1.00 37.61  ? 3889 ARG A NE    1 
ATOM   17824 C  CZ    . ARG A 1 3889 ? 181.728 127.997 169.371 1.00 36.62  ? 3889 ARG A CZ    1 
ATOM   17825 N  NH1   . ARG A 1 3889 ? 181.805 129.310 169.511 1.00 38.39  ? 3889 ARG A NH1   1 
ATOM   17826 N  NH2   . ARG A 1 3889 ? 182.325 127.211 170.262 1.00 37.16  ? 3889 ARG A NH2   1 
ATOM   17827 N  N     . ILE A 1 3890 ? 175.765 124.859 167.384 1.00 15.92  ? 3890 ILE A N     1 
ATOM   17828 C  CA    . ILE A 1 3890 ? 174.815 124.135 168.225 1.00 14.12  ? 3890 ILE A CA    1 
ATOM   17829 C  C     . ILE A 1 3890 ? 174.712 122.682 167.783 1.00 16.47  ? 3890 ILE A C     1 
ATOM   17830 O  O     . ILE A 1 3890 ? 174.726 121.762 168.611 1.00 23.94  ? 3890 ILE A O     1 
ATOM   17831 C  CB    . ILE A 1 3890 ? 173.442 124.834 168.200 1.00 12.63  ? 3890 ILE A CB    1 
ATOM   17832 C  CG1   . ILE A 1 3890 ? 173.498 126.148 168.978 1.00 10.47  ? 3890 ILE A CG1   1 
ATOM   17833 C  CG2   . ILE A 1 3890 ? 172.369 123.929 168.781 1.00 12.97  ? 3890 ILE A CG2   1 
ATOM   17834 C  CD1   . ILE A 1 3890 ? 172.225 126.955 168.893 1.00 9.14   ? 3890 ILE A CD1   1 
ATOM   17835 N  N     . LYS A 1 3891 ? 174.607 122.449 166.473 1.00 18.62  ? 3891 LYS A N     1 
ATOM   17836 C  CA    . LYS A 1 3891 ? 174.528 121.081 165.970 1.00 20.76  ? 3891 LYS A CA    1 
ATOM   17837 C  C     . LYS A 1 3891 ? 175.848 120.346 166.159 1.00 24.45  ? 3891 LYS A C     1 
ATOM   17838 O  O     . LYS A 1 3891 ? 175.861 119.133 166.399 1.00 28.06  ? 3891 LYS A O     1 
ATOM   17839 C  CB    . LYS A 1 3891 ? 174.119 121.083 164.497 1.00 17.51  ? 3891 LYS A CB    1 
ATOM   17840 C  CG    . LYS A 1 3891 ? 173.772 119.709 163.954 1.00 17.07  ? 3891 LYS A CG    1 
ATOM   17841 C  CD    . LYS A 1 3891 ? 172.897 119.805 162.717 1.00 20.50  ? 3891 LYS A CD    1 
ATOM   17842 C  CE    . LYS A 1 3891 ? 173.664 119.406 161.469 1.00 22.82  ? 3891 LYS A CE    1 
ATOM   17843 N  NZ    . LYS A 1 3891 ? 173.903 117.938 161.409 1.00 25.73  ? 3891 LYS A NZ    1 
ATOM   17844 N  N     . LEU A 1 3892 ? 176.969 121.063 166.047 1.00 25.78  ? 3892 LEU A N     1 
ATOM   17845 C  CA    . LEU A 1 3892 ? 178.270 120.439 166.267 1.00 28.39  ? 3892 LEU A CA    1 
ATOM   17846 C  C     . LEU A 1 3892 ? 178.414 119.957 167.704 1.00 31.96  ? 3892 LEU A C     1 
ATOM   17847 O  O     . LEU A 1 3892 ? 178.964 118.878 167.953 1.00 36.46  ? 3892 LEU A O     1 
ATOM   17848 C  CB    . LEU A 1 3892 ? 179.387 121.420 165.912 1.00 24.61  ? 3892 LEU A CB    1 
ATOM   17849 C  CG    . LEU A 1 3892 ? 180.812 120.883 166.041 1.00 30.98  ? 3892 LEU A CG    1 
ATOM   17850 C  CD1   . LEU A 1 3892 ? 180.972 119.620 165.216 1.00 35.36  ? 3892 LEU A CD1   1 
ATOM   17851 C  CD2   . LEU A 1 3892 ? 181.823 121.936 165.616 1.00 32.11  ? 3892 LEU A CD2   1 
ATOM   17852 N  N     . LYS A 1 3893 ? 177.927 120.746 168.666 1.00 32.11  ? 3893 LYS A N     1 
ATOM   17853 C  CA    . LYS A 1 3893 ? 177.969 120.331 170.063 1.00 34.67  ? 3893 LYS A CA    1 
ATOM   17854 C  C     . LYS A 1 3893 ? 177.094 119.115 170.329 1.00 33.92  ? 3893 LYS A C     1 
ATOM   17855 O  O     . LYS A 1 3893 ? 177.333 118.393 171.303 1.00 40.28  ? 3893 LYS A O     1 
ATOM   17856 C  CB    . LYS A 1 3893 ? 177.542 121.490 170.966 1.00 31.03  ? 3893 LYS A CB    1 
ATOM   17857 C  CG    . LYS A 1 3893 ? 178.697 122.340 171.469 1.00 39.75  ? 3893 LYS A CG    1 
ATOM   17858 C  CD    . LYS A 1 3893 ? 178.198 123.550 172.241 1.00 48.07  ? 3893 LYS A CD    1 
ATOM   17859 C  CE    . LYS A 1 3893 ? 179.003 123.766 173.513 1.00 54.58  ? 3893 LYS A CE    1 
ATOM   17860 N  NZ    . LYS A 1 3893 ? 178.131 123.871 174.717 1.00 47.76  ? 3893 LYS A NZ    1 
ATOM   17861 N  N     . GLY A 1 3894 ? 176.093 118.871 169.490 1.00 30.22  ? 3894 GLY A N     1 
ATOM   17862 C  CA    . GLY A 1 3894 ? 175.209 117.735 169.625 1.00 34.43  ? 3894 GLY A CA    1 
ATOM   17863 C  C     . GLY A 1 3894 ? 175.669 116.474 168.929 1.00 41.16  ? 3894 GLY A C     1 
ATOM   17864 O  O     . GLY A 1 3894 ? 174.917 115.495 168.892 1.00 45.12  ? 3894 GLY A O     1 
ATOM   17865 N  N     . THR A 1 3895 ? 176.878 116.463 168.374 1.00 47.68  ? 3895 THR A N     1 
ATOM   17866 C  CA    . THR A 1 3895 ? 177.419 115.296 167.689 1.00 52.21  ? 3895 THR A CA    1 
ATOM   17867 C  C     . THR A 1 3895 ? 178.374 114.570 168.628 1.00 59.97  ? 3895 THR A C     1 
ATOM   17868 O  O     . THR A 1 3895 ? 179.354 115.157 169.101 1.00 56.18  ? 3895 THR A O     1 
ATOM   17869 C  CB    . THR A 1 3895 ? 178.136 115.700 166.401 1.00 51.18  ? 3895 THR A CB    1 
ATOM   17870 O  OG1   . THR A 1 3895 ? 177.241 116.450 165.571 1.00 46.70  ? 3895 THR A OG1   1 
ATOM   17871 C  CG2   . THR A 1 3895 ? 178.601 114.465 165.645 1.00 52.16  ? 3895 THR A CG2   1 
ATOM   17872 N  N     . VAL A 1 3896 ? 178.084 113.295 168.897 1.00 65.18  ? 3896 VAL A N     1 
ATOM   17873 C  CA    . VAL A 1 3896 ? 178.912 112.516 169.812 1.00 68.49  ? 3896 VAL A CA    1 
ATOM   17874 C  C     . VAL A 1 3896 ? 180.284 112.250 169.204 1.00 70.75  ? 3896 VAL A C     1 
ATOM   17875 O  O     . VAL A 1 3896 ? 181.301 112.253 169.908 1.00 70.16  ? 3896 VAL A O     1 
ATOM   17876 C  CB    . VAL A 1 3896 ? 178.196 111.208 170.192 1.00 72.31  ? 3896 VAL A CB    1 
ATOM   17877 C  CG1   . VAL A 1 3896 ? 178.931 110.510 171.326 1.00 70.88  ? 3896 VAL A CG1   1 
ATOM   17878 C  CG2   . VAL A 1 3896 ? 176.751 111.486 170.575 1.00 68.09  ? 3896 VAL A CG2   1 
ATOM   17879 N  N     . GLY A 1 3897 ? 180.338 112.022 167.895 1.00 66.70  ? 3897 GLY A N     1 
ATOM   17880 C  CA    . GLY A 1 3897 ? 181.571 111.669 167.223 1.00 64.24  ? 3897 GLY A CA    1 
ATOM   17881 C  C     . GLY A 1 3897 ? 182.504 112.812 166.902 1.00 66.06  ? 3897 GLY A C     1 
ATOM   17882 O  O     . GLY A 1 3897 ? 183.561 112.581 166.307 1.00 67.65  ? 3897 GLY A O     1 
ATOM   17883 N  N     . GLU A 1 3898 ? 182.152 114.045 167.273 1.00 62.91  ? 3898 GLU A N     1 
ATOM   17884 C  CA    . GLU A 1 3898 ? 183.001 115.180 166.956 1.00 59.79  ? 3898 GLU A CA    1 
ATOM   17885 C  C     . GLU A 1 3898 ? 183.681 115.720 168.208 1.00 54.87  ? 3898 GLU A C     1 
ATOM   17886 O  O     . GLU A 1 3898 ? 183.096 115.681 169.296 1.00 54.76  ? 3898 GLU A O     1 
ATOM   17887 C  CB    . GLU A 1 3898 ? 182.192 116.305 166.301 1.00 57.48  ? 3898 GLU A CB    1 
ATOM   17888 C  CG    . GLU A 1 3898 ? 181.845 116.056 164.845 1.00 55.07  ? 3898 GLU A CG    1 
ATOM   17889 C  CD    . GLU A 1 3898 ? 183.069 115.803 163.991 1.00 61.48  ? 3898 GLU A CD    1 
ATOM   17890 O  OE1   . GLU A 1 3898 ? 183.998 116.637 164.017 1.00 57.72  ? 3898 GLU A OE1   1 
ATOM   17891 O  OE2   . GLU A 1 3898 ? 183.102 114.768 163.293 1.00 63.85  ? 3898 GLU A OE2   1 
ATOM   17892 N  N     . PRO A 1 3899 ? 184.907 116.220 168.088 1.00 53.42  ? 3899 PRO A N     1 
ATOM   17893 C  CA    . PRO A 1 3899 ? 185.560 116.870 169.229 1.00 52.16  ? 3899 PRO A CA    1 
ATOM   17894 C  C     . PRO A 1 3899 ? 184.898 118.201 169.555 1.00 50.34  ? 3899 PRO A C     1 
ATOM   17895 O  O     . PRO A 1 3899 ? 184.072 118.727 168.807 1.00 49.39  ? 3899 PRO A O     1 
ATOM   17896 C  CB    . PRO A 1 3899 ? 187.005 117.064 168.758 1.00 47.79  ? 3899 PRO A CB    1 
ATOM   17897 C  CG    . PRO A 1 3899 ? 187.176 116.092 167.634 1.00 49.47  ? 3899 PRO A CG    1 
ATOM   17898 C  CD    . PRO A 1 3899 ? 185.838 116.012 166.968 1.00 51.45  ? 3899 PRO A CD    1 
ATOM   17899 N  N     . THR A 1 3900 ? 185.279 118.748 170.712 1.00 50.59  ? 3900 THR A N     1 
ATOM   17900 C  CA    . THR A 1 3900 ? 184.675 119.994 171.174 1.00 50.59  ? 3900 THR A CA    1 
ATOM   17901 C  C     . THR A 1 3900 ? 185.110 121.190 170.334 1.00 49.06  ? 3900 THR A C     1 
ATOM   17902 O  O     . THR A 1 3900 ? 184.312 122.111 170.120 1.00 50.67  ? 3900 THR A O     1 
ATOM   17903 C  CB    . THR A 1 3900 ? 185.009 120.229 172.649 1.00 50.44  ? 3900 THR A CB    1 
ATOM   17904 O  OG1   . THR A 1 3900 ? 184.499 121.503 173.062 1.00 44.79  ? 3900 THR A OG1   1 
ATOM   17905 C  CG2   . THR A 1 3900 ? 186.514 120.182 172.884 1.00 49.63  ? 3900 THR A CG2   1 
ATOM   17906 N  N     . TYR A 1 3901 ? 186.356 121.196 169.854 1.00 52.31  ? 3901 TYR A N     1 
ATOM   17907 C  CA    . TYR A 1 3901 ? 186.917 122.331 169.116 1.00 50.98  ? 3901 TYR A CA    1 
ATOM   17908 C  C     . TYR A 1 3901 ? 186.818 123.621 169.928 1.00 50.26  ? 3901 TYR A C     1 
ATOM   17909 O  O     . TYR A 1 3901 ? 186.653 124.714 169.382 1.00 50.47  ? 3901 TYR A O     1 
ATOM   17910 C  CB    . TYR A 1 3901 ? 186.245 122.496 167.751 1.00 46.28  ? 3901 TYR A CB    1 
ATOM   17911 C  CG    . TYR A 1 3901 ? 186.291 121.266 166.874 1.00 44.07  ? 3901 TYR A CG    1 
ATOM   17912 C  CD1   . TYR A 1 3901 ? 185.124 120.614 166.500 1.00 43.00  ? 3901 TYR A CD1   1 
ATOM   17913 C  CD2   . TYR A 1 3901 ? 187.498 120.768 166.405 1.00 42.76  ? 3901 TYR A CD2   1 
ATOM   17914 C  CE1   . TYR A 1 3901 ? 185.160 119.495 165.693 1.00 45.22  ? 3901 TYR A CE1   1 
ATOM   17915 C  CE2   . TYR A 1 3901 ? 187.543 119.649 165.597 1.00 43.96  ? 3901 TYR A CE2   1 
ATOM   17916 C  CZ    . TYR A 1 3901 ? 186.371 119.017 165.245 1.00 46.74  ? 3901 TYR A CZ    1 
ATOM   17917 O  OH    . TYR A 1 3901 ? 186.413 117.903 164.439 1.00 56.42  ? 3901 TYR A OH    1 
ATOM   17918 N  N     . ASP A 1 3902 ? 186.916 123.490 171.252 1.00 52.34  ? 3902 ASP A N     1 
ATOM   17919 C  CA    . ASP A 1 3902 ? 186.789 124.653 172.124 1.00 52.92  ? 3902 ASP A CA    1 
ATOM   17920 C  C     . ASP A 1 3902 ? 187.944 125.627 171.919 1.00 53.62  ? 3902 ASP A C     1 
ATOM   17921 O  O     . ASP A 1 3902 ? 187.736 126.843 171.830 1.00 50.57  ? 3902 ASP A O     1 
ATOM   17922 C  CB    . ASP A 1 3902 ? 186.712 124.205 173.584 1.00 54.44  ? 3902 ASP A CB    1 
ATOM   17923 C  CG    . ASP A 1 3902 ? 185.640 124.941 174.362 1.00 59.96  ? 3902 ASP A CG    1 
ATOM   17924 O  OD1   . ASP A 1 3902 ? 184.754 125.551 173.727 1.00 57.98  ? 3902 ASP A OD1   1 
ATOM   17925 O  OD2   . ASP A 1 3902 ? 185.681 124.909 175.610 1.00 56.17  ? 3902 ASP A OD2   1 
ATOM   17926 N  N     . ALA A 1 3903 ? 189.173 125.110 171.843 1.00 52.99  ? 3903 ALA A N     1 
ATOM   17927 C  CA    . ALA A 1 3903 ? 190.331 125.979 171.662 1.00 48.76  ? 3903 ALA A CA    1 
ATOM   17928 C  C     . ALA A 1 3903 ? 190.346 126.603 170.273 1.00 49.31  ? 3903 ALA A C     1 
ATOM   17929 O  O     . ALA A 1 3903 ? 190.760 127.757 170.108 1.00 49.39  ? 3903 ALA A O     1 
ATOM   17930 C  CB    . ALA A 1 3903 ? 191.619 125.196 171.913 1.00 48.81  ? 3903 ALA A CB    1 
ATOM   17931 N  N     . GLU A 1 3904 ? 189.908 125.852 169.261 1.00 52.18  ? 3904 GLU A N     1 
ATOM   17932 C  CA    . GLU A 1 3904 ? 189.887 126.373 167.899 1.00 42.80  ? 3904 GLU A CA    1 
ATOM   17933 C  C     . GLU A 1 3904 ? 188.891 127.520 167.763 1.00 39.77  ? 3904 GLU A C     1 
ATOM   17934 O  O     . GLU A 1 3904 ? 189.191 128.547 167.143 1.00 39.90  ? 3904 GLU A O     1 
ATOM   17935 C  CB    . GLU A 1 3904 ? 189.566 125.252 166.905 1.00 42.83  ? 3904 GLU A CB    1 
ATOM   17936 C  CG    . GLU A 1 3904 ? 190.554 124.070 166.858 1.00 47.05  ? 3904 GLU A CG    1 
ATOM   17937 C  CD    . GLU A 1 3904 ? 190.658 123.268 168.150 1.00 55.73  ? 3904 GLU A CD    1 
ATOM   17938 O  OE1   . GLU A 1 3904 ? 191.511 122.357 168.209 1.00 52.22  ? 3904 GLU A OE1   1 
ATOM   17939 O  OE2   . GLU A 1 3904 ? 189.891 123.532 169.099 1.00 54.73  ? 3904 GLU A OE2   1 
ATOM   17940 N  N     . PHE A 1 3905 ? 187.696 127.364 168.338 1.00 42.39  ? 3905 PHE A N     1 
ATOM   17941 C  CA    . PHE A 1 3905 ? 186.710 128.438 168.270 1.00 40.93  ? 3905 PHE A CA    1 
ATOM   17942 C  C     . PHE A 1 3905 ? 187.084 129.605 169.173 1.00 41.42  ? 3905 PHE A C     1 
ATOM   17943 O  O     . PHE A 1 3905 ? 186.718 130.750 168.884 1.00 44.62  ? 3905 PHE A O     1 
ATOM   17944 C  CB    . PHE A 1 3905 ? 185.321 127.914 168.631 1.00 39.72  ? 3905 PHE A CB    1 
ATOM   17945 C  CG    . PHE A 1 3905 ? 184.592 127.293 167.477 1.00 40.18  ? 3905 PHE A CG    1 
ATOM   17946 C  CD1   . PHE A 1 3905 ? 184.543 125.918 167.329 1.00 39.78  ? 3905 PHE A CD1   1 
ATOM   17947 C  CD2   . PHE A 1 3905 ? 183.968 128.086 166.529 1.00 37.49  ? 3905 PHE A CD2   1 
ATOM   17948 C  CE1   . PHE A 1 3905 ? 183.874 125.346 166.267 1.00 37.55  ? 3905 PHE A CE1   1 
ATOM   17949 C  CE2   . PHE A 1 3905 ? 183.301 127.520 165.462 1.00 38.02  ? 3905 PHE A CE2   1 
ATOM   17950 C  CZ    . PHE A 1 3905 ? 183.254 126.148 165.331 1.00 41.13  ? 3905 PHE A CZ    1 
ATOM   17951 N  N     . GLN A 1 3906 ? 187.798 129.339 170.270 1.00 45.04  ? 3906 GLN A N     1 
ATOM   17952 C  CA    . GLN A 1 3906 ? 188.263 130.425 171.125 1.00 45.47  ? 3906 GLN A CA    1 
ATOM   17953 C  C     . GLN A 1 3906 ? 189.226 131.336 170.374 1.00 45.99  ? 3906 GLN A C     1 
ATOM   17954 O  O     . GLN A 1 3906 ? 189.142 132.566 170.481 1.00 48.26  ? 3906 GLN A O     1 
ATOM   17955 C  CB    . GLN A 1 3906 ? 188.923 129.856 172.383 1.00 49.38  ? 3906 GLN A CB    1 
ATOM   17956 C  CG    . GLN A 1 3906 ? 190.074 130.688 172.932 1.00 56.85  ? 3906 GLN A CG    1 
ATOM   17957 C  CD    . GLN A 1 3906 ? 189.610 131.822 173.829 1.00 62.37  ? 3906 GLN A CD    1 
ATOM   17958 O  OE1   . GLN A 1 3906 ? 188.477 132.291 173.726 1.00 63.35  ? 3906 GLN A OE1   1 
ATOM   17959 N  NE2   . GLN A 1 3906 ? 190.490 132.267 174.718 1.00 58.12  ? 3906 GLN A NE2   1 
ATOM   17960 N  N     . HIS A 1 3907 ? 190.143 130.751 169.602 1.00 44.40  ? 3907 HIS A N     1 
ATOM   17961 C  CA    . HIS A 1 3907 ? 191.053 131.557 168.796 1.00 45.10  ? 3907 HIS A CA    1 
ATOM   17962 C  C     . HIS A 1 3907 ? 190.318 132.233 167.645 1.00 46.21  ? 3907 HIS A C     1 
ATOM   17963 O  O     . HIS A 1 3907 ? 190.652 133.358 167.258 1.00 49.34  ? 3907 HIS A O     1 
ATOM   17964 C  CB    . HIS A 1 3907 ? 192.197 130.694 168.268 1.00 44.75  ? 3907 HIS A CB    1 
ATOM   17965 C  CG    . HIS A 1 3907 ? 193.254 131.476 167.555 1.00 52.93  ? 3907 HIS A CG    1 
ATOM   17966 N  ND1   . HIS A 1 3907 ? 194.131 132.311 168.211 1.00 53.99  ? 3907 HIS A ND1   1 
ATOM   17967 C  CD2   . HIS A 1 3907 ? 193.562 131.564 166.240 1.00 53.75  ? 3907 HIS A CD2   1 
ATOM   17968 C  CE1   . HIS A 1 3907 ? 194.939 132.875 167.332 1.00 54.26  ? 3907 HIS A CE1   1 
ATOM   17969 N  NE2   . HIS A 1 3907 ? 194.616 132.438 166.128 1.00 53.79  ? 3907 HIS A NE2   1 
ATOM   17970 N  N     . PHE A 1 3908 ? 189.320 131.553 167.076 1.00 46.55  ? 3908 PHE A N     1 
ATOM   17971 C  CA    . PHE A 1 3908 ? 188.569 132.135 165.969 1.00 37.34  ? 3908 PHE A CA    1 
ATOM   17972 C  C     . PHE A 1 3908 ? 187.810 133.385 166.399 1.00 36.68  ? 3908 PHE A C     1 
ATOM   17973 O  O     . PHE A 1 3908 ? 187.534 134.259 165.570 1.00 34.98  ? 3908 PHE A O     1 
ATOM   17974 C  CB    . PHE A 1 3908 ? 187.606 131.098 165.389 1.00 32.17  ? 3908 PHE A CB    1 
ATOM   17975 C  CG    . PHE A 1 3908 ? 186.748 131.622 164.273 1.00 36.07  ? 3908 PHE A CG    1 
ATOM   17976 C  CD1   . PHE A 1 3908 ? 187.311 131.987 163.062 1.00 36.41  ? 3908 PHE A CD1   1 
ATOM   17977 C  CD2   . PHE A 1 3908 ? 185.378 131.748 164.434 1.00 35.58  ? 3908 PHE A CD2   1 
ATOM   17978 C  CE1   . PHE A 1 3908 ? 186.526 132.470 162.033 1.00 31.34  ? 3908 PHE A CE1   1 
ATOM   17979 C  CE2   . PHE A 1 3908 ? 184.587 132.229 163.408 1.00 28.45  ? 3908 PHE A CE2   1 
ATOM   17980 C  CZ    . PHE A 1 3908 ? 185.163 132.591 162.207 1.00 33.45  ? 3908 PHE A CZ    1 
ATOM   17981 N  N     . LEU A 1 3909 ? 187.475 133.493 167.685 1.00 39.48  ? 3909 LEU A N     1 
ATOM   17982 C  CA    . LEU A 1 3909 ? 186.694 134.621 168.175 1.00 37.94  ? 3909 LEU A CA    1 
ATOM   17983 C  C     . LEU A 1 3909 ? 187.524 135.637 168.947 1.00 41.91  ? 3909 LEU A C     1 
ATOM   17984 O  O     . LEU A 1 3909 ? 187.178 136.824 168.958 1.00 46.11  ? 3909 LEU A O     1 
ATOM   17985 C  CB    . LEU A 1 3909 ? 185.551 134.121 169.063 1.00 39.66  ? 3909 LEU A CB    1 
ATOM   17986 C  CG    . LEU A 1 3909 ? 184.389 133.442 168.339 1.00 39.32  ? 3909 LEU A CG    1 
ATOM   17987 C  CD1   . LEU A 1 3909 ? 183.251 133.145 169.303 1.00 35.11  ? 3909 LEU A CD1   1 
ATOM   17988 C  CD2   . LEU A 1 3909 ? 183.907 134.300 167.182 1.00 35.52  ? 3909 LEU A CD2   1 
ATOM   17989 N  N     . ARG A 1 3910 ? 188.608 135.207 169.592 1.00 48.34  ? 3910 ARG A N     1 
ATOM   17990 C  CA    . ARG A 1 3910 ? 189.435 136.094 170.406 1.00 55.61  ? 3910 ARG A CA    1 
ATOM   17991 C  C     . ARG A 1 3910 ? 190.905 135.948 170.039 1.00 59.85  ? 3910 ARG A C     1 
ATOM   17992 O  O     . ARG A 1 3910 ? 191.789 136.031 170.898 1.00 64.62  ? 3910 ARG A O     1 
ATOM   17993 C  CB    . ARG A 1 3910 ? 189.229 135.831 171.898 1.00 57.05  ? 3910 ARG A CB    1 
ATOM   17994 C  CG    . ARG A 1 3910 ? 187.901 136.324 172.442 1.00 56.79  ? 3910 ARG A CG    1 
ATOM   17995 C  CD    . ARG A 1 3910 ? 187.720 135.926 173.900 1.00 62.71  ? 3910 ARG A CD    1 
ATOM   17996 N  NE    . ARG A 1 3910 ? 186.355 135.504 174.194 1.00 67.33  ? 3910 ARG A NE    1 
ATOM   17997 C  CZ    . ARG A 1 3910 ? 185.833 134.338 173.839 1.00 70.13  ? 3910 ARG A CZ    1 
ATOM   17998 N  NH1   . ARG A 1 3910 ? 186.537 133.439 173.170 1.00 63.39  ? 3910 ARG A NH1   1 
ATOM   17999 N  NH2   . ARG A 1 3910 ? 184.571 134.068 174.160 1.00 65.89  ? 3910 ARG A NH2   1 
ATOM   18000 N  N     . GLY A 1 3911 ? 191.190 135.732 168.753 1.00 61.74  ? 3911 GLY A N     1 
ATOM   18001 C  CA    . GLY A 1 3911 ? 192.570 135.626 168.315 1.00 60.33  ? 3911 GLY A CA    1 
ATOM   18002 C  C     . GLY A 1 3911 ? 193.299 136.950 168.244 1.00 66.23  ? 3911 GLY A C     1 
ATOM   18003 O  O     . GLY A 1 3911 ? 194.534 136.964 168.228 1.00 66.69  ? 3911 GLY A O     1 
ATOM   18004 N  N     . ASN A 1 3912 ? 192.566 138.063 168.200 1.00 69.99  ? 3912 ASN A N     1 
ATOM   18005 C  CA    . ASN A 1 3912 ? 193.190 139.379 168.162 1.00 71.18  ? 3912 ASN A CA    1 
ATOM   18006 C  C     . ASN A 1 3912 ? 193.619 139.878 169.536 1.00 72.08  ? 3912 ASN A C     1 
ATOM   18007 O  O     . ASN A 1 3912 ? 194.393 140.838 169.613 1.00 76.89  ? 3912 ASN A O     1 
ATOM   18008 C  CB    . ASN A 1 3912 ? 192.243 140.393 167.506 1.00 75.14  ? 3912 ASN A CB    1 
ATOM   18009 C  CG    . ASN A 1 3912 ? 190.938 140.567 168.269 1.00 79.08  ? 3912 ASN A CG    1 
ATOM   18010 O  OD1   . ASN A 1 3912 ? 190.752 140.017 169.355 1.00 80.22  ? 3912 ASN A OD1   1 
ATOM   18011 N  ND2   . ASN A 1 3912 ? 190.024 141.343 167.697 1.00 74.47  ? 3912 ASN A ND2   1 
ATOM   18012 N  N     . GLU A 1 3913 ? 193.142 139.255 170.614 1.00 75.81  ? 3913 GLU A N     1 
ATOM   18013 C  CA    . GLU A 1 3913 ? 193.520 139.658 171.962 1.00 75.64  ? 3913 GLU A CA    1 
ATOM   18014 C  C     . GLU A 1 3913 ? 194.894 139.148 172.373 1.00 76.75  ? 3913 GLU A C     1 
ATOM   18015 O  O     . GLU A 1 3913 ? 195.400 139.560 173.423 1.00 75.28  ? 3913 GLU A O     1 
ATOM   18016 C  CB    . GLU A 1 3913 ? 192.475 139.173 172.969 1.00 73.99  ? 3913 GLU A CB    1 
ATOM   18017 C  CG    . GLU A 1 3913 ? 191.071 139.692 172.710 1.00 74.55  ? 3913 GLU A CG    1 
ATOM   18018 C  CD    . GLU A 1 3913 ? 190.107 139.339 173.825 1.00 75.74  ? 3913 GLU A CD    1 
ATOM   18019 O  OE1   . GLU A 1 3913 ? 188.925 139.733 173.739 1.00 76.14  ? 3913 GLU A OE1   1 
ATOM   18020 O  OE2   . GLU A 1 3913 ? 190.531 138.665 174.787 1.00 72.32  ? 3913 GLU A OE2   1 
ATOM   18021 N  N     . ILE A 1 3914 ? 195.507 138.270 171.581 1.00 77.20  ? 3914 ILE A N     1 
ATOM   18022 C  CA    . ILE A 1 3914 ? 196.821 137.714 171.899 1.00 76.94  ? 3914 ILE A CA    1 
ATOM   18023 C  C     . ILE A 1 3914 ? 197.853 138.801 171.613 1.00 83.43  ? 3914 ILE A C     1 
ATOM   18024 O  O     . ILE A 1 3914 ? 198.227 139.033 170.462 1.00 83.29  ? 3914 ILE A O     1 
ATOM   18025 C  CB    . ILE A 1 3914 ? 197.107 136.436 171.107 1.00 73.42  ? 3914 ILE A CB    1 
ATOM   18026 C  CG1   . ILE A 1 3914 ? 196.021 135.392 171.377 1.00 68.70  ? 3914 ILE A CG1   1 
ATOM   18027 C  CG2   . ILE A 1 3914 ? 198.480 135.886 171.461 1.00 73.73  ? 3914 ILE A CG2   1 
ATOM   18028 C  CD1   . ILE A 1 3914 ? 196.254 134.070 170.680 1.00 62.30  ? 3914 ILE A CD1   1 
ATOM   18029 N  N     . VAL A 1 3915 ? 198.317 139.472 172.667 1.00 88.27  ? 3915 VAL A N     1 
ATOM   18030 C  CA    . VAL A 1 3915 ? 199.258 140.574 172.506 1.00 89.45  ? 3915 VAL A CA    1 
ATOM   18031 C  C     . VAL A 1 3915 ? 200.621 140.029 172.104 1.00 88.42  ? 3915 VAL A C     1 
ATOM   18032 O  O     . VAL A 1 3915 ? 201.128 139.072 172.704 1.00 84.12  ? 3915 VAL A O     1 
ATOM   18033 C  CB    . VAL A 1 3915 ? 199.345 141.398 173.799 1.00 87.65  ? 3915 VAL A CB    1 
ATOM   18034 C  CG1   . VAL A 1 3915 ? 200.392 142.495 173.664 1.00 81.13  ? 3915 VAL A CG1   1 
ATOM   18035 C  CG2   . VAL A 1 3915 ? 197.987 141.990 174.142 1.00 82.79  ? 3915 VAL A CG2   1 
ATOM   18036 N  N     . LEU A 1 3916 ? 201.218 140.636 171.082 1.00 89.04  ? 3916 LEU A N     1 
ATOM   18037 C  CA    . LEU A 1 3916 ? 202.539 140.266 170.597 1.00 91.79  ? 3916 LEU A CA    1 
ATOM   18038 C  C     . LEU A 1 3916 ? 203.482 141.453 170.734 1.00 97.78  ? 3916 LEU A C     1 
ATOM   18039 O  O     . LEU A 1 3916 ? 203.102 142.595 170.459 1.00 95.74  ? 3916 LEU A O     1 
ATOM   18040 C  CB    . LEU A 1 3916 ? 202.483 139.806 169.137 1.00 90.44  ? 3916 LEU A CB    1 
ATOM   18041 C  CG    . LEU A 1 3916 ? 201.650 138.555 168.854 1.00 87.62  ? 3916 LEU A CG    1 
ATOM   18042 C  CD1   . LEU A 1 3916 ? 201.720 138.189 167.381 1.00 83.41  ? 3916 LEU A CD1   1 
ATOM   18043 C  CD2   . LEU A 1 3916 ? 202.116 137.394 169.719 1.00 85.16  ? 3916 LEU A CD2   1 
ATOM   18044 N  N     . SER A 1 3917 ? 204.711 141.177 171.162 1.00 103.41 ? 3917 SER A N     1 
ATOM   18045 C  CA    . SER A 1 3917 ? 205.701 142.223 171.362 1.00 105.36 ? 3917 SER A CA    1 
ATOM   18046 C  C     . SER A 1 3917 ? 206.327 142.623 170.027 1.00 110.99 ? 3917 SER A C     1 
ATOM   18047 O  O     . SER A 1 3917 ? 205.982 142.101 168.962 1.00 113.78 ? 3917 SER A O     1 
ATOM   18048 C  CB    . SER A 1 3917 ? 206.766 141.761 172.354 1.00 101.18 ? 3917 SER A CB    1 
ATOM   18049 O  OG    . SER A 1 3917 ? 206.189 141.432 173.606 1.00 93.98  ? 3917 SER A OG    1 
ATOM   18050 N  N     . ALA A 1 3918 ? 207.261 143.577 170.086 1.00 110.55 ? 3918 ALA A N     1 
ATOM   18051 C  CA    . ALA A 1 3918 ? 207.928 144.038 168.873 1.00 113.01 ? 3918 ALA A CA    1 
ATOM   18052 C  C     . ALA A 1 3918 ? 208.738 142.922 168.226 1.00 118.30 ? 3918 ALA A C     1 
ATOM   18053 O  O     . ALA A 1 3918 ? 208.720 142.761 167.000 1.00 117.64 ? 3918 ALA A O     1 
ATOM   18054 C  CB    . ALA A 1 3918 ? 208.823 145.237 169.190 1.00 104.47 ? 3918 ALA A CB    1 
ATOM   18055 N  N     . GLY A 1 3919 ? 209.455 142.140 169.033 1.00 117.14 ? 3919 GLY A N     1 
ATOM   18056 C  CA    . GLY A 1 3919 ? 210.240 141.038 168.511 1.00 117.23 ? 3919 GLY A CA    1 
ATOM   18057 C  C     . GLY A 1 3919 ? 209.464 139.772 168.230 1.00 116.23 ? 3919 GLY A C     1 
ATOM   18058 O  O     . GLY A 1 3919 ? 210.041 138.811 167.713 1.00 114.67 ? 3919 GLY A O     1 
ATOM   18059 N  N     . SER A 1 3920 ? 208.171 139.747 168.563 1.00 116.48 ? 3920 SER A N     1 
ATOM   18060 C  CA    . SER A 1 3920 ? 207.363 138.557 168.314 1.00 114.03 ? 3920 SER A CA    1 
ATOM   18061 C  C     . SER A 1 3920 ? 207.221 138.284 166.822 1.00 109.81 ? 3920 SER A C     1 
ATOM   18062 O  O     . SER A 1 3920 ? 207.255 137.125 166.391 1.00 104.47 ? 3920 SER A O     1 
ATOM   18063 C  CB    . SER A 1 3920 ? 205.989 138.711 168.966 1.00 105.13 ? 3920 SER A CB    1 
ATOM   18064 O  OG    . SER A 1 3920 ? 206.107 138.891 170.366 1.00 100.94 ? 3920 SER A OG    1 
ATOM   18065 N  N     . THR A 1 3921 ? 207.059 139.329 166.022 1.00 110.33 ? 3921 THR A N     1 
ATOM   18066 C  CA    . THR A 1 3921 ? 206.897 139.159 164.582 1.00 106.88 ? 3921 THR A CA    1 
ATOM   18067 C  C     . THR A 1 3921 ? 208.230 138.788 163.947 1.00 105.58 ? 3921 THR A C     1 
ATOM   18068 O  O     . THR A 1 3921 ? 209.195 139.556 164.060 1.00 104.63 ? 3921 THR A O     1 
ATOM   18069 C  CB    . THR A 1 3921 ? 206.352 140.440 163.954 1.00 102.95 ? 3921 THR A CB    1 
ATOM   18070 O  OG1   . THR A 1 3921 ? 205.053 140.723 164.488 1.00 98.29  ? 3921 THR A OG1   1 
ATOM   18071 C  CG2   . THR A 1 3921 ? 206.254 140.293 162.443 1.00 97.17  ? 3921 THR A CG2   1 
ATOM   18072 N  N     . PRO A 1 3922 ? 208.335 137.642 163.276 1.00 105.69 ? 3922 PRO A N     1 
ATOM   18073 C  CA    . PRO A 1 3922 ? 209.595 137.254 162.631 1.00 106.80 ? 3922 PRO A CA    1 
ATOM   18074 C  C     . PRO A 1 3922 ? 209.750 137.723 161.193 1.00 102.43 ? 3922 PRO A C     1 
ATOM   18075 O  O     . PRO A 1 3922 ? 210.778 137.418 160.577 1.00 101.42 ? 3922 PRO A O     1 
ATOM   18076 C  CB    . PRO A 1 3922 ? 209.530 135.723 162.694 1.00 105.63 ? 3922 PRO A CB    1 
ATOM   18077 C  CG    . PRO A 1 3922 ? 208.065 135.413 162.587 1.00 101.67 ? 3922 PRO A CG    1 
ATOM   18078 C  CD    . PRO A 1 3922 ? 207.298 136.607 163.120 1.00 103.33 ? 3922 PRO A CD    1 
ATOM   18079 N  N     . ARG A 1 3923 ? 208.768 138.446 160.651 1.00 99.34  ? 3923 ARG A N     1 
ATOM   18080 C  CA    . ARG A 1 3923 ? 208.810 138.967 159.285 1.00 99.02  ? 3923 ARG A CA    1 
ATOM   18081 C  C     . ARG A 1 3923 ? 208.998 137.834 158.272 1.00 97.69  ? 3923 ARG A C     1 
ATOM   18082 O  O     . ARG A 1 3923 ? 210.013 137.736 157.579 1.00 93.05  ? 3923 ARG A O     1 
ATOM   18083 C  CB    . ARG A 1 3923 ? 209.901 140.036 159.140 1.00 99.52  ? 3923 ARG A CB    1 
ATOM   18084 C  CG    . ARG A 1 3923 ? 209.764 140.906 157.900 1.00 97.69  ? 3923 ARG A CG    1 
ATOM   18085 C  CD    . ARG A 1 3923 ? 210.993 141.777 157.699 1.00 100.49 ? 3923 ARG A CD    1 
ATOM   18086 N  NE    . ARG A 1 3923 ? 212.224 140.996 157.711 1.00 108.00 ? 3923 ARG A NE    1 
ATOM   18087 C  CZ    . ARG A 1 3923 ? 213.439 141.513 157.587 1.00 107.35 ? 3923 ARG A CZ    1 
ATOM   18088 N  NH1   . ARG A 1 3923 ? 213.625 142.814 157.440 1.00 107.64 ? 3923 ARG A NH1   1 
ATOM   18089 N  NH2   . ARG A 1 3923 ? 214.494 140.703 157.610 1.00 102.31 ? 3923 ARG A NH2   1 
ATOM   18090 N  N     . ILE A 1 3924 ? 207.989 136.961 158.212 1.00 98.83  ? 3924 ILE A N     1 
ATOM   18091 C  CA    . ILE A 1 3924 ? 208.022 135.842 157.278 1.00 93.73  ? 3924 ILE A CA    1 
ATOM   18092 C  C     . ILE A 1 3924 ? 208.023 136.365 155.849 1.00 89.87  ? 3924 ILE A C     1 
ATOM   18093 O  O     . ILE A 1 3924 ? 207.307 137.316 155.510 1.00 87.71  ? 3924 ILE A O     1 
ATOM   18094 C  CB    . ILE A 1 3924 ? 206.831 134.900 157.525 1.00 90.29  ? 3924 ILE A CB    1 
ATOM   18095 C  CG1   . ILE A 1 3924 ? 206.800 134.443 158.985 1.00 88.83  ? 3924 ILE A CG1   1 
ATOM   18096 C  CG2   . ILE A 1 3924 ? 206.894 133.695 156.598 1.00 84.01  ? 3924 ILE A CG2   1 
ATOM   18097 C  CD1   . ILE A 1 3924 ? 205.740 135.127 159.818 1.00 88.25  ? 3924 ILE A CD1   1 
ATOM   18098 N  N     . GLN A 1 3925 ? 208.841 135.744 155.002 1.00 90.14  ? 3925 GLN A N     1 
ATOM   18099 C  CA    . GLN A 1 3925 ? 208.934 136.152 153.608 1.00 89.81  ? 3925 GLN A CA    1 
ATOM   18100 C  C     . GLN A 1 3925 ? 207.620 135.888 152.884 1.00 86.97  ? 3925 GLN A C     1 
ATOM   18101 O  O     . GLN A 1 3925 ? 206.977 134.854 153.082 1.00 82.64  ? 3925 GLN A O     1 
ATOM   18102 C  CB    . GLN A 1 3925 ? 210.085 135.415 152.918 1.00 87.93  ? 3925 GLN A CB    1 
ATOM   18103 C  CG    . GLN A 1 3925 ? 210.489 135.978 151.558 1.00 87.70  ? 3925 GLN A CG    1 
ATOM   18104 C  CD    . GLN A 1 3925 ? 209.736 135.350 150.396 1.00 88.31  ? 3925 GLN A CD    1 
ATOM   18105 O  OE1   . GLN A 1 3925 ? 208.788 134.588 150.586 1.00 87.31  ? 3925 GLN A OE1   1 
ATOM   18106 N  NE2   . GLN A 1 3925 ? 210.160 135.671 149.179 1.00 84.86  ? 3925 GLN A NE2   1 
ATOM   18107 N  N     . GLY A 1 3926 ? 207.222 136.838 152.039 1.00 84.69  ? 3926 GLY A N     1 
ATOM   18108 C  CA    . GLY A 1 3926 ? 206.005 136.720 151.267 1.00 77.32  ? 3926 GLY A CA    1 
ATOM   18109 C  C     . GLY A 1 3926 ? 204.733 137.071 152.005 1.00 75.37  ? 3926 GLY A C     1 
ATOM   18110 O  O     . GLY A 1 3926 ? 203.649 136.968 151.416 1.00 73.16  ? 3926 GLY A O     1 
ATOM   18111 N  N     . LEU A 1 3927 ? 204.822 137.482 153.267 1.00 77.11  ? 3927 LEU A N     1 
ATOM   18112 C  CA    . LEU A 1 3927 ? 203.658 137.807 154.078 1.00 71.62  ? 3927 LEU A CA    1 
ATOM   18113 C  C     . LEU A 1 3927 ? 203.724 139.257 154.533 1.00 69.55  ? 3927 LEU A C     1 
ATOM   18114 O  O     . LEU A 1 3927 ? 204.796 139.761 154.886 1.00 73.58  ? 3927 LEU A O     1 
ATOM   18115 C  CB    . LEU A 1 3927 ? 203.549 136.890 155.305 1.00 69.84  ? 3927 LEU A CB    1 
ATOM   18116 C  CG    . LEU A 1 3927 ? 202.745 135.589 155.202 1.00 65.01  ? 3927 LEU A CG    1 
ATOM   18117 C  CD1   . LEU A 1 3927 ? 203.017 134.849 153.905 1.00 64.72  ? 3927 LEU A CD1   1 
ATOM   18118 C  CD2   . LEU A 1 3927 ? 203.027 134.693 156.400 1.00 67.15  ? 3927 LEU A CD2   1 
ATOM   18119 N  N     . THR A 1 3928 ? 202.572 139.920 154.520 1.00 65.78  ? 3928 THR A N     1 
ATOM   18120 C  CA    . THR A 1 3928 ? 202.465 141.275 155.033 1.00 66.91  ? 3928 THR A CA    1 
ATOM   18121 C  C     . THR A 1 3928 ? 202.637 141.259 156.554 1.00 67.23  ? 3928 THR A C     1 
ATOM   18122 O  O     . THR A 1 3928 ? 202.427 140.238 157.215 1.00 69.01  ? 3928 THR A O     1 
ATOM   18123 C  CB    . THR A 1 3928 ? 201.115 141.880 154.625 1.00 62.28  ? 3928 THR A CB    1 
ATOM   18124 O  OG1   . THR A 1 3928 ? 201.018 141.889 153.196 1.00 54.11  ? 3928 THR A OG1   1 
ATOM   18125 C  CG2   . THR A 1 3928 ? 200.963 143.316 155.116 1.00 66.56  ? 3928 THR A CG2   1 
ATOM   18126 N  N     . VAL A 1 3929 ? 203.051 142.405 157.104 1.00 64.85  ? 3929 VAL A N     1 
ATOM   18127 C  CA    . VAL A 1 3929 ? 203.294 142.509 158.542 1.00 69.74  ? 3929 VAL A CA    1 
ATOM   18128 C  C     . VAL A 1 3929 ? 202.054 142.093 159.325 1.00 73.18  ? 3929 VAL A C     1 
ATOM   18129 O  O     . VAL A 1 3929 ? 202.139 141.345 160.307 1.00 72.51  ? 3929 VAL A O     1 
ATOM   18130 C  CB    . VAL A 1 3929 ? 203.739 143.937 158.906 1.00 69.80  ? 3929 VAL A CB    1 
ATOM   18131 C  CG1   . VAL A 1 3929 ? 203.754 144.123 160.414 1.00 68.72  ? 3929 VAL A CG1   1 
ATOM   18132 C  CG2   . VAL A 1 3929 ? 205.107 144.235 158.312 1.00 66.39  ? 3929 VAL A CG2   1 
ATOM   18133 N  N     . GLU A 1 3930 ? 200.882 142.571 158.902 1.00 75.05  ? 3930 GLU A N     1 
ATOM   18134 C  CA    . GLU A 1 3930 ? 199.643 142.167 159.561 1.00 72.52  ? 3930 GLU A CA    1 
ATOM   18135 C  C     . GLU A 1 3930 ? 199.369 140.682 159.358 1.00 67.43  ? 3930 GLU A C     1 
ATOM   18136 O  O     . GLU A 1 3930 ? 198.871 140.006 160.267 1.00 70.38  ? 3930 GLU A O     1 
ATOM   18137 C  CB    . GLU A 1 3930 ? 198.473 143.010 159.049 1.00 73.74  ? 3930 GLU A CB    1 
ATOM   18138 C  CG    . GLU A 1 3930 ? 198.500 144.489 159.460 1.00 80.74  ? 3930 GLU A CG    1 
ATOM   18139 C  CD    . GLU A 1 3930 ? 198.322 144.736 160.959 1.00 91.19  ? 3930 GLU A CD    1 
ATOM   18140 O  OE1   . GLU A 1 3930 ? 198.520 143.813 161.777 1.00 88.31  ? 3930 GLU A OE1   1 
ATOM   18141 O  OE2   . GLU A 1 3930 ? 197.977 145.880 161.322 1.00 95.11  ? 3930 GLU A OE2   1 
ATOM   18142 N  N     . GLN A 1 3931 ? 199.675 140.156 158.169 1.00 64.42  ? 3931 GLN A N     1 
ATOM   18143 C  CA    . GLN A 1 3931 ? 199.540 138.720 157.941 1.00 64.49  ? 3931 GLN A CA    1 
ATOM   18144 C  C     . GLN A 1 3931 ? 200.495 137.933 158.828 1.00 69.91  ? 3931 GLN A C     1 
ATOM   18145 O  O     . GLN A 1 3931 ? 200.125 136.891 159.382 1.00 70.21  ? 3931 GLN A O     1 
ATOM   18146 C  CB    . GLN A 1 3931 ? 199.787 138.391 156.469 1.00 54.78  ? 3931 GLN A CB    1 
ATOM   18147 C  CG    . GLN A 1 3931 ? 198.660 138.793 155.536 1.00 49.62  ? 3931 GLN A CG    1 
ATOM   18148 C  CD    . GLN A 1 3931 ? 198.841 138.236 154.138 1.00 52.27  ? 3931 GLN A CD    1 
ATOM   18149 O  OE1   . GLN A 1 3931 ? 199.825 137.556 153.851 1.00 61.34  ? 3931 GLN A OE1   1 
ATOM   18150 N  NE2   . GLN A 1 3931 ? 197.889 138.524 153.258 1.00 51.21  ? 3931 GLN A NE2   1 
ATOM   18151 N  N     . ALA A 1 3932 ? 201.733 138.414 158.968 1.00 72.90  ? 3932 ALA A N     1 
ATOM   18152 C  CA    . ALA A 1 3932 ? 202.698 137.744 159.833 1.00 70.73  ? 3932 ALA A CA    1 
ATOM   18153 C  C     . ALA A 1 3932 ? 202.242 137.759 161.285 1.00 70.90  ? 3932 ALA A C     1 
ATOM   18154 O  O     . ALA A 1 3932 ? 202.406 136.767 162.006 1.00 73.54  ? 3932 ALA A O     1 
ATOM   18155 C  CB    . ALA A 1 3932 ? 204.071 138.401 159.694 1.00 78.06  ? 3932 ALA A CB    1 
ATOM   18156 N  N     . GLU A 1 3933 ? 201.675 138.881 161.736 1.00 68.90  ? 3933 GLU A N     1 
ATOM   18157 C  CA    . GLU A 1 3933 ? 201.186 138.965 163.108 1.00 73.95  ? 3933 GLU A CA    1 
ATOM   18158 C  C     . GLU A 1 3933 ? 200.077 137.953 163.364 1.00 72.57  ? 3933 GLU A C     1 
ATOM   18159 O  O     . GLU A 1 3933 ? 200.045 137.308 164.419 1.00 71.36  ? 3933 GLU A O     1 
ATOM   18160 C  CB    . GLU A 1 3933 ? 200.697 140.382 163.404 1.00 76.07  ? 3933 GLU A CB    1 
ATOM   18161 C  CG    . GLU A 1 3933 ? 200.467 140.663 164.880 1.00 84.04  ? 3933 GLU A CG    1 
ATOM   18162 C  CD    . GLU A 1 3933 ? 200.868 142.070 165.274 1.00 90.26  ? 3933 GLU A CD    1 
ATOM   18163 O  OE1   . GLU A 1 3933 ? 200.549 142.485 166.407 1.00 92.67  ? 3933 GLU A OE1   1 
ATOM   18164 O  OE2   . GLU A 1 3933 ? 201.502 142.761 164.449 1.00 88.01  ? 3933 GLU A OE2   1 
ATOM   18165 N  N     . ALA A 1 3934 ? 199.157 137.800 162.409 1.00 71.43  ? 3934 ALA A N     1 
ATOM   18166 C  CA    . ALA A 1 3934 ? 198.081 136.828 162.568 1.00 68.92  ? 3934 ALA A CA    1 
ATOM   18167 C  C     . ALA A 1 3934 ? 198.617 135.402 162.574 1.00 68.92  ? 3934 ALA A C     1 
ATOM   18168 O  O     . ALA A 1 3934 ? 198.008 134.505 163.169 1.00 67.34  ? 3934 ALA A O     1 
ATOM   18169 C  CB    . ALA A 1 3934 ? 197.043 137.010 161.461 1.00 59.84  ? 3934 ALA A CB    1 
ATOM   18170 N  N     . VAL A 1 3935 ? 199.753 135.170 161.912 1.00 68.50  ? 3935 VAL A N     1 
ATOM   18171 C  CA    . VAL A 1 3935 ? 200.346 133.836 161.896 1.00 70.37  ? 3935 VAL A CA    1 
ATOM   18172 C  C     . VAL A 1 3935 ? 200.868 133.465 163.279 1.00 72.31  ? 3935 VAL A C     1 
ATOM   18173 O  O     . VAL A 1 3935 ? 200.625 132.358 163.774 1.00 69.77  ? 3935 VAL A O     1 
ATOM   18174 C  CB    . VAL A 1 3935 ? 201.458 133.756 160.834 1.00 69.13  ? 3935 VAL A CB    1 
ATOM   18175 C  CG1   . VAL A 1 3935 ? 202.342 132.541 161.077 1.00 71.96  ? 3935 VAL A CG1   1 
ATOM   18176 C  CG2   . VAL A 1 3935 ? 200.853 133.706 159.447 1.00 60.98  ? 3935 VAL A CG2   1 
ATOM   18177 N  N     . VAL A 1 3936 ? 201.592 134.384 163.923 1.00 68.96  ? 3936 VAL A N     1 
ATOM   18178 C  CA    . VAL A 1 3936 ? 202.159 134.099 165.238 1.00 72.55  ? 3936 VAL A CA    1 
ATOM   18179 C  C     . VAL A 1 3936 ? 201.053 133.865 166.257 1.00 74.57  ? 3936 VAL A C     1 
ATOM   18180 O  O     . VAL A 1 3936 ? 201.166 132.997 167.132 1.00 74.89  ? 3936 VAL A O     1 
ATOM   18181 C  CB    . VAL A 1 3936 ? 203.102 135.235 165.674 1.00 78.28  ? 3936 VAL A CB    1 
ATOM   18182 C  CG1   . VAL A 1 3936 ? 203.853 134.845 166.937 1.00 76.63  ? 3936 VAL A CG1   1 
ATOM   18183 C  CG2   . VAL A 1 3936 ? 204.075 135.573 164.557 1.00 81.75  ? 3936 VAL A CG2   1 
ATOM   18184 N  N     . ARG A 1 3937 ? 199.969 134.639 166.168 1.00 73.50  ? 3937 ARG A N     1 
ATOM   18185 C  CA    . ARG A 1 3937 ? 198.828 134.412 167.047 1.00 66.89  ? 3937 ARG A CA    1 
ATOM   18186 C  C     . ARG A 1 3937 ? 198.216 133.038 166.802 1.00 64.75  ? 3937 ARG A C     1 
ATOM   18187 O  O     . ARG A 1 3937 ? 197.869 132.326 167.751 1.00 66.62  ? 3937 ARG A O     1 
ATOM   18188 C  CB    . ARG A 1 3937 ? 197.787 135.512 166.845 1.00 63.03  ? 3937 ARG A CB    1 
ATOM   18189 C  CG    . ARG A 1 3937 ? 198.227 136.873 167.356 1.00 67.26  ? 3937 ARG A CG    1 
ATOM   18190 C  CD    . ARG A 1 3937 ? 197.343 137.981 166.812 1.00 72.78  ? 3937 ARG A CD    1 
ATOM   18191 N  NE    . ARG A 1 3937 ? 197.991 139.285 166.895 1.00 77.29  ? 3937 ARG A NE    1 
ATOM   18192 C  CZ    . ARG A 1 3937 ? 197.605 140.265 167.700 1.00 79.72  ? 3937 ARG A CZ    1 
ATOM   18193 N  NH1   . ARG A 1 3937 ? 196.573 140.123 168.515 1.00 82.26  ? 3937 ARG A NH1   1 
ATOM   18194 N  NH2   . ARG A 1 3937 ? 198.271 141.415 167.688 1.00 82.09  ? 3937 ARG A NH2   1 
ATOM   18195 N  N     . LEU A 1 3938 ? 198.085 132.646 165.532 1.00 60.86  ? 3938 LEU A N     1 
ATOM   18196 C  CA    . LEU A 1 3938 ? 197.565 131.321 165.213 1.00 60.46  ? 3938 LEU A CA    1 
ATOM   18197 C  C     . LEU A 1 3938 ? 198.521 130.221 165.656 1.00 65.74  ? 3938 LEU A C     1 
ATOM   18198 O  O     . LEU A 1 3938 ? 198.082 129.105 165.958 1.00 66.90  ? 3938 LEU A O     1 
ATOM   18199 C  CB    . LEU A 1 3938 ? 197.287 131.216 163.713 1.00 57.32  ? 3938 LEU A CB    1 
ATOM   18200 C  CG    . LEU A 1 3938 ? 196.658 129.917 163.204 1.00 53.71  ? 3938 LEU A CG    1 
ATOM   18201 C  CD1   . LEU A 1 3938 ? 195.312 129.678 163.865 1.00 47.27  ? 3938 LEU A CD1   1 
ATOM   18202 C  CD2   . LEU A 1 3938 ? 196.519 129.944 161.691 1.00 48.72  ? 3938 LEU A CD2   1 
ATOM   18203 N  N     . SER A 1 3939 ? 199.822 130.514 165.708 1.00 69.57  ? 3939 SER A N     1 
ATOM   18204 C  CA    . SER A 1 3939 ? 200.807 129.525 166.127 1.00 69.81  ? 3939 SER A CA    1 
ATOM   18205 C  C     . SER A 1 3939 ? 200.653 129.116 167.586 1.00 68.11  ? 3939 SER A C     1 
ATOM   18206 O  O     . SER A 1 3939 ? 201.227 128.098 167.986 1.00 68.00  ? 3939 SER A O     1 
ATOM   18207 C  CB    . SER A 1 3939 ? 202.221 130.057 165.889 1.00 69.97  ? 3939 SER A CB    1 
ATOM   18208 O  OG    . SER A 1 3939 ? 202.490 131.177 166.713 1.00 69.79  ? 3939 SER A OG    1 
ATOM   18209 N  N     . CYS A 1 3940 ? 199.904 129.881 168.385 1.00 71.12  ? 3940 CYS A N     1 
ATOM   18210 C  CA    . CYS A 1 3940 ? 199.695 129.515 169.782 1.00 67.71  ? 3940 CYS A CA    1 
ATOM   18211 C  C     . CYS A 1 3940 ? 198.953 128.191 169.912 1.00 68.72  ? 3940 CYS A C     1 
ATOM   18212 O  O     . CYS A 1 3940 ? 199.147 127.466 170.895 1.00 70.14  ? 3940 CYS A O     1 
ATOM   18213 C  CB    . CYS A 1 3940 ? 198.932 130.623 170.507 1.00 66.88  ? 3940 CYS A CB    1 
ATOM   18214 S  SG    . CYS A 1 3940 ? 199.774 132.222 170.530 1.00 77.29  ? 3940 CYS A SG    1 
ATOM   18215 N  N     . LEU A 1 3941 ? 198.103 127.862 168.944 1.00 68.54  ? 3941 LEU A N     1 
ATOM   18216 C  CA    . LEU A 1 3941 ? 197.392 126.596 168.980 1.00 69.21  ? 3941 LEU A CA    1 
ATOM   18217 C  C     . LEU A 1 3941 ? 198.361 125.437 168.746 1.00 71.52  ? 3941 LEU A C     1 
ATOM   18218 O  O     . LEU A 1 3941 ? 199.353 125.580 168.026 1.00 70.69  ? 3941 LEU A O     1 
ATOM   18219 C  CB    . LEU A 1 3941 ? 196.286 126.571 167.928 1.00 70.94  ? 3941 LEU A CB    1 
ATOM   18220 C  CG    . LEU A 1 3941 ? 195.122 127.551 168.104 1.00 67.02  ? 3941 LEU A CG    1 
ATOM   18221 C  CD1   . LEU A 1 3941 ? 193.878 127.030 167.401 1.00 58.38  ? 3941 LEU A CD1   1 
ATOM   18222 C  CD2   . LEU A 1 3941 ? 194.837 127.811 169.577 1.00 60.91  ? 3941 LEU A CD2   1 
ATOM   18223 N  N     . PRO A 1 3942 ? 198.102 124.279 169.360 1.00 75.71  ? 3942 PRO A N     1 
ATOM   18224 C  CA    . PRO A 1 3942 ? 199.005 123.131 169.168 1.00 73.13  ? 3942 PRO A CA    1 
ATOM   18225 C  C     . PRO A 1 3942 ? 199.112 122.668 167.725 1.00 71.27  ? 3942 PRO A C     1 
ATOM   18226 O  O     . PRO A 1 3942 ? 200.179 122.196 167.316 1.00 71.62  ? 3942 PRO A O     1 
ATOM   18227 C  CB    . PRO A 1 3942 ? 198.387 122.047 170.063 1.00 71.51  ? 3942 PRO A CB    1 
ATOM   18228 C  CG    . PRO A 1 3942 ? 197.567 122.796 171.063 1.00 73.32  ? 3942 PRO A CG    1 
ATOM   18229 C  CD    . PRO A 1 3942 ? 197.038 123.992 170.336 1.00 72.25  ? 3942 PRO A CD    1 
ATOM   18230 N  N     . ALA A 1 3943 ? 198.039 122.784 166.940 1.00 66.73  ? 3943 ALA A N     1 
ATOM   18231 C  CA    . ALA A 1 3943 ? 198.063 122.283 165.571 1.00 67.45  ? 3943 ALA A CA    1 
ATOM   18232 C  C     . ALA A 1 3943 ? 198.848 123.184 164.626 1.00 67.30  ? 3943 ALA A C     1 
ATOM   18233 O  O     . ALA A 1 3943 ? 199.198 122.747 163.525 1.00 63.46  ? 3943 ALA A O     1 
ATOM   18234 C  CB    . ALA A 1 3943 ? 196.637 122.105 165.050 1.00 65.14  ? 3943 ALA A CB    1 
ATOM   18235 N  N     . PHE A 1 3944 ? 199.132 124.424 165.024 1.00 69.44  ? 3944 PHE A N     1 
ATOM   18236 C  CA    . PHE A 1 3944 ? 199.844 125.377 164.182 1.00 68.44  ? 3944 PHE A CA    1 
ATOM   18237 C  C     . PHE A 1 3944 ? 201.172 125.810 164.798 1.00 73.61  ? 3944 PHE A C     1 
ATOM   18238 O  O     . PHE A 1 3944 ? 201.652 126.914 164.533 1.00 74.02  ? 3944 PHE A O     1 
ATOM   18239 C  CB    . PHE A 1 3944 ? 198.970 126.597 163.898 1.00 64.68  ? 3944 PHE A CB    1 
ATOM   18240 C  CG    . PHE A 1 3944 ? 197.729 126.285 163.113 1.00 62.56  ? 3944 PHE A CG    1 
ATOM   18241 C  CD1   . PHE A 1 3944 ? 197.797 126.047 161.750 1.00 60.54  ? 3944 PHE A CD1   1 
ATOM   18242 C  CD2   . PHE A 1 3944 ? 196.494 126.231 163.737 1.00 63.37  ? 3944 PHE A CD2   1 
ATOM   18243 C  CE1   . PHE A 1 3944 ? 196.656 125.761 161.025 1.00 56.77  ? 3944 PHE A CE1   1 
ATOM   18244 C  CE2   . PHE A 1 3944 ? 195.350 125.945 163.017 1.00 52.23  ? 3944 PHE A CE2   1 
ATOM   18245 C  CZ    . PHE A 1 3944 ? 195.431 125.709 161.660 1.00 50.56  ? 3944 PHE A CZ    1 
ATOM   18246 N  N     . LYS A 1 3945 ? 201.776 124.949 165.621 1.00 77.41  ? 3945 LYS A N     1 
ATOM   18247 C  CA    . LYS A 1 3945 ? 203.032 125.308 166.273 1.00 77.76  ? 3945 LYS A CA    1 
ATOM   18248 C  C     . LYS A 1 3945 ? 204.142 125.538 165.254 1.00 77.47  ? 3945 LYS A C     1 
ATOM   18249 O  O     . LYS A 1 3945 ? 204.940 126.471 165.395 1.00 78.18  ? 3945 LYS A O     1 
ATOM   18250 C  CB    . LYS A 1 3945 ? 203.435 124.222 167.271 1.00 78.42  ? 3945 LYS A CB    1 
ATOM   18251 C  CG    . LYS A 1 3945 ? 203.304 122.805 166.739 1.00 76.29  ? 3945 LYS A CG    1 
ATOM   18252 C  CD    . LYS A 1 3945 ? 203.879 121.797 167.718 1.00 74.37  ? 3945 LYS A CD    1 
ATOM   18253 C  CE    . LYS A 1 3945 ? 205.393 121.908 167.794 1.00 69.49  ? 3945 LYS A CE    1 
ATOM   18254 N  NZ    . LYS A 1 3945 ? 206.055 121.276 166.621 1.00 71.51  ? 3945 LYS A NZ    1 
ATOM   18255 N  N     . ASP A 1 3946 ? 204.207 124.701 164.221 1.00 76.38  ? 3946 ASP A N     1 
ATOM   18256 C  CA    . ASP A 1 3946 ? 205.218 124.810 163.170 1.00 78.24  ? 3946 ASP A CA    1 
ATOM   18257 C  C     . ASP A 1 3946 ? 204.638 125.377 161.880 1.00 75.45  ? 3946 ASP A C     1 
ATOM   18258 O  O     . ASP A 1 3946 ? 205.017 124.961 160.781 1.00 74.42  ? 3946 ASP A O     1 
ATOM   18259 C  CB    . ASP A 1 3946 ? 205.866 123.451 162.919 1.00 82.57  ? 3946 ASP A CB    1 
ATOM   18260 C  CG    . ASP A 1 3946 ? 204.850 122.368 162.608 1.00 87.33  ? 3946 ASP A CG    1 
ATOM   18261 O  OD1   . ASP A 1 3946 ? 203.640 122.611 162.797 1.00 86.69  ? 3946 ASP A OD1   1 
ATOM   18262 O  OD2   . ASP A 1 3946 ? 205.264 121.272 162.174 1.00 87.70  ? 3946 ASP A OD2   1 
ATOM   18263 N  N     . LEU A 1 3947 ? 203.708 126.328 161.992 1.00 72.62  ? 3947 LEU A N     1 
ATOM   18264 C  CA    . LEU A 1 3947 ? 203.091 126.913 160.805 1.00 71.46  ? 3947 LEU A CA    1 
ATOM   18265 C  C     . LEU A 1 3947 ? 204.091 127.736 160.001 1.00 69.65  ? 3947 LEU A C     1 
ATOM   18266 O  O     . LEU A 1 3947 ? 204.074 127.705 158.765 1.00 71.41  ? 3947 LEU A O     1 
ATOM   18267 C  CB    . LEU A 1 3947 ? 201.892 127.770 161.208 1.00 68.48  ? 3947 LEU A CB    1 
ATOM   18268 C  CG    . LEU A 1 3947 ? 201.115 128.432 160.069 1.00 64.93  ? 3947 LEU A CG    1 
ATOM   18269 C  CD1   . LEU A 1 3947 ? 200.363 127.393 159.257 1.00 58.99  ? 3947 LEU A CD1   1 
ATOM   18270 C  CD2   . LEU A 1 3947 ? 200.163 129.486 160.610 1.00 62.27  ? 3947 LEU A CD2   1 
ATOM   18271 N  N     . ILE A 1 3948 ? 204.962 128.483 160.684 1.00 67.91  ? 3948 ILE A N     1 
ATOM   18272 C  CA    . ILE A 1 3948 ? 205.904 129.357 159.989 1.00 68.55  ? 3948 ILE A CA    1 
ATOM   18273 C  C     . ILE A 1 3948 ? 206.848 128.541 159.114 1.00 70.29  ? 3948 ILE A C     1 
ATOM   18274 O  O     . ILE A 1 3948 ? 207.126 128.907 157.965 1.00 70.73  ? 3948 ILE A O     1 
ATOM   18275 C  CB    . ILE A 1 3948 ? 206.676 130.223 161.002 1.00 69.30  ? 3948 ILE A CB    1 
ATOM   18276 C  CG1   . ILE A 1 3948 ? 205.707 131.074 161.825 1.00 65.27  ? 3948 ILE A CG1   1 
ATOM   18277 C  CG2   . ILE A 1 3948 ? 207.687 131.108 160.288 1.00 71.47  ? 3948 ILE A CG2   1 
ATOM   18278 C  CD1   . ILE A 1 3948 ? 205.510 130.577 163.239 1.00 58.93  ? 3948 ILE A CD1   1 
ATOM   18279 N  N     . ALA A 1 3949 ? 207.358 127.426 159.642 1.00 72.97  ? 3949 ALA A N     1 
ATOM   18280 C  CA    . ALA A 1 3949 ? 208.227 126.564 158.849 1.00 71.51  ? 3949 ALA A CA    1 
ATOM   18281 C  C     . ALA A 1 3949 ? 207.485 125.982 157.652 1.00 72.96  ? 3949 ALA A C     1 
ATOM   18282 O  O     . ALA A 1 3949 ? 208.037 125.901 156.549 1.00 73.08  ? 3949 ALA A O     1 
ATOM   18283 C  CB    . ALA A 1 3949 ? 208.799 125.448 159.722 1.00 66.68  ? 3949 ALA A CB    1 
ATOM   18284 N  N     . LYS A 1 3950 ? 206.232 125.564 157.854 1.00 69.84  ? 3950 LYS A N     1 
ATOM   18285 C  CA    . LYS A 1 3950 ? 205.443 125.026 156.750 1.00 72.34  ? 3950 LYS A CA    1 
ATOM   18286 C  C     . LYS A 1 3950 ? 205.191 126.083 155.682 1.00 70.12  ? 3950 LYS A C     1 
ATOM   18287 O  O     . LYS A 1 3950 ? 205.284 125.799 154.482 1.00 68.40  ? 3950 LYS A O     1 
ATOM   18288 C  CB    . LYS A 1 3950 ? 204.119 124.470 157.276 1.00 70.39  ? 3950 LYS A CB    1 
ATOM   18289 C  CG    . LYS A 1 3950 ? 204.098 122.959 157.441 1.00 66.25  ? 3950 LYS A CG    1 
ATOM   18290 C  CD    . LYS A 1 3950 ? 203.018 122.529 158.420 1.00 65.98  ? 3950 LYS A CD    1 
ATOM   18291 C  CE    . LYS A 1 3950 ? 202.545 121.112 158.138 1.00 63.87  ? 3950 LYS A CE    1 
ATOM   18292 N  NZ    . LYS A 1 3950 ? 203.117 120.132 159.101 1.00 69.23  ? 3950 LYS A NZ    1 
ATOM   18293 N  N     . VAL A 1 3951 ? 204.864 127.308 156.100 1.00 69.22  ? 3951 VAL A N     1 
ATOM   18294 C  CA    . VAL A 1 3951 ? 204.606 128.382 155.144 1.00 70.51  ? 3951 VAL A CA    1 
ATOM   18295 C  C     . VAL A 1 3951 ? 205.864 128.702 154.347 1.00 73.42  ? 3951 VAL A C     1 
ATOM   18296 O  O     . VAL A 1 3951 ? 205.818 128.866 153.121 1.00 72.73  ? 3951 VAL A O     1 
ATOM   18297 C  CB    . VAL A 1 3951 ? 204.064 129.626 155.874 1.00 70.11  ? 3951 VAL A CB    1 
ATOM   18298 C  CG1   . VAL A 1 3951 ? 204.204 130.866 155.003 1.00 66.23  ? 3951 VAL A CG1   1 
ATOM   18299 C  CG2   . VAL A 1 3951 ? 202.614 129.414 156.279 1.00 64.97  ? 3951 VAL A CG2   1 
ATOM   18300 N  N     . GLN A 1 3952 ? 207.009 128.792 155.029 1.00 73.53  ? 3952 GLN A N     1 
ATOM   18301 C  CA    . GLN A 1 3952 ? 208.259 129.114 154.349 1.00 70.33  ? 3952 GLN A CA    1 
ATOM   18302 C  C     . GLN A 1 3952 ? 208.696 128.001 153.405 1.00 68.23  ? 3952 GLN A C     1 
ATOM   18303 O  O     . GLN A 1 3952 ? 209.335 128.274 152.383 1.00 69.78  ? 3952 GLN A O     1 
ATOM   18304 C  CB    . GLN A 1 3952 ? 209.355 129.395 155.377 1.00 71.41  ? 3952 GLN A CB    1 
ATOM   18305 C  CG    . GLN A 1 3952 ? 209.186 130.707 156.123 1.00 76.90  ? 3952 GLN A CG    1 
ATOM   18306 C  CD    . GLN A 1 3952 ? 210.172 130.855 157.265 1.00 81.71  ? 3952 GLN A CD    1 
ATOM   18307 O  OE1   . GLN A 1 3952 ? 210.934 129.936 157.564 1.00 78.66  ? 3952 GLN A OE1   1 
ATOM   18308 N  NE2   . GLN A 1 3952 ? 210.161 132.015 157.911 1.00 79.74  ? 3952 GLN A NE2   1 
ATOM   18309 N  N     . ALA A 1 3953 ? 208.365 126.750 153.725 1.00 70.88  ? 3953 ALA A N     1 
ATOM   18310 C  CA    . ALA A 1 3953 ? 208.801 125.616 152.922 1.00 71.17  ? 3953 ALA A CA    1 
ATOM   18311 C  C     . ALA A 1 3953 ? 207.920 125.364 151.706 1.00 74.88  ? 3953 ALA A C     1 
ATOM   18312 O  O     . ALA A 1 3953 ? 208.230 124.466 150.915 1.00 75.93  ? 3953 ALA A O     1 
ATOM   18313 C  CB    . ALA A 1 3953 ? 208.853 124.351 153.783 1.00 69.89  ? 3953 ALA A CB    1 
ATOM   18314 N  N     . ASP A 1 3954 ? 206.839 126.121 151.534 1.00 75.75  ? 3954 ASP A N     1 
ATOM   18315 C  CA    . ASP A 1 3954 ? 205.925 125.938 150.413 1.00 77.89  ? 3954 ASP A CA    1 
ATOM   18316 C  C     . ASP A 1 3954 ? 206.213 126.989 149.348 1.00 81.88  ? 3954 ASP A C     1 
ATOM   18317 O  O     . ASP A 1 3954 ? 206.039 128.188 149.590 1.00 79.39  ? 3954 ASP A O     1 
ATOM   18318 C  CB    . ASP A 1 3954 ? 204.471 126.031 150.876 1.00 77.32  ? 3954 ASP A CB    1 
ATOM   18319 C  CG    . ASP A 1 3954 ? 203.916 124.695 151.324 1.00 82.13  ? 3954 ASP A CG    1 
ATOM   18320 O  OD1   . ASP A 1 3954 ? 204.330 123.658 150.764 1.00 80.28  ? 3954 ASP A OD1   1 
ATOM   18321 O  OD2   . ASP A 1 3954 ? 203.062 124.681 152.236 1.00 82.30  ? 3954 ASP A OD2   1 
ATOM   18322 N  N     . GLU A 1 3955 ? 206.652 126.535 148.172 1.00 87.43  ? 3955 GLU A N     1 
ATOM   18323 C  CA    . GLU A 1 3955 ? 206.875 127.449 147.057 1.00 90.41  ? 3955 GLU A CA    1 
ATOM   18324 C  C     . GLU A 1 3955 ? 205.567 127.885 146.409 1.00 85.41  ? 3955 GLU A C     1 
ATOM   18325 O  O     . GLU A 1 3955 ? 205.484 129.001 145.883 1.00 80.52  ? 3955 GLU A O     1 
ATOM   18326 C  CB    . GLU A 1 3955 ? 207.790 126.801 146.016 1.00 90.95  ? 3955 GLU A CB    1 
ATOM   18327 C  CG    . GLU A 1 3955 ? 207.318 125.441 145.526 1.00 90.68  ? 3955 GLU A CG    1 
ATOM   18328 C  CD    . GLU A 1 3955 ? 207.908 124.297 146.327 1.00 92.08  ? 3955 GLU A CD    1 
ATOM   18329 O  OE1   . GLU A 1 3955 ? 208.709 124.564 147.247 1.00 90.26  ? 3955 GLU A OE1   1 
ATOM   18330 O  OE2   . GLU A 1 3955 ? 207.570 123.130 146.036 1.00 93.26  ? 3955 GLU A OE2   1 
ATOM   18331 N  N     . GLN A 1 3956 ? 204.546 127.031 146.436 1.00 84.06  ? 3956 GLN A N     1 
ATOM   18332 C  CA    . GLN A 1 3956 ? 203.243 127.361 145.875 1.00 81.66  ? 3956 GLN A CA    1 
ATOM   18333 C  C     . GLN A 1 3956 ? 202.363 128.142 146.841 1.00 71.84  ? 3956 GLN A C     1 
ATOM   18334 O  O     . GLN A 1 3956 ? 201.222 128.463 146.490 1.00 63.08  ? 3956 GLN A O     1 
ATOM   18335 C  CB    . GLN A 1 3956 ? 202.518 126.084 145.439 1.00 82.47  ? 3956 GLN A CB    1 
ATOM   18336 C  CG    . GLN A 1 3956 ? 202.770 125.687 143.995 1.00 83.10  ? 3956 GLN A CG    1 
ATOM   18337 C  CD    . GLN A 1 3956 ? 204.148 125.093 143.785 1.00 85.86  ? 3956 GLN A CD    1 
ATOM   18338 O  OE1   . GLN A 1 3956 ? 204.504 124.088 144.400 1.00 85.40  ? 3956 GLN A OE1   1 
ATOM   18339 N  NE2   . GLN A 1 3956 ? 204.934 125.716 142.915 1.00 85.48  ? 3956 GLN A NE2   1 
ATOM   18340 N  N     . PHE A 1 3957 ? 202.859 128.443 148.044 1.00 71.02  ? 3957 PHE A N     1 
ATOM   18341 C  CA    . PHE A 1 3957 ? 202.064 129.196 149.009 1.00 63.56  ? 3957 PHE A CA    1 
ATOM   18342 C  C     . PHE A 1 3957 ? 201.722 130.586 148.487 1.00 62.54  ? 3957 PHE A C     1 
ATOM   18343 O  O     . PHE A 1 3957 ? 200.601 131.071 148.681 1.00 64.44  ? 3957 PHE A O     1 
ATOM   18344 C  CB    . PHE A 1 3957 ? 202.807 129.294 150.339 1.00 62.87  ? 3957 PHE A CB    1 
ATOM   18345 C  CG    . PHE A 1 3957 ? 202.012 129.961 151.421 1.00 61.90  ? 3957 PHE A CG    1 
ATOM   18346 C  CD1   . PHE A 1 3957 ? 200.997 129.283 152.072 1.00 60.73  ? 3957 PHE A CD1   1 
ATOM   18347 C  CD2   . PHE A 1 3957 ? 202.273 131.272 151.778 1.00 57.22  ? 3957 PHE A CD2   1 
ATOM   18348 C  CE1   . PHE A 1 3957 ? 200.261 129.899 153.063 1.00 58.41  ? 3957 PHE A CE1   1 
ATOM   18349 C  CE2   . PHE A 1 3957 ? 201.539 131.891 152.768 1.00 57.79  ? 3957 PHE A CE2   1 
ATOM   18350 C  CZ    . PHE A 1 3957 ? 200.534 131.204 153.411 1.00 57.38  ? 3957 PHE A CZ    1 
ATOM   18351 N  N     . GLY A 1 3958 ? 202.679 131.247 147.833 1.00 60.50  ? 3958 GLY A N     1 
ATOM   18352 C  CA    . GLY A 1 3958 ? 202.412 132.565 147.283 1.00 56.27  ? 3958 GLY A CA    1 
ATOM   18353 C  C     . GLY A 1 3958 ? 201.343 132.557 146.210 1.00 54.87  ? 3958 GLY A C     1 
ATOM   18354 O  O     . GLY A 1 3958 ? 200.587 133.524 146.073 1.00 50.74  ? 3958 GLY A O     1 
ATOM   18355 N  N     . ILE A 1 3959 ? 201.268 131.478 145.429 1.00 55.56  ? 3959 ILE A N     1 
ATOM   18356 C  CA    . ILE A 1 3959 ? 200.237 131.366 144.401 1.00 55.48  ? 3959 ILE A CA    1 
ATOM   18357 C  C     . ILE A 1 3959 ? 198.854 131.311 145.040 1.00 55.90  ? 3959 ILE A C     1 
ATOM   18358 O  O     . ILE A 1 3959 ? 197.912 131.972 144.587 1.00 52.66  ? 3959 ILE A O     1 
ATOM   18359 C  CB    . ILE A 1 3959 ? 200.498 130.138 143.511 1.00 56.46  ? 3959 ILE A CB    1 
ATOM   18360 C  CG1   . ILE A 1 3959 ? 201.923 130.175 142.956 1.00 56.16  ? 3959 ILE A CG1   1 
ATOM   18361 C  CG2   . ILE A 1 3959 ? 199.481 130.068 142.383 1.00 49.06  ? 3959 ILE A CG2   1 
ATOM   18362 C  CD1   . ILE A 1 3959 ? 202.225 131.406 142.130 1.00 53.62  ? 3959 ILE A CD1   1 
ATOM   18363 N  N     . TRP A 1 3960 ? 198.713 130.515 146.103 1.00 55.04  ? 3960 TRP A N     1 
ATOM   18364 C  CA    . TRP A 1 3960 ? 197.427 130.406 146.785 1.00 47.11  ? 3960 TRP A CA    1 
ATOM   18365 C  C     . TRP A 1 3960 ? 197.053 131.710 147.479 1.00 46.58  ? 3960 TRP A C     1 
ATOM   18366 O  O     . TRP A 1 3960 ? 195.873 132.077 147.527 1.00 49.33  ? 3960 TRP A O     1 
ATOM   18367 C  CB    . TRP A 1 3960 ? 197.463 129.253 147.789 1.00 48.60  ? 3960 TRP A CB    1 
ATOM   18368 C  CG    . TRP A 1 3960 ? 196.293 129.233 148.724 1.00 45.86  ? 3960 TRP A CG    1 
ATOM   18369 C  CD1   . TRP A 1 3960 ? 195.057 128.708 148.480 1.00 44.00  ? 3960 TRP A CD1   1 
ATOM   18370 C  CD2   . TRP A 1 3960 ? 196.250 129.758 150.056 1.00 45.09  ? 3960 TRP A CD2   1 
ATOM   18371 N  NE1   . TRP A 1 3960 ? 194.247 128.876 149.577 1.00 42.57  ? 3960 TRP A NE1   1 
ATOM   18372 C  CE2   . TRP A 1 3960 ? 194.955 129.520 150.557 1.00 42.17  ? 3960 TRP A CE2   1 
ATOM   18373 C  CE3   . TRP A 1 3960 ? 197.180 130.409 150.872 1.00 46.93  ? 3960 TRP A CE3   1 
ATOM   18374 C  CZ2   . TRP A 1 3960 ? 194.568 129.906 151.838 1.00 45.46  ? 3960 TRP A CZ2   1 
ATOM   18375 C  CZ3   . TRP A 1 3960 ? 196.794 130.793 152.142 1.00 42.26  ? 3960 TRP A CZ3   1 
ATOM   18376 C  CH2   . TRP A 1 3960 ? 195.499 130.540 152.613 1.00 44.00  ? 3960 TRP A CH2   1 
ATOM   18377 N  N     . LEU A 1 3961 ? 198.042 132.420 148.027 1.00 47.42  ? 3961 LEU A N     1 
ATOM   18378 C  CA    . LEU A 1 3961 ? 197.764 133.654 148.754 1.00 46.53  ? 3961 LEU A CA    1 
ATOM   18379 C  C     . LEU A 1 3961 ? 197.174 134.738 147.862 1.00 45.84  ? 3961 LEU A C     1 
ATOM   18380 O  O     . LEU A 1 3961 ? 196.492 135.636 148.368 1.00 45.03  ? 3961 LEU A O     1 
ATOM   18381 C  CB    . LEU A 1 3961 ? 199.041 134.168 149.421 1.00 44.61  ? 3961 LEU A CB    1 
ATOM   18382 C  CG    . LEU A 1 3961 ? 198.855 134.979 150.704 1.00 47.66  ? 3961 LEU A CG    1 
ATOM   18383 C  CD1   . LEU A 1 3961 ? 198.119 134.159 151.750 1.00 51.76  ? 3961 LEU A CD1   1 
ATOM   18384 C  CD2   . LEU A 1 3961 ? 200.197 135.456 151.238 1.00 52.14  ? 3961 LEU A CD2   1 
ATOM   18385 N  N     . ASP A 1 3962 ? 197.418 134.680 146.554 1.00 51.57  ? 3962 ASP A N     1 
ATOM   18386 C  CA    . ASP A 1 3962 ? 196.882 135.656 145.615 1.00 52.18  ? 3962 ASP A CA    1 
ATOM   18387 C  C     . ASP A 1 3962 ? 195.726 135.103 144.791 1.00 50.92  ? 3962 ASP A C     1 
ATOM   18388 O  O     . ASP A 1 3962 ? 195.293 135.755 143.835 1.00 50.85  ? 3962 ASP A O     1 
ATOM   18389 C  CB    . ASP A 1 3962 ? 197.990 136.165 144.691 1.00 55.05  ? 3962 ASP A CB    1 
ATOM   18390 C  CG    . ASP A 1 3962 ? 199.057 136.941 145.435 1.00 62.69  ? 3962 ASP A CG    1 
ATOM   18391 O  OD1   . ASP A 1 3962 ? 200.183 136.420 145.577 1.00 64.88  ? 3962 ASP A OD1   1 
ATOM   18392 O  OD2   . ASP A 1 3962 ? 198.769 138.072 145.880 1.00 69.57  ? 3962 ASP A OD2   1 
ATOM   18393 N  N     . SER A 1 3963 ? 195.221 133.922 145.132 1.00 50.54  ? 3963 SER A N     1 
ATOM   18394 C  CA    . SER A 1 3963 ? 194.113 133.339 144.391 1.00 49.69  ? 3963 SER A CA    1 
ATOM   18395 C  C     . SER A 1 3963 ? 192.829 134.124 144.630 1.00 49.48  ? 3963 SER A C     1 
ATOM   18396 O  O     . SER A 1 3963 ? 192.633 134.736 145.684 1.00 47.40  ? 3963 SER A O     1 
ATOM   18397 C  CB    . SER A 1 3963 ? 193.914 131.876 144.788 1.00 47.48  ? 3963 SER A CB    1 
ATOM   18398 O  OG    . SER A 1 3963 ? 192.781 131.324 144.142 1.00 50.68  ? 3963 SER A OG    1 
ATOM   18399 N  N     . SER A 1 3964 ? 191.949 134.107 143.626 1.00 48.40  ? 3964 SER A N     1 
ATOM   18400 C  CA    . SER A 1 3964 ? 190.681 134.820 143.738 1.00 45.10  ? 3964 SER A CA    1 
ATOM   18401 C  C     . SER A 1 3964 ? 189.803 134.228 144.834 1.00 49.27  ? 3964 SER A C     1 
ATOM   18402 O  O     . SER A 1 3964 ? 189.175 134.968 145.600 1.00 46.21  ? 3964 SER A O     1 
ATOM   18403 C  CB    . SER A 1 3964 ? 189.949 134.802 142.396 1.00 43.42  ? 3964 SER A CB    1 
ATOM   18404 O  OG    . SER A 1 3964 ? 189.743 133.475 141.946 1.00 47.28  ? 3964 SER A OG    1 
ATOM   18405 N  N     . SER A 1 3965 ? 189.746 132.900 144.925 1.00 46.04  ? 3965 SER A N     1 
ATOM   18406 C  CA    . SER A 1 3965 ? 188.941 132.200 145.925 1.00 39.50  ? 3965 SER A CA    1 
ATOM   18407 C  C     . SER A 1 3965 ? 189.828 131.190 146.639 1.00 38.40  ? 3965 SER A C     1 
ATOM   18408 O  O     . SER A 1 3965 ? 189.746 129.980 146.385 1.00 42.28  ? 3965 SER A O     1 
ATOM   18409 C  CB    . SER A 1 3965 ? 187.727 131.524 145.284 1.00 42.24  ? 3965 SER A CB    1 
ATOM   18410 O  OG    . SER A 1 3965 ? 188.022 130.188 144.916 1.00 54.23  ? 3965 SER A OG    1 
ATOM   18411 N  N     . PRO A 1 3966 ? 190.699 131.655 147.539 1.00 36.26  ? 3966 PRO A N     1 
ATOM   18412 C  CA    . PRO A 1 3966 ? 191.595 130.720 148.239 1.00 39.40  ? 3966 PRO A CA    1 
ATOM   18413 C  C     . PRO A 1 3966 ? 190.869 129.715 149.115 1.00 45.92  ? 3966 PRO A C     1 
ATOM   18414 O  O     . PRO A 1 3966 ? 191.422 128.644 149.396 1.00 52.34  ? 3966 PRO A O     1 
ATOM   18415 C  CB    . PRO A 1 3966 ? 192.486 131.651 149.074 1.00 38.63  ? 3966 PRO A CB    1 
ATOM   18416 C  CG    . PRO A 1 3966 ? 191.695 132.901 149.222 1.00 32.93  ? 3966 PRO A CG    1 
ATOM   18417 C  CD    . PRO A 1 3966 ? 190.922 133.049 147.953 1.00 36.38  ? 3966 PRO A CD    1 
ATOM   18418 N  N     . GLU A 1 3967 ? 189.649 130.025 149.561 1.00 41.71  ? 3967 GLU A N     1 
ATOM   18419 C  CA    . GLU A 1 3967 ? 188.943 129.140 150.481 1.00 37.70  ? 3967 GLU A CA    1 
ATOM   18420 C  C     . GLU A 1 3967 ? 188.580 127.804 149.844 1.00 44.41  ? 3967 GLU A C     1 
ATOM   18421 O  O     . GLU A 1 3967 ? 188.324 126.836 150.568 1.00 50.89  ? 3967 GLU A O     1 
ATOM   18422 C  CB    . GLU A 1 3967 ? 187.683 129.829 151.011 1.00 34.73  ? 3967 GLU A CB    1 
ATOM   18423 C  CG    . GLU A 1 3967 ? 186.446 129.630 150.152 1.00 42.46  ? 3967 GLU A CG    1 
ATOM   18424 C  CD    . GLU A 1 3967 ? 186.387 130.590 148.980 1.00 49.43  ? 3967 GLU A CD    1 
ATOM   18425 O  OE1   . GLU A 1 3967 ? 187.163 131.568 148.971 1.00 45.41  ? 3967 GLU A OE1   1 
ATOM   18426 O  OE2   . GLU A 1 3967 ? 185.564 130.365 148.067 1.00 48.66  ? 3967 GLU A OE2   1 
ATOM   18427 N  N     . GLN A 1 3968 ? 188.550 127.727 148.513 1.00 43.61  ? 3968 GLN A N     1 
ATOM   18428 C  CA    . GLN A 1 3968 ? 188.222 126.465 147.858 1.00 48.17  ? 3968 GLN A CA    1 
ATOM   18429 C  C     . GLN A 1 3968 ? 189.384 125.481 147.934 1.00 53.64  ? 3968 GLN A C     1 
ATOM   18430 O  O     . GLN A 1 3968 ? 189.171 124.268 148.043 1.00 58.09  ? 3968 GLN A O     1 
ATOM   18431 C  CB    . GLN A 1 3968 ? 187.824 126.716 146.402 1.00 44.45  ? 3968 GLN A CB    1 
ATOM   18432 C  CG    . GLN A 1 3968 ? 186.376 127.180 146.168 1.00 50.46  ? 3968 GLN A CG    1 
ATOM   18433 C  CD    . GLN A 1 3968 ? 185.290 126.204 146.631 1.00 63.25  ? 3968 GLN A CD    1 
ATOM   18434 O  OE1   . GLN A 1 3968 ? 185.604 125.129 147.142 1.00 62.78  ? 3968 GLN A OE1   1 
ATOM   18435 N  NE2   . GLN A 1 3968 ? 184.024 126.593 146.512 1.00 62.62  ? 3968 GLN A NE2   1 
ATOM   18436 N  N     . THR A 1 3969 ? 190.615 125.981 147.877 1.00 52.53  ? 3969 THR A N     1 
ATOM   18437 C  CA    . THR A 1 3969 ? 191.817 125.155 147.804 1.00 52.91  ? 3969 THR A CA    1 
ATOM   18438 C  C     . THR A 1 3969 ? 192.791 125.524 148.915 1.00 49.92  ? 3969 THR A C     1 
ATOM   18439 O  O     . THR A 1 3969 ? 193.977 125.764 148.681 1.00 51.75  ? 3969 THR A O     1 
ATOM   18440 C  CB    . THR A 1 3969 ? 192.498 125.284 146.442 1.00 59.62  ? 3969 THR A CB    1 
ATOM   18441 O  OG1   . THR A 1 3969 ? 193.172 126.546 146.360 1.00 62.68  ? 3969 THR A OG1   1 
ATOM   18442 C  CG2   . THR A 1 3969 ? 191.479 125.182 145.315 1.00 51.80  ? 3969 THR A CG2   1 
ATOM   18443 N  N     . VAL A 1 3970 ? 192.293 125.589 150.147 1.00 55.20  ? 3970 VAL A N     1 
ATOM   18444 C  CA    . VAL A 1 3970 ? 193.174 125.910 151.277 1.00 51.01  ? 3970 VAL A CA    1 
ATOM   18445 C  C     . VAL A 1 3970 ? 194.197 124.793 151.450 1.00 51.75  ? 3970 VAL A C     1 
ATOM   18446 O  O     . VAL A 1 3970 ? 193.813 123.614 151.578 1.00 50.84  ? 3970 VAL A O     1 
ATOM   18447 C  CB    . VAL A 1 3970 ? 192.358 126.107 152.564 1.00 44.74  ? 3970 VAL A CB    1 
ATOM   18448 C  CG1   . VAL A 1 3970 ? 193.284 126.368 153.743 1.00 43.76  ? 3970 VAL A CG1   1 
ATOM   18449 C  CG2   . VAL A 1 3970 ? 191.371 127.248 152.397 1.00 45.14  ? 3970 VAL A CG2   1 
ATOM   18450 N  N     . PRO A 1 3971 ? 195.492 125.094 151.458 1.00 49.46  ? 3971 PRO A N     1 
ATOM   18451 C  CA    . PRO A 1 3971 ? 196.495 124.034 151.585 1.00 52.46  ? 3971 PRO A CA    1 
ATOM   18452 C  C     . PRO A 1 3971 ? 196.583 123.499 153.006 1.00 57.43  ? 3971 PRO A C     1 
ATOM   18453 O  O     . PRO A 1 3971 ? 196.113 124.117 153.964 1.00 60.39  ? 3971 PRO A O     1 
ATOM   18454 C  CB    . PRO A 1 3971 ? 197.795 124.728 151.168 1.00 49.76  ? 3971 PRO A CB    1 
ATOM   18455 C  CG    . PRO A 1 3971 ? 197.558 126.164 151.474 1.00 46.14  ? 3971 PRO A CG    1 
ATOM   18456 C  CD    . PRO A 1 3971 ? 196.105 126.407 151.200 1.00 47.17  ? 3971 PRO A CD    1 
ATOM   18457 N  N     . TYR A 1 3972 ? 197.206 122.326 153.127 1.00 54.94  ? 3972 TYR A N     1 
ATOM   18458 C  CA    . TYR A 1 3972 ? 197.275 121.574 154.380 1.00 54.73  ? 3972 TYR A CA    1 
ATOM   18459 C  C     . TYR A 1 3972 ? 198.509 122.004 155.172 1.00 57.37  ? 3972 TYR A C     1 
ATOM   18460 O  O     . TYR A 1 3972 ? 199.597 121.434 155.057 1.00 60.20  ? 3972 TYR A O     1 
ATOM   18461 C  CB    . TYR A 1 3972 ? 197.296 120.082 154.070 1.00 59.41  ? 3972 TYR A CB    1 
ATOM   18462 C  CG    . TYR A 1 3972 ? 197.282 119.174 155.274 1.00 61.69  ? 3972 TYR A CG    1 
ATOM   18463 C  CD1   . TYR A 1 3972 ? 196.171 119.103 156.102 1.00 59.45  ? 3972 TYR A CD1   1 
ATOM   18464 C  CD2   . TYR A 1 3972 ? 198.373 118.370 155.570 1.00 63.44  ? 3972 TYR A CD2   1 
ATOM   18465 C  CE1   . TYR A 1 3972 ? 196.154 118.264 157.198 1.00 63.92  ? 3972 TYR A CE1   1 
ATOM   18466 C  CE2   . TYR A 1 3972 ? 198.365 117.531 156.662 1.00 66.74  ? 3972 TYR A CE2   1 
ATOM   18467 C  CZ    . TYR A 1 3972 ? 197.254 117.481 157.472 1.00 70.16  ? 3972 TYR A CZ    1 
ATOM   18468 O  OH    . TYR A 1 3972 ? 197.250 116.642 158.560 1.00 70.70  ? 3972 TYR A OH    1 
ATOM   18469 N  N     . LEU A 1 3973 ? 198.333 123.039 155.999 1.00 54.41  ? 3973 LEU A N     1 
ATOM   18470 C  CA    . LEU A 1 3973 ? 199.412 123.584 156.819 1.00 61.10  ? 3973 LEU A CA    1 
ATOM   18471 C  C     . LEU A 1 3973 ? 199.194 123.367 158.314 1.00 63.29  ? 3973 LEU A C     1 
ATOM   18472 O  O     . LEU A 1 3973 ? 199.644 124.183 159.123 1.00 67.00  ? 3973 LEU A O     1 
ATOM   18473 C  CB    . LEU A 1 3973 ? 199.618 125.076 156.545 1.00 57.27  ? 3973 LEU A CB    1 
ATOM   18474 C  CG    . LEU A 1 3973 ? 200.246 125.627 155.257 1.00 63.84  ? 3973 LEU A CG    1 
ATOM   18475 C  CD1   . LEU A 1 3973 ? 199.814 124.907 153.999 1.00 59.42  ? 3973 LEU A CD1   1 
ATOM   18476 C  CD2   . LEU A 1 3973 ? 199.954 127.115 155.142 1.00 59.98  ? 3973 LEU A CD2   1 
ATOM   18477 N  N     . TRP A 1 3974 ? 198.519 122.290 158.703 1.00 59.29  ? 3974 TRP A N     1 
ATOM   18478 C  CA    . TRP A 1 3974 ? 198.362 121.963 160.111 1.00 62.17  ? 3974 TRP A CA    1 
ATOM   18479 C  C     . TRP A 1 3974 ? 198.715 120.500 160.333 1.00 66.99  ? 3974 TRP A C     1 
ATOM   18480 O  O     . TRP A 1 3974 ? 198.476 119.642 159.479 1.00 66.71  ? 3974 TRP A O     1 
ATOM   18481 C  CB    . TRP A 1 3974 ? 196.940 122.269 160.609 1.00 59.04  ? 3974 TRP A CB    1 
ATOM   18482 C  CG    . TRP A 1 3974 ? 195.909 121.254 160.233 1.00 61.06  ? 3974 TRP A CG    1 
ATOM   18483 C  CD1   . TRP A 1 3974 ? 195.616 120.099 160.897 1.00 64.10  ? 3974 TRP A CD1   1 
ATOM   18484 C  CD2   . TRP A 1 3974 ? 195.023 121.307 159.109 1.00 59.28  ? 3974 TRP A CD2   1 
ATOM   18485 N  NE1   . TRP A 1 3974 ? 194.607 119.427 160.254 1.00 63.72  ? 3974 TRP A NE1   1 
ATOM   18486 C  CE2   . TRP A 1 3974 ? 194.224 120.148 159.154 1.00 62.03  ? 3974 TRP A CE2   1 
ATOM   18487 C  CE3   . TRP A 1 3974 ? 194.828 122.220 158.068 1.00 52.83  ? 3974 TRP A CE3   1 
ATOM   18488 C  CZ2   . TRP A 1 3974 ? 193.247 119.876 158.198 1.00 58.06  ? 3974 TRP A CZ2   1 
ATOM   18489 C  CZ3   . TRP A 1 3974 ? 193.857 121.949 157.121 1.00 53.07  ? 3974 TRP A CZ3   1 
ATOM   18490 C  CH2   . TRP A 1 3974 ? 193.079 120.787 157.192 1.00 53.69  ? 3974 TRP A CH2   1 
ATOM   18491 N  N     . SER A 1 3975 ? 199.291 120.224 161.499 1.00 64.60  ? 3975 SER A N     1 
ATOM   18492 C  CA    . SER A 1 3975 ? 199.782 118.897 161.843 1.00 66.22  ? 3975 SER A CA    1 
ATOM   18493 C  C     . SER A 1 3975 ? 198.838 118.242 162.840 1.00 68.36  ? 3975 SER A C     1 
ATOM   18494 O  O     . SER A 1 3975 ? 198.508 118.834 163.873 1.00 66.50  ? 3975 SER A O     1 
ATOM   18495 C  CB    . SER A 1 3975 ? 201.196 118.971 162.424 1.00 67.25  ? 3975 SER A CB    1 
ATOM   18496 O  OG    . SER A 1 3975 ? 202.172 118.769 161.417 1.00 69.04  ? 3975 SER A OG    1 
ATOM   18497 N  N     . GLU A 1 3976 ? 198.412 117.021 162.528 1.00 73.20  ? 3976 GLU A N     1 
ATOM   18498 C  CA    . GLU A 1 3976 ? 197.532 116.246 163.389 1.00 74.15  ? 3976 GLU A CA    1 
ATOM   18499 C  C     . GLU A 1 3976 ? 198.094 114.844 163.559 1.00 80.84  ? 3976 GLU A C     1 
ATOM   18500 O  O     . GLU A 1 3976 ? 198.594 114.245 162.602 1.00 74.87  ? 3976 GLU A O     1 
ATOM   18501 C  CB    . GLU A 1 3976 ? 196.111 116.176 162.816 1.00 73.78  ? 3976 GLU A CB    1 
ATOM   18502 C  CG    . GLU A 1 3976 ? 196.052 115.764 161.353 1.00 75.32  ? 3976 GLU A CG    1 
ATOM   18503 C  CD    . GLU A 1 3976 ? 194.750 116.158 160.684 1.00 75.98  ? 3976 GLU A CD    1 
ATOM   18504 O  OE1   . GLU A 1 3976 ? 194.278 117.289 160.917 1.00 76.53  ? 3976 GLU A OE1   1 
ATOM   18505 O  OE2   . GLU A 1 3976 ? 194.203 115.339 159.916 1.00 67.24  ? 3976 GLU A OE2   1 
ATOM   18506 N  N     . GLU A 1 3977 ? 198.017 114.327 164.787 1.00 85.97  ? 3977 GLU A N     1 
ATOM   18507 C  CA    . GLU A 1 3977 ? 198.455 112.958 165.036 1.00 89.01  ? 3977 GLU A CA    1 
ATOM   18508 C  C     . GLU A 1 3977 ? 197.503 111.947 164.411 1.00 86.92  ? 3977 GLU A C     1 
ATOM   18509 O  O     . GLU A 1 3977 ? 197.931 110.858 164.011 1.00 85.42  ? 3977 GLU A O     1 
ATOM   18510 C  CB    . GLU A 1 3977 ? 198.587 112.711 166.540 1.00 87.31  ? 3977 GLU A CB    1 
ATOM   18511 C  CG    . GLU A 1 3977 ? 199.697 113.508 167.211 1.00 91.60  ? 3977 GLU A CG    1 
ATOM   18512 C  CD    . GLU A 1 3977 ? 199.290 114.935 167.531 1.00 95.25  ? 3977 GLU A CD    1 
ATOM   18513 O  OE1   . GLU A 1 3977 ? 198.118 115.291 167.288 1.00 90.57  ? 3977 GLU A OE1   1 
ATOM   18514 O  OE2   . GLU A 1 3977 ? 200.145 115.700 168.026 1.00 96.02  ? 3977 GLU A OE2   1 
ATOM   18515 N  N     . THR A 1 3978 ? 196.222 112.285 164.319 1.00 86.75  ? 3978 THR A N     1 
ATOM   18516 C  CA    . THR A 1 3978 ? 195.211 111.446 163.701 1.00 84.82  ? 3978 THR A CA    1 
ATOM   18517 C  C     . THR A 1 3978 ? 194.447 112.254 162.664 1.00 82.94  ? 3978 THR A C     1 
ATOM   18518 O  O     . THR A 1 3978 ? 194.301 113.473 162.808 1.00 78.62  ? 3978 THR A O     1 
ATOM   18519 C  CB    . THR A 1 3978 ? 194.236 110.889 164.751 1.00 82.61  ? 3978 THR A CB    1 
ATOM   18520 O  OG1   . THR A 1 3978 ? 193.199 110.139 164.106 1.00 81.62  ? 3978 THR A OG1   1 
ATOM   18521 C  CG2   . THR A 1 3978 ? 193.615 112.018 165.564 1.00 81.34  ? 3978 THR A CG2   1 
ATOM   18522 N  N     . PRO A 1 3979 ? 193.967 111.609 161.599 1.00 83.87  ? 3979 PRO A N     1 
ATOM   18523 C  CA    . PRO A 1 3979 ? 193.204 112.341 160.581 1.00 79.02  ? 3979 PRO A CA    1 
ATOM   18524 C  C     . PRO A 1 3979 ? 191.986 113.027 161.181 1.00 76.73  ? 3979 PRO A C     1 
ATOM   18525 O  O     . PRO A 1 3979 ? 191.316 112.489 162.066 1.00 73.52  ? 3979 PRO A O     1 
ATOM   18526 C  CB    . PRO A 1 3979 ? 192.803 111.246 159.588 1.00 70.97  ? 3979 PRO A CB    1 
ATOM   18527 C  CG    . PRO A 1 3979 ? 193.876 110.224 159.720 1.00 74.42  ? 3979 PRO A CG    1 
ATOM   18528 C  CD    . PRO A 1 3979 ? 194.287 110.237 161.168 1.00 79.12  ? 3979 PRO A CD    1 
ATOM   18529 N  N     . ALA A 1 3980 ? 191.707 114.230 160.690 1.00 72.94  ? 3980 ALA A N     1 
ATOM   18530 C  CA    . ALA A 1 3980 ? 190.619 115.042 161.209 1.00 60.50  ? 3980 ALA A CA    1 
ATOM   18531 C  C     . ALA A 1 3980 ? 189.367 114.875 160.358 1.00 56.52  ? 3980 ALA A C     1 
ATOM   18532 O  O     . ALA A 1 3980 ? 189.436 114.635 159.150 1.00 58.24  ? 3980 ALA A O     1 
ATOM   18533 C  CB    . ALA A 1 3980 ? 191.021 116.517 161.260 1.00 55.56  ? 3980 ALA A CB    1 
ATOM   18534 N  N     . THR A 1 3981 ? 188.216 115.008 161.011 1.00 54.73  ? 3981 THR A N     1 
ATOM   18535 C  CA    . THR A 1 3981 ? 186.938 114.884 160.337 1.00 53.53  ? 3981 THR A CA    1 
ATOM   18536 C  C     . THR A 1 3981 ? 186.712 116.074 159.404 1.00 52.26  ? 3981 THR A C     1 
ATOM   18537 O  O     . THR A 1 3981 ? 187.358 117.115 159.547 1.00 51.15  ? 3981 THR A O     1 
ATOM   18538 C  CB    . THR A 1 3981 ? 185.812 114.792 161.364 1.00 54.89  ? 3981 THR A CB    1 
ATOM   18539 O  OG1   . THR A 1 3981 ? 186.117 115.633 162.484 1.00 52.22  ? 3981 THR A OG1   1 
ATOM   18540 C  CG2   . THR A 1 3981 ? 185.653 113.357 161.843 1.00 56.09  ? 3981 THR A CG2   1 
ATOM   18541 N  N     . PRO A 1 3982 ? 185.812 115.934 158.424 1.00 52.93  ? 3982 PRO A N     1 
ATOM   18542 C  CA    . PRO A 1 3982 ? 185.548 117.062 157.513 1.00 50.47  ? 3982 PRO A CA    1 
ATOM   18543 C  C     . PRO A 1 3982 ? 185.134 118.337 158.225 1.00 42.24  ? 3982 PRO A C     1 
ATOM   18544 O  O     . PRO A 1 3982 ? 185.485 119.430 157.764 1.00 39.19  ? 3982 PRO A O     1 
ATOM   18545 C  CB    . PRO A 1 3982 ? 184.422 116.532 156.608 1.00 42.21  ? 3982 PRO A CB    1 
ATOM   18546 C  CG    . PRO A 1 3982 ? 183.983 115.223 157.211 1.00 39.72  ? 3982 PRO A CG    1 
ATOM   18547 C  CD    . PRO A 1 3982 ? 185.152 114.701 157.968 1.00 44.97  ? 3982 PRO A CD    1 
ATOM   18548 N  N     . ILE A 1 3983 ? 184.391 118.236 159.330 1.00 41.17  ? 3983 ILE A N     1 
ATOM   18549 C  CA    . ILE A 1 3983 ? 184.070 119.427 160.110 1.00 38.61  ? 3983 ILE A CA    1 
ATOM   18550 C  C     . ILE A 1 3983 ? 185.336 120.033 160.700 1.00 38.35  ? 3983 ILE A C     1 
ATOM   18551 O  O     . ILE A 1 3983 ? 185.552 121.249 160.626 1.00 36.82  ? 3983 ILE A O     1 
ATOM   18552 C  CB    . ILE A 1 3983 ? 183.040 119.089 161.203 1.00 37.35  ? 3983 ILE A CB    1 
ATOM   18553 C  CG1   . ILE A 1 3983 ? 181.645 118.947 160.593 1.00 31.59  ? 3983 ILE A CG1   1 
ATOM   18554 C  CG2   . ILE A 1 3983 ? 183.042 120.156 162.286 1.00 34.33  ? 3983 ILE A CG2   1 
ATOM   18555 C  CD1   . ILE A 1 3983 ? 180.707 118.096 161.416 1.00 33.42  ? 3983 ILE A CD1   1 
ATOM   18556 N  N     . GLY A 1 3984 ? 186.196 119.198 161.288 1.00 41.66  ? 3984 GLY A N     1 
ATOM   18557 C  CA    . GLY A 1 3984 ? 187.458 119.697 161.808 1.00 38.95  ? 3984 GLY A CA    1 
ATOM   18558 C  C     . GLY A 1 3984 ? 188.355 120.249 160.718 1.00 41.29  ? 3984 GLY A C     1 
ATOM   18559 O  O     . GLY A 1 3984 ? 189.122 121.188 160.947 1.00 41.94  ? 3984 GLY A O     1 
ATOM   18560 N  N     . GLN A 1 3985 ? 188.278 119.666 159.519 1.00 41.28  ? 3985 GLN A N     1 
ATOM   18561 C  CA    . GLN A 1 3985 ? 189.039 120.186 158.389 1.00 37.81  ? 3985 GLN A CA    1 
ATOM   18562 C  C     . GLN A 1 3985 ? 188.628 121.615 158.060 1.00 37.52  ? 3985 GLN A C     1 
ATOM   18563 O  O     . GLN A 1 3985 ? 189.482 122.478 157.829 1.00 42.08  ? 3985 GLN A O     1 
ATOM   18564 C  CB    . GLN A 1 3985 ? 188.849 119.284 157.170 1.00 41.97  ? 3985 GLN A CB    1 
ATOM   18565 C  CG    . GLN A 1 3985 ? 190.141 118.806 156.533 1.00 50.17  ? 3985 GLN A CG    1 
ATOM   18566 C  CD    . GLN A 1 3985 ? 189.910 117.716 155.507 1.00 53.16  ? 3985 GLN A CD    1 
ATOM   18567 O  OE1   . GLN A 1 3985 ? 188.780 117.279 155.293 1.00 46.08  ? 3985 GLN A OE1   1 
ATOM   18568 N  NE2   . GLN A 1 3985 ? 190.984 117.269 154.865 1.00 55.94  ? 3985 GLN A NE2   1 
ATOM   18569 N  N     . ALA A 1 3986 ? 187.320 121.884 158.043 1.00 33.79  ? 3986 ALA A N     1 
ATOM   18570 C  CA    . ALA A 1 3986 ? 186.841 123.227 157.735 1.00 27.20  ? 3986 ALA A CA    1 
ATOM   18571 C  C     . ALA A 1 3986 ? 187.249 124.224 158.812 1.00 32.70  ? 3986 ALA A C     1 
ATOM   18572 O  O     . ALA A 1 3986 ? 187.526 125.392 158.513 1.00 36.95  ? 3986 ALA A O     1 
ATOM   18573 C  CB    . ALA A 1 3986 ? 185.323 123.216 157.560 1.00 26.02  ? 3986 ALA A CB    1 
ATOM   18574 N  N     . ILE A 1 3987 ? 187.279 123.785 160.073 1.00 32.12  ? 3987 ILE A N     1 
ATOM   18575 C  CA    . ILE A 1 3987 ? 187.645 124.682 161.167 1.00 28.18  ? 3987 ILE A CA    1 
ATOM   18576 C  C     . ILE A 1 3987 ? 189.075 125.175 160.997 1.00 35.09  ? 3987 ILE A C     1 
ATOM   18577 O  O     . ILE A 1 3987 ? 189.356 126.372 161.130 1.00 39.06  ? 3987 ILE A O     1 
ATOM   18578 C  CB    . ILE A 1 3987 ? 187.450 123.977 162.521 1.00 31.04  ? 3987 ILE A CB    1 
ATOM   18579 C  CG1   . ILE A 1 3987 ? 185.972 123.677 162.750 1.00 34.34  ? 3987 ILE A CG1   1 
ATOM   18580 C  CG2   . ILE A 1 3987 ? 187.997 124.834 163.650 1.00 31.32  ? 3987 ILE A CG2   1 
ATOM   18581 C  CD1   . ILE A 1 3987 ? 185.656 123.188 164.133 1.00 29.92  ? 3987 ILE A CD1   1 
ATOM   18582 N  N     . HIS A 1 3988 ? 190.001 124.261 160.700 1.00 37.53  ? 3988 HIS A N     1 
ATOM   18583 C  CA    . HIS A 1 3988 ? 191.383 124.658 160.463 1.00 35.60  ? 3988 HIS A CA    1 
ATOM   18584 C  C     . HIS A 1 3988 ? 191.494 125.526 159.217 1.00 35.65  ? 3988 HIS A C     1 
ATOM   18585 O  O     . HIS A 1 3988 ? 192.286 126.475 159.181 1.00 40.15  ? 3988 HIS A O     1 
ATOM   18586 C  CB    . HIS A 1 3988 ? 192.269 123.419 160.346 1.00 44.14  ? 3988 HIS A CB    1 
ATOM   18587 C  CG    . HIS A 1 3988 ? 192.552 122.755 161.657 1.00 48.35  ? 3988 HIS A CG    1 
ATOM   18588 N  ND1   . HIS A 1 3988 ? 193.279 123.363 162.658 1.00 49.34  ? 3988 HIS A ND1   1 
ATOM   18589 C  CD2   . HIS A 1 3988 ? 192.198 121.539 162.135 1.00 47.80  ? 3988 HIS A CD2   1 
ATOM   18590 C  CE1   . HIS A 1 3988 ? 193.365 122.547 163.694 1.00 50.88  ? 3988 HIS A CE1   1 
ATOM   18591 N  NE2   . HIS A 1 3988 ? 192.717 121.434 163.402 1.00 52.07  ? 3988 HIS A NE2   1 
ATOM   18592 N  N     . ARG A 1 3989 ? 190.712 125.208 158.182 1.00 35.47  ? 3989 ARG A N     1 
ATOM   18593 C  CA    . ARG A 1 3989 ? 190.652 126.063 157.001 1.00 32.70  ? 3989 ARG A CA    1 
ATOM   18594 C  C     . ARG A 1 3989 ? 190.109 127.443 157.353 1.00 33.07  ? 3989 ARG A C     1 
ATOM   18595 O  O     . ARG A 1 3989 ? 190.597 128.459 156.846 1.00 34.10  ? 3989 ARG A O     1 
ATOM   18596 C  CB    . ARG A 1 3989 ? 189.792 125.401 155.926 1.00 27.06  ? 3989 ARG A CB    1 
ATOM   18597 C  CG    . ARG A 1 3989 ? 190.405 124.147 155.328 1.00 29.44  ? 3989 ARG A CG    1 
ATOM   18598 C  CD    . ARG A 1 3989 ? 189.867 123.865 153.938 1.00 39.62  ? 3989 ARG A CD    1 
ATOM   18599 N  NE    . ARG A 1 3989 ? 190.225 122.526 153.484 1.00 45.15  ? 3989 ARG A NE    1 
ATOM   18600 C  CZ    . ARG A 1 3989 ? 189.448 121.460 153.611 1.00 41.99  ? 3989 ARG A CZ    1 
ATOM   18601 N  NH1   . ARG A 1 3989 ? 188.255 121.537 154.178 1.00 39.41  ? 3989 ARG A NH1   1 
ATOM   18602 N  NH2   . ARG A 1 3989 ? 189.880 120.285 153.162 1.00 38.14  ? 3989 ARG A NH2   1 
ATOM   18603 N  N     . LEU A 1 3990 ? 189.092 127.495 158.217 1.00 30.66  ? 3990 LEU A N     1 
ATOM   18604 C  CA    . LEU A 1 3990 ? 188.569 128.777 158.677 1.00 29.62  ? 3990 LEU A CA    1 
ATOM   18605 C  C     . LEU A 1 3990 ? 189.626 129.561 159.444 1.00 32.50  ? 3990 LEU A C     1 
ATOM   18606 O  O     . LEU A 1 3990 ? 189.757 130.778 159.268 1.00 36.78  ? 3990 LEU A O     1 
ATOM   18607 C  CB    . LEU A 1 3990 ? 187.332 128.551 159.548 1.00 33.06  ? 3990 LEU A CB    1 
ATOM   18608 C  CG    . LEU A 1 3990 ? 186.373 129.724 159.764 1.00 33.50  ? 3990 LEU A CG    1 
ATOM   18609 C  CD1   . LEU A 1 3990 ? 185.913 130.312 158.442 1.00 27.89  ? 3990 LEU A CD1   1 
ATOM   18610 C  CD2   . LEU A 1 3990 ? 185.181 129.284 160.598 1.00 27.18  ? 3990 LEU A CD2   1 
ATOM   18611 N  N     . LEU A 1 3991 ? 190.386 128.880 160.304 1.00 34.96  ? 3991 LEU A N     1 
ATOM   18612 C  CA    . LEU A 1 3991 ? 191.433 129.553 161.066 1.00 34.17  ? 3991 LEU A CA    1 
ATOM   18613 C  C     . LEU A 1 3991 ? 192.536 130.072 160.153 1.00 34.41  ? 3991 LEU A C     1 
ATOM   18614 O  O     . LEU A 1 3991 ? 193.039 131.186 160.345 1.00 34.10  ? 3991 LEU A O     1 
ATOM   18615 C  CB    . LEU A 1 3991 ? 192.007 128.601 162.115 1.00 37.28  ? 3991 LEU A CB    1 
ATOM   18616 C  CG    . LEU A 1 3991 ? 191.079 128.231 163.273 1.00 35.05  ? 3991 LEU A CG    1 
ATOM   18617 C  CD1   . LEU A 1 3991 ? 191.728 127.186 164.165 1.00 39.92  ? 3991 LEU A CD1   1 
ATOM   18618 C  CD2   . LEU A 1 3991 ? 190.701 129.464 164.075 1.00 36.24  ? 3991 LEU A CD2   1 
ATOM   18619 N  N     . LEU A 1 3992 ? 192.929 129.276 159.156 1.00 35.28  ? 3992 LEU A N     1 
ATOM   18620 C  CA    . LEU A 1 3992 ? 193.984 129.698 158.240 1.00 36.00  ? 3992 LEU A CA    1 
ATOM   18621 C  C     . LEU A 1 3992 ? 193.541 130.881 157.390 1.00 35.70  ? 3992 LEU A C     1 
ATOM   18622 O  O     . LEU A 1 3992 ? 194.325 131.805 157.142 1.00 37.63  ? 3992 LEU A O     1 
ATOM   18623 C  CB    . LEU A 1 3992 ? 194.403 128.528 157.351 1.00 34.26  ? 3992 LEU A CB    1 
ATOM   18624 C  CG    . LEU A 1 3992 ? 195.407 127.544 157.952 1.00 38.88  ? 3992 LEU A CG    1 
ATOM   18625 C  CD1   . LEU A 1 3992 ? 195.512 126.292 157.095 1.00 44.81  ? 3992 LEU A CD1   1 
ATOM   18626 C  CD2   . LEU A 1 3992 ? 196.768 128.197 158.120 1.00 38.34  ? 3992 LEU A CD2   1 
ATOM   18627 N  N     . ILE A 1 3993 ? 192.289 130.867 156.929 1.00 34.38  ? 3993 ILE A N     1 
ATOM   18628 C  CA    . ILE A 1 3993 ? 191.791 131.951 156.087 1.00 29.16  ? 3993 ILE A CA    1 
ATOM   18629 C  C     . ILE A 1 3993 ? 191.762 133.262 156.862 1.00 32.55  ? 3993 ILE A C     1 
ATOM   18630 O  O     . ILE A 1 3993 ? 192.155 134.313 156.343 1.00 41.49  ? 3993 ILE A O     1 
ATOM   18631 C  CB    . ILE A 1 3993 ? 190.408 131.589 155.518 1.00 26.52  ? 3993 ILE A CB    1 
ATOM   18632 C  CG1   . ILE A 1 3993 ? 190.552 130.580 154.377 1.00 29.59  ? 3993 ILE A CG1   1 
ATOM   18633 C  CG2   . ILE A 1 3993 ? 189.677 132.831 155.036 1.00 29.24  ? 3993 ILE A CG2   1 
ATOM   18634 C  CD1   . ILE A 1 3993 ? 191.272 131.128 153.169 1.00 33.67  ? 3993 ILE A CD1   1 
ATOM   18635 N  N     . GLN A 1 3994 ? 191.311 133.220 158.118 1.00 28.63  ? 3994 GLN A N     1 
ATOM   18636 C  CA    . GLN A 1 3994 ? 191.245 134.433 158.926 1.00 29.16  ? 3994 GLN A CA    1 
ATOM   18637 C  C     . GLN A 1 3994 ? 192.621 135.068 159.088 1.00 34.56  ? 3994 GLN A C     1 
ATOM   18638 O  O     . GLN A 1 3994 ? 192.752 136.298 159.078 1.00 39.67  ? 3994 GLN A O     1 
ATOM   18639 C  CB    . GLN A 1 3994 ? 190.636 134.117 160.293 1.00 32.20  ? 3994 GLN A CB    1 
ATOM   18640 C  CG    . GLN A 1 3994 ? 190.651 135.279 161.269 1.00 30.65  ? 3994 GLN A CG    1 
ATOM   18641 C  CD    . GLN A 1 3994 ? 189.854 134.993 162.524 1.00 29.17  ? 3994 GLN A CD    1 
ATOM   18642 O  OE1   . GLN A 1 3994 ? 189.831 133.864 163.014 1.00 36.27  ? 3994 GLN A OE1   1 
ATOM   18643 N  NE2   . GLN A 1 3994 ? 189.195 136.017 163.054 1.00 32.91  ? 3994 GLN A NE2   1 
ATOM   18644 N  N     . ALA A 1 3995 ? 193.660 134.245 159.238 1.00 39.98  ? 3995 ALA A N     1 
ATOM   18645 C  CA    . ALA A 1 3995 ? 195.008 134.778 159.399 1.00 36.27  ? 3995 ALA A CA    1 
ATOM   18646 C  C     . ALA A 1 3995 ? 195.560 135.317 158.085 1.00 40.47  ? 3995 ALA A C     1 
ATOM   18647 O  O     . ALA A 1 3995 ? 196.177 136.389 158.059 1.00 46.29  ? 3995 ALA A O     1 
ATOM   18648 C  CB    . ALA A 1 3995 ? 195.933 133.703 159.967 1.00 39.78  ? 3995 ALA A CB    1 
ATOM   18649 N  N     . PHE A 1 3996 ? 195.350 134.594 156.986 1.00 38.33  ? 3996 PHE A N     1 
ATOM   18650 C  CA    . PHE A 1 3996 ? 195.958 134.926 155.703 1.00 37.67  ? 3996 PHE A CA    1 
ATOM   18651 C  C     . PHE A 1 3996 ? 195.081 135.821 154.836 1.00 39.81  ? 3996 PHE A C     1 
ATOM   18652 O  O     . PHE A 1 3996 ? 195.534 136.875 154.382 1.00 44.64  ? 3996 PHE A O     1 
ATOM   18653 C  CB    . PHE A 1 3996 ? 196.298 133.641 154.938 1.00 42.23  ? 3996 PHE A CB    1 
ATOM   18654 C  CG    . PHE A 1 3996 ? 197.436 132.868 155.533 1.00 51.23  ? 3996 PHE A CG    1 
ATOM   18655 C  CD1   . PHE A 1 3996 ? 198.641 133.490 155.810 1.00 48.67  ? 3996 PHE A CD1   1 
ATOM   18656 C  CD2   . PHE A 1 3996 ? 197.301 131.520 155.820 1.00 46.51  ? 3996 PHE A CD2   1 
ATOM   18657 C  CE1   . PHE A 1 3996 ? 199.690 132.782 156.356 1.00 49.52  ? 3996 PHE A CE1   1 
ATOM   18658 C  CE2   . PHE A 1 3996 ? 198.347 130.807 156.369 1.00 45.66  ? 3996 PHE A CE2   1 
ATOM   18659 C  CZ    . PHE A 1 3996 ? 199.542 131.439 156.641 1.00 52.75  ? 3996 PHE A CZ    1 
ATOM   18660 N  N     . ARG A 1 3997 ? 193.831 135.427 154.598 1.00 36.24  ? 3997 ARG A N     1 
ATOM   18661 C  CA    . ARG A 1 3997 ? 192.947 136.113 153.655 1.00 32.63  ? 3997 ARG A CA    1 
ATOM   18662 C  C     . ARG A 1 3997 ? 191.639 136.453 154.354 1.00 31.39  ? 3997 ARG A C     1 
ATOM   18663 O  O     . ARG A 1 3997 ? 190.607 135.813 154.111 1.00 32.55  ? 3997 ARG A O     1 
ATOM   18664 C  CB    . ARG A 1 3997 ? 192.702 135.251 152.415 1.00 33.24  ? 3997 ARG A CB    1 
ATOM   18665 C  CG    . ARG A 1 3997 ? 193.952 134.982 151.593 1.00 35.45  ? 3997 ARG A CG    1 
ATOM   18666 C  CD    . ARG A 1 3997 ? 194.414 136.231 150.865 1.00 36.49  ? 3997 ARG A CD    1 
ATOM   18667 N  NE    . ARG A 1 3997 ? 193.364 136.770 150.010 1.00 36.38  ? 3997 ARG A NE    1 
ATOM   18668 C  CZ    . ARG A 1 3997 ? 193.119 136.352 148.776 1.00 34.98  ? 3997 ARG A CZ    1 
ATOM   18669 N  NH1   . ARG A 1 3997 ? 193.842 135.398 148.212 1.00 38.20  ? 3997 ARG A NH1   1 
ATOM   18670 N  NH2   . ARG A 1 3997 ? 192.122 136.903 148.091 1.00 39.22  ? 3997 ARG A NH2   1 
ATOM   18671 N  N     . PRO A 1 3998 ? 191.645 137.457 155.236 1.00 32.47  ? 3998 PRO A N     1 
ATOM   18672 C  CA    . PRO A 1 3998 ? 190.401 137.813 155.939 1.00 29.27  ? 3998 PRO A CA    1 
ATOM   18673 C  C     . PRO A 1 3998 ? 189.299 138.294 155.013 1.00 29.22  ? 3998 PRO A C     1 
ATOM   18674 O  O     . PRO A 1 3998 ? 188.122 138.250 155.392 1.00 29.52  ? 3998 PRO A O     1 
ATOM   18675 C  CB    . PRO A 1 3998 ? 190.847 138.919 156.907 1.00 24.81  ? 3998 PRO A CB    1 
ATOM   18676 C  CG    . PRO A 1 3998 ? 192.117 139.446 156.334 1.00 28.54  ? 3998 PRO A CG    1 
ATOM   18677 C  CD    . PRO A 1 3998 ? 192.782 138.288 155.664 1.00 30.95  ? 3998 PRO A CD    1 
ATOM   18678 N  N     . ASP A 1 3999 ? 189.643 138.758 153.809 1.00 26.94  ? 3999 ASP A N     1 
ATOM   18679 C  CA    . ASP A 1 3999 ? 188.621 139.199 152.866 1.00 25.51  ? 3999 ASP A CA    1 
ATOM   18680 C  C     . ASP A 1 3999 ? 187.768 138.036 152.377 1.00 24.39  ? 3999 ASP A C     1 
ATOM   18681 O  O     . ASP A 1 3999 ? 186.659 138.248 151.874 1.00 28.97  ? 3999 ASP A O     1 
ATOM   18682 C  CB    . ASP A 1 3999 ? 189.275 139.920 151.685 1.00 31.60  ? 3999 ASP A CB    1 
ATOM   18683 C  CG    . ASP A 1 3999 ? 190.291 139.057 150.963 1.00 36.25  ? 3999 ASP A CG    1 
ATOM   18684 O  OD1   . ASP A 1 3999 ? 191.448 138.983 151.427 1.00 33.65  ? 3999 ASP A OD1   1 
ATOM   18685 O  OD2   . ASP A 1 3999 ? 189.936 138.459 149.926 1.00 38.32  ? 3999 ASP A OD2   1 
ATOM   18686 N  N     . ARG A 1 4000 ? 188.261 136.808 152.513 1.00 26.29  ? 4000 ARG A N     1 
ATOM   18687 C  CA    . ARG A 1 4000 ? 187.517 135.615 152.135 1.00 24.12  ? 4000 ARG A CA    1 
ATOM   18688 C  C     . ARG A 1 4000 ? 186.931 134.880 153.333 1.00 22.14  ? 4000 ARG A C     1 
ATOM   18689 O  O     . ARG A 1 4000 ? 186.504 133.730 153.186 1.00 25.09  ? 4000 ARG A O     1 
ATOM   18690 C  CB    . ARG A 1 4000 ? 188.418 134.664 151.341 1.00 25.97  ? 4000 ARG A CB    1 
ATOM   18691 C  CG    . ARG A 1 4000 ? 189.071 135.300 150.129 1.00 24.04  ? 4000 ARG A CG    1 
ATOM   18692 C  CD    . ARG A 1 4000 ? 188.037 135.873 149.177 1.00 27.58  ? 4000 ARG A CD    1 
ATOM   18693 N  NE    . ARG A 1 4000 ? 187.145 134.844 148.656 1.00 34.84  ? 4000 ARG A NE    1 
ATOM   18694 C  CZ    . ARG A 1 4000 ? 185.991 135.091 148.053 1.00 34.33  ? 4000 ARG A CZ    1 
ATOM   18695 N  NH1   . ARG A 1 4000 ? 185.554 136.327 147.877 1.00 30.12  ? 4000 ARG A NH1   1 
ATOM   18696 N  NH2   . ARG A 1 4000 ? 185.258 134.072 147.612 1.00 28.63  ? 4000 ARG A NH2   1 
ATOM   18697 N  N     . LEU A 1 4001 ? 186.910 135.508 154.510 1.00 24.54  ? 4001 LEU A N     1 
ATOM   18698 C  CA    . LEU A 1 4001 ? 186.428 134.835 155.712 1.00 20.44  ? 4001 LEU A CA    1 
ATOM   18699 C  C     . LEU A 1 4001 ? 184.944 134.502 155.606 1.00 18.97  ? 4001 LEU A C     1 
ATOM   18700 O  O     . LEU A 1 4001 ? 184.504 133.431 156.039 1.00 22.60  ? 4001 LEU A O     1 
ATOM   18701 C  CB    . LEU A 1 4001 ? 186.702 135.706 156.939 1.00 18.95  ? 4001 LEU A CB    1 
ATOM   18702 C  CG    . LEU A 1 4001 ? 186.302 135.129 158.297 1.00 21.87  ? 4001 LEU A CG    1 
ATOM   18703 C  CD1   . LEU A 1 4001 ? 187.145 133.909 158.621 1.00 26.10  ? 4001 LEU A CD1   1 
ATOM   18704 C  CD2   . LEU A 1 4001 ? 186.436 136.179 159.385 1.00 27.10  ? 4001 LEU A CD2   1 
ATOM   18705 N  N     . LEU A 1 4002 ? 184.156 135.416 155.036 1.00 20.80  ? 4002 LEU A N     1 
ATOM   18706 C  CA    . LEU A 1 4002 ? 182.723 135.179 154.889 1.00 16.86  ? 4002 LEU A CA    1 
ATOM   18707 C  C     . LEU A 1 4002 ? 182.453 133.990 153.975 1.00 18.71  ? 4002 LEU A C     1 
ATOM   18708 O  O     . LEU A 1 4002 ? 181.566 133.172 154.243 1.00 23.71  ? 4002 LEU A O     1 
ATOM   18709 C  CB    . LEU A 1 4002 ? 182.037 136.436 154.353 1.00 15.92  ? 4002 LEU A CB    1 
ATOM   18710 C  CG    . LEU A 1 4002 ? 181.679 137.512 155.377 1.00 21.43  ? 4002 LEU A CG    1 
ATOM   18711 C  CD1   . LEU A 1 4002 ? 180.911 138.639 154.708 1.00 22.17  ? 4002 LEU A CD1   1 
ATOM   18712 C  CD2   . LEU A 1 4002 ? 180.879 136.917 156.524 1.00 20.61  ? 4002 LEU A CD2   1 
ATOM   18713 N  N     . ALA A 1 4003 ? 183.207 133.886 152.880 1.00 18.44  ? 4003 ALA A N     1 
ATOM   18714 C  CA    . ALA A 1 4003 ? 183.043 132.756 151.972 1.00 17.42  ? 4003 ALA A CA    1 
ATOM   18715 C  C     . ALA A 1 4003 ? 183.416 131.446 152.654 1.00 22.70  ? 4003 ALA A C     1 
ATOM   18716 O  O     . ALA A 1 4003 ? 182.739 130.427 152.481 1.00 24.21  ? 4003 ALA A O     1 
ATOM   18717 C  CB    . ALA A 1 4003 ? 183.882 132.971 150.712 1.00 20.61  ? 4003 ALA A CB    1 
ATOM   18718 N  N     . MET A 1 4004 ? 184.499 131.454 153.435 1.00 22.31  ? 4004 MET A N     1 
ATOM   18719 C  CA    . MET A 1 4004 ? 184.908 130.246 154.143 1.00 20.76  ? 4004 MET A CA    1 
ATOM   18720 C  C     . MET A 1 4004 ? 183.932 129.910 155.264 1.00 20.84  ? 4004 MET A C     1 
ATOM   18721 O  O     . MET A 1 4004 ? 183.712 128.734 155.576 1.00 23.41  ? 4004 MET A O     1 
ATOM   18722 C  CB    . MET A 1 4004 ? 186.326 130.413 154.689 1.00 22.66  ? 4004 MET A CB    1 
ATOM   18723 C  CG    . MET A 1 4004 ? 186.946 129.135 155.235 1.00 26.46  ? 4004 MET A CG    1 
ATOM   18724 S  SD    . MET A 1 4004 ? 187.086 127.829 154.002 1.00 43.75  ? 4004 MET A SD    1 
ATOM   18725 C  CE    . MET A 1 4004 ? 186.367 126.449 154.889 1.00 27.99  ? 4004 MET A CE    1 
ATOM   18726 N  N     . ALA A 1 4005 ? 183.339 130.934 155.884 1.00 20.70  ? 4005 ALA A N     1 
ATOM   18727 C  CA    . ALA A 1 4005 ? 182.323 130.698 156.904 1.00 15.34  ? 4005 ALA A CA    1 
ATOM   18728 C  C     . ALA A 1 4005 ? 181.113 129.984 156.318 1.00 17.87  ? 4005 ALA A C     1 
ATOM   18729 O  O     . ALA A 1 4005 ? 180.508 129.129 156.975 1.00 22.55  ? 4005 ALA A O     1 
ATOM   18730 C  CB    . ALA A 1 4005 ? 181.908 132.020 157.547 1.00 16.10  ? 4005 ALA A CB    1 
ATOM   18731 N  N     . HIS A 1 4006 ? 180.741 130.327 155.082 1.00 17.46  ? 4006 HIS A N     1 
ATOM   18732 C  CA    . HIS A 1 4006 ? 179.648 129.627 154.416 1.00 17.34  ? 4006 HIS A CA    1 
ATOM   18733 C  C     . HIS A 1 4006 ? 180.000 128.165 154.178 1.00 17.03  ? 4006 HIS A C     1 
ATOM   18734 O  O     . HIS A 1 4006 ? 179.129 127.289 154.248 1.00 16.23  ? 4006 HIS A O     1 
ATOM   18735 C  CB    . HIS A 1 4006 ? 179.306 130.321 153.097 1.00 19.29  ? 4006 HIS A CB    1 
ATOM   18736 C  CG    . HIS A 1 4006 ? 178.448 131.537 153.258 1.00 21.84  ? 4006 HIS A CG    1 
ATOM   18737 N  ND1   . HIS A 1 4006 ? 178.947 132.749 153.685 1.00 24.31  ? 4006 HIS A ND1   1 
ATOM   18738 C  CD2   . HIS A 1 4006 ? 177.124 131.728 153.049 1.00 22.28  ? 4006 HIS A CD2   1 
ATOM   18739 C  CE1   . HIS A 1 4006 ? 177.967 133.634 153.732 1.00 28.40  ? 4006 HIS A CE1   1 
ATOM   18740 N  NE2   . HIS A 1 4006 ? 176.851 133.040 153.351 1.00 31.21  ? 4006 HIS A NE2   1 
ATOM   18741 N  N     . MET A 1 4007 ? 181.272 127.882 153.884 1.00 19.91  ? 4007 MET A N     1 
ATOM   18742 C  CA    . MET A 1 4007 ? 181.696 126.501 153.672 1.00 21.17  ? 4007 MET A CA    1 
ATOM   18743 C  C     . MET A 1 4007 ? 181.543 125.669 154.940 1.00 22.84  ? 4007 MET A C     1 
ATOM   18744 O  O     . MET A 1 4007 ? 181.164 124.494 154.875 1.00 26.03  ? 4007 MET A O     1 
ATOM   18745 C  CB    . MET A 1 4007 ? 183.141 126.462 153.178 1.00 24.54  ? 4007 MET A CB    1 
ATOM   18746 C  CG    . MET A 1 4007 ? 183.399 127.293 151.936 1.00 28.04  ? 4007 MET A CG    1 
ATOM   18747 S  SD    . MET A 1 4007 ? 184.663 126.560 150.879 1.00 49.92  ? 4007 MET A SD    1 
ATOM   18748 C  CE    . MET A 1 4007 ? 183.923 124.971 150.512 1.00 39.13  ? 4007 MET A CE    1 
ATOM   18749 N  N     . PHE A 1 4008 ? 181.851 126.254 156.101 1.00 19.09  ? 4008 PHE A N     1 
ATOM   18750 C  CA    . PHE A 1 4008 ? 181.692 125.522 157.354 1.00 17.34  ? 4008 PHE A CA    1 
ATOM   18751 C  C     . PHE A 1 4008 ? 180.228 125.178 157.589 1.00 20.44  ? 4008 PHE A C     1 
ATOM   18752 O  O     . PHE A 1 4008 ? 179.903 124.063 158.016 1.00 25.00  ? 4008 PHE A O     1 
ATOM   18753 C  CB    . PHE A 1 4008 ? 182.259 126.346 158.516 1.00 20.12  ? 4008 PHE A CB    1 
ATOM   18754 C  CG    . PHE A 1 4008 ? 182.015 125.752 159.889 1.00 25.94  ? 4008 PHE A CG    1 
ATOM   18755 C  CD1   . PHE A 1 4008 ? 180.765 125.798 160.493 1.00 26.71  ? 4008 PHE A CD1   1 
ATOM   18756 C  CD2   . PHE A 1 4008 ? 183.058 125.169 160.587 1.00 26.44  ? 4008 PHE A CD2   1 
ATOM   18757 C  CE1   . PHE A 1 4008 ? 180.563 125.264 161.748 1.00 22.94  ? 4008 PHE A CE1   1 
ATOM   18758 C  CE2   . PHE A 1 4008 ? 182.855 124.633 161.844 1.00 33.40  ? 4008 PHE A CE2   1 
ATOM   18759 C  CZ    . PHE A 1 4008 ? 181.608 124.681 162.424 1.00 28.99  ? 4008 PHE A CZ    1 
ATOM   18760 N  N     . VAL A 1 4009 ? 179.330 126.128 157.320 1.00 18.76  ? 4009 VAL A N     1 
ATOM   18761 C  CA    . VAL A 1 4009 ? 177.901 125.874 157.475 1.00 16.40  ? 4009 VAL A CA    1 
ATOM   18762 C  C     . VAL A 1 4009 ? 177.460 124.766 156.528 1.00 21.19  ? 4009 VAL A C     1 
ATOM   18763 O  O     . VAL A 1 4009 ? 176.643 123.909 156.886 1.00 22.71  ? 4009 VAL A O     1 
ATOM   18764 C  CB    . VAL A 1 4009 ? 177.101 127.171 157.249 1.00 12.46  ? 4009 VAL A CB    1 
ATOM   18765 C  CG1   . VAL A 1 4009 ? 175.611 126.910 157.377 1.00 11.80  ? 4009 VAL A CG1   1 
ATOM   18766 C  CG2   . VAL A 1 4009 ? 177.544 128.242 158.229 1.00 14.16  ? 4009 VAL A CG2   1 
ATOM   18767 N  N     . SER A 1 4010 ? 177.999 124.763 155.306 1.00 19.13  ? 4010 SER A N     1 
ATOM   18768 C  CA    . SER A 1 4010 ? 177.724 123.670 154.381 1.00 21.38  ? 4010 SER A CA    1 
ATOM   18769 C  C     . SER A 1 4010 ? 178.259 122.346 154.909 1.00 24.81  ? 4010 SER A C     1 
ATOM   18770 O  O     . SER A 1 4010 ? 177.603 121.309 154.762 1.00 27.49  ? 4010 SER A O     1 
ATOM   18771 C  CB    . SER A 1 4010 ? 178.325 123.976 153.010 1.00 24.25  ? 4010 SER A CB    1 
ATOM   18772 O  OG    . SER A 1 4010 ? 177.918 125.252 152.549 1.00 29.83  ? 4010 SER A OG    1 
ATOM   18773 N  N     . THR A 1 4011 ? 179.447 122.358 155.517 1.00 21.87  ? 4011 THR A N     1 
ATOM   18774 C  CA    . THR A 1 4011 ? 180.014 121.137 156.076 1.00 21.88  ? 4011 THR A CA    1 
ATOM   18775 C  C     . THR A 1 4011 ? 179.178 120.592 157.228 1.00 26.05  ? 4011 THR A C     1 
ATOM   18776 O  O     . THR A 1 4011 ? 178.979 119.376 157.322 1.00 31.57  ? 4011 THR A O     1 
ATOM   18777 C  CB    . THR A 1 4011 ? 181.448 121.391 156.546 1.00 26.84  ? 4011 THR A CB    1 
ATOM   18778 O  OG1   . THR A 1 4011 ? 182.221 121.919 155.461 1.00 28.36  ? 4011 THR A OG1   1 
ATOM   18779 C  CG2   . THR A 1 4011 ? 182.087 120.100 157.027 1.00 28.78  ? 4011 THR A CG2   1 
ATOM   18780 N  N     . ASN A 1 4012 ? 178.676 121.465 158.101 1.00 26.50  ? 4012 ASN A N     1 
ATOM   18781 C  CA    . ASN A 1 4012 ? 177.879 121.056 159.251 1.00 19.51  ? 4012 ASN A CA    1 
ATOM   18782 C  C     . ASN A 1 4012 ? 176.404 120.879 158.913 1.00 20.31  ? 4012 ASN A C     1 
ATOM   18783 O  O     . ASN A 1 4012 ? 175.839 119.806 159.142 1.00 21.52  ? 4012 ASN A O     1 
ATOM   18784 C  CB    . ASN A 1 4012 ? 178.026 122.081 160.383 1.00 19.23  ? 4012 ASN A CB    1 
ATOM   18785 C  CG    . ASN A 1 4012 ? 179.411 122.082 160.994 1.00 28.75  ? 4012 ASN A CG    1 
ATOM   18786 O  OD1   . ASN A 1 4012 ? 180.396 122.399 160.329 1.00 28.78  ? 4012 ASN A OD1   1 
ATOM   18787 N  ND2   . ASN A 1 4012 ? 179.493 121.728 162.271 1.00 30.58  ? 4012 ASN A ND2   1 
ATOM   18788 N  N     . LEU A 1 4013 ? 175.771 121.914 158.360 1.00 20.26  ? 4013 LEU A N     1 
ATOM   18789 C  CA    . LEU A 1 4013 ? 174.329 121.929 158.163 1.00 17.68  ? 4013 LEU A CA    1 
ATOM   18790 C  C     . LEU A 1 4013 ? 173.885 121.501 156.772 1.00 20.13  ? 4013 LEU A C     1 
ATOM   18791 O  O     . LEU A 1 4013 ? 172.760 121.015 156.629 1.00 22.97  ? 4013 LEU A O     1 
ATOM   18792 C  CB    . LEU A 1 4013 ? 173.778 123.333 158.452 1.00 15.42  ? 4013 LEU A CB    1 
ATOM   18793 C  CG    . LEU A 1 4013 ? 173.941 123.784 159.905 1.00 11.91  ? 4013 LEU A CG    1 
ATOM   18794 C  CD1   . LEU A 1 4013 ? 173.638 125.262 160.061 1.00 12.27  ? 4013 LEU A CD1   1 
ATOM   18795 C  CD2   . LEU A 1 4013 ? 173.050 122.963 160.817 1.00 11.59  ? 4013 LEU A CD2   1 
ATOM   18796 N  N     . GLY A 1 4014 ? 174.726 121.663 155.755 1.00 22.24  ? 4014 GLY A N     1 
ATOM   18797 C  CA    . GLY A 1 4014 ? 174.358 121.270 154.409 1.00 22.70  ? 4014 GLY A CA    1 
ATOM   18798 C  C     . GLY A 1 4014 ? 174.589 122.353 153.376 1.00 30.51  ? 4014 GLY A C     1 
ATOM   18799 O  O     . GLY A 1 4014 ? 174.586 123.543 153.703 1.00 33.35  ? 4014 GLY A O     1 
ATOM   18800 N  N     . GLU A 1 4015 ? 174.788 121.948 152.119 1.00 34.03  ? 4015 GLU A N     1 
ATOM   18801 C  CA    . GLU A 1 4015 ? 175.070 122.912 151.060 1.00 32.67  ? 4015 GLU A CA    1 
ATOM   18802 C  C     . GLU A 1 4015 ? 173.885 123.839 150.817 1.00 38.57  ? 4015 GLU A C     1 
ATOM   18803 O  O     . GLU A 1 4015 ? 174.066 125.038 150.576 1.00 39.28  ? 4015 GLU A O     1 
ATOM   18804 C  CB    . GLU A 1 4015 ? 175.447 122.180 149.772 1.00 37.82  ? 4015 GLU A CB    1 
ATOM   18805 C  CG    . GLU A 1 4015 ? 174.714 120.864 149.569 1.00 51.04  ? 4015 GLU A CG    1 
ATOM   18806 C  CD    . GLU A 1 4015 ? 174.794 120.367 148.139 1.00 69.66  ? 4015 GLU A CD    1 
ATOM   18807 O  OE1   . GLU A 1 4015 ? 173.893 120.702 147.342 1.00 65.39  ? 4015 GLU A OE1   1 
ATOM   18808 O  OE2   . GLU A 1 4015 ? 175.757 119.642 147.812 1.00 76.22  ? 4015 GLU A OE2   1 
ATOM   18809 N  N     . SER A 1 4016 ? 172.666 123.304 150.871 1.00 36.54  ? 4016 SER A N     1 
ATOM   18810 C  CA    . SER A 1 4016 ? 171.461 124.070 150.588 1.00 35.26  ? 4016 SER A CA    1 
ATOM   18811 C  C     . SER A 1 4016 ? 170.791 124.610 151.847 1.00 30.76  ? 4016 SER A C     1 
ATOM   18812 O  O     . SER A 1 4016 ? 169.596 124.926 151.812 1.00 33.58  ? 4016 SER A O     1 
ATOM   18813 C  CB    . SER A 1 4016 ? 170.471 123.215 149.795 1.00 39.68  ? 4016 SER A CB    1 
ATOM   18814 O  OG    . SER A 1 4016 ? 170.049 122.094 150.551 1.00 33.19  ? 4016 SER A OG    1 
ATOM   18815 N  N     . PHE A 1 4017 ? 171.527 124.716 152.956 1.00 26.24  ? 4017 PHE A N     1 
ATOM   18816 C  CA    . PHE A 1 4017 ? 170.936 125.223 154.191 1.00 20.45  ? 4017 PHE A CA    1 
ATOM   18817 C  C     . PHE A 1 4017 ? 170.528 126.685 154.048 1.00 20.94  ? 4017 PHE A C     1 
ATOM   18818 O  O     . PHE A 1 4017 ? 169.465 127.095 154.528 1.00 23.67  ? 4017 PHE A O     1 
ATOM   18819 C  CB    . PHE A 1 4017 ? 171.914 125.054 155.354 1.00 18.13  ? 4017 PHE A CB    1 
ATOM   18820 C  CG    . PHE A 1 4017 ? 171.315 125.369 156.692 1.00 14.63  ? 4017 PHE A CG    1 
ATOM   18821 C  CD1   . PHE A 1 4017 ? 170.492 124.456 157.328 1.00 14.81  ? 4017 PHE A CD1   1 
ATOM   18822 C  CD2   . PHE A 1 4017 ? 171.548 126.590 157.301 1.00 11.75  ? 4017 PHE A CD2   1 
ATOM   18823 C  CE1   . PHE A 1 4017 ? 169.932 124.746 158.555 1.00 12.23  ? 4017 PHE A CE1   1 
ATOM   18824 C  CE2   . PHE A 1 4017 ? 170.987 126.888 158.525 1.00 8.00   ? 4017 PHE A CE2   1 
ATOM   18825 C  CZ    . PHE A 1 4017 ? 170.179 125.963 159.154 1.00 9.62   ? 4017 PHE A CZ    1 
ATOM   18826 N  N     . MET A 1 4018 ? 171.367 127.487 153.396 1.00 21.13  ? 4018 MET A N     1 
ATOM   18827 C  CA    . MET A 1 4018 ? 171.115 128.907 153.204 1.00 19.91  ? 4018 MET A CA    1 
ATOM   18828 C  C     . MET A 1 4018 ? 170.558 129.221 151.821 1.00 28.71  ? 4018 MET A C     1 
ATOM   18829 O  O     . MET A 1 4018 ? 170.473 130.396 151.450 1.00 31.16  ? 4018 MET A O     1 
ATOM   18830 C  CB    . MET A 1 4018 ? 172.399 129.703 153.440 1.00 19.52  ? 4018 MET A CB    1 
ATOM   18831 C  CG    . MET A 1 4018 ? 172.815 129.794 154.896 1.00 19.00  ? 4018 MET A CG    1 
ATOM   18832 S  SD    . MET A 1 4018 ? 174.414 130.598 155.107 1.00 25.19  ? 4018 MET A SD    1 
ATOM   18833 C  CE    . MET A 1 4018 ? 173.903 132.257 155.540 1.00 18.80  ? 4018 MET A CE    1 
ATOM   18834 N  N     . SER A 1 4019 ? 170.179 128.199 151.050 1.00 26.52  ? 4019 SER A N     1 
ATOM   18835 C  CA    . SER A 1 4019 ? 169.764 128.421 149.669 1.00 30.58  ? 4019 SER A CA    1 
ATOM   18836 C  C     . SER A 1 4019 ? 168.422 129.136 149.577 1.00 35.22  ? 4019 SER A C     1 
ATOM   18837 O  O     . SER A 1 4019 ? 168.163 129.834 148.591 1.00 42.76  ? 4019 SER A O     1 
ATOM   18838 C  CB    . SER A 1 4019 ? 169.704 127.090 148.921 1.00 34.91  ? 4019 SER A CB    1 
ATOM   18839 O  OG    . SER A 1 4019 ? 170.918 126.836 148.236 1.00 47.38  ? 4019 SER A OG    1 
ATOM   18840 N  N     . ILE A 1 4020 ? 167.556 128.977 150.581 1.00 32.42  ? 4020 ILE A N     1 
ATOM   18841 C  CA    . ILE A 1 4020 ? 166.223 129.563 150.505 1.00 30.59  ? 4020 ILE A CA    1 
ATOM   18842 C  C     . ILE A 1 4020 ? 166.257 131.080 150.647 1.00 27.79  ? 4020 ILE A C     1 
ATOM   18843 O  O     . ILE A 1 4020 ? 165.332 131.762 150.194 1.00 29.94  ? 4020 ILE A O     1 
ATOM   18844 C  CB    . ILE A 1 4020 ? 165.297 128.918 151.560 1.00 28.50  ? 4020 ILE A CB    1 
ATOM   18845 C  CG1   . ILE A 1 4020 ? 163.832 129.066 151.148 1.00 25.09  ? 4020 ILE A CG1   1 
ATOM   18846 C  CG2   . ILE A 1 4020 ? 165.535 129.519 152.930 1.00 27.45  ? 4020 ILE A CG2   1 
ATOM   18847 C  CD1   . ILE A 1 4020 ? 163.477 128.315 149.884 1.00 28.19  ? 4020 ILE A CD1   1 
ATOM   18848 N  N     . MET A 1 4021 ? 167.306 131.632 151.260 1.00 25.01  ? 4021 MET A N     1 
ATOM   18849 C  CA    . MET A 1 4021 ? 167.425 133.081 151.377 1.00 26.08  ? 4021 MET A CA    1 
ATOM   18850 C  C     . MET A 1 4021 ? 167.789 133.756 150.062 1.00 32.25  ? 4021 MET A C     1 
ATOM   18851 O  O     . MET A 1 4021 ? 167.596 134.969 149.932 1.00 27.83  ? 4021 MET A O     1 
ATOM   18852 C  CB    . MET A 1 4021 ? 168.460 133.444 152.444 1.00 24.36  ? 4021 MET A CB    1 
ATOM   18853 C  CG    . MET A 1 4021 ? 168.027 133.138 153.868 1.00 26.53  ? 4021 MET A CG    1 
ATOM   18854 S  SD    . MET A 1 4021 ? 166.478 133.963 154.287 1.00 36.85  ? 4021 MET A SD    1 
ATOM   18855 C  CE    . MET A 1 4021 ? 165.451 132.577 154.756 1.00 19.47  ? 4021 MET A CE    1 
ATOM   18856 N  N     . GLU A 1 4022 ? 168.308 133.008 149.090 1.00 36.17  ? 4022 GLU A N     1 
ATOM   18857 C  CA    . GLU A 1 4022 ? 168.648 133.571 147.791 1.00 31.30  ? 4022 GLU A CA    1 
ATOM   18858 C  C     . GLU A 1 4022 ? 167.455 133.662 146.849 1.00 30.51  ? 4022 GLU A C     1 
ATOM   18859 O  O     . GLU A 1 4022 ? 167.547 134.346 145.824 1.00 36.08  ? 4022 GLU A O     1 
ATOM   18860 C  CB    . GLU A 1 4022 ? 169.756 132.743 147.130 1.00 34.44  ? 4022 GLU A CB    1 
ATOM   18861 C  CG    . GLU A 1 4022 ? 170.813 132.237 148.097 1.00 38.36  ? 4022 GLU A CG    1 
ATOM   18862 C  CD    . GLU A 1 4022 ? 171.780 131.266 147.448 1.00 49.67  ? 4022 GLU A CD    1 
ATOM   18863 O  OE1   . GLU A 1 4022 ? 171.421 130.670 146.411 1.00 52.82  ? 4022 GLU A OE1   1 
ATOM   18864 O  OE2   . GLU A 1 4022 ? 172.900 131.099 147.974 1.00 39.75  ? 4022 GLU A OE2   1 
ATOM   18865 N  N     . GLN A 1 4023 ? 166.344 132.994 147.168 1.00 31.55  ? 4023 GLN A N     1 
ATOM   18866 C  CA    . GLN A 1 4023 ? 165.137 133.014 146.362 1.00 32.79  ? 4023 GLN A CA    1 
ATOM   18867 C  C     . GLN A 1 4023 ? 164.209 134.138 146.810 1.00 33.04  ? 4023 GLN A C     1 
ATOM   18868 O  O     . GLN A 1 4023 ? 164.269 134.577 147.963 1.00 33.54  ? 4023 GLN A O     1 
ATOM   18869 C  CB    . GLN A 1 4023 ? 164.402 131.673 146.461 1.00 30.91  ? 4023 GLN A CB    1 
ATOM   18870 C  CG    . GLN A 1 4023 ? 165.241 130.480 146.038 1.00 36.20  ? 4023 GLN A CG    1 
ATOM   18871 C  CD    . GLN A 1 4023 ? 165.404 130.387 144.533 1.00 42.66  ? 4023 GLN A CD    1 
ATOM   18872 O  OE1   . GLN A 1 4023 ? 164.451 130.588 143.780 1.00 41.26  ? 4023 GLN A OE1   1 
ATOM   18873 N  NE2   . GLN A 1 4023 ? 166.618 130.085 144.086 1.00 40.71  ? 4023 GLN A NE2   1 
ATOM   18874 N  N     . PRO A 1 4024 ? 163.353 134.636 145.917 1.00 38.48  ? 4024 PRO A N     1 
ATOM   18875 C  CA    . PRO A 1 4024 ? 162.405 135.682 146.316 1.00 38.19  ? 4024 PRO A CA    1 
ATOM   18876 C  C     . PRO A 1 4024 ? 161.454 135.190 147.397 1.00 38.01  ? 4024 PRO A C     1 
ATOM   18877 O  O     . PRO A 1 4024 ? 161.082 134.016 147.443 1.00 39.17  ? 4024 PRO A O     1 
ATOM   18878 C  CB    . PRO A 1 4024 ? 161.657 136.004 145.016 1.00 30.35  ? 4024 PRO A CB    1 
ATOM   18879 C  CG    . PRO A 1 4024 ? 161.907 134.832 144.118 1.00 29.87  ? 4024 PRO A CG    1 
ATOM   18880 C  CD    . PRO A 1 4024 ? 163.266 134.332 144.479 1.00 35.81  ? 4024 PRO A CD    1 
ATOM   18881 N  N     . LEU A 1 4025 ? 161.069 136.111 148.278 1.00 35.68  ? 4025 LEU A N     1 
ATOM   18882 C  CA    . LEU A 1 4025 ? 160.180 135.772 149.381 1.00 34.75  ? 4025 LEU A CA    1 
ATOM   18883 C  C     . LEU A 1 4025 ? 158.814 135.348 148.857 1.00 40.54  ? 4025 LEU A C     1 
ATOM   18884 O  O     . LEU A 1 4025 ? 158.249 135.988 147.966 1.00 47.78  ? 4025 LEU A O     1 
ATOM   18885 C  CB    . LEU A 1 4025 ? 160.040 136.965 150.326 1.00 29.86  ? 4025 LEU A CB    1 
ATOM   18886 C  CG    . LEU A 1 4025 ? 159.052 136.816 151.484 1.00 32.85  ? 4025 LEU A CG    1 
ATOM   18887 C  CD1   . LEU A 1 4025 ? 159.457 135.664 152.383 1.00 32.97  ? 4025 LEU A CD1   1 
ATOM   18888 C  CD2   . LEU A 1 4025 ? 158.954 138.109 152.278 1.00 26.24  ? 4025 LEU A CD2   1 
ATOM   18889 N  N     . ASP A 1 4026 ? 158.284 134.262 149.416 1.00 37.65  ? 4026 ASP A N     1 
ATOM   18890 C  CA    . ASP A 1 4026 ? 156.988 133.716 149.014 1.00 39.90  ? 4026 ASP A CA    1 
ATOM   18891 C  C     . ASP A 1 4026 ? 156.016 134.122 150.119 1.00 43.18  ? 4026 ASP A C     1 
ATOM   18892 O  O     . ASP A 1 4026 ? 155.901 133.457 151.149 1.00 45.45  ? 4026 ASP A O     1 
ATOM   18893 C  CB    . ASP A 1 4026 ? 157.088 132.203 148.809 1.00 42.23  ? 4026 ASP A CB    1 
ATOM   18894 C  CG    . ASP A 1 4026 ? 155.728 131.502 148.664 1.00 49.71  ? 4026 ASP A CG    1 
ATOM   18895 O  OD1   . ASP A 1 4026 ? 155.684 130.498 147.924 1.00 54.17  ? 4026 ASP A OD1   1 
ATOM   18896 O  OD2   . ASP A 1 4026 ? 154.713 131.908 149.268 1.00 51.00  ? 4026 ASP A OD2   1 
ATOM   18897 N  N     . LEU A 1 4027 ? 155.324 135.242 149.904 1.00 39.09  ? 4027 LEU A N     1 
ATOM   18898 C  CA    . LEU A 1 4027 ? 154.377 135.726 150.902 1.00 36.47  ? 4027 LEU A CA    1 
ATOM   18899 C  C     . LEU A 1 4027 ? 153.065 134.952 150.862 1.00 38.55  ? 4027 LEU A C     1 
ATOM   18900 O  O     . LEU A 1 4027 ? 152.284 135.011 151.818 1.00 39.88  ? 4027 LEU A O     1 
ATOM   18901 C  CB    . LEU A 1 4027 ? 154.116 137.218 150.699 1.00 34.93  ? 4027 LEU A CB    1 
ATOM   18902 C  CG    . LEU A 1 4027 ? 154.881 138.162 151.627 1.00 36.95  ? 4027 LEU A CG    1 
ATOM   18903 C  CD1   . LEU A 1 4027 ? 154.546 139.612 151.316 1.00 32.96  ? 4027 LEU A CD1   1 
ATOM   18904 C  CD2   . LEU A 1 4027 ? 154.583 137.836 153.080 1.00 31.95  ? 4027 LEU A CD2   1 
ATOM   18905 N  N     . THR A 1 4028 ? 152.803 134.234 149.769 1.00 42.09  ? 4028 THR A N     1 
ATOM   18906 C  CA    . THR A 1 4028 ? 151.553 133.491 149.644 1.00 42.21  ? 4028 THR A CA    1 
ATOM   18907 C  C     . THR A 1 4028 ? 151.452 132.394 150.697 1.00 47.47  ? 4028 THR A C     1 
ATOM   18908 O  O     . THR A 1 4028 ? 150.453 132.299 151.420 1.00 52.30  ? 4028 THR A O     1 
ATOM   18909 C  CB    . THR A 1 4028 ? 151.439 132.898 148.239 1.00 44.48  ? 4028 THR A CB    1 
ATOM   18910 O  OG1   . THR A 1 4028 ? 151.424 133.955 147.271 1.00 44.73  ? 4028 THR A OG1   1 
ATOM   18911 C  CG2   . THR A 1 4028 ? 150.175 132.065 148.106 1.00 46.03  ? 4028 THR A CG2   1 
ATOM   18912 N  N     . HIS A 1 4029 ? 152.481 131.551 150.797 1.00 44.68  ? 4029 HIS A N     1 
ATOM   18913 C  CA    . HIS A 1 4029 ? 152.415 130.406 151.699 1.00 44.68  ? 4029 HIS A CA    1 
ATOM   18914 C  C     . HIS A 1 4029 ? 152.536 130.829 153.158 1.00 45.84  ? 4029 HIS A C     1 
ATOM   18915 O  O     . HIS A 1 4029 ? 151.831 130.297 154.023 1.00 47.92  ? 4029 HIS A O     1 
ATOM   18916 C  CB    . HIS A 1 4029 ? 153.504 129.396 151.340 1.00 43.74  ? 4029 HIS A CB    1 
ATOM   18917 C  CG    . HIS A 1 4029 ? 153.597 128.244 152.291 1.00 58.76  ? 4029 HIS A CG    1 
ATOM   18918 N  ND1   . HIS A 1 4029 ? 152.531 127.412 152.558 1.00 64.16  ? 4029 HIS A ND1   1 
ATOM   18919 C  CD2   . HIS A 1 4029 ? 154.628 127.788 153.041 1.00 56.54  ? 4029 HIS A CD2   1 
ATOM   18920 C  CE1   . HIS A 1 4029 ? 152.902 126.491 153.429 1.00 56.55  ? 4029 HIS A CE1   1 
ATOM   18921 N  NE2   . HIS A 1 4029 ? 154.169 126.697 153.739 1.00 58.86  ? 4029 HIS A NE2   1 
ATOM   18922 N  N     . ILE A 1 4030 ? 153.428 131.778 153.452 1.00 41.41  ? 4030 ILE A N     1 
ATOM   18923 C  CA    . ILE A 1 4030 ? 153.705 132.136 154.842 1.00 40.31  ? 4030 ILE A CA    1 
ATOM   18924 C  C     . ILE A 1 4030 ? 152.483 132.768 155.495 1.00 37.85  ? 4030 ILE A C     1 
ATOM   18925 O  O     . ILE A 1 4030 ? 152.112 132.415 156.622 1.00 37.62  ? 4030 ILE A O     1 
ATOM   18926 C  CB    . ILE A 1 4030 ? 154.931 133.064 154.920 1.00 34.36  ? 4030 ILE A CB    1 
ATOM   18927 C  CG1   . ILE A 1 4030 ? 156.122 132.429 154.201 1.00 33.97  ? 4030 ILE A CG1   1 
ATOM   18928 C  CG2   . ILE A 1 4030 ? 155.276 133.363 156.369 1.00 32.56  ? 4030 ILE A CG2   1 
ATOM   18929 C  CD1   . ILE A 1 4030 ? 157.382 133.257 154.264 1.00 34.23  ? 4030 ILE A CD1   1 
ATOM   18930 N  N     . VAL A 1 4031 ? 151.841 133.714 154.808 1.00 35.95  ? 4031 VAL A N     1 
ATOM   18931 C  CA    . VAL A 1 4031 ? 150.687 134.395 155.388 1.00 37.03  ? 4031 VAL A CA    1 
ATOM   18932 C  C     . VAL A 1 4031 ? 149.518 133.430 155.547 1.00 37.40  ? 4031 VAL A C     1 
ATOM   18933 O  O     . VAL A 1 4031 ? 148.844 133.414 156.584 1.00 32.24  ? 4031 VAL A O     1 
ATOM   18934 C  CB    . VAL A 1 4031 ? 150.305 135.616 154.532 1.00 31.62  ? 4031 VAL A CB    1 
ATOM   18935 C  CG1   . VAL A 1 4031 ? 148.916 136.116 154.900 1.00 27.08  ? 4031 VAL A CG1   1 
ATOM   18936 C  CG2   . VAL A 1 4031 ? 151.335 136.721 154.701 1.00 28.85  ? 4031 VAL A CG2   1 
ATOM   18937 N  N     . GLY A 1 4032 ? 149.265 132.606 154.529 1.00 41.82  ? 4032 GLY A N     1 
ATOM   18938 C  CA    . GLY A 1 4032 ? 148.140 131.689 154.594 1.00 40.39  ? 4032 GLY A CA    1 
ATOM   18939 C  C     . GLY A 1 4032 ? 148.302 130.611 155.649 1.00 43.16  ? 4032 GLY A C     1 
ATOM   18940 O  O     . GLY A 1 4032 ? 147.324 130.195 156.278 1.00 46.82  ? 4032 GLY A O     1 
ATOM   18941 N  N     . THR A 1 4033 ? 149.531 130.142 155.861 1.00 45.01  ? 4033 THR A N     1 
ATOM   18942 C  CA    . THR A 1 4033 ? 149.783 128.989 156.717 1.00 45.87  ? 4033 THR A CA    1 
ATOM   18943 C  C     . THR A 1 4033 ? 150.545 129.326 157.990 1.00 45.64  ? 4033 THR A C     1 
ATOM   18944 O  O     . THR A 1 4033 ? 150.081 129.005 159.089 1.00 44.86  ? 4033 THR A O     1 
ATOM   18945 C  CB    . THR A 1 4033 ? 150.550 127.914 155.933 1.00 47.19  ? 4033 THR A CB    1 
ATOM   18946 O  OG1   . THR A 1 4033 ? 149.885 127.660 154.689 1.00 55.60  ? 4033 THR A OG1   1 
ATOM   18947 C  CG2   . THR A 1 4033 ? 150.627 126.625 156.734 1.00 45.33  ? 4033 THR A CG2   1 
ATOM   18948 N  N     . GLU A 1 4034 ? 151.707 129.965 157.877 1.00 43.46  ? 4034 GLU A N     1 
ATOM   18949 C  CA    . GLU A 1 4034 ? 152.611 130.128 159.009 1.00 38.12  ? 4034 GLU A CA    1 
ATOM   18950 C  C     . GLU A 1 4034 ? 152.252 131.298 159.916 1.00 38.53  ? 4034 GLU A C     1 
ATOM   18951 O  O     . GLU A 1 4034 ? 152.867 131.445 160.977 1.00 39.75  ? 4034 GLU A O     1 
ATOM   18952 C  CB    . GLU A 1 4034 ? 154.050 130.299 158.514 1.00 38.36  ? 4034 GLU A CB    1 
ATOM   18953 C  CG    . GLU A 1 4034 ? 154.516 129.214 157.562 1.00 43.22  ? 4034 GLU A CG    1 
ATOM   18954 C  CD    . GLU A 1 4034 ? 155.993 129.319 157.246 1.00 47.06  ? 4034 GLU A CD    1 
ATOM   18955 O  OE1   . GLU A 1 4034 ? 156.521 130.451 157.235 1.00 41.93  ? 4034 GLU A OE1   1 
ATOM   18956 O  OE2   . GLU A 1 4034 ? 156.627 128.269 157.007 1.00 48.67  ? 4034 GLU A OE2   1 
ATOM   18957 N  N     . VAL A 1 4035 ? 151.285 132.128 159.539 1.00 41.15  ? 4035 VAL A N     1 
ATOM   18958 C  CA    . VAL A 1 4035 ? 150.925 133.312 160.310 1.00 36.32  ? 4035 VAL A CA    1 
ATOM   18959 C  C     . VAL A 1 4035 ? 149.519 133.120 160.859 1.00 37.21  ? 4035 VAL A C     1 
ATOM   18960 O  O     . VAL A 1 4035 ? 148.575 132.880 160.095 1.00 35.92  ? 4035 VAL A O     1 
ATOM   18961 C  CB    . VAL A 1 4035 ? 151.012 134.593 159.466 1.00 30.47  ? 4035 VAL A CB    1 
ATOM   18962 C  CG1   . VAL A 1 4035 ? 150.580 135.797 160.287 1.00 32.20  ? 4035 VAL A CG1   1 
ATOM   18963 C  CG2   . VAL A 1 4035 ? 152.424 134.784 158.941 1.00 31.64  ? 4035 VAL A CG2   1 
ATOM   18964 N  N     . LYS A 1 4036 ? 149.383 133.222 162.178 1.00 34.49  ? 4036 LYS A N     1 
ATOM   18965 C  CA    . LYS A 1 4036 ? 148.079 133.183 162.816 1.00 30.34  ? 4036 LYS A CA    1 
ATOM   18966 C  C     . LYS A 1 4036 ? 147.387 134.539 162.680 1.00 33.08  ? 4036 LYS A C     1 
ATOM   18967 O  O     . LYS A 1 4036 ? 148.051 135.570 162.542 1.00 35.26  ? 4036 LYS A O     1 
ATOM   18968 C  CB    . LYS A 1 4036 ? 148.218 132.818 164.291 1.00 36.34  ? 4036 LYS A CB    1 
ATOM   18969 C  CG    . LYS A 1 4036 ? 148.307 131.323 164.558 1.00 32.45  ? 4036 LYS A CG    1 
ATOM   18970 C  CD    . LYS A 1 4036 ? 149.113 131.037 165.816 1.00 36.03  ? 4036 LYS A CD    1 
ATOM   18971 C  CE    . LYS A 1 4036 ? 149.736 129.652 165.772 1.00 34.78  ? 4036 LYS A CE    1 
ATOM   18972 N  NZ    . LYS A 1 4036 ? 150.667 129.499 164.621 1.00 42.73  ? 4036 LYS A NZ    1 
ATOM   18973 N  N     . PRO A 1 4037 ? 146.052 134.563 162.704 1.00 32.95  ? 4037 PRO A N     1 
ATOM   18974 C  CA    . PRO A 1 4037 ? 145.349 135.853 162.617 1.00 31.78  ? 4037 PRO A CA    1 
ATOM   18975 C  C     . PRO A 1 4037 ? 145.668 136.793 163.764 1.00 30.24  ? 4037 PRO A C     1 
ATOM   18976 O  O     . PRO A 1 4037 ? 145.537 138.013 163.610 1.00 36.14  ? 4037 PRO A O     1 
ATOM   18977 C  CB    . PRO A 1 4037 ? 143.867 135.447 162.611 1.00 31.26  ? 4037 PRO A CB    1 
ATOM   18978 C  CG    . PRO A 1 4037 ? 143.840 134.069 163.182 1.00 29.10  ? 4037 PRO A CG    1 
ATOM   18979 C  CD    . PRO A 1 4037 ? 145.117 133.427 162.749 1.00 29.68  ? 4037 PRO A CD    1 
ATOM   18980 N  N     . ASN A 1 4038 ? 146.084 136.263 164.915 1.00 28.56  ? 4038 ASN A N     1 
ATOM   18981 C  CA    . ASN A 1 4038 ? 146.446 137.114 166.041 1.00 29.45  ? 4038 ASN A CA    1 
ATOM   18982 C  C     . ASN A 1 4038 ? 147.794 137.794 165.843 1.00 31.93  ? 4038 ASN A C     1 
ATOM   18983 O  O     . ASN A 1 4038 ? 148.018 138.874 166.400 1.00 28.75  ? 4038 ASN A O     1 
ATOM   18984 C  CB    . ASN A 1 4038 ? 146.465 136.291 167.329 1.00 33.51  ? 4038 ASN A CB    1 
ATOM   18985 C  CG    . ASN A 1 4038 ? 145.598 136.889 168.413 1.00 38.96  ? 4038 ASN A CG    1 
ATOM   18986 O  OD1   . ASN A 1 4038 ? 145.606 138.099 168.632 1.00 37.29  ? 4038 ASN A OD1   1 
ATOM   18987 N  ND2   . ASN A 1 4038 ? 144.842 136.042 169.102 1.00 42.26  ? 4038 ASN A ND2   1 
ATOM   18988 N  N     . THR A 1 4039 ? 148.691 137.191 165.065 1.00 29.80  ? 4039 THR A N     1 
ATOM   18989 C  CA    . THR A 1 4039 ? 150.041 137.712 164.901 1.00 21.72  ? 4039 THR A CA    1 
ATOM   18990 C  C     . THR A 1 4039 ? 150.078 138.709 163.752 1.00 23.56  ? 4039 THR A C     1 
ATOM   18991 O  O     . THR A 1 4039 ? 149.790 138.328 162.609 1.00 25.46  ? 4039 THR A O     1 
ATOM   18992 C  CB    . THR A 1 4039 ? 151.019 136.581 164.635 1.00 23.96  ? 4039 THR A CB    1 
ATOM   18993 O  OG1   . THR A 1 4039 ? 151.014 135.671 165.742 1.00 35.46  ? 4039 THR A OG1   1 
ATOM   18994 C  CG2   . THR A 1 4039 ? 152.424 137.125 164.437 1.00 16.96  ? 4039 THR A CG2   1 
ATOM   18995 N  N     . PRO A 1 4040 ? 150.414 139.973 163.996 1.00 17.08  ? 4040 PRO A N     1 
ATOM   18996 C  CA    . PRO A 1 4040 ? 150.542 140.926 162.890 1.00 10.59  ? 4040 PRO A CA    1 
ATOM   18997 C  C     . PRO A 1 4040 ? 151.742 140.607 162.016 1.00 12.56  ? 4040 PRO A C     1 
ATOM   18998 O  O     . PRO A 1 4040 ? 152.729 140.015 162.461 1.00 15.39  ? 4040 PRO A O     1 
ATOM   18999 C  CB    . PRO A 1 4040 ? 150.714 142.275 163.599 1.00 11.21  ? 4040 PRO A CB    1 
ATOM   19000 C  CG    . PRO A 1 4040 ? 151.237 141.929 164.951 1.00 11.54  ? 4040 PRO A CG    1 
ATOM   19001 C  CD    . PRO A 1 4040 ? 150.625 140.609 165.308 1.00 15.16  ? 4040 PRO A CD    1 
ATOM   19002 N  N     . VAL A 1 4041 ? 151.646 141.007 160.753 1.00 16.39  ? 4041 VAL A N     1 
ATOM   19003 C  CA    . VAL A 1 4041 ? 152.715 140.818 159.781 1.00 8.33   ? 4041 VAL A CA    1 
ATOM   19004 C  C     . VAL A 1 4041 ? 153.486 142.131 159.707 1.00 8.64   ? 4041 VAL A C     1 
ATOM   19005 O  O     . VAL A 1 4041 ? 153.074 143.071 159.023 1.00 10.80  ? 4041 VAL A O     1 
ATOM   19006 C  CB    . VAL A 1 4041 ? 152.173 140.401 158.412 1.00 8.13   ? 4041 VAL A CB    1 
ATOM   19007 C  CG1   . VAL A 1 4041 ? 153.318 140.095 157.460 1.00 14.91  ? 4041 VAL A CG1   1 
ATOM   19008 C  CG2   . VAL A 1 4041 ? 151.251 139.202 158.548 1.00 11.60  ? 4041 VAL A CG2   1 
ATOM   19009 N  N     . LEU A 1 4042 ? 154.613 142.199 160.411 1.00 11.19  ? 4042 LEU A N     1 
ATOM   19010 C  CA    . LEU A 1 4042 ? 155.462 143.385 160.409 1.00 8.89   ? 4042 LEU A CA    1 
ATOM   19011 C  C     . LEU A 1 4042 ? 156.382 143.319 159.197 1.00 10.14  ? 4042 LEU A C     1 
ATOM   19012 O  O     . LEU A 1 4042 ? 157.248 142.443 159.111 1.00 10.87  ? 4042 LEU A O     1 
ATOM   19013 C  CB    . LEU A 1 4042 ? 156.262 143.485 161.705 1.00 10.86  ? 4042 LEU A CB    1 
ATOM   19014 C  CG    . LEU A 1 4042 ? 155.502 143.194 162.999 1.00 13.10  ? 4042 LEU A CG    1 
ATOM   19015 C  CD1   . LEU A 1 4042 ? 156.411 143.380 164.198 1.00 15.64  ? 4042 LEU A CD1   1 
ATOM   19016 C  CD2   . LEU A 1 4042 ? 154.279 144.087 163.114 1.00 12.07  ? 4042 LEU A CD2   1 
ATOM   19017 N  N     . MET A 1 4043 ? 156.195 144.246 158.261 1.00 14.13  ? 4043 MET A N     1 
ATOM   19018 C  CA    . MET A 1 4043 ? 156.934 144.251 157.002 1.00 11.63  ? 4043 MET A CA    1 
ATOM   19019 C  C     . MET A 1 4043 ? 157.897 145.432 157.045 1.00 11.46  ? 4043 MET A C     1 
ATOM   19020 O  O     . MET A 1 4043 ? 157.589 146.517 156.546 1.00 14.68  ? 4043 MET A O     1 
ATOM   19021 C  CB    . MET A 1 4043 ? 155.977 144.341 155.818 1.00 11.81  ? 4043 MET A CB    1 
ATOM   19022 C  CG    . MET A 1 4043 ? 154.861 143.307 155.861 1.00 16.04  ? 4043 MET A CG    1 
ATOM   19023 S  SD    . MET A 1 4043 ? 154.601 142.392 154.334 1.00 55.61  ? 4043 MET A SD    1 
ATOM   19024 C  CE    . MET A 1 4043 ? 155.704 141.007 154.595 1.00 28.15  ? 4043 MET A CE    1 
ATOM   19025 N  N     . CYS A 1 4044 ? 159.069 145.214 157.634 1.00 13.74  ? 4044 CYS A N     1 
ATOM   19026 C  CA    . CYS A 1 4044 ? 160.046 146.271 157.861 1.00 12.67  ? 4044 CYS A CA    1 
ATOM   19027 C  C     . CYS A 1 4044 ? 161.039 146.307 156.708 1.00 13.13  ? 4044 CYS A C     1 
ATOM   19028 O  O     . CYS A 1 4044 ? 161.525 145.260 156.270 1.00 12.01  ? 4044 CYS A O     1 
ATOM   19029 C  CB    . CYS A 1 4044 ? 160.778 146.056 159.186 1.00 15.00  ? 4044 CYS A CB    1 
ATOM   19030 S  SG    . CYS A 1 4044 ? 159.725 145.486 160.538 1.00 21.33  ? 4044 CYS A SG    1 
ATOM   19031 N  N     . SER A 1 4045 ? 161.337 147.509 156.220 1.00 16.20  ? 4045 SER A N     1 
ATOM   19032 C  CA    . SER A 1 4045 ? 162.193 147.679 155.057 1.00 16.62  ? 4045 SER A CA    1 
ATOM   19033 C  C     . SER A 1 4045 ? 163.223 148.771 155.306 1.00 19.06  ? 4045 SER A C     1 
ATOM   19034 O  O     . SER A 1 4045 ? 162.997 149.698 156.088 1.00 19.42  ? 4045 SER A O     1 
ATOM   19035 C  CB    . SER A 1 4045 ? 161.372 148.019 153.806 1.00 18.63  ? 4045 SER A CB    1 
ATOM   19036 O  OG    . SER A 1 4045 ? 160.125 147.346 153.819 1.00 21.75  ? 4045 SER A OG    1 
ATOM   19037 N  N     . VAL A 1 4046 ? 164.362 148.643 154.633 1.00 27.46  ? 4046 VAL A N     1 
ATOM   19038 C  CA    . VAL A 1 4046 ? 165.398 149.672 154.625 1.00 28.26  ? 4046 VAL A CA    1 
ATOM   19039 C  C     . VAL A 1 4046 ? 164.899 150.835 153.774 1.00 30.60  ? 4046 VAL A C     1 
ATOM   19040 O  O     . VAL A 1 4046 ? 163.976 150.649 152.967 1.00 31.60  ? 4046 VAL A O     1 
ATOM   19041 C  CB    . VAL A 1 4046 ? 166.731 149.115 154.100 1.00 20.50  ? 4046 VAL A CB    1 
ATOM   19042 C  CG1   . VAL A 1 4046 ? 167.213 147.978 154.986 1.00 19.30  ? 4046 VAL A CG1   1 
ATOM   19043 C  CG2   . VAL A 1 4046 ? 166.582 148.648 152.662 1.00 21.16  ? 4046 VAL A CG2   1 
ATOM   19044 N  N     . PRO A 1 4047 ? 165.446 152.043 153.928 1.00 29.31  ? 4047 PRO A N     1 
ATOM   19045 C  CA    . PRO A 1 4047 ? 164.986 153.166 153.101 1.00 28.20  ? 4047 PRO A CA    1 
ATOM   19046 C  C     . PRO A 1 4047 ? 165.155 152.875 151.617 1.00 33.36  ? 4047 PRO A C     1 
ATOM   19047 O  O     . PRO A 1 4047 ? 166.130 152.252 151.191 1.00 30.34  ? 4047 PRO A O     1 
ATOM   19048 C  CB    . PRO A 1 4047 ? 165.876 154.327 153.554 1.00 30.48  ? 4047 PRO A CB    1 
ATOM   19049 C  CG    . PRO A 1 4047 ? 166.267 153.973 154.946 1.00 32.37  ? 4047 PRO A CG    1 
ATOM   19050 C  CD    . PRO A 1 4047 ? 166.400 152.478 154.963 1.00 31.28  ? 4047 PRO A CD    1 
ATOM   19051 N  N     . GLY A 1 4048 ? 164.187 153.338 150.828 1.00 37.66  ? 4048 GLY A N     1 
ATOM   19052 C  CA    . GLY A 1 4048 ? 164.139 153.051 149.412 1.00 36.45  ? 4048 GLY A CA    1 
ATOM   19053 C  C     . GLY A 1 4048 ? 163.366 151.805 149.039 1.00 30.67  ? 4048 GLY A C     1 
ATOM   19054 O  O     . GLY A 1 4048 ? 163.182 151.544 147.844 1.00 33.53  ? 4048 GLY A O     1 
ATOM   19055 N  N     . TYR A 1 4049 ? 162.910 151.028 150.018 1.00 29.62  ? 4049 TYR A N     1 
ATOM   19056 C  CA    . TYR A 1 4049 ? 162.119 149.830 149.779 1.00 31.10  ? 4049 TYR A CA    1 
ATOM   19057 C  C     . TYR A 1 4049 ? 160.790 149.938 150.512 1.00 35.80  ? 4049 TYR A C     1 
ATOM   19058 O  O     . TYR A 1 4049 ? 160.742 150.339 151.679 1.00 40.09  ? 4049 TYR A O     1 
ATOM   19059 C  CB    . TYR A 1 4049 ? 162.873 148.571 150.220 1.00 23.15  ? 4049 TYR A CB    1 
ATOM   19060 C  CG    . TYR A 1 4049 ? 163.848 148.078 149.178 1.00 26.49  ? 4049 TYR A CG    1 
ATOM   19061 C  CD1   . TYR A 1 4049 ? 165.026 148.765 148.922 1.00 27.04  ? 4049 TYR A CD1   1 
ATOM   19062 C  CD2   . TYR A 1 4049 ? 163.582 146.934 148.438 1.00 22.61  ? 4049 TYR A CD2   1 
ATOM   19063 C  CE1   . TYR A 1 4049 ? 165.915 148.325 147.963 1.00 23.72  ? 4049 TYR A CE1   1 
ATOM   19064 C  CE2   . TYR A 1 4049 ? 164.466 146.485 147.478 1.00 28.20  ? 4049 TYR A CE2   1 
ATOM   19065 C  CZ    . TYR A 1 4049 ? 165.631 147.185 147.245 1.00 30.78  ? 4049 TYR A CZ    1 
ATOM   19066 O  OH    . TYR A 1 4049 ? 166.514 146.743 146.289 1.00 36.19  ? 4049 TYR A OH    1 
ATOM   19067 N  N     . ASP A 1 4050 ? 159.711 149.588 149.816 1.00 31.80  ? 4050 ASP A N     1 
ATOM   19068 C  CA    . ASP A 1 4050 ? 158.365 149.669 150.368 1.00 30.30  ? 4050 ASP A CA    1 
ATOM   19069 C  C     . ASP A 1 4050 ? 157.631 148.381 150.037 1.00 31.38  ? 4050 ASP A C     1 
ATOM   19070 O  O     . ASP A 1 4050 ? 157.444 148.057 148.861 1.00 30.11  ? 4050 ASP A O     1 
ATOM   19071 C  CB    . ASP A 1 4050 ? 157.613 150.883 149.814 1.00 32.68  ? 4050 ASP A CB    1 
ATOM   19072 C  CG    . ASP A 1 4050 ? 156.157 150.910 150.231 1.00 35.60  ? 4050 ASP A CG    1 
ATOM   19073 O  OD1   . ASP A 1 4050 ? 155.881 150.781 151.442 1.00 33.49  ? 4050 ASP A OD1   1 
ATOM   19074 O  OD2   . ASP A 1 4050 ? 155.288 151.065 149.349 1.00 33.45  ? 4050 ASP A OD2   1 
ATOM   19075 N  N     . ALA A 1 4051 ? 157.216 147.652 151.070 1.00 31.88  ? 4051 ALA A N     1 
ATOM   19076 C  CA    . ALA A 1 4051 ? 156.538 146.375 150.900 1.00 26.71  ? 4051 ALA A CA    1 
ATOM   19077 C  C     . ALA A 1 4051 ? 155.029 146.514 150.772 1.00 29.51  ? 4051 ALA A C     1 
ATOM   19078 O  O     . ALA A 1 4051 ? 154.333 145.495 150.704 1.00 35.65  ? 4051 ALA A O     1 
ATOM   19079 C  CB    . ALA A 1 4051 ? 156.869 145.442 152.069 1.00 27.48  ? 4051 ALA A CB    1 
ATOM   19080 N  N     . SER A 1 4052 ? 154.506 147.743 150.749 1.00 27.38  ? 4052 SER A N     1 
ATOM   19081 C  CA    . SER A 1 4052 ? 153.070 147.931 150.565 1.00 25.49  ? 4052 SER A CA    1 
ATOM   19082 C  C     . SER A 1 4052 ? 152.611 147.361 149.230 1.00 27.47  ? 4052 SER A C     1 
ATOM   19083 O  O     . SER A 1 4052 ? 151.514 146.799 149.130 1.00 30.52  ? 4052 SER A O     1 
ATOM   19084 C  CB    . SER A 1 4052 ? 152.715 149.414 150.670 1.00 26.70  ? 4052 SER A CB    1 
ATOM   19085 O  OG    . SER A 1 4052 ? 153.532 150.066 151.626 1.00 36.52  ? 4052 SER A OG    1 
ATOM   19086 N  N     . GLY A 1 4053 ? 153.435 147.502 148.191 1.00 26.82  ? 4053 GLY A N     1 
ATOM   19087 C  CA    . GLY A 1 4053 ? 153.098 146.910 146.907 1.00 28.41  ? 4053 GLY A CA    1 
ATOM   19088 C  C     . GLY A 1 4053 ? 153.026 145.396 146.963 1.00 30.41  ? 4053 GLY A C     1 
ATOM   19089 O  O     . GLY A 1 4053 ? 152.211 144.779 146.274 1.00 35.57  ? 4053 GLY A O     1 
ATOM   19090 N  N     . HIS A 1 4054 ? 153.879 144.777 147.782 1.00 30.99  ? 4054 HIS A N     1 
ATOM   19091 C  CA    . HIS A 1 4054 ? 153.846 143.324 147.922 1.00 30.04  ? 4054 HIS A CA    1 
ATOM   19092 C  C     . HIS A 1 4054 ? 152.505 142.859 148.473 1.00 29.30  ? 4054 HIS A C     1 
ATOM   19093 O  O     . HIS A 1 4054 ? 151.933 141.871 148.000 1.00 30.62  ? 4054 HIS A O     1 
ATOM   19094 C  CB    . HIS A 1 4054 ? 154.989 142.857 148.824 1.00 32.30  ? 4054 HIS A CB    1 
ATOM   19095 C  CG    . HIS A 1 4054 ? 156.344 142.987 148.202 1.00 35.03  ? 4054 HIS A CG    1 
ATOM   19096 N  ND1   . HIS A 1 4054 ? 157.203 141.919 148.062 1.00 35.61  ? 4054 HIS A ND1   1 
ATOM   19097 C  CD2   . HIS A 1 4054 ? 156.990 144.059 147.686 1.00 36.11  ? 4054 HIS A CD2   1 
ATOM   19098 C  CE1   . HIS A 1 4054 ? 158.319 142.326 147.484 1.00 40.46  ? 4054 HIS A CE1   1 
ATOM   19099 N  NE2   . HIS A 1 4054 ? 158.216 143.621 147.246 1.00 39.97  ? 4054 HIS A NE2   1 
ATOM   19100 N  N     . VAL A 1 4055 ? 151.986 143.566 149.478 1.00 30.84  ? 4055 VAL A N     1 
ATOM   19101 C  CA    . VAL A 1 4055 ? 150.714 143.181 150.078 1.00 31.45  ? 4055 VAL A CA    1 
ATOM   19102 C  C     . VAL A 1 4055 ? 149.565 143.428 149.108 1.00 32.18  ? 4055 VAL A C     1 
ATOM   19103 O  O     . VAL A 1 4055 ? 148.626 142.627 149.022 1.00 34.25  ? 4055 VAL A O     1 
ATOM   19104 C  CB    . VAL A 1 4055 ? 150.507 143.922 151.411 1.00 23.89  ? 4055 VAL A CB    1 
ATOM   19105 C  CG1   . VAL A 1 4055 ? 149.346 143.315 152.177 1.00 20.32  ? 4055 VAL A CG1   1 
ATOM   19106 C  CG2   . VAL A 1 4055 ? 151.780 143.881 152.244 1.00 25.60  ? 4055 VAL A CG2   1 
ATOM   19107 N  N     . GLU A 1 4056 ? 149.612 144.541 148.369 1.00 29.31  ? 4056 GLU A N     1 
ATOM   19108 C  CA    . GLU A 1 4056 ? 148.554 144.831 147.404 1.00 27.52  ? 4056 GLU A CA    1 
ATOM   19109 C  C     . GLU A 1 4056 ? 148.494 143.771 146.311 1.00 34.38  ? 4056 GLU A C     1 
ATOM   19110 O  O     . GLU A 1 4056 ? 147.409 143.293 145.959 1.00 39.98  ? 4056 GLU A O     1 
ATOM   19111 C  CB    . GLU A 1 4056 ? 148.760 146.215 146.789 1.00 34.07  ? 4056 GLU A CB    1 
ATOM   19112 C  CG    . GLU A 1 4056 ? 148.160 147.363 147.587 1.00 39.84  ? 4056 GLU A CG    1 
ATOM   19113 C  CD    . GLU A 1 4056 ? 149.155 148.477 147.849 1.00 43.40  ? 4056 GLU A CD    1 
ATOM   19114 O  OE1   . GLU A 1 4056 ? 149.899 148.844 146.914 1.00 33.08  ? 4056 GLU A OE1   1 
ATOM   19115 O  OE2   . GLU A 1 4056 ? 149.189 148.992 148.985 1.00 43.66  ? 4056 GLU A OE2   1 
ATOM   19116 N  N     . ASP A 1 4057 ? 149.650 143.394 145.759 1.00 32.90  ? 4057 ASP A N     1 
ATOM   19117 C  CA    . ASP A 1 4057 ? 149.677 142.338 144.751 1.00 34.27  ? 4057 ASP A CA    1 
ATOM   19118 C  C     . ASP A 1 4057 ? 149.273 140.994 145.343 1.00 37.96  ? 4057 ASP A C     1 
ATOM   19119 O  O     . ASP A 1 4057 ? 148.553 140.218 144.704 1.00 43.38  ? 4057 ASP A O     1 
ATOM   19120 C  CB    . ASP A 1 4057 ? 151.063 142.255 144.113 1.00 35.67  ? 4057 ASP A CB    1 
ATOM   19121 C  CG    . ASP A 1 4057 ? 151.466 143.546 143.427 1.00 45.69  ? 4057 ASP A CG    1 
ATOM   19122 O  OD1   . ASP A 1 4057 ? 152.222 143.481 142.435 1.00 52.19  ? 4057 ASP A OD1   1 
ATOM   19123 O  OD2   . ASP A 1 4057 ? 151.009 144.624 143.861 1.00 39.44  ? 4057 ASP A OD2   1 
ATOM   19124 N  N     . LEU A 1 4058 ? 149.732 140.696 146.561 1.00 32.62  ? 4058 LEU A N     1 
ATOM   19125 C  CA    . LEU A 1 4058 ? 149.364 139.434 147.197 1.00 34.58  ? 4058 LEU A CA    1 
ATOM   19126 C  C     . LEU A 1 4058 ? 147.865 139.365 147.457 1.00 34.38  ? 4058 LEU A C     1 
ATOM   19127 O  O     . LEU A 1 4058 ? 147.240 138.319 147.248 1.00 38.82  ? 4058 LEU A O     1 
ATOM   19128 C  CB    . LEU A 1 4058 ? 150.145 139.254 148.499 1.00 36.53  ? 4058 LEU A CB    1 
ATOM   19129 C  CG    . LEU A 1 4058 ? 149.694 138.126 149.430 1.00 33.38  ? 4058 LEU A CG    1 
ATOM   19130 C  CD1   . LEU A 1 4058 ? 149.844 136.776 148.749 1.00 33.18  ? 4058 LEU A CD1   1 
ATOM   19131 C  CD2   . LEU A 1 4058 ? 150.472 138.160 150.735 1.00 34.07  ? 4058 LEU A CD2   1 
ATOM   19132 N  N     . ALA A 1 4059 ? 147.271 140.470 147.913 1.00 34.54  ? 4059 ALA A N     1 
ATOM   19133 C  CA    . ALA A 1 4059 ? 145.838 140.481 148.187 1.00 37.15  ? 4059 ALA A CA    1 
ATOM   19134 C  C     . ALA A 1 4059 ? 145.030 140.285 146.912 1.00 42.40  ? 4059 ALA A C     1 
ATOM   19135 O  O     . ALA A 1 4059 ? 144.003 139.595 146.918 1.00 43.22  ? 4059 ALA A O     1 
ATOM   19136 C  CB    . ALA A 1 4059 ? 145.445 141.786 148.877 1.00 33.24  ? 4059 ALA A CB    1 
ATOM   19137 N  N     . ALA A 1 4060 ? 145.472 140.893 145.809 1.00 40.26  ? 4060 ALA A N     1 
ATOM   19138 C  CA    . ALA A 1 4060 ? 144.762 140.738 144.543 1.00 44.57  ? 4060 ALA A CA    1 
ATOM   19139 C  C     . ALA A 1 4060 ? 144.823 139.299 144.046 1.00 50.46  ? 4060 ALA A C     1 
ATOM   19140 O  O     . ALA A 1 4060 ? 143.845 138.785 143.491 1.00 53.38  ? 4060 ALA A O     1 
ATOM   19141 C  CB    . ALA A 1 4060 ? 145.340 141.690 143.497 1.00 34.59  ? 4060 ALA A CB    1 
ATOM   19142 N  N     . GLU A 1 4061 ? 145.967 138.637 144.228 1.00 46.04  ? 4061 GLU A N     1 
ATOM   19143 C  CA    . GLU A 1 4061 ? 146.134 137.291 143.690 1.00 45.84  ? 4061 GLU A CA    1 
ATOM   19144 C  C     . GLU A 1 4061 ? 145.258 136.288 144.436 1.00 49.09  ? 4061 GLU A C     1 
ATOM   19145 O  O     . GLU A 1 4061 ? 144.748 135.334 143.836 1.00 51.21  ? 4061 GLU A O     1 
ATOM   19146 C  CB    . GLU A 1 4061 ? 147.622 136.914 143.717 1.00 46.88  ? 4061 GLU A CB    1 
ATOM   19147 C  CG    . GLU A 1 4061 ? 148.005 135.433 143.567 1.00 52.20  ? 4061 GLU A CG    1 
ATOM   19148 C  CD    . GLU A 1 4061 ? 147.664 134.575 144.770 1.00 59.54  ? 4061 GLU A CD    1 
ATOM   19149 O  OE1   . GLU A 1 4061 ? 146.863 133.629 144.623 1.00 59.56  ? 4061 GLU A OE1   1 
ATOM   19150 O  OE2   . GLU A 1 4061 ? 148.200 134.850 145.862 1.00 59.24  ? 4061 GLU A OE2   1 
ATOM   19151 N  N     . GLN A 1 4062 ? 145.069 136.484 145.740 1.00 50.08  ? 4062 GLN A N     1 
ATOM   19152 C  CA    . GLN A 1 4062 ? 144.107 135.701 146.508 1.00 50.92  ? 4062 GLN A CA    1 
ATOM   19153 C  C     . GLN A 1 4062 ? 142.675 136.180 146.328 1.00 50.66  ? 4062 GLN A C     1 
ATOM   19154 O  O     . GLN A 1 4062 ? 141.755 135.538 146.847 1.00 48.50  ? 4062 GLN A O     1 
ATOM   19155 C  CB    . GLN A 1 4062 ? 144.451 135.730 148.003 1.00 49.64  ? 4062 GLN A CB    1 
ATOM   19156 C  CG    . GLN A 1 4062 ? 145.919 135.582 148.337 1.00 48.73  ? 4062 GLN A CG    1 
ATOM   19157 C  CD    . GLN A 1 4062 ? 146.387 134.144 148.254 1.00 52.85  ? 4062 GLN A CD    1 
ATOM   19158 O  OE1   . GLN A 1 4062 ? 147.584 133.869 148.275 1.00 54.23  ? 4062 GLN A OE1   1 
ATOM   19159 N  NE2   . GLN A 1 4062 ? 145.441 133.216 148.172 1.00 48.04  ? 4062 GLN A NE2   1 
ATOM   19160 N  N     . ASN A 1 4063 ? 142.469 137.289 145.616 1.00 52.23  ? 4063 ASN A N     1 
ATOM   19161 C  CA    . ASN A 1 4063 ? 141.151 137.906 145.465 1.00 51.37  ? 4063 ASN A CA    1 
ATOM   19162 C  C     . ASN A 1 4063 ? 140.533 138.219 146.826 1.00 53.57  ? 4063 ASN A C     1 
ATOM   19163 O  O     . ASN A 1 4063 ? 139.328 138.065 147.034 1.00 58.23  ? 4063 ASN A O     1 
ATOM   19164 C  CB    . ASN A 1 4063 ? 140.217 137.027 144.629 1.00 54.94  ? 4063 ASN A CB    1 
ATOM   19165 C  CG    . ASN A 1 4063 ? 140.852 136.577 143.329 1.00 59.82  ? 4063 ASN A CG    1 
ATOM   19166 O  OD1   . ASN A 1 4063 ? 141.013 135.381 143.086 1.00 57.68  ? 4063 ASN A OD1   1 
ATOM   19167 N  ND2   . ASN A 1 4063 ? 141.221 137.535 142.487 1.00 59.71  ? 4063 ASN A ND2   1 
ATOM   19168 N  N     . THR A 1 4064 ? 141.370 138.659 147.761 1.00 48.75  ? 4064 THR A N     1 
ATOM   19169 C  CA    . THR A 1 4064 ? 140.934 139.057 149.092 1.00 44.83  ? 4064 THR A CA    1 
ATOM   19170 C  C     . THR A 1 4064 ? 140.937 140.575 149.179 1.00 44.48  ? 4064 THR A C     1 
ATOM   19171 O  O     . THR A 1 4064 ? 141.966 141.213 148.929 1.00 46.02  ? 4064 THR A O     1 
ATOM   19172 C  CB    . THR A 1 4064 ? 141.843 138.466 150.174 1.00 44.78  ? 4064 THR A CB    1 
ATOM   19173 O  OG1   . THR A 1 4064 ? 142.093 137.084 149.891 1.00 49.83  ? 4064 THR A OG1   1 
ATOM   19174 C  CG2   . THR A 1 4064 ? 141.190 138.589 151.541 1.00 36.51  ? 4064 THR A CG2   1 
ATOM   19175 N  N     . GLN A 1 4065 ? 139.789 141.149 149.528 1.00 46.04  ? 4065 GLN A N     1 
ATOM   19176 C  CA    . GLN A 1 4065 ? 139.687 142.596 149.648 1.00 42.21  ? 4065 GLN A CA    1 
ATOM   19177 C  C     . GLN A 1 4065 ? 140.499 143.076 150.843 1.00 37.94  ? 4065 GLN A C     1 
ATOM   19178 O  O     . GLN A 1 4065 ? 140.442 142.483 151.925 1.00 36.19  ? 4065 GLN A O     1 
ATOM   19179 C  CB    . GLN A 1 4065 ? 138.225 143.017 149.788 1.00 44.34  ? 4065 GLN A CB    1 
ATOM   19180 C  CG    . GLN A 1 4065 ? 137.460 143.091 148.473 1.00 54.91  ? 4065 GLN A CG    1 
ATOM   19181 C  CD    . GLN A 1 4065 ? 137.356 141.749 147.773 1.00 62.74  ? 4065 GLN A CD    1 
ATOM   19182 O  OE1   . GLN A 1 4065 ? 138.115 141.457 146.849 1.00 56.96  ? 4065 GLN A OE1   1 
ATOM   19183 N  NE2   . GLN A 1 4065 ? 136.412 140.924 148.212 1.00 62.09  ? 4065 GLN A NE2   1 
ATOM   19184 N  N     . ILE A 1 4066 ? 141.259 144.150 150.647 1.00 32.18  ? 4066 ILE A N     1 
ATOM   19185 C  CA    . ILE A 1 4066 ? 142.164 144.669 151.664 1.00 25.37  ? 4066 ILE A CA    1 
ATOM   19186 C  C     . ILE A 1 4066 ? 141.874 146.149 151.870 1.00 27.44  ? 4066 ILE A C     1 
ATOM   19187 O  O     . ILE A 1 4066 ? 141.688 146.894 150.901 1.00 33.87  ? 4066 ILE A O     1 
ATOM   19188 C  CB    . ILE A 1 4066 ? 143.641 144.448 151.280 1.00 26.43  ? 4066 ILE A CB    1 
ATOM   19189 C  CG1   . ILE A 1 4066 ? 144.569 145.070 152.324 1.00 26.69  ? 4066 ILE A CG1   1 
ATOM   19190 C  CG2   . ILE A 1 4066 ? 143.936 145.002 149.893 1.00 26.08  ? 4066 ILE A CG2   1 
ATOM   19191 C  CD1   . ILE A 1 4066 ? 146.022 144.736 152.114 1.00 26.47  ? 4066 ILE A CD1   1 
ATOM   19192 N  N     . THR A 1 4067 ? 141.814 146.568 153.132 1.00 22.67  ? 4067 THR A N     1 
ATOM   19193 C  CA    . THR A 1 4067 ? 141.670 147.972 153.492 1.00 22.85  ? 4067 THR A CA    1 
ATOM   19194 C  C     . THR A 1 4067 ? 143.046 148.499 153.882 1.00 21.23  ? 4067 THR A C     1 
ATOM   19195 O  O     . THR A 1 4067 ? 143.623 148.066 154.885 1.00 19.41  ? 4067 THR A O     1 
ATOM   19196 C  CB    . THR A 1 4067 ? 140.668 148.147 154.632 1.00 24.86  ? 4067 THR A CB    1 
ATOM   19197 O  OG1   . THR A 1 4067 ? 139.362 147.755 154.189 1.00 31.73  ? 4067 THR A OG1   1 
ATOM   19198 C  CG2   . THR A 1 4067 ? 140.629 149.597 155.088 1.00 21.11  ? 4067 THR A CG2   1 
ATOM   19199 N  N     . SER A 1 4068 ? 143.572 149.427 153.089 1.00 20.95  ? 4068 SER A N     1 
ATOM   19200 C  CA    . SER A 1 4068 ? 144.894 149.994 153.315 1.00 14.03  ? 4068 SER A CA    1 
ATOM   19201 C  C     . SER A 1 4068 ? 144.756 151.418 153.834 1.00 16.16  ? 4068 SER A C     1 
ATOM   19202 O  O     . SER A 1 4068 ? 144.018 152.225 153.259 1.00 21.94  ? 4068 SER A O     1 
ATOM   19203 C  CB    . SER A 1 4068 ? 145.724 149.975 152.031 1.00 14.63  ? 4068 SER A CB    1 
ATOM   19204 O  OG    . SER A 1 4068 ? 145.738 148.682 151.454 1.00 23.61  ? 4068 SER A OG    1 
ATOM   19205 N  N     . ILE A 1 4069 ? 145.465 151.722 154.918 1.00 12.90  ? 4069 ILE A N     1 
ATOM   19206 C  CA    . ILE A 1 4069 ? 145.400 153.024 155.569 1.00 12.67  ? 4069 ILE A CA    1 
ATOM   19207 C  C     . ILE A 1 4069 ? 146.821 153.517 155.799 1.00 16.30  ? 4069 ILE A C     1 
ATOM   19208 O  O     . ILE A 1 4069 ? 147.691 152.745 156.217 1.00 18.69  ? 4069 ILE A O     1 
ATOM   19209 C  CB    . ILE A 1 4069 ? 144.623 152.958 156.898 1.00 15.18  ? 4069 ILE A CB    1 
ATOM   19210 C  CG1   . ILE A 1 4069 ? 143.157 152.610 156.639 1.00 16.31  ? 4069 ILE A CG1   1 
ATOM   19211 C  CG2   . ILE A 1 4069 ? 144.721 154.275 157.651 1.00 18.70  ? 4069 ILE A CG2   1 
ATOM   19212 C  CD1   . ILE A 1 4069 ? 142.531 151.764 157.719 1.00 16.05  ? 4069 ILE A CD1   1 
ATOM   19213 N  N     . ALA A 1 4070 ? 147.055 154.797 155.519 1.00 14.44  ? 4070 ALA A N     1 
ATOM   19214 C  CA    . ALA A 1 4070 ? 148.341 155.434 155.763 1.00 10.56  ? 4070 ALA A CA    1 
ATOM   19215 C  C     . ALA A 1 4070 ? 148.293 156.138 157.113 1.00 14.36  ? 4070 ALA A C     1 
ATOM   19216 O  O     . ALA A 1 4070 ? 147.404 156.959 157.359 1.00 17.29  ? 4070 ALA A O     1 
ATOM   19217 C  CB    . ALA A 1 4070 ? 148.682 156.422 154.649 1.00 16.56  ? 4070 ALA A CB    1 
ATOM   19218 N  N     . ILE A 1 4071 ? 149.247 155.817 157.977 1.00 17.15  ? 4071 ILE A N     1 
ATOM   19219 C  CA    . ILE A 1 4071 ? 149.280 156.350 159.333 1.00 16.56  ? 4071 ILE A CA    1 
ATOM   19220 C  C     . ILE A 1 4071 ? 149.843 157.765 159.312 1.00 14.44  ? 4071 ILE A C     1 
ATOM   19221 O  O     . ILE A 1 4071 ? 150.701 158.104 158.490 1.00 15.52  ? 4071 ILE A O     1 
ATOM   19222 C  CB    . ILE A 1 4071 ? 150.107 155.416 160.242 1.00 13.45  ? 4071 ILE A CB    1 
ATOM   19223 C  CG1   . ILE A 1 4071 ? 149.433 154.048 160.355 1.00 11.35  ? 4071 ILE A CG1   1 
ATOM   19224 C  CG2   . ILE A 1 4071 ? 150.300 156.010 161.629 1.00 17.51  ? 4071 ILE A CG2   1 
ATOM   19225 C  CD1   . ILE A 1 4071 ? 147.968 154.115 160.711 1.00 15.36  ? 4071 ILE A CD1   1 
ATOM   19226 N  N     . GLY A 1 4072 ? 149.354 158.607 160.222 1.00 16.97  ? 4072 GLY A N     1 
ATOM   19227 C  CA    . GLY A 1 4072 ? 149.919 159.931 160.385 1.00 16.48  ? 4072 GLY A CA    1 
ATOM   19228 C  C     . GLY A 1 4072 ? 148.941 161.032 160.742 1.00 19.15  ? 4072 GLY A C     1 
ATOM   19229 O  O     . GLY A 1 4072 ? 149.349 162.079 161.251 1.00 19.75  ? 4072 GLY A O     1 
ATOM   19230 N  N     . SER A 1 4073 ? 147.653 160.818 160.490 1.00 20.04  ? 4073 SER A N     1 
ATOM   19231 C  CA    . SER A 1 4073 ? 146.635 161.813 160.790 1.00 19.26  ? 4073 SER A CA    1 
ATOM   19232 C  C     . SER A 1 4073 ? 145.708 161.290 161.879 1.00 24.94  ? 4073 SER A C     1 
ATOM   19233 O  O     . SER A 1 4073 ? 145.619 160.084 162.124 1.00 30.46  ? 4073 SER A O     1 
ATOM   19234 C  CB    . SER A 1 4073 ? 145.821 162.188 159.543 1.00 21.69  ? 4073 SER A CB    1 
ATOM   19235 O  OG    . SER A 1 4073 ? 145.356 161.034 158.865 1.00 21.29  ? 4073 SER A OG    1 
ATOM   19236 N  N     . ALA A 1 4074 ? 145.020 162.224 162.540 1.00 22.57  ? 4074 ALA A N     1 
ATOM   19237 C  CA    . ALA A 1 4074 ? 144.050 161.849 163.563 1.00 25.63  ? 4074 ALA A CA    1 
ATOM   19238 C  C     . ALA A 1 4074 ? 142.905 161.047 162.957 1.00 28.62  ? 4074 ALA A C     1 
ATOM   19239 O  O     . ALA A 1 4074 ? 142.418 160.083 163.558 1.00 29.25  ? 4074 ALA A O     1 
ATOM   19240 C  CB    . ALA A 1 4074 ? 143.523 163.098 164.270 1.00 24.43  ? 4074 ALA A CB    1 
ATOM   19241 N  N     . GLU A 1 4075 ? 142.460 161.439 161.761 1.00 26.73  ? 4075 GLU A N     1 
ATOM   19242 C  CA    . GLU A 1 4075 ? 141.410 160.693 161.079 1.00 30.02  ? 4075 GLU A CA    1 
ATOM   19243 C  C     . GLU A 1 4075 ? 141.887 159.298 160.692 1.00 31.13  ? 4075 GLU A C     1 
ATOM   19244 O  O     . GLU A 1 4075 ? 141.089 158.353 160.665 1.00 34.14  ? 4075 GLU A O     1 
ATOM   19245 C  CB    . GLU A 1 4075 ? 140.945 161.476 159.847 1.00 32.65  ? 4075 GLU A CB    1 
ATOM   19246 C  CG    . GLU A 1 4075 ? 140.380 160.638 158.712 1.00 39.35  ? 4075 GLU A CG    1 
ATOM   19247 C  CD    . GLU A 1 4075 ? 138.937 160.238 158.953 1.00 47.24  ? 4075 GLU A CD    1 
ATOM   19248 O  OE1   . GLU A 1 4075 ? 138.051 161.105 158.811 1.00 45.49  ? 4075 GLU A OE1   1 
ATOM   19249 O  OE2   . GLU A 1 4075 ? 138.686 159.065 159.294 1.00 48.02  ? 4075 GLU A OE2   1 
ATOM   19250 N  N     . GLY A 1 4076 ? 143.184 159.146 160.412 1.00 29.97  ? 4076 GLY A N     1 
ATOM   19251 C  CA    . GLY A 1 4076 ? 143.705 157.844 160.026 1.00 24.73  ? 4076 GLY A CA    1 
ATOM   19252 C  C     . GLY A 1 4076 ? 143.635 156.821 161.144 1.00 28.40  ? 4076 GLY A C     1 
ATOM   19253 O  O     . GLY A 1 4076 ? 143.351 155.645 160.903 1.00 28.58  ? 4076 GLY A O     1 
ATOM   19254 N  N     . PHE A 1 4077 ? 143.904 157.250 162.380 1.00 30.10  ? 4077 PHE A N     1 
ATOM   19255 C  CA    . PHE A 1 4077 ? 143.774 156.346 163.520 1.00 25.83  ? 4077 PHE A CA    1 
ATOM   19256 C  C     . PHE A 1 4077 ? 142.335 155.879 163.689 1.00 26.59  ? 4077 PHE A C     1 
ATOM   19257 O  O     . PHE A 1 4077 ? 142.088 154.717 164.033 1.00 32.51  ? 4077 PHE A O     1 
ATOM   19258 C  CB    . PHE A 1 4077 ? 144.274 157.023 164.796 1.00 23.20  ? 4077 PHE A CB    1 
ATOM   19259 C  CG    . PHE A 1 4077 ? 145.734 157.370 164.769 1.00 25.24  ? 4077 PHE A CG    1 
ATOM   19260 C  CD1   . PHE A 1 4077 ? 146.677 156.425 164.402 1.00 26.69  ? 4077 PHE A CD1   1 
ATOM   19261 C  CD2   . PHE A 1 4077 ? 146.166 158.639 165.117 1.00 26.64  ? 4077 PHE A CD2   1 
ATOM   19262 C  CE1   . PHE A 1 4077 ? 148.021 156.739 164.379 1.00 26.14  ? 4077 PHE A CE1   1 
ATOM   19263 C  CE2   . PHE A 1 4077 ? 147.509 158.959 165.096 1.00 25.90  ? 4077 PHE A CE2   1 
ATOM   19264 C  CZ    . PHE A 1 4077 ? 148.438 158.007 164.727 1.00 25.26  ? 4077 PHE A CZ    1 
ATOM   19265 N  N     . ASN A 1 4078 ? 141.371 156.774 163.463 1.00 25.09  ? 4078 ASN A N     1 
ATOM   19266 C  CA    . ASN A 1 4078 ? 139.968 156.377 163.518 1.00 28.63  ? 4078 ASN A CA    1 
ATOM   19267 C  C     . ASN A 1 4078 ? 139.648 155.343 162.446 1.00 31.21  ? 4078 ASN A C     1 
ATOM   19268 O  O     . ASN A 1 4078 ? 138.935 154.367 162.708 1.00 32.00  ? 4078 ASN A O     1 
ATOM   19269 C  CB    . ASN A 1 4078 ? 139.071 157.605 163.367 1.00 35.35  ? 4078 ASN A CB    1 
ATOM   19270 C  CG    . ASN A 1 4078 ? 139.119 158.512 164.579 1.00 39.38  ? 4078 ASN A CG    1 
ATOM   19271 O  OD1   . ASN A 1 4078 ? 139.391 158.064 165.693 1.00 38.73  ? 4078 ASN A OD1   1 
ATOM   19272 N  ND2   . ASN A 1 4078 ? 138.858 159.796 164.367 1.00 37.32  ? 4078 ASN A ND2   1 
ATOM   19273 N  N     . GLN A 1 4079 ? 140.162 155.542 161.230 1.00 33.32  ? 4079 GLN A N     1 
ATOM   19274 C  CA    . GLN A 1 4079 ? 139.960 154.557 160.173 1.00 31.08  ? 4079 GLN A CA    1 
ATOM   19275 C  C     . GLN A 1 4079 ? 140.646 153.240 160.508 1.00 29.13  ? 4079 GLN A C     1 
ATOM   19276 O  O     . GLN A 1 4079 ? 140.090 152.163 160.266 1.00 29.10  ? 4079 GLN A O     1 
ATOM   19277 C  CB    . GLN A 1 4079 ? 140.471 155.098 158.837 1.00 28.61  ? 4079 GLN A CB    1 
ATOM   19278 C  CG    . GLN A 1 4079 ? 139.716 156.300 158.251 1.00 37.75  ? 4079 GLN A CG    1 
ATOM   19279 C  CD    . GLN A 1 4079 ? 138.222 156.069 158.016 1.00 53.17  ? 4079 GLN A CD    1 
ATOM   19280 O  OE1   . GLN A 1 4079 ? 137.497 155.575 158.881 1.00 48.43  ? 4079 GLN A OE1   1 
ATOM   19281 N  NE2   . GLN A 1 4079 ? 137.760 156.436 156.826 1.00 56.03  ? 4079 GLN A NE2   1 
ATOM   19282 N  N     . ALA A 1 4080 ? 141.859 153.307 161.062 1.00 29.04  ? 4080 ALA A N     1 
ATOM   19283 C  CA    . ALA A 1 4080 ? 142.589 152.091 161.401 1.00 23.66  ? 4080 ALA A CA    1 
ATOM   19284 C  C     . ALA A 1 4080 ? 141.844 151.280 162.453 1.00 28.05  ? 4080 ALA A C     1 
ATOM   19285 O  O     . ALA A 1 4080 ? 141.721 150.056 162.338 1.00 32.71  ? 4080 ALA A O     1 
ATOM   19286 C  CB    . ALA A 1 4080 ? 143.996 152.442 161.885 1.00 24.63  ? 4080 ALA A CB    1 
ATOM   19287 N  N     . ASP A 1 4081 ? 141.336 151.951 163.489 1.00 29.98  ? 4081 ASP A N     1 
ATOM   19288 C  CA    . ASP A 1 4081 ? 140.589 151.251 164.529 1.00 26.55  ? 4081 ASP A CA    1 
ATOM   19289 C  C     . ASP A 1 4081 ? 139.301 150.655 163.974 1.00 28.51  ? 4081 ASP A C     1 
ATOM   19290 O  O     . ASP A 1 4081 ? 138.944 149.515 164.291 1.00 28.99  ? 4081 ASP A O     1 
ATOM   19291 C  CB    . ASP A 1 4081 ? 140.292 152.202 165.688 1.00 30.84  ? 4081 ASP A CB    1 
ATOM   19292 C  CG    . ASP A 1 4081 ? 141.545 152.623 166.432 1.00 47.22  ? 4081 ASP A CG    1 
ATOM   19293 O  OD1   . ASP A 1 4081 ? 142.655 152.298 165.960 1.00 43.73  ? 4081 ASP A OD1   1 
ATOM   19294 O  OD2   . ASP A 1 4081 ? 141.420 153.279 167.488 1.00 54.36  ? 4081 ASP A OD2   1 
ATOM   19295 N  N     . LYS A 1 4082 ? 138.588 151.418 163.142 1.00 27.58  ? 4082 LYS A N     1 
ATOM   19296 C  CA    . LYS A 1 4082 ? 137.348 150.916 162.557 1.00 23.87  ? 4082 LYS A CA    1 
ATOM   19297 C  C     . LYS A 1 4082 ? 137.612 149.752 161.610 1.00 26.23  ? 4082 LYS A C     1 
ATOM   19298 O  O     . LYS A 1 4082 ? 136.882 148.753 161.625 1.00 29.37  ? 4082 LYS A O     1 
ATOM   19299 C  CB    . LYS A 1 4082 ? 136.616 152.042 161.828 1.00 29.97  ? 4082 LYS A CB    1 
ATOM   19300 C  CG    . LYS A 1 4082 ? 135.478 152.660 162.623 1.00 38.10  ? 4082 LYS A CG    1 
ATOM   19301 C  CD    . LYS A 1 4082 ? 135.145 154.053 162.117 1.00 38.16  ? 4082 LYS A CD    1 
ATOM   19302 C  CE    . LYS A 1 4082 ? 135.622 155.123 163.084 1.00 39.45  ? 4082 LYS A CE    1 
ATOM   19303 N  NZ    . LYS A 1 4082 ? 135.680 156.465 162.440 1.00 41.50  ? 4082 LYS A NZ    1 
ATOM   19304 N  N     . ALA A 1 4083 ? 138.648 149.864 160.774 1.00 28.68  ? 4083 ALA A N     1 
ATOM   19305 C  CA    . ALA A 1 4083 ? 138.950 148.800 159.821 1.00 25.32  ? 4083 ALA A CA    1 
ATOM   19306 C  C     . ALA A 1 4083 ? 139.351 147.514 160.531 1.00 29.05  ? 4083 ALA A C     1 
ATOM   19307 O  O     . ALA A 1 4083 ? 138.933 146.422 160.130 1.00 31.81  ? 4083 ALA A O     1 
ATOM   19308 C  CB    . ALA A 1 4083 ? 140.052 149.248 158.862 1.00 21.15  ? 4083 ALA A CB    1 
ATOM   19309 N  N     . ILE A 1 4084 ? 140.167 147.621 161.582 1.00 25.59  ? 4084 ILE A N     1 
ATOM   19310 C  CA    . ILE A 1 4084 ? 140.568 146.436 162.336 1.00 24.35  ? 4084 ILE A CA    1 
ATOM   19311 C  C     . ILE A 1 4084 ? 139.356 145.785 162.990 1.00 28.92  ? 4084 ILE A C     1 
ATOM   19312 O  O     . ILE A 1 4084 ? 139.190 144.561 162.942 1.00 30.54  ? 4084 ILE A O     1 
ATOM   19313 C  CB    . ILE A 1 4084 ? 141.648 146.801 163.371 1.00 27.59  ? 4084 ILE A CB    1 
ATOM   19314 C  CG1   . ILE A 1 4084 ? 142.968 147.127 162.669 1.00 24.53  ? 4084 ILE A CG1   1 
ATOM   19315 C  CG2   . ILE A 1 4084 ? 141.838 145.671 164.372 1.00 25.96  ? 4084 ILE A CG2   1 
ATOM   19316 C  CD1   . ILE A 1 4084 ? 143.959 147.857 163.543 1.00 17.22  ? 4084 ILE A CD1   1 
ATOM   19317 N  N     . ASN A 1 4085 ? 138.483 146.593 163.598 1.00 31.53  ? 4085 ASN A N     1 
ATOM   19318 C  CA    . ASN A 1 4085 ? 137.303 146.046 164.262 1.00 24.64  ? 4085 ASN A CA    1 
ATOM   19319 C  C     . ASN A 1 4085 ? 136.402 145.312 163.277 1.00 26.36  ? 4085 ASN A C     1 
ATOM   19320 O  O     . ASN A 1 4085 ? 135.879 144.235 163.586 1.00 29.02  ? 4085 ASN A O     1 
ATOM   19321 C  CB    . ASN A 1 4085 ? 136.531 147.163 164.963 1.00 22.91  ? 4085 ASN A CB    1 
ATOM   19322 C  CG    . ASN A 1 4085 ? 137.213 147.638 166.228 1.00 25.50  ? 4085 ASN A CG    1 
ATOM   19323 O  OD1   . ASN A 1 4085 ? 138.085 146.959 166.769 1.00 26.70  ? 4085 ASN A OD1   1 
ATOM   19324 N  ND2   . ASN A 1 4085 ? 136.819 148.811 166.706 1.00 26.54  ? 4085 ASN A ND2   1 
ATOM   19325 N  N     . THR A 1 4086 ? 136.201 145.884 162.089 1.00 28.86  ? 4086 THR A N     1 
ATOM   19326 C  CA    . THR A 1 4086 ? 135.372 145.230 161.082 1.00 28.29  ? 4086 THR A CA    1 
ATOM   19327 C  C     . THR A 1 4086 ? 136.029 143.958 160.558 1.00 30.94  ? 4086 THR A C     1 
ATOM   19328 O  O     . THR A 1 4086 ? 135.353 142.944 160.350 1.00 34.16  ? 4086 THR A O     1 
ATOM   19329 C  CB    . THR A 1 4086 ? 135.084 146.196 159.933 1.00 26.46  ? 4086 THR A CB    1 
ATOM   19330 O  OG1   . THR A 1 4086 ? 134.526 147.409 160.453 1.00 33.27  ? 4086 THR A OG1   1 
ATOM   19331 C  CG2   . THR A 1 4086 ? 134.105 145.578 158.946 1.00 30.50  ? 4086 THR A CG2   1 
ATOM   19332 N  N     . ALA A 1 4087 ? 137.346 143.992 160.342 1.00 31.54  ? 4087 ALA A N     1 
ATOM   19333 C  CA    . ALA A 1 4087 ? 138.029 142.878 159.694 1.00 27.33  ? 4087 ALA A CA    1 
ATOM   19334 C  C     . ALA A 1 4087 ? 138.145 141.651 160.591 1.00 30.44  ? 4087 ALA A C     1 
ATOM   19335 O  O     . ALA A 1 4087 ? 138.064 140.523 160.093 1.00 30.44  ? 4087 ALA A O     1 
ATOM   19336 C  CB    . ALA A 1 4087 ? 139.417 143.314 159.229 1.00 23.12  ? 4087 ALA A CB    1 
ATOM   19337 N  N     . VAL A 1 4088 ? 138.341 141.839 161.899 1.00 25.97  ? 4088 VAL A N     1 
ATOM   19338 C  CA    . VAL A 1 4088 ? 138.479 140.695 162.795 1.00 27.49  ? 4088 VAL A CA    1 
ATOM   19339 C  C     . VAL A 1 4088 ? 137.190 139.892 162.893 1.00 34.50  ? 4088 VAL A C     1 
ATOM   19340 O  O     . VAL A 1 4088 ? 137.214 138.739 163.336 1.00 36.55  ? 4088 VAL A O     1 
ATOM   19341 C  CB    . VAL A 1 4088 ? 138.949 141.151 164.192 1.00 28.90  ? 4088 VAL A CB    1 
ATOM   19342 C  CG1   . VAL A 1 4088 ? 140.272 141.890 164.089 1.00 24.45  ? 4088 VAL A CG1   1 
ATOM   19343 C  CG2   . VAL A 1 4088 ? 137.894 142.023 164.852 1.00 33.05  ? 4088 VAL A CG2   1 
ATOM   19344 N  N     . LYS A 1 4089 ? 136.061 140.471 162.491 1.00 30.86  ? 4089 LYS A N     1 
ATOM   19345 C  CA    . LYS A 1 4089 ? 134.794 139.755 162.434 1.00 33.50  ? 4089 LYS A CA    1 
ATOM   19346 C  C     . LYS A 1 4089 ? 134.487 139.212 161.046 1.00 36.97  ? 4089 LYS A C     1 
ATOM   19347 O  O     . LYS A 1 4089 ? 133.921 138.122 160.922 1.00 41.47  ? 4089 LYS A O     1 
ATOM   19348 C  CB    . LYS A 1 4089 ? 133.648 140.666 162.887 1.00 35.54  ? 4089 LYS A CB    1 
ATOM   19349 C  CG    . LYS A 1 4089 ? 133.312 140.560 164.366 1.00 42.59  ? 4089 LYS A CG    1 
ATOM   19350 C  CD    . LYS A 1 4089 ? 133.139 141.932 164.994 1.00 43.87  ? 4089 LYS A CD    1 
ATOM   19351 C  CE    . LYS A 1 4089 ? 132.411 141.841 166.326 1.00 47.83  ? 4089 LYS A CE    1 
ATOM   19352 N  NZ    . LYS A 1 4089 ? 133.052 140.861 167.245 1.00 48.35  ? 4089 LYS A NZ    1 
ATOM   19353 N  N     . SER A 1 4090 ? 134.854 139.949 159.996 1.00 32.61  ? 4090 SER A N     1 
ATOM   19354 C  CA    . SER A 1 4090 ? 134.549 139.543 158.631 1.00 34.65  ? 4090 SER A CA    1 
ATOM   19355 C  C     . SER A 1 4090 ? 135.666 138.736 157.980 1.00 39.34  ? 4090 SER A C     1 
ATOM   19356 O  O     . SER A 1 4090 ? 135.400 137.996 157.026 1.00 36.65  ? 4090 SER A O     1 
ATOM   19357 C  CB    . SER A 1 4090 ? 134.238 140.777 157.785 1.00 35.86  ? 4090 SER A CB    1 
ATOM   19358 O  OG    . SER A 1 4090 ? 135.388 141.589 157.641 1.00 36.79  ? 4090 SER A OG    1 
ATOM   19359 N  N     . GLY A 1 4091 ? 136.901 138.858 158.463 1.00 37.92  ? 4091 GLY A N     1 
ATOM   19360 C  CA    . GLY A 1 4091 ? 137.997 138.089 157.907 1.00 32.59  ? 4091 GLY A CA    1 
ATOM   19361 C  C     . GLY A 1 4091 ? 138.751 138.752 156.779 1.00 31.30  ? 4091 GLY A C     1 
ATOM   19362 O  O     . GLY A 1 4091 ? 139.507 138.076 156.074 1.00 30.52  ? 4091 GLY A O     1 
ATOM   19363 N  N     . ARG A 1 4092 ? 138.567 140.066 156.631 1.00 31.69  ? 4092 ARG A N     1 
ATOM   19364 C  CA    . ARG A 1 4092 ? 139.254 140.830 155.559 1.00 27.17  ? 4092 ARG A CA    1 
ATOM   19365 C  C     . ARG A 1 4092 ? 140.730 141.040 155.922 1.00 26.77  ? 4092 ARG A C     1 
ATOM   19366 O  O     . ARG A 1 4092 ? 141.160 140.544 156.987 1.00 25.28  ? 4092 ARG A O     1 
ATOM   19367 C  CB    . ARG A 1 4092 ? 138.580 142.195 155.396 1.00 29.64  ? 4092 ARG A CB    1 
ATOM   19368 C  CG    . ARG A 1 4092 ? 137.235 142.176 154.687 1.00 35.17  ? 4092 ARG A CG    1 
ATOM   19369 C  CD    . ARG A 1 4092 ? 137.417 142.490 153.213 1.00 44.02  ? 4092 ARG A CD    1 
ATOM   19370 N  NE    . ARG A 1 4092 ? 138.267 143.674 153.040 1.00 57.06  ? 4092 ARG A NE    1 
ATOM   19371 C  CZ    . ARG A 1 4092 ? 137.882 144.804 152.463 1.00 50.02  ? 4092 ARG A CZ    1 
ATOM   19372 N  NH1   . ARG A 1 4092 ? 136.623 144.964 152.099 1.00 43.41  ? 4092 ARG A NH1   1 
ATOM   19373 N  NH2   . ARG A 1 4092 ? 138.758 145.770 152.253 1.00 41.42  ? 4092 ARG A NH2   1 
ATOM   19374 N  N     . TRP A 1 4093 ? 141.469 141.751 155.067 1.00 27.70  ? 4093 TRP A N     1 
ATOM   19375 C  CA    . TRP A 1 4093 ? 142.897 142.051 155.343 1.00 19.61  ? 4093 TRP A CA    1 
ATOM   19376 C  C     . TRP A 1 4093 ? 143.055 143.557 155.544 1.00 17.93  ? 4093 TRP A C     1 
ATOM   19377 O  O     . TRP A 1 4093 ? 142.524 144.330 154.720 1.00 22.03  ? 4093 TRP A O     1 
ATOM   19378 C  CB    . TRP A 1 4093 ? 143.770 141.558 154.182 1.00 19.69  ? 4093 TRP A CB    1 
ATOM   19379 C  CG    . TRP A 1 4093 ? 144.017 140.074 154.183 1.00 18.64  ? 4093 TRP A CG    1 
ATOM   19380 C  CD1   . TRP A 1 4093 ? 143.332 139.123 154.880 1.00 18.34  ? 4093 TRP A CD1   1 
ATOM   19381 C  CD2   . TRP A 1 4093 ? 145.012 139.367 153.411 1.00 21.18  ? 4093 TRP A CD2   1 
ATOM   19382 N  NE1   . TRP A 1 4093 ? 143.843 137.880 154.615 1.00 20.09  ? 4093 TRP A NE1   1 
ATOM   19383 C  CE2   . TRP A 1 4093 ? 144.869 137.996 153.715 1.00 21.59  ? 4093 TRP A CE2   1 
ATOM   19384 C  CE3   . TRP A 1 4093 ? 146.003 139.757 152.503 1.00 25.10  ? 4093 TRP A CE3   1 
ATOM   19385 C  CZ2   . TRP A 1 4093 ? 145.681 137.021 153.142 1.00 25.46  ? 4093 TRP A CZ2   1 
ATOM   19386 C  CZ3   . TRP A 1 4093 ? 146.804 138.790 151.937 1.00 23.71  ? 4093 TRP A CZ3   1 
ATOM   19387 C  CH2   . TRP A 1 4093 ? 146.643 137.442 152.253 1.00 25.83  ? 4093 TRP A CH2   1 
ATOM   19388 N  N     . VAL A 1 4094 ? 143.750 143.960 156.609 1.00 12.37  ? 4094 VAL A N     1 
ATOM   19389 C  CA    . VAL A 1 4094 ? 143.994 145.413 156.858 1.00 14.64  ? 4094 VAL A CA    1 
ATOM   19390 C  C     . VAL A 1 4094 ? 145.506 145.671 156.777 1.00 14.51  ? 4094 VAL A C     1 
ATOM   19391 O  O     . VAL A 1 4094 ? 146.268 144.937 157.443 1.00 11.46  ? 4094 VAL A O     1 
ATOM   19392 C  CB    . VAL A 1 4094 ? 143.420 145.887 158.208 1.00 13.84  ? 4094 VAL A CB    1 
ATOM   19393 C  CG1   . VAL A 1 4094 ? 143.813 147.327 158.515 1.00 12.34  ? 4094 VAL A CG1   1 
ATOM   19394 C  CG2   . VAL A 1 4094 ? 141.907 145.717 158.271 1.00 19.48  ? 4094 VAL A CG2   1 
ATOM   19395 N  N     . MET A 1 4095 ? 145.915 146.667 155.989 1.00 12.68  ? 4095 MET A N     1 
ATOM   19396 C  CA    . MET A 1 4095 ? 147.353 147.027 155.912 1.00 7.81   ? 4095 MET A CA    1 
ATOM   19397 C  C     . MET A 1 4095 ? 147.543 148.461 156.424 1.00 7.13   ? 4095 MET A C     1 
ATOM   19398 O  O     . MET A 1 4095 ? 146.893 149.375 155.876 1.00 9.71   ? 4095 MET A O     1 
ATOM   19399 C  CB    . MET A 1 4095 ? 147.885 146.918 154.479 1.00 14.86  ? 4095 MET A CB    1 
ATOM   19400 C  CG    . MET A 1 4095 ? 149.269 147.511 154.300 1.00 16.43  ? 4095 MET A CG    1 
ATOM   19401 S  SD    . MET A 1 4095 ? 150.040 147.063 152.732 1.00 42.92  ? 4095 MET A SD    1 
ATOM   19402 C  CE    . MET A 1 4095 ? 148.701 147.413 151.586 1.00 28.67  ? 4095 MET A CE    1 
ATOM   19403 N  N     . LEU A 1 4096 ? 148.390 148.639 157.440 1.00 9.05   ? 4096 LEU A N     1 
ATOM   19404 C  CA    . LEU A 1 4096 ? 148.692 149.997 157.961 1.00 8.16   ? 4096 LEU A CA    1 
ATOM   19405 C  C     . LEU A 1 4096 ? 150.126 150.347 157.543 1.00 8.77   ? 4096 LEU A C     1 
ATOM   19406 O  O     . LEU A 1 4096 ? 151.042 149.562 157.872 1.00 10.97  ? 4096 LEU A O     1 
ATOM   19407 C  CB    . LEU A 1 4096 ? 148.499 150.003 159.475 1.00 8.12   ? 4096 LEU A CB    1 
ATOM   19408 C  CG    . LEU A 1 4096 ? 147.139 149.496 159.965 1.00 8.01   ? 4096 LEU A CG    1 
ATOM   19409 C  CD1   . LEU A 1 4096 ? 147.063 149.477 161.480 1.00 13.67  ? 4096 LEU A CD1   1 
ATOM   19410 C  CD2   . LEU A 1 4096 ? 146.011 150.328 159.380 1.00 9.47   ? 4096 LEU A CD2   1 
ATOM   19411 N  N     . LYS A 1 4097 ? 150.316 151.471 156.848 1.00 8.44   ? 4097 LYS A N     1 
ATOM   19412 C  CA    . LYS A 1 4097 ? 151.663 151.793 156.306 1.00 9.05   ? 4097 LYS A CA    1 
ATOM   19413 C  C     . LYS A 1 4097 ? 152.376 152.846 157.164 1.00 8.00   ? 4097 LYS A C     1 
ATOM   19414 O  O     . LYS A 1 4097 ? 151.679 153.622 157.854 1.00 12.71  ? 4097 LYS A O     1 
ATOM   19415 C  CB    . LYS A 1 4097 ? 151.508 152.288 154.864 1.00 12.35  ? 4097 LYS A CB    1 
ATOM   19416 C  CG    . LYS A 1 4097 ? 150.688 151.373 153.965 1.00 10.49  ? 4097 LYS A CG    1 
ATOM   19417 C  CD    . LYS A 1 4097 ? 150.429 151.962 152.584 1.00 13.11  ? 4097 LYS A CD    1 
ATOM   19418 C  CE    . LYS A 1 4097 ? 149.552 151.085 151.749 1.00 26.13  ? 4097 LYS A CE    1 
ATOM   19419 N  NZ    . LYS A 1 4097 ? 149.287 151.678 150.435 1.00 23.66  ? 4097 LYS A NZ    1 
ATOM   19420 N  N     . ASN A 1 4098 ? 153.711 152.864 157.116 1.00 7.39   ? 4098 ASN A N     1 
ATOM   19421 C  CA    . ASN A 1 4098 ? 154.506 153.882 157.859 1.00 10.02  ? 4098 ASN A CA    1 
ATOM   19422 C  C     . ASN A 1 4098 ? 154.035 153.950 159.314 1.00 9.55   ? 4098 ASN A C     1 
ATOM   19423 O  O     . ASN A 1 4098 ? 153.857 155.077 159.825 1.00 13.09  ? 4098 ASN A O     1 
ATOM   19424 C  CB    . ASN A 1 4098 ? 154.440 155.242 157.174 1.00 12.79  ? 4098 ASN A CB    1 
ATOM   19425 C  CG    . ASN A 1 4098 ? 154.693 155.143 155.689 1.00 10.21  ? 4098 ASN A CG    1 
ATOM   19426 O  OD1   . ASN A 1 4098 ? 155.764 154.692 155.270 1.00 12.09  ? 4098 ASN A OD1   1 
ATOM   19427 N  ND2   . ASN A 1 4098 ? 153.726 155.554 154.882 1.00 9.79   ? 4098 ASN A ND2   1 
ATOM   19428 N  N     . VAL A 1 4099 ? 153.849 152.794 159.956 1.00 10.26  ? 4099 VAL A N     1 
ATOM   19429 C  CA    . VAL A 1 4099 ? 153.447 152.793 161.358 1.00 9.59   ? 4099 VAL A CA    1 
ATOM   19430 C  C     . VAL A 1 4099 ? 154.573 153.206 162.291 1.00 12.24  ? 4099 VAL A C     1 
ATOM   19431 O  O     . VAL A 1 4099 ? 154.325 153.433 163.481 1.00 15.85  ? 4099 VAL A O     1 
ATOM   19432 C  CB    . VAL A 1 4099 ? 152.913 151.405 161.764 1.00 8.38   ? 4099 VAL A CB    1 
ATOM   19433 C  CG1   . VAL A 1 4099 ? 151.671 151.063 160.958 1.00 6.25   ? 4099 VAL A CG1   1 
ATOM   19434 C  CG2   . VAL A 1 4099 ? 153.986 150.347 161.577 1.00 11.97  ? 4099 VAL A CG2   1 
ATOM   19435 N  N     . HIS A 1 4100 ? 155.802 153.316 161.785 1.00 13.54  ? 4100 HIS A N     1 
ATOM   19436 C  CA    . HIS A 1 4100 ? 156.915 153.791 162.595 1.00 9.68   ? 4100 HIS A CA    1 
ATOM   19437 C  C     . HIS A 1 4100 ? 156.795 155.266 162.951 1.00 10.67  ? 4100 HIS A C     1 
ATOM   19438 O  O     . HIS A 1 4100 ? 157.550 155.742 163.805 1.00 17.67  ? 4100 HIS A O     1 
ATOM   19439 C  CB    . HIS A 1 4100 ? 158.238 153.544 161.868 1.00 12.24  ? 4100 HIS A CB    1 
ATOM   19440 C  CG    . HIS A 1 4100 ? 158.375 154.308 160.588 1.00 14.69  ? 4100 HIS A CG    1 
ATOM   19441 N  ND1   . HIS A 1 4100 ? 157.792 153.895 159.409 1.00 12.79  ? 4100 HIS A ND1   1 
ATOM   19442 C  CD2   . HIS A 1 4100 ? 159.025 155.460 160.302 1.00 16.21  ? 4100 HIS A CD2   1 
ATOM   19443 C  CE1   . HIS A 1 4100 ? 158.079 154.760 158.452 1.00 11.65  ? 4100 HIS A CE1   1 
ATOM   19444 N  NE2   . HIS A 1 4100 ? 158.827 155.719 158.968 1.00 14.04  ? 4100 HIS A NE2   1 
ATOM   19445 N  N     . LEU A 1 4101 ? 155.874 155.996 162.321 1.00 11.65  ? 4101 LEU A N     1 
ATOM   19446 C  CA    . LEU A 1 4101 ? 155.688 157.410 162.611 1.00 12.71  ? 4101 LEU A CA    1 
ATOM   19447 C  C     . LEU A 1 4101 ? 154.789 157.658 163.813 1.00 17.47  ? 4101 LEU A C     1 
ATOM   19448 O  O     . LEU A 1 4101 ? 154.645 158.812 164.229 1.00 17.67  ? 4101 LEU A O     1 
ATOM   19449 C  CB    . LEU A 1 4101 ? 155.115 158.125 161.385 1.00 13.23  ? 4101 LEU A CB    1 
ATOM   19450 C  CG    . LEU A 1 4101 ? 155.967 158.059 160.117 1.00 11.02  ? 4101 LEU A CG    1 
ATOM   19451 C  CD1   . LEU A 1 4101 ? 155.141 158.410 158.891 1.00 13.68  ? 4101 LEU A CD1   1 
ATOM   19452 C  CD2   . LEU A 1 4101 ? 157.176 158.974 160.236 1.00 12.21  ? 4101 LEU A CD2   1 
ATOM   19453 N  N     . ALA A 1 4102 ? 154.183 156.614 164.377 1.00 22.06  ? 4102 ALA A N     1 
ATOM   19454 C  CA    . ALA A 1 4102 ? 153.339 156.726 165.566 1.00 17.62  ? 4102 ALA A CA    1 
ATOM   19455 C  C     . ALA A 1 4102 ? 153.747 155.645 166.558 1.00 21.30  ? 4102 ALA A C     1 
ATOM   19456 O  O     . ALA A 1 4102 ? 153.023 154.660 166.753 1.00 23.18  ? 4102 ALA A O     1 
ATOM   19457 C  CB    . ALA A 1 4102 ? 151.857 156.616 165.206 1.00 23.88  ? 4102 ALA A CB    1 
ATOM   19458 N  N     . PRO A 1 4103 ? 154.915 155.790 167.195 1.00 27.45  ? 4103 PRO A N     1 
ATOM   19459 C  CA    . PRO A 1 4103 ? 155.326 154.775 168.180 1.00 26.76  ? 4103 PRO A CA    1 
ATOM   19460 C  C     . PRO A 1 4103 ? 154.368 154.651 169.351 1.00 23.69  ? 4103 PRO A C     1 
ATOM   19461 O  O     . PRO A 1 4103 ? 154.173 153.545 169.870 1.00 28.82  ? 4103 PRO A O     1 
ATOM   19462 C  CB    . PRO A 1 4103 ? 156.714 155.259 168.626 1.00 23.81  ? 4103 PRO A CB    1 
ATOM   19463 C  CG    . PRO A 1 4103 ? 156.747 156.709 168.288 1.00 23.51  ? 4103 PRO A CG    1 
ATOM   19464 C  CD    . PRO A 1 4103 ? 155.898 156.878 167.070 1.00 19.96  ? 4103 PRO A CD    1 
ATOM   19465 N  N     . GLY A 1 4104 ? 153.765 155.759 169.786 1.00 21.16  ? 4104 GLY A N     1 
ATOM   19466 C  CA    . GLY A 1 4104 ? 152.829 155.690 170.897 1.00 24.44  ? 4104 GLY A CA    1 
ATOM   19467 C  C     . GLY A 1 4104 ? 151.574 154.909 170.561 1.00 27.61  ? 4104 GLY A C     1 
ATOM   19468 O  O     . GLY A 1 4104 ? 151.107 154.092 171.358 1.00 30.27  ? 4104 GLY A O     1 
ATOM   19469 N  N     . TRP A 1 4105 ? 151.008 155.152 169.376 1.00 28.70  ? 4105 TRP A N     1 
ATOM   19470 C  CA    . TRP A 1 4105 ? 149.824 154.412 168.955 1.00 26.01  ? 4105 TRP A CA    1 
ATOM   19471 C  C     . TRP A 1 4105 ? 150.141 152.942 168.712 1.00 24.71  ? 4105 TRP A C     1 
ATOM   19472 O  O     . TRP A 1 4105 ? 149.248 152.090 168.796 1.00 24.87  ? 4105 TRP A O     1 
ATOM   19473 C  CB    . TRP A 1 4105 ? 149.232 155.053 167.698 1.00 23.24  ? 4105 TRP A CB    1 
ATOM   19474 C  CG    . TRP A 1 4105 ? 148.115 154.272 167.081 1.00 25.28  ? 4105 TRP A CG    1 
ATOM   19475 C  CD1   . TRP A 1 4105 ? 146.803 154.285 167.450 1.00 26.80  ? 4105 TRP A CD1   1 
ATOM   19476 C  CD2   . TRP A 1 4105 ? 148.213 153.364 165.979 1.00 24.83  ? 4105 TRP A CD2   1 
ATOM   19477 N  NE1   . TRP A 1 4105 ? 146.076 153.439 166.649 1.00 25.87  ? 4105 TRP A NE1   1 
ATOM   19478 C  CE2   . TRP A 1 4105 ? 146.919 152.861 165.737 1.00 23.35  ? 4105 TRP A CE2   1 
ATOM   19479 C  CE3   . TRP A 1 4105 ? 149.269 152.925 165.175 1.00 24.77  ? 4105 TRP A CE3   1 
ATOM   19480 C  CZ2   . TRP A 1 4105 ? 146.654 151.943 164.725 1.00 25.58  ? 4105 TRP A CZ2   1 
ATOM   19481 C  CZ3   . TRP A 1 4105 ? 149.003 152.015 164.172 1.00 19.52  ? 4105 TRP A CZ3   1 
ATOM   19482 C  CH2   . TRP A 1 4105 ? 147.706 151.533 163.955 1.00 20.67  ? 4105 TRP A CH2   1 
ATOM   19483 N  N     . LEU A 1 4106 ? 151.403 152.625 168.415 1.00 22.13  ? 4106 LEU A N     1 
ATOM   19484 C  CA    . LEU A 1 4106 ? 151.785 151.236 168.186 1.00 23.99  ? 4106 LEU A CA    1 
ATOM   19485 C  C     . LEU A 1 4106 ? 151.708 150.421 169.472 1.00 28.03  ? 4106 LEU A C     1 
ATOM   19486 O  O     . LEU A 1 4106 ? 151.350 149.238 169.442 1.00 29.22  ? 4106 LEU A O     1 
ATOM   19487 C  CB    . LEU A 1 4106 ? 153.190 151.174 167.588 1.00 25.18  ? 4106 LEU A CB    1 
ATOM   19488 C  CG    . LEU A 1 4106 ? 153.266 151.184 166.060 1.00 21.07  ? 4106 LEU A CG    1 
ATOM   19489 C  CD1   . LEU A 1 4106 ? 154.673 150.858 165.589 1.00 20.32  ? 4106 LEU A CD1   1 
ATOM   19490 C  CD2   . LEU A 1 4106 ? 152.262 150.210 165.467 1.00 16.53  ? 4106 LEU A CD2   1 
ATOM   19491 N  N     . MET A 1 4107 ? 152.051 151.032 170.609 1.00 28.53  ? 4107 MET A N     1 
ATOM   19492 C  CA    . MET A 1 4107 ? 151.918 150.342 171.888 1.00 26.77  ? 4107 MET A CA    1 
ATOM   19493 C  C     . MET A 1 4107 ? 150.457 150.038 172.198 1.00 26.77  ? 4107 MET A C     1 
ATOM   19494 O  O     . MET A 1 4107 ? 150.134 148.958 172.707 1.00 29.85  ? 4107 MET A O     1 
ATOM   19495 C  CB    . MET A 1 4107 ? 152.544 151.177 173.004 1.00 27.43  ? 4107 MET A CB    1 
ATOM   19496 C  CG    . MET A 1 4107 ? 153.930 151.705 172.674 1.00 34.81  ? 4107 MET A CG    1 
ATOM   19497 S  SD    . MET A 1 4107 ? 154.438 153.068 173.738 1.00 62.61  ? 4107 MET A SD    1 
ATOM   19498 C  CE    . MET A 1 4107 ? 156.070 153.413 173.086 1.00 41.03  ? 4107 MET A CE    1 
ATOM   19499 N  N     . GLN A 1 4108 ? 149.562 150.984 171.906 1.00 25.00  ? 4108 GLN A N     1 
ATOM   19500 C  CA    . GLN A 1 4108 ? 148.136 150.742 172.098 1.00 27.01  ? 4108 GLN A CA    1 
ATOM   19501 C  C     . GLN A 1 4108 ? 147.638 149.628 171.187 1.00 26.00  ? 4108 GLN A C     1 
ATOM   19502 O  O     . GLN A 1 4108 ? 146.832 148.787 171.603 1.00 27.55  ? 4108 GLN A O     1 
ATOM   19503 C  CB    . GLN A 1 4108 ? 147.348 152.027 171.843 1.00 30.63  ? 4108 GLN A CB    1 
ATOM   19504 C  CG    . GLN A 1 4108 ? 147.807 153.220 172.663 1.00 37.70  ? 4108 GLN A CG    1 
ATOM   19505 C  CD    . GLN A 1 4108 ? 147.167 154.516 172.205 1.00 46.41  ? 4108 GLN A CD    1 
ATOM   19506 O  OE1   . GLN A 1 4108 ? 146.143 154.508 171.523 1.00 49.26  ? 4108 GLN A OE1   1 
ATOM   19507 N  NE2   . GLN A 1 4108 ? 147.772 155.638 172.575 1.00 42.52  ? 4108 GLN A NE2   1 
ATOM   19508 N  N     . LEU A 1 4109 ? 148.101 149.611 169.934 1.00 24.67  ? 4109 LEU A N     1 
ATOM   19509 C  CA    . LEU A 1 4109 ? 147.626 148.618 168.976 1.00 28.35  ? 4109 LEU A CA    1 
ATOM   19510 C  C     . LEU A 1 4109 ? 148.056 147.210 169.369 1.00 26.50  ? 4109 LEU A C     1 
ATOM   19511 O  O     . LEU A 1 4109 ? 147.274 146.260 169.243 1.00 27.41  ? 4109 LEU A O     1 
ATOM   19512 C  CB    . LEU A 1 4109 ? 148.129 148.965 167.574 1.00 24.12  ? 4109 LEU A CB    1 
ATOM   19513 C  CG    . LEU A 1 4109 ? 148.015 147.873 166.511 1.00 22.12  ? 4109 LEU A CG    1 
ATOM   19514 C  CD1   . LEU A 1 4109 ? 146.561 147.642 166.148 1.00 20.67  ? 4109 LEU A CD1   1 
ATOM   19515 C  CD2   . LEU A 1 4109 ? 148.827 148.237 165.279 1.00 21.24  ? 4109 LEU A CD2   1 
ATOM   19516 N  N     . GLU A 1 4110 ? 149.294 147.055 169.844 1.00 27.26  ? 4110 GLU A N     1 
ATOM   19517 C  CA    . GLU A 1 4110 ? 149.769 145.739 170.261 1.00 27.39  ? 4110 GLU A CA    1 
ATOM   19518 C  C     . GLU A 1 4110 ? 148.937 145.200 171.417 1.00 29.01  ? 4110 GLU A C     1 
ATOM   19519 O  O     . GLU A 1 4110 ? 148.635 144.003 171.472 1.00 33.54  ? 4110 GLU A O     1 
ATOM   19520 C  CB    . GLU A 1 4110 ? 151.246 145.815 170.647 1.00 25.63  ? 4110 GLU A CB    1 
ATOM   19521 C  CG    . GLU A 1 4110 ? 151.908 144.465 170.874 1.00 27.69  ? 4110 GLU A CG    1 
ATOM   19522 C  CD    . GLU A 1 4110 ? 151.827 144.004 172.317 1.00 35.81  ? 4110 GLU A CD    1 
ATOM   19523 O  OE1   . GLU A 1 4110 ? 152.140 144.809 173.219 1.00 38.52  ? 4110 GLU A OE1   1 
ATOM   19524 O  OE2   . GLU A 1 4110 ? 151.454 142.836 172.548 1.00 35.65  ? 4110 GLU A OE2   1 
ATOM   19525 N  N     . LYS A 1 4111 ? 148.565 146.074 172.354 1.00 29.01  ? 4111 LYS A N     1 
ATOM   19526 C  CA    . LYS A 1 4111 ? 147.706 145.664 173.460 1.00 25.25  ? 4111 LYS A CA    1 
ATOM   19527 C  C     . LYS A 1 4111 ? 146.334 145.234 172.956 1.00 26.64  ? 4111 LYS A C     1 
ATOM   19528 O  O     . LYS A 1 4111 ? 145.772 144.239 173.430 1.00 31.48  ? 4111 LYS A O     1 
ATOM   19529 C  CB    . LYS A 1 4111 ? 147.580 146.811 174.460 1.00 28.85  ? 4111 LYS A CB    1 
ATOM   19530 C  CG    . LYS A 1 4111 ? 148.796 146.976 175.356 1.00 40.33  ? 4111 LYS A CG    1 
ATOM   19531 C  CD    . LYS A 1 4111 ? 148.918 148.407 175.853 1.00 44.07  ? 4111 LYS A CD    1 
ATOM   19532 C  CE    . LYS A 1 4111 ? 150.074 148.567 176.829 1.00 47.82  ? 4111 LYS A CE    1 
ATOM   19533 N  NZ    . LYS A 1 4111 ? 151.335 147.987 176.295 1.00 45.82  ? 4111 LYS A NZ    1 
ATOM   19534 N  N     . LYS A 1 4112 ? 145.780 145.976 171.994 1.00 26.84  ? 4112 LYS A N     1 
ATOM   19535 C  CA    . LYS A 1 4112 ? 144.488 145.617 171.418 1.00 24.48  ? 4112 LYS A CA    1 
ATOM   19536 C  C     . LYS A 1 4112 ? 144.555 144.277 170.696 1.00 25.34  ? 4112 LYS A C     1 
ATOM   19537 O  O     . LYS A 1 4112 ? 143.617 143.475 170.770 1.00 29.41  ? 4112 LYS A O     1 
ATOM   19538 C  CB    . LYS A 1 4112 ? 144.026 146.717 170.464 1.00 26.26  ? 4112 LYS A CB    1 
ATOM   19539 C  CG    . LYS A 1 4112 ? 142.676 146.465 169.819 1.00 26.28  ? 4112 LYS A CG    1 
ATOM   19540 C  CD    . LYS A 1 4112 ? 142.275 147.637 168.941 1.00 25.83  ? 4112 LYS A CD    1 
ATOM   19541 C  CE    . LYS A 1 4112 ? 140.920 147.411 168.299 1.00 27.60  ? 4112 LYS A CE    1 
ATOM   19542 N  NZ    . LYS A 1 4112 ? 140.514 148.573 167.463 1.00 33.36  ? 4112 LYS A NZ    1 
ATOM   19543 N  N     . LEU A 1 4113 ? 145.654 144.023 169.983 1.00 25.67  ? 4113 LEU A N     1 
ATOM   19544 C  CA    . LEU A 1 4113 ? 145.793 142.768 169.251 1.00 27.09  ? 4113 LEU A CA    1 
ATOM   19545 C  C     . LEU A 1 4113 ? 145.872 141.575 170.195 1.00 31.27  ? 4113 LEU A C     1 
ATOM   19546 O  O     . LEU A 1 4113 ? 145.305 140.515 169.909 1.00 30.61  ? 4113 LEU A O     1 
ATOM   19547 C  CB    . LEU A 1 4113 ? 147.028 142.821 168.353 1.00 26.44  ? 4113 LEU A CB    1 
ATOM   19548 C  CG    . LEU A 1 4113 ? 146.874 143.566 167.028 1.00 24.49  ? 4113 LEU A CG    1 
ATOM   19549 C  CD1   . LEU A 1 4113 ? 148.237 143.902 166.446 1.00 22.07  ? 4113 LEU A CD1   1 
ATOM   19550 C  CD2   . LEU A 1 4113 ? 146.055 142.743 166.048 1.00 18.63  ? 4113 LEU A CD2   1 
ATOM   19551 N  N     . HIS A 1 4114 ? 146.574 141.728 171.321 1.00 30.85  ? 4114 HIS A N     1 
ATOM   19552 C  CA    . HIS A 1 4114 ? 146.786 140.601 172.225 1.00 26.89  ? 4114 HIS A CA    1 
ATOM   19553 C  C     . HIS A 1 4114 ? 145.471 140.082 172.793 1.00 30.86  ? 4114 HIS A C     1 
ATOM   19554 O  O     . HIS A 1 4114 ? 145.239 138.868 172.832 1.00 32.92  ? 4114 HIS A O     1 
ATOM   19555 C  CB    . HIS A 1 4114 ? 147.730 141.010 173.355 1.00 28.54  ? 4114 HIS A CB    1 
ATOM   19556 C  CG    . HIS A 1 4114 ? 147.953 139.937 174.374 1.00 33.10  ? 4114 HIS A CG    1 
ATOM   19557 N  ND1   . HIS A 1 4114 ? 148.782 138.859 174.151 1.00 30.98  ? 4114 HIS A ND1   1 
ATOM   19558 C  CD2   . HIS A 1 4114 ? 147.453 139.775 175.622 1.00 29.28  ? 4114 HIS A CD2   1 
ATOM   19559 C  CE1   . HIS A 1 4114 ? 148.785 138.080 175.218 1.00 27.23  ? 4114 HIS A CE1   1 
ATOM   19560 N  NE2   . HIS A 1 4114 ? 147.986 138.613 176.125 1.00 29.18  ? 4114 HIS A NE2   1 
ATOM   19561 N  N     . SER A 1 4115 ? 144.597 140.983 173.235 1.00 32.57  ? 4115 SER A N     1 
ATOM   19562 C  CA    . SER A 1 4115 ? 143.305 140.597 173.798 1.00 36.10  ? 4115 SER A CA    1 
ATOM   19563 C  C     . SER A 1 4115 ? 142.238 140.657 172.706 1.00 39.00  ? 4115 SER A C     1 
ATOM   19564 O  O     . SER A 1 4115 ? 141.341 141.500 172.702 1.00 42.35  ? 4115 SER A O     1 
ATOM   19565 C  CB    . SER A 1 4115 ? 142.954 141.493 174.981 1.00 36.48  ? 4115 SER A CB    1 
ATOM   19566 O  OG    . SER A 1 4115 ? 142.936 142.857 174.597 1.00 38.31  ? 4115 SER A OG    1 
ATOM   19567 N  N     . LEU A 1 4116 ? 142.357 139.724 171.764 1.00 38.64  ? 4116 LEU A N     1 
ATOM   19568 C  CA    . LEU A 1 4116 ? 141.487 139.712 170.598 1.00 41.31  ? 4116 LEU A CA    1 
ATOM   19569 C  C     . LEU A 1 4116 ? 141.460 138.309 170.011 1.00 46.69  ? 4116 LEU A C     1 
ATOM   19570 O  O     . LEU A 1 4116 ? 142.474 137.607 170.021 1.00 48.83  ? 4116 LEU A O     1 
ATOM   19571 C  CB    . LEU A 1 4116 ? 141.965 140.726 169.552 1.00 37.19  ? 4116 LEU A CB    1 
ATOM   19572 C  CG    . LEU A 1 4116 ? 141.040 141.032 168.377 1.00 36.21  ? 4116 LEU A CG    1 
ATOM   19573 C  CD1   . LEU A 1 4116 ? 139.761 141.690 168.867 1.00 36.02  ? 4116 LEU A CD1   1 
ATOM   19574 C  CD2   . LEU A 1 4116 ? 141.757 141.925 167.382 1.00 36.11  ? 4116 LEU A CD2   1 
ATOM   19575 N  N     . GLN A 1 4117 ? 140.296 137.912 169.501 1.00 47.55  ? 4117 GLN A N     1 
ATOM   19576 C  CA    . GLN A 1 4117 ? 140.096 136.605 168.877 1.00 48.57  ? 4117 GLN A CA    1 
ATOM   19577 C  C     . GLN A 1 4117 ? 139.506 136.839 167.493 1.00 46.18  ? 4117 GLN A C     1 
ATOM   19578 O  O     . GLN A 1 4117 ? 138.291 136.717 167.291 1.00 44.22  ? 4117 GLN A O     1 
ATOM   19579 C  CB    . GLN A 1 4117 ? 139.194 135.711 169.728 1.00 52.61  ? 4117 GLN A CB    1 
ATOM   19580 C  CG    . GLN A 1 4117 ? 139.800 135.311 171.063 1.00 62.64  ? 4117 GLN A CG    1 
ATOM   19581 C  CD    . GLN A 1 4117 ? 139.547 133.856 171.403 1.00 69.82  ? 4117 GLN A CD    1 
ATOM   19582 O  OE1   . GLN A 1 4117 ? 138.909 133.130 170.641 1.00 64.40  ? 4117 GLN A OE1   1 
ATOM   19583 N  NE2   . GLN A 1 4117 ? 140.046 133.421 172.555 1.00 68.88  ? 4117 GLN A NE2   1 
ATOM   19584 N  N     . PRO A 1 4118 ? 140.339 137.176 166.519 1.00 45.39  ? 4118 PRO A N     1 
ATOM   19585 C  CA    . PRO A 1 4118 ? 139.844 137.572 165.198 1.00 42.59  ? 4118 PRO A CA    1 
ATOM   19586 C  C     . PRO A 1 4118 ? 139.387 136.365 164.384 1.00 39.20  ? 4118 PRO A C     1 
ATOM   19587 O  O     . PRO A 1 4118 ? 139.532 135.213 164.786 1.00 40.10  ? 4118 PRO A O     1 
ATOM   19588 C  CB    . PRO A 1 4118 ? 141.061 138.246 164.563 1.00 34.52  ? 4118 PRO A CB    1 
ATOM   19589 C  CG    . PRO A 1 4118 ? 142.228 137.577 165.197 1.00 39.29  ? 4118 PRO A CG    1 
ATOM   19590 C  CD    . PRO A 1 4118 ? 141.811 137.204 166.594 1.00 39.99  ? 4118 PRO A CD    1 
ATOM   19591 N  N     . HIS A 1 4119 ? 138.819 136.662 163.219 1.00 34.40  ? 4119 HIS A N     1 
ATOM   19592 C  CA    . HIS A 1 4119 ? 138.380 135.631 162.293 1.00 32.43  ? 4119 HIS A CA    1 
ATOM   19593 C  C     . HIS A 1 4119 ? 139.577 134.837 161.775 1.00 37.79  ? 4119 HIS A C     1 
ATOM   19594 O  O     . HIS A 1 4119 ? 140.720 135.304 161.786 1.00 41.05  ? 4119 HIS A O     1 
ATOM   19595 C  CB    . HIS A 1 4119 ? 137.609 136.259 161.130 1.00 35.14  ? 4119 HIS A CB    1 
ATOM   19596 C  CG    . HIS A 1 4119 ? 136.968 135.263 160.214 1.00 39.23  ? 4119 HIS A CG    1 
ATOM   19597 N  ND1   . HIS A 1 4119 ? 137.591 134.783 159.083 1.00 38.31  ? 4119 HIS A ND1   1 
ATOM   19598 C  CD2   . HIS A 1 4119 ? 135.756 134.663 160.259 1.00 44.34  ? 4119 HIS A CD2   1 
ATOM   19599 C  CE1   . HIS A 1 4119 ? 136.792 133.928 158.472 1.00 37.16  ? 4119 HIS A CE1   1 
ATOM   19600 N  NE2   . HIS A 1 4119 ? 135.671 133.837 159.165 1.00 44.32  ? 4119 HIS A NE2   1 
ATOM   19601 N  N     . ALA A 1 4120 ? 139.299 133.612 161.320 1.00 34.40  ? 4120 ALA A N     1 
ATOM   19602 C  CA    . ALA A 1 4120 ? 140.366 132.720 160.877 1.00 33.90  ? 4120 ALA A CA    1 
ATOM   19603 C  C     . ALA A 1 4120 ? 141.147 133.301 159.705 1.00 38.14  ? 4120 ALA A C     1 
ATOM   19604 O  O     . ALA A 1 4120 ? 142.370 133.132 159.632 1.00 39.05  ? 4120 ALA A O     1 
ATOM   19605 C  CB    . ALA A 1 4120 ? 139.787 131.356 160.501 1.00 35.31  ? 4120 ALA A CB    1 
ATOM   19606 N  N     . CYS A 1 4121 ? 140.470 133.983 158.785 1.00 36.84  ? 4121 CYS A N     1 
ATOM   19607 C  CA    . CYS A 1 4121 ? 141.112 134.536 157.601 1.00 32.72  ? 4121 CYS A CA    1 
ATOM   19608 C  C     . CYS A 1 4121 ? 141.618 135.959 157.800 1.00 31.87  ? 4121 CYS A C     1 
ATOM   19609 O  O     . CYS A 1 4121 ? 142.168 136.539 156.858 1.00 31.53  ? 4121 CYS A O     1 
ATOM   19610 C  CB    . CYS A 1 4121 ? 140.144 134.498 156.414 1.00 35.31  ? 4121 CYS A CB    1 
ATOM   19611 S  SG    . CYS A 1 4121 ? 139.695 132.831 155.876 1.00 59.08  ? 4121 CYS A SG    1 
ATOM   19612 N  N     . PHE A 1 4122 ? 141.446 136.534 158.988 1.00 30.08  ? 4122 PHE A N     1 
ATOM   19613 C  CA    . PHE A 1 4122 ? 141.910 137.892 159.234 1.00 23.36  ? 4122 PHE A CA    1 
ATOM   19614 C  C     . PHE A 1 4122 ? 143.431 137.956 159.208 1.00 24.19  ? 4122 PHE A C     1 
ATOM   19615 O  O     . PHE A 1 4122 ? 144.117 137.094 159.764 1.00 29.49  ? 4122 PHE A O     1 
ATOM   19616 C  CB    . PHE A 1 4122 ? 141.398 138.402 160.581 1.00 23.24  ? 4122 PHE A CB    1 
ATOM   19617 C  CG    . PHE A 1 4122 ? 142.042 139.686 161.024 1.00 19.71  ? 4122 PHE A CG    1 
ATOM   19618 C  CD1   . PHE A 1 4122 ? 141.729 140.882 160.403 1.00 15.49  ? 4122 PHE A CD1   1 
ATOM   19619 C  CD2   . PHE A 1 4122 ? 142.969 139.695 162.052 1.00 22.23  ? 4122 PHE A CD2   1 
ATOM   19620 C  CE1   . PHE A 1 4122 ? 142.323 142.063 160.804 1.00 12.96  ? 4122 PHE A CE1   1 
ATOM   19621 C  CE2   . PHE A 1 4122 ? 143.564 140.873 162.457 1.00 14.28  ? 4122 PHE A CE2   1 
ATOM   19622 C  CZ    . PHE A 1 4122 ? 143.240 142.058 161.832 1.00 9.66   ? 4122 PHE A CZ    1 
ATOM   19623 N  N     . ARG A 1 4123 ? 143.956 138.989 158.554 1.00 18.64  ? 4123 ARG A N     1 
ATOM   19624 C  CA    . ARG A 1 4123 ? 145.383 139.266 158.544 1.00 13.97  ? 4123 ARG A CA    1 
ATOM   19625 C  C     . ARG A 1 4123 ? 145.591 140.762 158.709 1.00 9.35   ? 4123 ARG A C     1 
ATOM   19626 O  O     . ARG A 1 4123 ? 144.848 141.564 158.136 1.00 13.39  ? 4123 ARG A O     1 
ATOM   19627 C  CB    . ARG A 1 4123 ? 146.046 138.785 157.247 1.00 14.28  ? 4123 ARG A CB    1 
ATOM   19628 C  CG    . ARG A 1 4123 ? 146.121 137.276 157.100 1.00 16.10  ? 4123 ARG A CG    1 
ATOM   19629 C  CD    . ARG A 1 4123 ? 146.968 136.646 158.194 1.00 21.03  ? 4123 ARG A CD    1 
ATOM   19630 N  NE    . ARG A 1 4123 ? 147.013 135.194 158.070 1.00 28.07  ? 4123 ARG A NE    1 
ATOM   19631 C  CZ    . ARG A 1 4123 ? 146.041 134.377 158.454 1.00 28.01  ? 4123 ARG A CZ    1 
ATOM   19632 N  NH1   . ARG A 1 4123 ? 144.933 134.835 159.012 1.00 26.58  ? 4123 ARG A NH1   1 
ATOM   19633 N  NH2   . ARG A 1 4123 ? 146.186 133.068 158.274 1.00 33.17  ? 4123 ARG A NH2   1 
ATOM   19634 N  N     . LEU A 1 4124 ? 146.598 141.133 159.493 1.00 7.39   ? 4124 LEU A N     1 
ATOM   19635 C  CA    . LEU A 1 4124 ? 146.973 142.530 159.682 1.00 6.79   ? 4124 LEU A CA    1 
ATOM   19636 C  C     . LEU A 1 4124 ? 148.426 142.692 159.262 1.00 6.55   ? 4124 LEU A C     1 
ATOM   19637 O  O     . LEU A 1 4124 ? 149.322 142.083 159.857 1.00 6.92   ? 4124 LEU A O     1 
ATOM   19638 C  CB    . LEU A 1 4124 ? 146.766 142.974 161.129 1.00 7.92   ? 4124 LEU A CB    1 
ATOM   19639 C  CG    . LEU A 1 4124 ? 147.278 144.380 161.450 1.00 5.92   ? 4124 LEU A CG    1 
ATOM   19640 C  CD1   . LEU A 1 4124 ? 146.429 145.430 160.754 1.00 7.89   ? 4124 LEU A CD1   1 
ATOM   19641 C  CD2   . LEU A 1 4124 ? 147.296 144.615 162.948 1.00 7.55   ? 4124 LEU A CD2   1 
ATOM   19642 N  N     . PHE A 1 4125 ? 148.652 143.514 158.235 1.00 6.96   ? 4125 PHE A N     1 
ATOM   19643 C  CA    . PHE A 1 4125 ? 150.032 143.758 157.738 1.00 7.22   ? 4125 PHE A CA    1 
ATOM   19644 C  C     . PHE A 1 4125 ? 150.444 145.167 158.138 1.00 7.58   ? 4125 PHE A C     1 
ATOM   19645 O  O     . PHE A 1 4125 ? 149.729 146.134 157.801 1.00 8.46   ? 4125 PHE A O     1 
ATOM   19646 C  CB    . PHE A 1 4125 ? 150.059 143.563 156.220 1.00 8.01   ? 4125 PHE A CB    1 
ATOM   19647 C  CG    . PHE A 1 4125 ? 149.459 142.245 155.750 1.00 6.99   ? 4125 PHE A CG    1 
ATOM   19648 C  CD1   . PHE A 1 4125 ? 148.095 142.129 155.508 1.00 8.08   ? 4125 PHE A CD1   1 
ATOM   19649 C  CD2   . PHE A 1 4125 ? 150.261 141.128 155.546 1.00 9.28   ? 4125 PHE A CD2   1 
ATOM   19650 C  CE1   . PHE A 1 4125 ? 147.552 140.929 155.082 1.00 9.73   ? 4125 PHE A CE1   1 
ATOM   19651 C  CE2   . PHE A 1 4125 ? 149.711 139.931 155.118 1.00 13.62  ? 4125 PHE A CE2   1 
ATOM   19652 C  CZ    . PHE A 1 4125 ? 148.360 139.834 154.887 1.00 14.47  ? 4125 PHE A CZ    1 
ATOM   19653 N  N     . LEU A 1 4126 ? 151.564 145.284 158.854 1.00 6.65   ? 4126 LEU A N     1 
ATOM   19654 C  CA    . LEU A 1 4126 ? 152.062 146.615 159.280 1.00 7.47   ? 4126 LEU A CA    1 
ATOM   19655 C  C     . LEU A 1 4126 ? 153.367 146.917 158.531 1.00 10.63  ? 4126 LEU A C     1 
ATOM   19656 O  O     . LEU A 1 4126 ? 154.377 146.234 158.802 1.00 11.69  ? 4126 LEU A O     1 
ATOM   19657 C  CB    . LEU A 1 4126 ? 152.261 146.624 160.794 1.00 8.80   ? 4126 LEU A CB    1 
ATOM   19658 C  CG    . LEU A 1 4126 ? 151.035 146.238 161.628 1.00 7.70   ? 4126 LEU A CG    1 
ATOM   19659 C  CD1   . LEU A 1 4126 ? 151.339 146.334 163.113 1.00 10.54  ? 4126 LEU A CD1   1 
ATOM   19660 C  CD2   . LEU A 1 4126 ? 149.849 147.112 161.265 1.00 7.34   ? 4126 LEU A CD2   1 
ATOM   19661 N  N     . THR A 1 4127 ? 153.337 147.896 157.624 1.00 12.13  ? 4127 THR A N     1 
ATOM   19662 C  CA    . THR A 1 4127 ? 154.552 148.272 156.871 1.00 10.27  ? 4127 THR A CA    1 
ATOM   19663 C  C     . THR A 1 4127 ? 155.229 149.410 157.602 1.00 8.06   ? 4127 THR A C     1 
ATOM   19664 O  O     . THR A 1 4127 ? 154.522 150.359 158.003 1.00 12.13  ? 4127 THR A O     1 
ATOM   19665 C  CB    . THR A 1 4127 ? 154.189 148.644 155.434 1.00 10.63  ? 4127 THR A CB    1 
ATOM   19666 O  OG1   . THR A 1 4127 ? 153.843 150.025 155.461 1.00 11.72  ? 4127 THR A OG1   1 
ATOM   19667 C  CG2   . THR A 1 4127 ? 153.034 147.820 154.895 1.00 13.92  ? 4127 THR A CG2   1 
ATOM   19668 N  N     . MET A 1 4128 ? 156.547 149.318 157.789 1.00 8.93   ? 4128 MET A N     1 
ATOM   19669 C  CA    . MET A 1 4128 ? 157.288 150.363 158.538 1.00 13.64  ? 4128 MET A CA    1 
ATOM   19670 C  C     . MET A 1 4128 ? 158.770 150.314 158.148 1.00 13.54  ? 4128 MET A C     1 
ATOM   19671 O  O     . MET A 1 4128 ? 159.202 149.282 157.593 1.00 14.79  ? 4128 MET A O     1 
ATOM   19672 C  CB    . MET A 1 4128 ? 157.179 150.120 160.046 1.00 17.81  ? 4128 MET A CB    1 
ATOM   19673 C  CG    . MET A 1 4128 ? 157.995 148.933 160.524 1.00 16.29  ? 4128 MET A CG    1 
ATOM   19674 S  SD    . MET A 1 4128 ? 157.348 148.152 162.016 1.00 25.05  ? 4128 MET A SD    1 
ATOM   19675 C  CE    . MET A 1 4128 ? 155.877 147.352 161.361 1.00 13.41  ? 4128 MET A CE    1 
ATOM   19676 N  N     . GLU A 1 4129 ? 159.511 151.390 158.419 1.00 13.18  ? 4129 GLU A N     1 
ATOM   19677 C  CA    . GLU A 1 4129 ? 160.973 151.377 158.164 1.00 12.46  ? 4129 GLU A CA    1 
ATOM   19678 C  C     . GLU A 1 4129 ? 161.646 150.678 159.353 1.00 19.03  ? 4129 GLU A C     1 
ATOM   19679 O  O     . GLU A 1 4129 ? 160.962 150.477 160.381 1.00 28.32  ? 4129 GLU A O     1 
ATOM   19680 C  CB    . GLU A 1 4129 ? 161.507 152.800 158.014 1.00 16.15  ? 4129 GLU A CB    1 
ATOM   19681 C  CG    . GLU A 1 4129 ? 161.567 153.553 159.340 1.00 23.16  ? 4129 GLU A CG    1 
ATOM   19682 C  CD    . GLU A 1 4129 ? 162.112 154.964 159.234 1.00 33.63  ? 4129 GLU A CD    1 
ATOM   19683 O  OE1   . GLU A 1 4129 ? 162.443 155.387 158.106 1.00 33.44  ? 4129 GLU A OE1   1 
ATOM   19684 O  OE2   . GLU A 1 4129 ? 162.208 155.640 160.279 1.00 34.24  ? 4129 GLU A OE2   1 
ATOM   19685 N  N     . ILE A 1 4130 ? 162.928 150.329 159.227 1.00 16.96  ? 4130 ILE A N     1 
ATOM   19686 C  CA    . ILE A 1 4130 ? 163.658 149.724 160.380 1.00 16.12  ? 4130 ILE A CA    1 
ATOM   19687 C  C     . ILE A 1 4130 ? 164.074 150.866 161.321 1.00 21.55  ? 4130 ILE A C     1 
ATOM   19688 O  O     . ILE A 1 4130 ? 165.240 151.308 161.235 1.00 28.34  ? 4130 ILE A O     1 
ATOM   19689 C  CB    . ILE A 1 4130 ? 164.858 148.890 159.895 1.00 17.42  ? 4130 ILE A CB    1 
ATOM   19690 C  CG1   . ILE A 1 4130 ? 164.456 147.939 158.768 1.00 17.36  ? 4130 ILE A CG1   1 
ATOM   19691 C  CG2   . ILE A 1 4130 ? 165.513 148.145 161.059 1.00 17.04  ? 4130 ILE A CG2   1 
ATOM   19692 C  CD1   . ILE A 1 4130 ? 165.588 147.064 158.261 1.00 16.58  ? 4130 ILE A CD1   1 
ATOM   19693 N  N     . ASN A 1 4131 ? 163.152 151.326 162.173 1.00 20.49  ? 4131 ASN A N     1 
ATOM   19694 C  CA    . ASN A 1 4131 ? 163.443 152.472 163.079 1.00 23.94  ? 4131 ASN A CA    1 
ATOM   19695 C  C     . ASN A 1 4131 ? 163.468 151.989 164.533 1.00 27.79  ? 4131 ASN A C     1 
ATOM   19696 O  O     . ASN A 1 4131 ? 162.553 151.235 164.926 1.00 26.40  ? 4131 ASN A O     1 
ATOM   19697 C  CB    . ASN A 1 4131 ? 162.437 153.601 162.882 1.00 28.40  ? 4131 ASN A CB    1 
ATOM   19698 C  CG    . ASN A 1 4131 ? 162.833 154.858 163.617 1.00 34.06  ? 4131 ASN A CG    1 
ATOM   19699 O  OD1   . ASN A 1 4131 ? 162.956 154.850 164.847 1.00 36.26  ? 4131 ASN A OD1   1 
ATOM   19700 N  ND2   . ASN A 1 4131 ? 163.036 155.945 162.888 1.00 31.91  ? 4131 ASN A ND2   1 
ATOM   19701 N  N     . PRO A 1 4132 ? 164.467 152.391 165.349 1.00 27.86  ? 4132 PRO A N     1 
ATOM   19702 C  CA    . PRO A 1 4132 ? 164.515 152.016 166.771 1.00 22.08  ? 4132 PRO A CA    1 
ATOM   19703 C  C     . PRO A 1 4132 ? 163.288 152.445 167.556 1.00 32.11  ? 4132 PRO A C     1 
ATOM   19704 O  O     . PRO A 1 4132 ? 163.020 151.869 168.618 1.00 36.46  ? 4132 PRO A O     1 
ATOM   19705 C  CB    . PRO A 1 4132 ? 165.780 152.725 167.281 1.00 20.59  ? 4132 PRO A CB    1 
ATOM   19706 C  CG    . PRO A 1 4132 ? 166.078 153.779 166.255 1.00 24.81  ? 4132 PRO A CG    1 
ATOM   19707 C  CD    . PRO A 1 4132 ? 165.620 153.215 164.953 1.00 24.66  ? 4132 PRO A CD    1 
ATOM   19708 N  N     . LYS A 1 4133 ? 162.534 153.435 167.072 1.00 32.13  ? 4133 LYS A N     1 
ATOM   19709 C  CA    . LYS A 1 4133 ? 161.361 153.911 167.796 1.00 29.59  ? 4133 LYS A CA    1 
ATOM   19710 C  C     . LYS A 1 4133 ? 160.227 152.895 167.809 1.00 31.49  ? 4133 LYS A C     1 
ATOM   19711 O  O     . LYS A 1 4133 ? 159.284 153.052 168.593 1.00 37.36  ? 4133 LYS A O     1 
ATOM   19712 C  CB    . LYS A 1 4133 ? 160.869 155.228 167.195 1.00 31.67  ? 4133 LYS A CB    1 
ATOM   19713 C  CG    . LYS A 1 4133 ? 161.848 156.380 167.341 1.00 34.89  ? 4133 LYS A CG    1 
ATOM   19714 C  CD    . LYS A 1 4133 ? 161.497 157.252 168.535 1.00 36.72  ? 4133 LYS A CD    1 
ATOM   19715 C  CE    . LYS A 1 4133 ? 162.313 158.534 168.541 1.00 45.42  ? 4133 LYS A CE    1 
ATOM   19716 N  NZ    . LYS A 1 4133 ? 161.515 159.701 168.075 1.00 46.10  ? 4133 LYS A NZ    1 
ATOM   19717 N  N     . VAL A 1 4134 ? 160.286 151.874 166.960 1.00 28.71  ? 4134 VAL A N     1 
ATOM   19718 C  CA    . VAL A 1 4134 ? 159.237 150.849 166.963 1.00 26.35  ? 4134 VAL A CA    1 
ATOM   19719 C  C     . VAL A 1 4134 ? 159.257 150.117 168.300 1.00 27.65  ? 4134 VAL A C     1 
ATOM   19720 O  O     . VAL A 1 4134 ? 160.333 149.667 168.742 1.00 31.92  ? 4134 VAL A O     1 
ATOM   19721 C  CB    . VAL A 1 4134 ? 159.437 149.868 165.795 1.00 29.99  ? 4134 VAL A CB    1 
ATOM   19722 C  CG1   . VAL A 1 4134 ? 158.422 148.738 165.867 1.00 30.83  ? 4134 VAL A CG1   1 
ATOM   19723 C  CG2   . VAL A 1 4134 ? 159.332 150.598 164.466 1.00 24.60  ? 4134 VAL A CG2   1 
ATOM   19724 N  N     . PRO A 1 4135 ? 158.123 149.982 168.988 1.00 30.58  ? 4135 PRO A N     1 
ATOM   19725 C  CA    . PRO A 1 4135 ? 158.126 149.317 170.296 1.00 25.78  ? 4135 PRO A CA    1 
ATOM   19726 C  C     . PRO A 1 4135 ? 158.584 147.869 170.198 1.00 21.92  ? 4135 PRO A C     1 
ATOM   19727 O  O     . PRO A 1 4135 ? 158.305 147.168 169.223 1.00 26.41  ? 4135 PRO A O     1 
ATOM   19728 C  CB    . PRO A 1 4135 ? 156.663 149.410 170.748 1.00 27.77  ? 4135 PRO A CB    1 
ATOM   19729 C  CG    . PRO A 1 4135 ? 156.075 150.518 169.934 1.00 29.69  ? 4135 PRO A CG    1 
ATOM   19730 C  CD    . PRO A 1 4135 ? 156.788 150.482 168.622 1.00 29.81  ? 4135 PRO A CD    1 
ATOM   19731 N  N     . VAL A 1 4136 ? 159.300 147.429 171.234 1.00 20.28  ? 4136 VAL A N     1 
ATOM   19732 C  CA    . VAL A 1 4136 ? 159.821 146.066 171.264 1.00 20.10  ? 4136 VAL A CA    1 
ATOM   19733 C  C     . VAL A 1 4136 ? 158.683 145.059 171.374 1.00 18.48  ? 4136 VAL A C     1 
ATOM   19734 O  O     . VAL A 1 4136 ? 158.712 143.997 170.740 1.00 21.18  ? 4136 VAL A O     1 
ATOM   19735 C  CB    . VAL A 1 4136 ? 160.835 145.915 172.413 1.00 20.00  ? 4136 VAL A CB    1 
ATOM   19736 C  CG1   . VAL A 1 4136 ? 161.004 144.453 172.802 1.00 22.80  ? 4136 VAL A CG1   1 
ATOM   19737 C  CG2   . VAL A 1 4136 ? 162.172 146.523 172.023 1.00 17.65  ? 4136 VAL A CG2   1 
ATOM   19738 N  N     . ASN A 1 4137 ? 157.658 145.378 172.170 1.00 18.52  ? 4137 ASN A N     1 
ATOM   19739 C  CA    . ASN A 1 4137 ? 156.559 144.439 172.378 1.00 20.70  ? 4137 ASN A CA    1 
ATOM   19740 C  C     . ASN A 1 4137 ? 155.819 144.149 171.078 1.00 20.77  ? 4137 ASN A C     1 
ATOM   19741 O  O     . ASN A 1 4137 ? 155.370 143.020 170.851 1.00 18.42  ? 4137 ASN A O     1 
ATOM   19742 C  CB    . ASN A 1 4137 ? 155.600 144.982 173.437 1.00 23.93  ? 4137 ASN A CB    1 
ATOM   19743 C  CG    . ASN A 1 4137 ? 155.502 146.492 173.412 1.00 30.89  ? 4137 ASN A CG    1 
ATOM   19744 O  OD1   . ASN A 1 4137 ? 156.464 147.193 173.730 1.00 31.60  ? 4137 ASN A OD1   1 
ATOM   19745 N  ND2   . ASN A 1 4137 ? 154.337 147.004 173.035 1.00 32.48  ? 4137 ASN A ND2   1 
ATOM   19746 N  N     . LEU A 1 4138 ? 155.673 145.158 170.215 1.00 19.85  ? 4138 LEU A N     1 
ATOM   19747 C  CA    . LEU A 1 4138 ? 155.065 144.923 168.910 1.00 16.40  ? 4138 LEU A CA    1 
ATOM   19748 C  C     . LEU A 1 4138 ? 155.928 143.999 168.060 1.00 14.33  ? 4138 LEU A C     1 
ATOM   19749 O  O     . LEU A 1 4138 ? 155.408 143.134 167.345 1.00 15.40  ? 4138 LEU A O     1 
ATOM   19750 C  CB    . LEU A 1 4138 ? 154.831 146.248 168.186 1.00 19.02  ? 4138 LEU A CB    1 
ATOM   19751 C  CG    . LEU A 1 4138 ? 154.143 146.112 166.825 1.00 18.87  ? 4138 LEU A CG    1 
ATOM   19752 C  CD1   . LEU A 1 4138 ? 152.635 145.999 166.987 1.00 19.66  ? 4138 LEU A CD1   1 
ATOM   19753 C  CD2   . LEU A 1 4138 ? 154.511 147.265 165.911 1.00 18.00  ? 4138 LEU A CD2   1 
ATOM   19754 N  N     . LEU A 1 4139 ? 157.250 144.174 168.120 1.00 15.02  ? 4139 LEU A N     1 
ATOM   19755 C  CA    . LEU A 1 4139 ? 158.148 143.302 167.370 1.00 15.32  ? 4139 LEU A CA    1 
ATOM   19756 C  C     . LEU A 1 4139 ? 158.050 141.861 167.855 1.00 13.42  ? 4139 LEU A C     1 
ATOM   19757 O  O     . LEU A 1 4139 ? 158.082 140.923 167.050 1.00 16.00  ? 4139 LEU A O     1 
ATOM   19758 C  CB    . LEU A 1 4139 ? 159.585 143.810 167.479 1.00 13.83  ? 4139 LEU A CB    1 
ATOM   19759 C  CG    . LEU A 1 4139 ? 159.898 145.118 166.749 1.00 18.46  ? 4139 LEU A CG    1 
ATOM   19760 C  CD1   . LEU A 1 4139 ? 161.297 145.600 167.094 1.00 17.55  ? 4139 LEU A CD1   1 
ATOM   19761 C  CD2   . LEU A 1 4139 ? 159.745 144.946 165.248 1.00 19.52  ? 4139 LEU A CD2   1 
ATOM   19762 N  N     . ARG A 1 4140 ? 157.933 141.664 169.170 1.00 14.77  ? 4140 ARG A N     1 
ATOM   19763 C  CA    . ARG A 1 4140 ? 157.786 140.315 169.706 1.00 13.54  ? 4140 ARG A CA    1 
ATOM   19764 C  C     . ARG A 1 4140 ? 156.415 139.732 169.394 1.00 11.89  ? 4140 ARG A C     1 
ATOM   19765 O  O     . ARG A 1 4140 ? 156.287 138.516 169.212 1.00 15.79  ? 4140 ARG A O     1 
ATOM   19766 C  CB    . ARG A 1 4140 ? 158.027 140.322 171.215 1.00 18.33  ? 4140 ARG A CB    1 
ATOM   19767 C  CG    . ARG A 1 4140 ? 159.435 140.717 171.622 1.00 17.75  ? 4140 ARG A CG    1 
ATOM   19768 C  CD    . ARG A 1 4140 ? 159.600 140.680 173.131 1.00 18.54  ? 4140 ARG A CD    1 
ATOM   19769 N  NE    . ARG A 1 4140 ? 158.865 139.573 173.731 1.00 30.55  ? 4140 ARG A NE    1 
ATOM   19770 C  CZ    . ARG A 1 4140 ? 159.433 138.527 174.316 1.00 31.52  ? 4140 ARG A CZ    1 
ATOM   19771 N  NH1   . ARG A 1 4140 ? 160.748 138.414 174.402 1.00 28.36  ? 4140 ARG A NH1   1 
ATOM   19772 N  NH2   . ARG A 1 4140 ? 158.662 137.572 174.827 1.00 26.35  ? 4140 ARG A NH2   1 
ATOM   19773 N  N     . ALA A 1 4141 ? 155.382 140.574 169.331 1.00 12.21  ? 4141 ALA A N     1 
ATOM   19774 C  CA    . ALA A 1 4141 ? 154.033 140.086 169.073 1.00 11.88  ? 4141 ALA A CA    1 
ATOM   19775 C  C     . ALA A 1 4141 ? 153.841 139.652 167.626 1.00 11.01  ? 4141 ALA A C     1 
ATOM   19776 O  O     . ALA A 1 4141 ? 153.061 138.731 167.361 1.00 12.77  ? 4141 ALA A O     1 
ATOM   19777 C  CB    . ALA A 1 4141 ? 153.007 141.161 169.433 1.00 12.84  ? 4141 ALA A CB    1 
ATOM   19778 N  N     . GLY A 1 4142 ? 154.532 140.294 166.684 1.00 13.39  ? 4142 GLY A N     1 
ATOM   19779 C  CA    . GLY A 1 4142 ? 154.369 140.006 165.278 1.00 14.52  ? 4142 GLY A CA    1 
ATOM   19780 C  C     . GLY A 1 4142 ? 155.529 139.212 164.694 1.00 13.08  ? 4142 GLY A C     1 
ATOM   19781 O  O     . GLY A 1 4142 ? 156.548 138.964 165.332 1.00 14.33  ? 4142 GLY A O     1 
ATOM   19782 N  N     . ARG A 1 4143 ? 155.345 138.812 163.438 1.00 12.98  ? 4143 ARG A N     1 
ATOM   19783 C  CA    . ARG A 1 4143 ? 156.377 138.130 162.670 1.00 14.54  ? 4143 ARG A CA    1 
ATOM   19784 C  C     . ARG A 1 4143 ? 157.044 139.135 161.742 1.00 11.71  ? 4143 ARG A C     1 
ATOM   19785 O  O     . ARG A 1 4143 ? 156.365 139.832 160.980 1.00 10.06  ? 4143 ARG A O     1 
ATOM   19786 C  CB    . ARG A 1 4143 ? 155.794 136.967 161.867 1.00 17.32  ? 4143 ARG A CB    1 
ATOM   19787 C  CG    . ARG A 1 4143 ? 156.230 135.599 162.369 1.00 23.06  ? 4143 ARG A CG    1 
ATOM   19788 C  CD    . ARG A 1 4143 ? 156.270 134.573 161.249 1.00 29.13  ? 4143 ARG A CD    1 
ATOM   19789 N  NE    . ARG A 1 4143 ? 157.513 134.638 160.490 1.00 27.26  ? 4143 ARG A NE    1 
ATOM   19790 C  CZ    . ARG A 1 4143 ? 157.885 133.744 159.585 1.00 30.15  ? 4143 ARG A CZ    1 
ATOM   19791 N  NH1   . ARG A 1 4143 ? 157.130 132.698 159.296 1.00 33.47  ? 4143 ARG A NH1   1 
ATOM   19792 N  NH2   . ARG A 1 4143 ? 159.044 133.904 158.953 1.00 26.90  ? 4143 ARG A NH2   1 
ATOM   19793 N  N     . ILE A 1 4144 ? 158.367 139.204 161.806 1.00 12.92  ? 4144 ILE A N     1 
ATOM   19794 C  CA    . ILE A 1 4144 ? 159.128 140.248 161.134 1.00 9.64   ? 4144 ILE A CA    1 
ATOM   19795 C  C     . ILE A 1 4144 ? 159.630 139.726 159.797 1.00 8.55   ? 4144 ILE A C     1 
ATOM   19796 O  O     . ILE A 1 4144 ? 160.191 138.627 159.716 1.00 10.21  ? 4144 ILE A O     1 
ATOM   19797 C  CB    . ILE A 1 4144 ? 160.294 140.723 162.016 1.00 10.13  ? 4144 ILE A CB    1 
ATOM   19798 C  CG1   . ILE A 1 4144 ? 159.755 141.441 163.253 1.00 17.04  ? 4144 ILE A CG1   1 
ATOM   19799 C  CG2   . ILE A 1 4144 ? 161.224 141.635 161.233 1.00 11.28  ? 4144 ILE A CG2   1 
ATOM   19800 C  CD1   . ILE A 1 4144 ? 160.700 141.423 164.428 1.00 18.79  ? 4144 ILE A CD1   1 
ATOM   19801 N  N     . PHE A 1 4145 ? 159.405 140.505 158.741 1.00 11.04  ? 4145 PHE A N     1 
ATOM   19802 C  CA    . PHE A 1 4145 ? 159.956 140.239 157.419 1.00 8.90   ? 4145 PHE A CA    1 
ATOM   19803 C  C     . PHE A 1 4145 ? 160.758 141.458 156.994 1.00 9.92   ? 4145 PHE A C     1 
ATOM   19804 O  O     . PHE A 1 4145 ? 160.243 142.580 157.015 1.00 14.64  ? 4145 PHE A O     1 
ATOM   19805 C  CB    . PHE A 1 4145 ? 158.850 139.941 156.406 1.00 12.07  ? 4145 PHE A CB    1 
ATOM   19806 C  CG    . PHE A 1 4145 ? 158.051 138.718 156.730 1.00 13.88  ? 4145 PHE A CG    1 
ATOM   19807 C  CD1   . PHE A 1 4145 ? 158.505 137.462 156.367 1.00 16.49  ? 4145 PHE A CD1   1 
ATOM   19808 C  CD2   . PHE A 1 4145 ? 156.848 138.822 157.405 1.00 13.87  ? 4145 PHE A CD2   1 
ATOM   19809 C  CE1   . PHE A 1 4145 ? 157.771 136.335 156.666 1.00 19.53  ? 4145 PHE A CE1   1 
ATOM   19810 C  CE2   . PHE A 1 4145 ? 156.110 137.699 157.709 1.00 20.74  ? 4145 PHE A CE2   1 
ATOM   19811 C  CZ    . PHE A 1 4145 ? 156.572 136.453 157.339 1.00 23.69  ? 4145 PHE A CZ    1 
ATOM   19812 N  N     . VAL A 1 4146 ? 162.012 141.240 156.613 1.00 9.19   ? 4146 VAL A N     1 
ATOM   19813 C  CA    . VAL A 1 4146 ? 162.916 142.318 156.234 1.00 10.09  ? 4146 VAL A CA    1 
ATOM   19814 C  C     . VAL A 1 4146 ? 162.961 142.410 154.717 1.00 10.06  ? 4146 VAL A C     1 
ATOM   19815 O  O     . VAL A 1 4146 ? 163.204 141.409 154.032 1.00 11.66  ? 4146 VAL A O     1 
ATOM   19816 C  CB    . VAL A 1 4146 ? 164.321 142.101 156.818 1.00 9.62   ? 4146 VAL A CB    1 
ATOM   19817 C  CG1   . VAL A 1 4146 ? 165.330 143.002 156.124 1.00 15.72  ? 4146 VAL A CG1   1 
ATOM   19818 C  CG2   . VAL A 1 4146 ? 164.312 142.375 158.308 1.00 8.78   ? 4146 VAL A CG2   1 
ATOM   19819 N  N     . PHE A 1 4147 ? 162.719 143.607 154.194 1.00 11.83  ? 4147 PHE A N     1 
ATOM   19820 C  CA    . PHE A 1 4147 ? 162.806 143.881 152.768 1.00 13.28  ? 4147 PHE A CA    1 
ATOM   19821 C  C     . PHE A 1 4147 ? 163.988 144.802 152.513 1.00 13.74  ? 4147 PHE A C     1 
ATOM   19822 O  O     . PHE A 1 4147 ? 164.055 145.906 153.064 1.00 15.91  ? 4147 PHE A O     1 
ATOM   19823 C  CB    . PHE A 1 4147 ? 161.510 144.498 152.247 1.00 14.05  ? 4147 PHE A CB    1 
ATOM   19824 C  CG    . PHE A 1 4147 ? 160.359 143.541 152.236 1.00 14.62  ? 4147 PHE A CG    1 
ATOM   19825 C  CD1   . PHE A 1 4147 ? 159.546 143.408 153.345 1.00 12.45  ? 4147 PHE A CD1   1 
ATOM   19826 C  CD2   . PHE A 1 4147 ? 160.096 142.767 151.119 1.00 20.28  ? 4147 PHE A CD2   1 
ATOM   19827 C  CE1   . PHE A 1 4147 ? 158.494 142.525 153.340 1.00 14.74  ? 4147 PHE A CE1   1 
ATOM   19828 C  CE2   . PHE A 1 4147 ? 159.040 141.882 151.108 1.00 22.31  ? 4147 PHE A CE2   1 
ATOM   19829 C  CZ    . PHE A 1 4147 ? 158.238 141.760 152.219 1.00 19.91  ? 4147 PHE A CZ    1 
ATOM   19830 N  N     . GLU A 1 4148 ? 164.910 144.342 151.679 1.00 11.13  ? 4148 GLU A N     1 
ATOM   19831 C  CA    . GLU A 1 4148 ? 166.178 145.020 151.459 1.00 16.12  ? 4148 GLU A CA    1 
ATOM   19832 C  C     . GLU A 1 4148 ? 166.658 144.658 150.062 1.00 22.17  ? 4148 GLU A C     1 
ATOM   19833 O  O     . GLU A 1 4148 ? 166.074 143.784 149.407 1.00 23.73  ? 4148 GLU A O     1 
ATOM   19834 C  CB    . GLU A 1 4148 ? 167.209 144.622 152.530 1.00 20.01  ? 4148 GLU A CB    1 
ATOM   19835 C  CG    . GLU A 1 4148 ? 167.377 143.125 152.703 1.00 20.57  ? 4148 GLU A CG    1 
ATOM   19836 C  CD    . GLU A 1 4148 ? 168.531 142.775 153.619 1.00 25.44  ? 4148 GLU A CD    1 
ATOM   19837 O  OE1   . GLU A 1 4148 ? 169.404 143.641 153.836 1.00 26.21  ? 4148 GLU A OE1   1 
ATOM   19838 O  OE2   . GLU A 1 4148 ? 168.564 141.633 154.124 1.00 29.50  ? 4148 GLU A OE2   1 
ATOM   19839 N  N     . PRO A 1 4149 ? 167.695 145.327 149.560 1.00 23.21  ? 4149 PRO A N     1 
ATOM   19840 C  CA    . PRO A 1 4149 ? 168.240 144.959 148.251 1.00 17.99  ? 4149 PRO A CA    1 
ATOM   19841 C  C     . PRO A 1 4149 ? 168.641 143.496 148.218 1.00 21.43  ? 4149 PRO A C     1 
ATOM   19842 O  O     . PRO A 1 4149 ? 169.216 142.977 149.187 1.00 24.13  ? 4149 PRO A O     1 
ATOM   19843 C  CB    . PRO A 1 4149 ? 169.461 145.877 148.106 1.00 19.73  ? 4149 PRO A CB    1 
ATOM   19844 C  CG    . PRO A 1 4149 ? 169.111 147.070 148.905 1.00 24.62  ? 4149 PRO A CG    1 
ATOM   19845 C  CD    . PRO A 1 4149 ? 168.288 146.582 150.062 1.00 23.18  ? 4149 PRO A CD    1 
ATOM   19846 N  N     . PRO A 1 4150 ? 168.332 142.796 147.128 1.00 21.32  ? 4150 PRO A N     1 
ATOM   19847 C  CA    . PRO A 1 4150 ? 168.698 141.388 147.038 1.00 18.51  ? 4150 PRO A CA    1 
ATOM   19848 C  C     . PRO A 1 4150 ? 170.203 141.219 147.117 1.00 19.91  ? 4150 PRO A C     1 
ATOM   19849 O  O     . PRO A 1 4150 ? 170.968 142.106 146.697 1.00 23.29  ? 4150 PRO A O     1 
ATOM   19850 C  CB    . PRO A 1 4150 ? 168.151 140.964 145.667 1.00 16.23  ? 4150 PRO A CB    1 
ATOM   19851 C  CG    . PRO A 1 4150 ? 167.737 142.223 144.976 1.00 16.72  ? 4150 PRO A CG    1 
ATOM   19852 C  CD    . PRO A 1 4150 ? 167.455 143.224 146.028 1.00 17.32  ? 4150 PRO A CD    1 
ATOM   19853 N  N     . PRO A 1 4151 ? 170.672 140.096 147.667 1.00 19.61  ? 4151 PRO A N     1 
ATOM   19854 C  CA    . PRO A 1 4151 ? 172.115 139.951 147.928 1.00 19.21  ? 4151 PRO A CA    1 
ATOM   19855 C  C     . PRO A 1 4151 ? 172.988 140.054 146.690 1.00 23.09  ? 4151 PRO A C     1 
ATOM   19856 O  O     . PRO A 1 4151 ? 174.110 140.568 146.782 1.00 28.60  ? 4151 PRO A O     1 
ATOM   19857 C  CB    . PRO A 1 4151 ? 172.217 138.559 148.569 1.00 13.84  ? 4151 PRO A CB    1 
ATOM   19858 C  CG    . PRO A 1 4151 ? 170.945 137.862 148.206 1.00 15.97  ? 4151 PRO A CG    1 
ATOM   19859 C  CD    . PRO A 1 4151 ? 169.904 138.926 148.119 1.00 18.06  ? 4151 PRO A CD    1 
ATOM   19860 N  N     . GLY A 1 4152 ? 172.520 139.586 145.536 1.00 16.14  ? 4152 GLY A N     1 
ATOM   19861 C  CA    . GLY A 1 4152 ? 173.362 139.584 144.358 1.00 14.58  ? 4152 GLY A CA    1 
ATOM   19862 C  C     . GLY A 1 4152 ? 172.632 139.781 143.046 1.00 15.98  ? 4152 GLY A C     1 
ATOM   19863 O  O     . GLY A 1 4152 ? 171.424 140.037 143.026 1.00 22.12  ? 4152 GLY A O     1 
ATOM   19864 N  N     . VAL A 1 4153 ? 173.370 139.668 141.940 1.00 15.34  ? 4153 VAL A N     1 
ATOM   19865 C  CA    . VAL A 1 4153 ? 172.781 139.866 140.617 1.00 13.85  ? 4153 VAL A CA    1 
ATOM   19866 C  C     . VAL A 1 4153 ? 171.746 138.787 140.328 1.00 13.08  ? 4153 VAL A C     1 
ATOM   19867 O  O     . VAL A 1 4153 ? 170.649 139.069 139.833 1.00 14.32  ? 4153 VAL A O     1 
ATOM   19868 C  CB    . VAL A 1 4153 ? 173.883 139.895 139.543 1.00 13.34  ? 4153 VAL A CB    1 
ATOM   19869 C  CG1   . VAL A 1 4153 ? 173.285 139.718 138.158 1.00 17.05  ? 4153 VAL A CG1   1 
ATOM   19870 C  CG2   . VAL A 1 4153 ? 174.670 141.189 139.628 1.00 12.27  ? 4153 VAL A CG2   1 
ATOM   19871 N  N     . LYS A 1 4154 ? 172.084 137.531 140.632 1.00 15.42  ? 4154 LYS A N     1 
ATOM   19872 C  CA    . LYS A 1 4154 ? 171.153 136.433 140.389 1.00 13.70  ? 4154 LYS A CA    1 
ATOM   19873 C  C     . LYS A 1 4154 ? 169.890 136.584 141.227 1.00 12.48  ? 4154 LYS A C     1 
ATOM   19874 O  O     . LYS A 1 4154 ? 168.777 136.373 140.731 1.00 13.37  ? 4154 LYS A O     1 
ATOM   19875 C  CB    . LYS A 1 4154 ? 171.834 135.097 140.678 1.00 13.27  ? 4154 LYS A CB    1 
ATOM   19876 C  CG    . LYS A 1 4154 ? 170.894 133.907 140.680 1.00 15.34  ? 4154 LYS A CG    1 
ATOM   19877 C  CD    . LYS A 1 4154 ? 171.619 132.638 141.085 1.00 20.99  ? 4154 LYS A CD    1 
ATOM   19878 C  CE    . LYS A 1 4154 ? 170.662 131.464 141.179 1.00 27.55  ? 4154 LYS A CE    1 
ATOM   19879 N  NZ    . LYS A 1 4154 ? 171.380 130.187 141.440 1.00 27.66  ? 4154 LYS A NZ    1 
ATOM   19880 N  N     . ALA A 1 4155 ? 170.043 136.952 142.501 1.00 14.61  ? 4155 ALA A N     1 
ATOM   19881 C  CA    . ALA A 1 4155 ? 168.877 137.191 143.345 1.00 14.41  ? 4155 ALA A CA    1 
ATOM   19882 C  C     . ALA A 1 4155 ? 168.073 138.385 142.848 1.00 13.30  ? 4155 ALA A C     1 
ATOM   19883 O  O     . ALA A 1 4155 ? 166.838 138.375 142.893 1.00 17.22  ? 4155 ALA A O     1 
ATOM   19884 C  CB    . ALA A 1 4155 ? 169.314 137.399 144.795 1.00 15.11  ? 4155 ALA A CB    1 
ATOM   19885 N  N     . ASN A 1 4156 ? 168.760 139.429 142.378 1.00 13.93  ? 4156 ASN A N     1 
ATOM   19886 C  CA    . ASN A 1 4156 ? 168.068 140.598 141.847 1.00 10.90  ? 4156 ASN A CA    1 
ATOM   19887 C  C     . ASN A 1 4156 ? 167.245 140.245 140.615 1.00 12.33  ? 4156 ASN A C     1 
ATOM   19888 O  O     . ASN A 1 4156 ? 166.099 140.687 140.477 1.00 13.66  ? 4156 ASN A O     1 
ATOM   19889 C  CB    . ASN A 1 4156 ? 169.082 141.694 141.518 1.00 9.95   ? 4156 ASN A CB    1 
ATOM   19890 C  CG    . ASN A 1 4156 ? 168.495 143.085 141.621 1.00 9.85   ? 4156 ASN A CG    1 
ATOM   19891 O  OD1   . ASN A 1 4156 ? 167.441 143.371 141.056 1.00 12.18  ? 4156 ASN A OD1   1 
ATOM   19892 N  ND2   . ASN A 1 4156 ? 169.179 143.962 142.345 1.00 11.44  ? 4156 ASN A ND2   1 
ATOM   19893 N  N     . MET A 1 4157 ? 167.814 139.448 139.709 1.00 12.07  ? 4157 MET A N     1 
ATOM   19894 C  CA    . MET A 1 4157 ? 167.102 139.091 138.487 1.00 11.48  ? 4157 MET A CA    1 
ATOM   19895 C  C     . MET A 1 4157 ? 165.949 138.137 138.772 1.00 14.35  ? 4157 MET A C     1 
ATOM   19896 O  O     . MET A 1 4157 ? 164.899 138.214 138.124 1.00 16.77  ? 4157 MET A O     1 
ATOM   19897 C  CB    . MET A 1 4157 ? 168.072 138.482 137.477 1.00 12.50  ? 4157 MET A CB    1 
ATOM   19898 C  CG    . MET A 1 4157 ? 168.914 139.509 136.739 1.00 9.89   ? 4157 MET A CG    1 
ATOM   19899 S  SD    . MET A 1 4157 ? 169.764 138.820 135.310 1.00 29.27  ? 4157 MET A SD    1 
ATOM   19900 C  CE    . MET A 1 4157 ? 168.475 138.914 134.072 1.00 18.73  ? 4157 MET A CE    1 
ATOM   19901 N  N     . LEU A 1 4158 ? 166.128 137.225 139.731 1.00 18.44  ? 4158 LEU A N     1 
ATOM   19902 C  CA    . LEU A 1 4158 ? 165.050 136.311 140.094 1.00 16.34  ? 4158 LEU A CA    1 
ATOM   19903 C  C     . LEU A 1 4158 ? 163.873 137.060 140.704 1.00 18.21  ? 4158 LEU A C     1 
ATOM   19904 O  O     . LEU A 1 4158 ? 162.711 136.729 140.439 1.00 20.07  ? 4158 LEU A O     1 
ATOM   19905 C  CB    . LEU A 1 4158 ? 165.565 135.246 141.061 1.00 16.79  ? 4158 LEU A CB    1 
ATOM   19906 C  CG    . LEU A 1 4158 ? 166.383 134.108 140.449 1.00 16.15  ? 4158 LEU A CG    1 
ATOM   19907 C  CD1   . LEU A 1 4158 ? 166.792 133.111 141.520 1.00 24.20  ? 4158 LEU A CD1   1 
ATOM   19908 C  CD2   . LEU A 1 4158 ? 165.598 133.421 139.346 1.00 18.83  ? 4158 LEU A CD2   1 
ATOM   19909 N  N     . ARG A 1 4159 ? 164.154 138.067 141.535 1.00 18.51  ? 4159 ARG A N     1 
ATOM   19910 C  CA    . ARG A 1 4159 ? 163.084 138.868 142.121 1.00 19.40  ? 4159 ARG A CA    1 
ATOM   19911 C  C     . ARG A 1 4159 ? 162.327 139.644 141.050 1.00 21.97  ? 4159 ARG A C     1 
ATOM   19912 O  O     . ARG A 1 4159 ? 161.099 139.774 141.117 1.00 27.02  ? 4159 ARG A O     1 
ATOM   19913 C  CB    . ARG A 1 4159 ? 163.659 139.816 143.173 1.00 20.32  ? 4159 ARG A CB    1 
ATOM   19914 C  CG    . ARG A 1 4159 ? 162.668 140.834 143.708 1.00 22.43  ? 4159 ARG A CG    1 
ATOM   19915 C  CD    . ARG A 1 4159 ? 163.131 141.402 145.039 1.00 27.44  ? 4159 ARG A CD    1 
ATOM   19916 N  NE    . ARG A 1 4159 ? 163.831 140.409 145.845 1.00 31.04  ? 4159 ARG A NE    1 
ATOM   19917 C  CZ    . ARG A 1 4159 ? 164.488 140.680 146.965 1.00 27.58  ? 4159 ARG A CZ    1 
ATOM   19918 N  NH1   . ARG A 1 4159 ? 164.555 141.910 147.446 1.00 22.16  ? 4159 ARG A NH1   1 
ATOM   19919 N  NH2   . ARG A 1 4159 ? 165.095 139.692 147.617 1.00 25.37  ? 4159 ARG A NH2   1 
ATOM   19920 N  N     . THR A 1 4160 ? 163.046 140.174 140.057 1.00 21.02  ? 4160 THR A N     1 
ATOM   19921 C  CA    . THR A 1 4160 ? 162.394 140.922 138.987 1.00 20.23  ? 4160 THR A CA    1 
ATOM   19922 C  C     . THR A 1 4160 ? 161.471 140.030 138.166 1.00 21.88  ? 4160 THR A C     1 
ATOM   19923 O  O     . THR A 1 4160 ? 160.332 140.409 137.868 1.00 30.03  ? 4160 THR A O     1 
ATOM   19924 C  CB    . THR A 1 4160 ? 163.448 141.573 138.090 1.00 16.08  ? 4160 THR A CB    1 
ATOM   19925 O  OG1   . THR A 1 4160 ? 164.074 142.654 138.793 1.00 19.72  ? 4160 THR A OG1   1 
ATOM   19926 C  CG2   . THR A 1 4160 ? 162.815 142.107 136.816 1.00 14.46  ? 4160 THR A CG2   1 
ATOM   19927 N  N     . PHE A 1 4161 ? 161.939 138.834 137.799 1.00 19.66  ? 4161 PHE A N     1 
ATOM   19928 C  CA    . PHE A 1 4161 ? 161.120 137.945 136.982 1.00 21.30  ? 4161 PHE A CA    1 
ATOM   19929 C  C     . PHE A 1 4161 ? 159.926 137.407 137.758 1.00 27.80  ? 4161 PHE A C     1 
ATOM   19930 O  O     . PHE A 1 4161 ? 158.910 137.041 137.156 1.00 33.65  ? 4161 PHE A O     1 
ATOM   19931 C  CB    . PHE A 1 4161 ? 161.970 136.796 136.441 1.00 20.65  ? 4161 PHE A CB    1 
ATOM   19932 C  CG    . PHE A 1 4161 ? 162.652 137.112 135.142 1.00 23.15  ? 4161 PHE A CG    1 
ATOM   19933 C  CD1   . PHE A 1 4161 ? 161.916 137.278 133.981 1.00 24.94  ? 4161 PHE A CD1   1 
ATOM   19934 C  CD2   . PHE A 1 4161 ? 164.029 137.250 135.082 1.00 24.58  ? 4161 PHE A CD2   1 
ATOM   19935 C  CE1   . PHE A 1 4161 ? 162.538 137.572 132.785 1.00 27.74  ? 4161 PHE A CE1   1 
ATOM   19936 C  CE2   . PHE A 1 4161 ? 164.657 137.544 133.888 1.00 31.32  ? 4161 PHE A CE2   1 
ATOM   19937 C  CZ    . PHE A 1 4161 ? 163.911 137.705 132.738 1.00 31.04  ? 4161 PHE A CZ    1 
ATOM   19938 N  N     . SER A 1 4162 ? 160.027 137.346 139.087 1.00 28.02  ? 4162 SER A N     1 
ATOM   19939 C  CA    . SER A 1 4162 ? 158.881 136.943 139.895 1.00 25.70  ? 4162 SER A CA    1 
ATOM   19940 C  C     . SER A 1 4162 ? 157.859 138.068 140.004 1.00 30.43  ? 4162 SER A C     1 
ATOM   19941 O  O     . SER A 1 4162 ? 156.648 137.818 139.991 1.00 42.59  ? 4162 SER A O     1 
ATOM   19942 C  CB    . SER A 1 4162 ? 159.347 136.502 141.282 1.00 26.73  ? 4162 SER A CB    1 
ATOM   19943 O  OG    . SER A 1 4162 ? 159.518 137.617 142.139 1.00 27.33  ? 4162 SER A OG    1 
ATOM   19944 N  N     . SER A 1 4163 ? 158.328 139.313 140.115 1.00 29.16  ? 4163 SER A N     1 
ATOM   19945 C  CA    . SER A 1 4163 ? 157.414 140.438 140.287 1.00 28.50  ? 4163 SER A CA    1 
ATOM   19946 C  C     . SER A 1 4163 ? 156.614 140.709 139.018 1.00 33.68  ? 4163 SER A C     1 
ATOM   19947 O  O     . SER A 1 4163 ? 155.419 141.017 139.087 1.00 35.52  ? 4163 SER A O     1 
ATOM   19948 C  CB    . SER A 1 4163 ? 158.193 141.685 140.705 1.00 33.29  ? 4163 SER A CB    1 
ATOM   19949 O  OG    . SER A 1 4163 ? 157.364 142.591 141.411 1.00 42.00  ? 4163 SER A OG    1 
ATOM   19950 N  N     . ILE A 1 4164 ? 157.250 140.606 137.860 1.00 33.34  ? 4164 ILE A N     1 
ATOM   19951 C  CA    . ILE A 1 4164 ? 156.564 140.878 136.595 1.00 35.02  ? 4164 ILE A CA    1 
ATOM   19952 C  C     . ILE A 1 4164 ? 155.700 139.673 136.233 1.00 34.42  ? 4164 ILE A C     1 
ATOM   19953 O  O     . ILE A 1 4164 ? 156.217 138.546 136.176 1.00 35.30  ? 4164 ILE A O     1 
ATOM   19954 C  CB    . ILE A 1 4164 ? 157.572 141.183 135.492 1.00 34.79  ? 4164 ILE A CB    1 
ATOM   19955 C  CG1   . ILE A 1 4164 ? 158.475 142.346 135.906 1.00 29.15  ? 4164 ILE A CG1   1 
ATOM   19956 C  CG2   . ILE A 1 4164 ? 156.853 141.505 134.192 1.00 33.04  ? 4164 ILE A CG2   1 
ATOM   19957 C  CD1   . ILE A 1 4164 ? 159.620 142.596 134.953 1.00 27.44  ? 4164 ILE A CD1   1 
ATOM   19958 N  N     . PRO A 1 4165 ? 154.402 139.861 135.997 1.00 34.09  ? 4165 PRO A N     1 
ATOM   19959 C  CA    . PRO A 1 4165 ? 153.546 138.728 135.630 1.00 35.38  ? 4165 PRO A CA    1 
ATOM   19960 C  C     . PRO A 1 4165 ? 153.980 138.096 134.316 1.00 36.20  ? 4165 PRO A C     1 
ATOM   19961 O  O     . PRO A 1 4165 ? 154.495 138.764 133.417 1.00 39.93  ? 4165 PRO A O     1 
ATOM   19962 C  CB    . PRO A 1 4165 ? 152.152 139.357 135.514 1.00 32.07  ? 4165 PRO A CB    1 
ATOM   19963 C  CG    . PRO A 1 4165 ? 152.230 140.613 136.322 1.00 34.06  ? 4165 PRO A CG    1 
ATOM   19964 C  CD    . PRO A 1 4165 ? 153.634 141.106 136.163 1.00 37.07  ? 4165 PRO A CD    1 
ATOM   19965 N  N     . VAL A 1 4166 ? 153.768 136.781 134.221 1.00 40.07  ? 4166 VAL A N     1 
ATOM   19966 C  CA    . VAL A 1 4166 ? 154.181 136.036 133.035 1.00 41.99  ? 4166 VAL A CA    1 
ATOM   19967 C  C     . VAL A 1 4166 ? 153.416 136.512 131.807 1.00 43.24  ? 4166 VAL A C     1 
ATOM   19968 O  O     . VAL A 1 4166 ? 153.986 136.657 130.719 1.00 41.86  ? 4166 VAL A O     1 
ATOM   19969 C  CB    . VAL A 1 4166 ? 153.997 134.525 133.265 1.00 42.63  ? 4166 VAL A CB    1 
ATOM   19970 C  CG1   . VAL A 1 4166 ? 154.336 133.747 132.003 1.00 43.55  ? 4166 VAL A CG1   1 
ATOM   19971 C  CG2   . VAL A 1 4166 ? 154.847 134.058 134.434 1.00 39.10  ? 4166 VAL A CG2   1 
ATOM   19972 N  N     . SER A 1 4167 ? 152.112 136.761 131.960 1.00 43.86  ? 4167 SER A N     1 
ATOM   19973 C  CA    . SER A 1 4167 ? 151.287 137.145 130.819 1.00 42.53  ? 4167 SER A CA    1 
ATOM   19974 C  C     . SER A 1 4167 ? 151.740 138.465 130.208 1.00 41.34  ? 4167 SER A C     1 
ATOM   19975 O  O     . SER A 1 4167 ? 151.512 138.706 129.017 1.00 43.92  ? 4167 SER A O     1 
ATOM   19976 C  CB    . SER A 1 4167 ? 149.820 137.231 131.241 1.00 37.69  ? 4167 SER A CB    1 
ATOM   19977 O  OG    . SER A 1 4167 ? 149.665 138.065 132.376 1.00 44.50  ? 4167 SER A OG    1 
ATOM   19978 N  N     . ARG A 1 4168 ? 152.376 139.330 131.000 1.00 34.50  ? 4168 ARG A N     1 
ATOM   19979 C  CA    . ARG A 1 4168 ? 152.893 140.581 130.456 1.00 34.06  ? 4168 ARG A CA    1 
ATOM   19980 C  C     . ARG A 1 4168 ? 154.110 140.340 129.571 1.00 34.86  ? 4168 ARG A C     1 
ATOM   19981 O  O     . ARG A 1 4168 ? 154.233 140.940 128.497 1.00 34.35  ? 4168 ARG A O     1 
ATOM   19982 C  CB    . ARG A 1 4168 ? 153.238 141.542 131.593 1.00 30.02  ? 4168 ARG A CB    1 
ATOM   19983 C  CG    . ARG A 1 4168 ? 153.762 142.885 131.124 1.00 26.52  ? 4168 ARG A CG    1 
ATOM   19984 C  CD    . ARG A 1 4168 ? 154.247 143.726 132.289 1.00 28.13  ? 4168 ARG A CD    1 
ATOM   19985 N  NE    . ARG A 1 4168 ? 154.021 145.147 132.059 1.00 26.73  ? 4168 ARG A NE    1 
ATOM   19986 C  CZ    . ARG A 1 4168 ? 154.220 146.094 132.965 1.00 25.12  ? 4168 ARG A CZ    1 
ATOM   19987 N  NH1   . ARG A 1 4168 ? 154.651 145.806 134.182 1.00 26.89  ? 4168 ARG A NH1   1 
ATOM   19988 N  NH2   . ARG A 1 4168 ? 153.983 147.361 132.640 1.00 27.09  ? 4168 ARG A NH2   1 
ATOM   19989 N  N     . ILE A 1 4169 ? 155.022 139.468 130.007 1.00 38.78  ? 4169 ILE A N     1 
ATOM   19990 C  CA    . ILE A 1 4169 ? 156.230 139.200 129.234 1.00 36.19  ? 4169 ILE A CA    1 
ATOM   19991 C  C     . ILE A 1 4169 ? 155.898 138.426 127.964 1.00 37.26  ? 4169 ILE A C     1 
ATOM   19992 O  O     . ILE A 1 4169 ? 156.484 138.668 126.902 1.00 32.87  ? 4169 ILE A O     1 
ATOM   19993 C  CB    . ILE A 1 4169 ? 157.260 138.452 130.099 1.00 34.15  ? 4169 ILE A CB    1 
ATOM   19994 C  CG1   . ILE A 1 4169 ? 157.420 139.147 131.453 1.00 33.45  ? 4169 ILE A CG1   1 
ATOM   19995 C  CG2   . ILE A 1 4169 ? 158.594 138.352 129.373 1.00 29.80  ? 4169 ILE A CG2   1 
ATOM   19996 C  CD1   . ILE A 1 4169 ? 158.748 138.887 132.131 1.00 40.07  ? 4169 ILE A CD1   1 
ATOM   19997 N  N     . CYS A 1 4170 ? 154.959 137.485 128.050 1.00 38.66  ? 4170 CYS A N     1 
ATOM   19998 C  CA    . CYS A 1 4170 ? 154.624 136.618 126.919 1.00 41.28  ? 4170 CYS A CA    1 
ATOM   19999 C  C     . CYS A 1 4170 ? 153.459 137.219 126.131 1.00 47.55  ? 4170 CYS A C     1 
ATOM   20000 O  O     . CYS A 1 4170 ? 152.341 136.702 126.102 1.00 52.70  ? 4170 CYS A O     1 
ATOM   20001 C  CB    . CYS A 1 4170 ? 154.308 135.211 127.407 1.00 50.11  ? 4170 CYS A CB    1 
ATOM   20002 S  SG    . CYS A 1 4170 ? 155.718 134.334 128.121 1.00 69.48  ? 4170 CYS A SG    1 
ATOM   20003 N  N     . LYS A 1 4171 ? 153.749 138.340 125.479 1.00 48.23  ? 4171 LYS A N     1 
ATOM   20004 C  CA    . LYS A 1 4171 ? 152.789 139.017 124.625 1.00 45.28  ? 4171 LYS A CA    1 
ATOM   20005 C  C     . LYS A 1 4171 ? 153.084 138.697 123.160 1.00 51.22  ? 4171 LYS A C     1 
ATOM   20006 O  O     . LYS A 1 4171 ? 153.907 137.831 122.844 1.00 55.91  ? 4171 LYS A O     1 
ATOM   20007 C  CB    . LYS A 1 4171 ? 152.798 140.521 124.902 1.00 38.57  ? 4171 LYS A CB    1 
ATOM   20008 C  CG    . LYS A 1 4171 ? 151.866 140.934 126.030 1.00 40.33  ? 4171 LYS A CG    1 
ATOM   20009 C  CD    . LYS A 1 4171 ? 151.768 142.444 126.151 1.00 43.27  ? 4171 LYS A CD    1 
ATOM   20010 C  CE    . LYS A 1 4171 ? 151.016 143.040 124.972 1.00 36.18  ? 4171 LYS A CE    1 
ATOM   20011 N  NZ    . LYS A 1 4171 ? 149.579 142.649 124.978 1.00 44.77  ? 4171 LYS A NZ    1 
ATOM   20012 N  N     . SER A 1 4172 ? 152.393 139.391 122.255 1.00 49.36  ? 4172 SER A N     1 
ATOM   20013 C  CA    . SER A 1 4172 ? 152.486 139.072 120.830 1.00 57.27  ? 4172 SER A CA    1 
ATOM   20014 C  C     . SER A 1 4172 ? 153.907 139.147 120.281 1.00 56.18  ? 4172 SER A C     1 
ATOM   20015 O  O     . SER A 1 4172 ? 154.324 138.199 119.592 1.00 58.88  ? 4172 SER A O     1 
ATOM   20016 C  CB    . SER A 1 4172 ? 151.534 139.976 120.040 1.00 62.28  ? 4172 SER A CB    1 
ATOM   20017 O  OG    . SER A 1 4172 ? 150.189 139.781 120.444 1.00 65.53  ? 4172 SER A OG    1 
ATOM   20018 N  N     . PRO A 1 4173 ? 154.694 140.200 120.521 1.00 53.29  ? 4173 PRO A N     1 
ATOM   20019 C  CA    . PRO A 1 4173 ? 156.065 140.209 119.989 1.00 51.38  ? 4173 PRO A CA    1 
ATOM   20020 C  C     . PRO A 1 4173 ? 156.957 139.248 120.763 1.00 50.58  ? 4173 PRO A C     1 
ATOM   20021 O  O     . PRO A 1 4173 ? 157.099 139.356 121.983 1.00 49.55  ? 4173 PRO A O     1 
ATOM   20022 C  CB    . PRO A 1 4173 ? 156.514 141.666 120.166 1.00 39.62  ? 4173 PRO A CB    1 
ATOM   20023 C  CG    . PRO A 1 4173 ? 155.267 142.437 120.471 1.00 43.75  ? 4173 PRO A CG    1 
ATOM   20024 C  CD    . PRO A 1 4173 ? 154.381 141.476 121.186 1.00 46.21  ? 4173 PRO A CD    1 
ATOM   20025 N  N     . ASN A 1 4174 ? 157.559 138.300 120.039 1.00 48.47  ? 4174 ASN A N     1 
ATOM   20026 C  CA    . ASN A 1 4174 ? 158.483 137.359 120.660 1.00 50.15  ? 4174 ASN A CA    1 
ATOM   20027 C  C     . ASN A 1 4174 ? 159.728 138.047 121.204 1.00 47.32  ? 4174 ASN A C     1 
ATOM   20028 O  O     . ASN A 1 4174 ? 160.396 137.490 122.082 1.00 44.49  ? 4174 ASN A O     1 
ATOM   20029 C  CB    . ASN A 1 4174 ? 158.889 136.268 119.663 1.00 52.68  ? 4174 ASN A CB    1 
ATOM   20030 C  CG    . ASN A 1 4174 ? 157.698 135.523 119.086 1.00 58.03  ? 4174 ASN A CG    1 
ATOM   20031 O  OD1   . ASN A 1 4174 ? 157.462 134.361 119.416 1.00 61.92  ? 4174 ASN A OD1   1 
ATOM   20032 N  ND2   . ASN A 1 4174 ? 156.955 136.179 118.205 1.00 58.11  ? 4174 ASN A ND2   1 
ATOM   20033 N  N     . GLU A 1 4175 ? 160.048 139.242 120.709 1.00 42.45  ? 4175 GLU A N     1 
ATOM   20034 C  CA    . GLU A 1 4175 ? 161.214 139.986 121.164 1.00 39.43  ? 4175 GLU A CA    1 
ATOM   20035 C  C     . GLU A 1 4175 ? 160.987 140.691 122.494 1.00 33.76  ? 4175 GLU A C     1 
ATOM   20036 O  O     . GLU A 1 4175 ? 161.942 141.239 123.055 1.00 30.84  ? 4175 GLU A O     1 
ATOM   20037 C  CB    . GLU A 1 4175 ? 161.625 141.010 120.101 1.00 41.31  ? 4175 GLU A CB    1 
ATOM   20038 C  CG    . GLU A 1 4175 ? 162.301 140.411 118.873 1.00 42.02  ? 4175 GLU A CG    1 
ATOM   20039 C  CD    . GLU A 1 4175 ? 161.363 139.590 118.006 1.00 48.95  ? 4175 GLU A CD    1 
ATOM   20040 O  OE1   . GLU A 1 4175 ? 160.134 139.647 118.223 1.00 55.25  ? 4175 GLU A OE1   1 
ATOM   20041 O  OE2   . GLU A 1 4175 ? 161.859 138.881 117.106 1.00 47.11  ? 4175 GLU A OE2   1 
ATOM   20042 N  N     . ARG A 1 4176 ? 159.753 140.695 123.004 1.00 33.44  ? 4176 ARG A N     1 
ATOM   20043 C  CA    . ARG A 1 4176 ? 159.478 141.346 124.281 1.00 28.62  ? 4176 ARG A CA    1 
ATOM   20044 C  C     . ARG A 1 4176 ? 160.193 140.643 125.428 1.00 26.85  ? 4176 ARG A C     1 
ATOM   20045 O  O     . ARG A 1 4176 ? 160.665 141.294 126.368 1.00 28.25  ? 4176 ARG A O     1 
ATOM   20046 C  CB    . ARG A 1 4176 ? 157.971 141.386 124.535 1.00 31.17  ? 4176 ARG A CB    1 
ATOM   20047 C  CG    . ARG A 1 4176 ? 157.573 142.130 125.800 1.00 30.02  ? 4176 ARG A CG    1 
ATOM   20048 C  CD    . ARG A 1 4176 ? 156.063 142.222 125.937 1.00 29.33  ? 4176 ARG A CD    1 
ATOM   20049 N  NE    . ARG A 1 4176 ? 155.430 142.660 124.700 1.00 36.29  ? 4176 ARG A NE    1 
ATOM   20050 C  CZ    . ARG A 1 4176 ? 154.700 143.760 124.580 1.00 33.13  ? 4176 ARG A CZ    1 
ATOM   20051 N  NH1   . ARG A 1 4176 ? 154.492 144.566 125.608 1.00 33.13  ? 4176 ARG A NH1   1 
ATOM   20052 N  NH2   . ARG A 1 4176 ? 154.167 144.059 123.400 1.00 35.62  ? 4176 ARG A NH2   1 
ATOM   20053 N  N     . ALA A 1 4177 ? 160.274 139.311 125.372 1.00 28.38  ? 4177 ALA A N     1 
ATOM   20054 C  CA    . ALA A 1 4177 ? 160.912 138.562 126.450 1.00 25.27  ? 4177 ALA A CA    1 
ATOM   20055 C  C     . ALA A 1 4177 ? 162.387 138.920 126.581 1.00 24.45  ? 4177 ALA A C     1 
ATOM   20056 O  O     . ALA A 1 4177 ? 162.901 139.061 127.696 1.00 24.64  ? 4177 ALA A O     1 
ATOM   20057 C  CB    . ALA A 1 4177 ? 160.742 137.061 126.217 1.00 28.66  ? 4177 ALA A CB    1 
ATOM   20058 N  N     . ARG A 1 4178 ? 163.086 139.065 125.452 1.00 23.23  ? 4178 ARG A N     1 
ATOM   20059 C  CA    . ARG A 1 4178 ? 164.491 139.457 125.504 1.00 19.27  ? 4178 ARG A CA    1 
ATOM   20060 C  C     . ARG A 1 4178 ? 164.654 140.858 126.078 1.00 19.43  ? 4178 ARG A C     1 
ATOM   20061 O  O     . ARG A 1 4178 ? 165.546 141.097 126.899 1.00 20.41  ? 4178 ARG A O     1 
ATOM   20062 C  CB    . ARG A 1 4178 ? 165.115 139.373 124.113 1.00 20.29  ? 4178 ARG A CB    1 
ATOM   20063 C  CG    . ARG A 1 4178 ? 166.632 139.373 124.127 1.00 24.17  ? 4178 ARG A CG    1 
ATOM   20064 C  CD    . ARG A 1 4178 ? 167.194 138.808 122.840 1.00 27.01  ? 4178 ARG A CD    1 
ATOM   20065 N  NE    . ARG A 1 4178 ? 168.512 138.220 123.035 1.00 33.58  ? 4178 ARG A NE    1 
ATOM   20066 C  CZ    . ARG A 1 4178 ? 168.819 136.965 122.740 1.00 37.85  ? 4178 ARG A CZ    1 
ATOM   20067 N  NH1   . ARG A 1 4178 ? 167.921 136.133 122.239 1.00 44.28  ? 4178 ARG A NH1   1 
ATOM   20068 N  NH2   . ARG A 1 4178 ? 170.060 136.534 122.950 1.00 38.16  ? 4178 ARG A NH2   1 
ATOM   20069 N  N     . LEU A 1 4179 ? 163.793 141.794 125.670 1.00 20.10  ? 4179 LEU A N     1 
ATOM   20070 C  CA    . LEU A 1 4179 ? 163.890 143.160 126.174 1.00 15.65  ? 4179 LEU A CA    1 
ATOM   20071 C  C     . LEU A 1 4179 ? 163.694 143.203 127.683 1.00 18.10  ? 4179 LEU A C     1 
ATOM   20072 O  O     . LEU A 1 4179 ? 164.358 143.977 128.383 1.00 23.10  ? 4179 LEU A O     1 
ATOM   20073 C  CB    . LEU A 1 4179 ? 162.867 144.054 125.475 1.00 16.75  ? 4179 LEU A CB    1 
ATOM   20074 C  CG    . LEU A 1 4179 ? 163.130 144.377 124.005 1.00 16.16  ? 4179 LEU A CG    1 
ATOM   20075 C  CD1   . LEU A 1 4179 ? 162.235 145.510 123.533 1.00 21.44  ? 4179 LEU A CD1   1 
ATOM   20076 C  CD2   . LEU A 1 4179 ? 164.590 144.721 123.793 1.00 17.52  ? 4179 LEU A CD2   1 
ATOM   20077 N  N     . TYR A 1 4180 ? 162.779 142.383 128.201 1.00 17.39  ? 4180 TYR A N     1 
ATOM   20078 C  CA    . TYR A 1 4180 ? 162.581 142.314 129.643 1.00 16.03  ? 4180 TYR A CA    1 
ATOM   20079 C  C     . TYR A 1 4180 ? 163.805 141.735 130.343 1.00 18.21  ? 4180 TYR A C     1 
ATOM   20080 O  O     . TYR A 1 4180 ? 164.116 142.118 131.477 1.00 25.02  ? 4180 TYR A O     1 
ATOM   20081 C  CB    . TYR A 1 4180 ? 161.333 141.491 129.958 1.00 23.17  ? 4180 TYR A CB    1 
ATOM   20082 C  CG    . TYR A 1 4180 ? 160.078 142.325 130.052 1.00 25.67  ? 4180 TYR A CG    1 
ATOM   20083 C  CD1   . TYR A 1 4180 ? 159.548 142.942 128.928 1.00 24.95  ? 4180 TYR A CD1   1 
ATOM   20084 C  CD2   . TYR A 1 4180 ? 159.425 142.502 131.264 1.00 29.06  ? 4180 TYR A CD2   1 
ATOM   20085 C  CE1   . TYR A 1 4180 ? 158.404 143.709 129.006 1.00 25.23  ? 4180 TYR A CE1   1 
ATOM   20086 C  CE2   . TYR A 1 4180 ? 158.279 143.268 131.351 1.00 31.87  ? 4180 TYR A CE2   1 
ATOM   20087 C  CZ    . TYR A 1 4180 ? 157.773 143.869 130.219 1.00 28.26  ? 4180 TYR A CZ    1 
ATOM   20088 O  OH    . TYR A 1 4180 ? 156.633 144.633 130.303 1.00 30.00  ? 4180 TYR A OH    1 
ATOM   20089 N  N     . PHE A 1 4181 ? 164.505 140.802 129.690 1.00 17.47  ? 4181 PHE A N     1 
ATOM   20090 C  CA    . PHE A 1 4181 ? 165.704 140.226 130.290 1.00 14.54  ? 4181 PHE A CA    1 
ATOM   20091 C  C     . PHE A 1 4181 ? 166.823 141.256 130.378 1.00 14.50  ? 4181 PHE A C     1 
ATOM   20092 O  O     . PHE A 1 4181 ? 167.488 141.372 131.415 1.00 17.68  ? 4181 PHE A O     1 
ATOM   20093 C  CB    . PHE A 1 4181 ? 166.147 138.992 129.496 1.00 20.19  ? 4181 PHE A CB    1 
ATOM   20094 C  CG    . PHE A 1 4181 ? 167.491 138.444 129.906 1.00 19.73  ? 4181 PHE A CG    1 
ATOM   20095 C  CD1   . PHE A 1 4181 ? 167.570 137.364 130.768 1.00 22.39  ? 4181 PHE A CD1   1 
ATOM   20096 C  CD2   . PHE A 1 4181 ? 168.667 138.969 129.393 1.00 24.42  ? 4181 PHE A CD2   1 
ATOM   20097 C  CE1   . PHE A 1 4181 ? 168.793 136.848 131.145 1.00 29.53  ? 4181 PHE A CE1   1 
ATOM   20098 C  CE2   . PHE A 1 4181 ? 169.892 138.456 129.767 1.00 25.90  ? 4181 PHE A CE2   1 
ATOM   20099 C  CZ    . PHE A 1 4181 ? 169.955 137.393 130.641 1.00 28.48  ? 4181 PHE A CZ    1 
ATOM   20100 N  N     . LEU A 1 4182 ? 167.057 142.004 129.297 1.00 16.70  ? 4182 LEU A N     1 
ATOM   20101 C  CA    . LEU A 1 4182 ? 168.007 143.110 129.363 1.00 13.97  ? 4182 LEU A CA    1 
ATOM   20102 C  C     . LEU A 1 4182 ? 167.572 144.138 130.398 1.00 11.46  ? 4182 LEU A C     1 
ATOM   20103 O  O     . LEU A 1 4182 ? 168.411 144.790 131.028 1.00 12.61  ? 4182 LEU A O     1 
ATOM   20104 C  CB    . LEU A 1 4182 ? 168.177 143.763 127.988 1.00 13.27  ? 4182 LEU A CB    1 
ATOM   20105 C  CG    . LEU A 1 4182 ? 169.054 143.108 126.910 1.00 14.26  ? 4182 LEU A CG    1 
ATOM   20106 C  CD1   . LEU A 1 4182 ? 170.484 142.950 127.415 1.00 18.20  ? 4182 LEU A CD1   1 
ATOM   20107 C  CD2   . LEU A 1 4182 ? 168.508 141.775 126.408 1.00 19.48  ? 4182 LEU A CD2   1 
ATOM   20108 N  N     . LEU A 1 4183 ? 166.261 144.300 130.585 1.00 11.94  ? 4183 LEU A N     1 
ATOM   20109 C  CA    . LEU A 1 4183 ? 165.775 145.182 131.638 1.00 11.02  ? 4183 LEU A CA    1 
ATOM   20110 C  C     . LEU A 1 4183 ? 166.148 144.656 133.017 1.00 12.00  ? 4183 LEU A C     1 
ATOM   20111 O  O     . LEU A 1 4183 ? 166.596 145.418 133.881 1.00 11.12  ? 4183 LEU A O     1 
ATOM   20112 C  CB    . LEU A 1 4183 ? 164.263 145.345 131.529 1.00 12.80  ? 4183 LEU A CB    1 
ATOM   20113 C  CG    . LEU A 1 4183 ? 163.812 146.798 131.543 1.00 13.78  ? 4183 LEU A CG    1 
ATOM   20114 C  CD1   . LEU A 1 4183 ? 164.712 147.586 130.619 1.00 14.95  ? 4183 LEU A CD1   1 
ATOM   20115 C  CD2   . LEU A 1 4183 ? 162.369 146.895 131.103 1.00 17.99  ? 4183 LEU A CD2   1 
ATOM   20116 N  N     . ALA A 1 4184 ? 165.951 143.356 133.246 1.00 10.10  ? 4184 ALA A N     1 
ATOM   20117 C  CA    . ALA A 1 4184 ? 166.308 142.768 134.533 1.00 10.35  ? 4184 ALA A CA    1 
ATOM   20118 C  C     . ALA A 1 4184 ? 167.811 142.817 134.763 1.00 11.30  ? 4184 ALA A C     1 
ATOM   20119 O  O     . ALA A 1 4184 ? 168.269 143.120 135.872 1.00 14.35  ? 4184 ALA A O     1 
ATOM   20120 C  CB    . ALA A 1 4184 ? 165.803 141.329 134.613 1.00 15.17  ? 4184 ALA A CB    1 
ATOM   20121 N  N     . TRP A 1 4185 ? 168.597 142.509 133.730 1.00 8.72   ? 4185 TRP A N     1 
ATOM   20122 C  CA    . TRP A 1 4185 ? 170.047 142.539 133.873 1.00 8.41   ? 4185 TRP A CA    1 
ATOM   20123 C  C     . TRP A 1 4185 ? 170.548 143.953 134.128 1.00 8.02   ? 4185 TRP A C     1 
ATOM   20124 O  O     . TRP A 1 4185 ? 171.401 144.169 134.996 1.00 8.70   ? 4185 TRP A O     1 
ATOM   20125 C  CB    . TRP A 1 4185 ? 170.712 141.953 132.630 1.00 11.86  ? 4185 TRP A CB    1 
ATOM   20126 C  CG    . TRP A 1 4185 ? 172.203 142.064 132.653 1.00 10.96  ? 4185 TRP A CG    1 
ATOM   20127 C  CD1   . TRP A 1 4185 ? 172.961 143.072 132.131 1.00 11.69  ? 4185 TRP A CD1   1 
ATOM   20128 C  CD2   . TRP A 1 4185 ? 173.119 141.137 133.241 1.00 10.51  ? 4185 TRP A CD2   1 
ATOM   20129 N  NE1   . TRP A 1 4185 ? 174.294 142.825 132.353 1.00 16.30  ? 4185 TRP A NE1   1 
ATOM   20130 C  CE2   . TRP A 1 4185 ? 174.417 141.642 133.033 1.00 14.46  ? 4185 TRP A CE2   1 
ATOM   20131 C  CE3   . TRP A 1 4185 ? 172.967 139.926 133.922 1.00 13.58  ? 4185 TRP A CE3   1 
ATOM   20132 C  CZ2   . TRP A 1 4185 ? 175.556 140.979 133.481 1.00 15.48  ? 4185 TRP A CZ2   1 
ATOM   20133 C  CZ3   . TRP A 1 4185 ? 174.098 139.269 134.365 1.00 17.77  ? 4185 TRP A CZ3   1 
ATOM   20134 C  CH2   . TRP A 1 4185 ? 175.376 139.797 134.143 1.00 17.28  ? 4185 TRP A CH2   1 
ATOM   20135 N  N     . PHE A 1 4186 ? 170.031 144.930 133.378 1.00 8.14   ? 4186 PHE A N     1 
ATOM   20136 C  CA    . PHE A 1 4186 ? 170.421 146.317 133.603 1.00 5.73   ? 4186 PHE A CA    1 
ATOM   20137 C  C     . PHE A 1 4186 ? 170.062 146.756 135.015 1.00 6.03   ? 4186 PHE A C     1 
ATOM   20138 O  O     . PHE A 1 4186 ? 170.874 147.374 135.711 1.00 6.60   ? 4186 PHE A O     1 
ATOM   20139 C  CB    . PHE A 1 4186 ? 169.753 147.228 132.572 1.00 7.63   ? 4186 PHE A CB    1 
ATOM   20140 C  CG    . PHE A 1 4186 ? 170.037 148.689 132.781 1.00 5.62   ? 4186 PHE A CG    1 
ATOM   20141 C  CD1   . PHE A 1 4186 ? 171.224 149.249 132.342 1.00 5.54   ? 4186 PHE A CD1   1 
ATOM   20142 C  CD2   . PHE A 1 4186 ? 169.118 149.500 133.426 1.00 5.57   ? 4186 PHE A CD2   1 
ATOM   20143 C  CE1   . PHE A 1 4186 ? 171.487 150.591 132.536 1.00 6.62   ? 4186 PHE A CE1   1 
ATOM   20144 C  CE2   . PHE A 1 4186 ? 169.376 150.842 133.626 1.00 4.98   ? 4186 PHE A CE2   1 
ATOM   20145 C  CZ    . PHE A 1 4186 ? 170.563 151.388 133.180 1.00 6.62   ? 4186 PHE A CZ    1 
ATOM   20146 N  N     . HIS A 1 4187 ? 168.845 146.435 135.457 1.00 7.68   ? 4187 HIS A N     1 
ATOM   20147 C  CA    . HIS A 1 4187 ? 168.431 146.799 136.807 1.00 5.37   ? 4187 HIS A CA    1 
ATOM   20148 C  C     . HIS A 1 4187 ? 169.295 146.109 137.854 1.00 6.20   ? 4187 HIS A C     1 
ATOM   20149 O  O     . HIS A 1 4187 ? 169.740 146.743 138.815 1.00 6.73   ? 4187 HIS A O     1 
ATOM   20150 C  CB    . HIS A 1 4187 ? 166.956 146.455 137.010 1.00 8.50   ? 4187 HIS A CB    1 
ATOM   20151 C  CG    . HIS A 1 4187 ? 166.360 147.057 138.243 1.00 9.66   ? 4187 HIS A CG    1 
ATOM   20152 N  ND1   . HIS A 1 4187 ? 166.150 148.412 138.383 1.00 8.65   ? 4187 HIS A ND1   1 
ATOM   20153 C  CD2   . HIS A 1 4187 ? 165.924 146.488 139.391 1.00 6.22   ? 4187 HIS A CD2   1 
ATOM   20154 C  CE1   . HIS A 1 4187 ? 165.613 148.652 139.566 1.00 9.40   ? 4187 HIS A CE1   1 
ATOM   20155 N  NE2   . HIS A 1 4187 ? 165.465 147.501 140.197 1.00 10.41  ? 4187 HIS A NE2   1 
ATOM   20156 N  N     . ALA A 1 4188 ? 169.562 144.813 137.672 1.00 8.01   ? 4188 ALA A N     1 
ATOM   20157 C  CA    . ALA A 1 4188 ? 170.356 144.072 138.648 1.00 6.22   ? 4188 ALA A CA    1 
ATOM   20158 C  C     . ALA A 1 4188 ? 171.771 144.625 138.750 1.00 7.46   ? 4188 ALA A C     1 
ATOM   20159 O  O     . ALA A 1 4188 ? 172.316 144.755 139.853 1.00 11.17  ? 4188 ALA A O     1 
ATOM   20160 C  CB    . ALA A 1 4188 ? 170.387 142.589 138.281 1.00 9.20   ? 4188 ALA A CB    1 
ATOM   20161 N  N     . ILE A 1 4189 ? 172.384 144.953 137.611 1.00 6.73   ? 4189 ILE A N     1 
ATOM   20162 C  CA    . ILE A 1 4189 ? 173.733 145.510 137.627 1.00 5.50   ? 4189 ILE A CA    1 
ATOM   20163 C  C     . ILE A 1 4189 ? 173.737 146.864 138.325 1.00 6.03   ? 4189 ILE A C     1 
ATOM   20164 O  O     . ILE A 1 4189 ? 174.687 147.214 139.036 1.00 8.87   ? 4189 ILE A O     1 
ATOM   20165 C  CB    . ILE A 1 4189 ? 174.288 145.610 136.192 1.00 7.48   ? 4189 ILE A CB    1 
ATOM   20166 C  CG1   . ILE A 1 4189 ? 174.467 144.219 135.577 1.00 9.01   ? 4189 ILE A CG1   1 
ATOM   20167 C  CG2   . ILE A 1 4189 ? 175.610 146.362 136.169 1.00 11.54  ? 4189 ILE A CG2   1 
ATOM   20168 C  CD1   . ILE A 1 4189 ? 175.073 143.197 136.506 1.00 12.02  ? 4189 ILE A CD1   1 
ATOM   20169 N  N     . ILE A 1 4190 ? 172.666 147.640 138.148 1.00 6.86   ? 4190 ILE A N     1 
ATOM   20170 C  CA    . ILE A 1 4190 ? 172.641 149.009 138.657 1.00 6.61   ? 4190 ILE A CA    1 
ATOM   20171 C  C     . ILE A 1 4190 ? 172.573 149.020 140.181 1.00 7.24   ? 4190 ILE A C     1 
ATOM   20172 O  O     . ILE A 1 4190 ? 173.296 149.773 140.844 1.00 9.34   ? 4190 ILE A O     1 
ATOM   20173 C  CB    . ILE A 1 4190 ? 171.472 149.789 138.026 1.00 8.11   ? 4190 ILE A CB    1 
ATOM   20174 C  CG1   . ILE A 1 4190 ? 171.807 150.194 136.588 1.00 7.54   ? 4190 ILE A CG1   1 
ATOM   20175 C  CG2   . ILE A 1 4190 ? 171.132 151.013 138.849 1.00 9.86   ? 4190 ILE A CG2   1 
ATOM   20176 C  CD1   . ILE A 1 4190 ? 173.244 150.611 136.375 1.00 9.60   ? 4190 ILE A CD1   1 
ATOM   20177 N  N     . GLN A 1 4191 ? 171.705 148.187 140.765 1.00 7.36   ? 4191 GLN A N     1 
ATOM   20178 C  CA    . GLN A 1 4191 ? 171.591 148.163 142.222 1.00 8.02   ? 4191 GLN A CA    1 
ATOM   20179 C  C     . GLN A 1 4191 ? 172.824 147.549 142.871 1.00 9.24   ? 4191 GLN A C     1 
ATOM   20180 O  O     . GLN A 1 4191 ? 173.268 148.010 143.928 1.00 10.57  ? 4191 GLN A O     1 
ATOM   20181 C  CB    . GLN A 1 4191 ? 170.342 147.403 142.667 1.00 11.37  ? 4191 GLN A CB    1 
ATOM   20182 C  CG    . GLN A 1 4191 ? 169.199 147.391 141.687 1.00 9.54   ? 4191 GLN A CG    1 
ATOM   20183 C  CD    . GLN A 1 4191 ? 167.858 147.302 142.381 1.00 14.43  ? 4191 GLN A CD    1 
ATOM   20184 O  OE1   . GLN A 1 4191 ? 167.161 146.295 142.277 1.00 26.46  ? 4191 GLN A OE1   1 
ATOM   20185 N  NE2   . GLN A 1 4191 ? 167.481 148.365 143.081 1.00 13.14  ? 4191 GLN A NE2   1 
ATOM   20186 N  N     . GLU A 1 4192 ? 173.372 146.489 142.276 1.00 7.96   ? 4192 GLU A N     1 
ATOM   20187 C  CA    . GLU A 1 4192 ? 174.553 145.861 142.854 1.00 9.20   ? 4192 GLU A CA    1 
ATOM   20188 C  C     . GLU A 1 4192 ? 175.744 146.811 142.869 1.00 11.26  ? 4192 GLU A C     1 
ATOM   20189 O  O     . GLU A 1 4192 ? 176.630 146.676 143.719 1.00 17.91  ? 4192 GLU A O     1 
ATOM   20190 C  CB    . GLU A 1 4192 ? 174.890 144.581 142.094 1.00 11.68  ? 4192 GLU A CB    1 
ATOM   20191 C  CG    . GLU A 1 4192 ? 174.193 143.343 142.637 1.00 18.90  ? 4192 GLU A CG    1 
ATOM   20192 C  CD    . GLU A 1 4192 ? 174.735 142.915 143.985 1.00 24.67  ? 4192 GLU A CD    1 
ATOM   20193 O  OE1   . GLU A 1 4192 ? 174.087 143.215 145.010 1.00 21.92  ? 4192 GLU A OE1   1 
ATOM   20194 O  OE2   . GLU A 1 4192 ? 175.809 142.281 144.021 1.00 26.99  ? 4192 GLU A OE2   1 
ATOM   20195 N  N     . ARG A 1 4193 ? 175.784 147.771 141.941 1.00 7.23   ? 4193 ARG A N     1 
ATOM   20196 C  CA    . ARG A 1 4193 ? 176.822 148.796 141.979 1.00 7.78   ? 4193 ARG A CA    1 
ATOM   20197 C  C     . ARG A 1 4193 ? 176.604 149.775 143.125 1.00 10.07  ? 4193 ARG A C     1 
ATOM   20198 O  O     . ARG A 1 4193 ? 177.554 150.431 143.567 1.00 12.85  ? 4193 ARG A O     1 
ATOM   20199 C  CB    . ARG A 1 4193 ? 176.874 149.546 140.649 1.00 9.22   ? 4193 ARG A CB    1 
ATOM   20200 C  CG    . ARG A 1 4193 ? 177.510 148.766 139.515 1.00 9.80   ? 4193 ARG A CG    1 
ATOM   20201 C  CD    . ARG A 1 4193 ? 177.757 149.652 138.307 1.00 11.08  ? 4193 ARG A CD    1 
ATOM   20202 N  NE    . ARG A 1 4193 ? 178.824 150.618 138.537 1.00 8.22   ? 4193 ARG A NE    1 
ATOM   20203 C  CZ    . ARG A 1 4193 ? 180.011 150.576 137.948 1.00 10.02  ? 4193 ARG A CZ    1 
ATOM   20204 N  NH1   . ARG A 1 4193 ? 180.330 149.608 137.105 1.00 10.40  ? 4193 ARG A NH1   1 
ATOM   20205 N  NH2   . ARG A 1 4193 ? 180.900 151.529 138.211 1.00 13.23  ? 4193 ARG A NH2   1 
ATOM   20206 N  N     . LEU A 1 4194 ? 175.367 149.892 143.613 1.00 10.00  ? 4194 LEU A N     1 
ATOM   20207 C  CA    . LEU A 1 4194 ? 175.080 150.803 144.715 1.00 12.23  ? 4194 LEU A CA    1 
ATOM   20208 C  C     . LEU A 1 4194 ? 175.746 150.365 146.010 1.00 14.94  ? 4194 LEU A C     1 
ATOM   20209 O  O     . LEU A 1 4194 ? 175.963 151.199 146.894 1.00 16.04  ? 4194 LEU A O     1 
ATOM   20210 C  CB    . LEU A 1 4194 ? 173.569 150.911 144.922 1.00 13.03  ? 4194 LEU A CB    1 
ATOM   20211 C  CG    . LEU A 1 4194 ? 172.810 151.949 144.098 1.00 13.07  ? 4194 LEU A CG    1 
ATOM   20212 C  CD1   . LEU A 1 4194 ? 171.318 151.808 144.341 1.00 13.77  ? 4194 LEU A CD1   1 
ATOM   20213 C  CD2   . LEU A 1 4194 ? 173.282 153.353 144.433 1.00 12.26  ? 4194 LEU A CD2   1 
ATOM   20214 N  N     . ARG A 1 4195 ? 176.076 149.078 146.139 1.00 15.01  ? 4195 ARG A N     1 
ATOM   20215 C  CA    . ARG A 1 4195 ? 176.725 148.591 147.351 1.00 14.13  ? 4195 ARG A CA    1 
ATOM   20216 C  C     . ARG A 1 4195 ? 178.095 149.232 147.534 1.00 15.38  ? 4195 ARG A C     1 
ATOM   20217 O  O     . ARG A 1 4195 ? 178.491 149.557 148.659 1.00 18.77  ? 4195 ARG A O     1 
ATOM   20218 C  CB    . ARG A 1 4195 ? 176.846 147.069 147.295 1.00 12.52  ? 4195 ARG A CB    1 
ATOM   20219 C  CG    . ARG A 1 4195 ? 175.511 146.347 147.305 1.00 13.87  ? 4195 ARG A CG    1 
ATOM   20220 C  CD    . ARG A 1 4195 ? 175.696 144.841 147.352 1.00 17.36  ? 4195 ARG A CD    1 
ATOM   20221 N  NE    . ARG A 1 4195 ? 174.422 144.135 147.293 1.00 25.32  ? 4195 ARG A NE    1 
ATOM   20222 C  CZ    . ARG A 1 4195 ? 173.594 143.991 148.320 1.00 24.04  ? 4195 ARG A CZ    1 
ATOM   20223 N  NH1   . ARG A 1 4195 ? 173.878 144.490 149.512 1.00 19.49  ? 4195 ARG A NH1   1 
ATOM   20224 N  NH2   . ARG A 1 4195 ? 172.454 143.329 148.145 1.00 21.62  ? 4195 ARG A NH2   1 
ATOM   20225 N  N     . TYR A 1 4196 ? 178.826 149.420 146.439 1.00 15.41  ? 4196 TYR A N     1 
ATOM   20226 C  CA    . TYR A 1 4196 ? 180.135 150.070 146.456 1.00 14.14  ? 4196 TYR A CA    1 
ATOM   20227 C  C     . TYR A 1 4196 ? 179.894 151.559 146.247 1.00 17.01  ? 4196 TYR A C     1 
ATOM   20228 O  O     . TYR A 1 4196 ? 179.905 152.064 145.124 1.00 21.18  ? 4196 TYR A O     1 
ATOM   20229 C  CB    . TYR A 1 4196 ? 181.037 149.464 145.389 1.00 11.06  ? 4196 TYR A CB    1 
ATOM   20230 C  CG    . TYR A 1 4196 ? 180.868 147.964 145.272 1.00 12.93  ? 4196 TYR A CG    1 
ATOM   20231 C  CD1   . TYR A 1 4196 ? 181.563 147.099 146.106 1.00 19.96  ? 4196 TYR A CD1   1 
ATOM   20232 C  CD2   . TYR A 1 4196 ? 179.994 147.414 144.345 1.00 13.05  ? 4196 TYR A CD2   1 
ATOM   20233 C  CE1   . TYR A 1 4196 ? 181.402 145.729 146.009 1.00 21.73  ? 4196 TYR A CE1   1 
ATOM   20234 C  CE2   . TYR A 1 4196 ? 179.827 146.047 144.242 1.00 14.49  ? 4196 TYR A CE2   1 
ATOM   20235 C  CZ    . TYR A 1 4196 ? 180.533 145.209 145.075 1.00 18.75  ? 4196 TYR A CZ    1 
ATOM   20236 O  OH    . TYR A 1 4196 ? 180.370 143.846 144.975 1.00 14.39  ? 4196 TYR A OH    1 
ATOM   20237 N  N     . ALA A 1 4197 ? 179.665 152.265 147.355 1.00 19.33  ? 4197 ALA A N     1 
ATOM   20238 C  CA    . ALA A 1 4197 ? 179.132 153.625 147.290 1.00 21.04  ? 4197 ALA A CA    1 
ATOM   20239 C  C     . ALA A 1 4197 ? 180.012 154.600 146.517 1.00 28.84  ? 4197 ALA A C     1 
ATOM   20240 O  O     . ALA A 1 4197 ? 179.471 155.354 145.691 1.00 33.99  ? 4197 ALA A O     1 
ATOM   20241 C  CB    . ALA A 1 4197 ? 178.854 154.134 148.708 1.00 30.86  ? 4197 ALA A CB    1 
ATOM   20242 N  N     . PRO A 1 4198 ? 181.342 154.665 146.725 1.00 28.56  ? 4198 PRO A N     1 
ATOM   20243 C  CA    . PRO A 1 4198 ? 182.129 155.669 145.994 1.00 18.04  ? 4198 PRO A CA    1 
ATOM   20244 C  C     . PRO A 1 4198 ? 182.479 155.257 144.571 1.00 18.30  ? 4198 PRO A C     1 
ATOM   20245 O  O     . PRO A 1 4198 ? 182.646 156.118 143.703 1.00 27.21  ? 4198 PRO A O     1 
ATOM   20246 C  CB    . PRO A 1 4198 ? 183.395 155.820 146.852 1.00 22.39  ? 4198 PRO A CB    1 
ATOM   20247 C  CG    . PRO A 1 4198 ? 183.097 155.112 148.145 1.00 27.98  ? 4198 PRO A CG    1 
ATOM   20248 C  CD    . PRO A 1 4198 ? 182.155 154.023 147.769 1.00 26.89  ? 4198 PRO A CD    1 
ATOM   20249 N  N     . LEU A 1 4199 ? 182.592 153.955 144.311 1.00 17.68  ? 4199 LEU A N     1 
ATOM   20250 C  CA    . LEU A 1 4199 ? 183.061 153.472 143.016 1.00 19.75  ? 4199 LEU A CA    1 
ATOM   20251 C  C     . LEU A 1 4199 ? 181.929 153.077 142.073 1.00 22.45  ? 4199 LEU A C     1 
ATOM   20252 O  O     . LEU A 1 4199 ? 181.924 153.496 140.912 1.00 27.76  ? 4199 LEU A O     1 
ATOM   20253 C  CB    . LEU A 1 4199 ? 184.016 152.289 143.210 1.00 19.88  ? 4199 LEU A CB    1 
ATOM   20254 C  CG    . LEU A 1 4199 ? 185.494 152.657 143.355 1.00 17.08  ? 4199 LEU A CG    1 
ATOM   20255 C  CD1   . LEU A 1 4199 ? 185.786 153.190 144.748 1.00 21.59  ? 4199 LEU A CD1   1 
ATOM   20256 C  CD2   . LEU A 1 4199 ? 186.377 151.464 143.043 1.00 20.33  ? 4199 LEU A CD2   1 
ATOM   20257 N  N     . GLY A 1 4200 ? 180.979 152.264 142.540 1.00 19.72  ? 4200 GLY A N     1 
ATOM   20258 C  CA    . GLY A 1 4200 ? 179.869 151.877 141.682 1.00 14.00  ? 4200 GLY A CA    1 
ATOM   20259 C  C     . GLY A 1 4200 ? 179.045 153.067 141.231 1.00 14.68  ? 4200 GLY A C     1 
ATOM   20260 O  O     . GLY A 1 4200 ? 178.646 153.157 140.068 1.00 13.96  ? 4200 GLY A O     1 
ATOM   20261 N  N     . TRP A 1 4201 ? 178.779 153.993 142.147 1.00 14.65  ? 4201 TRP A N     1 
ATOM   20262 C  CA    . TRP A 1 4201 ? 178.153 155.269 141.834 1.00 14.72  ? 4201 TRP A CA    1 
ATOM   20263 C  C     . TRP A 1 4201 ? 178.891 156.340 142.627 1.00 16.03  ? 4201 TRP A C     1 
ATOM   20264 O  O     . TRP A 1 4201 ? 179.977 156.102 143.159 1.00 25.66  ? 4201 TRP A O     1 
ATOM   20265 C  CB    . TRP A 1 4201 ? 176.651 155.230 142.139 1.00 15.63  ? 4201 TRP A CB    1 
ATOM   20266 C  CG    . TRP A 1 4201 ? 175.897 154.332 141.219 1.00 10.47  ? 4201 TRP A CG    1 
ATOM   20267 C  CD1   . TRP A 1 4201 ? 175.348 153.121 141.520 1.00 9.64   ? 4201 TRP A CD1   1 
ATOM   20268 C  CD2   . TRP A 1 4201 ? 175.618 154.567 139.837 1.00 11.93  ? 4201 TRP A CD2   1 
ATOM   20269 N  NE1   . TRP A 1 4201 ? 174.740 152.589 140.411 1.00 9.12   ? 4201 TRP A NE1   1 
ATOM   20270 C  CE2   . TRP A 1 4201 ? 174.892 153.458 139.363 1.00 9.57   ? 4201 TRP A CE2   1 
ATOM   20271 C  CE3   . TRP A 1 4201 ? 175.909 155.610 138.953 1.00 14.38  ? 4201 TRP A CE3   1 
ATOM   20272 C  CZ2   . TRP A 1 4201 ? 174.452 153.363 138.047 1.00 8.20   ? 4201 TRP A CZ2   1 
ATOM   20273 C  CZ3   . TRP A 1 4201 ? 175.473 155.513 137.647 1.00 13.68  ? 4201 TRP A CZ3   1 
ATOM   20274 C  CH2   . TRP A 1 4201 ? 174.753 154.397 137.205 1.00 11.25  ? 4201 TRP A CH2   1 
ATOM   20275 N  N     . SER A 1 4202 ? 178.319 157.539 142.691 1.00 16.95  ? 4202 SER A N     1 
ATOM   20276 C  CA    . SER A 1 4202 ? 178.870 158.576 143.551 1.00 18.17  ? 4202 SER A CA    1 
ATOM   20277 C  C     . SER A 1 4202 ? 178.093 158.745 144.847 1.00 24.48  ? 4202 SER A C     1 
ATOM   20278 O  O     . SER A 1 4202 ? 178.615 159.351 145.789 1.00 29.76  ? 4202 SER A O     1 
ATOM   20279 C  CB    . SER A 1 4202 ? 178.920 159.917 142.812 1.00 22.73  ? 4202 SER A CB    1 
ATOM   20280 O  OG    . SER A 1 4202 ? 179.939 159.914 141.827 1.00 28.21  ? 4202 SER A OG    1 
ATOM   20281 N  N     . LYS A 1 4203 ? 176.870 158.224 144.916 1.00 20.75  ? 4203 LYS A N     1 
ATOM   20282 C  CA    . LYS A 1 4203 ? 176.041 158.351 146.104 1.00 18.62  ? 4203 LYS A CA    1 
ATOM   20283 C  C     . LYS A 1 4203 ? 174.948 157.293 146.061 1.00 18.69  ? 4203 LYS A C     1 
ATOM   20284 O  O     . LYS A 1 4203 ? 174.724 156.639 145.039 1.00 19.40  ? 4203 LYS A O     1 
ATOM   20285 C  CB    . LYS A 1 4203 ? 175.448 159.758 146.218 1.00 21.03  ? 4203 LYS A CB    1 
ATOM   20286 C  CG    . LYS A 1 4203 ? 174.853 160.280 144.927 1.00 18.55  ? 4203 LYS A CG    1 
ATOM   20287 C  CD    . LYS A 1 4203 ? 174.712 161.788 144.973 1.00 27.23  ? 4203 LYS A CD    1 
ATOM   20288 C  CE    . LYS A 1 4203 ? 175.724 162.451 144.053 1.00 30.05  ? 4203 LYS A CE    1 
ATOM   20289 N  NZ    . LYS A 1 4203 ? 175.498 163.918 143.945 1.00 25.25  ? 4203 LYS A NZ    1 
ATOM   20290 N  N     . LYS A 1 4204 ? 174.262 157.134 147.194 1.00 20.00  ? 4204 LYS A N     1 
ATOM   20291 C  CA    . LYS A 1 4204 ? 173.188 156.151 147.332 1.00 18.48  ? 4204 LYS A CA    1 
ATOM   20292 C  C     . LYS A 1 4204 ? 171.958 156.653 146.581 1.00 20.59  ? 4204 LYS A C     1 
ATOM   20293 O  O     . LYS A 1 4204 ? 171.014 157.202 147.155 1.00 25.48  ? 4204 LYS A O     1 
ATOM   20294 C  CB    . LYS A 1 4204 ? 172.872 155.903 148.802 1.00 24.29  ? 4204 LYS A CB    1 
ATOM   20295 C  CG    . LYS A 1 4204 ? 173.720 154.841 149.486 1.00 24.79  ? 4204 LYS A CG    1 
ATOM   20296 C  CD    . LYS A 1 4204 ? 173.766 153.552 148.685 1.00 23.89  ? 4204 LYS A CD    1 
ATOM   20297 C  CE    . LYS A 1 4204 ? 174.578 152.491 149.409 1.00 30.61  ? 4204 LYS A CE    1 
ATOM   20298 N  NZ    . LYS A 1 4204 ? 175.963 152.941 149.708 1.00 33.19  ? 4204 LYS A NZ    1 
ATOM   20299 N  N     . TYR A 1 4205 ? 171.975 156.462 145.265 1.00 16.31  ? 4205 TYR A N     1 
ATOM   20300 C  CA    . TYR A 1 4205 ? 170.790 156.740 144.469 1.00 15.30  ? 4205 TYR A CA    1 
ATOM   20301 C  C     . TYR A 1 4205 ? 169.685 155.749 144.809 1.00 17.59  ? 4205 TYR A C     1 
ATOM   20302 O  O     . TYR A 1 4205 ? 169.937 154.576 145.094 1.00 16.95  ? 4205 TYR A O     1 
ATOM   20303 C  CB    . TYR A 1 4205 ? 171.103 156.670 142.976 1.00 13.21  ? 4205 TYR A CB    1 
ATOM   20304 C  CG    . TYR A 1 4205 ? 172.002 157.772 142.470 1.00 12.16  ? 4205 TYR A CG    1 
ATOM   20305 C  CD1   . TYR A 1 4205 ? 171.620 159.101 142.563 1.00 12.66  ? 4205 TYR A CD1   1 
ATOM   20306 C  CD2   . TYR A 1 4205 ? 173.221 157.482 141.877 1.00 13.02  ? 4205 TYR A CD2   1 
ATOM   20307 C  CE1   . TYR A 1 4205 ? 172.434 160.111 142.095 1.00 13.61  ? 4205 TYR A CE1   1 
ATOM   20308 C  CE2   . TYR A 1 4205 ? 174.041 158.486 141.404 1.00 15.08  ? 4205 TYR A CE2   1 
ATOM   20309 C  CZ    . TYR A 1 4205 ? 173.643 159.798 141.516 1.00 17.02  ? 4205 TYR A CZ    1 
ATOM   20310 O  OH    . TYR A 1 4205 ? 174.457 160.802 141.047 1.00 22.81  ? 4205 TYR A OH    1 
ATOM   20311 N  N     . GLU A 1 4206 ? 168.449 156.232 144.778 1.00 20.42  ? 4206 GLU A N     1 
ATOM   20312 C  CA    . GLU A 1 4206 ? 167.298 155.393 145.107 1.00 19.44  ? 4206 GLU A CA    1 
ATOM   20313 C  C     . GLU A 1 4206 ? 166.779 154.648 143.882 1.00 15.87  ? 4206 GLU A C     1 
ATOM   20314 O  O     . GLU A 1 4206 ? 165.596 154.703 143.549 1.00 21.04  ? 4206 GLU A O     1 
ATOM   20315 C  CB    . GLU A 1 4206 ? 166.204 156.240 145.742 1.00 23.64  ? 4206 GLU A CB    1 
ATOM   20316 C  CG    . GLU A 1 4206 ? 166.718 157.224 146.778 1.00 27.10  ? 4206 GLU A CG    1 
ATOM   20317 C  CD    . GLU A 1 4206 ? 165.604 157.868 147.575 1.00 41.40  ? 4206 GLU A CD    1 
ATOM   20318 O  OE1   . GLU A 1 4206 ? 165.238 159.021 147.265 1.00 35.42  ? 4206 GLU A OE1   1 
ATOM   20319 O  OE2   . GLU A 1 4206 ? 165.094 157.219 148.513 1.00 50.45  ? 4206 GLU A OE2   1 
ATOM   20320 N  N     . PHE A 1 4207 ? 167.676 153.940 143.198 1.00 12.96  ? 4207 PHE A N     1 
ATOM   20321 C  CA    . PHE A 1 4207 ? 167.283 153.062 142.102 1.00 10.92  ? 4207 PHE A CA    1 
ATOM   20322 C  C     . PHE A 1 4207 ? 166.471 151.907 142.673 1.00 11.86  ? 4207 PHE A C     1 
ATOM   20323 O  O     . PHE A 1 4207 ? 167.023 151.016 143.327 1.00 15.02  ? 4207 PHE A O     1 
ATOM   20324 C  CB    . PHE A 1 4207 ? 168.515 152.549 141.364 1.00 10.94  ? 4207 PHE A CB    1 
ATOM   20325 C  CG    . PHE A 1 4207 ? 169.288 153.620 140.649 1.00 13.26  ? 4207 PHE A CG    1 
ATOM   20326 C  CD1   . PHE A 1 4207 ? 168.651 154.500 139.792 1.00 10.90  ? 4207 PHE A CD1   1 
ATOM   20327 C  CD2   . PHE A 1 4207 ? 170.656 153.743 140.831 1.00 10.54  ? 4207 PHE A CD2   1 
ATOM   20328 C  CE1   . PHE A 1 4207 ? 169.362 155.482 139.131 1.00 10.60  ? 4207 PHE A CE1   1 
ATOM   20329 C  CE2   . PHE A 1 4207 ? 171.373 154.719 140.168 1.00 9.43   ? 4207 PHE A CE2   1 
ATOM   20330 C  CZ    . PHE A 1 4207 ? 170.725 155.592 139.321 1.00 11.41  ? 4207 PHE A CZ    1 
ATOM   20331 N  N     . GLY A 1 4208 ? 165.164 151.917 142.436 1.00 10.83  ? 4208 GLY A N     1 
ATOM   20332 C  CA    . GLY A 1 4208 ? 164.301 150.937 143.063 1.00 11.32  ? 4208 GLY A CA    1 
ATOM   20333 C  C     . GLY A 1 4208 ? 163.259 150.327 142.151 1.00 10.22  ? 4208 GLY A C     1 
ATOM   20334 O  O     . GLY A 1 4208 ? 163.401 150.342 140.925 1.00 10.36  ? 4208 GLY A O     1 
ATOM   20335 N  N     . GLU A 1 4209 ? 162.200 149.784 142.756 1.00 13.87  ? 4209 GLU A N     1 
ATOM   20336 C  CA    . GLU A 1 4209 ? 161.163 149.106 141.990 1.00 14.64  ? 4209 GLU A CA    1 
ATOM   20337 C  C     . GLU A 1 4209 ? 160.399 150.072 141.093 1.00 11.70  ? 4209 GLU A C     1 
ATOM   20338 O  O     . GLU A 1 4209 ? 159.949 149.684 140.009 1.00 16.83  ? 4209 GLU A O     1 
ATOM   20339 C  CB    . GLU A 1 4209 ? 160.209 148.383 142.943 1.00 24.45  ? 4209 GLU A CB    1 
ATOM   20340 C  CG    . GLU A 1 4209 ? 159.016 147.725 142.274 1.00 36.95  ? 4209 GLU A CG    1 
ATOM   20341 C  CD    . GLU A 1 4209 ? 159.144 146.216 142.227 1.00 45.62  ? 4209 GLU A CD    1 
ATOM   20342 O  OE1   . GLU A 1 4209 ? 158.104 145.529 142.164 1.00 50.26  ? 4209 GLU A OE1   1 
ATOM   20343 O  OE2   . GLU A 1 4209 ? 160.288 145.716 142.252 1.00 43.45  ? 4209 GLU A OE2   1 
ATOM   20344 N  N     . SER A 1 4210 ? 160.252 151.330 141.519 1.00 9.92   ? 4210 SER A N     1 
ATOM   20345 C  CA    . SER A 1 4210 ? 159.539 152.308 140.704 1.00 11.62  ? 4210 SER A CA    1 
ATOM   20346 C  C     . SER A 1 4210 ? 160.247 152.541 139.376 1.00 11.40  ? 4210 SER A C     1 
ATOM   20347 O  O     . SER A 1 4210 ? 159.597 152.670 138.331 1.00 11.70  ? 4210 SER A O     1 
ATOM   20348 C  CB    . SER A 1 4210 ? 159.389 153.621 141.470 1.00 11.78  ? 4210 SER A CB    1 
ATOM   20349 O  OG    . SER A 1 4210 ? 160.654 154.172 141.791 1.00 15.53  ? 4210 SER A OG    1 
ATOM   20350 N  N     . ASP A 1 4211 ? 161.580 152.605 139.397 1.00 13.37  ? 4211 ASP A N     1 
ATOM   20351 C  CA    . ASP A 1 4211 ? 162.332 152.753 138.155 1.00 7.87   ? 4211 ASP A CA    1 
ATOM   20352 C  C     . ASP A 1 4211 ? 162.148 151.541 137.252 1.00 8.03   ? 4211 ASP A C     1 
ATOM   20353 O  O     . ASP A 1 4211 ? 162.019 151.681 136.031 1.00 10.91  ? 4211 ASP A O     1 
ATOM   20354 C  CB    . ASP A 1 4211 ? 163.813 152.973 138.463 1.00 8.04   ? 4211 ASP A CB    1 
ATOM   20355 C  CG    . ASP A 1 4211 ? 164.050 154.169 139.361 1.00 14.27  ? 4211 ASP A CG    1 
ATOM   20356 O  OD1   . ASP A 1 4211 ? 164.761 155.103 138.935 1.00 16.04  ? 4211 ASP A OD1   1 
ATOM   20357 O  OD2   . ASP A 1 4211 ? 163.528 154.177 140.495 1.00 15.67  ? 4211 ASP A OD2   1 
ATOM   20358 N  N     . LEU A 1 4212 ? 162.138 150.340 137.835 1.00 8.27   ? 4212 LEU A N     1 
ATOM   20359 C  CA    . LEU A 1 4212 ? 161.941 149.134 137.038 1.00 7.26   ? 4212 LEU A CA    1 
ATOM   20360 C  C     . LEU A 1 4212 ? 160.538 149.084 136.444 1.00 8.45   ? 4212 LEU A C     1 
ATOM   20361 O  O     . LEU A 1 4212 ? 160.366 148.734 135.271 1.00 11.25  ? 4212 LEU A O     1 
ATOM   20362 C  CB    . LEU A 1 4212 ? 162.213 147.895 137.891 1.00 11.33  ? 4212 LEU A CB    1 
ATOM   20363 C  CG    . LEU A 1 4212 ? 162.007 146.537 137.221 1.00 10.93  ? 4212 LEU A CG    1 
ATOM   20364 C  CD1   . LEU A 1 4212 ? 162.997 146.343 136.087 1.00 11.63  ? 4212 LEU A CD1   1 
ATOM   20365 C  CD2   . LEU A 1 4212 ? 162.139 145.426 138.244 1.00 11.74  ? 4212 LEU A CD2   1 
ATOM   20366 N  N     . ARG A 1 4213 ? 159.520 149.427 137.240 1.00 12.66  ? 4213 ARG A N     1 
ATOM   20367 C  CA    . ARG A 1 4213 ? 158.153 149.432 136.728 1.00 12.21  ? 4213 ARG A CA    1 
ATOM   20368 C  C     . ARG A 1 4213 ? 157.976 150.465 135.623 1.00 11.20  ? 4213 ARG A C     1 
ATOM   20369 O  O     . ARG A 1 4213 ? 157.338 150.188 134.601 1.00 13.60  ? 4213 ARG A O     1 
ATOM   20370 C  CB    . ARG A 1 4213 ? 157.162 149.691 137.863 1.00 14.93  ? 4213 ARG A CB    1 
ATOM   20371 C  CG    . ARG A 1 4213 ? 157.141 148.620 138.939 1.00 24.87  ? 4213 ARG A CG    1 
ATOM   20372 C  CD    . ARG A 1 4213 ? 155.727 148.396 139.444 1.00 33.08  ? 4213 ARG A CD    1 
ATOM   20373 N  NE    . ARG A 1 4213 ? 155.692 147.552 140.631 1.00 42.39  ? 4213 ARG A NE    1 
ATOM   20374 C  CZ    . ARG A 1 4213 ? 155.598 146.230 140.606 1.00 50.26  ? 4213 ARG A CZ    1 
ATOM   20375 N  NH1   . ARG A 1 4213 ? 155.532 145.563 139.465 1.00 51.57  ? 4213 ARG A NH1   1 
ATOM   20376 N  NH2   . ARG A 1 4213 ? 155.570 145.559 141.754 1.00 47.25  ? 4213 ARG A NH2   1 
ATOM   20377 N  N     . SER A 1 4214 ? 158.530 151.665 135.812 1.00 9.82   ? 4214 SER A N     1 
ATOM   20378 C  CA    . SER A 1 4214 ? 158.452 152.684 134.770 1.00 7.90   ? 4214 SER A CA    1 
ATOM   20379 C  C     . SER A 1 4214 ? 159.207 152.245 133.524 1.00 10.65  ? 4214 SER A C     1 
ATOM   20380 O  O     . SER A 1 4214 ? 158.777 152.520 132.397 1.00 11.99  ? 4214 SER A O     1 
ATOM   20381 C  CB    . SER A 1 4214 ? 158.997 154.013 135.292 1.00 8.02   ? 4214 SER A CB    1 
ATOM   20382 O  OG    . SER A 1 4214 ? 158.343 154.398 136.488 1.00 15.35  ? 4214 SER A OG    1 
ATOM   20383 N  N     . ALA A 1 4215 ? 160.341 151.567 133.708 1.00 9.95   ? 4215 ALA A N     1 
ATOM   20384 C  CA    . ALA A 1 4215 ? 161.081 151.029 132.572 1.00 7.50   ? 4215 ALA A CA    1 
ATOM   20385 C  C     . ALA A 1 4215 ? 160.267 149.977 131.830 1.00 12.45  ? 4215 ALA A C     1 
ATOM   20386 O  O     . ALA A 1 4215 ? 160.260 149.948 130.594 1.00 14.18  ? 4215 ALA A O     1 
ATOM   20387 C  CB    . ALA A 1 4215 ? 162.409 150.444 133.049 1.00 8.74   ? 4215 ALA A CB    1 
ATOM   20388 N  N     . CYS A 1 4216 ? 159.581 149.100 132.567 1.00 15.07  ? 4216 CYS A N     1 
ATOM   20389 C  CA    . CYS A 1 4216 ? 158.761 148.074 131.931 1.00 13.68  ? 4216 CYS A CA    1 
ATOM   20390 C  C     . CYS A 1 4216 ? 157.602 148.692 131.160 1.00 17.61  ? 4216 CYS A C     1 
ATOM   20391 O  O     . CYS A 1 4216 ? 157.267 148.240 130.059 1.00 20.78  ? 4216 CYS A O     1 
ATOM   20392 C  CB    . CYS A 1 4216 ? 158.248 147.089 132.981 1.00 16.50  ? 4216 CYS A CB    1 
ATOM   20393 S  SG    . CYS A 1 4216 ? 159.529 146.034 133.694 1.00 31.87  ? 4216 CYS A SG    1 
ATOM   20394 N  N     . ASP A 1 4217 ? 156.970 149.722 131.729 1.00 17.44  ? 4217 ASP A N     1 
ATOM   20395 C  CA    . ASP A 1 4217 ? 155.890 150.410 131.029 1.00 17.14  ? 4217 ASP A CA    1 
ATOM   20396 C  C     . ASP A 1 4217 ? 156.394 151.082 129.759 1.00 14.71  ? 4217 ASP A C     1 
ATOM   20397 O  O     . ASP A 1 4217 ? 155.719 151.055 128.724 1.00 17.71  ? 4217 ASP A O     1 
ATOM   20398 C  CB    . ASP A 1 4217 ? 155.235 151.437 131.954 1.00 16.13  ? 4217 ASP A CB    1 
ATOM   20399 C  CG    . ASP A 1 4217 ? 154.564 150.799 133.154 1.00 22.23  ? 4217 ASP A CG    1 
ATOM   20400 O  OD1   . ASP A 1 4217 ? 154.300 149.581 133.110 1.00 26.94  ? 4217 ASP A OD1   1 
ATOM   20401 O  OD2   . ASP A 1 4217 ? 154.299 151.517 134.140 1.00 26.55  ? 4217 ASP A OD2   1 
ATOM   20402 N  N     . THR A 1 4218 ? 157.577 151.697 129.823 1.00 13.95  ? 4218 THR A N     1 
ATOM   20403 C  CA    . THR A 1 4218 ? 158.125 152.379 128.654 1.00 10.80  ? 4218 THR A CA    1 
ATOM   20404 C  C     . THR A 1 4218 ? 158.422 151.398 127.527 1.00 14.12  ? 4218 THR A C     1 
ATOM   20405 O  O     . THR A 1 4218 ? 158.159 151.691 126.355 1.00 17.17  ? 4218 THR A O     1 
ATOM   20406 C  CB    . THR A 1 4218 ? 159.388 153.147 129.040 1.00 10.30  ? 4218 THR A CB    1 
ATOM   20407 O  OG1   . THR A 1 4218 ? 159.171 153.837 130.277 1.00 13.49  ? 4218 THR A OG1   1 
ATOM   20408 C  CG2   . THR A 1 4218 ? 159.743 154.153 127.964 1.00 11.73  ? 4218 THR A CG2   1 
ATOM   20409 N  N     . VAL A 1 4219 ? 158.976 150.232 127.861 1.00 17.48  ? 4219 VAL A N     1 
ATOM   20410 C  CA    . VAL A 1 4219 ? 159.262 149.222 126.844 1.00 16.49  ? 4219 VAL A CA    1 
ATOM   20411 C  C     . VAL A 1 4219 ? 157.965 148.724 126.218 1.00 20.04  ? 4219 VAL A C     1 
ATOM   20412 O  O     . VAL A 1 4219 ? 157.859 148.579 124.995 1.00 23.94  ? 4219 VAL A O     1 
ATOM   20413 C  CB    . VAL A 1 4219 ? 160.081 148.069 127.451 1.00 16.82  ? 4219 VAL A CB    1 
ATOM   20414 C  CG1   . VAL A 1 4219 ? 159.950 146.812 126.606 1.00 17.78  ? 4219 VAL A CG1   1 
ATOM   20415 C  CG2   . VAL A 1 4219 ? 161.540 148.472 127.588 1.00 20.73  ? 4219 VAL A CG2   1 
ATOM   20416 N  N     . ASP A 1 4220 ? 156.956 148.463 127.052 1.00 21.91  ? 4220 ASP A N     1 
ATOM   20417 C  CA    . ASP A 1 4220 ? 155.670 147.994 126.545 1.00 20.94  ? 4220 ASP A CA    1 
ATOM   20418 C  C     . ASP A 1 4220 ? 155.029 149.029 125.631 1.00 22.85  ? 4220 ASP A C     1 
ATOM   20419 O  O     . ASP A 1 4220 ? 154.466 148.688 124.584 1.00 28.89  ? 4220 ASP A O     1 
ATOM   20420 C  CB    . ASP A 1 4220 ? 154.741 147.659 127.712 1.00 22.20  ? 4220 ASP A CB    1 
ATOM   20421 C  CG    . ASP A 1 4220 ? 155.006 146.287 128.292 1.00 30.89  ? 4220 ASP A CG    1 
ATOM   20422 O  OD1   . ASP A 1 4220 ? 155.625 145.454 127.598 1.00 33.59  ? 4220 ASP A OD1   1 
ATOM   20423 O  OD2   . ASP A 1 4220 ? 154.595 146.040 129.445 1.00 36.24  ? 4220 ASP A OD2   1 
ATOM   20424 N  N     . THR A 1 4221 ? 155.099 150.305 126.017 1.00 19.44  ? 4221 THR A N     1 
ATOM   20425 C  CA    . THR A 1 4221 ? 154.476 151.360 125.224 1.00 22.02  ? 4221 THR A CA    1 
ATOM   20426 C  C     . THR A 1 4221 ? 155.119 151.472 123.845 1.00 22.01  ? 4221 THR A C     1 
ATOM   20427 O  O     . THR A 1 4221 ? 154.422 151.543 122.826 1.00 26.43  ? 4221 THR A O     1 
ATOM   20428 C  CB    . THR A 1 4221 ? 154.565 152.694 125.968 1.00 20.18  ? 4221 THR A CB    1 
ATOM   20429 O  OG1   . THR A 1 4221 ? 153.759 152.638 127.152 1.00 23.92  ? 4221 THR A OG1   1 
ATOM   20430 C  CG2   . THR A 1 4221 ? 154.079 153.834 125.086 1.00 22.31  ? 4221 THR A CG2   1 
ATOM   20431 N  N     . TRP A 1 4222 ? 156.451 151.479 123.793 1.00 19.75  ? 4222 TRP A N     1 
ATOM   20432 C  CA    . TRP A 1 4222 ? 157.135 151.729 122.530 1.00 22.13  ? 4222 TRP A CA    1 
ATOM   20433 C  C     . TRP A 1 4222 ? 157.263 150.475 121.677 1.00 26.79  ? 4222 TRP A C     1 
ATOM   20434 O  O     . TRP A 1 4222 ? 157.404 150.580 120.453 1.00 29.10  ? 4222 TRP A O     1 
ATOM   20435 C  CB    . TRP A 1 4222 ? 158.510 152.343 122.796 1.00 21.77  ? 4222 TRP A CB    1 
ATOM   20436 C  CG    . TRP A 1 4222 ? 158.417 153.772 123.227 1.00 18.07  ? 4222 TRP A CG    1 
ATOM   20437 C  CD1   . TRP A 1 4222 ? 158.380 154.242 124.506 1.00 14.41  ? 4222 TRP A CD1   1 
ATOM   20438 C  CD2   . TRP A 1 4222 ? 158.319 154.919 122.375 1.00 14.92  ? 4222 TRP A CD2   1 
ATOM   20439 N  NE1   . TRP A 1 4222 ? 158.278 155.611 124.506 1.00 15.57  ? 4222 TRP A NE1   1 
ATOM   20440 C  CE2   . TRP A 1 4222 ? 158.239 156.051 123.209 1.00 15.73  ? 4222 TRP A CE2   1 
ATOM   20441 C  CE3   . TRP A 1 4222 ? 158.299 155.099 120.989 1.00 18.94  ? 4222 TRP A CE3   1 
ATOM   20442 C  CZ2   . TRP A 1 4222 ? 158.139 157.345 122.703 1.00 17.94  ? 4222 TRP A CZ2   1 
ATOM   20443 C  CZ3   . TRP A 1 4222 ? 158.201 156.384 120.488 1.00 20.33  ? 4222 TRP A CZ3   1 
ATOM   20444 C  CH2   . TRP A 1 4222 ? 158.122 157.490 121.343 1.00 18.64  ? 4222 TRP A CH2   1 
ATOM   20445 N  N     . LEU A 1 4223 ? 157.220 149.289 122.288 1.00 29.38  ? 4223 LEU A N     1 
ATOM   20446 C  CA    . LEU A 1 4223 ? 157.202 148.065 121.493 1.00 29.26  ? 4223 LEU A CA    1 
ATOM   20447 C  C     . LEU A 1 4223 ? 155.869 147.897 120.777 1.00 33.98  ? 4223 LEU A C     1 
ATOM   20448 O  O     . LEU A 1 4223 ? 155.834 147.543 119.593 1.00 38.47  ? 4223 LEU A O     1 
ATOM   20449 C  CB    . LEU A 1 4223 ? 157.493 146.852 122.376 1.00 26.35  ? 4223 LEU A CB    1 
ATOM   20450 C  CG    . LEU A 1 4223 ? 158.114 145.646 121.668 1.00 29.94  ? 4223 LEU A CG    1 
ATOM   20451 C  CD1   . LEU A 1 4223 ? 159.291 146.073 120.806 1.00 25.91  ? 4223 LEU A CD1   1 
ATOM   20452 C  CD2   . LEU A 1 4223 ? 158.538 144.591 122.676 1.00 31.91  ? 4223 LEU A CD2   1 
ATOM   20453 N  N     . ASP A 1 4224 ? 154.760 148.146 121.478 1.00 32.49  ? 4224 ASP A N     1 
ATOM   20454 C  CA    . ASP A 1 4224 ? 153.449 148.065 120.844 1.00 35.53  ? 4224 ASP A CA    1 
ATOM   20455 C  C     . ASP A 1 4224 ? 153.258 149.169 119.812 1.00 40.64  ? 4224 ASP A C     1 
ATOM   20456 O  O     . ASP A 1 4224 ? 152.508 148.990 118.846 1.00 45.91  ? 4224 ASP A O     1 
ATOM   20457 C  CB    . ASP A 1 4224 ? 152.347 148.129 121.900 1.00 34.40  ? 4224 ASP A CB    1 
ATOM   20458 C  CG    . ASP A 1 4224 ? 152.485 147.046 122.951 1.00 45.11  ? 4224 ASP A CG    1 
ATOM   20459 O  OD1   . ASP A 1 4224 ? 153.427 146.233 122.848 1.00 47.55  ? 4224 ASP A OD1   1 
ATOM   20460 O  OD2   . ASP A 1 4224 ? 151.652 147.007 123.880 1.00 47.74  ? 4224 ASP A OD2   1 
ATOM   20461 N  N     . ASP A 1 4225 ? 153.913 150.315 120.003 1.00 37.67  ? 4225 ASP A N     1 
ATOM   20462 C  CA    . ASP A 1 4225 ? 153.820 151.391 119.023 1.00 38.52  ? 4225 ASP A CA    1 
ATOM   20463 C  C     . ASP A 1 4225 ? 154.507 151.006 117.718 1.00 43.10  ? 4225 ASP A C     1 
ATOM   20464 O  O     . ASP A 1 4225 ? 153.948 151.191 116.632 1.00 48.58  ? 4225 ASP A O     1 
ATOM   20465 C  CB    . ASP A 1 4225 ? 154.426 152.673 119.594 1.00 41.05  ? 4225 ASP A CB    1 
ATOM   20466 C  CG    . ASP A 1 4225 ? 154.278 153.855 118.658 1.00 54.40  ? 4225 ASP A CG    1 
ATOM   20467 O  OD1   . ASP A 1 4225 ? 153.170 154.426 118.593 1.00 57.13  ? 4225 ASP A OD1   1 
ATOM   20468 O  OD2   . ASP A 1 4225 ? 155.269 154.214 117.988 1.00 56.27  ? 4225 ASP A OD2   1 
ATOM   20469 N  N     . THR A 1 4226 ? 155.727 150.471 117.806 1.00 39.66  ? 4226 THR A N     1 
ATOM   20470 C  CA    . THR A 1 4226 ? 156.451 150.093 116.598 1.00 42.54  ? 4226 THR A CA    1 
ATOM   20471 C  C     . THR A 1 4226 ? 155.889 148.812 115.992 1.00 47.78  ? 4226 THR A C     1 
ATOM   20472 O  O     . THR A 1 4226 ? 155.703 148.724 114.772 1.00 51.31  ? 4226 THR A O     1 
ATOM   20473 C  CB    . THR A 1 4226 ? 157.941 149.939 116.909 1.00 39.48  ? 4226 THR A CB    1 
ATOM   20474 O  OG1   . THR A 1 4226 ? 158.538 151.235 117.036 1.00 42.52  ? 4226 THR A OG1   1 
ATOM   20475 C  CG2   . THR A 1 4226 ? 158.644 149.185 115.795 1.00 40.02  ? 4226 THR A CG2   1 
ATOM   20476 N  N     . ALA A 1 4227 ? 155.595 147.815 116.825 1.00 44.70  ? 4227 ALA A N     1 
ATOM   20477 C  CA    . ALA A 1 4227 ? 155.052 146.540 116.368 1.00 49.33  ? 4227 ALA A CA    1 
ATOM   20478 C  C     . ALA A 1 4227 ? 153.537 146.578 116.527 1.00 59.95  ? 4227 ALA A C     1 
ATOM   20479 O  O     . ALA A 1 4227 ? 153.022 146.528 117.649 1.00 62.77  ? 4227 ALA A O     1 
ATOM   20480 C  CB    . ALA A 1 4227 ? 155.661 145.376 117.147 1.00 45.16  ? 4227 ALA A CB    1 
ATOM   20481 N  N     . LYS A 1 4228 ? 152.826 146.657 115.402 1.00 59.99  ? 4228 LYS A N     1 
ATOM   20482 C  CA    . LYS A 1 4228 ? 151.369 146.782 115.407 1.00 58.04  ? 4228 LYS A CA    1 
ATOM   20483 C  C     . LYS A 1 4228 ? 150.709 145.405 115.515 1.00 59.19  ? 4228 LYS A C     1 
ATOM   20484 O  O     . LYS A 1 4228 ? 150.026 144.928 114.609 1.00 66.02  ? 4228 LYS A O     1 
ATOM   20485 C  CB    . LYS A 1 4228 ? 150.904 147.523 114.160 1.00 59.90  ? 4228 LYS A CB    1 
ATOM   20486 C  CG    . LYS A 1 4228 ? 151.682 148.794 113.867 1.00 60.49  ? 4228 LYS A CG    1 
ATOM   20487 C  CD    . LYS A 1 4228 ? 151.588 149.778 115.018 1.00 61.31  ? 4228 LYS A CD    1 
ATOM   20488 C  CE    . LYS A 1 4228 ? 150.162 150.263 115.221 1.00 68.98  ? 4228 LYS A CE    1 
ATOM   20489 N  NZ    . LYS A 1 4228 ? 150.055 151.213 116.363 1.00 65.16  ? 4228 LYS A NZ    1 
ATOM   20490 N  N     . GLY A 1 4229 ? 150.928 144.765 116.660 1.00 53.58  ? 4229 GLY A N     1 
ATOM   20491 C  CA    . GLY A 1 4229 ? 150.358 143.459 116.912 1.00 55.58  ? 4229 GLY A CA    1 
ATOM   20492 C  C     . GLY A 1 4229 ? 151.011 142.320 116.164 1.00 62.51  ? 4229 GLY A C     1 
ATOM   20493 O  O     . GLY A 1 4229 ? 150.457 141.215 116.146 1.00 63.42  ? 4229 GLY A O     1 
ATOM   20494 N  N     . ARG A 1 4230 ? 152.166 142.550 115.546 1.00 62.29  ? 4230 ARG A N     1 
ATOM   20495 C  CA    . ARG A 1 4230 ? 152.850 141.495 114.816 1.00 54.90  ? 4230 ARG A CA    1 
ATOM   20496 C  C     . ARG A 1 4230 ? 153.460 140.486 115.782 1.00 55.88  ? 4230 ARG A C     1 
ATOM   20497 O  O     . ARG A 1 4230 ? 153.767 140.801 116.935 1.00 58.73  ? 4230 ARG A O     1 
ATOM   20498 C  CB    . ARG A 1 4230 ? 153.939 142.086 113.921 1.00 59.01  ? 4230 ARG A CB    1 
ATOM   20499 C  CG    . ARG A 1 4230 ? 153.467 142.451 112.523 1.00 60.36  ? 4230 ARG A CG    1 
ATOM   20500 C  CD    . ARG A 1 4230 ? 153.502 143.955 112.314 1.00 59.91  ? 4230 ARG A CD    1 
ATOM   20501 N  NE    . ARG A 1 4230 ? 154.834 144.424 111.951 1.00 65.83  ? 4230 ARG A NE    1 
ATOM   20502 C  CZ    . ARG A 1 4230 ? 155.109 145.654 111.541 1.00 62.88  ? 4230 ARG A CZ    1 
ATOM   20503 N  NH1   . ARG A 1 4230 ? 154.165 146.574 111.431 1.00 57.47  ? 4230 ARG A NH1   1 
ATOM   20504 N  NH2   . ARG A 1 4230 ? 156.365 145.970 111.237 1.00 47.00  ? 4230 ARG A NH2   1 
ATOM   20505 N  N     . GLN A 1 4231 ? 153.631 139.255 115.299 1.00 59.85  ? 4231 GLN A N     1 
ATOM   20506 C  CA    . GLN A 1 4231 ? 154.198 138.211 116.146 1.00 58.21  ? 4231 GLN A CA    1 
ATOM   20507 C  C     . GLN A 1 4231 ? 155.702 138.385 116.314 1.00 58.50  ? 4231 GLN A C     1 
ATOM   20508 O  O     . GLN A 1 4231 ? 156.239 138.157 117.403 1.00 59.23  ? 4231 GLN A O     1 
ATOM   20509 C  CB    . GLN A 1 4231 ? 153.875 136.833 115.568 1.00 54.06  ? 4231 GLN A CB    1 
ATOM   20510 C  CG    . GLN A 1 4231 ? 153.673 135.752 116.620 1.00 59.75  ? 4231 GLN A CG    1 
ATOM   20511 C  CD    . GLN A 1 4231 ? 152.693 136.159 117.704 1.00 64.07  ? 4231 GLN A CD    1 
ATOM   20512 O  OE1   . GLN A 1 4231 ? 151.635 136.722 117.423 1.00 60.28  ? 4231 GLN A OE1   1 
ATOM   20513 N  NE2   . GLN A 1 4231 ? 153.043 135.874 118.953 1.00 66.54  ? 4231 GLN A NE2   1 
ATOM   20514 N  N     . ASN A 1 4232 ? 156.396 138.796 115.256 1.00 56.75  ? 4232 ASN A N     1 
ATOM   20515 C  CA    . ASN A 1 4232 ? 157.843 138.939 115.286 1.00 54.15  ? 4232 ASN A CA    1 
ATOM   20516 C  C     . ASN A 1 4232 ? 158.245 140.287 114.710 1.00 52.71  ? 4232 ASN A C     1 
ATOM   20517 O  O     . ASN A 1 4232 ? 157.660 140.755 113.728 1.00 53.06  ? 4232 ASN A O     1 
ATOM   20518 C  CB    . ASN A 1 4232 ? 158.531 137.813 114.505 1.00 55.72  ? 4232 ASN A CB    1 
ATOM   20519 C  CG    . ASN A 1 4232 ? 158.194 136.439 115.048 1.00 57.96  ? 4232 ASN A CG    1 
ATOM   20520 O  OD1   . ASN A 1 4232 ? 157.100 135.921 114.825 1.00 62.06  ? 4232 ASN A OD1   1 
ATOM   20521 N  ND2   . ASN A 1 4232 ? 159.136 135.841 115.769 1.00 53.80  ? 4232 ASN A ND2   1 
ATOM   20522 N  N     . ILE A 1 4233 ? 159.244 140.907 115.332 1.00 51.00  ? 4233 ILE A N     1 
ATOM   20523 C  CA    . ILE A 1 4233 ? 159.806 142.172 114.879 1.00 50.54  ? 4233 ILE A CA    1 
ATOM   20524 C  C     . ILE A 1 4233 ? 161.318 142.015 114.796 1.00 46.12  ? 4233 ILE A C     1 
ATOM   20525 O  O     . ILE A 1 4233 ? 161.946 141.512 115.735 1.00 48.48  ? 4233 ILE A O     1 
ATOM   20526 C  CB    . ILE A 1 4233 ? 159.424 143.336 115.816 1.00 51.41  ? 4233 ILE A CB    1 
ATOM   20527 C  CG1   . ILE A 1 4233 ? 160.224 144.593 115.472 1.00 44.23  ? 4233 ILE A CG1   1 
ATOM   20528 C  CG2   . ILE A 1 4233 ? 159.613 142.945 117.278 1.00 46.76  ? 4233 ILE A CG2   1 
ATOM   20529 C  CD1   . ILE A 1 4233 ? 159.781 145.814 116.236 1.00 43.16  ? 4233 ILE A CD1   1 
ATOM   20530 N  N     . SER A 1 4234 ? 161.896 142.423 113.672 1.00 41.08  ? 4234 SER A N     1 
ATOM   20531 C  CA    . SER A 1 4234 ? 163.340 142.342 113.524 1.00 42.42  ? 4234 SER A CA    1 
ATOM   20532 C  C     . SER A 1 4234 ? 164.011 143.280 114.524 1.00 44.23  ? 4234 SER A C     1 
ATOM   20533 O  O     . SER A 1 4234 ? 163.480 144.358 114.818 1.00 44.91  ? 4234 SER A O     1 
ATOM   20534 C  CB    . SER A 1 4234 ? 163.758 142.700 112.096 1.00 44.86  ? 4234 SER A CB    1 
ATOM   20535 O  OG    . SER A 1 4234 ? 165.168 142.747 111.970 1.00 50.37  ? 4234 SER A OG    1 
ATOM   20536 N  N     . PRO A 1 4235 ? 165.167 142.901 115.076 1.00 39.88  ? 4235 PRO A N     1 
ATOM   20537 C  CA    . PRO A 1 4235 ? 165.807 143.749 116.095 1.00 40.05  ? 4235 PRO A CA    1 
ATOM   20538 C  C     . PRO A 1 4235 ? 166.194 145.129 115.593 1.00 40.65  ? 4235 PRO A C     1 
ATOM   20539 O  O     . PRO A 1 4235 ? 166.385 146.035 116.414 1.00 43.87  ? 4235 PRO A O     1 
ATOM   20540 C  CB    . PRO A 1 4235 ? 167.043 142.935 116.503 1.00 37.98  ? 4235 PRO A CB    1 
ATOM   20541 C  CG    . PRO A 1 4235 ? 166.704 141.525 116.140 1.00 39.47  ? 4235 PRO A CG    1 
ATOM   20542 C  CD    . PRO A 1 4235 ? 165.872 141.621 114.899 1.00 40.08  ? 4235 PRO A CD    1 
ATOM   20543 N  N     . ASP A 1 4236 ? 166.321 145.322 114.279 1.00 40.01  ? 4236 ASP A N     1 
ATOM   20544 C  CA    . ASP A 1 4236 ? 166.679 146.637 113.759 1.00 42.69  ? 4236 ASP A CA    1 
ATOM   20545 C  C     . ASP A 1 4236 ? 165.554 147.649 113.945 1.00 44.73  ? 4236 ASP A C     1 
ATOM   20546 O  O     . ASP A 1 4236 ? 165.823 148.840 114.139 1.00 47.95  ? 4236 ASP A O     1 
ATOM   20547 C  CB    . ASP A 1 4236 ? 167.062 146.533 112.284 1.00 45.94  ? 4236 ASP A CB    1 
ATOM   20548 C  CG    . ASP A 1 4236 ? 168.527 146.836 112.040 1.00 61.29  ? 4236 ASP A CG    1 
ATOM   20549 O  OD1   . ASP A 1 4236 ? 169.289 146.921 113.026 1.00 57.87  ? 4236 ASP A OD1   1 
ATOM   20550 O  OD2   . ASP A 1 4236 ? 168.916 146.992 110.864 1.00 72.21  ? 4236 ASP A OD2   1 
ATOM   20551 N  N     . LYS A 1 4237 ? 164.298 147.204 113.892 1.00 39.32  ? 4237 LYS A N     1 
ATOM   20552 C  CA    . LYS A 1 4237 ? 163.170 148.118 114.021 1.00 41.25  ? 4237 LYS A CA    1 
ATOM   20553 C  C     . LYS A 1 4237 ? 162.799 148.415 115.468 1.00 36.33  ? 4237 LYS A C     1 
ATOM   20554 O  O     . LYS A 1 4237 ? 161.928 149.260 115.700 1.00 35.35  ? 4237 LYS A O     1 
ATOM   20555 C  CB    . LYS A 1 4237 ? 161.945 147.561 113.291 1.00 43.15  ? 4237 LYS A CB    1 
ATOM   20556 C  CG    . LYS A 1 4237 ? 162.241 146.978 111.922 1.00 41.59  ? 4237 LYS A CG    1 
ATOM   20557 C  CD    . LYS A 1 4237 ? 161.714 145.561 111.809 1.00 51.07  ? 4237 LYS A CD    1 
ATOM   20558 C  CE    . LYS A 1 4237 ? 160.232 145.545 111.476 1.00 51.74  ? 4237 LYS A CE    1 
ATOM   20559 N  NZ    . LYS A 1 4237 ? 159.690 144.159 111.431 1.00 45.55  ? 4237 LYS A NZ    1 
ATOM   20560 N  N     . ILE A 1 4238 ? 163.420 147.749 116.432 1.00 34.34  ? 4238 ILE A N     1 
ATOM   20561 C  CA    . ILE A 1 4238 ? 163.130 148.032 117.842 1.00 32.69  ? 4238 ILE A CA    1 
ATOM   20562 C  C     . ILE A 1 4238 ? 163.577 149.453 118.169 1.00 29.57  ? 4238 ILE A C     1 
ATOM   20563 O  O     . ILE A 1 4238 ? 164.721 149.827 117.853 1.00 32.44  ? 4238 ILE A O     1 
ATOM   20564 C  CB    . ILE A 1 4238 ? 163.825 147.010 118.744 1.00 31.48  ? 4238 ILE A CB    1 
ATOM   20565 C  CG1   . ILE A 1 4238 ? 163.178 145.633 118.584 1.00 31.74  ? 4238 ILE A CG1   1 
ATOM   20566 C  CG2   . ILE A 1 4238 ? 163.785 147.457 120.198 1.00 25.88  ? 4238 ILE A CG2   1 
ATOM   20567 C  CD1   . ILE A 1 4238 ? 163.791 144.566 119.461 1.00 32.22  ? 4238 ILE A CD1   1 
ATOM   20568 N  N     . PRO A 1 4239 ? 162.729 150.278 118.789 1.00 27.26  ? 4239 PRO A N     1 
ATOM   20569 C  CA    . PRO A 1 4239 ? 163.127 151.662 119.080 1.00 26.59  ? 4239 PRO A CA    1 
ATOM   20570 C  C     . PRO A 1 4239 ? 164.181 151.743 120.171 1.00 24.50  ? 4239 PRO A C     1 
ATOM   20571 O  O     . PRO A 1 4239 ? 163.880 152.107 121.312 1.00 26.32  ? 4239 PRO A O     1 
ATOM   20572 C  CB    . PRO A 1 4239 ? 161.811 152.317 119.515 1.00 27.25  ? 4239 PRO A CB    1 
ATOM   20573 C  CG    . PRO A 1 4239 ? 161.005 151.194 120.061 1.00 25.76  ? 4239 PRO A CG    1 
ATOM   20574 C  CD    . PRO A 1 4239 ? 161.351 149.994 119.224 1.00 27.46  ? 4239 PRO A CD    1 
ATOM   20575 N  N     . TRP A 1 4240 ? 165.425 151.404 119.823 1.00 24.07  ? 4240 TRP A N     1 
ATOM   20576 C  CA    . TRP A 1 4240 ? 166.504 151.421 120.805 1.00 20.11  ? 4240 TRP A CA    1 
ATOM   20577 C  C     . TRP A 1 4240 ? 166.766 152.831 121.316 1.00 19.71  ? 4240 TRP A C     1 
ATOM   20578 O  O     . TRP A 1 4240 ? 167.009 153.032 122.512 1.00 21.35  ? 4240 TRP A O     1 
ATOM   20579 C  CB    . TRP A 1 4240 ? 167.775 150.829 120.197 1.00 20.38  ? 4240 TRP A CB    1 
ATOM   20580 C  CG    . TRP A 1 4240 ? 167.640 149.396 119.791 1.00 22.57  ? 4240 TRP A CG    1 
ATOM   20581 C  CD1   . TRP A 1 4240 ? 167.630 148.904 118.519 1.00 26.45  ? 4240 TRP A CD1   1 
ATOM   20582 C  CD2   . TRP A 1 4240 ? 167.499 148.265 120.659 1.00 25.04  ? 4240 TRP A CD2   1 
ATOM   20583 N  NE1   . TRP A 1 4240 ? 167.489 147.539 118.540 1.00 30.44  ? 4240 TRP A NE1   1 
ATOM   20584 C  CE2   . TRP A 1 4240 ? 167.407 147.121 119.842 1.00 27.85  ? 4240 TRP A CE2   1 
ATOM   20585 C  CE3   . TRP A 1 4240 ? 167.440 148.110 122.047 1.00 25.25  ? 4240 TRP A CE3   1 
ATOM   20586 C  CZ2   . TRP A 1 4240 ? 167.261 145.840 120.366 1.00 28.21  ? 4240 TRP A CZ2   1 
ATOM   20587 C  CZ3   . TRP A 1 4240 ? 167.296 146.837 122.565 1.00 20.17  ? 4240 TRP A CZ3   1 
ATOM   20588 C  CH2   . TRP A 1 4240 ? 167.209 145.719 121.726 1.00 23.13  ? 4240 TRP A CH2   1 
ATOM   20589 N  N     . SER A 1 4241 ? 166.730 153.821 120.420 1.00 20.19  ? 4241 SER A N     1 
ATOM   20590 C  CA    . SER A 1 4241 ? 167.001 155.197 120.825 1.00 18.00  ? 4241 SER A CA    1 
ATOM   20591 C  C     . SER A 1 4241 ? 165.959 155.698 121.816 1.00 17.90  ? 4241 SER A C     1 
ATOM   20592 O  O     . SER A 1 4241 ? 166.294 156.400 122.777 1.00 15.81  ? 4241 SER A O     1 
ATOM   20593 C  CB    . SER A 1 4241 ? 167.053 156.103 119.595 1.00 20.89  ? 4241 SER A CB    1 
ATOM   20594 O  OG    . SER A 1 4241 ? 167.991 155.623 118.647 1.00 28.97  ? 4241 SER A OG    1 
ATOM   20595 N  N     . ALA A 1 4242 ? 164.689 155.352 121.596 1.00 20.85  ? 4242 ALA A N     1 
ATOM   20596 C  CA    . ALA A 1 4242 ? 163.633 155.779 122.508 1.00 15.90  ? 4242 ALA A CA    1 
ATOM   20597 C  C     . ALA A 1 4242 ? 163.839 155.194 123.899 1.00 14.84  ? 4242 ALA A C     1 
ATOM   20598 O  O     . ALA A 1 4242 ? 163.748 155.906 124.905 1.00 16.34  ? 4242 ALA A O     1 
ATOM   20599 C  CB    . ALA A 1 4242 ? 162.267 155.377 121.951 1.00 16.30  ? 4242 ALA A CB    1 
ATOM   20600 N  N     . LEU A 1 4243 ? 164.117 153.890 123.975 1.00 17.30  ? 4243 LEU A N     1 
ATOM   20601 C  CA    . LEU A 1 4243 ? 164.322 153.251 125.270 1.00 13.65  ? 4243 LEU A CA    1 
ATOM   20602 C  C     . LEU A 1 4243 ? 165.565 153.796 125.963 1.00 12.73  ? 4243 LEU A C     1 
ATOM   20603 O  O     . LEU A 1 4243 ? 165.545 154.076 127.166 1.00 14.65  ? 4243 LEU A O     1 
ATOM   20604 C  CB    . LEU A 1 4243 ? 164.422 151.735 125.099 1.00 12.51  ? 4243 LEU A CB    1 
ATOM   20605 C  CG    . LEU A 1 4243 ? 163.308 151.055 124.303 1.00 13.62  ? 4243 LEU A CG    1 
ATOM   20606 C  CD1   . LEU A 1 4243 ? 163.542 149.555 124.236 1.00 19.75  ? 4243 LEU A CD1   1 
ATOM   20607 C  CD2   . LEU A 1 4243 ? 161.949 151.360 124.908 1.00 15.24  ? 4243 LEU A CD2   1 
ATOM   20608 N  N     . LYS A 1 4244 ? 166.659 153.954 125.217 1.00 14.04  ? 4244 LYS A N     1 
ATOM   20609 C  CA    . LYS A 1 4244 ? 167.907 154.416 125.817 1.00 13.15  ? 4244 LYS A CA    1 
ATOM   20610 C  C     . LYS A 1 4244 ? 167.783 155.848 126.324 1.00 10.43  ? 4244 LYS A C     1 
ATOM   20611 O  O     . LYS A 1 4244 ? 168.217 156.164 127.437 1.00 10.42  ? 4244 LYS A O     1 
ATOM   20612 C  CB    . LYS A 1 4244 ? 169.044 154.299 124.802 1.00 15.02  ? 4244 LYS A CB    1 
ATOM   20613 C  CG    . LYS A 1 4244 ? 169.812 152.991 124.875 1.00 20.02  ? 4244 LYS A CG    1 
ATOM   20614 C  CD    . LYS A 1 4244 ? 170.951 152.973 123.872 1.00 20.67  ? 4244 LYS A CD    1 
ATOM   20615 C  CE    . LYS A 1 4244 ? 170.427 153.079 122.450 1.00 20.12  ? 4244 LYS A CE    1 
ATOM   20616 N  NZ    . LYS A 1 4244 ? 171.176 154.089 121.655 1.00 29.29  ? 4244 LYS A NZ    1 
ATOM   20617 N  N     . THR A 1 4245 ? 167.188 156.730 125.517 1.00 11.02  ? 4245 THR A N     1 
ATOM   20618 C  CA    . THR A 1 4245 ? 167.119 158.140 125.889 1.00 9.75   ? 4245 THR A CA    1 
ATOM   20619 C  C     . THR A 1 4245 ? 166.166 158.365 127.055 1.00 10.45  ? 4245 THR A C     1 
ATOM   20620 O  O     . THR A 1 4245 ? 166.503 159.077 128.008 1.00 10.97  ? 4245 THR A O     1 
ATOM   20621 C  CB    . THR A 1 4245 ? 166.697 158.984 124.687 1.00 14.13  ? 4245 THR A CB    1 
ATOM   20622 O  OG1   . THR A 1 4245 ? 167.448 158.585 123.534 1.00 19.06  ? 4245 THR A OG1   1 
ATOM   20623 C  CG2   . THR A 1 4245 ? 166.942 160.463 124.961 1.00 14.76  ? 4245 THR A CG2   1 
ATOM   20624 N  N     . LEU A 1 4246 ? 164.974 157.767 127.003 1.00 10.32  ? 4246 LEU A N     1 
ATOM   20625 C  CA    . LEU A 1 4246 ? 164.021 157.933 128.095 1.00 9.57   ? 4246 LEU A CA    1 
ATOM   20626 C  C     . LEU A 1 4246 ? 164.547 157.337 129.393 1.00 9.07   ? 4246 LEU A C     1 
ATOM   20627 O  O     . LEU A 1 4246 ? 164.193 157.806 130.479 1.00 12.01  ? 4246 LEU A O     1 
ATOM   20628 C  CB    . LEU A 1 4246 ? 162.678 157.302 127.727 1.00 9.39   ? 4246 LEU A CB    1 
ATOM   20629 C  CG    . LEU A 1 4246 ? 161.780 158.114 126.792 1.00 8.01   ? 4246 LEU A CG    1 
ATOM   20630 C  CD1   . LEU A 1 4246 ? 160.437 157.426 126.593 1.00 10.63  ? 4246 LEU A CD1   1 
ATOM   20631 C  CD2   . LEU A 1 4246 ? 161.588 159.526 127.321 1.00 10.89  ? 4246 LEU A CD2   1 
ATOM   20632 N  N     . MET A 1 4247 ? 165.380 156.304 129.300 1.00 9.82   ? 4247 MET A N     1 
ATOM   20633 C  CA    . MET A 1 4247 ? 165.926 155.665 130.488 1.00 6.63   ? 4247 MET A CA    1 
ATOM   20634 C  C     . MET A 1 4247 ? 167.075 156.465 131.083 1.00 7.99   ? 4247 MET A C     1 
ATOM   20635 O  O     . MET A 1 4247 ? 167.248 156.488 132.308 1.00 7.25   ? 4247 MET A O     1 
ATOM   20636 C  CB    . MET A 1 4247 ? 166.389 154.259 130.127 1.00 6.79   ? 4247 MET A CB    1 
ATOM   20637 C  CG    . MET A 1 4247 ? 165.422 153.192 130.546 1.00 7.52   ? 4247 MET A CG    1 
ATOM   20638 S  SD    . MET A 1 4247 ? 165.509 151.805 129.411 1.00 25.62  ? 4247 MET A SD    1 
ATOM   20639 C  CE    . MET A 1 4247 ? 164.154 150.849 130.042 1.00 31.11  ? 4247 MET A CE    1 
ATOM   20640 N  N     . ALA A 1 4248 ? 167.867 157.116 130.231 1.00 9.55   ? 4248 ALA A N     1 
ATOM   20641 C  CA    . ALA A 1 4248 ? 169.011 157.891 130.690 1.00 9.00   ? 4248 ALA A CA    1 
ATOM   20642 C  C     . ALA A 1 4248 ? 168.616 159.285 131.152 1.00 10.71  ? 4248 ALA A C     1 
ATOM   20643 O  O     . ALA A 1 4248 ? 169.361 159.915 131.909 1.00 18.37  ? 4248 ALA A O     1 
ATOM   20644 C  CB    . ALA A 1 4248 ? 170.052 157.990 129.576 1.00 10.61  ? 4248 ALA A CB    1 
ATOM   20645 N  N     . GLN A 1 4249 ? 167.470 159.788 130.699 1.00 9.26   ? 4249 GLN A N     1 
ATOM   20646 C  CA    . GLN A 1 4249 ? 167.038 161.140 131.023 1.00 7.68   ? 4249 GLN A CA    1 
ATOM   20647 C  C     . GLN A 1 4249 ? 165.888 161.200 132.013 1.00 10.39  ? 4249 GLN A C     1 
ATOM   20648 O  O     . GLN A 1 4249 ? 165.818 162.149 132.796 1.00 14.06  ? 4249 GLN A O     1 
ATOM   20649 C  CB    . GLN A 1 4249 ? 166.627 161.884 129.746 1.00 11.06  ? 4249 GLN A CB    1 
ATOM   20650 C  CG    . GLN A 1 4249 ? 167.702 161.934 128.673 1.00 9.54   ? 4249 GLN A CG    1 
ATOM   20651 C  CD    . GLN A 1 4249 ? 168.783 162.948 128.978 1.00 13.69  ? 4249 GLN A CD    1 
ATOM   20652 O  OE1   . GLN A 1 4249 ? 168.512 164.141 129.107 1.00 15.15  ? 4249 GLN A OE1   1 
ATOM   20653 N  NE2   . GLN A 1 4249 ? 170.019 162.479 129.096 1.00 12.76  ? 4249 GLN A NE2   1 
ATOM   20654 N  N     . SER A 1 4250 ? 164.988 160.219 132.003 1.00 10.36  ? 4250 SER A N     1 
ATOM   20655 C  CA    . SER A 1 4250 ? 163.772 160.290 132.805 1.00 6.62   ? 4250 SER A CA    1 
ATOM   20656 C  C     . SER A 1 4250 ? 163.675 159.194 133.854 1.00 7.57   ? 4250 SER A C     1 
ATOM   20657 O  O     . SER A 1 4250 ? 163.459 159.493 135.033 1.00 11.54  ? 4250 SER A O     1 
ATOM   20658 C  CB    . SER A 1 4250 ? 162.539 160.242 131.891 1.00 8.69   ? 4250 SER A CB    1 
ATOM   20659 O  OG    . SER A 1 4250 ? 162.504 161.359 131.022 1.00 8.18   ? 4250 SER A OG    1 
ATOM   20660 N  N     . ILE A 1 4251 ? 163.821 157.929 133.461 1.00 8.51   ? 4251 ILE A N     1 
ATOM   20661 C  CA    . ILE A 1 4251 ? 163.547 156.826 134.379 1.00 8.53   ? 4251 ILE A CA    1 
ATOM   20662 C  C     . ILE A 1 4251 ? 164.661 156.688 135.410 1.00 9.06   ? 4251 ILE A C     1 
ATOM   20663 O  O     . ILE A 1 4251 ? 164.439 156.847 136.615 1.00 13.86  ? 4251 ILE A O     1 
ATOM   20664 C  CB    . ILE A 1 4251 ? 163.338 155.516 133.599 1.00 7.42   ? 4251 ILE A CB    1 
ATOM   20665 C  CG1   . ILE A 1 4251 ? 162.188 155.665 132.603 1.00 5.41   ? 4251 ILE A CG1   1 
ATOM   20666 C  CG2   . ILE A 1 4251 ? 163.072 154.369 134.554 1.00 6.80   ? 4251 ILE A CG2   1 
ATOM   20667 C  CD1   . ILE A 1 4251 ? 162.202 154.633 131.503 1.00 5.82   ? 4251 ILE A CD1   1 
ATOM   20668 N  N     . TYR A 1 4252 ? 165.873 156.386 134.953 1.00 9.37   ? 4252 TYR A N     1 
ATOM   20669 C  CA    . TYR A 1 4252 ? 166.993 156.210 135.867 1.00 8.81   ? 4252 TYR A CA    1 
ATOM   20670 C  C     . TYR A 1 4252 ? 167.857 157.455 135.980 1.00 8.66   ? 4252 TYR A C     1 
ATOM   20671 O  O     . TYR A 1 4252 ? 168.447 157.697 137.039 1.00 10.96  ? 4252 TYR A O     1 
ATOM   20672 C  CB    . TYR A 1 4252 ? 167.857 155.026 135.424 1.00 8.24   ? 4252 TYR A CB    1 
ATOM   20673 C  CG    . TYR A 1 4252 ? 167.221 153.677 135.668 1.00 6.37   ? 4252 TYR A CG    1 
ATOM   20674 C  CD1   . TYR A 1 4252 ? 167.367 153.027 136.885 1.00 6.39   ? 4252 TYR A CD1   1 
ATOM   20675 C  CD2   . TYR A 1 4252 ? 166.469 153.056 134.683 1.00 6.36   ? 4252 TYR A CD2   1 
ATOM   20676 C  CE1   . TYR A 1 4252 ? 166.788 151.793 137.109 1.00 7.15   ? 4252 TYR A CE1   1 
ATOM   20677 C  CE2   . TYR A 1 4252 ? 165.884 151.825 134.900 1.00 5.50   ? 4252 TYR A CE2   1 
ATOM   20678 C  CZ    . TYR A 1 4252 ? 166.046 151.198 136.114 1.00 5.21   ? 4252 TYR A CZ    1 
ATOM   20679 O  OH    . TYR A 1 4252 ? 165.465 149.971 136.332 1.00 7.05   ? 4252 TYR A OH    1 
ATOM   20680 N  N     . GLY A 1 4253 ? 167.943 158.252 134.916 1.00 8.18   ? 4253 GLY A N     1 
ATOM   20681 C  CA    . GLY A 1 4253 ? 168.726 159.470 134.958 1.00 7.77   ? 4253 GLY A CA    1 
ATOM   20682 C  C     . GLY A 1 4253 ? 168.095 160.613 135.716 1.00 9.72   ? 4253 GLY A C     1 
ATOM   20683 O  O     . GLY A 1 4253 ? 168.782 161.597 136.007 1.00 13.22  ? 4253 GLY A O     1 
ATOM   20684 N  N     . GLY A 1 4254 ? 166.804 160.512 136.037 1.00 7.70   ? 4254 GLY A N     1 
ATOM   20685 C  CA    . GLY A 1 4254 ? 166.166 161.553 136.823 1.00 7.40   ? 4254 GLY A CA    1 
ATOM   20686 C  C     . GLY A 1 4254 ? 166.762 161.680 138.212 1.00 11.79  ? 4254 GLY A C     1 
ATOM   20687 O  O     . GLY A 1 4254 ? 166.946 162.789 138.720 1.00 12.39  ? 4254 GLY A O     1 
ATOM   20688 N  N     . ARG A 1 4255 ? 167.076 160.547 138.844 1.00 12.46  ? 4255 ARG A N     1 
ATOM   20689 C  CA    . ARG A 1 4255 ? 167.700 160.577 140.160 1.00 11.66  ? 4255 ARG A CA    1 
ATOM   20690 C  C     . ARG A 1 4255 ? 169.167 160.975 140.096 1.00 13.88  ? 4255 ARG A C     1 
ATOM   20691 O  O     . ARG A 1 4255 ? 169.730 161.385 141.117 1.00 19.96  ? 4255 ARG A O     1 
ATOM   20692 C  CB    . ARG A 1 4255 ? 167.572 159.213 140.838 1.00 15.28  ? 4255 ARG A CB    1 
ATOM   20693 C  CG    . ARG A 1 4255 ? 166.231 158.534 140.631 1.00 18.93  ? 4255 ARG A CG    1 
ATOM   20694 C  CD    . ARG A 1 4255 ? 166.199 157.173 141.308 1.00 18.10  ? 4255 ARG A CD    1 
ATOM   20695 N  NE    . ARG A 1 4255 ? 164.849 156.630 141.380 1.00 21.48  ? 4255 ARG A NE    1 
ATOM   20696 C  CZ    . ARG A 1 4255 ? 163.941 156.994 142.275 1.00 19.10  ? 4255 ARG A CZ    1 
ATOM   20697 N  NH1   . ARG A 1 4255 ? 164.207 157.903 143.199 1.00 18.25  ? 4255 ARG A NH1   1 
ATOM   20698 N  NH2   . ARG A 1 4255 ? 162.737 156.429 142.245 1.00 19.29  ? 4255 ARG A NH2   1 
ATOM   20699 N  N     . VAL A 1 4256 ? 169.794 160.872 138.928 1.00 13.14  ? 4256 VAL A N     1 
ATOM   20700 C  CA    . VAL A 1 4256 ? 171.221 161.143 138.793 1.00 13.94  ? 4256 VAL A CA    1 
ATOM   20701 C  C     . VAL A 1 4256 ? 171.433 162.649 138.719 1.00 15.21  ? 4256 VAL A C     1 
ATOM   20702 O  O     . VAL A 1 4256 ? 170.853 163.329 137.866 1.00 15.98  ? 4256 VAL A O     1 
ATOM   20703 C  CB    . VAL A 1 4256 ? 171.800 160.440 137.557 1.00 13.13  ? 4256 VAL A CB    1 
ATOM   20704 C  CG1   . VAL A 1 4256 ? 173.199 160.953 137.263 1.00 18.53  ? 4256 VAL A CG1   1 
ATOM   20705 C  CG2   . VAL A 1 4256 ? 171.812 158.935 137.762 1.00 10.78  ? 4256 VAL A CG2   1 
ATOM   20706 N  N     . ASP A 1 4257 ? 172.267 163.174 139.618 1.00 17.82  ? 4257 ASP A N     1 
ATOM   20707 C  CA    . ASP A 1 4257 ? 172.599 164.594 139.651 1.00 21.50  ? 4257 ASP A CA    1 
ATOM   20708 C  C     . ASP A 1 4257 ? 174.091 164.836 139.455 1.00 20.46  ? 4257 ASP A C     1 
ATOM   20709 O  O     . ASP A 1 4257 ? 174.585 165.923 139.766 1.00 18.44  ? 4257 ASP A O     1 
ATOM   20710 C  CB    . ASP A 1 4257 ? 172.131 165.221 140.965 1.00 21.43  ? 4257 ASP A CB    1 
ATOM   20711 C  CG    . ASP A 1 4257 ? 172.338 164.306 142.151 1.00 27.82  ? 4257 ASP A CG    1 
ATOM   20712 O  OD1   . ASP A 1 4257 ? 173.499 163.934 142.414 1.00 28.81  ? 4257 ASP A OD1   1 
ATOM   20713 O  OD2   . ASP A 1 4257 ? 171.341 163.959 142.820 1.00 32.89  ? 4257 ASP A OD2   1 
ATOM   20714 N  N     . ASN A 1 4258 ? 174.816 163.846 138.946 1.00 23.74  ? 4258 ASN A N     1 
ATOM   20715 C  CA    . ASN A 1 4258 ? 176.255 163.935 138.759 1.00 21.19  ? 4258 ASN A CA    1 
ATOM   20716 C  C     . ASN A 1 4258 ? 176.551 163.671 137.289 1.00 20.33  ? 4258 ASN A C     1 
ATOM   20717 O  O     . ASN A 1 4258 ? 175.970 162.766 136.682 1.00 21.10  ? 4258 ASN A O     1 
ATOM   20718 C  CB    . ASN A 1 4258 ? 176.979 162.936 139.699 1.00 16.27  ? 4258 ASN A CB    1 
ATOM   20719 C  CG    . ASN A 1 4258 ? 178.451 162.692 139.342 1.00 21.20  ? 4258 ASN A CG    1 
ATOM   20720 O  OD1   . ASN A 1 4258 ? 178.853 162.662 138.181 1.00 25.12  ? 4258 ASN A OD1   1 
ATOM   20721 N  ND2   . ASN A 1 4258 ? 179.264 162.512 140.376 1.00 23.12  ? 4258 ASN A ND2   1 
ATOM   20722 N  N     . GLU A 1 4259 ? 177.454 164.475 136.722 1.00 17.36  ? 4259 GLU A N     1 
ATOM   20723 C  CA    . GLU A 1 4259 ? 177.775 164.354 135.304 1.00 16.29  ? 4259 GLU A CA    1 
ATOM   20724 C  C     . GLU A 1 4259 ? 178.401 163.002 134.983 1.00 18.22  ? 4259 GLU A C     1 
ATOM   20725 O  O     . GLU A 1 4259 ? 178.050 162.368 133.981 1.00 21.95  ? 4259 GLU A O     1 
ATOM   20726 C  CB    . GLU A 1 4259 ? 178.708 165.490 134.886 1.00 22.15  ? 4259 GLU A CB    1 
ATOM   20727 C  CG    . GLU A 1 4259 ? 179.576 165.180 133.679 1.00 33.09  ? 4259 GLU A CG    1 
ATOM   20728 C  CD    . GLU A 1 4259 ? 180.517 166.316 133.334 1.00 46.17  ? 4259 GLU A CD    1 
ATOM   20729 O  OE1   . GLU A 1 4259 ? 180.475 167.355 134.025 1.00 44.98  ? 4259 GLU A OE1   1 
ATOM   20730 O  OE2   . GLU A 1 4259 ? 181.302 166.169 132.374 1.00 52.80  ? 4259 GLU A OE2   1 
ATOM   20731 N  N     . PHE A 1 4260 ? 179.330 162.544 135.823 1.00 18.30  ? 4260 PHE A N     1 
ATOM   20732 C  CA    . PHE A 1 4260 ? 180.020 161.286 135.564 1.00 15.17  ? 4260 PHE A CA    1 
ATOM   20733 C  C     . PHE A 1 4260 ? 179.147 160.078 135.871 1.00 16.31  ? 4260 PHE A C     1 
ATOM   20734 O  O     . PHE A 1 4260 ? 179.323 159.022 135.252 1.00 18.98  ? 4260 PHE A O     1 
ATOM   20735 C  CB    . PHE A 1 4260 ? 181.320 161.242 136.367 1.00 18.79  ? 4260 PHE A CB    1 
ATOM   20736 C  CG    . PHE A 1 4260 ? 182.223 162.411 136.100 1.00 19.95  ? 4260 PHE A CG    1 
ATOM   20737 C  CD1   . PHE A 1 4260 ? 183.104 162.391 135.033 1.00 22.51  ? 4260 PHE A CD1   1 
ATOM   20738 C  CD2   . PHE A 1 4260 ? 182.165 163.545 136.892 1.00 19.22  ? 4260 PHE A CD2   1 
ATOM   20739 C  CE1   . PHE A 1 4260 ? 183.927 163.467 134.774 1.00 25.16  ? 4260 PHE A CE1   1 
ATOM   20740 C  CE2   . PHE A 1 4260 ? 182.982 164.627 136.636 1.00 26.42  ? 4260 PHE A CE2   1 
ATOM   20741 C  CZ    . PHE A 1 4260 ? 183.866 164.588 135.576 1.00 27.91  ? 4260 PHE A CZ    1 
ATOM   20742 N  N     . ASP A 1 4261 ? 178.212 160.205 136.815 1.00 16.61  ? 4261 ASP A N     1 
ATOM   20743 C  CA    . ASP A 1 4261 ? 177.215 159.156 137.002 1.00 15.66  ? 4261 ASP A CA    1 
ATOM   20744 C  C     . ASP A 1 4261 ? 176.317 159.038 135.778 1.00 15.02  ? 4261 ASP A C     1 
ATOM   20745 O  O     . ASP A 1 4261 ? 175.931 157.932 135.384 1.00 16.12  ? 4261 ASP A O     1 
ATOM   20746 C  CB    . ASP A 1 4261 ? 176.383 159.432 138.252 1.00 16.10  ? 4261 ASP A CB    1 
ATOM   20747 C  CG    . ASP A 1 4261 ? 177.161 159.208 139.531 1.00 20.73  ? 4261 ASP A CG    1 
ATOM   20748 O  OD1   . ASP A 1 4261 ? 178.164 158.465 139.501 1.00 24.67  ? 4261 ASP A OD1   1 
ATOM   20749 O  OD2   . ASP A 1 4261 ? 176.762 159.773 140.569 1.00 22.81  ? 4261 ASP A OD2   1 
ATOM   20750 N  N     . GLN A 1 4262 ? 175.970 160.175 135.169 1.00 13.75  ? 4262 GLN A N     1 
ATOM   20751 C  CA    . GLN A 1 4262 ? 175.190 160.153 133.936 1.00 13.89  ? 4262 GLN A CA    1 
ATOM   20752 C  C     . GLN A 1 4262 ? 175.954 159.458 132.817 1.00 12.29  ? 4262 GLN A C     1 
ATOM   20753 O  O     . GLN A 1 4262 ? 175.381 158.662 132.064 1.00 13.42  ? 4262 GLN A O     1 
ATOM   20754 C  CB    . GLN A 1 4262 ? 174.823 161.580 133.528 1.00 15.13  ? 4262 GLN A CB    1 
ATOM   20755 C  CG    . GLN A 1 4262 ? 173.912 161.672 132.317 1.00 14.86  ? 4262 GLN A CG    1 
ATOM   20756 C  CD    . GLN A 1 4262 ? 172.541 161.086 132.575 1.00 14.77  ? 4262 GLN A CD    1 
ATOM   20757 O  OE1   . GLN A 1 4262 ? 171.901 161.395 133.580 1.00 17.97  ? 4262 GLN A OE1   1 
ATOM   20758 N  NE2   . GLN A 1 4262 ? 172.082 160.235 131.667 1.00 13.06  ? 4262 GLN A NE2   1 
ATOM   20759 N  N     . ARG A 1 4263 ? 177.251 159.747 132.694 1.00 12.64  ? 4263 ARG A N     1 
ATOM   20760 C  CA    . ARG A 1 4263 ? 178.068 159.101 131.672 1.00 13.82  ? 4263 ARG A CA    1 
ATOM   20761 C  C     . ARG A 1 4263 ? 178.153 157.597 131.901 1.00 14.92  ? 4263 ARG A C     1 
ATOM   20762 O  O     . ARG A 1 4263 ? 178.086 156.812 130.948 1.00 14.06  ? 4263 ARG A O     1 
ATOM   20763 C  CB    . ARG A 1 4263 ? 179.461 159.731 131.653 1.00 16.56  ? 4263 ARG A CB    1 
ATOM   20764 C  CG    . ARG A 1 4263 ? 180.508 158.948 130.885 1.00 19.59  ? 4263 ARG A CG    1 
ATOM   20765 C  CD    . ARG A 1 4263 ? 181.835 159.682 130.910 1.00 20.05  ? 4263 ARG A CD    1 
ATOM   20766 N  NE    . ARG A 1 4263 ? 182.537 159.483 132.172 1.00 27.14  ? 4263 ARG A NE    1 
ATOM   20767 C  CZ    . ARG A 1 4263 ? 183.725 160.000 132.458 1.00 31.80  ? 4263 ARG A CZ    1 
ATOM   20768 N  NH1   . ARG A 1 4263 ? 184.371 160.766 131.594 1.00 30.33  ? 4263 ARG A NH1   1 
ATOM   20769 N  NH2   . ARG A 1 4263 ? 184.278 159.738 133.638 1.00 27.34  ? 4263 ARG A NH2   1 
ATOM   20770 N  N     . LEU A 1 4264 ? 178.305 157.178 133.159 1.00 13.96  ? 4264 LEU A N     1 
ATOM   20771 C  CA    . LEU A 1 4264 ? 178.327 155.752 133.467 1.00 9.89   ? 4264 LEU A CA    1 
ATOM   20772 C  C     . LEU A 1 4264 ? 176.990 155.097 133.144 1.00 12.80  ? 4264 LEU A C     1 
ATOM   20773 O  O     . LEU A 1 4264 ? 176.952 153.988 132.598 1.00 17.44  ? 4264 LEU A O     1 
ATOM   20774 C  CB    . LEU A 1 4264 ? 178.688 155.541 134.936 1.00 12.56  ? 4264 LEU A CB    1 
ATOM   20775 C  CG    . LEU A 1 4264 ? 178.671 154.097 135.438 1.00 14.43  ? 4264 LEU A CG    1 
ATOM   20776 C  CD1   . LEU A 1 4264 ? 179.637 153.248 134.634 1.00 12.37  ? 4264 LEU A CD1   1 
ATOM   20777 C  CD2   . LEU A 1 4264 ? 179.002 154.040 136.919 1.00 12.52  ? 4264 LEU A CD2   1 
ATOM   20778 N  N     . LEU A 1 4265 ? 175.883 155.765 133.478 1.00 13.82  ? 4265 LEU A N     1 
ATOM   20779 C  CA    . LEU A 1 4265 ? 174.566 155.226 133.157 1.00 12.18  ? 4265 LEU A CA    1 
ATOM   20780 C  C     . LEU A 1 4265 ? 174.365 155.125 131.651 1.00 10.74  ? 4265 LEU A C     1 
ATOM   20781 O  O     . LEU A 1 4265 ? 173.792 154.146 131.157 1.00 11.07  ? 4265 LEU A O     1 
ATOM   20782 C  CB    . LEU A 1 4265 ? 173.478 156.094 133.791 1.00 15.39  ? 4265 LEU A CB    1 
ATOM   20783 C  CG    . LEU A 1 4265 ? 172.046 155.562 133.718 1.00 19.96  ? 4265 LEU A CG    1 
ATOM   20784 C  CD1   . LEU A 1 4265 ? 171.804 154.529 134.805 1.00 16.83  ? 4265 LEU A CD1   1 
ATOM   20785 C  CD2   . LEU A 1 4265 ? 171.046 156.700 133.824 1.00 12.82  ? 4265 LEU A CD2   1 
ATOM   20786 N  N     . ASN A 1 4266 ? 174.826 156.131 130.904 1.00 12.30  ? 4266 ASN A N     1 
ATOM   20787 C  CA    . ASN A 1 4266 ? 174.723 156.084 129.449 1.00 11.24  ? 4266 ASN A CA    1 
ATOM   20788 C  C     . ASN A 1 4266 ? 175.565 154.954 128.873 1.00 12.91  ? 4266 ASN A C     1 
ATOM   20789 O  O     . ASN A 1 4266 ? 175.172 154.316 127.889 1.00 13.62  ? 4266 ASN A O     1 
ATOM   20790 C  CB    . ASN A 1 4266 ? 175.148 157.424 128.848 1.00 12.36  ? 4266 ASN A CB    1 
ATOM   20791 C  CG    . ASN A 1 4266 ? 174.234 158.560 129.253 1.00 13.76  ? 4266 ASN A CG    1 
ATOM   20792 O  OD1   . ASN A 1 4266 ? 173.185 158.342 129.855 1.00 15.02  ? 4266 ASN A OD1   1 
ATOM   20793 N  ND2   . ASN A 1 4266 ? 174.630 159.785 128.928 1.00 15.06  ? 4266 ASN A ND2   1 
ATOM   20794 N  N     . THR A 1 4267 ? 176.733 154.699 129.467 1.00 15.69  ? 4267 THR A N     1 
ATOM   20795 C  CA    . THR A 1 4267 ? 177.617 153.652 128.962 1.00 13.74  ? 4267 THR A CA    1 
ATOM   20796 C  C     . THR A 1 4267 ? 176.962 152.279 129.063 1.00 17.87  ? 4267 THR A C     1 
ATOM   20797 O  O     . THR A 1 4267 ? 177.043 151.471 128.131 1.00 20.90  ? 4267 THR A O     1 
ATOM   20798 C  CB    . THR A 1 4267 ? 178.942 153.674 129.724 1.00 17.60  ? 4267 THR A CB    1 
ATOM   20799 O  OG1   . THR A 1 4267 ? 179.418 155.023 129.818 1.00 24.72  ? 4267 THR A OG1   1 
ATOM   20800 C  CG2   . THR A 1 4267 ? 179.980 152.826 129.009 1.00 30.50  ? 4267 THR A CG2   1 
ATOM   20801 N  N     . PHE A 1 4268 ? 176.311 151.996 130.194 1.00 14.95  ? 4268 PHE A N     1 
ATOM   20802 C  CA    . PHE A 1 4268 ? 175.613 150.722 130.345 1.00 11.52  ? 4268 PHE A CA    1 
ATOM   20803 C  C     . PHE A 1 4268 ? 174.447 150.609 129.372 1.00 14.14  ? 4268 PHE A C     1 
ATOM   20804 O  O     . PHE A 1 4268 ? 174.221 149.546 128.783 1.00 18.10  ? 4268 PHE A O     1 
ATOM   20805 C  CB    . PHE A 1 4268 ? 175.122 150.554 131.783 1.00 13.02  ? 4268 PHE A CB    1 
ATOM   20806 C  CG    . PHE A 1 4268 ? 176.202 150.179 132.756 1.00 14.13  ? 4268 PHE A CG    1 
ATOM   20807 C  CD1   . PHE A 1 4268 ? 177.023 149.092 132.512 1.00 16.74  ? 4268 PHE A CD1   1 
ATOM   20808 C  CD2   . PHE A 1 4268 ? 176.390 150.907 133.917 1.00 12.53  ? 4268 PHE A CD2   1 
ATOM   20809 C  CE1   . PHE A 1 4268 ? 178.015 148.741 133.405 1.00 22.14  ? 4268 PHE A CE1   1 
ATOM   20810 C  CE2   . PHE A 1 4268 ? 177.378 150.561 134.815 1.00 17.14  ? 4268 PHE A CE2   1 
ATOM   20811 C  CZ    . PHE A 1 4268 ? 178.193 149.478 134.559 1.00 22.00  ? 4268 PHE A CZ    1 
ATOM   20812 N  N     . LEU A 1 4269 ? 173.690 151.694 129.198 1.00 14.58  ? 4269 LEU A N     1 
ATOM   20813 C  CA    . LEU A 1 4269 ? 172.528 151.656 128.317 1.00 13.02  ? 4269 LEU A CA    1 
ATOM   20814 C  C     . LEU A 1 4269 ? 172.935 151.435 126.865 1.00 14.58  ? 4269 LEU A C     1 
ATOM   20815 O  O     . LEU A 1 4269 ? 172.299 150.655 126.148 1.00 14.59  ? 4269 LEU A O     1 
ATOM   20816 C  CB    . LEU A 1 4269 ? 171.722 152.946 128.463 1.00 12.64  ? 4269 LEU A CB    1 
ATOM   20817 C  CG    . LEU A 1 4269 ? 170.796 153.004 129.679 1.00 7.82   ? 4269 LEU A CG    1 
ATOM   20818 C  CD1   . LEU A 1 4269 ? 170.521 154.444 130.067 1.00 8.29   ? 4269 LEU A CD1   1 
ATOM   20819 C  CD2   . LEU A 1 4269 ? 169.498 152.265 129.406 1.00 8.49   ? 4269 LEU A CD2   1 
ATOM   20820 N  N     . GLU A 1 4270 ? 173.993 152.113 126.413 1.00 19.37  ? 4270 GLU A N     1 
ATOM   20821 C  CA    . GLU A 1 4270 ? 174.456 151.920 125.043 1.00 18.63  ? 4270 GLU A CA    1 
ATOM   20822 C  C     . GLU A 1 4270 ? 175.146 150.574 124.867 1.00 15.57  ? 4270 GLU A C     1 
ATOM   20823 O  O     . GLU A 1 4270 ? 175.223 150.061 123.746 1.00 19.74  ? 4270 GLU A O     1 
ATOM   20824 C  CB    . GLU A 1 4270 ? 175.395 153.055 124.637 1.00 18.98  ? 4270 GLU A CB    1 
ATOM   20825 C  CG    . GLU A 1 4270 ? 174.681 154.310 124.160 1.00 24.13  ? 4270 GLU A CG    1 
ATOM   20826 C  CD    . GLU A 1 4270 ? 174.138 154.174 122.749 1.00 34.19  ? 4270 GLU A CD    1 
ATOM   20827 O  OE1   . GLU A 1 4270 ? 174.484 153.186 122.066 1.00 30.38  ? 4270 GLU A OE1   1 
ATOM   20828 O  OE2   . GLU A 1 4270 ? 173.362 155.055 122.322 1.00 36.29  ? 4270 GLU A OE2   1 
ATOM   20829 N  N     . ARG A 1 4271 ? 175.660 149.993 125.951 1.00 18.86  ? 4271 ARG A N     1 
ATOM   20830 C  CA    . ARG A 1 4271 ? 176.293 148.683 125.850 1.00 21.86  ? 4271 ARG A CA    1 
ATOM   20831 C  C     . ARG A 1 4271 ? 175.257 147.570 125.751 1.00 21.46  ? 4271 ARG A C     1 
ATOM   20832 O  O     . ARG A 1 4271 ? 175.518 146.527 125.142 1.00 22.98  ? 4271 ARG A O     1 
ATOM   20833 C  CB    . ARG A 1 4271 ? 177.210 148.449 127.049 1.00 20.72  ? 4271 ARG A CB    1 
ATOM   20834 C  CG    . ARG A 1 4271 ? 178.515 147.752 126.708 1.00 27.61  ? 4271 ARG A CG    1 
ATOM   20835 C  CD    . ARG A 1 4271 ? 179.332 147.479 127.961 1.00 38.65  ? 4271 ARG A CD    1 
ATOM   20836 N  NE    . ARG A 1 4271 ? 178.543 146.818 128.995 1.00 36.27  ? 4271 ARG A NE    1 
ATOM   20837 C  CZ    . ARG A 1 4271 ? 178.220 145.532 128.986 1.00 39.70  ? 4271 ARG A CZ    1 
ATOM   20838 N  NH1   . ARG A 1 4271 ? 178.605 144.728 128.008 1.00 39.08  ? 4271 ARG A NH1   1 
ATOM   20839 N  NH2   . ARG A 1 4271 ? 177.491 145.040 129.984 1.00 35.80  ? 4271 ARG A NH2   1 
ATOM   20840 N  N     . LEU A 1 4272 ? 174.077 147.773 126.335 1.00 18.34  ? 4272 LEU A N     1 
ATOM   20841 C  CA    . LEU A 1 4272 ? 173.111 146.692 126.485 1.00 19.78  ? 4272 LEU A CA    1 
ATOM   20842 C  C     . LEU A 1 4272 ? 171.946 146.797 125.506 1.00 20.31  ? 4272 LEU A C     1 
ATOM   20843 O  O     . LEU A 1 4272 ? 171.524 145.789 124.932 1.00 26.45  ? 4272 LEU A O     1 
ATOM   20844 C  CB    . LEU A 1 4272 ? 172.580 146.667 127.922 1.00 17.09  ? 4272 LEU A CB    1 
ATOM   20845 C  CG    . LEU A 1 4272 ? 173.510 146.074 128.981 1.00 17.52  ? 4272 LEU A CG    1 
ATOM   20846 C  CD1   . LEU A 1 4272 ? 172.904 146.221 130.368 1.00 14.09  ? 4272 LEU A CD1   1 
ATOM   20847 C  CD2   . LEU A 1 4272 ? 173.814 144.621 128.672 1.00 23.20  ? 4272 LEU A CD2   1 
ATOM   20848 N  N     . PHE A 1 4273 ? 171.387 148.000 125.356 1.00 18.63  ? 4273 PHE A N     1 
ATOM   20849 C  CA    . PHE A 1 4273 ? 170.171 148.152 124.509 1.00 16.87  ? 4273 PHE A CA    1 
ATOM   20850 C  C     . PHE A 1 4273 ? 170.580 148.406 123.063 1.00 22.89  ? 4273 PHE A C     1 
ATOM   20851 O  O     . PHE A 1 4273 ? 170.529 149.568 122.608 1.00 29.27  ? 4273 PHE A O     1 
ATOM   20852 C  CB    . PHE A 1 4273 ? 169.307 149.243 125.147 1.00 16.83  ? 4273 PHE A CB    1 
ATOM   20853 C  CG    . PHE A 1 4273 ? 168.949 148.923 126.592 1.00 18.11  ? 4273 PHE A CG    1 
ATOM   20854 C  CD1   . PHE A 1 4273 ? 169.783 149.307 127.636 1.00 17.17  ? 4273 PHE A CD1   1 
ATOM   20855 C  CD2   . PHE A 1 4273 ? 167.791 148.219 126.902 1.00 14.11  ? 4273 PHE A CD2   1 
ATOM   20856 C  CE1   . PHE A 1 4273 ? 169.462 149.003 128.950 1.00 14.80  ? 4273 PHE A CE1   1 
ATOM   20857 C  CE2   . PHE A 1 4273 ? 167.474 147.920 128.217 1.00 13.51  ? 4273 PHE A CE2   1 
ATOM   20858 C  CZ    . PHE A 1 4273 ? 168.308 148.313 129.238 1.00 14.98  ? 4273 PHE A CZ    1 
ATOM   20859 N  N     . THR A 1 4274 ? 170.966 147.341 122.355 1.00 26.77  ? 4274 THR A N     1 
ATOM   20860 C  CA    . THR A 1 4274 ? 171.371 147.463 120.938 1.00 25.01  ? 4274 THR A CA    1 
ATOM   20861 C  C     . THR A 1 4274 ? 170.847 146.263 120.183 1.00 25.77  ? 4274 THR A C     1 
ATOM   20862 O  O     . THR A 1 4274 ? 170.442 145.283 120.843 1.00 26.06  ? 4274 THR A O     1 
ATOM   20863 C  CB    . THR A 1 4274 ? 172.892 147.552 120.849 1.00 28.50  ? 4274 THR A CB    1 
ATOM   20864 O  OG1   . THR A 1 4274 ? 173.367 146.340 121.426 1.00 33.62  ? 4274 THR A OG1   1 
ATOM   20865 C  CG2   . THR A 1 4274 ? 173.455 148.742 121.605 1.00 23.19  ? 4274 THR A CG2   1 
ATOM   20866 N  N     . THR A 1 4275 ? 170.853 146.323 118.849 1.00 29.80  ? 4275 THR A N     1 
ATOM   20867 C  CA    . THR A 1 4275 ? 170.427 145.165 118.034 1.00 33.99  ? 4275 THR A CA    1 
ATOM   20868 C  C     . THR A 1 4275 ? 171.389 144.020 118.280 1.00 37.07  ? 4275 THR A C     1 
ATOM   20869 O  O     . THR A 1 4275 ? 170.962 142.852 118.157 1.00 40.36  ? 4275 THR A O     1 
ATOM   20870 C  CB    . THR A 1 4275 ? 170.379 145.572 116.563 1.00 35.09  ? 4275 THR A CB    1 
ATOM   20871 O  OG1   . THR A 1 4275 ? 169.367 146.571 116.488 1.00 37.03  ? 4275 THR A OG1   1 
ATOM   20872 C  CG2   . THR A 1 4275 ? 170.025 144.417 115.644 1.00 40.65  ? 4275 THR A CG2   1 
ATOM   20873 N  N     . ARG A 1 4276 ? 172.639 144.334 118.633 1.00 33.52  ? 4276 ARG A N     1 
ATOM   20874 C  CA    . ARG A 1 4276 ? 173.670 143.290 118.874 1.00 37.45  ? 4276 ARG A CA    1 
ATOM   20875 C  C     . ARG A 1 4276 ? 173.245 142.401 120.052 1.00 34.30  ? 4276 ARG A C     1 
ATOM   20876 O  O     . ARG A 1 4276 ? 173.726 141.251 120.130 1.00 39.68  ? 4276 ARG A O     1 
ATOM   20877 C  CB    . ARG A 1 4276 ? 175.029 143.942 119.151 1.00 38.14  ? 4276 ARG A CB    1 
ATOM   20878 C  CG    . ARG A 1 4276 ? 175.547 144.779 117.991 1.00 39.40  ? 4276 ARG A CG    1 
ATOM   20879 C  CD    . ARG A 1 4276 ? 175.556 143.979 116.699 1.00 48.59  ? 4276 ARG A CD    1 
ATOM   20880 N  NE    . ARG A 1 4276 ? 176.218 144.685 115.597 1.00 50.61  ? 4276 ARG A NE    1 
ATOM   20881 C  CZ    . ARG A 1 4276 ? 177.494 145.048 115.586 1.00 58.13  ? 4276 ARG A CZ    1 
ATOM   20882 N  NH1   . ARG A 1 4276 ? 178.315 144.615 116.526 1.00 61.98  ? 4276 ARG A NH1   1 
ATOM   20883 N  NH2   . ARG A 1 4276 ? 177.948 145.836 114.628 1.00 55.04  ? 4276 ARG A NH2   1 
ATOM   20884 N  N     . SER A 1 4277 ? 172.386 142.917 120.934 1.00 33.65  ? 4277 SER A N     1 
ATOM   20885 C  CA    . SER A 1 4277 ? 171.909 142.130 122.101 1.00 32.58  ? 4277 SER A CA    1 
ATOM   20886 C  C     . SER A 1 4277 ? 171.141 140.899 121.605 1.00 33.52  ? 4277 SER A C     1 
ATOM   20887 O  O     . SER A 1 4277 ? 170.983 139.942 122.394 1.00 36.97  ? 4277 SER A O     1 
ATOM   20888 C  CB    . SER A 1 4277 ? 171.058 142.977 123.000 1.00 30.04  ? 4277 SER A CB    1 
ATOM   20889 O  OG    . SER A 1 4277 ? 171.621 144.275 123.129 1.00 33.40  ? 4277 SER A OG    1 
ATOM   20890 N  N     . PHE A 1 4278 ? 170.682 140.928 120.351 1.00 36.29  ? 4278 PHE A N     1 
ATOM   20891 C  CA    . PHE A 1 4278 ? 169.923 139.787 119.773 1.00 37.00  ? 4278 PHE A CA    1 
ATOM   20892 C  C     . PHE A 1 4278 ? 170.889 138.859 119.037 1.00 42.26  ? 4278 PHE A C     1 
ATOM   20893 O  O     . PHE A 1 4278 ? 170.425 137.969 118.292 1.00 42.40  ? 4278 PHE A O     1 
ATOM   20894 C  CB    . PHE A 1 4278 ? 168.818 140.340 118.868 1.00 32.65  ? 4278 PHE A CB    1 
ATOM   20895 C  CG    . PHE A 1 4278 ? 167.600 140.864 119.615 1.00 34.04  ? 4278 PHE A CG    1 
ATOM   20896 C  CD1   . PHE A 1 4278 ? 167.566 142.165 120.103 1.00 33.47  ? 4278 PHE A CD1   1 
ATOM   20897 C  CD2   . PHE A 1 4278 ? 166.486 140.057 119.816 1.00 33.59  ? 4278 PHE A CD2   1 
ATOM   20898 C  CE1   . PHE A 1 4278 ? 166.454 142.636 120.783 1.00 30.58  ? 4278 PHE A CE1   1 
ATOM   20899 C  CE2   . PHE A 1 4278 ? 165.377 140.535 120.495 1.00 34.48  ? 4278 PHE A CE2   1 
ATOM   20900 C  CZ    . PHE A 1 4278 ? 165.363 141.823 120.976 1.00 32.45  ? 4278 PHE A CZ    1 
ATOM   20901 N  N     . ASP A 1 4279 ? 172.196 139.059 119.235 1.00 47.54  ? 4279 ASP A N     1 
ATOM   20902 C  CA    . ASP A 1 4279 ? 173.219 138.191 118.586 1.00 47.99  ? 4279 ASP A CA    1 
ATOM   20903 C  C     . ASP A 1 4279 ? 173.479 136.964 119.464 1.00 54.16  ? 4279 ASP A C     1 
ATOM   20904 O  O     . ASP A 1 4279 ? 173.215 137.043 120.684 1.00 51.75  ? 4279 ASP A O     1 
ATOM   20905 C  CB    . ASP A 1 4279 ? 174.497 138.959 118.289 1.00 51.24  ? 4279 ASP A CB    1 
ATOM   20906 C  CG    . ASP A 1 4279 ? 174.330 140.193 117.415 1.00 50.23  ? 4279 ASP A CG    1 
ATOM   20907 O  OD1   . ASP A 1 4279 ? 173.180 140.481 117.021 1.00 48.37  ? 4279 ASP A OD1   1 
ATOM   20908 O  OD2   . ASP A 1 4279 ? 175.351 140.856 117.138 1.00 52.62  ? 4279 ASP A OD2   1 
ATOM   20909 N  N     . SER A 1 4280 ? 173.980 135.877 118.870 1.00 61.52  ? 4280 SER A N     1 
ATOM   20910 C  CA    . SER A 1 4280 ? 174.251 134.658 119.618 1.00 61.35  ? 4280 SER A CA    1 
ATOM   20911 C  C     . SER A 1 4280 ? 175.567 134.717 120.380 1.00 59.67  ? 4280 SER A C     1 
ATOM   20912 O  O     . SER A 1 4280 ? 175.832 133.827 121.195 1.00 63.45  ? 4280 SER A O     1 
ATOM   20913 C  CB    . SER A 1 4280 ? 174.255 133.454 118.675 1.00 58.50  ? 4280 SER A CB    1 
ATOM   20914 O  OG    . SER A 1 4280 ? 174.761 133.811 117.400 1.00 59.44  ? 4280 SER A OG    1 
ATOM   20915 N  N     . GLU A 1 4281 ? 176.392 135.737 120.137 1.00 55.58  ? 4281 GLU A N     1 
ATOM   20916 C  CA    . GLU A 1 4281 ? 177.691 135.868 120.785 1.00 56.84  ? 4281 GLU A CA    1 
ATOM   20917 C  C     . GLU A 1 4281 ? 177.800 137.124 121.641 1.00 55.35  ? 4281 GLU A C     1 
ATOM   20918 O  O     . GLU A 1 4281 ? 178.909 137.488 122.048 1.00 53.63  ? 4281 GLU A O     1 
ATOM   20919 C  CB    . GLU A 1 4281 ? 178.804 135.835 119.729 1.00 65.94  ? 4281 GLU A CB    1 
ATOM   20920 C  CG    . GLU A 1 4281 ? 178.726 136.940 118.675 1.00 72.78  ? 4281 GLU A CG    1 
ATOM   20921 C  CD    . GLU A 1 4281 ? 179.483 138.199 119.061 1.00 73.07  ? 4281 GLU A CD    1 
ATOM   20922 O  OE1   . GLU A 1 4281 ? 180.400 138.113 119.904 1.00 69.35  ? 4281 GLU A OE1   1 
ATOM   20923 O  OE2   . GLU A 1 4281 ? 179.160 139.277 118.519 1.00 69.75  ? 4281 GLU A OE2   1 
ATOM   20924 N  N     . PHE A 1 4282 ? 176.682 137.784 121.941 1.00 53.18  ? 4282 PHE A N     1 
ATOM   20925 C  CA    . PHE A 1 4282 ? 176.722 139.008 122.731 1.00 44.00  ? 4282 PHE A CA    1 
ATOM   20926 C  C     . PHE A 1 4282 ? 177.200 138.720 124.150 1.00 38.80  ? 4282 PHE A C     1 
ATOM   20927 O  O     . PHE A 1 4282 ? 176.887 137.678 124.731 1.00 41.07  ? 4282 PHE A O     1 
ATOM   20928 C  CB    . PHE A 1 4282 ? 175.340 139.660 122.764 1.00 38.54  ? 4282 PHE A CB    1 
ATOM   20929 C  CG    . PHE A 1 4282 ? 175.316 140.993 123.454 1.00 34.50  ? 4282 PHE A CG    1 
ATOM   20930 C  CD1   . PHE A 1 4282 ? 176.023 142.067 122.940 1.00 34.46  ? 4282 PHE A CD1   1 
ATOM   20931 C  CD2   . PHE A 1 4282 ? 174.596 141.169 124.623 1.00 32.44  ? 4282 PHE A CD2   1 
ATOM   20932 C  CE1   . PHE A 1 4282 ? 176.004 143.292 123.575 1.00 31.59  ? 4282 PHE A CE1   1 
ATOM   20933 C  CE2   . PHE A 1 4282 ? 174.574 142.391 125.262 1.00 31.02  ? 4282 PHE A CE2   1 
ATOM   20934 C  CZ    . PHE A 1 4282 ? 175.279 143.454 124.737 1.00 33.60  ? 4282 PHE A CZ    1 
ATOM   20935 N  N     . LYS A 1 4283 ? 177.967 139.656 124.705 1.00 36.22  ? 4283 LYS A N     1 
ATOM   20936 C  CA    . LYS A 1 4283 ? 178.558 139.520 126.033 1.00 37.43  ? 4283 LYS A CA    1 
ATOM   20937 C  C     . LYS A 1 4283 ? 177.882 140.507 126.977 1.00 33.70  ? 4283 LYS A C     1 
ATOM   20938 O  O     . LYS A 1 4283 ? 177.960 141.723 126.772 1.00 35.14  ? 4283 LYS A O     1 
ATOM   20939 C  CB    . LYS A 1 4283 ? 180.064 139.765 125.986 1.00 41.99  ? 4283 LYS A CB    1 
ATOM   20940 C  CG    . LYS A 1 4283 ? 180.781 139.099 124.823 1.00 48.08  ? 4283 LYS A CG    1 
ATOM   20941 C  CD    . LYS A 1 4283 ? 180.570 137.596 124.820 1.00 51.16  ? 4283 LYS A CD    1 
ATOM   20942 C  CE    . LYS A 1 4283 ? 181.627 136.899 123.980 1.00 57.38  ? 4283 LYS A CE    1 
ATOM   20943 N  NZ    . LYS A 1 4283 ? 182.935 137.609 124.036 1.00 57.11  ? 4283 LYS A NZ    1 
ATOM   20944 N  N     . LEU A 1 4284 ? 177.220 139.983 128.011 1.00 27.97  ? 4284 LEU A N     1 
ATOM   20945 C  CA    . LEU A 1 4284 ? 176.677 140.853 129.050 1.00 24.63  ? 4284 LEU A CA    1 
ATOM   20946 C  C     . LEU A 1 4284 ? 177.791 141.443 129.905 1.00 32.47  ? 4284 LEU A C     1 
ATOM   20947 O  O     . LEU A 1 4284 ? 177.790 142.644 130.198 1.00 39.49  ? 4284 LEU A O     1 
ATOM   20948 C  CB    . LEU A 1 4284 ? 175.686 140.080 129.920 1.00 21.00  ? 4284 LEU A CB    1 
ATOM   20949 C  CG    . LEU A 1 4284 ? 174.345 139.722 129.279 1.00 20.62  ? 4284 LEU A CG    1 
ATOM   20950 C  CD1   . LEU A 1 4284 ? 173.530 138.835 130.204 1.00 19.79  ? 4284 LEU A CD1   1 
ATOM   20951 C  CD2   . LEU A 1 4284 ? 173.572 140.978 128.927 1.00 22.70  ? 4284 LEU A CD2   1 
ATOM   20952 N  N     . ALA A 1 4285 ? 178.746 140.612 130.316 1.00 33.94  ? 4285 ALA A N     1 
ATOM   20953 C  CA    . ALA A 1 4285 ? 179.931 141.057 131.030 1.00 32.27  ? 4285 ALA A CA    1 
ATOM   20954 C  C     . ALA A 1 4285 ? 181.148 140.399 130.398 1.00 43.33  ? 4285 ALA A C     1 
ATOM   20955 O  O     . ALA A 1 4285 ? 181.067 139.281 129.884 1.00 41.28  ? 4285 ALA A O     1 
ATOM   20956 C  CB    . ALA A 1 4285 ? 179.857 140.722 132.526 1.00 25.66  ? 4285 ALA A CB    1 
ATOM   20957 N  N     . CYS A 1 4286 ? 182.277 141.102 130.435 1.00 50.69  ? 4286 CYS A N     1 
ATOM   20958 C  CA    . CYS A 1 4286 ? 183.495 140.661 129.770 1.00 53.74  ? 4286 CYS A CA    1 
ATOM   20959 C  C     . CYS A 1 4286 ? 184.606 140.480 130.792 1.00 59.49  ? 4286 CYS A C     1 
ATOM   20960 O  O     . CYS A 1 4286 ? 184.874 141.386 131.589 1.00 62.18  ? 4286 CYS A O     1 
ATOM   20961 C  CB    . CYS A 1 4286 ? 183.925 141.662 128.695 1.00 59.77  ? 4286 CYS A CB    1 
ATOM   20962 S  SG    . CYS A 1 4286 ? 183.039 141.499 127.129 1.00 74.29  ? 4286 CYS A SG    1 
ATOM   20963 N  N     . LYS A 1 4287 ? 185.249 139.311 130.759 1.00 62.79  ? 4287 LYS A N     1 
ATOM   20964 C  CA    . LYS A 1 4287 ? 186.405 139.003 131.602 1.00 65.92  ? 4287 LYS A CA    1 
ATOM   20965 C  C     . LYS A 1 4287 ? 186.073 139.193 133.084 1.00 59.28  ? 4287 LYS A C     1 
ATOM   20966 O  O     . LYS A 1 4287 ? 186.649 140.032 133.780 1.00 61.96  ? 4287 LYS A O     1 
ATOM   20967 C  CB    . LYS A 1 4287 ? 187.617 139.846 131.191 1.00 68.14  ? 4287 LYS A CB    1 
ATOM   20968 C  CG    . LYS A 1 4287 ? 188.564 139.152 130.223 1.00 69.45  ? 4287 LYS A CG    1 
ATOM   20969 C  CD    . LYS A 1 4287 ? 187.906 138.917 128.871 1.00 67.10  ? 4287 LYS A CD    1 
ATOM   20970 C  CE    . LYS A 1 4287 ? 187.608 140.229 128.162 1.00 69.91  ? 4287 LYS A CE    1 
ATOM   20971 N  NZ    . LYS A 1 4287 ? 186.918 140.012 126.860 1.00 66.40  ? 4287 LYS A NZ    1 
ATOM   20972 N  N     . VAL A 1 4288 ? 185.115 138.393 133.556 1.00 59.57  ? 4288 VAL A N     1 
ATOM   20973 C  CA    . VAL A 1 4288 ? 184.704 138.475 134.953 1.00 56.19  ? 4288 VAL A CA    1 
ATOM   20974 C  C     . VAL A 1 4288 ? 185.813 137.974 135.872 1.00 60.70  ? 4288 VAL A C     1 
ATOM   20975 O  O     . VAL A 1 4288 ? 186.029 138.519 136.960 1.00 59.52  ? 4288 VAL A O     1 
ATOM   20976 C  CB    . VAL A 1 4288 ? 183.387 137.708 135.171 1.00 44.74  ? 4288 VAL A CB    1 
ATOM   20977 C  CG1   . VAL A 1 4288 ? 182.227 138.470 134.551 1.00 39.66  ? 4288 VAL A CG1   1 
ATOM   20978 C  CG2   . VAL A 1 4288 ? 183.479 136.312 134.582 1.00 51.88  ? 4288 VAL A CG2   1 
ATOM   20979 N  N     . ASP A 1 4289 ? 186.532 136.931 135.456 1.00 62.53  ? 4289 ASP A N     1 
ATOM   20980 C  CA    . ASP A 1 4289 ? 187.659 136.415 136.224 1.00 71.91  ? 4289 ASP A CA    1 
ATOM   20981 C  C     . ASP A 1 4289 ? 188.900 136.284 135.351 1.00 77.82  ? 4289 ASP A C     1 
ATOM   20982 O  O     . ASP A 1 4289 ? 189.762 135.439 135.607 1.00 79.56  ? 4289 ASP A O     1 
ATOM   20983 C  CB    . ASP A 1 4289 ? 187.313 135.078 136.879 1.00 73.84  ? 4289 ASP A CB    1 
ATOM   20984 C  CG    . ASP A 1 4289 ? 186.673 134.101 135.914 1.00 75.78  ? 4289 ASP A CG    1 
ATOM   20985 O  OD1   . ASP A 1 4289 ? 187.278 133.819 134.858 1.00 75.99  ? 4289 ASP A OD1   1 
ATOM   20986 O  OD2   . ASP A 1 4289 ? 185.566 133.609 136.218 1.00 74.91  ? 4289 ASP A OD2   1 
ATOM   20987 N  N     . GLY A 1 4290 ? 189.002 137.114 134.313 1.00 75.35  ? 4290 GLY A N     1 
ATOM   20988 C  CA    . GLY A 1 4290 ? 190.147 137.141 133.436 1.00 80.97  ? 4290 GLY A CA    1 
ATOM   20989 C  C     . GLY A 1 4290 ? 190.039 136.257 132.209 1.00 86.31  ? 4290 GLY A C     1 
ATOM   20990 O  O     . GLY A 1 4290 ? 190.636 136.576 131.176 1.00 86.40  ? 4290 GLY A O     1 
ATOM   20991 N  N     . HIS A 1 4291 ? 189.295 135.154 132.293 1.00 86.64  ? 4291 HIS A N     1 
ATOM   20992 C  CA    . HIS A 1 4291 ? 189.191 134.208 131.189 1.00 85.91  ? 4291 HIS A CA    1 
ATOM   20993 C  C     . HIS A 1 4291 ? 187.786 134.136 130.605 1.00 84.90  ? 4291 HIS A C     1 
ATOM   20994 O  O     . HIS A 1 4291 ? 187.607 134.340 129.401 1.00 82.81  ? 4291 HIS A O     1 
ATOM   20995 C  CB    . HIS A 1 4291 ? 189.649 132.816 131.649 1.00 82.57  ? 4291 HIS A CB    1 
ATOM   20996 C  CG    . HIS A 1 4291 ? 190.964 132.816 132.363 1.00 91.55  ? 4291 HIS A CG    1 
ATOM   20997 N  ND1   . HIS A 1 4291 ? 191.103 133.230 133.671 1.00 92.28  ? 4291 HIS A ND1   1 
ATOM   20998 C  CD2   . HIS A 1 4291 ? 192.202 132.452 131.951 1.00 94.93  ? 4291 HIS A CD2   1 
ATOM   20999 C  CE1   . HIS A 1 4291 ? 192.369 133.121 134.033 1.00 92.22  ? 4291 HIS A CE1   1 
ATOM   21000 N  NE2   . HIS A 1 4291 ? 193.057 132.652 133.008 1.00 94.98  ? 4291 HIS A NE2   1 
ATOM   21001 N  N     . LYS A 1 4292 ? 186.778 133.854 131.424 1.00 80.66  ? 4292 LYS A N     1 
ATOM   21002 C  CA    . LYS A 1 4292 ? 185.434 133.630 130.917 1.00 68.94  ? 4292 LYS A CA    1 
ATOM   21003 C  C     . LYS A 1 4292 ? 184.615 134.919 130.943 1.00 65.22  ? 4292 LYS A C     1 
ATOM   21004 O  O     . LYS A 1 4292 ? 184.977 135.911 131.580 1.00 62.19  ? 4292 LYS A O     1 
ATOM   21005 C  CB    . LYS A 1 4292 ? 184.733 132.534 131.721 1.00 67.77  ? 4292 LYS A CB    1 
ATOM   21006 C  CG    . LYS A 1 4292 ? 184.693 132.780 133.218 1.00 69.18  ? 4292 LYS A CG    1 
ATOM   21007 C  CD    . LYS A 1 4292 ? 183.495 132.094 133.855 1.00 73.16  ? 4292 LYS A CD    1 
ATOM   21008 C  CE    . LYS A 1 4292 ? 182.270 132.995 133.847 1.00 70.41  ? 4292 LYS A CE    1 
ATOM   21009 N  NZ    . LYS A 1 4292 ? 181.190 132.475 134.731 1.00 56.69  ? 4292 LYS A NZ    1 
ATOM   21010 N  N     . ASP A 1 4293 ? 183.489 134.891 130.232 1.00 62.94  ? 4293 ASP A N     1 
ATOM   21011 C  CA    . ASP A 1 4293 ? 182.585 136.028 130.156 1.00 56.31  ? 4293 ASP A CA    1 
ATOM   21012 C  C     . ASP A 1 4293 ? 181.145 135.535 130.212 1.00 46.84  ? 4293 ASP A C     1 
ATOM   21013 O  O     . ASP A 1 4293 ? 180.840 134.396 129.851 1.00 49.47  ? 4293 ASP A O     1 
ATOM   21014 C  CB    . ASP A 1 4293 ? 182.831 136.857 128.885 1.00 57.72  ? 4293 ASP A CB    1 
ATOM   21015 C  CG    . ASP A 1 4293 ? 183.013 135.998 127.647 1.00 62.08  ? 4293 ASP A CG    1 
ATOM   21016 O  OD1   . ASP A 1 4293 ? 183.816 136.385 126.772 1.00 66.42  ? 4293 ASP A OD1   1 
ATOM   21017 O  OD2   . ASP A 1 4293 ? 182.358 134.940 127.541 1.00 59.91  ? 4293 ASP A OD2   1 
ATOM   21018 N  N     . ILE A 1 4294 ? 180.261 136.412 130.678 1.00 38.75  ? 4294 ILE A N     1 
ATOM   21019 C  CA    . ILE A 1 4294 ? 178.846 136.082 130.821 1.00 34.65  ? 4294 ILE A CA    1 
ATOM   21020 C  C     . ILE A 1 4294 ? 178.177 136.181 129.455 1.00 36.06  ? 4294 ILE A C     1 
ATOM   21021 O  O     . ILE A 1 4294 ? 178.342 137.176 128.742 1.00 37.37  ? 4294 ILE A O     1 
ATOM   21022 C  CB    . ILE A 1 4294 ? 178.167 137.001 131.846 1.00 31.50  ? 4294 ILE A CB    1 
ATOM   21023 C  CG1   . ILE A 1 4294 ? 178.827 136.834 133.216 1.00 30.93  ? 4294 ILE A CG1   1 
ATOM   21024 C  CG2   . ILE A 1 4294 ? 176.681 136.700 131.933 1.00 27.09  ? 4294 ILE A CG2   1 
ATOM   21025 C  CD1   . ILE A 1 4294 ? 178.254 137.728 134.289 1.00 22.21  ? 4294 ILE A CD1   1 
ATOM   21026 N  N     . GLN A 1 4295 ? 177.420 135.150 129.091 1.00 35.99  ? 4295 GLN A N     1 
ATOM   21027 C  CA    . GLN A 1 4295 ? 176.873 135.023 127.748 1.00 35.28  ? 4295 GLN A CA    1 
ATOM   21028 C  C     . GLN A 1 4295 ? 175.415 135.465 127.681 1.00 35.48  ? 4295 GLN A C     1 
ATOM   21029 O  O     . GLN A 1 4295 ? 174.621 135.216 128.592 1.00 30.28  ? 4295 GLN A O     1 
ATOM   21030 C  CB    . GLN A 1 4295 ? 176.992 133.578 127.261 1.00 38.06  ? 4295 GLN A CB    1 
ATOM   21031 C  CG    . GLN A 1 4295 ? 178.248 133.291 126.460 1.00 38.13  ? 4295 GLN A CG    1 
ATOM   21032 C  CD    . GLN A 1 4295 ? 178.274 134.030 125.138 1.00 49.18  ? 4295 GLN A CD    1 
ATOM   21033 O  OE1   . GLN A 1 4295 ? 177.240 134.211 124.496 1.00 49.85  ? 4295 GLN A OE1   1 
ATOM   21034 N  NE2   . GLN A 1 4295 ? 179.458 134.458 124.722 1.00 49.96  ? 4295 GLN A NE2   1 
ATOM   21035 N  N     . MET A 1 4296 ? 175.078 136.123 126.581 1.00 35.30  ? 4296 MET A N     1 
ATOM   21036 C  CA    . MET A 1 4296 ? 173.689 136.443 126.274 1.00 31.72  ? 4296 MET A CA    1 
ATOM   21037 C  C     . MET A 1 4296 ? 172.945 135.145 125.980 1.00 36.76  ? 4296 MET A C     1 
ATOM   21038 O  O     . MET A 1 4296 ? 173.332 134.415 125.059 1.00 41.37  ? 4296 MET A O     1 
ATOM   21039 C  CB    . MET A 1 4296 ? 173.661 137.373 125.058 1.00 40.45  ? 4296 MET A CB    1 
ATOM   21040 C  CG    . MET A 1 4296 ? 172.476 138.333 124.846 1.00 36.74  ? 4296 MET A CG    1 
ATOM   21041 S  SD    . MET A 1 4296 ? 171.597 139.045 126.256 1.00 32.97  ? 4296 MET A SD    1 
ATOM   21042 C  CE    . MET A 1 4296 ? 170.086 138.087 126.236 1.00 31.92  ? 4296 MET A CE    1 
ATOM   21043 N  N     . PRO A 1 4297 ? 171.902 134.807 126.737 1.00 37.84  ? 4297 PRO A N     1 
ATOM   21044 C  CA    . PRO A 1 4297 ? 171.160 133.571 126.454 1.00 29.87  ? 4297 PRO A CA    1 
ATOM   21045 C  C     . PRO A 1 4297 ? 170.557 133.576 125.056 1.00 41.13  ? 4297 PRO A C     1 
ATOM   21046 O  O     . PRO A 1 4297 ? 170.120 134.611 124.547 1.00 43.62  ? 4297 PRO A O     1 
ATOM   21047 C  CB    . PRO A 1 4297 ? 170.076 133.546 127.539 1.00 27.69  ? 4297 PRO A CB    1 
ATOM   21048 C  CG    . PRO A 1 4297 ? 170.563 134.471 128.595 1.00 32.77  ? 4297 PRO A CG    1 
ATOM   21049 C  CD    . PRO A 1 4297 ? 171.386 135.508 127.924 1.00 34.92  ? 4297 PRO A CD    1 
ATOM   21050 N  N     . ASP A 1 4298 ? 170.542 132.399 124.436 1.00 45.56  ? 4298 ASP A N     1 
ATOM   21051 C  CA    . ASP A 1 4298 ? 170.077 132.231 123.067 1.00 43.78  ? 4298 ASP A CA    1 
ATOM   21052 C  C     . ASP A 1 4298 ? 168.576 131.992 122.967 1.00 51.02  ? 4298 ASP A C     1 
ATOM   21053 O  O     . ASP A 1 4298 ? 168.047 131.932 121.851 1.00 57.88  ? 4298 ASP A O     1 
ATOM   21054 C  CB    . ASP A 1 4298 ? 170.829 131.073 122.398 1.00 51.12  ? 4298 ASP A CB    1 
ATOM   21055 C  CG    . ASP A 1 4298 ? 172.225 131.467 121.945 1.00 66.21  ? 4298 ASP A CG    1 
ATOM   21056 O  OD1   . ASP A 1 4298 ? 172.379 132.580 121.400 1.00 65.44  ? 4298 ASP A OD1   1 
ATOM   21057 O  OD2   . ASP A 1 4298 ? 173.167 130.668 122.131 1.00 64.04  ? 4298 ASP A OD2   1 
ATOM   21058 N  N     . GLY A 1 4299 ? 167.881 131.861 124.093 1.00 47.36  ? 4299 GLY A N     1 
ATOM   21059 C  CA    . GLY A 1 4299 ? 166.456 131.612 124.064 1.00 46.56  ? 4299 GLY A CA    1 
ATOM   21060 C  C     . GLY A 1 4299 ? 165.665 132.824 123.611 1.00 47.59  ? 4299 GLY A C     1 
ATOM   21061 O  O     . GLY A 1 4299 ? 166.141 133.959 123.593 1.00 42.90  ? 4299 GLY A O     1 
ATOM   21062 N  N     . ILE A 1 4300 ? 164.413 132.566 123.235 1.00 47.75  ? 4300 ILE A N     1 
ATOM   21063 C  CA    . ILE A 1 4300 ? 163.494 133.603 122.792 1.00 45.61  ? 4300 ILE A CA    1 
ATOM   21064 C  C     . ILE A 1 4300 ? 162.233 133.661 123.650 1.00 49.37  ? 4300 ILE A C     1 
ATOM   21065 O  O     . ILE A 1 4300 ? 161.392 134.539 123.453 1.00 54.75  ? 4300 ILE A O     1 
ATOM   21066 C  CB    . ILE A 1 4300 ? 163.178 133.447 121.285 1.00 45.43  ? 4300 ILE A CB    1 
ATOM   21067 C  CG1   . ILE A 1 4300 ? 162.230 132.277 120.972 1.00 49.35  ? 4300 ILE A CG1   1 
ATOM   21068 C  CG2   . ILE A 1 4300 ? 164.464 133.307 120.476 1.00 52.58  ? 4300 ILE A CG2   1 
ATOM   21069 C  CD1   . ILE A 1 4300 ? 160.746 132.540 121.128 1.00 50.45  ? 4300 ILE A CD1   1 
ATOM   21070 N  N     . ARG A 1 4301 ? 162.102 132.761 124.624 1.00 48.16  ? 4301 ARG A N     1 
ATOM   21071 C  CA    . ARG A 1 4301 ? 160.955 132.730 125.520 1.00 40.20  ? 4301 ARG A CA    1 
ATOM   21072 C  C     . ARG A 1 4301 ? 161.395 133.088 126.934 1.00 41.84  ? 4301 ARG A C     1 
ATOM   21073 O  O     . ARG A 1 4301 ? 162.561 132.930 127.303 1.00 46.69  ? 4301 ARG A O     1 
ATOM   21074 C  CB    . ARG A 1 4301 ? 160.274 131.355 125.520 1.00 50.35  ? 4301 ARG A CB    1 
ATOM   21075 C  CG    . ARG A 1 4301 ? 159.838 130.884 124.145 1.00 52.68  ? 4301 ARG A CG    1 
ATOM   21076 C  CD    . ARG A 1 4301 ? 159.848 129.365 124.049 1.00 52.63  ? 4301 ARG A CD    1 
ATOM   21077 N  NE    . ARG A 1 4301 ? 159.330 128.726 125.255 1.00 59.64  ? 4301 ARG A NE    1 
ATOM   21078 C  CZ    . ARG A 1 4301 ? 158.054 128.723 125.617 1.00 60.61  ? 4301 ARG A CZ    1 
ATOM   21079 N  NH1   . ARG A 1 4301 ? 157.124 129.309 124.880 1.00 57.15  ? 4301 ARG A NH1   1 
ATOM   21080 N  NH2   . ARG A 1 4301 ? 157.700 128.115 126.746 1.00 58.03  ? 4301 ARG A NH2   1 
ATOM   21081 N  N     . ARG A 1 4302 ? 160.432 133.573 127.723 1.00 40.42  ? 4302 ARG A N     1 
ATOM   21082 C  CA    . ARG A 1 4302 ? 160.724 133.998 129.089 1.00 37.85  ? 4302 ARG A CA    1 
ATOM   21083 C  C     . ARG A 1 4302 ? 161.245 132.843 129.934 1.00 42.46  ? 4302 ARG A C     1 
ATOM   21084 O  O     . ARG A 1 4302 ? 162.142 133.028 130.766 1.00 43.55  ? 4302 ARG A O     1 
ATOM   21085 C  CB    . ARG A 1 4302 ? 159.472 134.602 129.728 1.00 41.62  ? 4302 ARG A CB    1 
ATOM   21086 C  CG    . ARG A 1 4302 ? 159.521 134.688 131.245 1.00 38.34  ? 4302 ARG A CG    1 
ATOM   21087 C  CD    . ARG A 1 4302 ? 158.135 134.855 131.841 1.00 43.46  ? 4302 ARG A CD    1 
ATOM   21088 N  NE    . ARG A 1 4302 ? 158.181 134.936 133.295 1.00 45.92  ? 4302 ARG A NE    1 
ATOM   21089 C  CZ    . ARG A 1 4302 ? 158.294 133.886 134.097 1.00 46.97  ? 4302 ARG A CZ    1 
ATOM   21090 N  NH1   . ARG A 1 4302 ? 158.375 132.656 133.618 1.00 51.38  ? 4302 ARG A NH1   1 
ATOM   21091 N  NH2   . ARG A 1 4302 ? 158.326 134.076 135.413 1.00 40.72  ? 4302 ARG A NH2   1 
ATOM   21092 N  N     . GLU A 1 4303 ? 160.697 131.642 129.733 1.00 50.30  ? 4303 GLU A N     1 
ATOM   21093 C  CA    . GLU A 1 4303 ? 161.095 130.497 130.547 1.00 43.55  ? 4303 GLU A CA    1 
ATOM   21094 C  C     . GLU A 1 4303 ? 162.579 130.192 130.385 1.00 44.36  ? 4303 GLU A C     1 
ATOM   21095 O  O     . GLU A 1 4303 ? 163.264 129.869 131.363 1.00 42.71  ? 4303 GLU A O     1 
ATOM   21096 C  CB    . GLU A 1 4303 ? 160.251 129.274 130.185 1.00 45.15  ? 4303 GLU A CB    1 
ATOM   21097 C  CG    . GLU A 1 4303 ? 158.855 129.244 130.809 1.00 55.92  ? 4303 GLU A CG    1 
ATOM   21098 C  CD    . GLU A 1 4303 ? 158.057 130.511 130.558 1.00 63.77  ? 4303 GLU A CD    1 
ATOM   21099 O  OE1   . GLU A 1 4303 ? 158.082 131.414 131.421 1.00 60.14  ? 4303 GLU A OE1   1 
ATOM   21100 O  OE2   . GLU A 1 4303 ? 157.399 130.599 129.499 1.00 58.73  ? 4303 GLU A OE2   1 
ATOM   21101 N  N     . GLU A 1 4304 ? 163.093 130.284 129.156 1.00 49.95  ? 4304 GLU A N     1 
ATOM   21102 C  CA    . GLU A 1 4304 ? 164.515 130.045 128.930 1.00 43.47  ? 4304 GLU A CA    1 
ATOM   21103 C  C     . GLU A 1 4304 ? 165.375 131.080 129.646 1.00 43.10  ? 4304 GLU A C     1 
ATOM   21104 O  O     . GLU A 1 4304 ? 166.427 130.744 130.203 1.00 43.94  ? 4304 GLU A O     1 
ATOM   21105 C  CB    . GLU A 1 4304 ? 164.816 130.041 127.432 1.00 40.28  ? 4304 GLU A CB    1 
ATOM   21106 C  CG    . GLU A 1 4304 ? 163.846 129.214 126.607 1.00 47.68  ? 4304 GLU A CG    1 
ATOM   21107 C  CD    . GLU A 1 4304 ? 164.297 129.054 125.169 1.00 58.22  ? 4304 GLU A CD    1 
ATOM   21108 O  OE1   . GLU A 1 4304 ? 165.361 128.440 124.943 1.00 54.87  ? 4304 GLU A OE1   1 
ATOM   21109 O  OE2   . GLU A 1 4304 ? 163.588 129.543 124.264 1.00 57.62  ? 4304 GLU A OE2   1 
ATOM   21110 N  N     . PHE A 1 4305 ? 164.952 132.347 129.632 1.00 40.61  ? 4305 PHE A N     1 
ATOM   21111 C  CA    . PHE A 1 4305 ? 165.700 133.382 130.340 1.00 33.63  ? 4305 PHE A CA    1 
ATOM   21112 C  C     . PHE A 1 4305 ? 165.683 133.148 131.845 1.00 36.46  ? 4305 PHE A C     1 
ATOM   21113 O  O     . PHE A 1 4305 ? 166.705 133.331 132.518 1.00 40.52  ? 4305 PHE A O     1 
ATOM   21114 C  CB    . PHE A 1 4305 ? 165.139 134.764 130.007 1.00 29.83  ? 4305 PHE A CB    1 
ATOM   21115 C  CG    . PHE A 1 4305 ? 165.363 135.183 128.584 1.00 31.90  ? 4305 PHE A CG    1 
ATOM   21116 C  CD1   . PHE A 1 4305 ? 166.645 135.360 128.094 1.00 33.79  ? 4305 PHE A CD1   1 
ATOM   21117 C  CD2   . PHE A 1 4305 ? 164.291 135.409 127.738 1.00 28.27  ? 4305 PHE A CD2   1 
ATOM   21118 C  CE1   . PHE A 1 4305 ? 166.855 135.748 126.784 1.00 31.56  ? 4305 PHE A CE1   1 
ATOM   21119 C  CE2   . PHE A 1 4305 ? 164.493 135.796 126.428 1.00 28.22  ? 4305 PHE A CE2   1 
ATOM   21120 C  CZ    . PHE A 1 4305 ? 165.777 135.967 125.952 1.00 30.29  ? 4305 PHE A CZ    1 
ATOM   21121 N  N     . VAL A 1 4306 ? 164.533 132.749 132.391 1.00 35.28  ? 4306 VAL A N     1 
ATOM   21122 C  CA    . VAL A 1 4306 ? 164.440 132.480 133.824 1.00 32.58  ? 4306 VAL A CA    1 
ATOM   21123 C  C     . VAL A 1 4306 ? 165.346 131.318 134.207 1.00 35.55  ? 4306 VAL A C     1 
ATOM   21124 O  O     . VAL A 1 4306 ? 166.024 131.354 135.242 1.00 37.00  ? 4306 VAL A O     1 
ATOM   21125 C  CB    . VAL A 1 4306 ? 162.975 132.217 134.223 1.00 34.28  ? 4306 VAL A CB    1 
ATOM   21126 C  CG1   . VAL A 1 4306 ? 162.893 131.711 135.654 1.00 30.60  ? 4306 VAL A CG1   1 
ATOM   21127 C  CG2   . VAL A 1 4306 ? 162.149 133.482 134.057 1.00 37.18  ? 4306 VAL A CG2   1 
ATOM   21128 N  N     . GLN A 1 4307 ? 165.375 130.269 133.380 1.00 37.83  ? 4307 GLN A N     1 
ATOM   21129 C  CA    . GLN A 1 4307 ? 166.270 129.147 133.641 1.00 38.75  ? 4307 GLN A CA    1 
ATOM   21130 C  C     . GLN A 1 4307 ? 167.727 129.590 133.623 1.00 36.96  ? 4307 GLN A C     1 
ATOM   21131 O  O     . GLN A 1 4307 ? 168.522 129.170 134.472 1.00 42.64  ? 4307 GLN A O     1 
ATOM   21132 C  CB    . GLN A 1 4307 ? 166.035 128.037 132.617 1.00 42.63  ? 4307 GLN A CB    1 
ATOM   21133 C  CG    . GLN A 1 4307 ? 164.696 127.335 132.757 1.00 53.51  ? 4307 GLN A CG    1 
ATOM   21134 C  CD    . GLN A 1 4307 ? 164.534 126.189 131.779 1.00 64.41  ? 4307 GLN A CD    1 
ATOM   21135 O  OE1   . GLN A 1 4307 ? 164.402 126.400 130.573 1.00 63.69  ? 4307 GLN A OE1   1 
ATOM   21136 N  NE2   . GLN A 1 4307 ? 164.545 124.966 132.294 1.00 68.91  ? 4307 GLN A NE2   1 
ATOM   21137 N  N     . TRP A 1 4308 ? 168.091 130.452 132.671 1.00 34.12  ? 4308 TRP A N     1 
ATOM   21138 C  CA    . TRP A 1 4308 ? 169.469 130.924 132.575 1.00 30.55  ? 4308 TRP A CA    1 
ATOM   21139 C  C     . TRP A 1 4308 ? 169.895 131.656 133.840 1.00 29.24  ? 4308 TRP A C     1 
ATOM   21140 O  O     . TRP A 1 4308 ? 171.038 131.517 134.292 1.00 30.75  ? 4308 TRP A O     1 
ATOM   21141 C  CB    . TRP A 1 4308 ? 169.622 131.825 131.350 1.00 29.79  ? 4308 TRP A CB    1 
ATOM   21142 C  CG    . TRP A 1 4308 ? 171.007 132.341 131.144 1.00 29.96  ? 4308 TRP A CG    1 
ATOM   21143 C  CD1   . TRP A 1 4308 ? 171.985 131.785 130.374 1.00 28.16  ? 4308 TRP A CD1   1 
ATOM   21144 C  CD2   . TRP A 1 4308 ? 171.564 133.539 131.696 1.00 30.61  ? 4308 TRP A CD2   1 
ATOM   21145 N  NE1   . TRP A 1 4308 ? 173.122 132.555 130.423 1.00 32.42  ? 4308 TRP A NE1   1 
ATOM   21146 C  CE2   . TRP A 1 4308 ? 172.888 133.639 131.227 1.00 29.53  ? 4308 TRP A CE2   1 
ATOM   21147 C  CE3   . TRP A 1 4308 ? 171.071 134.536 132.545 1.00 28.48  ? 4308 TRP A CE3   1 
ATOM   21148 C  CZ2   . TRP A 1 4308 ? 173.726 134.693 131.580 1.00 25.39  ? 4308 TRP A CZ2   1 
ATOM   21149 C  CZ3   . TRP A 1 4308 ? 171.904 135.580 132.894 1.00 26.00  ? 4308 TRP A CZ3   1 
ATOM   21150 C  CH2   . TRP A 1 4308 ? 173.216 135.651 132.411 1.00 25.04  ? 4308 TRP A CH2   1 
ATOM   21151 N  N     . VAL A 1 4309 ? 168.993 132.448 134.423 1.00 28.43  ? 4309 VAL A N     1 
ATOM   21152 C  CA    . VAL A 1 4309 ? 169.302 133.130 135.677 1.00 29.19  ? 4309 VAL A CA    1 
ATOM   21153 C  C     . VAL A 1 4309 ? 169.529 132.115 136.791 1.00 32.89  ? 4309 VAL A C     1 
ATOM   21154 O  O     . VAL A 1 4309 ? 170.410 132.290 137.642 1.00 30.72  ? 4309 VAL A O     1 
ATOM   21155 C  CB    . VAL A 1 4309 ? 168.183 134.126 136.033 1.00 25.92  ? 4309 VAL A CB    1 
ATOM   21156 C  CG1   . VAL A 1 4309 ? 168.461 134.789 137.374 1.00 20.29  ? 4309 VAL A CG1   1 
ATOM   21157 C  CG2   . VAL A 1 4309 ? 168.036 135.171 134.940 1.00 27.17  ? 4309 VAL A CG2   1 
ATOM   21158 N  N     . GLU A 1 4310 ? 168.741 131.037 136.801 1.00 36.02  ? 4310 GLU A N     1 
ATOM   21159 C  CA    . GLU A 1 4310 ? 168.869 130.031 137.851 1.00 32.48  ? 4310 GLU A CA    1 
ATOM   21160 C  C     . GLU A 1 4310 ? 170.191 129.278 137.762 1.00 33.61  ? 4310 GLU A C     1 
ATOM   21161 O  O     . GLU A 1 4310 ? 170.733 128.863 138.792 1.00 34.15  ? 4310 GLU A O     1 
ATOM   21162 C  CB    . GLU A 1 4310 ? 167.695 129.054 137.788 1.00 34.85  ? 4310 GLU A CB    1 
ATOM   21163 C  CG    . GLU A 1 4310 ? 166.360 129.651 138.216 1.00 37.55  ? 4310 GLU A CG    1 
ATOM   21164 C  CD    . GLU A 1 4310 ? 166.163 129.655 139.723 1.00 44.79  ? 4310 GLU A CD    1 
ATOM   21165 O  OE1   . GLU A 1 4310 ? 164.997 129.646 140.167 1.00 48.87  ? 4310 GLU A OE1   1 
ATOM   21166 O  OE2   . GLU A 1 4310 ? 167.169 129.664 140.464 1.00 47.42  ? 4310 GLU A OE2   1 
ATOM   21167 N  N     . LEU A 1 4311 ? 170.726 129.093 136.557 1.00 31.42  ? 4311 LEU A N     1 
ATOM   21168 C  CA    . LEU A 1 4311 ? 172.004 128.421 136.371 1.00 29.59  ? 4311 LEU A CA    1 
ATOM   21169 C  C     . LEU A 1 4311 ? 173.197 129.357 136.527 1.00 31.50  ? 4311 LEU A C     1 
ATOM   21170 O  O     . LEU A 1 4311 ? 174.326 128.952 136.229 1.00 32.86  ? 4311 LEU A O     1 
ATOM   21171 C  CB    . LEU A 1 4311 ? 172.061 127.739 135.000 1.00 26.95  ? 4311 LEU A CB    1 
ATOM   21172 C  CG    . LEU A 1 4311 ? 171.398 126.365 134.866 1.00 36.91  ? 4311 LEU A CG    1 
ATOM   21173 C  CD1   . LEU A 1 4311 ? 170.037 126.459 134.202 1.00 35.85  ? 4311 LEU A CD1   1 
ATOM   21174 C  CD2   . LEU A 1 4311 ? 172.304 125.415 134.096 1.00 35.15  ? 4311 LEU A CD2   1 
ATOM   21175 N  N     . LEU A 1 4312 ? 172.978 130.589 136.974 1.00 29.38  ? 4312 LEU A N     1 
ATOM   21176 C  CA    . LEU A 1 4312 ? 174.093 131.489 137.222 1.00 27.44  ? 4312 LEU A CA    1 
ATOM   21177 C  C     . LEU A 1 4312 ? 174.948 130.957 138.370 1.00 32.27  ? 4312 LEU A C     1 
ATOM   21178 O  O     . LEU A 1 4312 ? 174.413 130.547 139.406 1.00 37.33  ? 4312 LEU A O     1 
ATOM   21179 C  CB    . LEU A 1 4312 ? 173.593 132.894 137.555 1.00 27.10  ? 4312 LEU A CB    1 
ATOM   21180 C  CG    . LEU A 1 4312 ? 173.332 133.840 136.383 1.00 26.33  ? 4312 LEU A CG    1 
ATOM   21181 C  CD1   . LEU A 1 4312 ? 173.052 135.246 136.889 1.00 25.96  ? 4312 LEU A CD1   1 
ATOM   21182 C  CD2   . LEU A 1 4312 ? 174.503 133.840 135.416 1.00 21.24  ? 4312 LEU A CD2   1 
ATOM   21183 N  N     . PRO A 1 4313 ? 176.269 130.939 138.216 1.00 33.97  ? 4313 PRO A N     1 
ATOM   21184 C  CA    . PRO A 1 4313 ? 177.130 130.469 139.305 1.00 30.53  ? 4313 PRO A CA    1 
ATOM   21185 C  C     . PRO A 1 4313 ? 177.047 131.383 140.517 1.00 31.93  ? 4313 PRO A C     1 
ATOM   21186 O  O     . PRO A 1 4313 ? 176.841 132.593 140.402 1.00 38.24  ? 4313 PRO A O     1 
ATOM   21187 C  CB    . PRO A 1 4313 ? 178.535 130.494 138.688 1.00 34.53  ? 4313 PRO A CB    1 
ATOM   21188 C  CG    . PRO A 1 4313 ? 178.313 130.544 137.205 1.00 32.80  ? 4313 PRO A CG    1 
ATOM   21189 C  CD    . PRO A 1 4313 ? 177.038 131.295 137.013 1.00 29.29  ? 4313 PRO A CD    1 
ATOM   21190 N  N     . ASP A 1 4314 ? 177.208 130.780 141.696 1.00 34.08  ? 4314 ASP A N     1 
ATOM   21191 C  CA    . ASP A 1 4314 ? 177.218 131.547 142.934 1.00 40.30  ? 4314 ASP A CA    1 
ATOM   21192 C  C     . ASP A 1 4314 ? 178.476 132.392 143.081 1.00 43.13  ? 4314 ASP A C     1 
ATOM   21193 O  O     . ASP A 1 4314 ? 178.493 133.314 143.904 1.00 44.61  ? 4314 ASP A O     1 
ATOM   21194 C  CB    . ASP A 1 4314 ? 177.072 130.602 144.131 1.00 42.57  ? 4314 ASP A CB    1 
ATOM   21195 C  CG    . ASP A 1 4314 ? 176.950 131.340 145.452 1.00 59.09  ? 4314 ASP A CG    1 
ATOM   21196 O  OD1   . ASP A 1 4314 ? 175.809 131.629 145.870 1.00 57.72  ? 4314 ASP A OD1   1 
ATOM   21197 O  OD2   . ASP A 1 4314 ? 177.993 131.622 146.078 1.00 64.83  ? 4314 ASP A OD2   1 
ATOM   21198 N  N     . THR A 1 4315 ? 179.513 132.118 142.290 1.00 38.77  ? 4315 THR A N     1 
ATOM   21199 C  CA    . THR A 1 4315 ? 180.772 132.856 142.370 1.00 37.31  ? 4315 THR A CA    1 
ATOM   21200 C  C     . THR A 1 4315 ? 180.604 134.193 141.654 1.00 35.54  ? 4315 THR A C     1 
ATOM   21201 O  O     . THR A 1 4315 ? 181.085 134.410 140.540 1.00 35.47  ? 4315 THR A O     1 
ATOM   21202 C  CB    . THR A 1 4315 ? 181.912 132.039 141.774 1.00 44.38  ? 4315 THR A CB    1 
ATOM   21203 O  OG1   . THR A 1 4315 ? 181.645 131.782 140.389 1.00 46.19  ? 4315 THR A OG1   1 
ATOM   21204 C  CG2   . THR A 1 4315 ? 182.054 130.714 142.507 1.00 42.96  ? 4315 THR A CG2   1 
ATOM   21205 N  N     . GLN A 1 4316 ? 179.900 135.107 142.317 1.00 30.76  ? 4316 GLN A N     1 
ATOM   21206 C  CA    . GLN A 1 4316 ? 179.714 136.455 141.802 1.00 19.27  ? 4316 GLN A CA    1 
ATOM   21207 C  C     . GLN A 1 4316 ? 180.812 137.371 142.323 1.00 21.72  ? 4316 GLN A C     1 
ATOM   21208 O  O     . GLN A 1 4316 ? 181.152 137.347 143.509 1.00 27.85  ? 4316 GLN A O     1 
ATOM   21209 C  CB    . GLN A 1 4316 ? 178.346 137.013 142.195 1.00 18.91  ? 4316 GLN A CB    1 
ATOM   21210 C  CG    . GLN A 1 4316 ? 177.985 138.294 141.458 1.00 18.25  ? 4316 GLN A CG    1 
ATOM   21211 C  CD    . GLN A 1 4316 ? 177.125 139.225 142.285 1.00 18.60  ? 4316 GLN A CD    1 
ATOM   21212 O  OE1   . GLN A 1 4316 ? 176.031 138.862 142.715 1.00 23.62  ? 4316 GLN A OE1   1 
ATOM   21213 N  NE2   . GLN A 1 4316 ? 177.615 140.438 142.512 1.00 15.13  ? 4316 GLN A NE2   1 
ATOM   21214 N  N     . THR A 1 4317 ? 181.358 138.178 141.428 1.00 20.99  ? 4317 THR A N     1 
ATOM   21215 C  CA    . THR A 1 4317 ? 182.429 139.115 141.723 1.00 21.10  ? 4317 THR A CA    1 
ATOM   21216 C  C     . THR A 1 4317 ? 182.042 140.486 141.196 1.00 17.62  ? 4317 THR A C     1 
ATOM   21217 O  O     . THR A 1 4317 ? 181.196 140.599 140.302 1.00 17.25  ? 4317 THR A O     1 
ATOM   21218 C  CB    . THR A 1 4317 ? 183.751 138.657 141.089 1.00 21.82  ? 4317 THR A CB    1 
ATOM   21219 O  OG1   . THR A 1 4317 ? 183.519 138.238 139.739 1.00 22.29  ? 4317 THR A OG1   1 
ATOM   21220 C  CG2   . THR A 1 4317 ? 184.347 137.501 141.879 1.00 19.56  ? 4317 THR A CG2   1 
ATOM   21221 N  N     . PRO A 1 4318 ? 182.633 141.555 141.738 1.00 15.55  ? 4318 PRO A N     1 
ATOM   21222 C  CA    . PRO A 1 4318 ? 182.298 142.902 141.244 1.00 16.32  ? 4318 PRO A CA    1 
ATOM   21223 C  C     . PRO A 1 4318 ? 182.616 143.110 139.774 1.00 13.13  ? 4318 PRO A C     1 
ATOM   21224 O  O     . PRO A 1 4318 ? 182.091 144.055 139.173 1.00 12.45  ? 4318 PRO A O     1 
ATOM   21225 C  CB    . PRO A 1 4318 ? 183.135 143.831 142.136 1.00 15.38  ? 4318 PRO A CB    1 
ATOM   21226 C  CG    . PRO A 1 4318 ? 184.089 142.948 142.873 1.00 19.72  ? 4318 PRO A CG    1 
ATOM   21227 C  CD    . PRO A 1 4318 ? 183.460 141.603 142.953 1.00 16.30  ? 4318 PRO A CD    1 
ATOM   21228 N  N     . SER A 1 4319 ? 183.463 142.268 139.176 1.00 15.64  ? 4319 SER A N     1 
ATOM   21229 C  CA    . SER A 1 4319 ? 183.701 142.343 137.739 1.00 12.69  ? 4319 SER A CA    1 
ATOM   21230 C  C     . SER A 1 4319 ? 182.449 142.033 136.932 1.00 16.12  ? 4319 SER A C     1 
ATOM   21231 O  O     . SER A 1 4319 ? 182.382 142.397 135.753 1.00 22.88  ? 4319 SER A O     1 
ATOM   21232 C  CB    . SER A 1 4319 ? 184.827 141.390 137.342 1.00 21.61  ? 4319 SER A CB    1 
ATOM   21233 O  OG    . SER A 1 4319 ? 184.617 140.101 137.891 1.00 24.43  ? 4319 SER A OG    1 
ATOM   21234 N  N     . TRP A 1 4320 ? 181.464 141.361 137.534 1.00 13.60  ? 4320 TRP A N     1 
ATOM   21235 C  CA    . TRP A 1 4320 ? 180.170 141.199 136.881 1.00 13.60  ? 4320 TRP A CA    1 
ATOM   21236 C  C     . TRP A 1 4320 ? 179.536 142.549 136.576 1.00 14.66  ? 4320 TRP A C     1 
ATOM   21237 O  O     . TRP A 1 4320 ? 178.814 142.689 135.583 1.00 19.82  ? 4320 TRP A O     1 
ATOM   21238 C  CB    . TRP A 1 4320 ? 179.231 140.376 137.764 1.00 15.64  ? 4320 TRP A CB    1 
ATOM   21239 C  CG    . TRP A 1 4320 ? 179.547 138.916 137.827 1.00 16.41  ? 4320 TRP A CG    1 
ATOM   21240 C  CD1   . TRP A 1 4320 ? 180.780 138.339 137.773 1.00 19.11  ? 4320 TRP A CD1   1 
ATOM   21241 C  CD2   . TRP A 1 4320 ? 178.607 137.845 137.967 1.00 18.35  ? 4320 TRP A CD2   1 
ATOM   21242 N  NE1   . TRP A 1 4320 ? 180.668 136.973 137.865 1.00 19.93  ? 4320 TRP A NE1   1 
ATOM   21243 C  CE2   . TRP A 1 4320 ? 179.343 136.645 137.985 1.00 20.43  ? 4320 TRP A CE2   1 
ATOM   21244 C  CE3   . TRP A 1 4320 ? 177.215 137.785 138.074 1.00 18.65  ? 4320 TRP A CE3   1 
ATOM   21245 C  CZ2   . TRP A 1 4320 ? 178.734 135.399 138.107 1.00 24.14  ? 4320 TRP A CZ2   1 
ATOM   21246 C  CZ3   . TRP A 1 4320 ? 176.612 136.548 138.196 1.00 19.04  ? 4320 TRP A CZ3   1 
ATOM   21247 C  CH2   . TRP A 1 4320 ? 177.371 135.371 138.211 1.00 20.72  ? 4320 TRP A CH2   1 
ATOM   21248 N  N     . LEU A 1 4321 ? 179.794 143.546 137.418 1.00 10.57  ? 4321 LEU A N     1 
ATOM   21249 C  CA    . LEU A 1 4321 ? 179.227 144.878 137.284 1.00 8.21   ? 4321 LEU A CA    1 
ATOM   21250 C  C     . LEU A 1 4321 ? 180.118 145.825 136.494 1.00 12.37  ? 4321 LEU A C     1 
ATOM   21251 O  O     . LEU A 1 4321 ? 179.771 147.002 136.348 1.00 23.15  ? 4321 LEU A O     1 
ATOM   21252 C  CB    . LEU A 1 4321 ? 178.968 145.471 138.672 1.00 11.41  ? 4321 LEU A CB    1 
ATOM   21253 C  CG    . LEU A 1 4321 ? 178.446 144.507 139.738 1.00 11.40  ? 4321 LEU A CG    1 
ATOM   21254 C  CD1   . LEU A 1 4321 ? 178.385 145.189 141.092 1.00 12.41  ? 4321 LEU A CD1   1 
ATOM   21255 C  CD2   . LEU A 1 4321 ? 177.087 143.967 139.350 1.00 10.00  ? 4321 LEU A CD2   1 
ATOM   21256 N  N     . GLY A 1 4322 ? 181.252 145.349 135.985 1.00 9.34   ? 4322 GLY A N     1 
ATOM   21257 C  CA    . GLY A 1 4322 ? 182.227 146.203 135.347 1.00 10.40  ? 4322 GLY A CA    1 
ATOM   21258 C  C     . GLY A 1 4322 ? 183.208 146.860 136.292 1.00 11.62  ? 4322 GLY A C     1 
ATOM   21259 O  O     . GLY A 1 4322 ? 184.069 147.621 135.835 1.00 19.08  ? 4322 GLY A O     1 
ATOM   21260 N  N     . LEU A 1 4323 ? 183.102 146.597 137.590 1.00 11.43  ? 4323 LEU A N     1 
ATOM   21261 C  CA    . LEU A 1 4323 ? 184.009 147.147 138.581 1.00 9.81   ? 4323 LEU A CA    1 
ATOM   21262 C  C     . LEU A 1 4323 ? 185.245 146.265 138.732 1.00 12.40  ? 4323 LEU A C     1 
ATOM   21263 O  O     . LEU A 1 4323 ? 185.227 145.088 138.367 1.00 16.20  ? 4323 LEU A O     1 
ATOM   21264 C  CB    . LEU A 1 4323 ? 183.293 147.282 139.921 1.00 8.32   ? 4323 LEU A CB    1 
ATOM   21265 C  CG    . LEU A 1 4323 ? 182.266 148.408 140.018 1.00 10.33  ? 4323 LEU A CG    1 
ATOM   21266 C  CD1   . LEU A 1 4323 ? 181.435 148.269 141.278 1.00 10.85  ? 4323 LEU A CD1   1 
ATOM   21267 C  CD2   . LEU A 1 4323 ? 182.973 149.749 139.995 1.00 17.01  ? 4323 LEU A CD2   1 
ATOM   21268 N  N     . PRO A 1 4324 ? 186.341 146.815 139.256 1.00 14.59  ? 4324 PRO A N     1 
ATOM   21269 C  CA    . PRO A 1 4324 ? 187.500 145.973 139.565 1.00 13.54  ? 4324 PRO A CA    1 
ATOM   21270 C  C     . PRO A 1 4324 ? 187.168 144.961 140.651 1.00 17.78  ? 4324 PRO A C     1 
ATOM   21271 O  O     . PRO A 1 4324 ? 186.324 145.198 141.519 1.00 14.16  ? 4324 PRO A O     1 
ATOM   21272 C  CB    . PRO A 1 4324 ? 188.559 146.978 140.035 1.00 13.93  ? 4324 PRO A CB    1 
ATOM   21273 C  CG    . PRO A 1 4324 ? 187.784 148.181 140.456 1.00 14.47  ? 4324 PRO A CG    1 
ATOM   21274 C  CD    . PRO A 1 4324 ? 186.607 148.237 139.534 1.00 15.84  ? 4324 PRO A CD    1 
ATOM   21275 N  N     . ASN A 1 4325 ? 187.846 143.813 140.591 1.00 19.97  ? 4325 ASN A N     1 
ATOM   21276 C  CA    . ASN A 1 4325 ? 187.520 142.704 141.478 1.00 18.01  ? 4325 ASN A CA    1 
ATOM   21277 C  C     . ASN A 1 4325 ? 187.902 142.973 142.928 1.00 23.56  ? 4325 ASN A C     1 
ATOM   21278 O  O     . ASN A 1 4325 ? 187.407 142.280 143.822 1.00 26.43  ? 4325 ASN A O     1 
ATOM   21279 C  CB    . ASN A 1 4325 ? 188.203 141.426 140.991 1.00 18.42  ? 4325 ASN A CB    1 
ATOM   21280 C  CG    . ASN A 1 4325 ? 187.274 140.546 140.182 1.00 21.88  ? 4325 ASN A CG    1 
ATOM   21281 O  OD1   . ASN A 1 4325 ? 186.054 140.663 140.278 1.00 18.72  ? 4325 ASN A OD1   1 
ATOM   21282 N  ND2   . ASN A 1 4325 ? 187.847 139.658 139.377 1.00 24.03  ? 4325 ASN A ND2   1 
ATOM   21283 N  N     . ASN A 1 4326 ? 188.760 143.957 143.182 1.00 23.74  ? 4326 ASN A N     1 
ATOM   21284 C  CA    . ASN A 1 4326 ? 189.195 144.275 144.535 1.00 25.09  ? 4326 ASN A CA    1 
ATOM   21285 C  C     . ASN A 1 4326 ? 188.313 145.311 145.219 1.00 26.69  ? 4326 ASN A C     1 
ATOM   21286 O  O     . ASN A 1 4326 ? 188.618 145.715 146.345 1.00 32.80  ? 4326 ASN A O     1 
ATOM   21287 C  CB    . ASN A 1 4326 ? 190.646 144.766 144.521 1.00 28.24  ? 4326 ASN A CB    1 
ATOM   21288 C  CG    . ASN A 1 4326 ? 190.881 145.866 143.505 1.00 28.87  ? 4326 ASN A CG    1 
ATOM   21289 O  OD1   . ASN A 1 4326 ? 189.939 146.423 142.944 1.00 28.80  ? 4326 ASN A OD1   1 
ATOM   21290 N  ND2   . ASN A 1 4326 ? 192.146 146.187 143.266 1.00 34.03  ? 4326 ASN A ND2   1 
ATOM   21291 N  N     . ALA A 1 4327 ? 187.235 145.755 144.567 1.00 23.80  ? 4327 ALA A N     1 
ATOM   21292 C  CA    . ALA A 1 4327 ? 186.375 146.770 145.167 1.00 26.44  ? 4327 ALA A CA    1 
ATOM   21293 C  C     . ALA A 1 4327 ? 185.637 146.236 146.387 1.00 27.97  ? 4327 ALA A C     1 
ATOM   21294 O  O     . ALA A 1 4327 ? 185.270 147.010 147.278 1.00 35.86  ? 4327 ALA A O     1 
ATOM   21295 C  CB    . ALA A 1 4327 ? 185.379 147.294 144.132 1.00 25.86  ? 4327 ALA A CB    1 
ATOM   21296 N  N     . GLU A 1 4328 ? 185.408 144.925 146.447 1.00 25.83  ? 4328 GLU A N     1 
ATOM   21297 C  CA    . GLU A 1 4328 ? 184.733 144.319 147.586 1.00 29.75  ? 4328 GLU A CA    1 
ATOM   21298 C  C     . GLU A 1 4328 ? 185.690 143.849 148.671 1.00 29.37  ? 4328 GLU A C     1 
ATOM   21299 O  O     . GLU A 1 4328 ? 185.230 143.453 149.748 1.00 30.91  ? 4328 GLU A O     1 
ATOM   21300 C  CB    . GLU A 1 4328 ? 183.884 143.129 147.127 1.00 25.90  ? 4328 GLU A CB    1 
ATOM   21301 C  CG    . GLU A 1 4328 ? 184.703 141.957 146.614 1.00 21.45  ? 4328 GLU A CG    1 
ATOM   21302 C  CD    . GLU A 1 4328 ? 183.858 140.731 146.336 1.00 29.91  ? 4328 GLU A CD    1 
ATOM   21303 O  OE1   . GLU A 1 4328 ? 182.625 140.805 146.516 1.00 26.69  ? 4328 GLU A OE1   1 
ATOM   21304 O  OE2   . GLU A 1 4328 ? 184.428 139.692 145.940 1.00 35.00  ? 4328 GLU A OE2   1 
ATOM   21305 N  N     . ARG A 1 4329 ? 187.000 143.888 148.418 1.00 31.10  ? 4329 ARG A N     1 
ATOM   21306 C  CA    . ARG A 1 4329 ? 187.966 143.305 149.344 1.00 31.76  ? 4329 ARG A CA    1 
ATOM   21307 C  C     . ARG A 1 4329 ? 187.919 143.991 150.705 1.00 28.67  ? 4329 ARG A C     1 
ATOM   21308 O  O     . ARG A 1 4329 ? 187.893 143.332 151.750 1.00 28.67  ? 4329 ARG A O     1 
ATOM   21309 C  CB    . ARG A 1 4329 ? 189.371 143.385 148.744 1.00 31.79  ? 4329 ARG A CB    1 
ATOM   21310 C  CG    . ARG A 1 4329 ? 190.490 143.291 149.767 1.00 32.43  ? 4329 ARG A CG    1 
ATOM   21311 C  CD    . ARG A 1 4329 ? 191.806 142.923 149.105 1.00 35.21  ? 4329 ARG A CD    1 
ATOM   21312 N  NE    . ARG A 1 4329 ? 191.676 141.741 148.262 1.00 40.96  ? 4329 ARG A NE    1 
ATOM   21313 C  CZ    . ARG A 1 4329 ? 192.577 140.772 148.184 1.00 44.76  ? 4329 ARG A CZ    1 
ATOM   21314 N  NH1   . ARG A 1 4329 ? 193.687 140.800 148.903 1.00 38.84  ? 4329 ARG A NH1   1 
ATOM   21315 N  NH2   . ARG A 1 4329 ? 192.359 139.748 147.364 1.00 45.23  ? 4329 ARG A NH2   1 
ATOM   21316 N  N     . VAL A 1 4330 ? 187.905 145.325 150.709 1.00 30.32  ? 4330 VAL A N     1 
ATOM   21317 C  CA    . VAL A 1 4330 ? 187.848 146.063 151.968 1.00 29.57  ? 4330 VAL A CA    1 
ATOM   21318 C  C     . VAL A 1 4330 ? 186.490 145.867 152.632 1.00 29.08  ? 4330 VAL A C     1 
ATOM   21319 O  O     . VAL A 1 4330 ? 186.393 145.681 153.851 1.00 30.91  ? 4330 VAL A O     1 
ATOM   21320 C  CB    . VAL A 1 4330 ? 188.159 147.552 151.731 1.00 31.36  ? 4330 VAL A CB    1 
ATOM   21321 C  CG1   . VAL A 1 4330 ? 187.693 148.396 152.908 1.00 28.28  ? 4330 VAL A CG1   1 
ATOM   21322 C  CG2   . VAL A 1 4330 ? 189.647 147.747 151.485 1.00 24.79  ? 4330 VAL A CG2   1 
ATOM   21323 N  N     . LEU A 1 4331 ? 185.420 145.900 151.834 1.00 31.39  ? 4331 LEU A N     1 
ATOM   21324 C  CA    . LEU A 1 4331 ? 184.077 145.705 152.372 1.00 30.30  ? 4331 LEU A CA    1 
ATOM   21325 C  C     . LEU A 1 4331 ? 183.914 144.308 152.962 1.00 24.94  ? 4331 LEU A C     1 
ATOM   21326 O  O     . LEU A 1 4331 ? 183.316 144.137 154.030 1.00 27.26  ? 4331 LEU A O     1 
ATOM   21327 C  CB    . LEU A 1 4331 ? 183.038 145.953 151.277 1.00 33.13  ? 4331 LEU A CB    1 
ATOM   21328 C  CG    . LEU A 1 4331 ? 181.571 145.923 151.708 1.00 40.80  ? 4331 LEU A CG    1 
ATOM   21329 C  CD1   . LEU A 1 4331 ? 181.140 147.282 152.240 1.00 37.30  ? 4331 LEU A CD1   1 
ATOM   21330 C  CD2   . LEU A 1 4331 ? 180.683 145.487 150.554 1.00 41.98  ? 4331 LEU A CD2   1 
ATOM   21331 N  N     . LEU A 1 4332 ? 184.437 143.293 152.270 1.00 25.13  ? 4332 LEU A N     1 
ATOM   21332 C  CA    . LEU A 1 4332 ? 184.320 141.921 152.752 1.00 23.51  ? 4332 LEU A CA    1 
ATOM   21333 C  C     . LEU A 1 4332 ? 185.088 141.723 154.055 1.00 26.78  ? 4332 LEU A C     1 
ATOM   21334 O  O     . LEU A 1 4332 ? 184.618 141.037 154.969 1.00 31.73  ? 4332 LEU A O     1 
ATOM   21335 C  CB    . LEU A 1 4332 ? 184.814 140.945 151.683 1.00 22.04  ? 4332 LEU A CB    1 
ATOM   21336 C  CG    . LEU A 1 4332 ? 183.840 140.616 150.549 1.00 17.68  ? 4332 LEU A CG    1 
ATOM   21337 C  CD1   . LEU A 1 4332 ? 184.385 139.489 149.689 1.00 16.74  ? 4332 LEU A CD1   1 
ATOM   21338 C  CD2   . LEU A 1 4332 ? 182.472 140.258 151.100 1.00 21.11  ? 4332 LEU A CD2   1 
ATOM   21339 N  N     . THR A 1 4333 ? 186.282 142.313 154.151 1.00 27.30  ? 4333 THR A N     1 
ATOM   21340 C  CA    . THR A 1 4333 ? 187.083 142.181 155.364 1.00 28.34  ? 4333 THR A CA    1 
ATOM   21341 C  C     . THR A 1 4333 ? 186.378 142.809 156.559 1.00 28.02  ? 4333 THR A C     1 
ATOM   21342 O  O     . THR A 1 4333 ? 186.356 142.239 157.656 1.00 34.38  ? 4333 THR A O     1 
ATOM   21343 C  CB    . THR A 1 4333 ? 188.458 142.818 155.157 1.00 31.12  ? 4333 THR A CB    1 
ATOM   21344 O  OG1   . THR A 1 4333 ? 189.092 142.229 154.015 1.00 31.12  ? 4333 THR A OG1   1 
ATOM   21345 C  CG2   . THR A 1 4333 ? 189.335 142.600 156.379 1.00 30.68  ? 4333 THR A CG2   1 
ATOM   21346 N  N     . THR A 1 4334 ? 185.793 143.993 156.362 1.00 24.59  ? 4334 THR A N     1 
ATOM   21347 C  CA    . THR A 1 4334 ? 185.061 144.650 157.440 1.00 25.24  ? 4334 THR A CA    1 
ATOM   21348 C  C     . THR A 1 4334 ? 183.846 143.828 157.854 1.00 27.38  ? 4334 THR A C     1 
ATOM   21349 O  O     . THR A 1 4334 ? 183.533 143.713 159.045 1.00 28.84  ? 4334 THR A O     1 
ATOM   21350 C  CB    . THR A 1 4334 ? 184.642 146.055 157.008 1.00 24.52  ? 4334 THR A CB    1 
ATOM   21351 O  OG1   . THR A 1 4334 ? 185.803 146.812 156.644 1.00 31.25  ? 4334 THR A OG1   1 
ATOM   21352 C  CG2   . THR A 1 4334 ? 183.915 146.769 158.138 1.00 24.02  ? 4334 THR A CG2   1 
ATOM   21353 N  N     . GLN A 1 4335 ? 183.148 143.246 156.876 1.00 27.25  ? 4335 GLN A N     1 
ATOM   21354 C  CA    . GLN A 1 4335 ? 181.985 142.419 157.182 1.00 25.52  ? 4335 GLN A CA    1 
ATOM   21355 C  C     . GLN A 1 4335 ? 182.382 141.175 157.968 1.00 24.66  ? 4335 GLN A C     1 
ATOM   21356 O  O     . GLN A 1 4335 ? 181.674 140.765 158.895 1.00 25.62  ? 4335 GLN A O     1 
ATOM   21357 C  CB    . GLN A 1 4335 ? 181.265 142.032 155.892 1.00 25.12  ? 4335 GLN A CB    1 
ATOM   21358 C  CG    . GLN A 1 4335 ? 180.366 143.119 155.330 1.00 27.87  ? 4335 GLN A CG    1 
ATOM   21359 C  CD    . GLN A 1 4335 ? 179.542 142.639 154.152 1.00 34.56  ? 4335 GLN A CD    1 
ATOM   21360 O  OE1   . GLN A 1 4335 ? 180.051 142.503 153.039 1.00 32.51  ? 4335 GLN A OE1   1 
ATOM   21361 N  NE2   . GLN A 1 4335 ? 178.262 142.378 154.392 1.00 27.56  ? 4335 GLN A NE2   1 
ATOM   21362 N  N     . GLY A 1 4336 ? 183.506 140.555 157.604 1.00 27.37  ? 4336 GLY A N     1 
ATOM   21363 C  CA    . GLY A 1 4336 ? 183.953 139.372 158.324 1.00 26.50  ? 4336 GLY A CA    1 
ATOM   21364 C  C     . GLY A 1 4336 ? 184.313 139.671 159.766 1.00 27.13  ? 4336 GLY A C     1 
ATOM   21365 O  O     . GLY A 1 4336 ? 184.016 138.887 160.670 1.00 25.68  ? 4336 GLY A O     1 
ATOM   21366 N  N     . VAL A 1 4337 ? 184.968 140.811 159.998 1.00 26.66  ? 4337 VAL A N     1 
ATOM   21367 C  CA    . VAL A 1 4337 ? 185.302 141.215 161.361 1.00 26.84  ? 4337 VAL A CA    1 
ATOM   21368 C  C     . VAL A 1 4337 ? 184.034 141.509 162.153 1.00 28.22  ? 4337 VAL A C     1 
ATOM   21369 O  O     . VAL A 1 4337 ? 183.940 141.191 163.345 1.00 30.19  ? 4337 VAL A O     1 
ATOM   21370 C  CB    . VAL A 1 4337 ? 186.256 142.425 161.339 1.00 24.96  ? 4337 VAL A CB    1 
ATOM   21371 C  CG1   . VAL A 1 4337 ? 186.452 142.982 162.740 1.00 27.41  ? 4337 VAL A CG1   1 
ATOM   21372 C  CG2   . VAL A 1 4337 ? 187.593 142.038 160.720 1.00 27.10  ? 4337 VAL A CG2   1 
ATOM   21373 N  N     . ASP A 1 4338 ? 183.037 142.114 161.502 1.00 27.00  ? 4338 ASP A N     1 
ATOM   21374 C  CA    . ASP A 1 4338 ? 181.760 142.360 162.165 1.00 26.42  ? 4338 ASP A CA    1 
ATOM   21375 C  C     . ASP A 1 4338 ? 181.105 141.052 162.588 1.00 24.34  ? 4338 ASP A C     1 
ATOM   21376 O  O     . ASP A 1 4338 ? 180.547 140.954 163.687 1.00 28.94  ? 4338 ASP A O     1 
ATOM   21377 C  CB    . ASP A 1 4338 ? 180.832 143.145 161.237 1.00 32.50  ? 4338 ASP A CB    1 
ATOM   21378 C  CG    . ASP A 1 4338 ? 180.835 144.632 161.529 1.00 39.02  ? 4338 ASP A CG    1 
ATOM   21379 O  OD1   . ASP A 1 4338 ? 181.524 145.053 162.480 1.00 38.38  ? 4338 ASP A OD1   1 
ATOM   21380 O  OD2   . ASP A 1 4338 ? 180.151 145.382 160.800 1.00 36.40  ? 4338 ASP A OD2   1 
ATOM   21381 N  N     . MET A 1 4339 ? 181.173 140.034 161.728 1.00 24.04  ? 4339 MET A N     1 
ATOM   21382 C  CA    . MET A 1 4339 ? 180.611 138.729 162.063 1.00 23.21  ? 4339 MET A CA    1 
ATOM   21383 C  C     . MET A 1 4339 ? 181.372 138.078 163.214 1.00 27.53  ? 4339 MET A C     1 
ATOM   21384 O  O     . MET A 1 4339 ? 180.804 137.291 163.978 1.00 30.39  ? 4339 MET A O     1 
ATOM   21385 C  CB    . MET A 1 4339 ? 180.589 137.850 160.808 1.00 22.22  ? 4339 MET A CB    1 
ATOM   21386 C  CG    . MET A 1 4339 ? 180.248 136.385 161.018 1.00 23.05  ? 4339 MET A CG    1 
ATOM   21387 S  SD    . MET A 1 4339 ? 181.469 135.325 160.216 1.00 44.88  ? 4339 MET A SD    1 
ATOM   21388 C  CE    . MET A 1 4339 ? 182.674 135.110 161.513 1.00 35.26  ? 4339 MET A CE    1 
ATOM   21389 N  N     . ILE A 1 4340 ? 182.658 138.402 163.361 1.00 32.14  ? 4340 ILE A N     1 
ATOM   21390 C  CA    . ILE A 1 4340 ? 183.388 138.013 164.568 1.00 31.25  ? 4340 ILE A CA    1 
ATOM   21391 C  C     . ILE A 1 4340 ? 182.820 138.734 165.786 1.00 26.98  ? 4340 ILE A C     1 
ATOM   21392 O  O     . ILE A 1 4340 ? 182.607 138.133 166.846 1.00 28.62  ? 4340 ILE A O     1 
ATOM   21393 C  CB    . ILE A 1 4340 ? 184.894 138.291 164.402 1.00 30.68  ? 4340 ILE A CB    1 
ATOM   21394 C  CG1   . ILE A 1 4340 ? 185.551 137.242 163.502 1.00 32.02  ? 4340 ILE A CG1   1 
ATOM   21395 C  CG2   . ILE A 1 4340 ? 185.585 138.342 165.758 1.00 35.95  ? 4340 ILE A CG2   1 
ATOM   21396 C  CD1   . ILE A 1 4340 ? 185.181 135.825 163.852 1.00 32.51  ? 4340 ILE A CD1   1 
ATOM   21397 N  N     . SER A 1 4341 ? 182.568 140.038 165.648 1.00 24.37  ? 4341 SER A N     1 
ATOM   21398 C  CA    . SER A 1 4341 ? 182.116 140.841 166.781 1.00 27.01  ? 4341 SER A CA    1 
ATOM   21399 C  C     . SER A 1 4341 ? 180.735 140.407 167.257 1.00 32.61  ? 4341 SER A C     1 
ATOM   21400 O  O     . SER A 1 4341 ? 180.466 140.362 168.463 1.00 36.35  ? 4341 SER A O     1 
ATOM   21401 C  CB    . SER A 1 4341 ? 182.112 142.320 166.398 1.00 25.94  ? 4341 SER A CB    1 
ATOM   21402 O  OG    . SER A 1 4341 ? 183.364 142.706 165.861 1.00 36.04  ? 4341 SER A OG    1 
ATOM   21403 N  N     . LYS A 1 4342 ? 179.839 140.097 166.318 1.00 29.91  ? 4342 LYS A N     1 
ATOM   21404 C  CA    . LYS A 1 4342 ? 178.472 139.739 166.684 1.00 28.37  ? 4342 LYS A CA    1 
ATOM   21405 C  C     . LYS A 1 4342 ? 178.438 138.449 167.493 1.00 33.68  ? 4342 LYS A C     1 
ATOM   21406 O  O     . LYS A 1 4342 ? 177.646 138.313 168.433 1.00 40.08  ? 4342 LYS A O     1 
ATOM   21407 C  CB    . LYS A 1 4342 ? 177.611 139.628 165.427 1.00 28.03  ? 4342 LYS A CB    1 
ATOM   21408 C  CG    . LYS A 1 4342 ? 177.521 140.932 164.648 1.00 24.09  ? 4342 LYS A CG    1 
ATOM   21409 C  CD    . LYS A 1 4342 ? 176.859 140.736 163.298 1.00 27.24  ? 4342 LYS A CD    1 
ATOM   21410 C  CE    . LYS A 1 4342 ? 177.060 141.948 162.403 1.00 32.30  ? 4342 LYS A CE    1 
ATOM   21411 N  NZ    . LYS A 1 4342 ? 176.665 143.216 163.074 1.00 32.77  ? 4342 LYS A NZ    1 
ATOM   21412 N  N     . MET A 1 4343 ? 179.287 137.483 167.139 1.00 27.29  ? 4343 MET A N     1 
ATOM   21413 C  CA    . MET A 1 4343 ? 179.403 136.274 167.944 1.00 28.89  ? 4343 MET A CA    1 
ATOM   21414 C  C     . MET A 1 4343 ? 179.875 136.569 169.356 1.00 37.84  ? 4343 MET A C     1 
ATOM   21415 O  O     . MET A 1 4343 ? 179.253 136.107 170.318 1.00 48.71  ? 4343 MET A O     1 
ATOM   21416 C  CB    . MET A 1 4343 ? 180.387 135.310 167.301 1.00 31.05  ? 4343 MET A CB    1 
ATOM   21417 C  CG    . MET A 1 4343 ? 180.069 134.982 165.883 1.00 32.68  ? 4343 MET A CG    1 
ATOM   21418 S  SD    . MET A 1 4343 ? 180.534 133.309 165.474 1.00 43.19  ? 4343 MET A SD    1 
ATOM   21419 C  CE    . MET A 1 4343 ? 180.530 133.491 163.711 1.00 36.21  ? 4343 MET A CE    1 
ATOM   21420 N  N     . LEU A 1 4344 ? 180.954 137.335 169.495 1.00 35.36  ? 4344 LEU A N     1 
ATOM   21421 C  CA    . LEU A 1 4344 ? 181.522 137.653 170.794 1.00 40.90  ? 4344 LEU A CA    1 
ATOM   21422 C  C     . LEU A 1 4344 ? 180.596 138.505 171.648 1.00 43.71  ? 4344 LEU A C     1 
ATOM   21423 O  O     . LEU A 1 4344 ? 180.774 138.558 172.870 1.00 50.69  ? 4344 LEU A O     1 
ATOM   21424 C  CB    . LEU A 1 4344 ? 182.862 138.369 170.602 1.00 41.31  ? 4344 LEU A CB    1 
ATOM   21425 C  CG    . LEU A 1 4344 ? 183.875 138.316 171.742 1.00 47.22  ? 4344 LEU A CG    1 
ATOM   21426 C  CD1   . LEU A 1 4344 ? 184.361 136.892 171.952 1.00 46.97  ? 4344 LEU A CD1   1 
ATOM   21427 C  CD2   . LEU A 1 4344 ? 185.035 139.249 171.440 1.00 49.36  ? 4344 LEU A CD2   1 
ATOM   21428 N  N     . LYS A 1 4345 ? 179.616 139.166 171.036 1.00 36.46  ? 4345 LYS A N     1 
ATOM   21429 C  CA    . LYS A 1 4345 ? 178.645 139.957 171.776 1.00 39.42  ? 4345 LYS A CA    1 
ATOM   21430 C  C     . LYS A 1 4345 ? 177.523 139.116 172.373 1.00 40.78  ? 4345 LYS A C     1 
ATOM   21431 O  O     . LYS A 1 4345 ? 176.807 139.606 173.253 1.00 39.02  ? 4345 LYS A O     1 
ATOM   21432 C  CB    . LYS A 1 4345 ? 178.058 141.032 170.860 1.00 36.76  ? 4345 LYS A CB    1 
ATOM   21433 C  CG    . LYS A 1 4345 ? 177.977 142.409 171.480 1.00 34.15  ? 4345 LYS A CG    1 
ATOM   21434 C  CD    . LYS A 1 4345 ? 177.203 143.357 170.587 1.00 33.59  ? 4345 LYS A CD    1 
ATOM   21435 C  CE    . LYS A 1 4345 ? 176.570 144.467 171.399 1.00 36.77  ? 4345 LYS A CE    1 
ATOM   21436 N  NZ    . LYS A 1 4345 ? 175.757 143.916 172.518 1.00 41.92  ? 4345 LYS A NZ    1 
ATOM   21437 N  N     . MET A 1 4346 ? 177.352 137.873 171.925 1.00 38.95  ? 4346 MET A N     1 
ATOM   21438 C  CA    . MET A 1 4346 ? 176.300 136.998 172.427 1.00 41.49  ? 4346 MET A CA    1 
ATOM   21439 C  C     . MET A 1 4346 ? 176.849 135.754 173.114 1.00 46.10  ? 4346 MET A C     1 
ATOM   21440 O  O     . MET A 1 4346 ? 176.108 134.783 173.300 1.00 51.52  ? 4346 MET A O     1 
ATOM   21441 C  CB    . MET A 1 4346 ? 175.357 136.600 171.290 1.00 35.97  ? 4346 MET A CB    1 
ATOM   21442 C  CG    . MET A 1 4346 ? 175.164 137.685 170.241 1.00 38.54  ? 4346 MET A CG    1 
ATOM   21443 S  SD    . MET A 1 4346 ? 173.862 137.332 169.044 1.00 33.86  ? 4346 MET A SD    1 
ATOM   21444 C  CE    . MET A 1 4346 ? 173.932 135.551 168.999 1.00 19.27  ? 4346 MET A CE    1 
ATOM   21445 N  N     . GLN A 1 4347 ? 178.125 135.754 173.487 1.00 49.91  ? 4347 GLN A N     1 
ATOM   21446 C  CA    . GLN A 1 4347 ? 178.712 134.627 174.200 1.00 49.82  ? 4347 GLN A CA    1 
ATOM   21447 C  C     . GLN A 1 4347 ? 178.488 134.762 175.702 1.00 46.21  ? 4347 GLN A C     1 
ATOM   21448 O  O     . GLN A 1 4347 ? 177.733 135.625 176.151 1.00 39.75  ? 4347 GLN A O     1 
ATOM   21449 C  CB    . GLN A 1 4347 ? 180.209 134.514 173.899 1.00 41.33  ? 4347 GLN A CB    1 
ATOM   21450 C  CG    . GLN A 1 4347 ? 180.795 133.133 174.167 1.00 50.38  ? 4347 GLN A CG    1 
ATOM   21451 C  CD    . GLN A 1 4347 ? 180.597 132.170 173.012 1.00 53.41  ? 4347 GLN A CD    1 
ATOM   21452 O  OE1   . GLN A 1 4347 ? 179.718 132.358 172.172 1.00 50.72  ? 4347 GLN A OE1   1 
ATOM   21453 N  NE2   . GLN A 1 4347 ? 181.415 131.124 172.970 1.00 52.00  ? 4347 GLN A NE2   1 
ATOM   21454 N  N     . PRO A 1 4374 ? 192.330 164.134 188.032 1.00 77.61  ? 4374 PRO A N     1 
ATOM   21455 C  CA    . PRO A 1 4374 ? 191.560 162.991 187.541 1.00 80.44  ? 4374 PRO A CA    1 
ATOM   21456 C  C     . PRO A 1 4374 ? 192.244 162.276 186.379 1.00 85.51  ? 4374 PRO A C     1 
ATOM   21457 O  O     . PRO A 1 4374 ? 193.192 162.810 185.802 1.00 85.71  ? 4374 PRO A O     1 
ATOM   21458 C  CB    . PRO A 1 4374 ? 190.243 163.634 187.096 1.00 85.31  ? 4374 PRO A CB    1 
ATOM   21459 C  CG    . PRO A 1 4374 ? 190.154 164.954 187.882 1.00 86.49  ? 4374 PRO A CG    1 
ATOM   21460 C  CD    . PRO A 1 4374 ? 191.448 165.137 188.645 1.00 78.94  ? 4374 PRO A CD    1 
ATOM   21461 N  N     . ALA A 1 4375 ? 191.762 161.076 186.046 1.00 86.04  ? 4375 ALA A N     1 
ATOM   21462 C  CA    . ALA A 1 4375 ? 192.387 160.293 184.985 1.00 84.00  ? 4375 ALA A CA    1 
ATOM   21463 C  C     . ALA A 1 4375 ? 192.223 160.967 183.628 1.00 85.90  ? 4375 ALA A C     1 
ATOM   21464 O  O     . ALA A 1 4375 ? 193.199 161.142 182.889 1.00 84.52  ? 4375 ALA A O     1 
ATOM   21465 C  CB    . ALA A 1 4375 ? 191.800 158.882 184.961 1.00 73.62  ? 4375 ALA A CB    1 
ATOM   21466 N  N     . TRP A 1 4376 ? 190.993 161.353 183.281 1.00 85.57  ? 4376 TRP A N     1 
ATOM   21467 C  CA    . TRP A 1 4376 ? 190.771 162.036 182.011 1.00 83.41  ? 4376 TRP A CA    1 
ATOM   21468 C  C     . TRP A 1 4376 ? 191.341 163.447 182.030 1.00 80.08  ? 4376 TRP A C     1 
ATOM   21469 O  O     . TRP A 1 4376 ? 191.760 163.959 180.986 1.00 78.12  ? 4376 TRP A O     1 
ATOM   21470 C  CB    . TRP A 1 4376 ? 189.276 162.056 181.678 1.00 79.60  ? 4376 TRP A CB    1 
ATOM   21471 C  CG    . TRP A 1 4376 ? 188.466 163.026 182.490 1.00 83.45  ? 4376 TRP A CG    1 
ATOM   21472 C  CD1   . TRP A 1 4376 ? 187.726 162.743 183.601 1.00 84.05  ? 4376 TRP A CD1   1 
ATOM   21473 C  CD2   . TRP A 1 4376 ? 188.288 164.427 182.238 1.00 84.33  ? 4376 TRP A CD2   1 
ATOM   21474 N  NE1   . TRP A 1 4376 ? 187.114 163.881 184.066 1.00 81.64  ? 4376 TRP A NE1   1 
ATOM   21475 C  CE2   . TRP A 1 4376 ? 187.442 164.928 183.246 1.00 82.25  ? 4376 TRP A CE2   1 
ATOM   21476 C  CE3   . TRP A 1 4376 ? 188.770 165.306 181.262 1.00 82.25  ? 4376 TRP A CE3   1 
ATOM   21477 C  CZ2   . TRP A 1 4376 ? 187.066 166.268 183.307 1.00 76.66  ? 4376 TRP A CZ2   1 
ATOM   21478 C  CZ3   . TRP A 1 4376 ? 188.397 166.635 181.326 1.00 79.05  ? 4376 TRP A CZ3   1 
ATOM   21479 C  CH2   . TRP A 1 4376 ? 187.553 167.103 182.340 1.00 76.24  ? 4376 TRP A CH2   1 
ATOM   21480 N  N     . MET A 1 4377 ? 191.359 164.089 183.200 1.00 82.81  ? 4377 MET A N     1 
ATOM   21481 C  CA    . MET A 1 4377 ? 191.920 165.432 183.307 1.00 83.18  ? 4377 MET A CA    1 
ATOM   21482 C  C     . MET A 1 4377 ? 193.411 165.424 182.989 1.00 82.72  ? 4377 MET A C     1 
ATOM   21483 O  O     . MET A 1 4377 ? 193.926 166.342 182.340 1.00 74.17  ? 4377 MET A O     1 
ATOM   21484 C  CB    . MET A 1 4377 ? 191.658 165.987 184.708 1.00 82.01  ? 4377 MET A CB    1 
ATOM   21485 C  CG    . MET A 1 4377 ? 190.546 167.026 184.765 1.00 83.05  ? 4377 MET A CG    1 
ATOM   21486 S  SD    . MET A 1 4377 ? 191.117 168.717 184.528 1.00 85.72  ? 4377 MET A SD    1 
ATOM   21487 C  CE    . MET A 1 4377 ? 192.194 168.894 185.947 1.00 73.09  ? 4377 MET A CE    1 
ATOM   21488 N  N     . ARG A 1 4378 ? 194.122 164.390 183.446 1.00 86.02  ? 4378 ARG A N     1 
ATOM   21489 C  CA    . ARG A 1 4378 ? 195.528 164.240 183.081 1.00 84.63  ? 4378 ARG A CA    1 
ATOM   21490 C  C     . ARG A 1 4378 ? 195.678 163.768 181.640 1.00 81.43  ? 4378 ARG A C     1 
ATOM   21491 O  O     . ARG A 1 4378 ? 196.601 164.191 180.935 1.00 78.97  ? 4378 ARG A O     1 
ATOM   21492 C  CB    . ARG A 1 4378 ? 196.221 163.266 184.034 1.00 82.06  ? 4378 ARG A CB    1 
ATOM   21493 C  CG    . ARG A 1 4378 ? 196.909 163.913 185.230 1.00 82.51  ? 4378 ARG A CG    1 
ATOM   21494 C  CD    . ARG A 1 4378 ? 195.941 164.698 186.101 1.00 85.55  ? 4378 ARG A CD    1 
ATOM   21495 N  NE    . ARG A 1 4378 ? 196.600 165.229 187.289 1.00 89.42  ? 4378 ARG A NE    1 
ATOM   21496 C  CZ    . ARG A 1 4378 ? 195.983 165.898 188.253 1.00 90.05  ? 4378 ARG A CZ    1 
ATOM   21497 N  NH1   . ARG A 1 4378 ? 194.685 166.144 188.204 1.00 87.21  ? 4378 ARG A NH1   1 
ATOM   21498 N  NH2   . ARG A 1 4378 ? 196.688 166.331 189.295 1.00 86.58  ? 4378 ARG A NH2   1 
ATOM   21499 N  N     . THR A 1 4379 ? 194.784 162.883 181.190 1.00 81.48  ? 4379 THR A N     1 
ATOM   21500 C  CA    . THR A 1 4379 ? 194.868 162.367 179.826 1.00 80.29  ? 4379 THR A CA    1 
ATOM   21501 C  C     . THR A 1 4379 ? 194.678 163.478 178.802 1.00 78.94  ? 4379 THR A C     1 
ATOM   21502 O  O     . THR A 1 4379 ? 195.396 163.537 177.796 1.00 74.74  ? 4379 THR A O     1 
ATOM   21503 C  CB    . THR A 1 4379 ? 193.828 161.266 179.618 1.00 78.04  ? 4379 THR A CB    1 
ATOM   21504 O  OG1   . THR A 1 4379 ? 193.932 160.300 180.671 1.00 78.27  ? 4379 THR A OG1   1 
ATOM   21505 C  CG2   . THR A 1 4379 ? 194.042 160.574 178.280 1.00 71.51  ? 4379 THR A CG2   1 
ATOM   21506 N  N     . LEU A 1 4380 ? 193.712 164.368 179.039 1.00 77.62  ? 4380 LEU A N     1 
ATOM   21507 C  CA    . LEU A 1 4380 ? 193.473 165.466 178.110 1.00 72.80  ? 4380 LEU A CA    1 
ATOM   21508 C  C     . LEU A 1 4380 ? 194.616 166.473 178.135 1.00 73.47  ? 4380 LEU A C     1 
ATOM   21509 O  O     . LEU A 1 4380 ? 194.899 167.123 177.122 1.00 74.95  ? 4380 LEU A O     1 
ATOM   21510 C  CB    . LEU A 1 4380 ? 192.143 166.145 178.439 1.00 71.23  ? 4380 LEU A CB    1 
ATOM   21511 C  CG    . LEU A 1 4380 ? 191.640 167.208 177.461 1.00 71.16  ? 4380 LEU A CG    1 
ATOM   21512 C  CD1   . LEU A 1 4380 ? 191.283 166.579 176.126 1.00 66.86  ? 4380 LEU A CD1   1 
ATOM   21513 C  CD2   . LEU A 1 4380 ? 190.443 167.937 178.048 1.00 67.50  ? 4380 LEU A CD2   1 
ATOM   21514 N  N     . HIS A 1 4381 ? 195.279 166.620 179.284 1.00 73.98  ? 4381 HIS A N     1 
ATOM   21515 C  CA    . HIS A 1 4381 ? 196.397 167.554 179.385 1.00 72.51  ? 4381 HIS A CA    1 
ATOM   21516 C  C     . HIS A 1 4381 ? 197.539 167.145 178.463 1.00 74.88  ? 4381 HIS A C     1 
ATOM   21517 O  O     . HIS A 1 4381 ? 198.111 167.981 177.755 1.00 74.73  ? 4381 HIS A O     1 
ATOM   21518 C  CB    . HIS A 1 4381 ? 196.878 167.638 180.834 1.00 73.99  ? 4381 HIS A CB    1 
ATOM   21519 C  CG    . HIS A 1 4381 ? 197.953 168.657 181.059 1.00 71.69  ? 4381 HIS A CG    1 
ATOM   21520 N  ND1   . HIS A 1 4381 ? 199.241 168.498 180.593 1.00 69.70  ? 4381 HIS A ND1   1 
ATOM   21521 C  CD2   . HIS A 1 4381 ? 197.932 169.847 181.705 1.00 71.48  ? 4381 HIS A CD2   1 
ATOM   21522 C  CE1   . HIS A 1 4381 ? 199.965 169.547 180.939 1.00 70.51  ? 4381 HIS A CE1   1 
ATOM   21523 N  NE2   . HIS A 1 4381 ? 199.194 170.380 181.616 1.00 72.59  ? 4381 HIS A NE2   1 
ATOM   21524 N  N     . THR A 1 4382 ? 197.890 165.857 178.466 1.00 76.79  ? 4382 THR A N     1 
ATOM   21525 C  CA    . THR A 1 4382 ? 198.973 165.385 177.610 1.00 75.45  ? 4382 THR A CA    1 
ATOM   21526 C  C     . THR A 1 4382 ? 198.613 165.523 176.137 1.00 74.79  ? 4382 THR A C     1 
ATOM   21527 O  O     . THR A 1 4382 ? 199.449 165.928 175.321 1.00 72.98  ? 4382 THR A O     1 
ATOM   21528 C  CB    . THR A 1 4382 ? 199.316 163.933 177.943 1.00 77.29  ? 4382 THR A CB    1 
ATOM   21529 O  OG1   . THR A 1 4382 ? 198.174 163.102 177.700 1.00 79.96  ? 4382 THR A OG1   1 
ATOM   21530 C  CG2   . THR A 1 4382 ? 199.727 163.806 179.401 1.00 70.39  ? 4382 THR A CG2   1 
ATOM   21531 N  N     . THR A 1 4383 ? 197.372 165.187 175.777 1.00 73.58  ? 4383 THR A N     1 
ATOM   21532 C  CA    . THR A 1 4383 ? 196.948 165.305 174.385 1.00 71.41  ? 4383 THR A CA    1 
ATOM   21533 C  C     . THR A 1 4383 ? 196.949 166.758 173.929 1.00 66.59  ? 4383 THR A C     1 
ATOM   21534 O  O     . THR A 1 4383 ? 197.397 167.067 172.819 1.00 65.66  ? 4383 THR A O     1 
ATOM   21535 C  CB    . THR A 1 4383 ? 195.561 164.689 174.204 1.00 66.58  ? 4383 THR A CB    1 
ATOM   21536 O  OG1   . THR A 1 4383 ? 195.538 163.378 174.781 1.00 66.67  ? 4383 THR A OG1   1 
ATOM   21537 C  CG2   . THR A 1 4383 ? 195.211 164.590 172.727 1.00 61.12  ? 4383 THR A CG2   1 
ATOM   21538 N  N     . ALA A 1 4384 ? 196.450 167.665 174.772 1.00 64.90  ? 4384 ALA A N     1 
ATOM   21539 C  CA    . ALA A 1 4384 ? 196.410 169.076 174.402 1.00 68.82  ? 4384 ALA A CA    1 
ATOM   21540 C  C     . ALA A 1 4384 ? 197.812 169.658 174.271 1.00 70.19  ? 4384 ALA A C     1 
ATOM   21541 O  O     . ALA A 1 4384 ? 198.084 170.435 173.348 1.00 66.04  ? 4384 ALA A O     1 
ATOM   21542 C  CB    . ALA A 1 4384 ? 195.592 169.863 175.426 1.00 70.53  ? 4384 ALA A CB    1 
ATOM   21543 N  N     . SER A 1 4385 ? 198.715 169.301 175.189 1.00 70.91  ? 4385 SER A N     1 
ATOM   21544 C  CA    . SER A 1 4385 ? 200.088 169.789 175.100 1.00 69.76  ? 4385 SER A CA    1 
ATOM   21545 C  C     . SER A 1 4385 ? 200.812 169.185 173.904 1.00 70.11  ? 4385 SER A C     1 
ATOM   21546 O  O     . SER A 1 4385 ? 201.557 169.880 173.203 1.00 70.98  ? 4385 SER A O     1 
ATOM   21547 C  CB    . SER A 1 4385 ? 200.839 169.484 176.395 1.00 67.81  ? 4385 SER A CB    1 
ATOM   21548 O  OG    . SER A 1 4385 ? 200.153 170.010 177.518 1.00 70.27  ? 4385 SER A OG    1 
ATOM   21549 N  N     . ASN A 1 4386 ? 200.612 167.887 173.658 1.00 68.17  ? 4386 ASN A N     1 
ATOM   21550 C  CA    . ASN A 1 4386 ? 201.217 167.253 172.491 1.00 67.33  ? 4386 ASN A CA    1 
ATOM   21551 C  C     . ASN A 1 4386 ? 200.661 167.839 171.200 1.00 69.67  ? 4386 ASN A C     1 
ATOM   21552 O  O     . ASN A 1 4386 ? 201.402 168.044 170.231 1.00 68.95  ? 4386 ASN A O     1 
ATOM   21553 C  CB    . ASN A 1 4386 ? 200.992 165.741 172.540 1.00 65.79  ? 4386 ASN A CB    1 
ATOM   21554 C  CG    . ASN A 1 4386 ? 201.517 165.030 171.308 1.00 71.33  ? 4386 ASN A CG    1 
ATOM   21555 O  OD1   . ASN A 1 4386 ? 200.836 164.945 170.286 1.00 70.24  ? 4386 ASN A OD1   1 
ATOM   21556 N  ND2   . ASN A 1 4386 ? 202.737 164.513 171.401 1.00 70.44  ? 4386 ASN A ND2   1 
ATOM   21557 N  N     . TRP A 1 4387 ? 199.355 168.109 171.168 1.00 66.50  ? 4387 TRP A N     1 
ATOM   21558 C  CA    . TRP A 1 4387 ? 198.747 168.707 169.984 1.00 63.34  ? 4387 TRP A CA    1 
ATOM   21559 C  C     . TRP A 1 4387 ? 199.306 170.099 169.724 1.00 64.38  ? 4387 TRP A C     1 
ATOM   21560 O  O     . TRP A 1 4387 ? 199.546 170.473 168.571 1.00 66.75  ? 4387 TRP A O     1 
ATOM   21561 C  CB    . TRP A 1 4387 ? 197.230 168.757 170.154 1.00 60.16  ? 4387 TRP A CB    1 
ATOM   21562 C  CG    . TRP A 1 4387 ? 196.553 167.493 169.742 1.00 61.56  ? 4387 TRP A CG    1 
ATOM   21563 C  CD1   . TRP A 1 4387 ? 197.145 166.384 169.213 1.00 64.42  ? 4387 TRP A CD1   1 
ATOM   21564 C  CD2   . TRP A 1 4387 ? 195.162 167.183 169.872 1.00 61.29  ? 4387 TRP A CD2   1 
ATOM   21565 N  NE1   . TRP A 1 4387 ? 196.204 165.412 168.979 1.00 62.63  ? 4387 TRP A NE1   1 
ATOM   21566 C  CE2   . TRP A 1 4387 ? 194.979 165.876 169.379 1.00 61.12  ? 4387 TRP A CE2   1 
ATOM   21567 C  CE3   . TRP A 1 4387 ? 194.052 167.886 170.348 1.00 58.09  ? 4387 TRP A CE3   1 
ATOM   21568 C  CZ2   . TRP A 1 4387 ? 193.731 165.259 169.347 1.00 60.36  ? 4387 TRP A CZ2   1 
ATOM   21569 C  CZ3   . TRP A 1 4387 ? 192.816 167.272 170.316 1.00 58.49  ? 4387 TRP A CZ3   1 
ATOM   21570 C  CH2   . TRP A 1 4387 ? 192.666 165.971 169.821 1.00 61.02  ? 4387 TRP A CH2   1 
ATOM   21571 N  N     . LEU A 1 4388 ? 199.526 170.878 170.786 1.00 66.95  ? 4388 LEU A N     1 
ATOM   21572 C  CA    . LEU A 1 4388 ? 200.082 172.217 170.620 1.00 66.90  ? 4388 LEU A CA    1 
ATOM   21573 C  C     . LEU A 1 4388 ? 201.480 172.163 170.017 1.00 69.24  ? 4388 LEU A C     1 
ATOM   21574 O  O     . LEU A 1 4388 ? 201.900 173.095 169.320 1.00 66.19  ? 4388 LEU A O     1 
ATOM   21575 C  CB    . LEU A 1 4388 ? 200.104 172.944 171.965 1.00 66.55  ? 4388 LEU A CB    1 
ATOM   21576 C  CG    . LEU A 1 4388 ? 198.828 173.690 172.362 1.00 63.89  ? 4388 LEU A CG    1 
ATOM   21577 C  CD1   . LEU A 1 4388 ? 199.028 174.430 173.676 1.00 60.32  ? 4388 LEU A CD1   1 
ATOM   21578 C  CD2   . LEU A 1 4388 ? 198.399 174.650 171.264 1.00 58.02  ? 4388 LEU A CD2   1 
ATOM   21579 N  N     . HIS A 1 4389 ? 202.219 171.082 170.277 1.00 72.73  ? 4389 HIS A N     1 
ATOM   21580 C  CA    . HIS A 1 4389 ? 203.540 170.927 169.677 1.00 71.57  ? 4389 HIS A CA    1 
ATOM   21581 C  C     . HIS A 1 4389 ? 203.442 170.705 168.172 1.00 68.52  ? 4389 HIS A C     1 
ATOM   21582 O  O     . HIS A 1 4389 ? 204.242 171.252 167.403 1.00 73.16  ? 4389 HIS A O     1 
ATOM   21583 C  CB    . HIS A 1 4389 ? 204.285 169.766 170.338 1.00 76.40  ? 4389 HIS A CB    1 
ATOM   21584 C  CG    . HIS A 1 4389 ? 204.590 169.989 171.787 1.00 78.92  ? 4389 HIS A CG    1 
ATOM   21585 N  ND1   . HIS A 1 4389 ? 204.384 169.022 172.747 1.00 79.64  ? 4389 HIS A ND1   1 
ATOM   21586 C  CD2   . HIS A 1 4389 ? 205.085 171.067 172.439 1.00 77.67  ? 4389 HIS A CD2   1 
ATOM   21587 C  CE1   . HIS A 1 4389 ? 204.739 169.494 173.928 1.00 80.86  ? 4389 HIS A CE1   1 
ATOM   21588 N  NE2   . HIS A 1 4389 ? 205.168 170.733 173.769 1.00 82.46  ? 4389 HIS A NE2   1 
ATOM   21589 N  N     . LEU A 1 4390 ? 202.471 169.901 167.734 1.00 65.97  ? 4390 LEU A N     1 
ATOM   21590 C  CA    . LEU A 1 4390 ? 202.358 169.573 166.316 1.00 65.72  ? 4390 LEU A CA    1 
ATOM   21591 C  C     . LEU A 1 4390 ? 201.919 170.782 165.498 1.00 64.52  ? 4390 LEU A C     1 
ATOM   21592 O  O     . LEU A 1 4390 ? 202.499 171.075 164.446 1.00 62.83  ? 4390 LEU A O     1 
ATOM   21593 C  CB    . LEU A 1 4390 ? 201.379 168.414 166.124 1.00 65.10  ? 4390 LEU A CB    1 
ATOM   21594 C  CG    . LEU A 1 4390 ? 201.760 167.082 166.770 1.00 66.27  ? 4390 LEU A CG    1 
ATOM   21595 C  CD1   . LEU A 1 4390 ? 200.530 166.402 167.351 1.00 58.72  ? 4390 LEU A CD1   1 
ATOM   21596 C  CD2   . LEU A 1 4390 ? 202.453 166.176 165.765 1.00 60.64  ? 4390 LEU A CD2   1 
ATOM   21597 N  N     . ILE A 1 4391 ? 200.896 171.489 165.960 1.00 62.41  ? 4391 ILE A N     1 
ATOM   21598 C  CA    . ILE A 1 4391 ? 200.365 172.626 165.200 1.00 59.32  ? 4391 ILE A CA    1 
ATOM   21599 C  C     . ILE A 1 4391 ? 201.378 173.763 165.217 1.00 60.37  ? 4391 ILE A C     1 
ATOM   21600 O  O     . ILE A 1 4391 ? 201.971 174.044 166.275 1.00 64.08  ? 4391 ILE A O     1 
ATOM   21601 C  CB    . ILE A 1 4391 ? 199.022 173.074 165.781 1.00 56.02  ? 4391 ILE A CB    1 
ATOM   21602 C  CG1   . ILE A 1 4391 ? 198.171 171.857 166.151 1.00 57.90  ? 4391 ILE A CG1   1 
ATOM   21603 C  CG2   . ILE A 1 4391 ? 198.281 173.950 164.789 1.00 54.09  ? 4391 ILE A CG2   1 
ATOM   21604 C  CD1   . ILE A 1 4391 ? 196.701 172.164 166.344 1.00 50.72  ? 4391 ILE A CD1   1 
ATOM   21605 N  N     . PRO A 1 4392 ? 201.621 174.437 164.088 1.00 62.64  ? 4392 PRO A N     1 
ATOM   21606 C  CA    . PRO A 1 4392 ? 202.518 175.601 164.098 1.00 61.27  ? 4392 PRO A CA    1 
ATOM   21607 C  C     . PRO A 1 4392 ? 201.954 176.761 164.905 1.00 64.51  ? 4392 PRO A C     1 
ATOM   21608 O  O     . PRO A 1 4392 ? 200.840 176.676 165.432 1.00 69.20  ? 4392 PRO A O     1 
ATOM   21609 C  CB    . PRO A 1 4392 ? 202.646 175.959 162.612 1.00 59.58  ? 4392 PRO A CB    1 
ATOM   21610 C  CG    . PRO A 1 4392 ? 202.308 174.698 161.886 1.00 61.83  ? 4392 PRO A CG    1 
ATOM   21611 C  CD    . PRO A 1 4392 ? 201.260 174.029 162.721 1.00 62.82  ? 4392 PRO A CD    1 
ATOM   21612 N  N     . GLN A 1 4393 ? 202.711 177.855 165.003 1.00 63.41  ? 4393 GLN A N     1 
ATOM   21613 C  CA    . GLN A 1 4393 ? 202.335 178.973 165.855 1.00 64.51  ? 4393 GLN A CA    1 
ATOM   21614 C  C     . GLN A 1 4393 ? 202.137 180.291 165.121 1.00 65.64  ? 4393 GLN A C     1 
ATOM   21615 O  O     . GLN A 1 4393 ? 201.416 181.152 165.637 1.00 64.78  ? 4393 GLN A O     1 
ATOM   21616 C  CB    . GLN A 1 4393 ? 203.389 179.184 166.954 1.00 66.00  ? 4393 GLN A CB    1 
ATOM   21617 C  CG    . GLN A 1 4393 ? 204.203 177.942 167.280 1.00 65.57  ? 4393 GLN A CG    1 
ATOM   21618 C  CD    . GLN A 1 4393 ? 204.791 177.978 168.676 1.00 66.75  ? 4393 GLN A CD    1 
ATOM   21619 O  OE1   . GLN A 1 4393 ? 205.482 178.926 169.046 1.00 65.14  ? 4393 GLN A OE1   1 
ATOM   21620 N  NE2   . GLN A 1 4393 ? 204.517 176.941 169.459 1.00 61.87  ? 4393 GLN A NE2   1 
ATOM   21621 N  N     . THR A 1 4394 ? 202.739 180.479 163.949 1.00 67.83  ? 4394 THR A N     1 
ATOM   21622 C  CA    . THR A 1 4394 ? 202.693 181.758 163.254 1.00 73.55  ? 4394 THR A CA    1 
ATOM   21623 C  C     . THR A 1 4394 ? 202.194 181.572 161.829 1.00 68.65  ? 4394 THR A C     1 
ATOM   21624 O  O     . THR A 1 4394 ? 202.527 180.585 161.166 1.00 68.14  ? 4394 THR A O     1 
ATOM   21625 C  CB    . THR A 1 4394 ? 204.074 182.429 163.232 1.00 74.87  ? 4394 THR A CB    1 
ATOM   21626 O  OG1   . THR A 1 4394 ? 205.033 181.539 162.647 1.00 78.43  ? 4394 THR A OG1   1 
ATOM   21627 C  CG2   . THR A 1 4394 ? 204.517 182.789 164.642 1.00 68.65  ? 4394 THR A CG2   1 
ATOM   21628 N  N     . LEU A 1 4395 ? 201.389 182.529 161.368 1.00 62.83  ? 4395 LEU A N     1 
ATOM   21629 C  CA    . LEU A 1 4395 ? 200.927 182.548 159.981 1.00 68.41  ? 4395 LEU A CA    1 
ATOM   21630 C  C     . LEU A 1 4395 ? 200.532 183.982 159.649 1.00 71.97  ? 4395 LEU A C     1 
ATOM   21631 O  O     . LEU A 1 4395 ? 199.508 184.468 160.137 1.00 70.24  ? 4395 LEU A O     1 
ATOM   21632 C  CB    . LEU A 1 4395 ? 199.760 181.590 159.779 1.00 68.31  ? 4395 LEU A CB    1 
ATOM   21633 C  CG    . LEU A 1 4395 ? 199.251 181.457 158.343 1.00 62.40  ? 4395 LEU A CG    1 
ATOM   21634 C  CD1   . LEU A 1 4395 ? 200.409 181.197 157.394 1.00 65.70  ? 4395 LEU A CD1   1 
ATOM   21635 C  CD2   . LEU A 1 4395 ? 198.214 180.352 158.237 1.00 59.53  ? 4395 LEU A CD2   1 
ATOM   21636 N  N     . SER A 1 4396 ? 201.336 184.648 158.824 1.00 71.98  ? 4396 SER A N     1 
ATOM   21637 C  CA    . SER A 1 4396 ? 201.149 186.062 158.532 1.00 71.83  ? 4396 SER A CA    1 
ATOM   21638 C  C     . SER A 1 4396 ? 200.223 186.259 157.339 1.00 76.17  ? 4396 SER A C     1 
ATOM   21639 O  O     . SER A 1 4396 ? 200.326 185.554 156.332 1.00 80.40  ? 4396 SER A O     1 
ATOM   21640 C  CB    . SER A 1 4396 ? 202.496 186.733 158.259 1.00 68.80  ? 4396 SER A CB    1 
ATOM   21641 O  OG    . SER A 1 4396 ? 203.180 186.085 157.201 1.00 73.58  ? 4396 SER A OG    1 
ATOM   21642 N  N     . HIS A 1 4397 ? 199.320 187.230 157.460 1.00 78.29  ? 4397 HIS A N     1 
ATOM   21643 C  CA    . HIS A 1 4397 ? 198.407 187.557 156.374 1.00 81.26  ? 4397 HIS A CA    1 
ATOM   21644 C  C     . HIS A 1 4397 ? 199.160 188.150 155.188 1.00 83.35  ? 4397 HIS A C     1 
ATOM   21645 O  O     . HIS A 1 4397 ? 200.200 188.797 155.340 1.00 84.05  ? 4397 HIS A O     1 
ATOM   21646 C  CB    . HIS A 1 4397 ? 197.341 188.546 156.847 1.00 78.42  ? 4397 HIS A CB    1 
ATOM   21647 C  CG    . HIS A 1 4397 ? 196.193 187.905 157.562 1.00 78.50  ? 4397 HIS A CG    1 
ATOM   21648 N  ND1   . HIS A 1 4397 ? 195.043 188.591 157.887 1.00 75.75  ? 4397 HIS A ND1   1 
ATOM   21649 C  CD2   . HIS A 1 4397 ? 196.016 186.641 158.013 1.00 79.62  ? 4397 HIS A CD2   1 
ATOM   21650 C  CE1   . HIS A 1 4397 ? 194.208 187.778 158.508 1.00 75.37  ? 4397 HIS A CE1   1 
ATOM   21651 N  NE2   . HIS A 1 4397 ? 194.774 186.588 158.598 1.00 76.83  ? 4397 HIS A NE2   1 
ATOM   21652 N  N     . LEU A 1 4398 ? 198.622 187.918 153.994 1.00 81.13  ? 4398 LEU A N     1 
ATOM   21653 C  CA    . LEU A 1 4398 ? 199.190 188.502 152.788 1.00 80.11  ? 4398 LEU A CA    1 
ATOM   21654 C  C     . LEU A 1 4398 ? 198.997 190.014 152.786 1.00 83.95  ? 4398 LEU A C     1 
ATOM   21655 O  O     . LEU A 1 4398 ? 198.054 190.545 153.380 1.00 85.89  ? 4398 LEU A O     1 
ATOM   21656 C  CB    . LEU A 1 4398 ? 198.551 187.884 151.545 1.00 76.15  ? 4398 LEU A CB    1 
ATOM   21657 C  CG    . LEU A 1 4398 ? 198.865 186.412 151.268 1.00 75.18  ? 4398 LEU A CG    1 
ATOM   21658 C  CD1   . LEU A 1 4398 ? 198.649 186.082 149.799 1.00 73.24  ? 4398 LEU A CD1   1 
ATOM   21659 C  CD2   . LEU A 1 4398 ? 200.286 186.068 151.691 1.00 77.47  ? 4398 LEU A CD2   1 
ATOM   21660 N  N     . LYS A 1 4399 ? 199.903 190.710 152.105 1.00 81.55  ? 4399 LYS A N     1 
ATOM   21661 C  CA    . LYS A 1 4399 ? 199.918 192.167 152.081 1.00 80.22  ? 4399 LYS A CA    1 
ATOM   21662 C  C     . LYS A 1 4399 ? 199.233 192.677 150.821 1.00 78.12  ? 4399 LYS A C     1 
ATOM   21663 O  O     . LYS A 1 4399 ? 199.563 192.248 149.711 1.00 80.43  ? 4399 LYS A O     1 
ATOM   21664 C  CB    . LYS A 1 4399 ? 201.351 192.697 152.150 1.00 76.46  ? 4399 LYS A CB    1 
ATOM   21665 C  CG    . LYS A 1 4399 ? 201.486 194.017 152.889 1.00 73.79  ? 4399 LYS A CG    1 
ATOM   21666 C  CD    . LYS A 1 4399 ? 202.807 194.694 152.566 1.00 71.80  ? 4399 LYS A CD    1 
ATOM   21667 C  CE    . LYS A 1 4399 ? 202.737 195.436 151.242 1.00 72.50  ? 4399 LYS A CE    1 
ATOM   21668 N  NZ    . LYS A 1 4399 ? 203.829 196.439 151.111 1.00 71.22  ? 4399 LYS A NZ    1 
ATOM   21669 N  N     . ARG A 1 4400 ? 198.286 193.596 150.998 1.00 75.25  ? 4400 ARG A N     1 
ATOM   21670 C  CA    . ARG A 1 4400 ? 197.589 194.197 149.871 1.00 76.87  ? 4400 ARG A CA    1 
ATOM   21671 C  C     . ARG A 1 4400 ? 198.483 195.216 149.175 1.00 77.99  ? 4400 ARG A C     1 
ATOM   21672 O  O     . ARG A 1 4400 ? 199.100 196.064 149.828 1.00 79.65  ? 4400 ARG A O     1 
ATOM   21673 C  CB    . ARG A 1 4400 ? 196.294 194.864 150.334 1.00 73.19  ? 4400 ARG A CB    1 
ATOM   21674 C  CG    . ARG A 1 4400 ? 195.271 193.914 150.936 1.00 70.57  ? 4400 ARG A CG    1 
ATOM   21675 C  CD    . ARG A 1 4400 ? 194.720 192.979 149.876 1.00 72.93  ? 4400 ARG A CD    1 
ATOM   21676 N  NE    . ARG A 1 4400 ? 193.671 192.104 150.387 1.00 75.77  ? 4400 ARG A NE    1 
ATOM   21677 C  CZ    . ARG A 1 4400 ? 192.376 192.384 150.337 1.00 65.88  ? 4400 ARG A CZ    1 
ATOM   21678 N  NH1   . ARG A 1 4400 ? 191.932 193.510 149.804 1.00 46.42  ? 4400 ARG A NH1   1 
ATOM   21679 N  NH2   . ARG A 1 4400 ? 191.504 191.509 150.830 1.00 64.88  ? 4400 ARG A NH2   1 
ATOM   21680 N  N     . THR A 1 4401 ? 198.550 195.127 147.849 1.00 76.80  ? 4401 THR A N     1 
ATOM   21681 C  CA    . THR A 1 4401 ? 199.289 196.075 147.030 1.00 78.17  ? 4401 THR A CA    1 
ATOM   21682 C  C     . THR A 1 4401 ? 198.441 196.407 145.810 1.00 78.06  ? 4401 THR A C     1 
ATOM   21683 O  O     . THR A 1 4401 ? 197.595 195.611 145.394 1.00 79.26  ? 4401 THR A O     1 
ATOM   21684 C  CB    . THR A 1 4401 ? 200.659 195.512 146.610 1.00 75.75  ? 4401 THR A CB    1 
ATOM   21685 O  OG1   . THR A 1 4401 ? 201.319 194.959 147.755 1.00 75.65  ? 4401 THR A OG1   1 
ATOM   21686 C  CG2   . THR A 1 4401 ? 201.543 196.604 146.019 1.00 63.93  ? 4401 THR A CG2   1 
ATOM   21687 N  N     . VAL A 1 4402 ? 198.672 197.593 145.241 1.00 80.58  ? 4402 VAL A N     1 
ATOM   21688 C  CA    . VAL A 1 4402 ? 197.847 198.062 144.129 1.00 78.00  ? 4402 VAL A CA    1 
ATOM   21689 C  C     . VAL A 1 4402 ? 197.954 197.116 142.937 1.00 79.70  ? 4402 VAL A C     1 
ATOM   21690 O  O     . VAL A 1 4402 ? 196.969 196.877 142.228 1.00 77.22  ? 4402 VAL A O     1 
ATOM   21691 C  CB    . VAL A 1 4402 ? 198.227 199.507 143.752 1.00 76.63  ? 4402 VAL A CB    1 
ATOM   21692 C  CG1   . VAL A 1 4402 ? 197.861 200.456 144.880 1.00 74.62  ? 4402 VAL A CG1   1 
ATOM   21693 C  CG2   . VAL A 1 4402 ? 199.712 199.610 143.438 1.00 76.77  ? 4402 VAL A CG2   1 
ATOM   21694 N  N     . GLU A 1 4403 ? 199.143 196.563 142.695 1.00 81.18  ? 4403 GLU A N     1 
ATOM   21695 C  CA    . GLU A 1 4403 ? 199.324 195.625 141.595 1.00 77.87  ? 4403 GLU A CA    1 
ATOM   21696 C  C     . GLU A 1 4403 ? 199.119 194.174 142.009 1.00 78.09  ? 4403 GLU A C     1 
ATOM   21697 O  O     . GLU A 1 4403 ? 198.908 193.322 141.138 1.00 75.97  ? 4403 GLU A O     1 
ATOM   21698 C  CB    . GLU A 1 4403 ? 200.717 195.794 140.976 1.00 80.06  ? 4403 GLU A CB    1 
ATOM   21699 C  CG    . GLU A 1 4403 ? 201.874 195.443 141.897 1.00 84.04  ? 4403 GLU A CG    1 
ATOM   21700 C  CD    . GLU A 1 4403 ? 202.410 194.046 141.650 1.00 88.50  ? 4403 GLU A CD    1 
ATOM   21701 O  OE1   . GLU A 1 4403 ? 202.098 193.468 140.587 1.00 91.87  ? 4403 GLU A OE1   1 
ATOM   21702 O  OE2   . GLU A 1 4403 ? 203.151 193.529 142.512 1.00 83.83  ? 4403 GLU A OE2   1 
ATOM   21703 N  N     . ASN A 1 4404 ? 199.175 193.873 143.309 1.00 76.81  ? 4404 ASN A N     1 
ATOM   21704 C  CA    . ASN A 1 4404 ? 198.904 192.514 143.767 1.00 69.88  ? 4404 ASN A CA    1 
ATOM   21705 C  C     . ASN A 1 4404 ? 197.442 192.135 143.571 1.00 66.99  ? 4404 ASN A C     1 
ATOM   21706 O  O     . ASN A 1 4404 ? 197.138 190.969 143.296 1.00 65.64  ? 4404 ASN A O     1 
ATOM   21707 C  CB    . ASN A 1 4404 ? 199.293 192.362 145.238 1.00 68.32  ? 4404 ASN A CB    1 
ATOM   21708 C  CG    . ASN A 1 4404 ? 200.789 192.232 145.435 1.00 68.45  ? 4404 ASN A CG    1 
ATOM   21709 O  OD1   . ASN A 1 4404 ? 201.577 192.824 144.699 1.00 69.59  ? 4404 ASN A OD1   1 
ATOM   21710 N  ND2   . ASN A 1 4404 ? 201.189 191.455 146.434 1.00 66.91  ? 4404 ASN A ND2   1 
ATOM   21711 N  N     . ILE A 1 4405 ? 196.528 193.099 143.717 1.00 67.83  ? 4405 ILE A N     1 
ATOM   21712 C  CA    . ILE A 1 4405 ? 195.103 192.817 143.567 1.00 67.81  ? 4405 ILE A CA    1 
ATOM   21713 C  C     . ILE A 1 4405 ? 194.789 192.339 142.157 1.00 69.22  ? 4405 ILE A C     1 
ATOM   21714 O  O     . ILE A 1 4405 ? 193.938 191.462 141.964 1.00 67.94  ? 4405 ILE A O     1 
ATOM   21715 C  CB    . ILE A 1 4405 ? 194.271 194.061 143.939 1.00 63.12  ? 4405 ILE A CB    1 
ATOM   21716 C  CG1   . ILE A 1 4405 ? 194.615 194.530 145.351 1.00 66.16  ? 4405 ILE A CG1   1 
ATOM   21717 C  CG2   . ILE A 1 4405 ? 192.791 193.752 143.866 1.00 54.90  ? 4405 ILE A CG2   1 
ATOM   21718 C  CD1   . ILE A 1 4405 ? 194.561 193.431 146.379 1.00 69.04  ? 4405 ILE A CD1   1 
ATOM   21719 N  N     . LYS A 1 4406 ? 195.465 192.898 141.151 1.00 67.35  ? 4406 LYS A N     1 
ATOM   21720 C  CA    . LYS A 1 4406 ? 195.233 192.502 139.767 1.00 67.02  ? 4406 LYS A CA    1 
ATOM   21721 C  C     . LYS A 1 4406 ? 195.632 191.059 139.487 1.00 64.09  ? 4406 LYS A C     1 
ATOM   21722 O  O     . LYS A 1 4406 ? 195.226 190.514 138.455 1.00 60.05  ? 4406 LYS A O     1 
ATOM   21723 C  CB    . LYS A 1 4406 ? 195.990 193.439 138.825 1.00 69.50  ? 4406 LYS A CB    1 
ATOM   21724 C  CG    . LYS A 1 4406 ? 195.623 194.905 138.988 1.00 74.69  ? 4406 LYS A CG    1 
ATOM   21725 C  CD    . LYS A 1 4406 ? 196.533 195.799 138.161 1.00 75.55  ? 4406 LYS A CD    1 
ATOM   21726 C  CE    . LYS A 1 4406 ? 196.903 197.061 138.923 1.00 74.75  ? 4406 LYS A CE    1 
ATOM   21727 N  NZ    . LYS A 1 4406 ? 197.947 197.853 138.216 1.00 74.54  ? 4406 LYS A NZ    1 
ATOM   21728 N  N     . ASP A 1 4407 ? 196.407 190.430 140.369 1.00 67.68  ? 4407 ASP A N     1 
ATOM   21729 C  CA    . ASP A 1 4407 ? 196.814 189.044 140.179 1.00 65.04  ? 4407 ASP A CA    1 
ATOM   21730 C  C     . ASP A 1 4407 ? 195.754 188.116 140.756 1.00 63.89  ? 4407 ASP A C     1 
ATOM   21731 O  O     . ASP A 1 4407 ? 195.528 188.137 141.973 1.00 62.96  ? 4407 ASP A O     1 
ATOM   21732 C  CB    . ASP A 1 4407 ? 198.152 188.780 140.847 1.00 61.81  ? 4407 ASP A CB    1 
ATOM   21733 C  CG    . ASP A 1 4407 ? 198.793 187.488 140.380 1.00 65.84  ? 4407 ASP A CG    1 
ATOM   21734 O  OD1   . ASP A 1 4407 ? 198.289 186.886 139.409 1.00 66.89  ? 4407 ASP A OD1   1 
ATOM   21735 O  OD2   . ASP A 1 4407 ? 199.804 187.073 140.984 1.00 71.09  ? 4407 ASP A OD2   1 
ATOM   21736 N  N     . PRO A 1 4408 ? 195.083 187.303 139.937 1.00 65.77  ? 4408 PRO A N     1 
ATOM   21737 C  CA    . PRO A 1 4408 ? 194.102 186.356 140.491 1.00 63.91  ? 4408 PRO A CA    1 
ATOM   21738 C  C     . PRO A 1 4408 ? 194.710 185.344 141.444 1.00 64.55  ? 4408 PRO A C     1 
ATOM   21739 O  O     . PRO A 1 4408 ? 194.035 184.914 142.388 1.00 67.61  ? 4408 PRO A O     1 
ATOM   21740 C  CB    . PRO A 1 4408 ? 193.527 185.678 139.241 1.00 55.20  ? 4408 PRO A CB    1 
ATOM   21741 C  CG    . PRO A 1 4408 ? 194.577 185.857 138.197 1.00 53.37  ? 4408 PRO A CG    1 
ATOM   21742 C  CD    . PRO A 1 4408 ? 195.198 187.189 138.474 1.00 56.59  ? 4408 PRO A CD    1 
ATOM   21743 N  N     . LEU A 1 4409 ? 195.963 184.940 141.219 1.00 62.62  ? 4409 LEU A N     1 
ATOM   21744 C  CA    . LEU A 1 4409 ? 196.607 183.994 142.123 1.00 65.27  ? 4409 LEU A CA    1 
ATOM   21745 C  C     . LEU A 1 4409 ? 196.747 184.583 143.521 1.00 69.46  ? 4409 LEU A C     1 
ATOM   21746 O  O     . LEU A 1 4409 ? 196.494 183.900 144.520 1.00 72.57  ? 4409 LEU A O     1 
ATOM   21747 C  CB    . LEU A 1 4409 ? 197.972 183.587 141.569 1.00 62.84  ? 4409 LEU A CB    1 
ATOM   21748 C  CG    . LEU A 1 4409 ? 198.450 182.178 141.920 1.00 64.96  ? 4409 LEU A CG    1 
ATOM   21749 C  CD1   . LEU A 1 4409 ? 197.559 181.131 141.271 1.00 55.92  ? 4409 LEU A CD1   1 
ATOM   21750 C  CD2   . LEU A 1 4409 ? 199.894 181.989 141.498 1.00 69.11  ? 4409 LEU A CD2   1 
ATOM   21751 N  N     . PHE A 1 4410 ? 197.145 185.853 143.611 1.00 67.97  ? 4410 PHE A N     1 
ATOM   21752 C  CA    . PHE A 1 4410 ? 197.192 186.522 144.906 1.00 67.32  ? 4410 PHE A CA    1 
ATOM   21753 C  C     . PHE A 1 4410 ? 195.790 186.722 145.468 1.00 64.04  ? 4410 PHE A C     1 
ATOM   21754 O  O     . PHE A 1 4410 ? 195.594 186.702 146.689 1.00 64.40  ? 4410 PHE A O     1 
ATOM   21755 C  CB    . PHE A 1 4410 ? 197.920 187.860 144.776 1.00 67.16  ? 4410 PHE A CB    1 
ATOM   21756 C  CG    . PHE A 1 4410 ? 198.451 188.390 146.076 1.00 68.94  ? 4410 PHE A CG    1 
ATOM   21757 C  CD1   . PHE A 1 4410 ? 197.673 189.208 146.877 1.00 69.26  ? 4410 PHE A CD1   1 
ATOM   21758 C  CD2   . PHE A 1 4410 ? 199.732 188.073 146.494 1.00 68.51  ? 4410 PHE A CD2   1 
ATOM   21759 C  CE1   . PHE A 1 4410 ? 198.162 189.696 148.073 1.00 71.99  ? 4410 PHE A CE1   1 
ATOM   21760 C  CE2   . PHE A 1 4410 ? 200.227 188.558 147.687 1.00 72.21  ? 4410 PHE A CE2   1 
ATOM   21761 C  CZ    . PHE A 1 4410 ? 199.441 189.371 148.478 1.00 76.31  ? 4410 PHE A CZ    1 
ATOM   21762 N  N     . ARG A 1 4411 ? 194.805 186.924 144.589 1.00 68.14  ? 4411 ARG A N     1 
ATOM   21763 C  CA    . ARG A 1 4411 ? 193.423 187.070 145.031 1.00 66.18  ? 4411 ARG A CA    1 
ATOM   21764 C  C     . ARG A 1 4411 ? 192.912 185.803 145.705 1.00 69.00  ? 4411 ARG A C     1 
ATOM   21765 O  O     . ARG A 1 4411 ? 192.194 185.879 146.708 1.00 67.31  ? 4411 ARG A O     1 
ATOM   21766 C  CB    . ARG A 1 4411 ? 192.533 187.437 143.843 1.00 54.23  ? 4411 ARG A CB    1 
ATOM   21767 C  CG    . ARG A 1 4411 ? 192.659 188.885 143.404 1.00 57.44  ? 4411 ARG A CG    1 
ATOM   21768 C  CD    . ARG A 1 4411 ? 191.449 189.332 142.601 1.00 57.64  ? 4411 ARG A CD    1 
ATOM   21769 N  NE    . ARG A 1 4411 ? 191.402 188.714 141.281 1.00 53.98  ? 4411 ARG A NE    1 
ATOM   21770 C  CZ    . ARG A 1 4411 ? 191.793 189.310 140.163 1.00 51.10  ? 4411 ARG A CZ    1 
ATOM   21771 N  NH1   . ARG A 1 4411 ? 192.265 190.546 140.167 1.00 54.32  ? 4411 ARG A NH1   1 
ATOM   21772 N  NH2   . ARG A 1 4411 ? 191.706 188.650 139.012 1.00 50.76  ? 4411 ARG A NH2   1 
ATOM   21773 N  N     . PHE A 1 4412 ? 193.256 184.636 145.165 1.00 70.73  ? 4412 PHE A N     1 
ATOM   21774 C  CA    . PHE A 1 4412 ? 192.885 183.369 145.782 1.00 68.64  ? 4412 PHE A CA    1 
ATOM   21775 C  C     . PHE A 1 4412 ? 193.715 183.057 147.021 1.00 67.32  ? 4412 PHE A C     1 
ATOM   21776 O  O     . PHE A 1 4412 ? 193.172 182.590 148.028 1.00 68.01  ? 4412 PHE A O     1 
ATOM   21777 C  CB    . PHE A 1 4412 ? 193.026 182.229 144.771 1.00 66.39  ? 4412 PHE A CB    1 
ATOM   21778 C  CG    . PHE A 1 4412 ? 193.152 180.874 145.403 1.00 60.83  ? 4412 PHE A CG    1 
ATOM   21779 C  CD1   . PHE A 1 4412 ? 192.049 180.251 145.963 1.00 57.59  ? 4412 PHE A CD1   1 
ATOM   21780 C  CD2   . PHE A 1 4412 ? 194.374 180.224 145.442 1.00 55.77  ? 4412 PHE A CD2   1 
ATOM   21781 C  CE1   . PHE A 1 4412 ? 192.163 179.006 146.548 1.00 57.30  ? 4412 PHE A CE1   1 
ATOM   21782 C  CE2   . PHE A 1 4412 ? 194.494 178.980 146.027 1.00 57.58  ? 4412 PHE A CE2   1 
ATOM   21783 C  CZ    . PHE A 1 4412 ? 193.386 178.370 146.579 1.00 59.10  ? 4412 PHE A CZ    1 
ATOM   21784 N  N     . PHE A 1 4413 ? 195.026 183.304 146.965 1.00 61.29  ? 4413 PHE A N     1 
ATOM   21785 C  CA    . PHE A 1 4413 ? 195.899 182.920 148.069 1.00 61.08  ? 4413 PHE A CA    1 
ATOM   21786 C  C     . PHE A 1 4413 ? 195.633 183.741 149.323 1.00 69.03  ? 4413 PHE A C     1 
ATOM   21787 O  O     . PHE A 1 4413 ? 195.787 183.226 150.436 1.00 73.55  ? 4413 PHE A O     1 
ATOM   21788 C  CB    . PHE A 1 4413 ? 197.365 183.045 147.654 1.00 67.37  ? 4413 PHE A CB    1 
ATOM   21789 C  CG    . PHE A 1 4413 ? 197.905 181.823 146.968 1.00 70.91  ? 4413 PHE A CG    1 
ATOM   21790 C  CD1   . PHE A 1 4413 ? 197.703 180.565 147.511 1.00 68.96  ? 4413 PHE A CD1   1 
ATOM   21791 C  CD2   . PHE A 1 4413 ? 198.624 181.930 145.789 1.00 70.03  ? 4413 PHE A CD2   1 
ATOM   21792 C  CE1   . PHE A 1 4413 ? 198.199 179.437 146.887 1.00 63.57  ? 4413 PHE A CE1   1 
ATOM   21793 C  CE2   . PHE A 1 4413 ? 199.124 180.805 145.162 1.00 66.68  ? 4413 PHE A CE2   1 
ATOM   21794 C  CZ    . PHE A 1 4413 ? 198.911 179.557 145.712 1.00 61.22  ? 4413 PHE A CZ    1 
ATOM   21795 N  N     . GLU A 1 4414 ? 195.244 185.010 149.175 1.00 71.31  ? 4414 GLU A N     1 
ATOM   21796 C  CA    . GLU A 1 4414 ? 194.986 185.834 150.352 1.00 72.20  ? 4414 GLU A CA    1 
ATOM   21797 C  C     . GLU A 1 4414 ? 193.828 185.278 151.172 1.00 68.71  ? 4414 GLU A C     1 
ATOM   21798 O  O     . GLU A 1 4414 ? 193.834 185.370 152.405 1.00 68.64  ? 4414 GLU A O     1 
ATOM   21799 C  CB    . GLU A 1 4414 ? 194.721 187.285 149.942 1.00 69.71  ? 4414 GLU A CB    1 
ATOM   21800 C  CG    . GLU A 1 4414 ? 193.460 187.501 149.127 1.00 71.13  ? 4414 GLU A CG    1 
ATOM   21801 C  CD    . GLU A 1 4414 ? 193.282 188.945 148.704 1.00 77.57  ? 4414 GLU A CD    1 
ATOM   21802 O  OE1   . GLU A 1 4414 ? 194.156 189.774 149.031 1.00 80.95  ? 4414 GLU A OE1   1 
ATOM   21803 O  OE2   . GLU A 1 4414 ? 192.268 189.250 148.042 1.00 74.41  ? 4414 GLU A OE2   1 
ATOM   21804 N  N     . ARG A 1 4415 ? 192.827 184.696 150.507 1.00 62.83  ? 4415 ARG A N     1 
ATOM   21805 C  CA    . ARG A 1 4415 ? 191.751 184.026 151.230 1.00 59.44  ? 4415 ARG A CA    1 
ATOM   21806 C  C     . ARG A 1 4415 ? 192.267 182.799 151.971 1.00 66.66  ? 4415 ARG A C     1 
ATOM   21807 O  O     . ARG A 1 4415 ? 191.824 182.507 153.088 1.00 70.21  ? 4415 ARG A O     1 
ATOM   21808 C  CB    . ARG A 1 4415 ? 190.633 183.635 150.264 1.00 52.66  ? 4415 ARG A CB    1 
ATOM   21809 C  CG    . ARG A 1 4415 ? 189.725 184.784 149.858 1.00 51.58  ? 4415 ARG A CG    1 
ATOM   21810 C  CD    . ARG A 1 4415 ? 188.537 184.283 149.053 1.00 47.43  ? 4415 ARG A CD    1 
ATOM   21811 N  NE    . ARG A 1 4415 ? 187.979 183.059 149.617 1.00 50.50  ? 4415 ARG A NE    1 
ATOM   21812 C  CZ    . ARG A 1 4415 ? 186.879 182.464 149.178 1.00 48.02  ? 4415 ARG A CZ    1 
ATOM   21813 N  NH1   . ARG A 1 4415 ? 186.186 182.953 148.162 1.00 47.52  ? 4415 ARG A NH1   1 
ATOM   21814 N  NH2   . ARG A 1 4415 ? 186.462 181.350 149.774 1.00 49.09  ? 4415 ARG A NH2   1 
ATOM   21815 N  N     . GLU A 1 4416 ? 193.198 182.064 151.358 1.00 64.84  ? 4416 GLU A N     1 
ATOM   21816 C  CA    . GLU A 1 4416 ? 193.712 180.842 151.970 1.00 66.84  ? 4416 GLU A CA    1 
ATOM   21817 C  C     . GLU A 1 4416 ? 194.425 181.138 153.283 1.00 66.12  ? 4416 GLU A C     1 
ATOM   21818 O  O     . GLU A 1 4416 ? 194.173 180.484 154.302 1.00 68.54  ? 4416 GLU A O     1 
ATOM   21819 C  CB    . GLU A 1 4416 ? 194.652 180.129 150.997 1.00 67.71  ? 4416 GLU A CB    1 
ATOM   21820 C  CG    . GLU A 1 4416 ? 193.947 179.322 149.922 1.00 66.55  ? 4416 GLU A CG    1 
ATOM   21821 C  CD    . GLU A 1 4416 ? 192.923 178.359 150.490 1.00 63.28  ? 4416 GLU A CD    1 
ATOM   21822 O  OE1   . GLU A 1 4416 ? 193.286 177.561 151.379 1.00 63.11  ? 4416 GLU A OE1   1 
ATOM   21823 O  OE2   . GLU A 1 4416 ? 191.756 178.400 150.046 1.00 60.71  ? 4416 GLU A OE2   1 
ATOM   21824 N  N     . VAL A 1 4417 ? 195.324 182.123 153.278 1.00 65.50  ? 4417 VAL A N     1 
ATOM   21825 C  CA    . VAL A 1 4417 ? 196.061 182.458 154.493 1.00 65.50  ? 4417 VAL A CA    1 
ATOM   21826 C  C     . VAL A 1 4417 ? 195.138 183.093 155.525 1.00 68.65  ? 4417 VAL A C     1 
ATOM   21827 O  O     . VAL A 1 4417 ? 195.266 182.839 156.729 1.00 67.47  ? 4417 VAL A O     1 
ATOM   21828 C  CB    . VAL A 1 4417 ? 197.255 183.370 154.162 1.00 68.90  ? 4417 VAL A CB    1 
ATOM   21829 C  CG1   . VAL A 1 4417 ? 198.296 183.287 155.258 1.00 74.82  ? 4417 VAL A CG1   1 
ATOM   21830 C  CG2   . VAL A 1 4417 ? 197.863 182.980 152.828 1.00 66.58  ? 4417 VAL A CG2   1 
ATOM   21831 N  N     . LYS A 1 4418 ? 194.200 183.931 155.077 1.00 67.50  ? 4418 LYS A N     1 
ATOM   21832 C  CA    . LYS A 1 4418 ? 193.280 184.581 156.006 1.00 68.71  ? 4418 LYS A CA    1 
ATOM   21833 C  C     . LYS A 1 4418 ? 192.433 183.554 156.746 1.00 71.58  ? 4418 LYS A C     1 
ATOM   21834 O  O     . LYS A 1 4418 ? 192.241 183.650 157.964 1.00 71.36  ? 4418 LYS A O     1 
ATOM   21835 C  CB    . LYS A 1 4418 ? 192.393 185.574 155.256 1.00 65.25  ? 4418 LYS A CB    1 
ATOM   21836 C  CG    . LYS A 1 4418 ? 191.889 186.726 156.109 1.00 69.21  ? 4418 LYS A CG    1 
ATOM   21837 C  CD    . LYS A 1 4418 ? 191.320 187.840 155.245 1.00 67.10  ? 4418 LYS A CD    1 
ATOM   21838 C  CE    . LYS A 1 4418 ? 192.303 188.252 154.158 1.00 70.38  ? 4418 LYS A CE    1 
ATOM   21839 N  NZ    . LYS A 1 4418 ? 191.749 189.318 153.278 1.00 71.02  ? 4418 LYS A NZ    1 
ATOM   21840 N  N     . MET A 1 4419 ? 191.913 182.561 156.022 1.00 66.54  ? 4419 MET A N     1 
ATOM   21841 C  CA    . MET A 1 4419 ? 191.195 181.472 156.676 1.00 64.34  ? 4419 MET A CA    1 
ATOM   21842 C  C     . MET A 1 4419 ? 192.130 180.647 157.551 1.00 62.74  ? 4419 MET A C     1 
ATOM   21843 O  O     . MET A 1 4419 ? 191.769 180.260 158.668 1.00 62.04  ? 4419 MET A O     1 
ATOM   21844 C  CB    . MET A 1 4419 ? 190.519 180.587 155.631 1.00 61.38  ? 4419 MET A CB    1 
ATOM   21845 C  CG    . MET A 1 4419 ? 189.005 180.713 155.591 1.00 58.43  ? 4419 MET A CG    1 
ATOM   21846 S  SD    . MET A 1 4419 ? 188.264 179.707 154.291 1.00 77.70  ? 4419 MET A SD    1 
ATOM   21847 C  CE    . MET A 1 4419 ? 188.897 180.522 152.827 1.00 64.80  ? 4419 MET A CE    1 
ATOM   21848 N  N     . GLY A 1 4420 ? 193.336 180.364 157.056 1.00 61.24  ? 4420 GLY A N     1 
ATOM   21849 C  CA    . GLY A 1 4420 ? 194.269 179.554 157.823 1.00 61.66  ? 4420 GLY A CA    1 
ATOM   21850 C  C     . GLY A 1 4420 ? 194.752 180.241 159.086 1.00 60.44  ? 4420 GLY A C     1 
ATOM   21851 O  O     . GLY A 1 4420 ? 194.805 179.628 160.154 1.00 54.46  ? 4420 GLY A O     1 
ATOM   21852 N  N     . ALA A 1 4421 ? 195.114 181.522 158.982 1.00 66.41  ? 4421 ALA A N     1 
ATOM   21853 C  CA    . ALA A 1 4421 ? 195.621 182.242 160.146 1.00 65.41  ? 4421 ALA A CA    1 
ATOM   21854 C  C     . ALA A 1 4421 ? 194.539 182.421 161.203 1.00 62.99  ? 4421 ALA A C     1 
ATOM   21855 O  O     . ALA A 1 4421 ? 194.809 182.289 162.402 1.00 61.87  ? 4421 ALA A O     1 
ATOM   21856 C  CB    . ALA A 1 4421 ? 196.188 183.597 159.724 1.00 68.78  ? 4421 ALA A CB    1 
ATOM   21857 N  N     . LYS A 1 4422 ? 193.314 182.734 160.777 1.00 62.67  ? 4422 LYS A N     1 
ATOM   21858 C  CA    . LYS A 1 4422 ? 192.212 182.873 161.722 1.00 62.05  ? 4422 LYS A CA    1 
ATOM   21859 C  C     . LYS A 1 4422 ? 191.937 181.559 162.442 1.00 60.93  ? 4422 LYS A C     1 
ATOM   21860 O  O     . LYS A 1 4422 ? 191.866 181.515 163.675 1.00 59.38  ? 4422 LYS A O     1 
ATOM   21861 C  CB    . LYS A 1 4422 ? 190.959 183.358 160.993 1.00 62.91  ? 4422 LYS A CB    1 
ATOM   21862 C  CG    . LYS A 1 4422 ? 189.847 183.837 161.910 1.00 60.74  ? 4422 LYS A CG    1 
ATOM   21863 C  CD    . LYS A 1 4422 ? 189.929 185.333 162.151 1.00 64.72  ? 4422 LYS A CD    1 
ATOM   21864 C  CE    . LYS A 1 4422 ? 189.176 185.723 163.411 1.00 68.70  ? 4422 LYS A CE    1 
ATOM   21865 N  NZ    . LYS A 1 4422 ? 189.613 184.920 164.586 1.00 70.89  ? 4422 LYS A NZ    1 
ATOM   21866 N  N     . LEU A 1 4423 ? 191.790 180.471 161.682 1.00 58.42  ? 4423 LEU A N     1 
ATOM   21867 C  CA    . LEU A 1 4423 ? 191.470 179.180 162.284 1.00 56.54  ? 4423 LEU A CA    1 
ATOM   21868 C  C     . LEU A 1 4423 ? 192.621 178.692 163.159 1.00 53.00  ? 4423 LEU A C     1 
ATOM   21869 O  O     . LEU A 1 4423 ? 192.396 178.097 164.219 1.00 54.67  ? 4423 LEU A O     1 
ATOM   21870 C  CB    . LEU A 1 4423 ? 191.133 178.171 161.181 1.00 57.31  ? 4423 LEU A CB    1 
ATOM   21871 C  CG    . LEU A 1 4423 ? 191.049 176.653 161.390 1.00 53.23  ? 4423 LEU A CG    1 
ATOM   21872 C  CD1   . LEU A 1 4423 ? 190.376 176.277 162.707 1.00 50.45  ? 4423 LEU A CD1   1 
ATOM   21873 C  CD2   . LEU A 1 4423 ? 190.336 175.997 160.213 1.00 53.36  ? 4423 LEU A CD2   1 
ATOM   21874 N  N     . LEU A 1 4424 ? 193.862 178.948 162.736 1.00 55.23  ? 4424 LEU A N     1 
ATOM   21875 C  CA    . LEU A 1 4424 ? 195.018 178.574 163.548 1.00 55.53  ? 4424 LEU A CA    1 
ATOM   21876 C  C     . LEU A 1 4424 ? 194.999 179.279 164.899 1.00 55.64  ? 4424 LEU A C     1 
ATOM   21877 O  O     . LEU A 1 4424 ? 195.307 178.670 165.930 1.00 55.55  ? 4424 LEU A O     1 
ATOM   21878 C  CB    . LEU A 1 4424 ? 196.310 178.892 162.793 1.00 53.38  ? 4424 LEU A CB    1 
ATOM   21879 C  CG    . LEU A 1 4424 ? 197.625 178.855 163.573 1.00 53.56  ? 4424 LEU A CG    1 
ATOM   21880 C  CD1   . LEU A 1 4424 ? 197.936 177.445 164.028 1.00 56.81  ? 4424 LEU A CD1   1 
ATOM   21881 C  CD2   . LEU A 1 4424 ? 198.764 179.402 162.728 1.00 55.38  ? 4424 LEU A CD2   1 
ATOM   21882 N  N     . GLN A 1 4425 ? 194.640 180.564 164.912 1.00 55.46  ? 4425 GLN A N     1 
ATOM   21883 C  CA    . GLN A 1 4425 ? 194.600 181.313 166.164 1.00 56.69  ? 4425 GLN A CA    1 
ATOM   21884 C  C     . GLN A 1 4425 ? 193.543 180.757 167.112 1.00 58.20  ? 4425 GLN A C     1 
ATOM   21885 O  O     . GLN A 1 4425 ? 193.785 180.635 168.319 1.00 57.45  ? 4425 GLN A O     1 
ATOM   21886 C  CB    . GLN A 1 4425 ? 194.346 182.792 165.875 1.00 59.49  ? 4425 GLN A CB    1 
ATOM   21887 C  CG    . GLN A 1 4425 ? 193.878 183.600 167.073 1.00 63.69  ? 4425 GLN A CG    1 
ATOM   21888 C  CD    . GLN A 1 4425 ? 193.114 184.846 166.669 1.00 67.72  ? 4425 GLN A CD    1 
ATOM   21889 O  OE1   . GLN A 1 4425 ? 193.094 185.222 165.497 1.00 66.28  ? 4425 GLN A OE1   1 
ATOM   21890 N  NE2   . GLN A 1 4425 ? 192.482 185.494 167.640 1.00 65.18  ? 4425 GLN A NE2   1 
ATOM   21891 N  N     . ASP A 1 4426 ? 192.390 180.381 166.554 1.00 56.13  ? 4426 ASP A N     1 
ATOM   21892 C  CA    . ASP A 1 4426 ? 191.270 179.862 167.387 1.00 54.12  ? 4426 ASP A CA    1 
ATOM   21893 C  C     . ASP A 1 4426 ? 191.645 178.510 168.000 1.00 55.91  ? 4426 ASP A C     1 
ATOM   21894 O  O     . ASP A 1 4426 ? 191.592 178.394 169.242 1.00 57.74  ? 4426 ASP A O     1 
ATOM   21895 C  CB    . ASP A 1 4426 ? 189.992 179.771 166.569 1.00 57.72  ? 4426 ASP A CB    1 
ATOM   21896 C  CG    . ASP A 1 4426 ? 189.614 181.036 165.812 1.00 66.79  ? 4426 ASP A CG    1 
ATOM   21897 O  OD1   . ASP A 1 4426 ? 190.345 182.040 165.945 1.00 64.16  ? 4426 ASP A OD1   1 
ATOM   21898 O  OD2   . ASP A 1 4426 ? 188.596 181.004 165.089 1.00 68.48  ? 4426 ASP A OD2   1 
ATOM   21899 N  N     . VAL A 1 4427 ? 192.015 177.530 167.170 1.00 52.08  ? 4427 VAL A N     1 
ATOM   21900 C  CA    . VAL A 1 4427 ? 192.295 176.155 167.687 1.00 47.53  ? 4427 VAL A CA    1 
ATOM   21901 C  C     . VAL A 1 4427 ? 193.386 176.218 168.768 1.00 52.20  ? 4427 VAL A C     1 
ATOM   21902 O  O     . VAL A 1 4427 ? 193.179 175.623 169.848 1.00 56.03  ? 4427 VAL A O     1 
ATOM   21903 C  CB    . VAL A 1 4427 ? 192.694 175.194 166.550 1.00 45.29  ? 4427 VAL A CB    1 
ATOM   21904 C  CG1   . VAL A 1 4427 ? 193.250 173.881 167.087 1.00 48.72  ? 4427 VAL A CG1   1 
ATOM   21905 C  CG2   . VAL A 1 4427 ? 191.535 174.937 165.596 1.00 44.06  ? 4427 VAL A CG2   1 
ATOM   21906 N  N     . ARG A 1 4428 ? 194.496 176.908 168.492 1.00 56.46  ? 4428 ARG A N     1 
ATOM   21907 C  CA    . ARG A 1 4428 ? 195.622 176.950 169.464 1.00 59.43  ? 4428 ARG A CA    1 
ATOM   21908 C  C     . ARG A 1 4428 ? 195.132 177.589 170.772 1.00 56.01  ? 4428 ARG A C     1 
ATOM   21909 O  O     . ARG A 1 4428 ? 195.445 177.042 171.849 1.00 56.04  ? 4428 ARG A O     1 
ATOM   21910 C  CB    . ARG A 1 4428 ? 196.815 177.726 168.895 1.00 60.58  ? 4428 ARG A CB    1 
ATOM   21911 C  CG    . ARG A 1 4428 ? 197.445 177.097 167.661 1.00 59.25  ? 4428 ARG A CG    1 
ATOM   21912 C  CD    . ARG A 1 4428 ? 198.727 177.817 167.275 1.00 63.77  ? 4428 ARG A CD    1 
ATOM   21913 N  NE    . ARG A 1 4428 ? 199.817 177.605 168.234 1.00 65.72  ? 4428 ARG A NE    1 
ATOM   21914 C  CZ    . ARG A 1 4428 ? 200.366 176.429 168.517 1.00 66.99  ? 4428 ARG A CZ    1 
ATOM   21915 N  NH1   . ARG A 1 4428 ? 200.038 175.357 167.820 1.00 66.29  ? 4428 ARG A NH1   1 
ATOM   21916 N  NH2   . ARG A 1 4428 ? 201.248 176.332 169.495 1.00 66.66  ? 4428 ARG A NH2   1 
ATOM   21917 N  N     . GLN A 1 4429 ? 194.388 178.694 170.672 1.00 56.32  ? 4429 GLN A N     1 
ATOM   21918 C  CA    . GLN A 1 4429 ? 193.858 179.381 171.879 1.00 56.57  ? 4429 GLN A CA    1 
ATOM   21919 C  C     . GLN A 1 4429 ? 192.946 178.410 172.644 1.00 56.10  ? 4429 GLN A C     1 
ATOM   21920 O  O     . GLN A 1 4429 ? 193.050 178.349 173.888 1.00 52.02  ? 4429 GLN A O     1 
ATOM   21921 C  CB    . GLN A 1 4429 ? 193.103 180.641 171.456 1.00 51.80  ? 4429 GLN A CB    1 
ATOM   21922 C  CG    . GLN A 1 4429 ? 193.014 181.711 172.539 1.00 57.18  ? 4429 GLN A CG    1 
ATOM   21923 C  CD    . GLN A 1 4429 ? 192.319 181.238 173.796 1.00 63.61  ? 4429 GLN A CD    1 
ATOM   21924 O  OE1   . GLN A 1 4429 ? 191.150 180.838 173.776 1.00 62.82  ? 4429 GLN A OE1   1 
ATOM   21925 N  NE2   . GLN A 1 4429 ? 193.040 181.276 174.907 1.00 58.40  ? 4429 GLN A NE2   1 
ATOM   21926 N  N     . ASP A 1 4430 ? 192.096 177.675 171.921 1.00 52.24  ? 4430 ASP A N     1 
ATOM   21927 C  CA    . ASP A 1 4430 ? 191.179 176.697 172.567 1.00 54.60  ? 4430 ASP A CA    1 
ATOM   21928 C  C     . ASP A 1 4430 ? 192.009 175.663 173.332 1.00 55.30  ? 4430 ASP A C     1 
ATOM   21929 O  O     . ASP A 1 4430 ? 191.710 175.424 174.522 1.00 58.49  ? 4430 ASP A O     1 
ATOM   21930 C  CB    . ASP A 1 4430 ? 190.257 176.045 171.548 1.00 55.79  ? 4430 ASP A CB    1 
ATOM   21931 C  CG    . ASP A 1 4430 ? 189.302 176.990 170.833 1.00 61.51  ? 4430 ASP A CG    1 
ATOM   21932 O  OD1   . ASP A 1 4430 ? 188.521 176.504 169.988 1.00 61.65  ? 4430 ASP A OD1   1 
ATOM   21933 O  OD2   . ASP A 1 4430 ? 189.346 178.202 171.129 1.00 64.66  ? 4430 ASP A OD2   1 
ATOM   21934 N  N     . LEU A 1 4431 ? 193.021 175.087 172.677 1.00 55.87  ? 4431 LEU A N     1 
ATOM   21935 C  CA    . LEU A 1 4431 ? 193.895 174.086 173.341 1.00 55.85  ? 4431 LEU A CA    1 
ATOM   21936 C  C     . LEU A 1 4431 ? 194.581 174.756 174.539 1.00 58.08  ? 4431 LEU A C     1 
ATOM   21937 O  O     . LEU A 1 4431 ? 194.603 174.146 175.628 1.00 55.40  ? 4431 LEU A O     1 
ATOM   21938 C  CB    . LEU A 1 4431 ? 194.911 173.542 172.338 1.00 56.62  ? 4431 LEU A CB    1 
ATOM   21939 C  CG    . LEU A 1 4431 ? 194.330 172.801 171.131 1.00 52.53  ? 4431 LEU A CG    1 
ATOM   21940 C  CD1   . LEU A 1 4431 ? 195.439 172.333 170.204 1.00 57.00  ? 4431 LEU A CD1   1 
ATOM   21941 C  CD2   . LEU A 1 4431 ? 193.480 171.627 171.585 1.00 52.39  ? 4431 LEU A CD2   1 
ATOM   21942 N  N     . ALA A 1 4432 ? 195.108 175.967 174.340 1.00 62.02  ? 4432 ALA A N     1 
ATOM   21943 C  CA    . ALA A 1 4432 ? 195.749 176.712 175.448 1.00 58.47  ? 4432 ALA A CA    1 
ATOM   21944 C  C     . ALA A 1 4432 ? 194.801 176.731 176.648 1.00 60.87  ? 4432 ALA A C     1 
ATOM   21945 O  O     . ALA A 1 4432 ? 195.221 176.333 177.756 1.00 60.08  ? 4432 ALA A O     1 
ATOM   21946 C  CB    . ALA A 1 4432 ? 196.097 178.110 174.990 1.00 50.66  ? 4432 ALA A CB    1 
ATOM   21947 N  N     . ASP A 1 4433 ? 193.558 177.171 176.430 1.00 62.73  ? 4433 ASP A N     1 
ATOM   21948 C  CA    . ASP A 1 4433 ? 192.577 177.187 177.509 1.00 59.59  ? 4433 ASP A CA    1 
ATOM   21949 C  C     . ASP A 1 4433 ? 192.397 175.798 178.109 1.00 56.68  ? 4433 ASP A C     1 
ATOM   21950 O  O     . ASP A 1 4433 ? 192.232 175.655 179.326 1.00 58.00  ? 4433 ASP A O     1 
ATOM   21951 C  CB    . ASP A 1 4433 ? 191.242 177.727 176.996 1.00 56.61  ? 4433 ASP A CB    1 
ATOM   21952 C  CG    . ASP A 1 4433 ? 191.288 179.214 176.710 1.00 64.03  ? 4433 ASP A CG    1 
ATOM   21953 O  OD1   . ASP A 1 4433 ? 192.338 179.838 176.967 1.00 64.11  ? 4433 ASP A OD1   1 
ATOM   21954 O  OD2   . ASP A 1 4433 ? 190.274 179.760 176.225 1.00 62.45  ? 4433 ASP A OD2   1 
ATOM   21955 N  N     . VAL A 1 4434 ? 192.417 174.762 177.265 1.00 57.39  ? 4434 VAL A N     1 
ATOM   21956 C  CA    . VAL A 1 4434 ? 192.220 173.396 177.747 1.00 57.35  ? 4434 VAL A CA    1 
ATOM   21957 C  C     . VAL A 1 4434 ? 193.342 172.990 178.696 1.00 61.47  ? 4434 VAL A C     1 
ATOM   21958 O  O     . VAL A 1 4434 ? 193.092 172.418 179.763 1.00 62.31  ? 4434 VAL A O     1 
ATOM   21959 C  CB    . VAL A 1 4434 ? 192.102 172.425 176.557 1.00 58.81  ? 4434 VAL A CB    1 
ATOM   21960 C  CG1   . VAL A 1 4434 ? 192.154 170.987 177.037 1.00 61.16  ? 4434 VAL A CG1   1 
ATOM   21961 C  CG2   . VAL A 1 4434 ? 190.813 172.684 175.792 1.00 56.21  ? 4434 VAL A CG2   1 
ATOM   21962 N  N     . VAL A 1 4435 ? 194.594 173.280 178.327 1.00 62.99  ? 4435 VAL A N     1 
ATOM   21963 C  CA    . VAL A 1 4435 ? 195.714 172.975 179.216 1.00 63.83  ? 4435 VAL A CA    1 
ATOM   21964 C  C     . VAL A 1 4435 ? 195.605 173.781 180.502 1.00 65.36  ? 4435 VAL A C     1 
ATOM   21965 O  O     . VAL A 1 4435 ? 195.953 173.300 181.587 1.00 68.13  ? 4435 VAL A O     1 
ATOM   21966 C  CB    . VAL A 1 4435 ? 197.058 173.224 178.507 1.00 60.85  ? 4435 VAL A CB    1 
ATOM   21967 C  CG1   . VAL A 1 4435 ? 198.164 172.442 179.192 1.00 62.13  ? 4435 VAL A CG1   1 
ATOM   21968 C  CG2   . VAL A 1 4435 ? 196.974 172.831 177.048 1.00 64.93  ? 4435 VAL A CG2   1 
ATOM   21969 N  N     . GLN A 1 4436 ? 195.130 175.024 180.400 1.00 67.46  ? 4436 GLN A N     1 
ATOM   21970 C  CA    . GLN A 1 4436 ? 194.942 175.847 181.590 1.00 63.00  ? 4436 GLN A CA    1 
ATOM   21971 C  C     . GLN A 1 4436 ? 193.904 175.234 182.523 1.00 61.40  ? 4436 GLN A C     1 
ATOM   21972 O  O     . GLN A 1 4436 ? 194.080 175.234 183.747 1.00 63.57  ? 4436 GLN A O     1 
ATOM   21973 C  CB    . GLN A 1 4436 ? 194.541 177.264 181.181 1.00 59.80  ? 4436 GLN A CB    1 
ATOM   21974 C  CG    . GLN A 1 4436 ? 194.627 178.288 182.296 1.00 66.58  ? 4436 GLN A CG    1 
ATOM   21975 C  CD    . GLN A 1 4436 ? 194.377 179.701 181.807 1.00 74.99  ? 4436 GLN A CD    1 
ATOM   21976 O  OE1   . GLN A 1 4436 ? 194.185 179.932 180.613 1.00 70.43  ? 4436 GLN A OE1   1 
ATOM   21977 N  NE2   . GLN A 1 4436 ? 194.379 180.656 182.730 1.00 75.23  ? 4436 GLN A NE2   1 
ATOM   21978 N  N     . VAL A 1 4437 ? 192.810 174.710 181.962 1.00 58.33  ? 4437 VAL A N     1 
ATOM   21979 C  CA    . VAL A 1 4437 ? 191.816 174.011 182.774 1.00 58.11  ? 4437 VAL A CA    1 
ATOM   21980 C  C     . VAL A 1 4437 ? 192.408 172.739 183.364 1.00 64.16  ? 4437 VAL A C     1 
ATOM   21981 O  O     . VAL A 1 4437 ? 192.194 172.423 184.541 1.00 64.56  ? 4437 VAL A O     1 
ATOM   21982 C  CB    . VAL A 1 4437 ? 190.556 173.712 181.941 1.00 54.89  ? 4437 VAL A CB    1 
ATOM   21983 C  CG1   . VAL A 1 4437 ? 189.582 172.856 182.736 1.00 53.54  ? 4437 VAL A CG1   1 
ATOM   21984 C  CG2   . VAL A 1 4437 ? 189.891 175.001 181.510 1.00 51.80  ? 4437 VAL A CG2   1 
ATOM   21985 N  N     . CYS A 1 4438 ? 193.162 171.987 182.556 1.00 67.85  ? 4438 CYS A N     1 
ATOM   21986 C  CA    . CYS A 1 4438 ? 193.729 170.729 183.028 1.00 65.71  ? 4438 CYS A CA    1 
ATOM   21987 C  C     . CYS A 1 4438 ? 194.730 170.947 184.155 1.00 66.14  ? 4438 CYS A C     1 
ATOM   21988 O  O     . CYS A 1 4438 ? 194.976 170.034 184.951 1.00 70.48  ? 4438 CYS A O     1 
ATOM   21989 C  CB    . CYS A 1 4438 ? 194.385 169.983 181.866 1.00 71.78  ? 4438 CYS A CB    1 
ATOM   21990 S  SG    . CYS A 1 4438 ? 193.219 169.335 180.646 1.00 76.86  ? 4438 CYS A SG    1 
ATOM   21991 N  N     . GLU A 1 4439 ? 195.324 172.133 184.233 1.00 67.92  ? 4439 GLU A N     1 
ATOM   21992 C  CA    . GLU A 1 4439 ? 196.176 172.495 185.357 1.00 67.57  ? 4439 GLU A CA    1 
ATOM   21993 C  C     . GLU A 1 4439 ? 195.421 173.238 186.451 1.00 69.09  ? 4439 GLU A C     1 
ATOM   21994 O  O     . GLU A 1 4439 ? 196.018 173.569 187.481 1.00 68.16  ? 4439 GLU A O     1 
ATOM   21995 C  CB    . GLU A 1 4439 ? 197.357 173.341 184.873 1.00 69.04  ? 4439 GLU A CB    1 
ATOM   21996 C  CG    . GLU A 1 4439 ? 198.433 172.540 184.160 1.00 72.22  ? 4439 GLU A CG    1 
ATOM   21997 C  CD    . GLU A 1 4439 ? 199.261 173.386 183.214 1.00 77.31  ? 4439 GLU A CD    1 
ATOM   21998 O  OE1   . GLU A 1 4439 ? 199.412 174.597 183.477 1.00 78.71  ? 4439 GLU A OE1   1 
ATOM   21999 O  OE2   . GLU A 1 4439 ? 199.758 172.839 182.207 1.00 76.91  ? 4439 GLU A OE2   1 
ATOM   22000 N  N     . GLY A 1 4440 ? 194.132 173.506 186.255 1.00 66.74  ? 4440 GLY A N     1 
ATOM   22001 C  CA    . GLY A 1 4440 ? 193.326 174.167 187.261 1.00 62.51  ? 4440 GLY A CA    1 
ATOM   22002 C  C     . GLY A 1 4440 ? 193.545 175.656 187.393 1.00 64.75  ? 4440 GLY A C     1 
ATOM   22003 O  O     . GLY A 1 4440 ? 193.023 176.259 188.337 1.00 62.76  ? 4440 GLY A O     1 
ATOM   22004 N  N     . LYS A 1 4441 ? 194.301 176.271 186.481 1.00 67.86  ? 4441 LYS A N     1 
ATOM   22005 C  CA    . LYS A 1 4441 ? 194.584 177.698 186.601 1.00 71.92  ? 4441 LYS A CA    1 
ATOM   22006 C  C     . LYS A 1 4441 ? 193.357 178.550 186.300 1.00 70.28  ? 4441 LYS A C     1 
ATOM   22007 O  O     . LYS A 1 4441 ? 193.189 179.619 186.898 1.00 74.17  ? 4441 LYS A O     1 
ATOM   22008 C  CB    . LYS A 1 4441 ? 195.740 178.082 185.678 1.00 71.72  ? 4441 LYS A CB    1 
ATOM   22009 C  CG    . LYS A 1 4441 ? 197.054 177.398 186.016 1.00 69.29  ? 4441 LYS A CG    1 
ATOM   22010 C  CD    . LYS A 1 4441 ? 198.096 177.634 184.936 1.00 74.66  ? 4441 LYS A CD    1 
ATOM   22011 C  CE    . LYS A 1 4441 ? 199.487 177.262 185.422 1.00 76.15  ? 4441 LYS A CE    1 
ATOM   22012 N  NZ    . LYS A 1 4441 ? 200.500 177.367 184.336 1.00 78.10  ? 4441 LYS A NZ    1 
ATOM   22013 N  N     . LYS A 1 4442 ? 192.495 178.104 185.389 1.00 63.15  ? 4442 LYS A N     1 
ATOM   22014 C  CA    . LYS A 1 4442 ? 191.294 178.844 185.032 1.00 63.34  ? 4442 LYS A CA    1 
ATOM   22015 C  C     . LYS A 1 4442 ? 190.068 177.966 185.244 1.00 60.14  ? 4442 LYS A C     1 
ATOM   22016 O  O     . LYS A 1 4442 ? 190.136 176.736 185.177 1.00 57.51  ? 4442 LYS A O     1 
ATOM   22017 C  CB    . LYS A 1 4442 ? 191.342 179.344 183.580 1.00 62.40  ? 4442 LYS A CB    1 
ATOM   22018 C  CG    . LYS A 1 4442 ? 191.003 178.289 182.541 1.00 56.83  ? 4442 LYS A CG    1 
ATOM   22019 C  CD    . LYS A 1 4442 ? 190.974 178.876 181.139 1.00 57.80  ? 4442 LYS A CD    1 
ATOM   22020 C  CE    . LYS A 1 4442 ? 189.851 179.890 180.987 1.00 62.06  ? 4442 LYS A CE    1 
ATOM   22021 N  NZ    . LYS A 1 4442 ? 189.788 180.444 179.606 1.00 57.58  ? 4442 LYS A NZ    1 
ATOM   22022 N  N     . LYS A 1 4443 ? 188.943 178.620 185.513 1.00 61.64  ? 4443 LYS A N     1 
ATOM   22023 C  CA    . LYS A 1 4443 ? 187.689 177.918 185.739 1.00 54.16  ? 4443 LYS A CA    1 
ATOM   22024 C  C     . LYS A 1 4443 ? 187.050 177.514 184.416 1.00 50.33  ? 4443 LYS A C     1 
ATOM   22025 O  O     . LYS A 1 4443 ? 187.260 178.148 183.378 1.00 47.92  ? 4443 LYS A O     1 
ATOM   22026 C  CB    . LYS A 1 4443 ? 186.722 178.790 186.539 1.00 59.50  ? 4443 LYS A CB    1 
ATOM   22027 C  CG    . LYS A 1 4443 ? 185.780 178.007 187.441 1.00 58.20  ? 4443 LYS A CG    1 
ATOM   22028 C  CD    . LYS A 1 4443 ? 184.486 178.767 187.691 1.00 60.56  ? 4443 LYS A CD    1 
ATOM   22029 C  CE    . LYS A 1 4443 ? 184.746 180.236 187.987 1.00 62.70  ? 4443 LYS A CE    1 
ATOM   22030 N  NZ    . LYS A 1 4443 ? 184.999 180.477 189.434 1.00 59.49  ? 4443 LYS A NZ    1 
ATOM   22031 N  N     . GLN A 1 4444 ? 186.262 176.444 184.465 1.00 48.55  ? 4444 GLN A N     1 
ATOM   22032 C  CA    . GLN A 1 4444 ? 185.578 175.944 183.282 1.00 44.26  ? 4444 GLN A CA    1 
ATOM   22033 C  C     . GLN A 1 4444 ? 184.380 176.827 182.953 1.00 45.80  ? 4444 GLN A C     1 
ATOM   22034 O  O     . GLN A 1 4444 ? 183.659 177.269 183.852 1.00 46.00  ? 4444 GLN A O     1 
ATOM   22035 C  CB    . GLN A 1 4444 ? 185.128 174.501 183.501 1.00 44.43  ? 4444 GLN A CB    1 
ATOM   22036 C  CG    . GLN A 1 4444 ? 185.218 173.623 182.268 1.00 47.70  ? 4444 GLN A CG    1 
ATOM   22037 C  CD    . GLN A 1 4444 ? 185.763 172.243 182.578 1.00 55.81  ? 4444 GLN A CD    1 
ATOM   22038 O  OE1   . GLN A 1 4444 ? 186.371 172.025 183.625 1.00 58.12  ? 4444 GLN A OE1   1 
ATOM   22039 N  NE2   . GLN A 1 4444 ? 185.539 171.301 181.670 1.00 49.81  ? 4444 GLN A NE2   1 
ATOM   22040 N  N     . THR A 1 4445 ? 184.173 177.081 181.666 1.00 44.88  ? 4445 THR A N     1 
ATOM   22041 C  CA    . THR A 1 4445 ? 183.046 177.859 181.173 1.00 32.97  ? 4445 THR A CA    1 
ATOM   22042 C  C     . THR A 1 4445 ? 182.118 176.957 180.366 1.00 34.84  ? 4445 THR A C     1 
ATOM   22043 O  O     . THR A 1 4445 ? 182.386 175.770 180.163 1.00 35.94  ? 4445 THR A O     1 
ATOM   22044 C  CB    . THR A 1 4445 ? 183.531 179.042 180.332 1.00 30.35  ? 4445 THR A CB    1 
ATOM   22045 O  OG1   . THR A 1 4445 ? 184.034 178.567 179.078 1.00 39.03  ? 4445 THR A OG1   1 
ATOM   22046 C  CG2   . THR A 1 4445 ? 184.631 179.799 181.061 1.00 28.90  ? 4445 THR A CG2   1 
ATOM   22047 N  N     . ASN A 1 4446 ? 181.005 177.534 179.907 1.00 35.92  ? 4446 ASN A N     1 
ATOM   22048 C  CA    . ASN A 1 4446 ? 180.046 176.767 179.118 1.00 33.89  ? 4446 ASN A CA    1 
ATOM   22049 C  C     . ASN A 1 4446 ? 180.659 176.308 177.801 1.00 38.01  ? 4446 ASN A C     1 
ATOM   22050 O  O     . ASN A 1 4446 ? 180.511 175.147 177.405 1.00 39.48  ? 4446 ASN A O     1 
ATOM   22051 C  CB    . ASN A 1 4446 ? 178.788 177.599 178.866 1.00 28.03  ? 4446 ASN A CB    1 
ATOM   22052 C  CG    . ASN A 1 4446 ? 177.867 177.639 180.067 1.00 26.94  ? 4446 ASN A CG    1 
ATOM   22053 O  OD1   . ASN A 1 4446 ? 177.780 176.675 180.827 1.00 27.71  ? 4446 ASN A OD1   1 
ATOM   22054 N  ND2   . ASN A 1 4446 ? 177.173 178.756 180.244 1.00 20.37  ? 4446 ASN A ND2   1 
ATOM   22055 N  N     . TYR A 1 4447 ? 181.351 177.212 177.104 1.00 42.19  ? 4447 TYR A N     1 
ATOM   22056 C  CA    . TYR A 1 4447 ? 182.016 176.831 175.863 1.00 42.49  ? 4447 TYR A CA    1 
ATOM   22057 C  C     . TYR A 1 4447 ? 183.164 175.868 176.130 1.00 42.67  ? 4447 TYR A C     1 
ATOM   22058 O  O     . TYR A 1 4447 ? 183.377 174.916 175.370 1.00 44.67  ? 4447 TYR A O     1 
ATOM   22059 C  CB    . TYR A 1 4447 ? 182.518 178.075 175.131 1.00 45.29  ? 4447 TYR A CB    1 
ATOM   22060 C  CG    . TYR A 1 4447 ? 183.409 177.762 173.952 1.00 52.42  ? 4447 TYR A CG    1 
ATOM   22061 C  CD1   . TYR A 1 4447 ? 182.880 177.234 172.782 1.00 50.23  ? 4447 TYR A CD1   1 
ATOM   22062 C  CD2   . TYR A 1 4447 ? 184.777 177.992 174.008 1.00 55.72  ? 4447 TYR A CD2   1 
ATOM   22063 C  CE1   . TYR A 1 4447 ? 183.687 176.943 171.701 1.00 57.69  ? 4447 TYR A CE1   1 
ATOM   22064 C  CE2   . TYR A 1 4447 ? 185.593 177.704 172.929 1.00 53.59  ? 4447 TYR A CE2   1 
ATOM   22065 C  CZ    . TYR A 1 4447 ? 185.042 177.180 171.779 1.00 61.66  ? 4447 TYR A CZ    1 
ATOM   22066 O  OH    . TYR A 1 4447 ? 185.843 176.891 170.700 1.00 67.56  ? 4447 TYR A OH    1 
ATOM   22067 N  N     . LEU A 1 4448 ? 183.918 176.106 177.205 1.00 43.22  ? 4448 LEU A N     1 
ATOM   22068 C  CA    . LEU A 1 4448 ? 185.029 175.224 177.544 1.00 42.89  ? 4448 LEU A CA    1 
ATOM   22069 C  C     . LEU A 1 4448 ? 184.532 173.842 177.950 1.00 44.84  ? 4448 LEU A C     1 
ATOM   22070 O  O     . LEU A 1 4448 ? 185.177 172.830 177.651 1.00 48.33  ? 4448 LEU A O     1 
ATOM   22071 C  CB    . LEU A 1 4448 ? 185.868 175.852 178.655 1.00 37.68  ? 4448 LEU A CB    1 
ATOM   22072 C  CG    . LEU A 1 4448 ? 187.252 176.348 178.237 1.00 43.26  ? 4448 LEU A CG    1 
ATOM   22073 C  CD1   . LEU A 1 4448 ? 187.148 177.255 177.023 1.00 47.42  ? 4448 LEU A CD1   1 
ATOM   22074 C  CD2   . LEU A 1 4448 ? 187.911 177.086 179.385 1.00 43.37  ? 4448 LEU A CD2   1 
ATOM   22075 N  N     . ARG A 1 4449 ? 183.390 173.779 178.639 1.00 43.97  ? 4449 ARG A N     1 
ATOM   22076 C  CA    . ARG A 1 4449 ? 182.792 172.488 178.965 1.00 42.28  ? 4449 ARG A CA    1 
ATOM   22077 C  C     . ARG A 1 4449 ? 182.406 171.733 177.700 1.00 48.19  ? 4449 ARG A C     1 
ATOM   22078 O  O     . ARG A 1 4449 ? 182.634 170.522 177.590 1.00 52.60  ? 4449 ARG A O     1 
ATOM   22079 C  CB    . ARG A 1 4449 ? 181.570 172.687 179.864 1.00 43.66  ? 4449 ARG A CB    1 
ATOM   22080 C  CG    . ARG A 1 4449 ? 181.875 172.661 181.350 1.00 39.71  ? 4449 ARG A CG    1 
ATOM   22081 C  CD    . ARG A 1 4449 ? 180.603 172.742 182.176 1.00 35.89  ? 4449 ARG A CD    1 
ATOM   22082 N  NE    . ARG A 1 4449 ? 180.060 174.095 182.209 1.00 34.53  ? 4449 ARG A NE    1 
ATOM   22083 C  CZ    . ARG A 1 4449 ? 180.445 175.036 183.061 1.00 34.14  ? 4449 ARG A CZ    1 
ATOM   22084 N  NH1   . ARG A 1 4449 ? 181.381 174.806 183.967 1.00 38.06  ? 4449 ARG A NH1   1 
ATOM   22085 N  NH2   . ARG A 1 4449 ? 179.876 176.237 183.003 1.00 25.92  ? 4449 ARG A NH2   1 
ATOM   22086 N  N     . THR A 1 4450 ? 181.813 172.435 176.732 1.00 45.28  ? 4450 THR A N     1 
ATOM   22087 C  CA    . THR A 1 4450 ? 181.452 171.800 175.469 1.00 51.02  ? 4450 THR A CA    1 
ATOM   22088 C  C     . THR A 1 4450 ? 182.690 171.363 174.696 1.00 54.59  ? 4450 THR A C     1 
ATOM   22089 O  O     . THR A 1 4450 ? 182.732 170.253 174.152 1.00 53.54  ? 4450 THR A O     1 
ATOM   22090 C  CB    . THR A 1 4450 ? 180.605 172.754 174.626 1.00 48.94  ? 4450 THR A CB    1 
ATOM   22091 O  OG1   . THR A 1 4450 ? 179.472 173.190 175.388 1.00 48.51  ? 4450 THR A OG1   1 
ATOM   22092 C  CG2   . THR A 1 4450 ? 180.120 172.062 173.361 1.00 45.51  ? 4450 THR A CG2   1 
ATOM   22093 N  N     . LEU A 1 4451 ? 183.709 172.224 174.637 1.00 50.82  ? 4451 LEU A N     1 
ATOM   22094 C  CA    . LEU A 1 4451 ? 184.922 171.890 173.897 1.00 49.18  ? 4451 LEU A CA    1 
ATOM   22095 C  C     . LEU A 1 4451 ? 185.645 170.704 174.521 1.00 54.31  ? 4451 LEU A C     1 
ATOM   22096 O  O     . LEU A 1 4451 ? 186.110 169.805 173.810 1.00 61.13  ? 4451 LEU A O     1 
ATOM   22097 C  CB    . LEU A 1 4451 ? 185.845 173.106 173.834 1.00 52.26  ? 4451 LEU A CB    1 
ATOM   22098 C  CG    . LEU A 1 4451 ? 187.220 172.888 173.200 1.00 51.92  ? 4451 LEU A CG    1 
ATOM   22099 C  CD1   . LEU A 1 4451 ? 187.086 172.650 171.708 1.00 49.44  ? 4451 LEU A CD1   1 
ATOM   22100 C  CD2   . LEU A 1 4451 ? 188.132 174.071 173.480 1.00 55.78  ? 4451 LEU A CD2   1 
ATOM   22101 N  N     . ILE A 1 4452 ? 185.751 170.684 175.852 1.00 53.51  ? 4452 ILE A N     1 
ATOM   22102 C  CA    . ILE A 1 4452 ? 186.429 169.582 176.529 1.00 50.90  ? 4452 ILE A CA    1 
ATOM   22103 C  C     . ILE A 1 4452 ? 185.635 168.291 176.371 1.00 54.65  ? 4452 ILE A C     1 
ATOM   22104 O  O     . ILE A 1 4452 ? 186.210 167.209 176.197 1.00 57.55  ? 4452 ILE A O     1 
ATOM   22105 C  CB    . ILE A 1 4452 ? 186.669 169.937 178.009 1.00 50.66  ? 4452 ILE A CB    1 
ATOM   22106 C  CG1   . ILE A 1 4452 ? 187.869 170.879 178.135 1.00 50.15  ? 4452 ILE A CG1   1 
ATOM   22107 C  CG2   . ILE A 1 4452 ? 186.874 168.685 178.849 1.00 54.19  ? 4452 ILE A CG2   1 
ATOM   22108 C  CD1   . ILE A 1 4452 ? 188.044 171.473 179.511 1.00 44.29  ? 4452 ILE A CD1   1 
ATOM   22109 N  N     . ASN A 1 4453 ? 184.304 168.387 176.406 1.00 54.43  ? 4453 ASN A N     1 
ATOM   22110 C  CA    . ASN A 1 4453 ? 183.468 167.201 176.243 1.00 55.32  ? 4453 ASN A CA    1 
ATOM   22111 C  C     . ASN A 1 4453 ? 183.712 166.531 174.896 1.00 61.05  ? 4453 ASN A C     1 
ATOM   22112 O  O     . ASN A 1 4453 ? 183.817 165.302 174.818 1.00 62.13  ? 4453 ASN A O     1 
ATOM   22113 C  CB    . ASN A 1 4453 ? 181.994 167.575 176.396 1.00 56.18  ? 4453 ASN A CB    1 
ATOM   22114 C  CG    . ASN A 1 4453 ? 181.096 166.361 176.538 1.00 59.52  ? 4453 ASN A CG    1 
ATOM   22115 O  OD1   . ASN A 1 4453 ? 180.739 165.720 175.550 1.00 59.31  ? 4453 ASN A OD1   1 
ATOM   22116 N  ND2   . ASN A 1 4453 ? 180.725 166.041 177.772 1.00 59.94  ? 4453 ASN A ND2   1 
ATOM   22117 N  N     . GLU A 1 4454 ? 183.807 167.337 173.835 1.00 62.04  ? 4454 GLU A N     1 
ATOM   22118 C  CA    . GLU A 1 4454 ? 184.032 166.780 172.475 1.00 60.07  ? 4454 GLU A CA    1 
ATOM   22119 C  C     . GLU A 1 4454 ? 185.422 166.129 172.416 1.00 60.55  ? 4454 GLU A C     1 
ATOM   22120 O  O     . GLU A 1 4454 ? 185.504 164.943 172.031 1.00 66.18  ? 4454 GLU A O     1 
ATOM   22121 C  CB    . GLU A 1 4454 ? 183.914 167.869 171.409 1.00 60.68  ? 4454 GLU A CB    1 
ATOM   22122 C  CG    . GLU A 1 4454 ? 182.557 168.565 171.404 1.00 66.56  ? 4454 GLU A CG    1 
ATOM   22123 C  CD    . GLU A 1 4454 ? 182.315 169.407 170.165 1.00 72.63  ? 4454 GLU A CD    1 
ATOM   22124 O  OE1   . GLU A 1 4454 ? 182.295 168.830 169.058 1.00 72.26  ? 4454 GLU A OE1   1 
ATOM   22125 O  OE2   . GLU A 1 4454 ? 182.154 170.638 170.305 1.00 68.33  ? 4454 GLU A OE2   1 
ATOM   22126 N  N     . LEU A 1 4455 ? 186.465 166.871 172.797 1.00 56.86  ? 4455 LEU A N     1 
ATOM   22127 C  CA    . LEU A 1 4455 ? 187.853 166.346 172.717 1.00 59.42  ? 4455 LEU A CA    1 
ATOM   22128 C  C     . LEU A 1 4455 ? 187.968 165.059 173.551 1.00 63.44  ? 4455 LEU A C     1 
ATOM   22129 O  O     . LEU A 1 4455 ? 188.597 164.094 173.066 1.00 67.29  ? 4455 LEU A O     1 
ATOM   22130 C  CB    . LEU A 1 4455 ? 188.822 167.424 173.200 1.00 57.48  ? 4455 LEU A CB    1 
ATOM   22131 C  CG    . LEU A 1 4455 ? 188.768 168.754 172.441 1.00 57.76  ? 4455 LEU A CG    1 
ATOM   22132 C  CD1   . LEU A 1 4455 ? 189.751 169.757 173.019 1.00 57.23  ? 4455 LEU A CD1   1 
ATOM   22133 C  CD2   . LEU A 1 4455 ? 189.026 168.539 170.959 1.00 58.18  ? 4455 LEU A CD2   1 
ATOM   22134 N  N     . VAL A 1 4456 ? 187.377 165.049 174.749 1.00 63.72  ? 4456 VAL A N     1 
ATOM   22135 C  CA    . VAL A 1 4456 ? 187.437 163.846 175.636 1.00 61.47  ? 4456 VAL A CA    1 
ATOM   22136 C  C     . VAL A 1 4456 ? 186.805 162.657 174.895 1.00 61.40  ? 4456 VAL A C     1 
ATOM   22137 O  O     . VAL A 1 4456 ? 187.334 161.532 175.023 1.00 61.28  ? 4456 VAL A O     1 
ATOM   22138 C  CB    . VAL A 1 4456 ? 186.744 164.097 176.989 1.00 63.53  ? 4456 VAL A CB    1 
ATOM   22139 C  CG1   . VAL A 1 4456 ? 186.413 162.797 177.711 1.00 67.28  ? 4456 VAL A CG1   1 
ATOM   22140 C  CG2   . VAL A 1 4456 ? 187.565 165.018 177.884 1.00 67.91  ? 4456 VAL A CG2   1 
ATOM   22141 N  N     . LYS A 1 4457 ? 185.728 162.903 174.143 1.00 64.19  ? 4457 LYS A N     1 
ATOM   22142 C  CA    . LYS A 1 4457 ? 185.038 161.813 173.404 1.00 66.39  ? 4457 LYS A CA    1 
ATOM   22143 C  C     . LYS A 1 4457 ? 185.679 161.658 172.016 1.00 65.08  ? 4457 LYS A C     1 
ATOM   22144 O  O     . LYS A 1 4457 ? 185.099 160.936 171.176 1.00 66.13  ? 4457 LYS A O     1 
ATOM   22145 C  CB    . LYS A 1 4457 ? 183.540 162.106 173.268 1.00 62.19  ? 4457 LYS A CB    1 
ATOM   22146 C  CG    . LYS A 1 4457 ? 182.854 162.607 174.530 1.00 60.97  ? 4457 LYS A CG    1 
ATOM   22147 C  CD    . LYS A 1 4457 ? 183.196 161.813 175.785 1.00 63.73  ? 4457 LYS A CD    1 
ATOM   22148 C  CE    . LYS A 1 4457 ? 182.663 162.468 177.019 1.00 63.51  ? 4457 LYS A CE    1 
ATOM   22149 N  NZ    . LYS A 1 4457 ? 183.032 161.726 178.227 1.00 60.45  ? 4457 LYS A NZ    1 
ATOM   22150 N  N     . GLY A 1 4458 ? 186.820 162.314 171.787 1.00 60.12  ? 4458 GLY A N     1 
ATOM   22151 C  CA    . GLY A 1 4458 ? 187.478 162.257 170.467 1.00 59.26  ? 4458 GLY A CA    1 
ATOM   22152 C  C     . GLY A 1 4458 ? 186.545 162.757 169.383 1.00 66.94  ? 4458 GLY A C     1 
ATOM   22153 O  O     . GLY A 1 4458 ? 186.586 162.201 168.265 1.00 68.87  ? 4458 GLY A O     1 
ATOM   22154 N  N     . ILE A 1 4459 ? 185.729 163.768 169.697 1.00 62.96  ? 4459 ILE A N     1 
ATOM   22155 C  CA    . ILE A 1 4459 ? 184.765 164.334 168.707 1.00 59.83  ? 4459 ILE A CA    1 
ATOM   22156 C  C     . ILE A 1 4459 ? 185.337 165.651 168.165 1.00 64.67  ? 4459 ILE A C     1 
ATOM   22157 O  O     . ILE A 1 4459 ? 185.695 166.521 168.989 1.00 67.85  ? 4459 ILE A O     1 
ATOM   22158 C  CB    . ILE A 1 4459 ? 183.384 164.548 169.352 1.00 60.41  ? 4459 ILE A CB    1 
ATOM   22159 C  CG1   . ILE A 1 4459 ? 182.838 163.256 169.957 1.00 62.03  ? 4459 ILE A CG1   1 
ATOM   22160 C  CG2   . ILE A 1 4459 ? 182.405 165.167 168.354 1.00 49.83  ? 4459 ILE A CG2   1 
ATOM   22161 C  CD1   . ILE A 1 4459 ? 181.489 163.416 170.635 1.00 58.40  ? 4459 ILE A CD1   1 
ATOM   22162 N  N     . LEU A 1 4460 ? 185.419 165.785 166.838 1.00 62.60  ? 4460 LEU A N     1 
ATOM   22163 C  CA    . LEU A 1 4460 ? 185.916 167.046 166.230 1.00 56.73  ? 4460 LEU A CA    1 
ATOM   22164 C  C     . LEU A 1 4460 ? 184.960 168.188 166.607 1.00 63.02  ? 4460 LEU A C     1 
ATOM   22165 O  O     . LEU A 1 4460 ? 183.774 168.127 166.218 1.00 65.55  ? 4460 LEU A O     1 
ATOM   22166 C  CB    . LEU A 1 4460 ? 186.053 166.910 164.715 1.00 56.43  ? 4460 LEU A CB    1 
ATOM   22167 C  CG    . LEU A 1 4460 ? 186.590 168.144 163.984 1.00 56.10  ? 4460 LEU A CG    1 
ATOM   22168 C  CD1   . LEU A 1 4460 ? 187.972 168.517 164.493 1.00 54.73  ? 4460 LEU A CD1   1 
ATOM   22169 C  CD2   . LEU A 1 4460 ? 186.613 167.924 162.482 1.00 53.23  ? 4460 LEU A CD2   1 
ATOM   22170 N  N     . PRO A 1 4461 ? 185.423 169.219 167.345 1.00 58.50  ? 4461 PRO A N     1 
ATOM   22171 C  CA    . PRO A 1 4461 ? 184.584 170.370 167.694 1.00 58.36  ? 4461 PRO A CA    1 
ATOM   22172 C  C     . PRO A 1 4461 ? 183.998 171.021 166.451 1.00 60.74  ? 4461 PRO A C     1 
ATOM   22173 O  O     . PRO A 1 4461 ? 184.652 171.123 165.411 1.00 65.13  ? 4461 PRO A O     1 
ATOM   22174 C  CB    . PRO A 1 4461 ? 185.555 171.311 168.416 1.00 57.43  ? 4461 PRO A CB    1 
ATOM   22175 C  CG    . PRO A 1 4461 ? 186.659 170.424 168.896 1.00 55.51  ? 4461 PRO A CG    1 
ATOM   22176 C  CD    . PRO A 1 4461 ? 186.796 169.354 167.859 1.00 55.53  ? 4461 PRO A CD    1 
ATOM   22177 N  N     . ARG A 1 4462 ? 182.745 171.465 166.568 1.00 65.01  ? 4462 ARG A N     1 
ATOM   22178 C  CA    . ARG A 1 4462 ? 182.102 172.149 165.453 1.00 67.87  ? 4462 ARG A CA    1 
ATOM   22179 C  C     . ARG A 1 4462 ? 182.709 173.525 165.216 1.00 68.87  ? 4462 ARG A C     1 
ATOM   22180 O  O     . ARG A 1 4462 ? 182.564 174.086 164.123 1.00 65.54  ? 4462 ARG A O     1 
ATOM   22181 C  CB    . ARG A 1 4462 ? 180.598 172.264 165.703 1.00 63.88  ? 4462 ARG A CB    1 
ATOM   22182 C  CG    . ARG A 1 4462 ? 179.859 170.934 165.670 1.00 66.04  ? 4462 ARG A CG    1 
ATOM   22183 C  CD    . ARG A 1 4462 ? 179.902 170.309 164.285 1.00 75.83  ? 4462 ARG A CD    1 
ATOM   22184 N  NE    . ARG A 1 4462 ? 180.938 169.287 164.179 1.00 83.56  ? 4462 ARG A NE    1 
ATOM   22185 C  CZ    . ARG A 1 4462 ? 181.494 168.899 163.040 1.00 80.96  ? 4462 ARG A CZ    1 
ATOM   22186 N  NH1   . ARG A 1 4462 ? 181.139 169.430 161.881 1.00 77.42  ? 4462 ARG A NH1   1 
ATOM   22187 N  NH2   . ARG A 1 4462 ? 182.431 167.955 163.063 1.00 75.25  ? 4462 ARG A NH2   1 
ATOM   22188 N  N     . SER A 1 4463 ? 183.387 174.084 166.221 1.00 63.53  ? 4463 SER A N     1 
ATOM   22189 C  CA    . SER A 1 4463 ? 184.008 175.393 166.058 1.00 62.96  ? 4463 SER A CA    1 
ATOM   22190 C  C     . SER A 1 4463 ? 185.294 175.303 165.245 1.00 67.37  ? 4463 SER A C     1 
ATOM   22191 O  O     . SER A 1 4463 ? 185.799 176.322 164.761 1.00 69.55  ? 4463 SER A O     1 
ATOM   22192 C  CB    . SER A 1 4463 ? 184.284 176.017 167.426 1.00 62.23  ? 4463 SER A CB    1 
ATOM   22193 O  OG    . SER A 1 4463 ? 184.917 177.277 167.293 1.00 65.86  ? 4463 SER A OG    1 
ATOM   22194 N  N     . TRP A 1 4464 ? 185.848 174.098 165.095 1.00 62.99  ? 4464 TRP A N     1 
ATOM   22195 C  CA    . TRP A 1 4464 ? 187.084 173.949 164.333 1.00 56.51  ? 4464 TRP A CA    1 
ATOM   22196 C  C     . TRP A 1 4464 ? 186.816 173.605 162.873 1.00 58.11  ? 4464 TRP A C     1 
ATOM   22197 O  O     . TRP A 1 4464 ? 187.655 173.885 162.009 1.00 61.37  ? 4464 TRP A O     1 
ATOM   22198 C  CB    . TRP A 1 4464 ? 187.975 172.879 164.967 1.00 49.86  ? 4464 TRP A CB    1 
ATOM   22199 C  CG    . TRP A 1 4464 ? 188.474 173.229 166.336 1.00 50.13  ? 4464 TRP A CG    1 
ATOM   22200 C  CD1   . TRP A 1 4464 ? 188.205 174.364 167.043 1.00 49.32  ? 4464 TRP A CD1   1 
ATOM   22201 C  CD2   . TRP A 1 4464 ? 189.338 172.439 167.161 1.00 50.68  ? 4464 TRP A CD2   1 
ATOM   22202 N  NE1   . TRP A 1 4464 ? 188.845 174.328 168.258 1.00 53.82  ? 4464 TRP A NE1   1 
ATOM   22203 C  CE2   . TRP A 1 4464 ? 189.547 173.156 168.355 1.00 51.33  ? 4464 TRP A CE2   1 
ATOM   22204 C  CE3   . TRP A 1 4464 ? 189.953 171.193 167.007 1.00 48.89  ? 4464 TRP A CE3   1 
ATOM   22205 C  CZ2   . TRP A 1 4464 ? 190.345 172.670 169.388 1.00 47.11  ? 4464 TRP A CZ2   1 
ATOM   22206 C  CZ3   . TRP A 1 4464 ? 190.745 170.712 168.033 1.00 51.73  ? 4464 TRP A CZ3   1 
ATOM   22207 C  CH2   . TRP A 1 4464 ? 190.934 171.449 169.209 1.00 52.21  ? 4464 TRP A CH2   1 
ATOM   22208 N  N     . SER A 1 4465 ? 185.666 173.008 162.577 1.00 55.34  ? 4465 SER A N     1 
ATOM   22209 C  CA    . SER A 1 4465 ? 185.370 172.524 161.230 1.00 58.28  ? 4465 SER A CA    1 
ATOM   22210 C  C     . SER A 1 4465 ? 184.978 173.696 160.339 1.00 64.10  ? 4465 SER A C     1 
ATOM   22211 O  O     . SER A 1 4465 ? 183.818 174.113 160.312 1.00 65.98  ? 4465 SER A O     1 
ATOM   22212 C  CB    . SER A 1 4465 ? 184.264 171.476 161.277 1.00 62.10  ? 4465 SER A CB    1 
ATOM   22213 O  OG    . SER A 1 4465 ? 183.936 171.023 159.975 1.00 63.41  ? 4465 SER A OG    1 
ATOM   22214 N  N     . HIS A 1 4466 ? 185.948 174.232 159.601 1.00 59.89  ? 4466 HIS A N     1 
ATOM   22215 C  CA    . HIS A 1 4466 ? 185.706 175.288 158.627 1.00 56.98  ? 4466 HIS A CA    1 
ATOM   22216 C  C     . HIS A 1 4466 ? 185.756 174.785 157.193 1.00 56.89  ? 4466 HIS A C     1 
ATOM   22217 O  O     . HIS A 1 4466 ? 184.799 174.975 156.437 1.00 61.82  ? 4466 HIS A O     1 
ATOM   22218 C  CB    . HIS A 1 4466 ? 186.723 176.426 158.808 1.00 58.66  ? 4466 HIS A CB    1 
ATOM   22219 C  CG    . HIS A 1 4466 ? 186.586 177.160 160.104 1.00 61.36  ? 4466 HIS A CG    1 
ATOM   22220 N  ND1   . HIS A 1 4466 ? 185.681 176.794 161.077 1.00 62.62  ? 4466 HIS A ND1   1 
ATOM   22221 C  CD2   . HIS A 1 4466 ? 187.237 178.246 160.585 1.00 61.92  ? 4466 HIS A CD2   1 
ATOM   22222 C  CE1   . HIS A 1 4466 ? 185.782 177.621 162.102 1.00 64.30  ? 4466 HIS A CE1   1 
ATOM   22223 N  NE2   . HIS A 1 4466 ? 186.720 178.510 161.829 1.00 67.05  ? 4466 HIS A NE2   1 
ATOM   22224 N  N     . TYR A 1 4467 ? 186.851 174.141 156.799 1.00 57.91  ? 4467 TYR A N     1 
ATOM   22225 C  CA    . TYR A 1 4467 ? 186.980 173.634 155.445 1.00 55.09  ? 4467 TYR A CA    1 
ATOM   22226 C  C     . TYR A 1 4467 ? 186.261 172.294 155.307 1.00 54.93  ? 4467 TYR A C     1 
ATOM   22227 O  O     . TYR A 1 4467 ? 185.842 171.676 156.288 1.00 54.44  ? 4467 TYR A O     1 
ATOM   22228 C  CB    . TYR A 1 4467 ? 188.454 173.503 155.059 1.00 49.15  ? 4467 TYR A CB    1 
ATOM   22229 C  CG    . TYR A 1 4467 ? 189.303 172.756 156.065 1.00 44.19  ? 4467 TYR A CG    1 
ATOM   22230 C  CD1   . TYR A 1 4467 ? 189.364 171.369 156.061 1.00 44.55  ? 4467 TYR A CD1   1 
ATOM   22231 C  CD2   . TYR A 1 4467 ? 190.049 173.439 157.016 1.00 44.24  ? 4467 TYR A CD2   1 
ATOM   22232 C  CE1   . TYR A 1 4467 ? 190.142 170.684 156.976 1.00 44.19  ? 4467 TYR A CE1   1 
ATOM   22233 C  CE2   . TYR A 1 4467 ? 190.829 172.763 157.935 1.00 42.68  ? 4467 TYR A CE2   1 
ATOM   22234 C  CZ    . TYR A 1 4467 ? 190.872 171.386 157.910 1.00 43.72  ? 4467 TYR A CZ    1 
ATOM   22235 O  OH    . TYR A 1 4467 ? 191.647 170.709 158.823 1.00 46.89  ? 4467 TYR A OH    1 
ATOM   22236 N  N     . THR A 1 4468 ? 186.119 171.849 154.061 1.00 56.90  ? 4468 THR A N     1 
ATOM   22237 C  CA    . THR A 1 4468 ? 185.417 170.603 153.789 1.00 56.45  ? 4468 THR A CA    1 
ATOM   22238 C  C     . THR A 1 4468 ? 186.209 169.420 154.332 1.00 59.16  ? 4468 THR A C     1 
ATOM   22239 O  O     . THR A 1 4468 ? 187.410 169.289 154.073 1.00 57.91  ? 4468 THR A O     1 
ATOM   22240 C  CB    . THR A 1 4468 ? 185.184 170.440 152.288 1.00 56.39  ? 4468 THR A CB    1 
ATOM   22241 O  OG1   . THR A 1 4468 ? 184.394 171.534 151.806 1.00 58.98  ? 4468 THR A OG1   1 
ATOM   22242 C  CG2   . THR A 1 4468 ? 184.459 169.135 152.003 1.00 54.30  ? 4468 THR A CG2   1 
ATOM   22243 N  N     . VAL A 1 4469 ? 185.530 168.558 155.084 1.00 60.11  ? 4469 VAL A N     1 
ATOM   22244 C  CA    . VAL A 1 4469 ? 186.178 167.415 155.726 1.00 57.76  ? 4469 VAL A CA    1 
ATOM   22245 C  C     . VAL A 1 4469 ? 185.316 166.181 155.536 1.00 60.05  ? 4469 VAL A C     1 
ATOM   22246 O  O     . VAL A 1 4469 ? 184.079 166.251 155.527 1.00 63.93  ? 4469 VAL A O     1 
ATOM   22247 C  CB    . VAL A 1 4469 ? 186.412 167.669 157.236 1.00 63.83  ? 4469 VAL A CB    1 
ATOM   22248 C  CG1   . VAL A 1 4469 ? 185.090 167.752 157.993 1.00 67.11  ? 4469 VAL A CG1   1 
ATOM   22249 C  CG2   . VAL A 1 4469 ? 187.323 166.617 157.846 1.00 59.10  ? 4469 VAL A CG2   1 
ATOM   22250 N  N     . PRO A 1 4470 ? 185.920 164.986 155.319 1.00 57.50  ? 4470 PRO A N     1 
ATOM   22251 C  CA    . PRO A 1 4470 ? 185.139 163.761 155.234 1.00 54.53  ? 4470 PRO A CA    1 
ATOM   22252 C  C     . PRO A 1 4470 ? 184.426 163.554 156.560 1.00 65.46  ? 4470 PRO A C     1 
ATOM   22253 O  O     . PRO A 1 4470 ? 185.007 163.879 157.615 1.00 65.99  ? 4470 PRO A O     1 
ATOM   22254 C  CB    . PRO A 1 4470 ? 186.178 162.670 154.949 1.00 48.28  ? 4470 PRO A CB    1 
ATOM   22255 C  CG    . PRO A 1 4470 ? 187.350 163.424 154.365 1.00 51.55  ? 4470 PRO A CG    1 
ATOM   22256 C  CD    . PRO A 1 4470 ? 187.346 164.755 155.096 1.00 54.34  ? 4470 PRO A CD    1 
ATOM   22257 N  N     . ALA A 1 4471 ? 183.202 163.022 156.519 1.00 68.30  ? 4471 ALA A N     1 
ATOM   22258 C  CA    . ALA A 1 4471 ? 182.404 162.856 157.758 1.00 68.23  ? 4471 ALA A CA    1 
ATOM   22259 C  C     . ALA A 1 4471 ? 183.193 162.040 158.783 1.00 65.12  ? 4471 ALA A C     1 
ATOM   22260 O  O     . ALA A 1 4471 ? 183.197 162.416 159.975 1.00 63.53  ? 4471 ALA A O     1 
ATOM   22261 C  CB    . ALA A 1 4471 ? 181.081 162.199 157.432 1.00 57.14  ? 4471 ALA A CB    1 
ATOM   22262 N  N     . GLY A 1 4472 ? 183.841 160.960 158.336 1.00 67.00  ? 4472 GLY A N     1 
ATOM   22263 C  CA    . GLY A 1 4472 ? 184.587 160.086 159.262 1.00 66.21  ? 4472 GLY A CA    1 
ATOM   22264 C  C     . GLY A 1 4472 ? 186.018 160.549 159.453 1.00 74.05  ? 4472 GLY A C     1 
ATOM   22265 O  O     . GLY A 1 4472 ? 186.915 159.946 158.828 1.00 77.44  ? 4472 GLY A O     1 
ATOM   22266 N  N     . MET A 1 4473 ? 186.236 161.580 160.276 1.00 73.54  ? 4473 MET A N     1 
ATOM   22267 C  CA    . MET A 1 4473 ? 187.623 162.021 160.587 1.00 69.27  ? 4473 MET A CA    1 
ATOM   22268 C  C     . MET A 1 4473 ? 187.742 162.289 162.095 1.00 64.08  ? 4473 MET A C     1 
ATOM   22269 O  O     . MET A 1 4473 ? 186.916 163.062 162.626 1.00 59.01  ? 4473 MET A O     1 
ATOM   22270 C  CB    . MET A 1 4473 ? 188.010 163.287 159.813 1.00 66.79  ? 4473 MET A CB    1 
ATOM   22271 C  CG    . MET A 1 4473 ? 189.389 163.810 160.177 1.00 65.58  ? 4473 MET A CG    1 
ATOM   22272 S  SD    . MET A 1 4473 ? 190.040 165.058 159.049 1.00 81.63  ? 4473 MET A SD    1 
ATOM   22273 C  CE    . MET A 1 4473 ? 190.106 164.120 157.517 1.00 67.47  ? 4473 MET A CE    1 
ATOM   22274 N  N     . THR A 1 4474 ? 188.734 161.677 162.750 1.00 61.48  ? 4474 THR A N     1 
ATOM   22275 C  CA    . THR A 1 4474 ? 188.939 161.883 164.200 1.00 60.22  ? 4474 THR A CA    1 
ATOM   22276 C  C     . THR A 1 4474 ? 189.592 163.231 164.417 1.00 58.67  ? 4474 THR A C     1 
ATOM   22277 O  O     . THR A 1 4474 ? 190.190 163.760 163.455 1.00 62.82  ? 4474 THR A O     1 
ATOM   22278 C  CB    . THR A 1 4474 ? 189.801 160.753 164.757 1.00 61.60  ? 4474 THR A CB    1 
ATOM   22279 O  OG1   . THR A 1 4474 ? 191.127 161.047 164.327 1.00 64.50  ? 4474 THR A OG1   1 
ATOM   22280 C  CG2   . THR A 1 4474 ? 189.371 159.389 164.247 1.00 59.41  ? 4474 THR A CG2   1 
ATOM   22281 N  N     . VAL A 1 4475 ? 189.498 163.771 165.636 1.00 57.67  ? 4475 VAL A N     1 
ATOM   22282 C  CA    . VAL A 1 4475 ? 190.188 165.057 165.951 1.00 57.90  ? 4475 VAL A CA    1 
ATOM   22283 C  C     . VAL A 1 4475 ? 191.690 164.842 165.711 1.00 56.40  ? 4475 VAL A C     1 
ATOM   22284 O  O     . VAL A 1 4475 ? 192.342 165.760 165.172 1.00 57.44  ? 4475 VAL A O     1 
ATOM   22285 C  CB    . VAL A 1 4475 ? 189.924 165.521 167.394 1.00 57.63  ? 4475 VAL A CB    1 
ATOM   22286 C  CG1   . VAL A 1 4475 ? 190.169 167.017 167.558 1.00 57.53  ? 4475 VAL A CG1   1 
ATOM   22287 C  CG2   . VAL A 1 4475 ? 188.520 165.156 167.859 1.00 57.71  ? 4475 VAL A CG2   1 
ATOM   22288 N  N     . ILE A 1 4476 ? 192.203 163.670 166.097 1.00 54.90  ? 4476 ILE A N     1 
ATOM   22289 C  CA    . ILE A 1 4476 ? 193.647 163.351 165.889 1.00 54.35  ? 4476 ILE A CA    1 
ATOM   22290 C  C     . ILE A 1 4476 ? 193.964 163.475 164.390 1.00 59.60  ? 4476 ILE A C     1 
ATOM   22291 O  O     . ILE A 1 4476 ? 194.882 164.251 164.044 1.00 57.48  ? 4476 ILE A O     1 
ATOM   22292 C  CB    . ILE A 1 4476 ? 193.979 161.948 166.427 1.00 59.72  ? 4476 ILE A CB    1 
ATOM   22293 C  CG1   . ILE A 1 4476 ? 193.587 161.806 167.897 1.00 55.96  ? 4476 ILE A CG1   1 
ATOM   22294 C  CG2   . ILE A 1 4476 ? 195.452 161.611 166.199 1.00 61.86  ? 4476 ILE A CG2   1 
ATOM   22295 C  CD1   . ILE A 1 4476 ? 193.920 160.452 168.497 1.00 51.31  ? 4476 ILE A CD1   1 
ATOM   22296 N  N     . GLN A 1 4477 ? 193.232 162.745 163.542 1.00 60.11  ? 4477 GLN A N     1 
ATOM   22297 C  CA    . GLN A 1 4477 ? 193.455 162.849 162.104 1.00 53.99  ? 4477 GLN A CA    1 
ATOM   22298 C  C     . GLN A 1 4477 ? 193.339 164.292 161.631 1.00 53.08  ? 4477 GLN A C     1 
ATOM   22299 O  O     . GLN A 1 4477 ? 194.140 164.751 160.808 1.00 56.70  ? 4477 GLN A O     1 
ATOM   22300 C  CB    . GLN A 1 4477 ? 192.459 161.965 161.355 1.00 57.01  ? 4477 GLN A CB    1 
ATOM   22301 C  CG    . GLN A 1 4477 ? 192.614 160.477 161.597 1.00 60.68  ? 4477 GLN A CG    1 
ATOM   22302 C  CD    . GLN A 1 4477 ? 191.679 159.655 160.731 1.00 59.82  ? 4477 GLN A CD    1 
ATOM   22303 O  OE1   . GLN A 1 4477 ? 190.470 159.884 160.713 1.00 59.56  ? 4477 GLN A OE1   1 
ATOM   22304 N  NE2   . GLN A 1 4477 ? 192.237 158.694 160.004 1.00 53.25  ? 4477 GLN A NE2   1 
ATOM   22305 N  N     . TRP A 1 4478 ? 192.340 165.022 162.136 1.00 54.32  ? 4478 TRP A N     1 
ATOM   22306 C  CA    . TRP A 1 4478 ? 192.149 166.409 161.723 1.00 53.19  ? 4478 TRP A CA    1 
ATOM   22307 C  C     . TRP A 1 4478 ? 193.309 167.286 162.176 1.00 50.72  ? 4478 TRP A C     1 
ATOM   22308 O  O     . TRP A 1 4478 ? 193.738 168.185 161.444 1.00 49.17  ? 4478 TRP A O     1 
ATOM   22309 C  CB    . TRP A 1 4478 ? 190.825 166.939 162.271 1.00 48.77  ? 4478 TRP A CB    1 
ATOM   22310 C  CG    . TRP A 1 4478 ? 190.485 168.328 161.814 1.00 45.72  ? 4478 TRP A CG    1 
ATOM   22311 C  CD1   . TRP A 1 4478 ? 189.714 168.672 160.742 1.00 42.23  ? 4478 TRP A CD1   1 
ATOM   22312 C  CD2   . TRP A 1 4478 ? 190.890 169.558 162.428 1.00 48.27  ? 4478 TRP A CD2   1 
ATOM   22313 N  NE1   . TRP A 1 4478 ? 189.622 170.039 160.644 1.00 43.18  ? 4478 TRP A NE1   1 
ATOM   22314 C  CE2   . TRP A 1 4478 ? 190.334 170.606 161.668 1.00 42.92  ? 4478 TRP A CE2   1 
ATOM   22315 C  CE3   . TRP A 1 4478 ? 191.672 169.875 163.543 1.00 49.88  ? 4478 TRP A CE3   1 
ATOM   22316 C  CZ2   . TRP A 1 4478 ? 190.535 171.948 161.986 1.00 41.95  ? 4478 TRP A CZ2   1 
ATOM   22317 C  CZ3   . TRP A 1 4478 ? 191.871 171.207 163.858 1.00 48.36  ? 4478 TRP A CZ3   1 
ATOM   22318 C  CH2   . TRP A 1 4478 ? 191.304 172.227 163.082 1.00 46.53  ? 4478 TRP A CH2   1 
ATOM   22319 N  N     . VAL A 1 4479 ? 193.823 167.046 163.385 1.00 50.93  ? 4479 VAL A N     1 
ATOM   22320 C  CA    . VAL A 1 4479 ? 194.956 167.825 163.879 1.00 52.14  ? 4479 VAL A CA    1 
ATOM   22321 C  C     . VAL A 1 4479 ? 196.173 167.615 162.988 1.00 53.97  ? 4479 VAL A C     1 
ATOM   22322 O  O     . VAL A 1 4479 ? 196.878 168.569 162.638 1.00 55.86  ? 4479 VAL A O     1 
ATOM   22323 C  CB    . VAL A 1 4479 ? 195.253 167.464 165.347 1.00 54.03  ? 4479 VAL A CB    1 
ATOM   22324 C  CG1   . VAL A 1 4479 ? 196.673 167.859 165.722 1.00 53.80  ? 4479 VAL A CG1   1 
ATOM   22325 C  CG2   . VAL A 1 4479 ? 194.251 168.137 166.270 1.00 55.58  ? 4479 VAL A CG2   1 
ATOM   22326 N  N     . SER A 1 4480 ? 196.436 166.364 162.603 1.00 50.38  ? 4480 SER A N     1 
ATOM   22327 C  CA    . SER A 1 4480 ? 197.541 166.090 161.689 1.00 47.62  ? 4480 SER A CA    1 
ATOM   22328 C  C     . SER A 1 4480 ? 197.303 166.733 160.329 1.00 51.94  ? 4480 SER A C     1 
ATOM   22329 O  O     . SER A 1 4480 ? 198.224 167.305 159.734 1.00 60.32  ? 4480 SER A O     1 
ATOM   22330 C  CB    . SER A 1 4480 ? 197.740 164.582 161.543 1.00 48.09  ? 4480 SER A CB    1 
ATOM   22331 O  OG    . SER A 1 4480 ? 198.005 163.979 162.796 1.00 51.49  ? 4480 SER A OG    1 
ATOM   22332 N  N     . ASP A 1 4481 ? 196.074 166.643 159.815 1.00 51.34  ? 4481 ASP A N     1 
ATOM   22333 C  CA    . ASP A 1 4481 ? 195.755 167.286 158.545 1.00 52.98  ? 4481 ASP A CA    1 
ATOM   22334 C  C     . ASP A 1 4481 ? 195.843 168.803 158.657 1.00 52.87  ? 4481 ASP A C     1 
ATOM   22335 O  O     . ASP A 1 4481 ? 196.351 169.472 157.750 1.00 53.46  ? 4481 ASP A O     1 
ATOM   22336 C  CB    . ASP A 1 4481 ? 194.364 166.861 158.075 1.00 58.01  ? 4481 ASP A CB    1 
ATOM   22337 C  CG    . ASP A 1 4481 ? 194.277 166.722 156.568 1.00 61.05  ? 4481 ASP A CG    1 
ATOM   22338 O  OD1   . ASP A 1 4481 ? 195.230 167.135 155.875 1.00 61.87  ? 4481 ASP A OD1   1 
ATOM   22339 O  OD2   . ASP A 1 4481 ? 193.255 166.200 156.076 1.00 63.10  ? 4481 ASP A OD2   1 
ATOM   22340 N  N     . PHE A 1 4482 ? 195.346 169.364 159.763 1.00 52.87  ? 4482 PHE A N     1 
ATOM   22341 C  CA    . PHE A 1 4482 ? 195.411 170.810 159.955 1.00 47.97  ? 4482 PHE A CA    1 
ATOM   22342 C  C     . PHE A 1 4482 ? 196.852 171.294 160.043 1.00 51.64  ? 4482 PHE A C     1 
ATOM   22343 O  O     . PHE A 1 4482 ? 197.189 172.362 159.519 1.00 52.15  ? 4482 PHE A O     1 
ATOM   22344 C  CB    . PHE A 1 4482 ? 194.635 171.209 161.209 1.00 48.92  ? 4482 PHE A CB    1 
ATOM   22345 C  CG    . PHE A 1 4482 ? 194.563 172.691 161.426 1.00 48.43  ? 4482 PHE A CG    1 
ATOM   22346 C  CD1   . PHE A 1 4482 ? 194.035 173.520 160.452 1.00 45.63  ? 4482 PHE A CD1   1 
ATOM   22347 C  CD2   . PHE A 1 4482 ? 195.023 173.255 162.604 1.00 47.81  ? 4482 PHE A CD2   1 
ATOM   22348 C  CE1   . PHE A 1 4482 ? 193.972 174.883 160.646 1.00 47.42  ? 4482 PHE A CE1   1 
ATOM   22349 C  CE2   . PHE A 1 4482 ? 194.958 174.620 162.805 1.00 51.11  ? 4482 PHE A CE2   1 
ATOM   22350 C  CZ    . PHE A 1 4482 ? 194.432 175.434 161.825 1.00 52.06  ? 4482 PHE A CZ    1 
ATOM   22351 N  N     . SER A 1 4483 ? 197.714 170.527 160.713 1.00 52.87  ? 4483 SER A N     1 
ATOM   22352 C  CA    . SER A 1 4483 ? 199.119 170.907 160.815 1.00 52.82  ? 4483 SER A CA    1 
ATOM   22353 C  C     . SER A 1 4483 ? 199.779 170.953 159.443 1.00 52.94  ? 4483 SER A C     1 
ATOM   22354 O  O     . SER A 1 4483 ? 200.550 171.872 159.147 1.00 54.96  ? 4483 SER A O     1 
ATOM   22355 C  CB    . SER A 1 4483 ? 199.857 169.935 161.734 1.00 54.67  ? 4483 SER A CB    1 
ATOM   22356 O  OG    . SER A 1 4483 ? 199.783 168.611 161.234 1.00 53.07  ? 4483 SER A OG    1 
ATOM   22357 N  N     . GLU A 1 4484 ? 199.489 169.965 158.593 1.00 52.17  ? 4484 GLU A N     1 
ATOM   22358 C  CA    . GLU A 1 4484 ? 200.057 169.954 157.249 1.00 53.15  ? 4484 GLU A CA    1 
ATOM   22359 C  C     . GLU A 1 4484 ? 199.566 171.141 156.429 1.00 54.69  ? 4484 GLU A C     1 
ATOM   22360 O  O     . GLU A 1 4484 ? 200.342 171.755 155.687 1.00 57.40  ? 4484 GLU A O     1 
ATOM   22361 C  CB    . GLU A 1 4484 ? 199.717 168.639 156.548 1.00 55.16  ? 4484 GLU A CB    1 
ATOM   22362 C  CG    . GLU A 1 4484 ? 200.855 168.064 155.723 1.00 62.09  ? 4484 GLU A CG    1 
ATOM   22363 C  CD    . GLU A 1 4484 ? 200.364 167.237 154.552 1.00 69.97  ? 4484 GLU A CD    1 
ATOM   22364 O  OE1   . GLU A 1 4484 ? 201.035 167.236 153.499 1.00 66.63  ? 4484 GLU A OE1   1 
ATOM   22365 O  OE2   . GLU A 1 4484 ? 199.305 166.588 154.684 1.00 74.43  ? 4484 GLU A OE2   1 
ATOM   22366 N  N     . ARG A 1 4485 ? 198.278 171.475 156.544 1.00 50.95  ? 4485 ARG A N     1 
ATOM   22367 C  CA    . ARG A 1 4485 ? 197.736 172.602 155.791 1.00 48.04  ? 4485 ARG A CA    1 
ATOM   22368 C  C     . ARG A 1 4485 ? 198.367 173.917 156.228 1.00 49.50  ? 4485 ARG A C     1 
ATOM   22369 O  O     . ARG A 1 4485 ? 198.678 174.773 155.391 1.00 56.60  ? 4485 ARG A O     1 
ATOM   22370 C  CB    . ARG A 1 4485 ? 196.218 172.661 155.949 1.00 48.04  ? 4485 ARG A CB    1 
ATOM   22371 C  CG    . ARG A 1 4485 ? 195.485 171.469 155.364 1.00 45.58  ? 4485 ARG A CG    1 
ATOM   22372 C  CD    . ARG A 1 4485 ? 193.989 171.579 155.593 1.00 43.07  ? 4485 ARG A CD    1 
ATOM   22373 N  NE    . ARG A 1 4485 ? 193.279 170.395 155.126 1.00 43.53  ? 4485 ARG A NE    1 
ATOM   22374 C  CZ    . ARG A 1 4485 ? 192.332 170.409 154.197 1.00 41.95  ? 4485 ARG A CZ    1 
ATOM   22375 N  NH1   . ARG A 1 4485 ? 191.958 171.533 153.609 1.00 41.32  ? 4485 ARG A NH1   1 
ATOM   22376 N  NH2   . ARG A 1 4485 ? 191.747 169.266 153.850 1.00 46.43  ? 4485 ARG A NH2   1 
ATOM   22377 N  N     . ILE A 1 4486 ? 198.558 174.100 157.535 1.00 48.89  ? 4486 ILE A N     1 
ATOM   22378 C  CA    . ILE A 1 4486 ? 199.141 175.343 158.030 1.00 52.58  ? 4486 ILE A CA    1 
ATOM   22379 C  C     . ILE A 1 4486 ? 200.597 175.460 157.594 1.00 55.03  ? 4486 ILE A C     1 
ATOM   22380 O  O     . ILE A 1 4486 ? 201.065 176.548 157.237 1.00 59.68  ? 4486 ILE A O     1 
ATOM   22381 C  CB    . ILE A 1 4486 ? 198.990 175.432 159.560 1.00 55.25  ? 4486 ILE A CB    1 
ATOM   22382 C  CG1   . ILE A 1 4486 ? 197.519 175.616 159.937 1.00 48.37  ? 4486 ILE A CG1   1 
ATOM   22383 C  CG2   . ILE A 1 4486 ? 199.806 176.588 160.114 1.00 58.13  ? 4486 ILE A CG2   1 
ATOM   22384 C  CD1   . ILE A 1 4486 ? 196.821 176.707 159.157 1.00 49.74  ? 4486 ILE A CD1   1 
ATOM   22385 N  N     . LYS A 1 4487 ? 201.332 174.345 157.605 1.00 52.90  ? 4487 LYS A N     1 
ATOM   22386 C  CA    . LYS A 1 4487 ? 202.720 174.368 157.150 1.00 51.41  ? 4487 LYS A CA    1 
ATOM   22387 C  C     . LYS A 1 4487 ? 202.812 174.798 155.692 1.00 54.67  ? 4487 LYS A C     1 
ATOM   22388 O  O     . LYS A 1 4487 ? 203.687 175.592 155.324 1.00 60.63  ? 4487 LYS A O     1 
ATOM   22389 C  CB    . LYS A 1 4487 ? 203.361 172.994 157.339 1.00 48.02  ? 4487 LYS A CB    1 
ATOM   22390 C  CG    . LYS A 1 4487 ? 203.630 172.615 158.784 1.00 55.51  ? 4487 LYS A CG    1 
ATOM   22391 C  CD    . LYS A 1 4487 ? 204.042 171.155 158.895 1.00 55.90  ? 4487 LYS A CD    1 
ATOM   22392 C  CE    . LYS A 1 4487 ? 203.764 170.601 160.283 1.00 56.60  ? 4487 LYS A CE    1 
ATOM   22393 N  NZ    . LYS A 1 4487 ? 204.268 171.502 161.355 1.00 56.66  ? 4487 LYS A NZ    1 
ATOM   22394 N  N     . GLN A 1 4488 ? 201.920 174.281 154.846 1.00 49.40  ? 4488 GLN A N     1 
ATOM   22395 C  CA    . GLN A 1 4488 ? 201.897 174.692 153.446 1.00 52.07  ? 4488 GLN A CA    1 
ATOM   22396 C  C     . GLN A 1 4488 ? 201.543 176.167 153.311 1.00 57.94  ? 4488 GLN A C     1 
ATOM   22397 O  O     . GLN A 1 4488 ? 202.138 176.885 152.499 1.00 62.88  ? 4488 GLN A O     1 
ATOM   22398 C  CB    . GLN A 1 4488 ? 200.911 173.822 152.667 1.00 52.01  ? 4488 GLN A CB    1 
ATOM   22399 C  CG    . GLN A 1 4488 ? 200.252 174.516 151.490 1.00 52.55  ? 4488 GLN A CG    1 
ATOM   22400 C  CD    . GLN A 1 4488 ? 199.907 173.557 150.372 1.00 47.52  ? 4488 GLN A CD    1 
ATOM   22401 O  OE1   . GLN A 1 4488 ? 200.670 172.641 150.066 1.00 45.69  ? 4488 GLN A OE1   1 
ATOM   22402 N  NE2   . GLN A 1 4488 ? 198.748 173.759 149.756 1.00 47.62  ? 4488 GLN A NE2   1 
ATOM   22403 N  N     . LEU A 1 4489 ? 200.576 176.639 154.103 1.00 59.34  ? 4489 LEU A N     1 
ATOM   22404 C  CA    . LEU A 1 4489 ? 200.191 178.046 154.044 1.00 59.43  ? 4489 LEU A CA    1 
ATOM   22405 C  C     . LEU A 1 4489 ? 201.323 178.952 154.512 1.00 68.54  ? 4489 LEU A C     1 
ATOM   22406 O  O     . LEU A 1 4489 ? 201.449 180.089 154.042 1.00 69.05  ? 4489 LEU A O     1 
ATOM   22407 C  CB    . LEU A 1 4489 ? 198.933 178.282 154.878 1.00 54.19  ? 4489 LEU A CB    1 
ATOM   22408 C  CG    . LEU A 1 4489 ? 197.616 177.843 154.238 1.00 59.19  ? 4489 LEU A CG    1 
ATOM   22409 C  CD1   . LEU A 1 4489 ? 196.442 178.194 155.137 1.00 60.89  ? 4489 LEU A CD1   1 
ATOM   22410 C  CD2   . LEU A 1 4489 ? 197.451 178.473 152.863 1.00 61.12  ? 4489 LEU A CD2   1 
ATOM   22411 N  N     . GLN A 1 4490 ? 202.149 178.473 155.447 1.00 66.01  ? 4490 GLN A N     1 
ATOM   22412 C  CA    . GLN A 1 4490 ? 203.314 179.246 155.862 1.00 59.70  ? 4490 GLN A CA    1 
ATOM   22413 C  C     . GLN A 1 4490 ? 204.282 179.441 154.703 1.00 67.85  ? 4490 GLN A C     1 
ATOM   22414 O  O     . GLN A 1 4490 ? 204.794 180.546 154.491 1.00 71.74  ? 4490 GLN A O     1 
ATOM   22415 C  CB    . GLN A 1 4490 ? 204.014 178.558 157.034 1.00 58.99  ? 4490 GLN A CB    1 
ATOM   22416 C  CG    . GLN A 1 4490 ? 203.250 178.623 158.345 1.00 63.98  ? 4490 GLN A CG    1 
ATOM   22417 C  CD    . GLN A 1 4490 ? 204.020 178.008 159.497 1.00 63.67  ? 4490 GLN A CD    1 
ATOM   22418 O  OE1   . GLN A 1 4490 ? 204.657 176.965 159.347 1.00 57.48  ? 4490 GLN A OE1   1 
ATOM   22419 N  NE2   . GLN A 1 4490 ? 203.966 178.653 160.656 1.00 72.75  ? 4490 GLN A NE2   1 
ATOM   22420 N  N     . ASN A 1 4491 ? 204.541 178.377 153.939 1.00 69.49  ? 4491 ASN A N     1 
ATOM   22421 C  CA    . ASN A 1 4491 ? 205.447 178.481 152.801 1.00 65.51  ? 4491 ASN A CA    1 
ATOM   22422 C  C     . ASN A 1 4491 ? 204.881 179.400 151.725 1.00 63.86  ? 4491 ASN A C     1 
ATOM   22423 O  O     . ASN A 1 4491 ? 205.623 180.168 151.101 1.00 68.37  ? 4491 ASN A O     1 
ATOM   22424 C  CB    . ASN A 1 4491 ? 205.731 177.093 152.228 1.00 59.73  ? 4491 ASN A CB    1 
ATOM   22425 C  CG    . ASN A 1 4491 ? 206.466 176.199 153.206 1.00 61.87  ? 4491 ASN A CG    1 
ATOM   22426 O  OD1   . ASN A 1 4491 ? 206.690 176.573 154.358 1.00 65.02  ? 4491 ASN A OD1   1 
ATOM   22427 N  ND2   . ASN A 1 4491 ? 206.845 175.010 152.753 1.00 60.21  ? 4491 ASN A ND2   1 
ATOM   22428 N  N     . ILE A 1 4492 ? 203.570 179.329 151.488 1.00 65.83  ? 4492 ILE A N     1 
ATOM   22429 C  CA    . ILE A 1 4492 ? 202.945 180.189 150.486 1.00 69.34  ? 4492 ILE A CA    1 
ATOM   22430 C  C     . ILE A 1 4492 ? 203.066 181.651 150.897 1.00 76.63  ? 4492 ILE A C     1 
ATOM   22431 O  O     . ILE A 1 4492 ? 203.412 182.518 150.085 1.00 81.27  ? 4492 ILE A O     1 
ATOM   22432 C  CB    . ILE A 1 4492 ? 201.476 179.781 150.269 1.00 69.56  ? 4492 ILE A CB    1 
ATOM   22433 C  CG1   . ILE A 1 4492 ? 201.399 178.443 149.531 1.00 68.65  ? 4492 ILE A CG1   1 
ATOM   22434 C  CG2   . ILE A 1 4492 ? 200.728 180.856 149.497 1.00 70.41  ? 4492 ILE A CG2   1 
ATOM   22435 C  CD1   . ILE A 1 4492 ? 200.048 177.768 149.634 1.00 65.37  ? 4492 ILE A CD1   1 
ATOM   22436 N  N     . SER A 1 4493 ? 202.789 181.946 152.169 1.00 76.99  ? 4493 SER A N     1 
ATOM   22437 C  CA    . SER A 1 4493 ? 202.943 183.311 152.661 1.00 77.01  ? 4493 SER A CA    1 
ATOM   22438 C  C     . SER A 1 4493 ? 204.411 183.711 152.724 1.00 76.99  ? 4493 SER A C     1 
ATOM   22439 O  O     . SER A 1 4493 ? 204.751 184.883 152.518 1.00 79.32  ? 4493 SER A O     1 
ATOM   22440 C  CB    . SER A 1 4493 ? 202.286 183.453 154.034 1.00 78.97  ? 4493 SER A CB    1 
ATOM   22441 O  OG    . SER A 1 4493 ? 202.217 184.812 154.429 1.00 74.25  ? 4493 SER A OG    1 
ATOM   22442 N  N     . LEU A 1 4494 ? 205.295 182.753 153.016 1.00 74.85  ? 4494 LEU A N     1 
ATOM   22443 C  CA    . LEU A 1 4494 ? 206.726 183.043 153.033 1.00 76.57  ? 4494 LEU A CA    1 
ATOM   22444 C  C     . LEU A 1 4494 ? 207.219 183.459 151.653 1.00 77.32  ? 4494 LEU A C     1 
ATOM   22445 O  O     . LEU A 1 4494 ? 208.006 184.404 151.524 1.00 77.54  ? 4494 LEU A O     1 
ATOM   22446 C  CB    . LEU A 1 4494 ? 207.501 181.824 153.534 1.00 73.66  ? 4494 LEU A CB    1 
ATOM   22447 C  CG    . LEU A 1 4494 ? 209.017 181.963 153.680 1.00 70.30  ? 4494 LEU A CG    1 
ATOM   22448 C  CD1   . LEU A 1 4494 ? 209.364 183.019 154.719 1.00 73.98  ? 4494 LEU A CD1   1 
ATOM   22449 C  CD2   . LEU A 1 4494 ? 209.643 180.622 154.037 1.00 57.98  ? 4494 LEU A CD2   1 
ATOM   22450 N  N     . ALA A 1 4495 ? 206.768 182.762 150.608 1.00 76.08  ? 4495 ALA A N     1 
ATOM   22451 C  CA    . ALA A 1 4495 ? 207.165 183.123 149.252 1.00 79.08  ? 4495 ALA A CA    1 
ATOM   22452 C  C     . ALA A 1 4495 ? 206.520 184.433 148.816 1.00 80.14  ? 4495 ALA A C     1 
ATOM   22453 O  O     . ALA A 1 4495 ? 207.146 185.240 148.120 1.00 84.35  ? 4495 ALA A O     1 
ATOM   22454 C  CB    . ALA A 1 4495 ? 206.807 181.997 148.282 1.00 78.69  ? 4495 ALA A CB    1 
ATOM   22455 N  N     . ALA A 1 4496 ? 205.261 184.654 149.205 1.00 80.09  ? 4496 ALA A N     1 
ATOM   22456 C  CA    . ALA A 1 4496 ? 204.577 185.889 148.832 1.00 81.85  ? 4496 ALA A CA    1 
ATOM   22457 C  C     . ALA A 1 4496 ? 205.254 187.107 149.448 1.00 84.44  ? 4496 ALA A C     1 
ATOM   22458 O  O     . ALA A 1 4496 ? 205.427 188.132 148.778 1.00 80.23  ? 4496 ALA A O     1 
ATOM   22459 C  CB    . ALA A 1 4496 ? 203.109 185.822 149.249 1.00 79.11  ? 4496 ALA A CB    1 
ATOM   22460 N  N     . ALA A 1 4497 ? 205.636 187.020 150.723 1.00 87.10  ? 4497 ALA A N     1 
ATOM   22461 C  CA    . ALA A 1 4497 ? 206.331 188.133 151.359 1.00 82.93  ? 4497 ALA A CA    1 
ATOM   22462 C  C     . ALA A 1 4497 ? 207.747 188.281 150.818 1.00 85.96  ? 4497 ALA A C     1 
ATOM   22463 O  O     . ALA A 1 4497 ? 208.225 189.403 150.611 1.00 86.99  ? 4497 ALA A O     1 
ATOM   22464 C  CB    . ALA A 1 4497 ? 206.350 187.946 152.875 1.00 76.14  ? 4497 ALA A CB    1 
ATOM   22465 N  N     . SER A 1 4498 ? 208.432 187.165 150.582 1.00 84.65  ? 4498 SER A N     1 
ATOM   22466 C  CA    . SER A 1 4498 ? 209.804 187.171 150.076 1.00 81.11  ? 4498 SER A CA    1 
ATOM   22467 C  C     . SER A 1 4498 ? 209.767 186.813 148.593 1.00 84.31  ? 4498 SER A C     1 
ATOM   22468 O  O     . SER A 1 4498 ? 209.952 185.658 148.208 1.00 83.39  ? 4498 SER A O     1 
ATOM   22469 C  CB    . SER A 1 4498 ? 210.676 186.205 150.869 1.00 80.83  ? 4498 SER A CB    1 
ATOM   22470 O  OG    . SER A 1 4498 ? 210.483 186.374 152.263 1.00 79.87  ? 4498 SER A OG    1 
ATOM   22471 N  N     . GLY A 1 4499 ? 209.532 187.820 147.756 1.00 86.32  ? 4499 GLY A N     1 
ATOM   22472 C  CA    . GLY A 1 4499 ? 209.538 187.622 146.320 1.00 88.43  ? 4499 GLY A CA    1 
ATOM   22473 C  C     . GLY A 1 4499 ? 208.322 188.177 145.608 1.00 90.57  ? 4499 GLY A C     1 
ATOM   22474 O  O     . GLY A 1 4499 ? 208.434 188.697 144.494 1.00 95.73  ? 4499 GLY A O     1 
ATOM   22475 N  N     . GLY A 1 4500 ? 207.154 188.079 146.236 1.00 83.30  ? 4500 GLY A N     1 
ATOM   22476 C  CA    . GLY A 1 4500 ? 205.949 188.635 145.653 1.00 82.14  ? 4500 GLY A CA    1 
ATOM   22477 C  C     . GLY A 1 4500 ? 205.109 187.639 144.881 1.00 85.08  ? 4500 GLY A C     1 
ATOM   22478 O  O     . GLY A 1 4500 ? 204.983 186.477 145.278 1.00 85.75  ? 4500 GLY A O     1 
ATOM   22479 N  N     . ALA A 1 4501 ? 204.528 188.090 143.767 1.00 88.83  ? 4501 ALA A N     1 
ATOM   22480 C  CA    . ALA A 1 4501 ? 203.635 187.244 142.983 1.00 86.90  ? 4501 ALA A CA    1 
ATOM   22481 C  C     . ALA A 1 4501 ? 204.384 186.214 142.147 1.00 83.65  ? 4501 ALA A C     1 
ATOM   22482 O  O     . ALA A 1 4501 ? 203.835 185.144 141.862 1.00 84.16  ? 4501 ALA A O     1 
ATOM   22483 C  CB    . ALA A 1 4501 ? 202.756 188.108 142.078 1.00 80.21  ? 4501 ALA A CB    1 
ATOM   22484 N  N     . LYS A 1 4502 ? 205.620 186.514 141.738 1.00 85.71  ? 4502 LYS A N     1 
ATOM   22485 C  CA    . LYS A 1 4502 ? 206.357 185.589 140.881 1.00 86.43  ? 4502 LYS A CA    1 
ATOM   22486 C  C     . LYS A 1 4502 ? 206.629 184.269 141.591 1.00 82.90  ? 4502 LYS A C     1 
ATOM   22487 O  O     . LYS A 1 4502 ? 206.527 183.197 140.983 1.00 79.81  ? 4502 LYS A O     1 
ATOM   22488 C  CB    . LYS A 1 4502 ? 207.665 186.228 140.412 1.00 91.19  ? 4502 LYS A CB    1 
ATOM   22489 C  CG    . LYS A 1 4502 ? 208.400 187.021 141.478 1.00 92.82  ? 4502 LYS A CG    1 
ATOM   22490 C  CD    . LYS A 1 4502 ? 209.581 187.768 140.879 1.00 91.81  ? 4502 LYS A CD    1 
ATOM   22491 C  CE    . LYS A 1 4502 ? 210.404 188.461 141.951 1.00 94.49  ? 4502 LYS A CE    1 
ATOM   22492 N  NZ    . LYS A 1 4502 ? 211.531 189.238 141.368 1.00 94.21  ? 4502 LYS A NZ    1 
ATOM   22493 N  N     . GLU A 1 4503 ? 206.983 184.324 142.877 1.00 84.07  ? 4503 GLU A N     1 
ATOM   22494 C  CA    . GLU A 1 4503 ? 207.181 183.094 143.637 1.00 84.35  ? 4503 GLU A CA    1 
ATOM   22495 C  C     . GLU A 1 4503 ? 205.874 182.327 143.795 1.00 78.42  ? 4503 GLU A C     1 
ATOM   22496 O  O     . GLU A 1 4503 ? 205.866 181.091 143.761 1.00 78.49  ? 4503 GLU A O     1 
ATOM   22497 C  CB    . GLU A 1 4503 ? 207.791 183.408 145.003 1.00 86.59  ? 4503 GLU A CB    1 
ATOM   22498 C  CG    . GLU A 1 4503 ? 209.013 184.306 144.941 1.00 92.82  ? 4503 GLU A CG    1 
ATOM   22499 C  CD    . GLU A 1 4503 ? 210.272 183.544 144.572 1.00 96.42  ? 4503 GLU A CD    1 
ATOM   22500 O  OE1   . GLU A 1 4503 ? 210.253 182.297 144.633 1.00 90.03  ? 4503 GLU A OE1   1 
ATOM   22501 O  OE2   . GLU A 1 4503 ? 211.281 184.193 144.223 1.00 95.95  ? 4503 GLU A OE2   1 
ATOM   22502 N  N     . LEU A 1 4504 ? 204.759 183.042 143.967 1.00 74.55  ? 4504 LEU A N     1 
ATOM   22503 C  CA    . LEU A 1 4504 ? 203.468 182.378 144.124 1.00 76.19  ? 4504 LEU A CA    1 
ATOM   22504 C  C     . LEU A 1 4504 ? 203.127 181.512 142.919 1.00 74.48  ? 4504 LEU A C     1 
ATOM   22505 O  O     . LEU A 1 4504 ? 202.445 180.491 143.061 1.00 73.92  ? 4504 LEU A O     1 
ATOM   22506 C  CB    . LEU A 1 4504 ? 202.369 183.415 144.354 1.00 76.18  ? 4504 LEU A CB    1 
ATOM   22507 C  CG    . LEU A 1 4504 ? 202.323 184.085 145.728 1.00 81.04  ? 4504 LEU A CG    1 
ATOM   22508 C  CD1   . LEU A 1 4504 ? 200.985 184.774 145.934 1.00 78.28  ? 4504 LEU A CD1   1 
ATOM   22509 C  CD2   . LEU A 1 4504 ? 202.584 183.071 146.831 1.00 78.16  ? 4504 LEU A CD2   1 
ATOM   22510 N  N     . LYS A 1 4505 ? 203.584 181.903 141.729 1.00 71.79  ? 4505 LYS A N     1 
ATOM   22511 C  CA    . LYS A 1 4505 ? 203.307 181.126 140.528 1.00 68.00  ? 4505 LYS A CA    1 
ATOM   22512 C  C     . LYS A 1 4505 ? 204.183 179.883 140.427 1.00 67.69  ? 4505 LYS A C     1 
ATOM   22513 O  O     . LYS A 1 4505 ? 203.731 178.854 139.912 1.00 67.26  ? 4505 LYS A O     1 
ATOM   22514 C  CB    . LYS A 1 4505 ? 203.492 182.004 139.288 1.00 64.17  ? 4505 LYS A CB    1 
ATOM   22515 C  CG    . LYS A 1 4505 ? 202.898 181.428 138.014 1.00 58.97  ? 4505 LYS A CG    1 
ATOM   22516 C  CD    . LYS A 1 4505 ? 203.948 180.707 137.185 1.00 54.04  ? 4505 LYS A CD    1 
ATOM   22517 C  CE    . LYS A 1 4505 ? 203.313 179.955 136.031 1.00 55.38  ? 4505 LYS A CE    1 
ATOM   22518 N  NZ    . LYS A 1 4505 ? 204.321 179.175 135.264 1.00 60.33  ? 4505 LYS A NZ    1 
ATOM   22519 N  N     . ASN A 1 4506 ? 205.421 179.952 140.909 1.00 66.55  ? 4506 ASN A N     1 
ATOM   22520 C  CA    . ASN A 1 4506 ? 206.406 178.906 140.666 1.00 64.89  ? 4506 ASN A CA    1 
ATOM   22521 C  C     . ASN A 1 4506 ? 206.491 177.869 141.780 1.00 64.60  ? 4506 ASN A C     1 
ATOM   22522 O  O     . ASN A 1 4506 ? 207.293 176.936 141.671 1.00 67.91  ? 4506 ASN A O     1 
ATOM   22523 C  CB    . ASN A 1 4506 ? 207.787 179.533 140.447 1.00 69.27  ? 4506 ASN A CB    1 
ATOM   22524 C  CG    . ASN A 1 4506 ? 208.648 178.728 139.495 1.00 72.19  ? 4506 ASN A CG    1 
ATOM   22525 O  OD1   . ASN A 1 4506 ? 208.198 177.737 138.921 1.00 72.44  ? 4506 ASN A OD1   1 
ATOM   22526 N  ND2   . ASN A 1 4506 ? 209.895 179.151 139.323 1.00 70.72  ? 4506 ASN A ND2   1 
ATOM   22527 N  N     . ILE A 1 4507 ? 205.697 177.996 142.837 1.00 62.19  ? 4507 ILE A N     1 
ATOM   22528 C  CA    . ILE A 1 4507 ? 205.745 177.053 143.950 1.00 63.51  ? 4507 ILE A CA    1 
ATOM   22529 C  C     . ILE A 1 4507 ? 204.693 175.970 143.753 1.00 60.08  ? 4507 ILE A C     1 
ATOM   22530 O  O     . ILE A 1 4507 ? 203.557 176.244 143.347 1.00 56.07  ? 4507 ILE A O     1 
ATOM   22531 C  CB    . ILE A 1 4507 ? 205.564 177.775 145.301 1.00 66.92  ? 4507 ILE A CB    1 
ATOM   22532 C  CG1   . ILE A 1 4507 ? 204.217 178.502 145.360 1.00 60.73  ? 4507 ILE A CG1   1 
ATOM   22533 C  CG2   . ILE A 1 4507 ? 206.736 178.710 145.575 1.00 67.48  ? 4507 ILE A CG2   1 
ATOM   22534 C  CD1   . ILE A 1 4507 ? 203.873 179.036 146.733 1.00 64.36  ? 4507 ILE A CD1   1 
ATOM   22535 N  N     . HIS A 1 4508 ? 205.084 174.728 144.023 1.00 56.72  ? 4508 HIS A N     1 
ATOM   22536 C  CA    . HIS A 1 4508 ? 204.166 173.602 143.934 1.00 49.52  ? 4508 HIS A CA    1 
ATOM   22537 C  C     . HIS A 1 4508 ? 203.190 173.631 145.102 1.00 49.99  ? 4508 HIS A C     1 
ATOM   22538 O  O     . HIS A 1 4508 ? 203.547 174.013 146.220 1.00 51.94  ? 4508 HIS A O     1 
ATOM   22539 C  CB    . HIS A 1 4508 ? 204.935 172.281 143.921 1.00 52.01  ? 4508 HIS A CB    1 
ATOM   22540 C  CG    . HIS A 1 4508 ? 206.072 172.251 142.947 1.00 55.18  ? 4508 HIS A CG    1 
ATOM   22541 N  ND1   . HIS A 1 4508 ? 207.118 171.359 143.053 1.00 54.85  ? 4508 HIS A ND1   1 
ATOM   22542 C  CD2   . HIS A 1 4508 ? 206.324 172.996 141.845 1.00 55.56  ? 4508 HIS A CD2   1 
ATOM   22543 C  CE1   . HIS A 1 4508 ? 207.967 171.560 142.062 1.00 60.73  ? 4508 HIS A CE1   1 
ATOM   22544 N  NE2   . HIS A 1 4508 ? 207.509 172.548 141.315 1.00 58.83  ? 4508 HIS A NE2   1 
ATOM   22545 N  N     . VAL A 1 4509 ? 201.952 173.224 144.838 1.00 49.51  ? 4509 VAL A N     1 
ATOM   22546 C  CA    . VAL A 1 4509 ? 200.880 173.304 145.818 1.00 43.13  ? 4509 VAL A CA    1 
ATOM   22547 C  C     . VAL A 1 4509 ? 200.239 171.933 145.977 1.00 41.98  ? 4509 VAL A C     1 
ATOM   22548 O  O     . VAL A 1 4509 ? 200.172 171.140 145.032 1.00 45.33  ? 4509 VAL A O     1 
ATOM   22549 C  CB    . VAL A 1 4509 ? 199.827 174.366 145.416 1.00 42.99  ? 4509 VAL A CB    1 
ATOM   22550 C  CG1   . VAL A 1 4509 ? 199.065 173.927 144.176 1.00 44.33  ? 4509 VAL A CG1   1 
ATOM   22551 C  CG2   . VAL A 1 4509 ? 198.877 174.656 146.567 1.00 49.22  ? 4509 VAL A CG2   1 
ATOM   22552 N  N     . CYS A 1 4510 ? 199.788 171.646 147.197 1.00 42.86  ? 4510 CYS A N     1 
ATOM   22553 C  CA    . CYS A 1 4510 ? 199.018 170.444 147.494 1.00 43.10  ? 4510 CYS A CA    1 
ATOM   22554 C  C     . CYS A 1 4510 ? 197.539 170.813 147.456 1.00 47.06  ? 4510 CYS A C     1 
ATOM   22555 O  O     . CYS A 1 4510 ? 197.069 171.602 148.281 1.00 48.38  ? 4510 CYS A O     1 
ATOM   22556 C  CB    . CYS A 1 4510 ? 199.409 169.864 148.852 1.00 39.34  ? 4510 CYS A CB    1 
ATOM   22557 S  SG    . CYS A 1 4510 ? 198.468 168.401 149.340 1.00 52.36  ? 4510 CYS A SG    1 
ATOM   22558 N  N     . LEU A 1 4511 ? 196.810 170.247 146.490 1.00 43.40  ? 4511 LEU A N     1 
ATOM   22559 C  CA    . LEU A 1 4511 ? 195.393 170.567 146.352 1.00 43.20  ? 4511 LEU A CA    1 
ATOM   22560 C  C     . LEU A 1 4511 ? 194.593 170.116 147.566 1.00 47.60  ? 4511 LEU A C     1 
ATOM   22561 O  O     . LEU A 1 4511 ? 193.561 170.717 147.886 1.00 51.39  ? 4511 LEU A O     1 
ATOM   22562 C  CB    . LEU A 1 4511 ? 194.833 169.931 145.079 1.00 41.00  ? 4511 LEU A CB    1 
ATOM   22563 C  CG    . LEU A 1 4511 ? 195.003 170.734 143.789 1.00 40.41  ? 4511 LEU A CG    1 
ATOM   22564 C  CD1   . LEU A 1 4511 ? 194.143 170.153 142.679 1.00 35.61  ? 4511 LEU A CD1   1 
ATOM   22565 C  CD2   . LEU A 1 4511 ? 194.668 172.199 144.019 1.00 45.62  ? 4511 LEU A CD2   1 
ATOM   22566 N  N     . GLY A 1 4512 ? 195.045 169.064 148.251 1.00 45.53  ? 4512 GLY A N     1 
ATOM   22567 C  CA    . GLY A 1 4512 ? 194.361 168.634 149.459 1.00 42.46  ? 4512 GLY A CA    1 
ATOM   22568 C  C     . GLY A 1 4512 ? 194.471 169.643 150.586 1.00 42.63  ? 4512 GLY A C     1 
ATOM   22569 O  O     . GLY A 1 4512 ? 193.522 169.841 151.349 1.00 44.30  ? 4512 GLY A O     1 
ATOM   22570 N  N     . GLY A 1 4513 ? 195.629 170.296 150.706 1.00 44.10  ? 4513 GLY A N     1 
ATOM   22571 C  CA    . GLY A 1 4513 ? 195.833 171.256 151.775 1.00 42.15  ? 4513 GLY A CA    1 
ATOM   22572 C  C     . GLY A 1 4513 ? 195.078 172.555 151.597 1.00 43.46  ? 4513 GLY A C     1 
ATOM   22573 O  O     . GLY A 1 4513 ? 194.851 173.268 152.580 1.00 44.48  ? 4513 GLY A O     1 
ATOM   22574 N  N     . LEU A 1 4514 ? 194.686 172.881 150.369 1.00 48.73  ? 4514 LEU A N     1 
ATOM   22575 C  CA    . LEU A 1 4514 ? 193.942 174.108 150.124 1.00 47.07  ? 4514 LEU A CA    1 
ATOM   22576 C  C     . LEU A 1 4514 ? 192.503 173.965 150.604 1.00 47.82  ? 4514 LEU A C     1 
ATOM   22577 O  O     . LEU A 1 4514 ? 191.855 172.938 150.381 1.00 53.26  ? 4514 LEU A O     1 
ATOM   22578 C  CB    . LEU A 1 4514 ? 193.974 174.456 148.637 1.00 47.05  ? 4514 LEU A CB    1 
ATOM   22579 C  CG    . LEU A 1 4514 ? 195.360 174.777 148.074 1.00 52.59  ? 4514 LEU A CG    1 
ATOM   22580 C  CD1   . LEU A 1 4514 ? 195.252 175.349 146.674 1.00 51.41  ? 4514 LEU A CD1   1 
ATOM   22581 C  CD2   . LEU A 1 4514 ? 196.103 175.739 148.989 1.00 48.79  ? 4514 LEU A CD2   1 
ATOM   22582 N  N     . PHE A 1 4515 ? 192.006 175.006 151.277 1.00 47.34  ? 4515 PHE A N     1 
ATOM   22583 C  CA    . PHE A 1 4515 ? 190.642 174.972 151.793 1.00 49.69  ? 4515 PHE A CA    1 
ATOM   22584 C  C     . PHE A 1 4515 ? 189.623 174.874 150.665 1.00 49.46  ? 4515 PHE A C     1 
ATOM   22585 O  O     . PHE A 1 4515 ? 188.637 174.136 150.774 1.00 55.44  ? 4515 PHE A O     1 
ATOM   22586 C  CB    . PHE A 1 4515 ? 190.376 176.205 152.656 1.00 56.20  ? 4515 PHE A CB    1 
ATOM   22587 C  CG    . PHE A 1 4515 ? 191.317 176.342 153.816 1.00 57.37  ? 4515 PHE A CG    1 
ATOM   22588 C  CD1   . PHE A 1 4515 ? 191.708 175.230 154.542 1.00 46.93  ? 4515 PHE A CD1   1 
ATOM   22589 C  CD2   . PHE A 1 4515 ? 191.812 177.582 154.180 1.00 57.08  ? 4515 PHE A CD2   1 
ATOM   22590 C  CE1   . PHE A 1 4515 ? 192.574 175.352 155.610 1.00 44.04  ? 4515 PHE A CE1   1 
ATOM   22591 C  CE2   . PHE A 1 4515 ? 192.679 177.710 155.247 1.00 58.27  ? 4515 PHE A CE2   1 
ATOM   22592 C  CZ    . PHE A 1 4515 ? 193.061 176.593 155.963 1.00 52.54  ? 4515 PHE A CZ    1 
ATOM   22593 N  N     . VAL A 1 4516 ? 189.841 175.609 149.580 1.00 47.95  ? 4516 VAL A N     1 
ATOM   22594 C  CA    . VAL A 1 4516 ? 188.974 175.530 148.408 1.00 46.83  ? 4516 VAL A CA    1 
ATOM   22595 C  C     . VAL A 1 4516 ? 189.866 175.246 147.205 1.00 48.38  ? 4516 VAL A C     1 
ATOM   22596 O  O     . VAL A 1 4516 ? 190.301 176.182 146.517 1.00 52.35  ? 4516 VAL A O     1 
ATOM   22597 C  CB    . VAL A 1 4516 ? 188.151 176.817 148.227 1.00 52.27  ? 4516 VAL A CB    1 
ATOM   22598 C  CG1   . VAL A 1 4516 ? 187.297 176.738 146.967 1.00 53.01  ? 4516 VAL A CG1   1 
ATOM   22599 C  CG2   . VAL A 1 4516 ? 187.281 177.073 149.450 1.00 50.84  ? 4516 VAL A CG2   1 
ATOM   22600 N  N     . PRO A 1 4517 ? 190.200 173.980 146.943 1.00 48.46  ? 4517 PRO A N     1 
ATOM   22601 C  CA    . PRO A 1 4517 ? 191.085 173.675 145.806 1.00 46.52  ? 4517 PRO A CA    1 
ATOM   22602 C  C     . PRO A 1 4517 ? 190.525 174.099 144.460 1.00 47.55  ? 4517 PRO A C     1 
ATOM   22603 O  O     . PRO A 1 4517 ? 191.302 174.459 143.567 1.00 50.61  ? 4517 PRO A O     1 
ATOM   22604 C  CB    . PRO A 1 4517 ? 191.257 172.151 145.892 1.00 49.85  ? 4517 PRO A CB    1 
ATOM   22605 C  CG    . PRO A 1 4517 ? 190.132 171.672 146.754 1.00 48.34  ? 4517 PRO A CG    1 
ATOM   22606 C  CD    . PRO A 1 4517 ? 189.848 172.778 147.715 1.00 48.15  ? 4517 PRO A CD    1 
ATOM   22607 N  N     . GLU A 1 4518 ? 189.201 174.065 144.282 1.00 49.18  ? 4518 GLU A N     1 
ATOM   22608 C  CA    . GLU A 1 4518 ? 188.623 174.429 142.992 1.00 49.16  ? 4518 GLU A CA    1 
ATOM   22609 C  C     . GLU A 1 4518 ? 188.855 175.898 142.665 1.00 52.32  ? 4518 GLU A C     1 
ATOM   22610 O  O     . GLU A 1 4518 ? 188.896 176.271 141.487 1.00 54.22  ? 4518 GLU A O     1 
ATOM   22611 C  CB    . GLU A 1 4518 ? 187.127 174.110 142.969 1.00 48.37  ? 4518 GLU A CB    1 
ATOM   22612 C  CG    . GLU A 1 4518 ? 186.361 174.571 144.198 1.00 51.64  ? 4518 GLU A CG    1 
ATOM   22613 C  CD    . GLU A 1 4518 ? 186.284 173.507 145.275 1.00 53.54  ? 4518 GLU A CD    1 
ATOM   22614 O  OE1   . GLU A 1 4518 ? 187.328 172.898 145.585 1.00 54.00  ? 4518 GLU A OE1   1 
ATOM   22615 O  OE2   . GLU A 1 4518 ? 185.179 173.278 145.810 1.00 51.57  ? 4518 GLU A OE2   1 
ATOM   22616 N  N     . ALA A 1 4519 ? 189.003 176.746 143.685 1.00 50.13  ? 4519 ALA A N     1 
ATOM   22617 C  CA    . ALA A 1 4519 ? 189.282 178.155 143.432 1.00 49.19  ? 4519 ALA A CA    1 
ATOM   22618 C  C     . ALA A 1 4519 ? 190.707 178.352 142.932 1.00 51.78  ? 4519 ALA A C     1 
ATOM   22619 O  O     . ALA A 1 4519 ? 190.985 179.296 142.184 1.00 55.18  ? 4519 ALA A O     1 
ATOM   22620 C  CB    . ALA A 1 4519 ? 189.034 178.977 144.696 1.00 44.58  ? 4519 ALA A CB    1 
ATOM   22621 N  N     . TYR A 1 4520 ? 191.627 177.476 143.344 1.00 49.26  ? 4520 TYR A N     1 
ATOM   22622 C  CA    . TYR A 1 4520 ? 192.991 177.541 142.830 1.00 46.67  ? 4520 TYR A CA    1 
ATOM   22623 C  C     . TYR A 1 4520 ? 193.026 177.265 141.333 1.00 46.53  ? 4520 TYR A C     1 
ATOM   22624 O  O     . TYR A 1 4520 ? 193.771 177.917 140.592 1.00 52.25  ? 4520 TYR A O     1 
ATOM   22625 C  CB    . TYR A 1 4520 ? 193.888 176.552 143.573 1.00 45.69  ? 4520 TYR A CB    1 
ATOM   22626 C  CG    . TYR A 1 4520 ? 195.298 176.488 143.031 1.00 41.27  ? 4520 TYR A CG    1 
ATOM   22627 C  CD1   . TYR A 1 4520 ? 196.229 177.465 143.352 1.00 44.34  ? 4520 TYR A CD1   1 
ATOM   22628 C  CD2   . TYR A 1 4520 ? 195.696 175.454 142.194 1.00 41.27  ? 4520 TYR A CD2   1 
ATOM   22629 C  CE1   . TYR A 1 4520 ? 197.518 177.414 142.859 1.00 44.80  ? 4520 TYR A CE1   1 
ATOM   22630 C  CE2   . TYR A 1 4520 ? 196.982 175.396 141.695 1.00 41.44  ? 4520 TYR A CE2   1 
ATOM   22631 C  CZ    . TYR A 1 4520 ? 197.888 176.378 142.031 1.00 41.93  ? 4520 TYR A CZ    1 
ATOM   22632 O  OH    . TYR A 1 4520 ? 199.171 176.323 141.537 1.00 47.52  ? 4520 TYR A OH    1 
ATOM   22633 N  N     . ILE A 1 4521 ? 192.236 176.292 140.875 1.00 42.94  ? 4521 ILE A N     1 
ATOM   22634 C  CA    . ILE A 1 4521 ? 192.166 175.994 139.448 1.00 44.10  ? 4521 ILE A CA    1 
ATOM   22635 C  C     . ILE A 1 4521 ? 191.629 177.196 138.684 1.00 48.64  ? 4521 ILE A C     1 
ATOM   22636 O  O     . ILE A 1 4521 ? 192.126 177.540 137.605 1.00 48.30  ? 4521 ILE A O     1 
ATOM   22637 C  CB    . ILE A 1 4521 ? 191.309 174.737 139.208 1.00 40.91  ? 4521 ILE A CB    1 
ATOM   22638 C  CG1   . ILE A 1 4521 ? 191.819 173.574 140.061 1.00 39.16  ? 4521 ILE A CG1   1 
ATOM   22639 C  CG2   . ILE A 1 4521 ? 191.314 174.359 137.735 1.00 40.33  ? 4521 ILE A CG2   1 
ATOM   22640 C  CD1   . ILE A 1 4521 ? 193.266 173.226 139.817 1.00 39.64  ? 4521 ILE A CD1   1 
ATOM   22641 N  N     . THR A 1 4522 ? 190.602 177.852 139.231 1.00 50.21  ? 4522 THR A N     1 
ATOM   22642 C  CA    . THR A 1 4522 ? 190.090 179.073 138.619 1.00 51.02  ? 4522 THR A CA    1 
ATOM   22643 C  C     . THR A 1 4522 ? 191.139 180.180 138.642 1.00 50.21  ? 4522 THR A C     1 
ATOM   22644 O  O     . THR A 1 4522 ? 191.266 180.946 137.679 1.00 56.57  ? 4522 THR A O     1 
ATOM   22645 C  CB    . THR A 1 4522 ? 188.816 179.521 139.336 1.00 56.71  ? 4522 THR A CB    1 
ATOM   22646 O  OG1   . THR A 1 4522 ? 187.825 178.490 139.239 1.00 58.76  ? 4522 THR A OG1   1 
ATOM   22647 C  CG2   . THR A 1 4522 ? 188.267 180.796 138.715 1.00 57.17  ? 4522 THR A CG2   1 
ATOM   22648 N  N     . ALA A 1 4523 ? 191.902 180.277 139.734 1.00 47.42  ? 4523 ALA A N     1 
ATOM   22649 C  CA    . ALA A 1 4523 ? 192.950 181.289 139.819 1.00 49.44  ? 4523 ALA A CA    1 
ATOM   22650 C  C     . ALA A 1 4523 ? 194.033 181.059 138.771 1.00 50.59  ? 4523 ALA A C     1 
ATOM   22651 O  O     . ALA A 1 4523 ? 194.492 182.010 138.128 1.00 56.10  ? 4523 ALA A O     1 
ATOM   22652 C  CB    . ALA A 1 4523 ? 193.554 181.302 141.222 1.00 52.71  ? 4523 ALA A CB    1 
ATOM   22653 N  N     . THR A 1 4524 ? 194.457 179.806 138.590 1.00 49.25  ? 4524 THR A N     1 
ATOM   22654 C  CA    . THR A 1 4524 ? 195.449 179.505 137.562 1.00 48.73  ? 4524 THR A CA    1 
ATOM   22655 C  C     . THR A 1 4524 ? 194.885 179.748 136.168 1.00 49.42  ? 4524 THR A C     1 
ATOM   22656 O  O     . THR A 1 4524 ? 195.599 180.215 135.273 1.00 50.98  ? 4524 THR A O     1 
ATOM   22657 C  CB    . THR A 1 4524 ? 195.932 178.061 137.701 1.00 46.22  ? 4524 THR A CB    1 
ATOM   22658 O  OG1   . THR A 1 4524 ? 194.806 177.175 137.701 1.00 51.28  ? 4524 THR A OG1   1 
ATOM   22659 C  CG2   . THR A 1 4524 ? 196.712 177.884 138.994 1.00 39.85  ? 4524 THR A CG2   1 
ATOM   22660 N  N     . ARG A 1 4525 ? 193.606 179.427 135.964 1.00 48.88  ? 4525 ARG A N     1 
ATOM   22661 C  CA    . ARG A 1 4525 ? 192.961 179.706 134.684 1.00 49.49  ? 4525 ARG A CA    1 
ATOM   22662 C  C     . ARG A 1 4525 ? 192.914 181.204 134.410 1.00 57.28  ? 4525 ARG A C     1 
ATOM   22663 O  O     . ARG A 1 4525 ? 193.174 181.652 133.288 1.00 58.96  ? 4525 ARG A O     1 
ATOM   22664 C  CB    . ARG A 1 4525 ? 191.553 179.112 134.672 1.00 49.83  ? 4525 ARG A CB    1 
ATOM   22665 C  CG    . ARG A 1 4525 ? 190.977 178.890 133.285 1.00 55.41  ? 4525 ARG A CG    1 
ATOM   22666 C  CD    . ARG A 1 4525 ? 189.458 178.876 133.324 1.00 58.70  ? 4525 ARG A CD    1 
ATOM   22667 N  NE    . ARG A 1 4525 ? 188.888 178.045 132.271 1.00 67.07  ? 4525 ARG A NE    1 
ATOM   22668 C  CZ    . ARG A 1 4525 ? 188.030 177.057 132.480 1.00 70.26  ? 4525 ARG A CZ    1 
ATOM   22669 N  NH1   . ARG A 1 4525 ? 187.621 176.742 133.699 1.00 61.81  ? 4525 ARG A NH1   1 
ATOM   22670 N  NH2   . ARG A 1 4525 ? 187.570 176.366 131.441 1.00 70.62  ? 4525 ARG A NH2   1 
ATOM   22671 N  N     . GLN A 1 4526 ? 192.578 181.995 135.431 1.00 57.26  ? 4526 GLN A N     1 
ATOM   22672 C  CA    . GLN A 1 4526 ? 192.512 183.442 135.259 1.00 57.02  ? 4526 GLN A CA    1 
ATOM   22673 C  C     . GLN A 1 4526 ? 193.901 184.041 135.071 1.00 55.45  ? 4526 GLN A C     1 
ATOM   22674 O  O     . GLN A 1 4526 ? 194.062 185.037 134.355 1.00 60.24  ? 4526 GLN A O     1 
ATOM   22675 C  CB    . GLN A 1 4526 ? 191.806 184.077 136.458 1.00 57.62  ? 4526 GLN A CB    1 
ATOM   22676 C  CG    . GLN A 1 4526 ? 191.505 185.561 136.307 1.00 63.14  ? 4526 GLN A CG    1 
ATOM   22677 C  CD    . GLN A 1 4526 ? 190.518 185.851 135.197 1.00 61.59  ? 4526 GLN A CD    1 
ATOM   22678 O  OE1   . GLN A 1 4526 ? 189.647 185.037 134.898 1.00 62.11  ? 4526 GLN A OE1   1 
ATOM   22679 N  NE2   . GLN A 1 4526 ? 190.647 187.021 134.582 1.00 60.32  ? 4526 GLN A NE2   1 
ATOM   22680 N  N     . TYR A 1 4527 ? 194.914 183.453 135.711 1.00 51.43  ? 4527 TYR A N     1 
ATOM   22681 C  CA    . TYR A 1 4527 ? 196.274 183.972 135.594 1.00 51.70  ? 4527 TYR A CA    1 
ATOM   22682 C  C     . TYR A 1 4527 ? 196.786 183.851 134.164 1.00 51.73  ? 4527 TYR A C     1 
ATOM   22683 O  O     . TYR A 1 4527 ? 197.385 184.788 133.624 1.00 53.51  ? 4527 TYR A O     1 
ATOM   22684 C  CB    . TYR A 1 4527 ? 197.194 183.238 136.573 1.00 51.55  ? 4527 TYR A CB    1 
ATOM   22685 C  CG    . TYR A 1 4527 ? 198.663 183.595 136.462 1.00 53.31  ? 4527 TYR A CG    1 
ATOM   22686 C  CD1   . TYR A 1 4527 ? 199.494 182.950 135.554 1.00 51.46  ? 4527 TYR A CD1   1 
ATOM   22687 C  CD2   . TYR A 1 4527 ? 199.219 184.576 137.271 1.00 56.72  ? 4527 TYR A CD2   1 
ATOM   22688 C  CE1   . TYR A 1 4527 ? 200.832 183.275 135.453 1.00 49.76  ? 4527 TYR A CE1   1 
ATOM   22689 C  CE2   . TYR A 1 4527 ? 200.557 184.907 137.177 1.00 54.82  ? 4527 TYR A CE2   1 
ATOM   22690 C  CZ    . TYR A 1 4527 ? 201.358 184.253 136.266 1.00 52.74  ? 4527 TYR A CZ    1 
ATOM   22691 O  OH    . TYR A 1 4527 ? 202.691 184.578 136.168 1.00 58.37  ? 4527 TYR A OH    1 
ATOM   22692 N  N     . VAL A 1 4528 ? 196.563 182.694 133.536 1.00 51.86  ? 4528 VAL A N     1 
ATOM   22693 C  CA    . VAL A 1 4528 ? 197.010 182.496 132.160 1.00 52.37  ? 4528 VAL A CA    1 
ATOM   22694 C  C     . VAL A 1 4528 ? 196.218 183.384 131.210 1.00 60.18  ? 4528 VAL A C     1 
ATOM   22695 O  O     . VAL A 1 4528 ? 196.770 183.947 130.256 1.00 69.28  ? 4528 VAL A O     1 
ATOM   22696 C  CB    . VAL A 1 4528 ? 196.904 181.008 131.775 1.00 56.57  ? 4528 VAL A CB    1 
ATOM   22697 C  CG1   . VAL A 1 4528 ? 197.193 180.813 130.294 1.00 62.85  ? 4528 VAL A CG1   1 
ATOM   22698 C  CG2   . VAL A 1 4528 ? 197.854 180.176 132.619 1.00 54.70  ? 4528 VAL A CG2   1 
ATOM   22699 N  N     . ALA A 1 4529 ? 194.914 183.527 131.456 1.00 60.40  ? 4529 ALA A N     1 
ATOM   22700 C  CA    . ALA A 1 4529 ? 194.084 184.363 130.595 1.00 66.32  ? 4529 ALA A CA    1 
ATOM   22701 C  C     . ALA A 1 4529 ? 194.532 185.818 130.634 1.00 65.81  ? 4529 ALA A C     1 
ATOM   22702 O  O     . ALA A 1 4529 ? 194.591 186.484 129.595 1.00 72.46  ? 4529 ALA A O     1 
ATOM   22703 C  CB    . ALA A 1 4529 ? 192.616 184.242 131.003 1.00 66.36  ? 4529 ALA A CB    1 
ATOM   22704 N  N     . GLN A 1 4530 ? 194.847 186.332 131.825 1.00 59.34  ? 4530 GLN A N     1 
ATOM   22705 C  CA    . GLN A 1 4530 ? 195.318 187.710 131.935 1.00 63.19  ? 4530 GLN A CA    1 
ATOM   22706 C  C     . GLN A 1 4530 ? 196.663 187.894 131.243 1.00 69.35  ? 4530 GLN A C     1 
ATOM   22707 O  O     . GLN A 1 4530 ? 196.884 188.902 130.561 1.00 70.52  ? 4530 GLN A O     1 
ATOM   22708 C  CB    . GLN A 1 4530 ? 195.415 188.118 133.404 1.00 61.88  ? 4530 GLN A CB    1 
ATOM   22709 C  CG    . GLN A 1 4530 ? 196.035 189.488 133.623 1.00 59.58  ? 4530 GLN A CG    1 
ATOM   22710 C  CD    . GLN A 1 4530 ? 196.108 189.869 135.087 1.00 64.53  ? 4530 GLN A CD    1 
ATOM   22711 O  OE1   . GLN A 1 4530 ? 195.654 189.126 135.956 1.00 68.83  ? 4530 GLN A OE1   1 
ATOM   22712 N  NE2   . GLN A 1 4530 ? 196.680 191.034 135.368 1.00 63.61  ? 4530 GLN A NE2   1 
ATOM   22713 N  N     . ALA A 1 4531 ? 197.574 186.931 131.409 1.00 67.83  ? 4531 ALA A N     1 
ATOM   22714 C  CA    . ALA A 1 4531 ? 198.905 187.060 130.825 1.00 66.52  ? 4531 ALA A CA    1 
ATOM   22715 C  C     . ALA A 1 4531 ? 198.851 187.049 129.302 1.00 69.05  ? 4531 ALA A C     1 
ATOM   22716 O  O     . ALA A 1 4531 ? 199.723 187.621 128.639 1.00 66.40  ? 4531 ALA A O     1 
ATOM   22717 C  CB    . ALA A 1 4531 ? 199.811 185.940 131.338 1.00 57.03  ? 4531 ALA A CB    1 
ATOM   22718 N  N     . ASN A 1 4532 ? 197.838 186.399 128.730 1.00 73.81  ? 4532 ASN A N     1 
ATOM   22719 C  CA    . ASN A 1 4532 ? 197.710 186.274 127.284 1.00 74.90  ? 4532 ASN A CA    1 
ATOM   22720 C  C     . ASN A 1 4532 ? 196.503 187.022 126.730 1.00 73.95  ? 4532 ASN A C     1 
ATOM   22721 O  O     . ASN A 1 4532 ? 196.245 186.949 125.524 1.00 73.08  ? 4532 ASN A O     1 
ATOM   22722 C  CB    . ASN A 1 4532 ? 197.641 184.798 126.892 1.00 75.05  ? 4532 ASN A CB    1 
ATOM   22723 C  CG    . ASN A 1 4532 ? 198.884 184.031 127.296 1.00 76.03  ? 4532 ASN A CG    1 
ATOM   22724 O  OD1   . ASN A 1 4532 ? 199.984 184.582 127.323 1.00 75.68  ? 4532 ASN A OD1   1 
ATOM   22725 N  ND2   . ASN A 1 4532 ? 198.715 182.754 127.616 1.00 76.22  ? 4532 ASN A ND2   1 
ATOM   22726 N  N     . SER A 1 4533 ? 195.764 187.738 127.581 1.00 74.29  ? 4533 SER A N     1 
ATOM   22727 C  CA    . SER A 1 4533 ? 194.620 188.551 127.161 1.00 76.50  ? 4533 SER A CA    1 
ATOM   22728 C  C     . SER A 1 4533 ? 193.575 187.710 126.426 1.00 76.53  ? 4533 SER A C     1 
ATOM   22729 O  O     . SER A 1 4533 ? 193.152 188.032 125.314 1.00 73.42  ? 4533 SER A O     1 
ATOM   22730 C  CB    . SER A 1 4533 ? 195.073 189.736 126.304 1.00 77.13  ? 4533 SER A CB    1 
ATOM   22731 O  OG    . SER A 1 4533 ? 193.973 190.547 125.931 1.00 73.00  ? 4533 SER A OG    1 
ATOM   22732 N  N     . TRP A 1 4534 ? 193.157 186.621 127.062 1.00 75.64  ? 4534 TRP A N     1 
ATOM   22733 C  CA    . TRP A 1 4534 ? 192.133 185.736 126.527 1.00 76.92  ? 4534 TRP A CA    1 
ATOM   22734 C  C     . TRP A 1 4534 ? 191.004 185.583 127.538 1.00 78.96  ? 4534 TRP A C     1 
ATOM   22735 O  O     . TRP A 1 4534 ? 191.076 186.073 128.668 1.00 78.76  ? 4534 TRP A O     1 
ATOM   22736 C  CB    . TRP A 1 4534 ? 192.715 184.362 126.170 1.00 79.56  ? 4534 TRP A CB    1 
ATOM   22737 C  CG    . TRP A 1 4534 ? 193.809 184.412 125.149 1.00 83.14  ? 4534 TRP A CG    1 
ATOM   22738 C  CD1   . TRP A 1 4534 ? 193.939 185.307 124.128 1.00 77.74  ? 4534 TRP A CD1   1 
ATOM   22739 C  CD2   . TRP A 1 4534 ? 194.926 183.520 125.044 1.00 80.88  ? 4534 TRP A CD2   1 
ATOM   22740 N  NE1   . TRP A 1 4534 ? 195.069 185.033 123.397 1.00 77.07  ? 4534 TRP A NE1   1 
ATOM   22741 C  CE2   . TRP A 1 4534 ? 195.693 183.940 123.938 1.00 79.83  ? 4534 TRP A CE2   1 
ATOM   22742 C  CE3   . TRP A 1 4534 ? 195.352 182.409 125.777 1.00 79.69  ? 4534 TRP A CE3   1 
ATOM   22743 C  CZ2   . TRP A 1 4534 ? 196.862 183.288 123.550 1.00 79.74  ? 4534 TRP A CZ2   1 
ATOM   22744 C  CZ3   . TRP A 1 4534 ? 196.513 181.763 125.390 1.00 78.61  ? 4534 TRP A CZ3   1 
ATOM   22745 C  CH2   . TRP A 1 4534 ? 197.254 182.205 124.286 1.00 78.89  ? 4534 TRP A CH2   1 
ATOM   22746 N  N     . SER A 1 4535 ? 189.950 184.893 127.117 1.00 78.29  ? 4535 SER A N     1 
ATOM   22747 C  CA    . SER A 1 4535 ? 188.806 184.632 127.975 1.00 81.12  ? 4535 SER A CA    1 
ATOM   22748 C  C     . SER A 1 4535 ? 188.934 183.265 128.640 1.00 77.99  ? 4535 SER A C     1 
ATOM   22749 O  O     . SER A 1 4535 ? 189.645 182.377 128.164 1.00 81.17  ? 4535 SER A O     1 
ATOM   22750 C  CB    . SER A 1 4535 ? 187.502 184.709 127.181 1.00 85.40  ? 4535 SER A CB    1 
ATOM   22751 O  OG    . SER A 1 4535 ? 186.385 184.420 128.003 1.00 80.85  ? 4535 SER A OG    1 
ATOM   22752 N  N     . LEU A 1 4536 ? 188.229 183.110 129.763 1.00 75.62  ? 4536 LEU A N     1 
ATOM   22753 C  CA    . LEU A 1 4536 ? 188.266 181.848 130.496 1.00 76.13  ? 4536 LEU A CA    1 
ATOM   22754 C  C     . LEU A 1 4536 ? 187.703 180.704 129.661 1.00 79.80  ? 4536 LEU A C     1 
ATOM   22755 O  O     . LEU A 1 4536 ? 188.260 179.600 129.651 1.00 79.77  ? 4536 LEU A O     1 
ATOM   22756 C  CB    . LEU A 1 4536 ? 187.493 181.980 131.808 1.00 76.84  ? 4536 LEU A CB    1 
ATOM   22757 C  CG    . LEU A 1 4536 ? 188.037 182.963 132.844 1.00 73.21  ? 4536 LEU A CG    1 
ATOM   22758 C  CD1   . LEU A 1 4536 ? 187.255 184.267 132.809 1.00 62.80  ? 4536 LEU A CD1   1 
ATOM   22759 C  CD2   . LEU A 1 4536 ? 187.985 182.342 134.229 1.00 63.88  ? 4536 LEU A CD2   1 
ATOM   22760 N  N     . GLU A 1 4537 ? 186.598 180.948 128.954 1.00 81.29  ? 4537 GLU A N     1 
ATOM   22761 C  CA    . GLU A 1 4537 ? 185.960 179.901 128.165 1.00 76.35  ? 4537 GLU A CA    1 
ATOM   22762 C  C     . GLU A 1 4537 ? 186.761 179.515 126.929 1.00 75.52  ? 4537 GLU A C     1 
ATOM   22763 O  O     . GLU A 1 4537 ? 186.439 178.503 126.297 1.00 78.30  ? 4537 GLU A O     1 
ATOM   22764 C  CB    . GLU A 1 4537 ? 184.553 180.339 127.758 1.00 73.13  ? 4537 GLU A CB    1 
ATOM   22765 C  CG    . GLU A 1 4537 ? 183.612 180.550 128.935 1.00 71.63  ? 4537 GLU A CG    1 
ATOM   22766 C  CD    . GLU A 1 4537 ? 182.215 180.950 128.504 1.00 63.02  ? 4537 GLU A CD    1 
ATOM   22767 O  OE1   . GLU A 1 4537 ? 181.636 180.257 127.641 1.00 66.22  ? 4537 GLU A OE1   1 
ATOM   22768 O  OE2   . GLU A 1 4537 ? 181.696 181.956 129.030 1.00 54.38  ? 4537 GLU A OE2   1 
ATOM   22769 N  N     . GLU A 1 4538 ? 187.786 180.284 126.570 1.00 75.25  ? 4538 GLU A N     1 
ATOM   22770 C  CA    . GLU A 1 4538 ? 188.656 179.947 125.452 1.00 78.90  ? 4538 GLU A CA    1 
ATOM   22771 C  C     . GLU A 1 4538 ? 189.875 179.140 125.875 1.00 75.74  ? 4538 GLU A C     1 
ATOM   22772 O  O     . GLU A 1 4538 ? 190.711 178.817 125.025 1.00 77.53  ? 4538 GLU A O     1 
ATOM   22773 C  CB    . GLU A 1 4538 ? 189.117 181.220 124.732 1.00 83.20  ? 4538 GLU A CB    1 
ATOM   22774 C  CG    . GLU A 1 4538 ? 188.004 182.202 124.409 1.00 88.54  ? 4538 GLU A CG    1 
ATOM   22775 C  CD    . GLU A 1 4538 ? 188.531 183.589 124.096 1.00 90.53  ? 4538 GLU A CD    1 
ATOM   22776 O  OE1   . GLU A 1 4538 ? 189.761 183.792 124.179 1.00 88.08  ? 4538 GLU A OE1   1 
ATOM   22777 O  OE2   . GLU A 1 4538 ? 187.716 184.478 123.771 1.00 94.53  ? 4538 GLU A OE2   1 
ATOM   22778 N  N     . LEU A 1 4539 ? 189.996 178.807 127.157 1.00 73.13  ? 4539 LEU A N     1 
ATOM   22779 C  CA    . LEU A 1 4539 ? 191.155 178.105 127.688 1.00 72.65  ? 4539 LEU A CA    1 
ATOM   22780 C  C     . LEU A 1 4539 ? 190.759 176.693 128.096 1.00 68.86  ? 4539 LEU A C     1 
ATOM   22781 O  O     . LEU A 1 4539 ? 189.814 176.507 128.870 1.00 71.86  ? 4539 LEU A O     1 
ATOM   22782 C  CB    . LEU A 1 4539 ? 191.743 178.853 128.887 1.00 67.04  ? 4539 LEU A CB    1 
ATOM   22783 C  CG    . LEU A 1 4539 ? 192.615 180.073 128.586 1.00 68.34  ? 4539 LEU A CG    1 
ATOM   22784 C  CD1   . LEU A 1 4539 ? 193.058 180.740 129.878 1.00 65.56  ? 4539 LEU A CD1   1 
ATOM   22785 C  CD2   . LEU A 1 4539 ? 193.817 179.683 127.743 1.00 72.13  ? 4539 LEU A CD2   1 
ATOM   22786 N  N     . CYS A 1 4540 ? 191.483 175.705 127.578 1.00 64.99  ? 4540 CYS A N     1 
ATOM   22787 C  CA    . CYS A 1 4540 ? 191.301 174.312 127.952 1.00 61.42  ? 4540 CYS A CA    1 
ATOM   22788 C  C     . CYS A 1 4540 ? 192.504 173.845 128.760 1.00 60.94  ? 4540 CYS A C     1 
ATOM   22789 O  O     . CYS A 1 4540 ? 193.631 174.307 128.563 1.00 68.30  ? 4540 CYS A O     1 
ATOM   22790 C  CB    . CYS A 1 4540 ? 191.105 173.417 126.721 1.00 62.39  ? 4540 CYS A CB    1 
ATOM   22791 S  SG    . CYS A 1 4540 ? 192.625 172.983 125.846 1.00 74.61  ? 4540 CYS A SG    1 
ATOM   22792 N  N     . LEU A 1 4541 ? 192.252 172.921 129.680 1.00 51.87  ? 4541 LEU A N     1 
ATOM   22793 C  CA    . LEU A 1 4541 ? 193.257 172.478 130.634 1.00 47.34  ? 4541 LEU A CA    1 
ATOM   22794 C  C     . LEU A 1 4541 ? 193.966 171.238 130.107 1.00 50.42  ? 4541 LEU A C     1 
ATOM   22795 O  O     . LEU A 1 4541 ? 193.321 170.235 129.787 1.00 55.08  ? 4541 LEU A O     1 
ATOM   22796 C  CB    . LEU A 1 4541 ? 192.620 172.187 131.993 1.00 45.75  ? 4541 LEU A CB    1 
ATOM   22797 C  CG    . LEU A 1 4541 ? 193.551 171.654 133.081 1.00 45.07  ? 4541 LEU A CG    1 
ATOM   22798 C  CD1   . LEU A 1 4541 ? 194.745 172.575 133.247 1.00 46.46  ? 4541 LEU A CD1   1 
ATOM   22799 C  CD2   . LEU A 1 4541 ? 192.804 171.504 134.395 1.00 40.86  ? 4541 LEU A CD2   1 
ATOM   22800 N  N     . GLU A 1 4542 ? 195.291 171.315 130.019 1.00 51.05  ? 4542 GLU A N     1 
ATOM   22801 C  CA    . GLU A 1 4542 ? 196.132 170.189 129.639 1.00 48.79  ? 4542 GLU A CA    1 
ATOM   22802 C  C     . GLU A 1 4542 ? 196.914 169.726 130.859 1.00 48.86  ? 4542 GLU A C     1 
ATOM   22803 O  O     . GLU A 1 4542 ? 197.409 170.548 131.637 1.00 53.11  ? 4542 GLU A O     1 
ATOM   22804 C  CB    . GLU A 1 4542 ? 197.088 170.569 128.502 1.00 51.42  ? 4542 GLU A CB    1 
ATOM   22805 C  CG    . GLU A 1 4542 ? 198.029 169.455 128.075 1.00 57.68  ? 4542 GLU A CG    1 
ATOM   22806 C  CD    . GLU A 1 4542 ? 199.238 169.970 127.321 1.00 68.20  ? 4542 GLU A CD    1 
ATOM   22807 O  OE1   . GLU A 1 4542 ? 199.059 170.527 126.217 1.00 68.91  ? 4542 GLU A OE1   1 
ATOM   22808 O  OE2   . GLU A 1 4542 ? 200.368 169.819 127.831 1.00 67.06  ? 4542 GLU A OE2   1 
ATOM   22809 N  N     . VAL A 1 4543 ? 197.021 168.411 131.027 1.00 47.16  ? 4543 VAL A N     1 
ATOM   22810 C  CA    . VAL A 1 4543 ? 197.636 167.815 132.206 1.00 44.67  ? 4543 VAL A CA    1 
ATOM   22811 C  C     . VAL A 1 4543 ? 198.826 166.976 131.764 1.00 46.52  ? 4543 VAL A C     1 
ATOM   22812 O  O     . VAL A 1 4543 ? 198.704 166.143 130.857 1.00 43.73  ? 4543 VAL A O     1 
ATOM   22813 C  CB    . VAL A 1 4543 ? 196.627 166.966 133.003 1.00 41.67  ? 4543 VAL A CB    1 
ATOM   22814 C  CG1   . VAL A 1 4543 ? 197.333 165.849 133.758 1.00 41.36  ? 4543 VAL A CG1   1 
ATOM   22815 C  CG2   . VAL A 1 4543 ? 195.843 167.848 133.959 1.00 44.75  ? 4543 VAL A CG2   1 
ATOM   22816 N  N     . ASN A 1 4544 ? 199.973 167.207 132.397 1.00 47.18  ? 4544 ASN A N     1 
ATOM   22817 C  CA    . ASN A 1 4544 ? 201.190 166.443 132.158 1.00 44.48  ? 4544 ASN A CA    1 
ATOM   22818 C  C     . ASN A 1 4544 ? 201.689 165.908 133.492 1.00 46.18  ? 4544 ASN A C     1 
ATOM   22819 O  O     . ASN A 1 4544 ? 201.921 166.684 134.426 1.00 50.21  ? 4544 ASN A O     1 
ATOM   22820 C  CB    . ASN A 1 4544 ? 202.257 167.308 131.485 1.00 47.31  ? 4544 ASN A CB    1 
ATOM   22821 C  CG    . ASN A 1 4544 ? 203.507 166.527 131.138 1.00 54.95  ? 4544 ASN A CG    1 
ATOM   22822 O  OD1   . ASN A 1 4544 ? 203.441 165.476 130.501 1.00 50.29  ? 4544 ASN A OD1   1 
ATOM   22823 N  ND2   . ASN A 1 4544 ? 204.659 167.040 131.554 1.00 60.75  ? 4544 ASN A ND2   1 
ATOM   22824 N  N     . VAL A 1 4545 ? 201.855 164.593 133.581 1.00 48.86  ? 4545 VAL A N     1 
ATOM   22825 C  CA    . VAL A 1 4545 ? 202.283 163.933 134.809 1.00 52.06  ? 4545 VAL A CA    1 
ATOM   22826 C  C     . VAL A 1 4545 ? 203.741 163.531 134.635 1.00 56.40  ? 4545 VAL A C     1 
ATOM   22827 O  O     . VAL A 1 4545 ? 204.069 162.687 133.793 1.00 56.43  ? 4545 VAL A O     1 
ATOM   22828 C  CB    . VAL A 1 4545 ? 201.404 162.720 135.137 1.00 48.90  ? 4545 VAL A CB    1 
ATOM   22829 C  CG1   . VAL A 1 4545 ? 201.892 162.039 136.405 1.00 47.04  ? 4545 VAL A CG1   1 
ATOM   22830 C  CG2   . VAL A 1 4545 ? 199.954 163.145 135.282 1.00 42.40  ? 4545 VAL A CG2   1 
ATOM   22831 N  N     . THR A 1 4546 ? 204.619 164.132 135.435 1.00 61.81  ? 4546 THR A N     1 
ATOM   22832 C  CA    . THR A 1 4546 ? 206.048 163.865 135.371 1.00 69.78  ? 4546 THR A CA    1 
ATOM   22833 C  C     . THR A 1 4546 ? 206.619 163.841 136.781 1.00 77.73  ? 4546 THR A C     1 
ATOM   22834 O  O     . THR A 1 4546 ? 205.981 164.278 137.741 1.00 74.46  ? 4546 THR A O     1 
ATOM   22835 C  CB    . THR A 1 4546 ? 206.793 164.912 134.528 1.00 72.49  ? 4546 THR A CB    1 
ATOM   22836 O  OG1   . THR A 1 4546 ? 206.378 166.228 134.918 1.00 72.92  ? 4546 THR A OG1   1 
ATOM   22837 C  CG2   . THR A 1 4546 ? 206.521 164.710 133.044 1.00 63.86  ? 4546 THR A CG2   1 
ATOM   22838 N  N     . THR A 1 4547 ? 207.835 163.314 136.892 1.00 86.34  ? 4547 THR A N     1 
ATOM   22839 C  CA    . THR A 1 4547 ? 208.542 163.312 138.163 1.00 89.86  ? 4547 THR A CA    1 
ATOM   22840 C  C     . THR A 1 4547 ? 208.855 164.743 138.592 1.00 90.30  ? 4547 THR A C     1 
ATOM   22841 O  O     . THR A 1 4547 ? 209.083 165.628 137.763 1.00 91.18  ? 4547 THR A O     1 
ATOM   22842 C  CB    . THR A 1 4547 ? 209.832 162.496 138.053 1.00 92.54  ? 4547 THR A CB    1 
ATOM   22843 O  OG1   . THR A 1 4547 ? 209.544 161.229 137.449 1.00 93.20  ? 4547 THR A OG1   1 
ATOM   22844 C  CG2   . THR A 1 4547 ? 210.442 162.257 139.428 1.00 89.16  ? 4547 THR A CG2   1 
ATOM   22845 N  N     . SER A 1 4548 ? 208.850 164.967 139.909 1.00 87.04  ? 4548 SER A N     1 
ATOM   22846 C  CA    . SER A 1 4548 ? 209.126 166.301 140.432 1.00 91.53  ? 4548 SER A CA    1 
ATOM   22847 C  C     . SER A 1 4548 ? 210.531 166.761 140.062 1.00 93.50  ? 4548 SER A C     1 
ATOM   22848 O  O     . SER A 1 4548 ? 210.738 167.929 139.713 1.00 88.97  ? 4548 SER A O     1 
ATOM   22849 C  CB    . SER A 1 4548 ? 208.937 166.321 141.949 1.00 83.40  ? 4548 SER A CB    1 
ATOM   22850 O  OG    . SER A 1 4548 ? 209.157 167.619 142.473 1.00 78.70  ? 4548 SER A OG    1 
ATOM   22851 N  N     . GLN A 1 4549 ? 211.511 165.858 140.140 1.00 93.02  ? 4549 GLN A N     1 
ATOM   22852 C  CA    . GLN A 1 4549 ? 212.875 166.208 139.756 1.00 94.17  ? 4549 GLN A CA    1 
ATOM   22853 C  C     . GLN A 1 4549 ? 212.957 166.554 138.274 1.00 93.64  ? 4549 GLN A C     1 
ATOM   22854 O  O     . GLN A 1 4549 ? 213.612 167.530 137.889 1.00 90.33  ? 4549 GLN A O     1 
ATOM   22855 C  CB    . GLN A 1 4549 ? 213.824 165.059 140.097 1.00 98.42  ? 4549 GLN A CB    1 
ATOM   22856 C  CG    . GLN A 1 4549 ? 213.714 164.572 141.533 1.00 104.94 ? 4549 GLN A CG    1 
ATOM   22857 C  CD    . GLN A 1 4549 ? 214.525 163.317 141.788 1.00 109.11 ? 4549 GLN A CD    1 
ATOM   22858 O  OE1   . GLN A 1 4549 ? 215.436 163.310 142.616 1.00 106.68 ? 4549 GLN A OE1   1 
ATOM   22859 N  NE2   . GLN A 1 4549 ? 214.197 162.246 141.076 1.00 106.64 ? 4549 GLN A NE2   1 
ATOM   22860 N  N     . GLY A 1 4550 ? 212.297 165.767 137.428 1.00 93.32  ? 4550 GLY A N     1 
ATOM   22861 C  CA    . GLY A 1 4550 ? 212.298 166.020 136.001 1.00 93.15  ? 4550 GLY A CA    1 
ATOM   22862 C  C     . GLY A 1 4550 ? 211.108 166.830 135.531 1.00 94.98  ? 4550 GLY A C     1 
ATOM   22863 O  O     . GLY A 1 4550 ? 210.354 166.385 134.660 1.00 90.01  ? 4550 GLY A O     1 
ATOM   22864 N  N     . ALA A 1 4551 ? 210.925 168.020 136.098 1.00 97.14  ? 4551 ALA A N     1 
ATOM   22865 C  CA    . ALA A 1 4551 ? 209.807 168.885 135.753 1.00 91.96  ? 4551 ALA A CA    1 
ATOM   22866 C  C     . ALA A 1 4551 ? 210.301 170.299 135.492 1.00 91.76  ? 4551 ALA A C     1 
ATOM   22867 O  O     . ALA A 1 4551 ? 211.171 170.806 136.208 1.00 85.72  ? 4551 ALA A O     1 
ATOM   22868 C  CB    . ALA A 1 4551 ? 208.752 168.899 136.864 1.00 86.85  ? 4551 ALA A CB    1 
ATOM   22869 N  N     . THR A 1 4552 ? 209.743 170.931 134.461 1.00 92.83  ? 4552 THR A N     1 
ATOM   22870 C  CA    . THR A 1 4552 ? 210.031 172.320 134.129 1.00 91.32  ? 4552 THR A CA    1 
ATOM   22871 C  C     . THR A 1 4552 ? 208.716 173.070 133.988 1.00 85.21  ? 4552 THR A C     1 
ATOM   22872 O  O     . THR A 1 4552 ? 207.833 172.643 133.238 1.00 80.82  ? 4552 THR A O     1 
ATOM   22873 C  CB    . THR A 1 4552 ? 210.847 172.433 132.836 1.00 89.27  ? 4552 THR A CB    1 
ATOM   22874 O  OG1   . THR A 1 4552 ? 210.174 171.735 131.780 1.00 92.94  ? 4552 THR A OG1   1 
ATOM   22875 C  CG2   . THR A 1 4552 ? 212.236 171.842 133.025 1.00 83.23  ? 4552 THR A CG2   1 
ATOM   22876 N  N     . LEU A 1 4553 ? 208.589 174.184 134.706 1.00 82.02  ? 4553 LEU A N     1 
ATOM   22877 C  CA    . LEU A 1 4553 ? 207.364 174.977 134.720 1.00 74.52  ? 4553 LEU A CA    1 
ATOM   22878 C  C     . LEU A 1 4553 ? 207.500 176.117 133.718 1.00 74.68  ? 4553 LEU A C     1 
ATOM   22879 O  O     . LEU A 1 4553 ? 208.344 177.004 133.884 1.00 77.36  ? 4553 LEU A O     1 
ATOM   22880 C  CB    . LEU A 1 4553 ? 207.081 175.511 136.123 1.00 69.78  ? 4553 LEU A CB    1 
ATOM   22881 C  CG    . LEU A 1 4553 ? 206.511 174.514 137.135 1.00 70.47  ? 4553 LEU A CG    1 
ATOM   22882 C  CD1   . LEU A 1 4553 ? 205.925 175.244 138.334 1.00 64.80  ? 4553 LEU A CD1   1 
ATOM   22883 C  CD2   . LEU A 1 4553 ? 205.466 173.622 136.485 1.00 60.89  ? 4553 LEU A CD2   1 
ATOM   22884 N  N     . ASP A 1 4554 ? 206.669 176.092 132.680 1.00 71.67  ? 4554 ASP A N     1 
ATOM   22885 C  CA    . ASP A 1 4554 ? 206.624 177.163 131.697 1.00 68.58  ? 4554 ASP A CA    1 
ATOM   22886 C  C     . ASP A 1 4554 ? 205.580 178.196 132.123 1.00 65.79  ? 4554 ASP A C     1 
ATOM   22887 O  O     . ASP A 1 4554 ? 205.097 178.192 133.259 1.00 67.21  ? 4554 ASP A O     1 
ATOM   22888 C  CB    . ASP A 1 4554 ? 206.356 176.599 130.303 1.00 65.56  ? 4554 ASP A CB    1 
ATOM   22889 C  CG    . ASP A 1 4554 ? 205.171 175.659 130.272 1.00 68.28  ? 4554 ASP A CG    1 
ATOM   22890 O  OD1   . ASP A 1 4554 ? 204.033 176.125 130.483 1.00 68.41  ? 4554 ASP A OD1   1 
ATOM   22891 O  OD2   . ASP A 1 4554 ? 205.377 174.450 130.034 1.00 70.72  ? 4554 ASP A OD2   1 
ATOM   22892 N  N     . ALA A 1 4555 ? 205.228 179.102 131.207 1.00 62.44  ? 4555 ALA A N     1 
ATOM   22893 C  CA    . ALA A 1 4555 ? 204.343 180.211 131.554 1.00 60.15  ? 4555 ALA A CA    1 
ATOM   22894 C  C     . ALA A 1 4555 ? 202.966 179.723 131.992 1.00 60.31  ? 4555 ALA A C     1 
ATOM   22895 O  O     . ALA A 1 4555 ? 202.398 180.241 132.961 1.00 60.72  ? 4555 ALA A O     1 
ATOM   22896 C  CB    . ALA A 1 4555 ? 204.220 181.170 130.371 1.00 55.84  ? 4555 ALA A CB    1 
ATOM   22897 N  N     . CYS A 1 4556 ? 202.409 178.738 131.292 1.00 62.31  ? 4556 CYS A N     1 
ATOM   22898 C  CA    . CYS A 1 4556 ? 201.069 178.244 131.581 1.00 62.64  ? 4556 CYS A CA    1 
ATOM   22899 C  C     . CYS A 1 4556 ? 201.065 177.024 132.495 1.00 58.25  ? 4556 CYS A C     1 
ATOM   22900 O  O     . CYS A 1 4556 ? 199.994 176.474 132.767 1.00 57.36  ? 4556 CYS A O     1 
ATOM   22901 C  CB    . CYS A 1 4556 ? 200.334 177.921 130.279 1.00 64.04  ? 4556 CYS A CB    1 
ATOM   22902 S  SG    . CYS A 1 4556 ? 201.262 176.887 129.123 1.00 74.19  ? 4556 CYS A SG    1 
ATOM   22903 N  N     . SER A 1 4557 ? 202.227 176.596 132.982 1.00 56.25  ? 4557 SER A N     1 
ATOM   22904 C  CA    . SER A 1 4557 ? 202.345 175.376 133.770 1.00 53.91  ? 4557 SER A CA    1 
ATOM   22905 C  C     . SER A 1 4557 ? 202.306 175.696 135.259 1.00 55.51  ? 4557 SER A C     1 
ATOM   22906 O  O     . SER A 1 4557 ? 202.988 176.616 135.722 1.00 58.16  ? 4557 SER A O     1 
ATOM   22907 C  CB    . SER A 1 4557 ? 203.637 174.632 133.431 1.00 61.68  ? 4557 SER A CB    1 
ATOM   22908 O  OG    . SER A 1 4557 ? 203.552 174.012 132.162 1.00 66.04  ? 4557 SER A OG    1 
ATOM   22909 N  N     . PHE A 1 4558 ? 201.506 174.932 136.000 1.00 51.72  ? 4558 PHE A N     1 
ATOM   22910 C  CA    . PHE A 1 4558 ? 201.433 175.020 137.450 1.00 43.51  ? 4558 PHE A CA    1 
ATOM   22911 C  C     . PHE A 1 4558 ? 201.636 173.634 138.043 1.00 49.09  ? 4558 PHE A C     1 
ATOM   22912 O  O     . PHE A 1 4558 ? 201.084 172.650 137.542 1.00 56.04  ? 4558 PHE A O     1 
ATOM   22913 C  CB    . PHE A 1 4558 ? 200.090 175.599 137.909 1.00 42.25  ? 4558 PHE A CB    1 
ATOM   22914 C  CG    . PHE A 1 4558 ? 199.846 177.006 137.446 1.00 47.55  ? 4558 PHE A CG    1 
ATOM   22915 C  CD1   . PHE A 1 4558 ? 200.268 178.082 138.209 1.00 44.82  ? 4558 PHE A CD1   1 
ATOM   22916 C  CD2   . PHE A 1 4558 ? 199.204 177.254 136.244 1.00 47.51  ? 4558 PHE A CD2   1 
ATOM   22917 C  CE1   . PHE A 1 4558 ? 200.046 179.377 137.786 1.00 50.23  ? 4558 PHE A CE1   1 
ATOM   22918 C  CE2   . PHE A 1 4558 ? 198.982 178.547 135.816 1.00 49.11  ? 4558 PHE A CE2   1 
ATOM   22919 C  CZ    . PHE A 1 4558 ? 199.404 179.610 136.588 1.00 49.30  ? 4558 PHE A CZ    1 
ATOM   22920 N  N     . GLY A 1 4559 ? 202.429 173.561 139.108 1.00 50.49  ? 4559 GLY A N     1 
ATOM   22921 C  CA    . GLY A 1 4559 ? 202.734 172.291 139.742 1.00 43.98  ? 4559 GLY A CA    1 
ATOM   22922 C  C     . GLY A 1 4559 ? 201.749 171.960 140.852 1.00 45.36  ? 4559 GLY A C     1 
ATOM   22923 O  O     . GLY A 1 4559 ? 201.450 172.792 141.706 1.00 50.68  ? 4559 GLY A O     1 
ATOM   22924 N  N     . VAL A 1 4560 ? 201.248 170.728 140.824 1.00 46.91  ? 4560 VAL A N     1 
ATOM   22925 C  CA    . VAL A 1 4560 ? 200.297 170.238 141.816 1.00 44.44  ? 4560 VAL A CA    1 
ATOM   22926 C  C     . VAL A 1 4560 ? 200.806 168.910 142.356 1.00 40.83  ? 4560 VAL A C     1 
ATOM   22927 O  O     . VAL A 1 4560 ? 201.135 168.005 141.583 1.00 41.21  ? 4560 VAL A O     1 
ATOM   22928 C  CB    . VAL A 1 4560 ? 198.882 170.080 141.225 1.00 40.53  ? 4560 VAL A CB    1 
ATOM   22929 C  CG1   . VAL A 1 4560 ? 198.007 169.250 142.149 1.00 40.41  ? 4560 VAL A CG1   1 
ATOM   22930 C  CG2   . VAL A 1 4560 ? 198.259 171.442 140.982 1.00 39.85  ? 4560 VAL A CG2   1 
ATOM   22931 N  N     . THR A 1 4561 ? 200.845 168.792 143.686 1.00 43.21  ? 4561 THR A N     1 
ATOM   22932 C  CA    . THR A 1 4561 ? 201.306 167.543 144.327 1.00 40.21  ? 4561 THR A CA    1 
ATOM   22933 C  C     . THR A 1 4561 ? 200.192 166.989 145.187 1.00 42.43  ? 4561 THR A C     1 
ATOM   22934 O  O     . THR A 1 4561 ? 199.311 167.781 145.589 1.00 43.84  ? 4561 THR A O     1 
ATOM   22935 C  CB    . THR A 1 4561 ? 202.555 167.841 145.154 1.00 40.50  ? 4561 THR A CB    1 
ATOM   22936 O  OG1   . THR A 1 4561 ? 202.130 168.788 146.129 1.00 39.86  ? 4561 THR A OG1   1 
ATOM   22937 C  CG2   . THR A 1 4561 ? 203.681 168.424 144.320 1.00 44.63  ? 4561 THR A CG2   1 
ATOM   22938 N  N     . GLY A 1 4562 ? 200.217 165.683 145.468 1.00 41.82  ? 4562 GLY A N     1 
ATOM   22939 C  CA    . GLY A 1 4562 ? 199.210 165.072 146.358 1.00 39.51  ? 4562 GLY A CA    1 
ATOM   22940 C  C     . GLY A 1 4562 ? 198.052 164.462 145.589 1.00 43.74  ? 4562 GLY A C     1 
ATOM   22941 O  O     . GLY A 1 4562 ? 197.154 163.887 146.238 1.00 47.93  ? 4562 GLY A O     1 
ATOM   22942 N  N     . LEU A 1 4563 ? 198.066 164.573 144.257 1.00 41.59  ? 4563 LEU A N     1 
ATOM   22943 C  CA    . LEU A 1 4563 ? 196.995 163.963 143.425 1.00 32.74  ? 4563 LEU A CA    1 
ATOM   22944 C  C     . LEU A 1 4563 ? 197.182 162.437 143.406 1.00 36.81  ? 4563 LEU A C     1 
ATOM   22945 O  O     . LEU A 1 4563 ? 198.317 161.982 143.153 1.00 40.39  ? 4563 LEU A O     1 
ATOM   22946 C  CB    . LEU A 1 4563 ? 197.005 164.553 142.016 1.00 35.26  ? 4563 LEU A CB    1 
ATOM   22947 C  CG    . LEU A 1 4563 ? 196.587 166.022 141.907 1.00 32.71  ? 4563 LEU A CG    1 
ATOM   22948 C  CD1   . LEU A 1 4563 ? 196.469 166.441 140.453 1.00 32.20  ? 4563 LEU A CD1   1 
ATOM   22949 C  CD2   . LEU A 1 4563 ? 195.281 166.266 142.645 1.00 32.58  ? 4563 LEU A CD2   1 
ATOM   22950 N  N     . LYS A 1 4564 ? 196.107 161.687 143.666 1.00 41.40  ? 4564 LYS A N     1 
ATOM   22951 C  CA    . LYS A 1 4564 ? 196.189 160.203 143.690 1.00 40.03  ? 4564 LYS A CA    1 
ATOM   22952 C  C     . LYS A 1 4564 ? 195.240 159.620 142.632 1.00 31.80  ? 4564 LYS A C     1 
ATOM   22953 O  O     . LYS A 1 4564 ? 194.021 159.884 142.722 1.00 33.31  ? 4564 LYS A O     1 
ATOM   22954 C  CB    . LYS A 1 4564 ? 195.826 159.677 145.082 1.00 37.32  ? 4564 LYS A CB    1 
ATOM   22955 C  CG    . LYS A 1 4564 ? 196.665 160.237 146.220 1.00 42.85  ? 4564 LYS A CG    1 
ATOM   22956 C  CD    . LYS A 1 4564 ? 198.152 159.961 146.040 1.00 42.51  ? 4564 LYS A CD    1 
ATOM   22957 C  CE    . LYS A 1 4564 ? 198.974 160.485 147.173 1.00 43.37  ? 4564 LYS A CE    1 
ATOM   22958 N  NZ    . LYS A 1 4564 ? 198.829 161.935 147.317 1.00 42.75  ? 4564 LYS A NZ    1 
ATOM   22959 N  N     . LEU A 1 4565 ? 195.778 158.860 141.675 1.00 28.33  ? 4565 LEU A N     1 
ATOM   22960 C  CA    . LEU A 1 4565 ? 194.929 158.207 140.645 1.00 28.14  ? 4565 LEU A CA    1 
ATOM   22961 C  C     . LEU A 1 4565 ? 194.293 156.952 141.261 1.00 32.48  ? 4565 LEU A C     1 
ATOM   22962 O  O     . LEU A 1 4565 ? 194.975 156.281 142.066 1.00 36.47  ? 4565 LEU A O     1 
ATOM   22963 C  CB    . LEU A 1 4565 ? 195.763 157.876 139.408 1.00 32.42  ? 4565 LEU A CB    1 
ATOM   22964 C  CG    . LEU A 1 4565 ? 195.015 157.199 138.256 1.00 28.62  ? 4565 LEU A CG    1 
ATOM   22965 C  CD1   . LEU A 1 4565 ? 193.763 157.982 137.901 1.00 29.34  ? 4565 LEU A CD1   1 
ATOM   22966 C  CD2   . LEU A 1 4565 ? 195.926 157.077 137.048 1.00 34.09  ? 4565 LEU A CD2   1 
ATOM   22967 N  N     . GLN A 1 4566 ? 193.042 156.653 140.901 1.00 26.59  ? 4566 GLN A N     1 
ATOM   22968 C  CA    . GLN A 1 4566 ? 192.335 155.499 141.514 1.00 27.01  ? 4566 GLN A CA    1 
ATOM   22969 C  C     . GLN A 1 4566 ? 192.003 154.455 140.439 1.00 26.82  ? 4566 GLN A C     1 
ATOM   22970 O  O     . GLN A 1 4566 ? 191.249 154.793 139.503 1.00 29.29  ? 4566 GLN A O     1 
ATOM   22971 C  CB    . GLN A 1 4566 ? 191.061 155.983 142.206 1.00 28.84  ? 4566 GLN A CB    1 
ATOM   22972 C  CG    . GLN A 1 4566 ? 191.291 157.128 143.187 1.00 31.35  ? 4566 GLN A CG    1 
ATOM   22973 C  CD    . GLN A 1 4566 ? 192.357 156.823 144.217 1.00 36.52  ? 4566 GLN A CD    1 
ATOM   22974 O  OE1   . GLN A 1 4566 ? 192.253 155.861 144.987 1.00 42.69  ? 4566 GLN A OE1   1 
ATOM   22975 N  NE2   . GLN A 1 4566 ? 193.398 157.641 144.238 1.00 36.72  ? 4566 GLN A NE2   1 
ATOM   22976 N  N     . GLY A 1 4567 ? 192.543 153.240 140.572 1.00 29.57  ? 4567 GLY A N     1 
ATOM   22977 C  CA    . GLY A 1 4567 ? 192.212 152.154 139.628 1.00 28.19  ? 4567 GLY A CA    1 
ATOM   22978 C  C     . GLY A 1 4567 ? 192.966 152.268 138.318 1.00 29.40  ? 4567 GLY A C     1 
ATOM   22979 O  O     . GLY A 1 4567 ? 192.579 151.567 137.360 1.00 31.70  ? 4567 GLY A O     1 
ATOM   22980 N  N     . ALA A 1 4568 ? 194.007 153.105 138.265 1.00 34.37  ? 4568 ALA A N     1 
ATOM   22981 C  CA    . ALA A 1 4568 ? 194.810 153.199 137.054 1.00 33.42  ? 4568 ALA A CA    1 
ATOM   22982 C  C     . ALA A 1 4568 ? 196.206 153.677 137.423 1.00 35.55  ? 4568 ALA A C     1 
ATOM   22983 O  O     . ALA A 1 4568 ? 196.432 154.233 138.500 1.00 38.58  ? 4568 ALA A O     1 
ATOM   22984 C  CB    . ALA A 1 4568 ? 194.164 154.133 136.026 1.00 33.08  ? 4568 ALA A CB    1 
ATOM   22985 N  N     . THR A 1 4569 ? 197.146 153.441 136.510 1.00 37.32  ? 4569 THR A N     1 
ATOM   22986 C  CA    . THR A 1 4569 ? 198.511 153.934 136.623 1.00 39.98  ? 4569 THR A CA    1 
ATOM   22987 C  C     . THR A 1 4569 ? 198.805 154.867 135.459 1.00 42.88  ? 4569 THR A C     1 
ATOM   22988 O  O     . THR A 1 4569 ? 198.304 154.665 134.348 1.00 43.27  ? 4569 THR A O     1 
ATOM   22989 C  CB    . THR A 1 4569 ? 199.537 152.792 136.631 1.00 40.42  ? 4569 THR A CB    1 
ATOM   22990 O  OG1   . THR A 1 4569 ? 199.875 152.439 135.284 1.00 47.50  ? 4569 THR A OG1   1 
ATOM   22991 C  CG2   . THR A 1 4569 ? 198.990 151.575 137.348 1.00 36.33  ? 4569 THR A CG2   1 
ATOM   22992 N  N     . CYS A 1 4570 ? 199.615 155.889 135.717 1.00 48.42  ? 4570 CYS A N     1 
ATOM   22993 C  CA    . CYS A 1 4570 ? 200.026 156.844 134.695 1.00 48.44  ? 4570 CYS A CA    1 
ATOM   22994 C  C     . CYS A 1 4570 ? 201.487 156.577 134.349 1.00 52.10  ? 4570 CYS A C     1 
ATOM   22995 O  O     . CYS A 1 4570 ? 202.370 156.720 135.201 1.00 52.68  ? 4570 CYS A O     1 
ATOM   22996 C  CB    . CYS A 1 4570 ? 199.825 158.279 135.175 1.00 46.44  ? 4570 CYS A CB    1 
ATOM   22997 S  SG    . CYS A 1 4570 ? 200.064 159.528 133.893 1.00 56.63  ? 4570 CYS A SG    1 
ATOM   22998 N  N     . ASN A 1 4571 ? 201.737 156.189 133.101 1.00 52.40  ? 4571 ASN A N     1 
ATOM   22999 C  CA    . ASN A 1 4571 ? 203.084 155.929 132.610 1.00 55.71  ? 4571 ASN A CA    1 
ATOM   23000 C  C     . ASN A 1 4571 ? 203.271 156.680 131.302 1.00 56.54  ? 4571 ASN A C     1 
ATOM   23001 O  O     . ASN A 1 4571 ? 202.543 156.431 130.335 1.00 60.28  ? 4571 ASN A O     1 
ATOM   23002 C  CB    . ASN A 1 4571 ? 203.322 154.429 132.412 1.00 52.94  ? 4571 ASN A CB    1 
ATOM   23003 C  CG    . ASN A 1 4571 ? 203.311 153.660 133.719 1.00 54.46  ? 4571 ASN A CG    1 
ATOM   23004 O  OD1   . ASN A 1 4571 ? 203.752 154.163 134.752 1.00 50.82  ? 4571 ASN A OD1   1 
ATOM   23005 N  ND2   . ASN A 1 4571 ? 202.803 152.433 133.679 1.00 50.47  ? 4571 ASN A ND2   1 
ATOM   23006 N  N     . ASN A 1 4572 ? 204.247 157.589 131.275 1.00 61.07  ? 4572 ASN A N     1 
ATOM   23007 C  CA    . ASN A 1 4572 ? 204.503 158.443 130.114 1.00 63.67  ? 4572 ASN A CA    1 
ATOM   23008 C  C     . ASN A 1 4572 ? 203.245 159.207 129.708 1.00 59.12  ? 4572 ASN A C     1 
ATOM   23009 O  O     . ASN A 1 4572 ? 202.885 159.275 128.530 1.00 54.57  ? 4572 ASN A O     1 
ATOM   23010 C  CB    . ASN A 1 4572 ? 205.052 157.629 128.941 1.00 67.04  ? 4572 ASN A CB    1 
ATOM   23011 C  CG    . ASN A 1 4572 ? 206.462 157.132 129.188 1.00 69.24  ? 4572 ASN A CG    1 
ATOM   23012 O  OD1   . ASN A 1 4572 ? 207.306 157.859 129.713 1.00 67.54  ? 4572 ASN A OD1   1 
ATOM   23013 N  ND2   . ASN A 1 4572 ? 206.724 155.886 128.812 1.00 65.78  ? 4572 ASN A ND2   1 
ATOM   23014 N  N     . ASN A 1 4573 ? 202.566 159.778 130.704 1.00 55.19  ? 4573 ASN A N     1 
ATOM   23015 C  CA    . ASN A 1 4573 ? 201.336 160.547 130.518 1.00 53.89  ? 4573 ASN A CA    1 
ATOM   23016 C  C     . ASN A 1 4573 ? 200.234 159.729 129.855 1.00 58.46  ? 4573 ASN A C     1 
ATOM   23017 O  O     . ASN A 1 4573 ? 199.347 160.288 129.203 1.00 56.46  ? 4573 ASN A O     1 
ATOM   23018 C  CB    . ASN A 1 4573 ? 201.593 161.829 129.718 1.00 48.73  ? 4573 ASN A CB    1 
ATOM   23019 C  CG    . ASN A 1 4573 ? 201.152 163.073 130.458 1.00 49.93  ? 4573 ASN A CG    1 
ATOM   23020 O  OD1   . ASN A 1 4573 ? 201.348 163.191 131.667 1.00 56.68  ? 4573 ASN A OD1   1 
ATOM   23021 N  ND2   . ASN A 1 4573 ? 200.550 164.011 129.735 1.00 50.24  ? 4573 ASN A ND2   1 
ATOM   23022 N  N     . LYS A 1 4574 ? 200.270 158.410 130.011 1.00 57.29  ? 4574 LYS A N     1 
ATOM   23023 C  CA    . LYS A 1 4574 ? 199.284 157.521 129.419 1.00 49.01  ? 4574 LYS A CA    1 
ATOM   23024 C  C     . LYS A 1 4574 ? 198.705 156.623 130.503 1.00 51.32  ? 4574 LYS A C     1 
ATOM   23025 O  O     . LYS A 1 4574 ? 199.438 156.118 131.359 1.00 54.31  ? 4574 LYS A O     1 
ATOM   23026 C  CB    . LYS A 1 4574 ? 199.905 156.683 128.301 1.00 49.20  ? 4574 LYS A CB    1 
ATOM   23027 C  CG    . LYS A 1 4574 ? 198.967 156.412 127.143 1.00 52.91  ? 4574 LYS A CG    1 
ATOM   23028 C  CD    . LYS A 1 4574 ? 199.702 156.456 125.814 1.00 52.20  ? 4574 LYS A CD    1 
ATOM   23029 C  CE    . LYS A 1 4574 ? 200.299 157.830 125.558 1.00 49.68  ? 4574 LYS A CE    1 
ATOM   23030 N  NZ    . LYS A 1 4574 ? 201.346 157.791 124.501 1.00 42.34  ? 4574 LYS A NZ    1 
ATOM   23031 N  N     . LEU A 1 4575 ? 197.390 156.431 130.465 1.00 49.82  ? 4575 LEU A N     1 
ATOM   23032 C  CA    . LEU A 1 4575 ? 196.691 155.703 131.514 1.00 41.45  ? 4575 LEU A CA    1 
ATOM   23033 C  C     . LEU A 1 4575 ? 196.489 154.244 131.133 1.00 48.07  ? 4575 LEU A C     1 
ATOM   23034 O  O     . LEU A 1 4575 ? 196.188 153.922 129.980 1.00 49.76  ? 4575 LEU A O     1 
ATOM   23035 C  CB    . LEU A 1 4575 ? 195.337 156.349 131.808 1.00 37.83  ? 4575 LEU A CB    1 
ATOM   23036 C  CG    . LEU A 1 4575 ? 195.366 157.672 132.571 1.00 39.49  ? 4575 LEU A CG    1 
ATOM   23037 C  CD1   . LEU A 1 4575 ? 194.009 157.940 133.188 1.00 35.51  ? 4575 LEU A CD1   1 
ATOM   23038 C  CD2   . LEU A 1 4575 ? 196.451 157.665 133.634 1.00 39.46  ? 4575 LEU A CD2   1 
ATOM   23039 N  N     . SER A 1 4576 ? 196.656 153.364 132.117 1.00 41.08  ? 4576 SER A N     1 
ATOM   23040 C  CA    . SER A 1 4576 ? 196.416 151.938 131.962 1.00 41.30  ? 4576 SER A CA    1 
ATOM   23041 C  C     . SER A 1 4576 ? 195.623 151.439 133.159 1.00 38.38  ? 4576 SER A C     1 
ATOM   23042 O  O     . SER A 1 4576 ? 195.852 151.880 134.289 1.00 41.41  ? 4576 SER A O     1 
ATOM   23043 C  CB    . SER A 1 4576 ? 197.730 151.158 131.835 1.00 47.49  ? 4576 SER A CB    1 
ATOM   23044 O  OG    . SER A 1 4576 ? 198.556 151.713 130.826 1.00 51.01  ? 4576 SER A OG    1 
ATOM   23045 N  N     . LEU A 1 4577 ? 194.687 150.527 132.907 1.00 36.18  ? 4577 LEU A N     1 
ATOM   23046 C  CA    . LEU A 1 4577 ? 193.863 149.992 133.982 1.00 33.81  ? 4577 LEU A CA    1 
ATOM   23047 C  C     . LEU A 1 4577 ? 194.726 149.230 134.980 1.00 34.35  ? 4577 LEU A C     1 
ATOM   23048 O  O     . LEU A 1 4577 ? 195.665 148.523 134.604 1.00 40.70  ? 4577 LEU A O     1 
ATOM   23049 C  CB    . LEU A 1 4577 ? 192.776 149.081 133.413 1.00 31.46  ? 4577 LEU A CB    1 
ATOM   23050 C  CG    . LEU A 1 4577 ? 191.527 149.795 132.893 1.00 28.79  ? 4577 LEU A CG    1 
ATOM   23051 C  CD1   . LEU A 1 4577 ? 190.517 148.796 132.350 1.00 27.34  ? 4577 LEU A CD1   1 
ATOM   23052 C  CD2   . LEU A 1 4577 ? 190.907 150.665 133.975 1.00 24.73  ? 4577 LEU A CD2   1 
ATOM   23053 N  N     . SER A 1 4578 ? 194.404 149.378 136.263 1.00 29.52  ? 4578 SER A N     1 
ATOM   23054 C  CA    . SER A 1 4578 ? 195.214 148.822 137.334 1.00 34.16  ? 4578 SER A CA    1 
ATOM   23055 C  C     . SER A 1 4578 ? 194.344 148.073 138.330 1.00 36.71  ? 4578 SER A C     1 
ATOM   23056 O  O     . SER A 1 4578 ? 193.151 148.354 138.477 1.00 42.35  ? 4578 SER A O     1 
ATOM   23057 C  CB    . SER A 1 4578 ? 195.994 149.916 138.070 1.00 35.28  ? 4578 SER A CB    1 
ATOM   23058 O  OG    . SER A 1 4578 ? 196.486 149.445 139.313 1.00 33.59  ? 4578 SER A OG    1 
ATOM   23059 N  N     . ASN A 1 4579 ? 194.961 147.115 139.015 1.00 34.92  ? 4579 ASN A N     1 
ATOM   23060 C  CA    . ASN A 1 4579 ? 194.329 146.404 140.116 1.00 34.02  ? 4579 ASN A CA    1 
ATOM   23061 C  C     . ASN A 1 4579 ? 194.689 146.994 141.472 1.00 35.52  ? 4579 ASN A C     1 
ATOM   23062 O  O     . ASN A 1 4579 ? 194.276 146.447 142.500 1.00 40.87  ? 4579 ASN A O     1 
ATOM   23063 C  CB    . ASN A 1 4579 ? 194.710 144.922 140.075 1.00 35.78  ? 4579 ASN A CB    1 
ATOM   23064 C  CG    . ASN A 1 4579 ? 194.145 144.209 138.862 1.00 42.70  ? 4579 ASN A CG    1 
ATOM   23065 O  OD1   . ASN A 1 4579 ? 194.878 143.576 138.102 1.00 42.75  ? 4579 ASN A OD1   1 
ATOM   23066 N  ND2   . ASN A 1 4579 ? 192.835 144.312 138.672 1.00 36.25  ? 4579 ASN A ND2   1 
ATOM   23067 N  N     . ALA A 1 4580 ? 195.450 148.083 141.500 1.00 33.38  ? 4580 ALA A N     1 
ATOM   23068 C  CA    . ALA A 1 4580 ? 195.793 148.764 142.738 1.00 32.73  ? 4580 ALA A CA    1 
ATOM   23069 C  C     . ALA A 1 4580 ? 194.739 149.810 143.073 1.00 37.10  ? 4580 ALA A C     1 
ATOM   23070 O  O     . ALA A 1 4580 ? 194.187 150.471 142.189 1.00 40.51  ? 4580 ALA A O     1 
ATOM   23071 C  CB    . ALA A 1 4580 ? 197.170 149.422 142.634 1.00 31.88  ? 4580 ALA A CB    1 
ATOM   23072 N  N     . ILE A 1 4581 ? 194.459 149.950 144.370 1.00 38.00  ? 4581 ILE A N     1 
ATOM   23073 C  CA    . ILE A 1 4581 ? 193.423 150.879 144.813 1.00 37.80  ? 4581 ILE A CA    1 
ATOM   23074 C  C     . ILE A 1 4581 ? 193.805 152.314 144.473 1.00 37.84  ? 4581 ILE A C     1 
ATOM   23075 O  O     . ILE A 1 4581 ? 192.985 153.086 143.961 1.00 38.44  ? 4581 ILE A O     1 
ATOM   23076 C  CB    . ILE A 1 4581 ? 193.161 150.707 146.320 1.00 34.82  ? 4581 ILE A CB    1 
ATOM   23077 C  CG1   . ILE A 1 4581 ? 192.681 149.285 146.618 1.00 34.90  ? 4581 ILE A CG1   1 
ATOM   23078 C  CG2   . ILE A 1 4581 ? 192.146 151.729 146.806 1.00 35.65  ? 4581 ILE A CG2   1 
ATOM   23079 C  CD1   . ILE A 1 4581 ? 191.452 148.881 145.838 1.00 31.31  ? 4581 ILE A CD1   1 
ATOM   23080 N  N     . SER A 1 4582 ? 195.051 152.694 144.746 1.00 39.84  ? 4582 SER A N     1 
ATOM   23081 C  CA    . SER A 1 4582 ? 195.496 154.061 144.527 1.00 36.34  ? 4582 SER A CA    1 
ATOM   23082 C  C     . SER A 1 4582 ? 196.902 154.063 143.945 1.00 39.79  ? 4582 SER A C     1 
ATOM   23083 O  O     . SER A 1 4582 ? 197.683 153.129 144.144 1.00 38.11  ? 4582 SER A O     1 
ATOM   23084 C  CB    . SER A 1 4582 ? 195.463 154.880 145.825 1.00 38.63  ? 4582 SER A CB    1 
ATOM   23085 O  OG    . SER A 1 4582 ? 195.497 156.270 145.551 1.00 45.51  ? 4582 SER A OG    1 
ATOM   23086 N  N     . THR A 1 4583 ? 197.211 155.133 143.217 1.00 42.22  ? 4583 THR A N     1 
ATOM   23087 C  CA    . THR A 1 4583 ? 198.544 155.362 142.672 1.00 39.75  ? 4583 THR A CA    1 
ATOM   23088 C  C     . THR A 1 4583 ? 198.870 156.836 142.846 1.00 37.83  ? 4583 THR A C     1 
ATOM   23089 O  O     . THR A 1 4583 ? 198.110 157.697 142.392 1.00 43.98  ? 4583 THR A O     1 
ATOM   23090 C  CB    . THR A 1 4583 ? 198.625 154.957 141.195 1.00 39.92  ? 4583 THR A CB    1 
ATOM   23091 O  OG1   . THR A 1 4583 ? 198.815 153.540 141.096 1.00 41.89  ? 4583 THR A OG1   1 
ATOM   23092 C  CG2   . THR A 1 4583 ? 199.784 155.661 140.506 1.00 44.09  ? 4583 THR A CG2   1 
ATOM   23093 N  N     . ALA A 1 4584 ? 199.988 157.126 143.505 1.00 41.81  ? 4584 ALA A N     1 
ATOM   23094 C  CA    . ALA A 1 4584 ? 200.359 158.502 143.807 1.00 41.04  ? 4584 ALA A CA    1 
ATOM   23095 C  C     . ALA A 1 4584 ? 201.029 159.137 142.594 1.00 41.98  ? 4584 ALA A C     1 
ATOM   23096 O  O     . ALA A 1 4584 ? 202.042 158.630 142.101 1.00 43.38  ? 4584 ALA A O     1 
ATOM   23097 C  CB    . ALA A 1 4584 ? 201.284 158.551 145.021 1.00 44.35  ? 4584 ALA A CB    1 
ATOM   23098 N  N     . LEU A 1 4585 ? 200.465 160.240 142.118 1.00 39.60  ? 4585 LEU A N     1 
ATOM   23099 C  CA    . LEU A 1 4585 ? 201.071 160.987 141.025 1.00 42.07  ? 4585 LEU A CA    1 
ATOM   23100 C  C     . LEU A 1 4585 ? 202.217 161.834 141.565 1.00 53.56  ? 4585 LEU A C     1 
ATOM   23101 O  O     . LEU A 1 4585 ? 201.999 162.636 142.480 1.00 57.15  ? 4585 LEU A O     1 
ATOM   23102 C  CB    . LEU A 1 4585 ? 200.036 161.870 140.341 1.00 41.91  ? 4585 LEU A CB    1 
ATOM   23103 C  CG    . LEU A 1 4585 ? 198.851 161.147 139.696 1.00 39.20  ? 4585 LEU A CG    1 
ATOM   23104 C  CD1   . LEU A 1 4585 ? 197.946 162.131 138.973 1.00 33.30  ? 4585 LEU A CD1   1 
ATOM   23105 C  CD2   . LEU A 1 4585 ? 199.336 160.062 138.747 1.00 40.45  ? 4585 LEU A CD2   1 
ATOM   23106 N  N     . PRO A 1 4586 ? 203.441 161.684 141.047 1.00 54.00  ? 4586 PRO A N     1 
ATOM   23107 C  CA    . PRO A 1 4586 ? 204.580 162.438 141.594 1.00 53.30  ? 4586 PRO A CA    1 
ATOM   23108 C  C     . PRO A 1 4586 ? 204.392 163.946 141.514 1.00 54.06  ? 4586 PRO A C     1 
ATOM   23109 O  O     . PRO A 1 4586 ? 204.443 164.639 142.535 1.00 50.59  ? 4586 PRO A O     1 
ATOM   23110 C  CB    . PRO A 1 4586 ? 205.759 161.974 140.726 1.00 63.97  ? 4586 PRO A CB    1 
ATOM   23111 C  CG    . PRO A 1 4586 ? 205.312 160.677 140.126 1.00 58.00  ? 4586 PRO A CG    1 
ATOM   23112 C  CD    . PRO A 1 4586 ? 203.838 160.813 139.929 1.00 52.55  ? 4586 PRO A CD    1 
ATOM   23113 N  N     . LEU A 1 4587 ? 204.170 164.461 140.308 1.00 54.09  ? 4587 LEU A N     1 
ATOM   23114 C  CA    . LEU A 1 4587 ? 203.938 165.885 140.110 1.00 52.15  ? 4587 LEU A CA    1 
ATOM   23115 C  C     . LEU A 1 4587 ? 203.053 166.072 138.890 1.00 52.93  ? 4587 LEU A C     1 
ATOM   23116 O  O     . LEU A 1 4587 ? 203.413 165.645 137.789 1.00 57.70  ? 4587 LEU A O     1 
ATOM   23117 C  CB    . LEU A 1 4587 ? 205.257 166.648 139.937 1.00 58.08  ? 4587 LEU A CB    1 
ATOM   23118 C  CG    . LEU A 1 4587 ? 205.137 168.164 139.753 1.00 54.95  ? 4587 LEU A CG    1 
ATOM   23119 C  CD1   . LEU A 1 4587 ? 204.232 168.768 140.811 1.00 46.09  ? 4587 LEU A CD1   1 
ATOM   23120 C  CD2   . LEU A 1 4587 ? 206.507 168.821 139.787 1.00 66.61  ? 4587 LEU A CD2   1 
ATOM   23121 N  N     . THR A 1 4588 ? 201.903 166.708 139.089 1.00 45.72  ? 4588 THR A N     1 
ATOM   23122 C  CA    . THR A 1 4588 ? 200.946 166.953 138.020 1.00 42.85  ? 4588 THR A CA    1 
ATOM   23123 C  C     . THR A 1 4588 ? 201.070 168.402 137.569 1.00 44.53  ? 4588 THR A C     1 
ATOM   23124 O  O     . THR A 1 4588 ? 200.962 169.322 138.387 1.00 41.89  ? 4588 THR A O     1 
ATOM   23125 C  CB    . THR A 1 4588 ? 199.519 166.655 138.482 1.00 45.65  ? 4588 THR A CB    1 
ATOM   23126 O  OG1   . THR A 1 4588 ? 199.523 165.510 139.342 1.00 48.87  ? 4588 THR A OG1   1 
ATOM   23127 C  CG2   . THR A 1 4588 ? 198.621 166.378 137.287 1.00 42.58  ? 4588 THR A CG2   1 
ATOM   23128 N  N     . GLN A 1 4589 ? 201.298 168.600 136.274 1.00 47.89  ? 4589 GLN A N     1 
ATOM   23129 C  CA    . GLN A 1 4589 ? 201.436 169.927 135.693 1.00 45.88  ? 4589 GLN A CA    1 
ATOM   23130 C  C     . GLN A 1 4589 ? 200.148 170.286 134.964 1.00 46.88  ? 4589 GLN A C     1 
ATOM   23131 O  O     . GLN A 1 4589 ? 199.692 169.535 134.095 1.00 50.96  ? 4589 GLN A O     1 
ATOM   23132 C  CB    . GLN A 1 4589 ? 202.628 169.984 134.738 1.00 50.94  ? 4589 GLN A CB    1 
ATOM   23133 C  CG    . GLN A 1 4589 ? 203.917 170.459 135.384 1.00 58.46  ? 4589 GLN A CG    1 
ATOM   23134 C  CD    . GLN A 1 4589 ? 205.137 169.746 134.840 1.00 67.75  ? 4589 GLN A CD    1 
ATOM   23135 O  OE1   . GLN A 1 4589 ? 205.485 168.656 135.291 1.00 70.11  ? 4589 GLN A OE1   1 
ATOM   23136 N  NE2   . GLN A 1 4589 ? 205.794 170.360 133.863 1.00 73.22  ? 4589 GLN A NE2   1 
ATOM   23137 N  N     . LEU A 1 4590 ? 199.566 171.427 135.319 1.00 44.74  ? 4590 LEU A N     1 
ATOM   23138 C  CA    . LEU A 1 4590 ? 198.344 171.913 134.694 1.00 46.54  ? 4590 LEU A CA    1 
ATOM   23139 C  C     . LEU A 1 4590 ? 198.694 173.055 133.749 1.00 50.69  ? 4590 LEU A C     1 
ATOM   23140 O  O     . LEU A 1 4590 ? 199.236 174.079 134.180 1.00 56.53  ? 4590 LEU A O     1 
ATOM   23141 C  CB    . LEU A 1 4590 ? 197.337 172.377 135.746 1.00 42.78  ? 4590 LEU A CB    1 
ATOM   23142 C  CG    . LEU A 1 4590 ? 197.215 171.538 137.018 1.00 41.18  ? 4590 LEU A CG    1 
ATOM   23143 C  CD1   . LEU A 1 4590 ? 196.301 172.230 138.013 1.00 42.83  ? 4590 LEU A CD1   1 
ATOM   23144 C  CD2   . LEU A 1 4590 ? 196.709 170.140 136.704 1.00 40.49  ? 4590 LEU A CD2   1 
ATOM   23145 N  N     . ARG A 1 4591 ? 198.386 172.878 132.468 1.00 51.61  ? 4591 ARG A N     1 
ATOM   23146 C  CA    . ARG A 1 4591 ? 198.644 173.884 131.449 1.00 49.64  ? 4591 ARG A CA    1 
ATOM   23147 C  C     . ARG A 1 4591 ? 197.327 174.391 130.884 1.00 54.26  ? 4591 ARG A C     1 
ATOM   23148 O  O     . ARG A 1 4591 ? 196.437 173.602 130.550 1.00 60.06  ? 4591 ARG A O     1 
ATOM   23149 C  CB    . ARG A 1 4591 ? 199.512 173.328 130.316 1.00 50.80  ? 4591 ARG A CB    1 
ATOM   23150 C  CG    . ARG A 1 4591 ? 200.917 172.946 130.734 1.00 57.88  ? 4591 ARG A CG    1 
ATOM   23151 C  CD    . ARG A 1 4591 ? 201.718 172.439 129.547 1.00 65.72  ? 4591 ARG A CD    1 
ATOM   23152 N  NE    . ARG A 1 4591 ? 201.287 173.063 128.302 1.00 66.60  ? 4591 ARG A NE    1 
ATOM   23153 C  CZ    . ARG A 1 4591 ? 202.104 173.432 127.325 1.00 69.42  ? 4591 ARG A CZ    1 
ATOM   23154 N  NH1   . ARG A 1 4591 ? 203.412 173.252 127.412 1.00 67.05  ? 4591 ARG A NH1   1 
ATOM   23155 N  NH2   . ARG A 1 4591 ? 201.596 173.996 126.233 1.00 68.46  ? 4591 ARG A NH2   1 
ATOM   23156 N  N     . TRP A 1 4592 ? 197.208 175.711 130.778 1.00 51.67  ? 4592 TRP A N     1 
ATOM   23157 C  CA    . TRP A 1 4592 ? 196.037 176.357 130.199 1.00 53.42  ? 4592 TRP A CA    1 
ATOM   23158 C  C     . TRP A 1 4592 ? 196.427 176.872 128.820 1.00 62.68  ? 4592 TRP A C     1 
ATOM   23159 O  O     . TRP A 1 4592 ? 197.274 177.764 128.700 1.00 69.82  ? 4592 TRP A O     1 
ATOM   23160 C  CB    . TRP A 1 4592 ? 195.535 177.486 131.095 1.00 52.67  ? 4592 TRP A CB    1 
ATOM   23161 C  CG    . TRP A 1 4592 ? 194.942 177.004 132.382 1.00 51.12  ? 4592 TRP A CG    1 
ATOM   23162 C  CD1   . TRP A 1 4592 ? 195.532 177.022 133.612 1.00 51.45  ? 4592 TRP A CD1   1 
ATOM   23163 C  CD2   . TRP A 1 4592 ? 193.648 176.420 132.566 1.00 50.89  ? 4592 TRP A CD2   1 
ATOM   23164 N  NE1   . TRP A 1 4592 ? 194.682 176.492 134.552 1.00 47.52  ? 4592 TRP A NE1   1 
ATOM   23165 C  CE2   . TRP A 1 4592 ? 193.519 176.114 133.935 1.00 47.88  ? 4592 TRP A CE2   1 
ATOM   23166 C  CE3   . TRP A 1 4592 ? 192.584 176.128 131.706 1.00 53.34  ? 4592 TRP A CE3   1 
ATOM   23167 C  CZ2   . TRP A 1 4592 ? 192.370 175.531 134.465 1.00 46.84  ? 4592 TRP A CZ2   1 
ATOM   23168 C  CZ3   . TRP A 1 4592 ? 191.444 175.550 132.234 1.00 50.91  ? 4592 TRP A CZ3   1 
ATOM   23169 C  CH2   . TRP A 1 4592 ? 191.346 175.257 133.600 1.00 46.08  ? 4592 TRP A CH2   1 
ATOM   23170 N  N     . VAL A 1 4593 ? 195.812 176.309 127.780 1.00 60.47  ? 4593 VAL A N     1 
ATOM   23171 C  CA    . VAL A 1 4593 ? 196.129 176.652 126.403 1.00 66.59  ? 4593 VAL A CA    1 
ATOM   23172 C  C     . VAL A 1 4593 ? 194.843 177.027 125.679 1.00 76.32  ? 4593 VAL A C     1 
ATOM   23173 O  O     . VAL A 1 4593 ? 193.738 176.686 126.106 1.00 73.74  ? 4593 VAL A O     1 
ATOM   23174 C  CB    . VAL A 1 4593 ? 196.848 175.504 125.662 1.00 64.61  ? 4593 VAL A CB    1 
ATOM   23175 C  CG1   . VAL A 1 4593 ? 198.176 175.189 126.331 1.00 66.39  ? 4593 VAL A CG1   1 
ATOM   23176 C  CG2   . VAL A 1 4593 ? 195.967 174.269 125.616 1.00 62.99  ? 4593 VAL A CG2   1 
ATOM   23177 N  N     . LYS A 1 4594 ? 195.006 177.750 124.573 1.00 77.35  ? 4594 LYS A N     1 
ATOM   23178 C  CA    . LYS A 1 4594 ? 193.862 178.193 123.789 1.00 79.39  ? 4594 LYS A CA    1 
ATOM   23179 C  C     . LYS A 1 4594 ? 193.105 176.995 123.230 1.00 80.06  ? 4594 LYS A C     1 
ATOM   23180 O  O     . LYS A 1 4594 ? 193.708 176.038 122.735 1.00 80.47  ? 4594 LYS A O     1 
ATOM   23181 C  CB    . LYS A 1 4594 ? 194.323 179.107 122.654 1.00 82.56  ? 4594 LYS A CB    1 
ATOM   23182 C  CG    . LYS A 1 4594 ? 193.189 179.743 121.868 1.00 82.11  ? 4594 LYS A CG    1 
ATOM   23183 C  CD    . LYS A 1 4594 ? 192.519 180.847 122.670 1.00 86.14  ? 4594 LYS A CD    1 
ATOM   23184 C  CE    . LYS A 1 4594 ? 191.561 181.653 121.809 1.00 87.71  ? 4594 LYS A CE    1 
ATOM   23185 N  NZ    . LYS A 1 4594 ? 190.381 180.847 121.390 1.00 84.43  ? 4594 LYS A NZ    1 
ATOM   23186 N  N     . GLN A 1 4595 ? 191.779 177.049 123.318 1.00 80.22  ? 4595 GLN A N     1 
ATOM   23187 C  CA    . GLN A 1 4595 ? 190.951 175.947 122.850 1.00 79.42  ? 4595 GLN A CA    1 
ATOM   23188 C  C     . GLN A 1 4595 ? 191.002 175.841 121.332 1.00 87.01  ? 4595 GLN A C     1 
ATOM   23189 O  O     . GLN A 1 4595 ? 190.964 176.848 120.619 1.00 88.97  ? 4595 GLN A O     1 
ATOM   23190 C  CB    . GLN A 1 4595 ? 189.507 176.136 123.312 1.00 78.94  ? 4595 GLN A CB    1 
ATOM   23191 C  CG    . GLN A 1 4595 ? 189.278 175.807 124.776 1.00 80.32  ? 4595 GLN A CG    1 
ATOM   23192 C  CD    . GLN A 1 4595 ? 188.017 174.998 125.002 1.00 82.91  ? 4595 GLN A CD    1 
ATOM   23193 O  OE1   . GLN A 1 4595 ? 187.786 173.988 124.337 1.00 91.04  ? 4595 GLN A OE1   1 
ATOM   23194 N  NE2   . GLN A 1 4595 ? 187.193 175.438 125.946 1.00 76.95  ? 4595 GLN A NE2   1 
ATOM   23195 N  N     . THR A 1 4596 ? 191.089 174.607 120.838 1.00 89.31  ? 4596 THR A N     1 
ATOM   23196 C  CA    . THR A 1 4596 ? 191.083 174.336 119.408 1.00 90.45  ? 4596 THR A CA    1 
ATOM   23197 C  C     . THR A 1 4596 ? 189.836 173.589 118.954 1.00 92.82  ? 4596 THR A C     1 
ATOM   23198 O  O     . THR A 1 4596 ? 189.751 173.226 117.777 1.00 95.23  ? 4596 THR A O     1 
ATOM   23199 C  CB    . THR A 1 4596 ? 192.333 173.541 119.011 1.00 88.61  ? 4596 THR A CB    1 
ATOM   23200 O  OG1   . THR A 1 4596 ? 192.343 172.285 119.701 1.00 89.87  ? 4596 THR A OG1   1 
ATOM   23201 C  CG2   . THR A 1 4596 ? 193.592 174.319 119.364 1.00 78.01  ? 4596 THR A CG2   1 
ATOM   23202 N  N     . ASN A 1 4597 ? 188.884 173.354 119.859 1.00 93.16  ? 4597 ASN A N     1 
ATOM   23203 C  CA    . ASN A 1 4597 ? 187.604 172.681 119.591 1.00 97.46  ? 4597 ASN A CA    1 
ATOM   23204 C  C     . ASN A 1 4597 ? 187.753 171.517 118.611 1.00 102.81 ? 4597 ASN A C     1 
ATOM   23205 O  O     . ASN A 1 4597 ? 186.995 171.367 117.651 1.00 100.27 ? 4597 ASN A O     1 
ATOM   23206 C  CB    . ASN A 1 4597 ? 186.538 173.682 119.124 1.00 93.86  ? 4597 ASN A CB    1 
ATOM   23207 C  CG    . ASN A 1 4597 ? 186.957 174.492 117.904 1.00 95.08  ? 4597 ASN A CG    1 
ATOM   23208 O  OD1   . ASN A 1 4597 ? 187.371 173.946 116.883 1.00 97.83  ? 4597 ASN A OD1   1 
ATOM   23209 N  ND2   . ASN A 1 4597 ? 186.849 175.811 118.013 1.00 89.89  ? 4597 ASN A ND2   1 
ATOM   23210 N  N     . THR A 1 4598 ? 188.742 170.667 118.881 1.00 103.07 ? 4598 THR A N     1 
ATOM   23211 C  CA    . THR A 1 4598 ? 188.986 169.472 118.086 1.00 100.83 ? 4598 THR A CA    1 
ATOM   23212 C  C     . THR A 1 4598 ? 188.361 168.222 118.695 1.00 101.83 ? 4598 THR A C     1 
ATOM   23213 O  O     . THR A 1 4598 ? 188.628 167.116 118.212 1.00 99.39  ? 4598 THR A O     1 
ATOM   23214 C  CB    . THR A 1 4598 ? 190.491 169.255 117.898 1.00 101.76 ? 4598 THR A CB    1 
ATOM   23215 O  OG1   . THR A 1 4598 ? 191.137 169.224 119.177 1.00 99.65  ? 4598 THR A OG1   1 
ATOM   23216 C  CG2   . THR A 1 4598 ? 191.093 170.368 117.054 1.00 96.56  ? 4598 THR A CG2   1 
ATOM   23217 N  N     . GLU A 1 4599 ? 187.552 168.375 119.737 1.00 103.26 ? 4599 GLU A N     1 
ATOM   23218 C  CA    . GLU A 1 4599 ? 186.872 167.262 120.425 1.00 97.44  ? 4599 GLU A CA    1 
ATOM   23219 C  C     . GLU A 1 4599 ? 187.956 166.346 121.004 1.00 92.15  ? 4599 GLU A C     1 
ATOM   23220 O  O     . GLU A 1 4599 ? 188.995 166.838 121.470 1.00 91.30  ? 4599 GLU A O     1 
ATOM   23221 C  CB    . GLU A 1 4599 ? 185.890 166.590 119.483 1.00 96.62  ? 4599 GLU A CB    1 
ATOM   23222 C  CG    . GLU A 1 4599 ? 184.779 167.506 118.993 1.00 93.80  ? 4599 GLU A CG    1 
ATOM   23223 C  CD    . GLU A 1 4599 ? 183.846 166.820 118.014 1.00 101.30 ? 4599 GLU A CD    1 
ATOM   23224 O  OE1   . GLU A 1 4599 ? 183.260 165.779 118.378 1.00 107.59 ? 4599 GLU A OE1   1 
ATOM   23225 O  OE2   . GLU A 1 4599 ? 183.699 167.322 116.880 1.00 99.33  ? 4599 GLU A OE2   1 
ATOM   23226 N  N     . LYS A 1 4600 ? 187.755 165.032 120.996 1.00 93.06  ? 4600 LYS A N     1 
ATOM   23227 C  CA    . LYS A 1 4600 ? 188.709 164.086 121.553 1.00 89.57  ? 4600 LYS A CA    1 
ATOM   23228 C  C     . LYS A 1 4600 ? 189.361 163.274 120.441 1.00 86.36  ? 4600 LYS A C     1 
ATOM   23229 O  O     . LYS A 1 4600 ? 188.866 163.206 119.313 1.00 83.14  ? 4600 LYS A O     1 
ATOM   23230 C  CB    . LYS A 1 4600 ? 188.031 163.148 122.558 1.00 82.79  ? 4600 LYS A CB    1 
ATOM   23231 C  CG    . LYS A 1 4600 ? 187.186 163.860 123.604 1.00 81.33  ? 4600 LYS A CG    1 
ATOM   23232 C  CD    . LYS A 1 4600 ? 187.975 164.955 124.304 1.00 75.94  ? 4600 LYS A CD    1 
ATOM   23233 C  CE    . LYS A 1 4600 ? 187.056 165.890 125.073 1.00 67.08  ? 4600 LYS A CE    1 
ATOM   23234 N  NZ    . LYS A 1 4600 ? 187.812 166.987 125.738 1.00 52.90  ? 4600 LYS A NZ    1 
ATOM   23235 N  N     . LYS A 1 4601 ? 190.490 162.652 120.781 1.00 83.78  ? 4601 LYS A N     1 
ATOM   23236 C  CA    . LYS A 1 4601 ? 191.258 161.841 119.846 1.00 83.11  ? 4601 LYS A CA    1 
ATOM   23237 C  C     . LYS A 1 4601 ? 190.852 160.371 119.874 1.00 82.92  ? 4601 LYS A C     1 
ATOM   23238 O  O     . LYS A 1 4601 ? 191.660 159.509 119.504 1.00 81.22  ? 4601 LYS A O     1 
ATOM   23239 C  CB    . LYS A 1 4601 ? 192.754 161.982 120.138 1.00 78.45  ? 4601 LYS A CB    1 
ATOM   23240 C  CG    . LYS A 1 4601 ? 193.636 161.973 118.899 1.00 78.99  ? 4601 LYS A CG    1 
ATOM   23241 C  CD    . LYS A 1 4601 ? 195.077 161.634 119.249 1.00 82.73  ? 4601 LYS A CD    1 
ATOM   23242 C  CE    . LYS A 1 4601 ? 195.626 162.579 120.305 1.00 82.41  ? 4601 LYS A CE    1 
ATOM   23243 N  NZ    . LYS A 1 4601 ? 197.065 162.321 120.590 1.00 75.28  ? 4601 LYS A NZ    1 
ATOM   23244 N  N     . ALA A 1 4602 ? 189.631 160.070 120.327 1.00 82.29  ? 4602 ALA A N     1 
ATOM   23245 C  CA    . ALA A 1 4602 ? 189.091 158.714 120.384 1.00 79.27  ? 4602 ALA A CA    1 
ATOM   23246 C  C     . ALA A 1 4602 ? 189.892 157.818 121.323 1.00 78.87  ? 4602 ALA A C     1 
ATOM   23247 O  O     . ALA A 1 4602 ? 189.680 156.602 121.361 1.00 71.41  ? 4602 ALA A O     1 
ATOM   23248 C  CB    . ALA A 1 4602 ? 189.026 158.093 118.985 1.00 72.51  ? 4602 ALA A CB    1 
ATOM   23249 N  N     . SER A 1 4603 ? 190.814 158.410 122.085 1.00 72.54  ? 4603 SER A N     1 
ATOM   23250 C  CA    . SER A 1 4603 ? 191.591 157.678 123.076 1.00 62.94  ? 4603 SER A CA    1 
ATOM   23251 C  C     . SER A 1 4603 ? 191.766 158.498 124.347 1.00 59.03  ? 4603 SER A C     1 
ATOM   23252 O  O     . SER A 1 4603 ? 192.679 158.239 125.138 1.00 58.72  ? 4603 SER A O     1 
ATOM   23253 C  CB    . SER A 1 4603 ? 192.958 157.274 122.520 1.00 64.17  ? 4603 SER A CB    1 
ATOM   23254 O  OG    . SER A 1 4603 ? 193.752 158.415 122.244 1.00 68.06  ? 4603 SER A OG    1 
ATOM   23255 N  N     . VAL A 1 4604 ? 190.902 159.488 124.558 1.00 57.90  ? 4604 VAL A N     1 
ATOM   23256 C  CA    . VAL A 1 4604 ? 190.996 160.403 125.688 1.00 50.78  ? 4604 VAL A CA    1 
ATOM   23257 C  C     . VAL A 1 4604 ? 189.771 160.215 126.571 1.00 46.62  ? 4604 VAL A C     1 
ATOM   23258 O  O     . VAL A 1 4604 ? 188.634 160.274 126.088 1.00 45.48  ? 4604 VAL A O     1 
ATOM   23259 C  CB    . VAL A 1 4604 ? 191.116 161.864 125.220 1.00 52.32  ? 4604 VAL A CB    1 
ATOM   23260 C  CG1   . VAL A 1 4604 ? 190.854 162.817 126.375 1.00 49.45  ? 4604 VAL A CG1   1 
ATOM   23261 C  CG2   . VAL A 1 4604 ? 192.487 162.115 124.616 1.00 51.13  ? 4604 VAL A CG2   1 
ATOM   23262 N  N     . VAL A 1 4605 ? 190.004 159.988 127.861 1.00 39.15  ? 4605 VAL A N     1 
ATOM   23263 C  CA    . VAL A 1 4605 ? 188.944 159.897 128.857 1.00 33.45  ? 4605 VAL A CA    1 
ATOM   23264 C  C     . VAL A 1 4605 ? 188.990 161.146 129.725 1.00 31.62  ? 4605 VAL A C     1 
ATOM   23265 O  O     . VAL A 1 4605 ? 190.050 161.763 129.891 1.00 36.16  ? 4605 VAL A O     1 
ATOM   23266 C  CB    . VAL A 1 4605 ? 189.068 158.621 129.715 1.00 32.08  ? 4605 VAL A CB    1 
ATOM   23267 C  CG1   . VAL A 1 4605 ? 189.258 157.408 128.829 1.00 37.15  ? 4605 VAL A CG1   1 
ATOM   23268 C  CG2   . VAL A 1 4605 ? 190.223 158.741 130.697 1.00 32.96  ? 4605 VAL A CG2   1 
ATOM   23269 N  N     . THR A 1 4606 ? 187.834 161.530 130.258 1.00 27.57  ? 4606 THR A N     1 
ATOM   23270 C  CA    . THR A 1 4606 ? 187.726 162.691 131.139 1.00 24.22  ? 4606 THR A CA    1 
ATOM   23271 C  C     . THR A 1 4606 ? 187.529 162.180 132.560 1.00 31.12  ? 4606 THR A C     1 
ATOM   23272 O  O     . THR A 1 4606 ? 186.425 161.791 132.947 1.00 37.39  ? 4606 THR A O     1 
ATOM   23273 C  CB    . THR A 1 4606 ? 186.582 163.599 130.702 1.00 27.00  ? 4606 THR A CB    1 
ATOM   23274 O  OG1   . THR A 1 4606 ? 186.834 164.081 129.376 1.00 36.27  ? 4606 THR A OG1   1 
ATOM   23275 C  CG2   . THR A 1 4606 ? 186.455 164.784 131.644 1.00 25.83  ? 4606 THR A CG2   1 
ATOM   23276 N  N     . LEU A 1 4607 ? 188.606 162.177 133.340 1.00 28.76  ? 4607 LEU A N     1 
ATOM   23277 C  CA    . LEU A 1 4607 ? 188.557 161.641 134.695 1.00 22.08  ? 4607 LEU A CA    1 
ATOM   23278 C  C     . LEU A 1 4607 ? 188.123 162.719 135.677 1.00 22.88  ? 4607 LEU A C     1 
ATOM   23279 O  O     . LEU A 1 4607 ? 188.683 163.822 135.663 1.00 31.87  ? 4607 LEU A O     1 
ATOM   23280 C  CB    . LEU A 1 4607 ? 189.911 161.093 135.115 1.00 28.45  ? 4607 LEU A CB    1 
ATOM   23281 C  CG    . LEU A 1 4607 ? 190.388 159.795 134.468 1.00 28.84  ? 4607 LEU A CG    1 
ATOM   23282 C  CD1   . LEU A 1 4607 ? 191.440 159.155 135.350 1.00 25.62  ? 4607 LEU A CD1   1 
ATOM   23283 C  CD2   . LEU A 1 4607 ? 189.225 158.844 134.245 1.00 24.58  ? 4607 LEU A CD2   1 
ATOM   23284 N  N     . PRO A 1 4608 ? 187.138 162.445 136.527 1.00 21.02  ? 4608 PRO A N     1 
ATOM   23285 C  CA    . PRO A 1 4608 ? 186.791 163.402 137.579 1.00 19.40  ? 4608 PRO A CA    1 
ATOM   23286 C  C     . PRO A 1 4608 ? 187.887 163.496 138.626 1.00 24.88  ? 4608 PRO A C     1 
ATOM   23287 O  O     . PRO A 1 4608 ? 188.573 162.519 138.936 1.00 27.08  ? 4608 PRO A O     1 
ATOM   23288 C  CB    . PRO A 1 4608 ? 185.505 162.820 138.174 1.00 17.29  ? 4608 PRO A CB    1 
ATOM   23289 C  CG    . PRO A 1 4608 ? 185.599 161.362 137.904 1.00 18.83  ? 4608 PRO A CG    1 
ATOM   23290 C  CD    . PRO A 1 4608 ? 186.315 161.225 136.590 1.00 24.24  ? 4608 PRO A CD    1 
ATOM   23291 N  N     . VAL A 1 4609 ? 188.048 164.697 139.173 1.00 29.96  ? 4609 VAL A N     1 
ATOM   23292 C  CA    . VAL A 1 4609 ? 188.971 164.945 140.274 1.00 27.14  ? 4609 VAL A CA    1 
ATOM   23293 C  C     . VAL A 1 4609 ? 188.139 165.384 141.470 1.00 25.97  ? 4609 VAL A C     1 
ATOM   23294 O  O     . VAL A 1 4609 ? 187.549 166.471 141.456 1.00 27.75  ? 4609 VAL A O     1 
ATOM   23295 C  CB    . VAL A 1 4609 ? 190.034 165.997 139.930 1.00 25.88  ? 4609 VAL A CB    1 
ATOM   23296 C  CG1   . VAL A 1 4609 ? 191.237 165.846 140.847 1.00 25.93  ? 4609 VAL A CG1   1 
ATOM   23297 C  CG2   . VAL A 1 4609 ? 190.462 165.863 138.479 1.00 24.90  ? 4609 VAL A CG2   1 
ATOM   23298 N  N     . TYR A 1 4610 ? 188.089 164.544 142.501 1.00 25.65  ? 4610 TYR A N     1 
ATOM   23299 C  CA    . TYR A 1 4610 ? 187.340 164.853 143.706 1.00 27.04  ? 4610 TYR A CA    1 
ATOM   23300 C  C     . TYR A 1 4610 ? 188.285 165.348 144.798 1.00 27.61  ? 4610 TYR A C     1 
ATOM   23301 O  O     . TYR A 1 4610 ? 189.511 165.300 144.667 1.00 30.60  ? 4610 TYR A O     1 
ATOM   23302 C  CB    . TYR A 1 4610 ? 186.551 163.632 144.176 1.00 23.83  ? 4610 TYR A CB    1 
ATOM   23303 C  CG    . TYR A 1 4610 ? 185.601 163.071 143.143 1.00 17.98  ? 4610 TYR A CG    1 
ATOM   23304 C  CD1   . TYR A 1 4610 ? 184.346 163.630 142.950 1.00 17.93  ? 4610 TYR A CD1   1 
ATOM   23305 C  CD2   . TYR A 1 4610 ? 185.956 161.976 142.370 1.00 21.02  ? 4610 TYR A CD2   1 
ATOM   23306 C  CE1   . TYR A 1 4610 ? 183.474 163.116 142.009 1.00 19.93  ? 4610 TYR A CE1   1 
ATOM   23307 C  CE2   . TYR A 1 4610 ? 185.091 161.456 141.429 1.00 18.06  ? 4610 TYR A CE2   1 
ATOM   23308 C  CZ    . TYR A 1 4610 ? 183.852 162.029 141.252 1.00 19.46  ? 4610 TYR A CZ    1 
ATOM   23309 O  OH    . TYR A 1 4610 ? 182.988 161.513 140.314 1.00 18.95  ? 4610 TYR A OH    1 
ATOM   23310 N  N     . LEU A 1 4611 ? 187.706 165.828 145.897 1.00 28.47  ? 4611 LEU A N     1 
ATOM   23311 C  CA    . LEU A 1 4611 ? 188.517 166.354 146.988 1.00 30.92  ? 4611 LEU A CA    1 
ATOM   23312 C  C     . LEU A 1 4611 ? 189.067 165.235 147.864 1.00 36.27  ? 4611 LEU A C     1 
ATOM   23313 O  O     . LEU A 1 4611 ? 190.252 165.244 148.214 1.00 44.42  ? 4611 LEU A O     1 
ATOM   23314 C  CB    . LEU A 1 4611 ? 187.693 167.338 147.820 1.00 28.36  ? 4611 LEU A CB    1 
ATOM   23315 C  CG    . LEU A 1 4611 ? 188.252 167.820 149.161 1.00 37.29  ? 4611 LEU A CG    1 
ATOM   23316 C  CD1   . LEU A 1 4611 ? 189.681 168.328 149.024 1.00 43.79  ? 4611 LEU A CD1   1 
ATOM   23317 C  CD2   . LEU A 1 4611 ? 187.359 168.899 149.744 1.00 38.81  ? 4611 LEU A CD2   1 
ATOM   23318 N  N     . ASN A 1 4612 ? 188.232 164.262 148.221 1.00 37.32  ? 4612 ASN A N     1 
ATOM   23319 C  CA    . ASN A 1 4612 ? 188.654 163.149 149.060 1.00 34.81  ? 4612 ASN A CA    1 
ATOM   23320 C  C     . ASN A 1 4612 ? 187.943 161.887 148.582 1.00 33.16  ? 4612 ASN A C     1 
ATOM   23321 O  O     . ASN A 1 4612 ? 187.256 161.887 147.556 1.00 31.56  ? 4612 ASN A O     1 
ATOM   23322 C  CB    . ASN A 1 4612 ? 188.389 163.455 150.540 1.00 33.94  ? 4612 ASN A CB    1 
ATOM   23323 C  CG    . ASN A 1 4612 ? 186.969 163.910 150.795 1.00 33.40  ? 4612 ASN A CG    1 
ATOM   23324 O  OD1   . ASN A 1 4612 ? 186.049 163.098 150.865 1.00 36.88  ? 4612 ASN A OD1   1 
ATOM   23325 N  ND2   . ASN A 1 4612 ? 186.784 165.217 150.938 1.00 32.65  ? 4612 ASN A ND2   1 
ATOM   23326 N  N     . PHE A 1 4613 ? 188.107 160.800 149.341 1.00 30.13  ? 4613 PHE A N     1 
ATOM   23327 C  CA    . PHE A 1 4613 ? 187.622 159.493 148.909 1.00 27.24  ? 4613 PHE A CA    1 
ATOM   23328 C  C     . PHE A 1 4613 ? 186.103 159.410 148.852 1.00 28.13  ? 4613 PHE A C     1 
ATOM   23329 O  O     . PHE A 1 4613 ? 185.572 158.518 148.183 1.00 30.55  ? 4613 PHE A O     1 
ATOM   23330 C  CB    . PHE A 1 4613 ? 188.158 158.389 149.827 1.00 28.83  ? 4613 PHE A CB    1 
ATOM   23331 C  CG    . PHE A 1 4613 ? 187.663 158.473 151.248 1.00 36.67  ? 4613 PHE A CG    1 
ATOM   23332 C  CD1   . PHE A 1 4613 ? 188.033 159.522 152.074 1.00 35.03  ? 4613 PHE A CD1   1 
ATOM   23333 C  CD2   . PHE A 1 4613 ? 186.823 157.495 151.754 1.00 39.07  ? 4613 PHE A CD2   1 
ATOM   23334 C  CE1   . PHE A 1 4613 ? 187.576 159.593 153.376 1.00 38.16  ? 4613 PHE A CE1   1 
ATOM   23335 C  CE2   . PHE A 1 4613 ? 186.364 157.560 153.055 1.00 39.01  ? 4613 PHE A CE2   1 
ATOM   23336 C  CZ    . PHE A 1 4613 ? 186.741 158.611 153.867 1.00 44.50  ? 4613 PHE A CZ    1 
ATOM   23337 N  N     . THR A 1 4614 ? 185.390 160.310 149.533 1.00 29.10  ? 4614 THR A N     1 
ATOM   23338 C  CA    . THR A 1 4614 ? 183.933 160.266 149.506 1.00 27.82  ? 4614 THR A CA    1 
ATOM   23339 C  C     . THR A 1 4614 ? 183.366 160.599 148.132 1.00 27.73  ? 4614 THR A C     1 
ATOM   23340 O  O     . THR A 1 4614 ? 182.202 160.279 147.866 1.00 32.26  ? 4614 THR A O     1 
ATOM   23341 C  CB    . THR A 1 4614 ? 183.351 161.223 150.548 1.00 29.36  ? 4614 THR A CB    1 
ATOM   23342 O  OG1   . THR A 1 4614 ? 183.674 162.574 150.196 1.00 30.24  ? 4614 THR A OG1   1 
ATOM   23343 C  CG2   . THR A 1 4614 ? 183.911 160.912 151.929 1.00 29.80  ? 4614 THR A CG2   1 
ATOM   23344 N  N     . ARG A 1 4615 ? 184.158 161.232 147.262 1.00 26.74  ? 4615 ARG A N     1 
ATOM   23345 C  CA    . ARG A 1 4615 ? 183.732 161.594 145.909 1.00 20.52  ? 4615 ARG A CA    1 
ATOM   23346 C  C     . ARG A 1 4615 ? 182.486 162.477 145.937 1.00 25.48  ? 4615 ARG A C     1 
ATOM   23347 O  O     . ARG A 1 4615 ? 181.654 162.438 145.029 1.00 31.23  ? 4615 ARG A O     1 
ATOM   23348 C  CB    . ARG A 1 4615 ? 183.497 160.350 145.050 1.00 17.35  ? 4615 ARG A CB    1 
ATOM   23349 C  CG    . ARG A 1 4615 ? 184.707 159.444 144.921 1.00 17.30  ? 4615 ARG A CG    1 
ATOM   23350 C  CD    . ARG A 1 4615 ? 184.618 158.591 143.672 1.00 14.88  ? 4615 ARG A CD    1 
ATOM   23351 N  NE    . ARG A 1 4615 ? 185.689 157.605 143.601 1.00 20.54  ? 4615 ARG A NE    1 
ATOM   23352 C  CZ    . ARG A 1 4615 ? 185.970 156.882 142.526 1.00 20.12  ? 4615 ARG A CZ    1 
ATOM   23353 N  NH1   . ARG A 1 4615 ? 185.278 157.011 141.407 1.00 19.61  ? 4615 ARG A NH1   1 
ATOM   23354 N  NH2   . ARG A 1 4615 ? 186.971 156.008 142.577 1.00 23.12  ? 4615 ARG A NH2   1 
ATOM   23355 N  N     . ALA A 1 4616 ? 182.359 163.283 146.990 1.00 25.39  ? 4616 ALA A N     1 
ATOM   23356 C  CA    . ALA A 1 4616 ? 181.189 164.133 147.169 1.00 26.28  ? 4616 ALA A CA    1 
ATOM   23357 C  C     . ALA A 1 4616 ? 181.350 165.492 146.500 1.00 30.85  ? 4616 ALA A C     1 
ATOM   23358 O  O     . ALA A 1 4616 ? 180.378 166.035 145.962 1.00 32.46  ? 4616 ALA A O     1 
ATOM   23359 C  CB    . ALA A 1 4616 ? 180.898 164.319 148.659 1.00 27.07  ? 4616 ALA A CB    1 
ATOM   23360 N  N     . ASP A 1 4617 ? 182.554 166.054 146.522 1.00 35.44  ? 4617 ASP A N     1 
ATOM   23361 C  CA    . ASP A 1 4617 ? 182.829 167.360 145.936 1.00 35.58  ? 4617 ASP A CA    1 
ATOM   23362 C  C     . ASP A 1 4617 ? 183.712 167.177 144.710 1.00 31.75  ? 4617 ASP A C     1 
ATOM   23363 O  O     . ASP A 1 4617 ? 184.781 166.564 144.797 1.00 32.21  ? 4617 ASP A O     1 
ATOM   23364 C  CB    . ASP A 1 4617 ? 183.499 168.286 146.951 1.00 37.35  ? 4617 ASP A CB    1 
ATOM   23365 C  CG    . ASP A 1 4617 ? 182.578 168.656 148.095 1.00 47.28  ? 4617 ASP A CG    1 
ATOM   23366 O  OD1   . ASP A 1 4617 ? 181.468 169.162 147.826 1.00 48.29  ? 4617 ASP A OD1   1 
ATOM   23367 O  OD2   . ASP A 1 4617 ? 182.960 168.437 149.262 1.00 46.73  ? 4617 ASP A OD2   1 
ATOM   23368 N  N     . LEU A 1 4618 ? 183.265 167.711 143.577 1.00 30.69  ? 4618 LEU A N     1 
ATOM   23369 C  CA    . LEU A 1 4618 ? 184.010 167.628 142.326 1.00 24.00  ? 4618 LEU A CA    1 
ATOM   23370 C  C     . LEU A 1 4618 ? 184.853 168.888 142.179 1.00 30.05  ? 4618 LEU A C     1 
ATOM   23371 O  O     . LEU A 1 4618 ? 184.317 169.999 142.113 1.00 34.40  ? 4618 LEU A O     1 
ATOM   23372 C  CB    . LEU A 1 4618 ? 183.061 167.457 141.144 1.00 19.70  ? 4618 LEU A CB    1 
ATOM   23373 C  CG    . LEU A 1 4618 ? 183.732 167.276 139.784 1.00 23.99  ? 4618 LEU A CG    1 
ATOM   23374 C  CD1   . LEU A 1 4618 ? 184.327 165.885 139.676 1.00 22.80  ? 4618 LEU A CD1   1 
ATOM   23375 C  CD2   . LEU A 1 4618 ? 182.742 167.533 138.662 1.00 23.58  ? 4618 LEU A CD2   1 
ATOM   23376 N  N     . ILE A 1 4619 ? 186.174 168.717 142.127 1.00 32.25  ? 4619 ILE A N     1 
ATOM   23377 C  CA    . ILE A 1 4619 ? 187.069 169.867 142.048 1.00 32.49  ? 4619 ILE A CA    1 
ATOM   23378 C  C     . ILE A 1 4619 ? 187.162 170.364 140.609 1.00 31.93  ? 4619 ILE A C     1 
ATOM   23379 O  O     . ILE A 1 4619 ? 186.826 171.515 140.307 1.00 35.96  ? 4619 ILE A O     1 
ATOM   23380 C  CB    . ILE A 1 4619 ? 188.455 169.511 142.614 1.00 33.74  ? 4619 ILE A CB    1 
ATOM   23381 C  CG1   . ILE A 1 4619 ? 188.323 168.920 144.020 1.00 31.95  ? 4619 ILE A CG1   1 
ATOM   23382 C  CG2   . ILE A 1 4619 ? 189.338 170.745 142.668 1.00 39.61  ? 4619 ILE A CG2   1 
ATOM   23383 C  CD1   . ILE A 1 4619 ? 187.486 169.751 144.964 1.00 33.91  ? 4619 ILE A CD1   1 
ATOM   23384 N  N     . PHE A 1 4620 ? 187.613 169.501 139.704 1.00 28.63  ? 4620 PHE A N     1 
ATOM   23385 C  CA    . PHE A 1 4620 ? 187.690 169.813 138.280 1.00 27.88  ? 4620 PHE A CA    1 
ATOM   23386 C  C     . PHE A 1 4620 ? 187.807 168.497 137.516 1.00 30.88  ? 4620 PHE A C     1 
ATOM   23387 O  O     . PHE A 1 4620 ? 187.699 167.413 138.098 1.00 32.48  ? 4620 PHE A O     1 
ATOM   23388 C  CB    . PHE A 1 4620 ? 188.845 170.780 137.984 1.00 28.52  ? 4620 PHE A CB    1 
ATOM   23389 C  CG    . PHE A 1 4620 ? 190.211 170.221 138.274 1.00 30.22  ? 4620 PHE A CG    1 
ATOM   23390 C  CD1   . PHE A 1 4620 ? 190.644 170.045 139.577 1.00 30.17  ? 4620 PHE A CD1   1 
ATOM   23391 C  CD2   . PHE A 1 4620 ? 191.075 169.902 137.242 1.00 29.89  ? 4620 PHE A CD2   1 
ATOM   23392 C  CE1   . PHE A 1 4620 ? 191.900 169.542 139.846 1.00 28.88  ? 4620 PHE A CE1   1 
ATOM   23393 C  CE2   . PHE A 1 4620 ? 192.334 169.403 137.506 1.00 29.61  ? 4620 PHE A CE2   1 
ATOM   23394 C  CZ    . PHE A 1 4620 ? 192.747 169.220 138.808 1.00 29.17  ? 4620 PHE A CZ    1 
ATOM   23395 N  N     . THR A 1 4621 ? 188.011 168.589 136.202 1.00 29.56  ? 4621 THR A N     1 
ATOM   23396 C  CA    . THR A 1 4621 ? 188.107 167.417 135.342 1.00 30.33  ? 4621 THR A CA    1 
ATOM   23397 C  C     . THR A 1 4621 ? 189.422 167.446 134.576 1.00 33.45  ? 4621 THR A C     1 
ATOM   23398 O  O     . THR A 1 4621 ? 189.976 168.514 134.299 1.00 34.71  ? 4621 THR A O     1 
ATOM   23399 C  CB    . THR A 1 4621 ? 186.935 167.332 134.348 1.00 29.38  ? 4621 THR A CB    1 
ATOM   23400 O  OG1   . THR A 1 4621 ? 187.260 168.053 133.154 1.00 36.40  ? 4621 THR A OG1   1 
ATOM   23401 C  CG2   . THR A 1 4621 ? 185.663 167.907 134.956 1.00 26.76  ? 4621 THR A CG2   1 
ATOM   23402 N  N     . VAL A 1 4622 ? 189.916 166.255 134.232 1.00 29.92  ? 4622 VAL A N     1 
ATOM   23403 C  CA    . VAL A 1 4622 ? 191.208 166.096 133.581 1.00 32.03  ? 4622 VAL A CA    1 
ATOM   23404 C  C     . VAL A 1 4622 ? 191.061 165.150 132.396 1.00 36.11  ? 4622 VAL A C     1 
ATOM   23405 O  O     . VAL A 1 4622 ? 190.404 164.110 132.478 1.00 37.81  ? 4622 VAL A O     1 
ATOM   23406 C  CB    . VAL A 1 4622 ? 192.284 165.571 134.558 1.00 31.90  ? 4622 VAL A CB    1 
ATOM   23407 C  CG1   . VAL A 1 4622 ? 193.502 165.083 133.803 1.00 33.61  ? 4622 VAL A CG1   1 
ATOM   23408 C  CG2   . VAL A 1 4622 ? 192.675 166.647 135.545 1.00 32.66  ? 4622 VAL A CG2   1 
ATOM   23409 N  N     . ASP A 1 4623 ? 191.687 165.527 131.284 1.00 37.06  ? 4623 ASP A N     1 
ATOM   23410 C  CA    . ASP A 1 4623 ? 191.735 164.706 130.080 1.00 35.35  ? 4623 ASP A CA    1 
ATOM   23411 C  C     . ASP A 1 4623 ? 193.043 163.924 130.068 1.00 35.38  ? 4623 ASP A C     1 
ATOM   23412 O  O     . ASP A 1 4623 ? 194.121 164.508 130.215 1.00 35.83  ? 4623 ASP A O     1 
ATOM   23413 C  CB    . ASP A 1 4623 ? 191.613 165.570 128.825 1.00 37.14  ? 4623 ASP A CB    1 
ATOM   23414 C  CG    . ASP A 1 4623 ? 190.242 166.200 128.682 1.00 42.14  ? 4623 ASP A CG    1 
ATOM   23415 O  OD1   . ASP A 1 4623 ? 189.564 166.394 129.712 1.00 35.30  ? 4623 ASP A OD1   1 
ATOM   23416 O  OD2   . ASP A 1 4623 ? 189.844 166.500 127.538 1.00 55.78  ? 4623 ASP A OD2   1 
ATOM   23417 N  N     . PHE A 1 4624 ? 192.943 162.607 129.892 1.00 42.08  ? 4624 PHE A N     1 
ATOM   23418 C  CA    . PHE A 1 4624 ? 194.097 161.720 129.827 1.00 41.30  ? 4624 PHE A CA    1 
ATOM   23419 C  C     . PHE A 1 4624 ? 193.987 160.843 128.591 1.00 43.56  ? 4624 PHE A C     1 
ATOM   23420 O  O     . PHE A 1 4624 ? 192.880 160.491 128.175 1.00 47.02  ? 4624 PHE A O     1 
ATOM   23421 C  CB    . PHE A 1 4624 ? 194.201 160.825 131.067 1.00 35.99  ? 4624 PHE A CB    1 
ATOM   23422 C  CG    . PHE A 1 4624 ? 195.064 161.382 132.160 1.00 38.22  ? 4624 PHE A CG    1 
ATOM   23423 C  CD1   . PHE A 1 4624 ? 196.434 161.480 131.993 1.00 44.40  ? 4624 PHE A CD1   1 
ATOM   23424 C  CD2   . PHE A 1 4624 ? 194.514 161.756 133.372 1.00 39.74  ? 4624 PHE A CD2   1 
ATOM   23425 C  CE1   . PHE A 1 4624 ? 197.236 161.976 133.002 1.00 46.96  ? 4624 PHE A CE1   1 
ATOM   23426 C  CE2   . PHE A 1 4624 ? 195.311 162.249 134.387 1.00 35.68  ? 4624 PHE A CE2   1 
ATOM   23427 C  CZ    . PHE A 1 4624 ? 196.672 162.361 134.201 1.00 40.69  ? 4624 PHE A CZ    1 
ATOM   23428 N  N     . GLU A 1 4625 ? 195.131 160.468 128.013 1.00 45.23  ? 4625 GLU A N     1 
ATOM   23429 C  CA    . GLU A 1 4625 ? 195.107 159.539 126.852 1.00 48.24  ? 4625 GLU A CA    1 
ATOM   23430 C  C     . GLU A 1 4625 ? 195.307 158.103 127.363 1.00 50.64  ? 4625 GLU A C     1 
ATOM   23431 O  O     . GLU A 1 4625 ? 196.317 157.856 128.055 1.00 50.87  ? 4625 GLU A O     1 
ATOM   23432 C  CB    . GLU A 1 4625 ? 196.174 159.892 125.816 1.00 50.74  ? 4625 GLU A CB    1 
ATOM   23433 C  CG    . GLU A 1 4625 ? 196.170 158.948 124.617 1.00 61.91  ? 4625 GLU A CG    1 
ATOM   23434 C  CD    . GLU A 1 4625 ? 197.167 159.306 123.531 1.00 71.91  ? 4625 GLU A CD    1 
ATOM   23435 O  OE1   . GLU A 1 4625 ? 198.046 158.469 123.235 1.00 66.06  ? 4625 GLU A OE1   1 
ATOM   23436 O  OE2   . GLU A 1 4625 ? 197.064 160.422 122.979 1.00 76.79  ? 4625 GLU A OE2   1 
ATOM   23437 N  N     . ILE A 1 4626 ? 194.374 157.203 127.038 1.00 54.42  ? 4626 ILE A N     1 
ATOM   23438 C  CA    . ILE A 1 4626 ? 194.472 155.783 127.492 1.00 53.36  ? 4626 ILE A CA    1 
ATOM   23439 C  C     . ILE A 1 4626 ? 195.611 155.097 126.722 1.00 53.71  ? 4626 ILE A C     1 
ATOM   23440 O  O     . ILE A 1 4626 ? 195.917 155.545 125.596 1.00 58.20  ? 4626 ILE A O     1 
ATOM   23441 C  CB    . ILE A 1 4626 ? 193.130 155.055 127.300 1.00 52.50  ? 4626 ILE A CB    1 
ATOM   23442 C  CG1   . ILE A 1 4626 ? 192.666 155.115 125.847 1.00 59.01  ? 4626 ILE A CG1   1 
ATOM   23443 C  CG2   . ILE A 1 4626 ? 192.071 155.606 128.254 1.00 42.68  ? 4626 ILE A CG2   1 
ATOM   23444 C  CD1   . ILE A 1 4626 ? 191.220 154.703 125.644 1.00 53.33  ? 4626 ILE A CD1   1 
ATOM   23445 N  N     . ALA A 1 4627 ? 196.208 154.056 127.309 1.00 57.52  ? 4627 ALA A N     1 
ATOM   23446 C  CA    . ALA A 1 4627 ? 197.347 153.361 126.663 1.00 65.63  ? 4627 ALA A CA    1 
ATOM   23447 C  C     . ALA A 1 4627 ? 196.852 152.143 125.883 1.00 73.01  ? 4627 ALA A C     1 
ATOM   23448 O  O     . ALA A 1 4627 ? 195.693 151.723 126.097 1.00 72.79  ? 4627 ALA A O     1 
ATOM   23449 C  CB    . ALA A 1 4627 ? 198.362 152.964 127.711 1.00 60.14  ? 4627 ALA A CB    1 
ATOM   23450 N  N     . THR A 1 4628 ? 197.694 151.605 124.994 1.00 80.59  ? 4628 THR A N     1 
ATOM   23451 C  CA    . THR A 1 4628 ? 197.338 150.387 124.229 1.00 82.24  ? 4628 THR A CA    1 
ATOM   23452 C  C     . THR A 1 4628 ? 195.980 150.559 123.583 1.00 77.15  ? 4628 THR A C     1 
ATOM   23453 O  O     . THR A 1 4628 ? 195.673 151.685 123.134 1.00 74.27  ? 4628 THR A O     1 
ATOM   23454 C  CB    . THR A 1 4628 ? 197.376 149.167 125.150 1.00 81.91  ? 4628 THR A CB    1 
ATOM   23455 O  OG1   . THR A 1 4628 ? 196.226 149.264 125.986 1.00 76.19  ? 4628 THR A OG1   1 
ATOM   23456 C  CG2   . THR A 1 4628 ? 198.634 149.120 125.999 1.00 75.56  ? 4628 THR A CG2   1 
ATOM   23457 N  N     . LYS A 1 4629 ? 195.189 149.483 123.536 1.00 76.30  ? 4629 LYS A N     1 
ATOM   23458 C  CA    . LYS A 1 4629 ? 193.847 149.533 122.899 1.00 79.09  ? 4629 LYS A CA    1 
ATOM   23459 C  C     . LYS A 1 4629 ? 192.768 149.472 123.992 1.00 76.63  ? 4629 LYS A C     1 
ATOM   23460 O  O     . LYS A 1 4629 ? 191.657 148.979 123.701 1.00 75.44  ? 4629 LYS A O     1 
ATOM   23461 C  CB    . LYS A 1 4629 ? 193.698 148.375 121.907 1.00 79.49  ? 4629 LYS A CB    1 
ATOM   23462 C  CG    . LYS A 1 4629 ? 193.938 146.994 122.500 1.00 78.48  ? 4629 LYS A CG    1 
ATOM   23463 C  CD    . LYS A 1 4629 ? 193.912 145.883 121.458 1.00 78.70  ? 4629 LYS A CD    1 
ATOM   23464 C  CE    . LYS A 1 4629 ? 194.943 146.086 120.393 1.00 79.21  ? 4629 LYS A CE    1 
ATOM   23465 N  NZ    . LYS A 1 4629 ? 194.911 145.013 119.397 1.00 75.36  ? 4629 LYS A NZ    1 
ATOM   23466 N  N     . GLU A 1 4630 ? 193.089 149.957 125.194 1.00 68.34  ? 4630 GLU A N     1 
ATOM   23467 C  CA    . GLU A 1 4630 ? 192.112 149.945 126.314 1.00 57.05  ? 4630 GLU A CA    1 
ATOM   23468 C  C     . GLU A 1 4630 ? 190.828 150.662 125.874 1.00 58.51  ? 4630 GLU A C     1 
ATOM   23469 O  O     . GLU A 1 4630 ? 190.932 151.679 125.156 1.00 65.09  ? 4630 GLU A O     1 
ATOM   23470 C  CB    . GLU A 1 4630 ? 192.687 150.631 127.552 1.00 57.50  ? 4630 GLU A CB    1 
ATOM   23471 C  CG    . GLU A 1 4630 ? 193.928 149.937 128.105 1.00 64.92  ? 4630 GLU A CG    1 
ATOM   23472 C  CD    . GLU A 1 4630 ? 194.416 150.565 129.396 1.00 53.33  ? 4630 GLU A CD    1 
ATOM   23473 O  OE1   . GLU A 1 4630 ? 194.492 149.847 130.414 1.00 44.78  ? 4630 GLU A OE1   1 
ATOM   23474 O  OE2   . GLU A 1 4630 ? 194.707 151.779 129.381 1.00 48.94  ? 4630 GLU A OE2   1 
ATOM   23475 N  N     . ASP A 1 4631 ? 189.668 150.145 126.288 1.00 58.05  ? 4631 ASP A N     1 
ATOM   23476 C  CA    . ASP A 1 4631 ? 188.369 150.781 125.940 1.00 53.49  ? 4631 ASP A CA    1 
ATOM   23477 C  C     . ASP A 1 4631 ? 188.070 151.890 126.951 1.00 48.57  ? 4631 ASP A C     1 
ATOM   23478 O  O     . ASP A 1 4631 ? 187.992 151.584 128.161 1.00 48.94  ? 4631 ASP A O     1 
ATOM   23479 C  CB    . ASP A 1 4631 ? 187.251 149.753 125.882 1.00 53.45  ? 4631 ASP A CB    1 
ATOM   23480 C  CG    . ASP A 1 4631 ? 185.866 150.298 125.569 1.00 61.78  ? 4631 ASP A CG    1 
ATOM   23481 O  OD1   . ASP A 1 4631 ? 185.745 151.524 125.361 1.00 57.88  ? 4631 ASP A OD1   1 
ATOM   23482 O  OD2   . ASP A 1 4631 ? 184.919 149.490 125.538 1.00 70.93  ? 4631 ASP A OD2   1 
ATOM   23483 N  N     . PRO A 1 4632 ? 187.893 153.157 126.520 1.00 47.72  ? 4632 PRO A N     1 
ATOM   23484 C  CA    . PRO A 1 4632 ? 187.529 154.245 127.444 1.00 41.78  ? 4632 PRO A CA    1 
ATOM   23485 C  C     . PRO A 1 4632 ? 186.287 153.941 128.261 1.00 34.33  ? 4632 PRO A C     1 
ATOM   23486 O  O     . PRO A 1 4632 ? 186.140 154.467 129.371 1.00 31.14  ? 4632 PRO A O     1 
ATOM   23487 C  CB    . PRO A 1 4632 ? 187.311 155.446 126.510 1.00 37.55  ? 4632 PRO A CB    1 
ATOM   23488 C  CG    . PRO A 1 4632 ? 187.195 154.868 125.131 1.00 40.18  ? 4632 PRO A CG    1 
ATOM   23489 C  CD    . PRO A 1 4632 ? 188.017 153.625 125.132 1.00 45.60  ? 4632 PRO A CD    1 
ATOM   23490 N  N     . ARG A 1 4633 ? 185.385 153.108 127.737 1.00 34.16  ? 4633 ARG A N     1 
ATOM   23491 C  CA    . ARG A 1 4633 ? 184.206 152.707 128.497 1.00 38.44  ? 4633 ARG A CA    1 
ATOM   23492 C  C     . ARG A 1 4633 ? 184.580 151.934 129.754 1.00 32.21  ? 4633 ARG A C     1 
ATOM   23493 O  O     . ARG A 1 4633 ? 183.924 152.083 130.792 1.00 28.37  ? 4633 ARG A O     1 
ATOM   23494 C  CB    . ARG A 1 4633 ? 183.283 151.868 127.614 1.00 47.19  ? 4633 ARG A CB    1 
ATOM   23495 C  CG    . ARG A 1 4633 ? 182.664 152.632 126.454 1.00 47.29  ? 4633 ARG A CG    1 
ATOM   23496 C  CD    . ARG A 1 4633 ? 181.546 151.891 125.686 1.00 55.12  ? 4633 ARG A CD    1 
ATOM   23497 N  NE    . ARG A 1 4633 ? 181.938 150.638 125.043 1.00 65.55  ? 4633 ARG A NE    1 
ATOM   23498 C  CZ    . ARG A 1 4633 ? 182.154 149.476 125.650 1.00 67.27  ? 4633 ARG A CZ    1 
ATOM   23499 N  NH1   . ARG A 1 4633 ? 181.884 149.299 126.932 1.00 54.59  ? 4633 ARG A NH1   1 
ATOM   23500 N  NH2   . ARG A 1 4633 ? 182.615 148.451 124.939 1.00 69.35  ? 4633 ARG A NH2   1 
ATOM   23501 N  N     . SER A 1 4634 ? 185.621 151.101 129.680 1.00 37.11  ? 4634 SER A N     1 
ATOM   23502 C  CA    . SER A 1 4634 ? 186.052 150.343 130.851 1.00 29.29  ? 4634 SER A CA    1 
ATOM   23503 C  C     . SER A 1 4634 ? 186.525 151.268 131.965 1.00 25.89  ? 4634 SER A C     1 
ATOM   23504 O  O     . SER A 1 4634 ? 186.337 150.971 133.151 1.00 29.41  ? 4634 SER A O     1 
ATOM   23505 C  CB    . SER A 1 4634 ? 187.157 149.361 130.464 1.00 30.10  ? 4634 SER A CB    1 
ATOM   23506 O  OG    . SER A 1 4634 ? 186.681 148.398 129.541 1.00 39.81  ? 4634 SER A OG    1 
ATOM   23507 N  N     . PHE A 1 4635 ? 187.153 152.389 131.604 1.00 26.88  ? 4635 PHE A N     1 
ATOM   23508 C  CA    . PHE A 1 4635 ? 187.552 153.368 132.609 1.00 25.04  ? 4635 PHE A CA    1 
ATOM   23509 C  C     . PHE A 1 4635 ? 186.339 153.931 133.338 1.00 22.74  ? 4635 PHE A C     1 
ATOM   23510 O  O     . PHE A 1 4635 ? 186.369 154.117 134.560 1.00 23.51  ? 4635 PHE A O     1 
ATOM   23511 C  CB    . PHE A 1 4635 ? 188.354 154.494 131.955 1.00 31.08  ? 4635 PHE A CB    1 
ATOM   23512 C  CG    . PHE A 1 4635 ? 189.810 154.176 131.775 1.00 25.80  ? 4635 PHE A CG    1 
ATOM   23513 C  CD1   . PHE A 1 4635 ? 190.226 153.320 130.769 1.00 28.30  ? 4635 PHE A CD1   1 
ATOM   23514 C  CD2   . PHE A 1 4635 ? 190.763 154.739 132.606 1.00 27.51  ? 4635 PHE A CD2   1 
ATOM   23515 C  CE1   . PHE A 1 4635 ? 191.564 153.026 130.600 1.00 32.96  ? 4635 PHE A CE1   1 
ATOM   23516 C  CE2   . PHE A 1 4635 ? 192.104 154.450 132.441 1.00 33.24  ? 4635 PHE A CE2   1 
ATOM   23517 C  CZ    . PHE A 1 4635 ? 192.505 153.592 131.437 1.00 33.25  ? 4635 PHE A CZ    1 
ATOM   23518 N  N     . TYR A 1 4636 ? 185.262 154.213 132.601 1.00 26.52  ? 4636 TYR A N     1 
ATOM   23519 C  CA    . TYR A 1 4636 ? 184.051 154.736 133.226 1.00 22.90  ? 4636 TYR A CA    1 
ATOM   23520 C  C     . TYR A 1 4636 ? 183.428 153.709 134.162 1.00 20.35  ? 4636 TYR A C     1 
ATOM   23521 O  O     . TYR A 1 4636 ? 182.962 154.055 135.254 1.00 22.53  ? 4636 TYR A O     1 
ATOM   23522 C  CB    . TYR A 1 4636 ? 183.040 155.153 132.155 1.00 22.46  ? 4636 TYR A CB    1 
ATOM   23523 C  CG    . TYR A 1 4636 ? 183.567 156.119 131.114 1.00 26.11  ? 4636 TYR A CG    1 
ATOM   23524 C  CD1   . TYR A 1 4636 ? 184.659 156.937 131.375 1.00 26.69  ? 4636 TYR A CD1   1 
ATOM   23525 C  CD2   . TYR A 1 4636 ? 182.968 156.209 129.865 1.00 24.64  ? 4636 TYR A CD2   1 
ATOM   23526 C  CE1   . TYR A 1 4636 ? 185.138 157.813 130.420 1.00 28.25  ? 4636 TYR A CE1   1 
ATOM   23527 C  CE2   . TYR A 1 4636 ? 183.439 157.084 128.907 1.00 28.07  ? 4636 TYR A CE2   1 
ATOM   23528 C  CZ    . TYR A 1 4636 ? 184.523 157.883 129.190 1.00 32.69  ? 4636 TYR A CZ    1 
ATOM   23529 O  OH    . TYR A 1 4636 ? 184.996 158.756 128.238 1.00 36.71  ? 4636 TYR A OH    1 
ATOM   23530 N  N     . GLU A 1 4637 ? 183.413 152.439 133.752 1.00 20.46  ? 4637 GLU A N     1 
ATOM   23531 C  CA    . GLU A 1 4637 ? 182.744 151.400 134.525 1.00 16.91  ? 4637 GLU A CA    1 
ATOM   23532 C  C     . GLU A 1 4637 ? 183.508 151.030 135.789 1.00 18.52  ? 4637 GLU A C     1 
ATOM   23533 O  O     . GLU A 1 4637 ? 182.895 150.596 136.771 1.00 20.75  ? 4637 GLU A O     1 
ATOM   23534 C  CB    . GLU A 1 4637 ? 182.538 150.157 133.659 1.00 21.87  ? 4637 GLU A CB    1 
ATOM   23535 C  CG    . GLU A 1 4637 ? 181.333 150.240 132.741 1.00 26.85  ? 4637 GLU A CG    1 
ATOM   23536 C  CD    . GLU A 1 4637 ? 181.304 149.122 131.720 1.00 35.60  ? 4637 GLU A CD    1 
ATOM   23537 O  OE1   . GLU A 1 4637 ? 182.038 148.128 131.903 1.00 33.50  ? 4637 GLU A OE1   1 
ATOM   23538 O  OE2   . GLU A 1 4637 ? 180.546 149.236 130.733 1.00 43.26  ? 4637 GLU A OE2   1 
ATOM   23539 N  N     . ARG A 1 4638 ? 184.828 151.184 135.789 1.00 19.57  ? 4638 ARG A N     1 
ATOM   23540 C  CA    . ARG A 1 4638 ? 185.647 150.826 136.937 1.00 16.71  ? 4638 ARG A CA    1 
ATOM   23541 C  C     . ARG A 1 4638 ? 185.815 151.971 137.927 1.00 21.82  ? 4638 ARG A C     1 
ATOM   23542 O  O     . ARG A 1 4638 ? 186.529 151.810 138.922 1.00 31.91  ? 4638 ARG A O     1 
ATOM   23543 C  CB    . ARG A 1 4638 ? 187.019 150.331 136.469 1.00 14.73  ? 4638 ARG A CB    1 
ATOM   23544 C  CG    . ARG A 1 4638 ? 186.976 148.950 135.836 1.00 14.86  ? 4638 ARG A CG    1 
ATOM   23545 C  CD    . ARG A 1 4638 ? 188.337 148.509 135.337 1.00 20.85  ? 4638 ARG A CD    1 
ATOM   23546 N  NE    . ARG A 1 4638 ? 189.308 148.389 136.418 1.00 19.77  ? 4638 ARG A NE    1 
ATOM   23547 C  CZ    . ARG A 1 4638 ? 190.133 147.363 136.571 1.00 17.31  ? 4638 ARG A CZ    1 
ATOM   23548 N  NH1   . ARG A 1 4638 ? 190.129 146.342 135.730 1.00 17.84  ? 4638 ARG A NH1   1 
ATOM   23549 N  NH2   . ARG A 1 4638 ? 190.984 147.362 137.593 1.00 22.52  ? 4638 ARG A NH2   1 
ATOM   23550 N  N     . GLY A 1 4639 ? 185.177 153.111 137.684 1.00 17.82  ? 4639 GLY A N     1 
ATOM   23551 C  CA    . GLY A 1 4639 ? 185.235 154.225 138.614 1.00 19.05  ? 4639 GLY A CA    1 
ATOM   23552 C  C     . GLY A 1 4639 ? 186.604 154.852 138.757 1.00 22.86  ? 4639 GLY A C     1 
ATOM   23553 O  O     . GLY A 1 4639 ? 187.000 155.221 139.870 1.00 26.62  ? 4639 GLY A O     1 
ATOM   23554 N  N     . VAL A 1 4640 ? 187.341 154.984 137.654 1.00 23.32  ? 4640 VAL A N     1 
ATOM   23555 C  CA    . VAL A 1 4640 ? 188.667 155.584 137.705 1.00 19.66  ? 4640 VAL A CA    1 
ATOM   23556 C  C     . VAL A 1 4640 ? 188.530 157.089 137.885 1.00 21.06  ? 4640 VAL A C     1 
ATOM   23557 O  O     . VAL A 1 4640 ? 187.811 157.757 137.132 1.00 26.77  ? 4640 VAL A O     1 
ATOM   23558 C  CB    . VAL A 1 4640 ? 189.458 155.242 136.434 1.00 19.18  ? 4640 VAL A CB    1 
ATOM   23559 C  CG1   . VAL A 1 4640 ? 190.864 155.803 136.516 1.00 26.33  ? 4640 VAL A CG1   1 
ATOM   23560 C  CG2   . VAL A 1 4640 ? 189.488 153.739 136.215 1.00 22.35  ? 4640 VAL A CG2   1 
ATOM   23561 N  N     . ALA A 1 4641 ? 189.219 157.630 138.886 1.00 19.94  ? 4641 ALA A N     1 
ATOM   23562 C  CA    . ALA A 1 4641 ? 189.138 159.052 139.189 1.00 20.65  ? 4641 ALA A CA    1 
ATOM   23563 C  C     . ALA A 1 4641 ? 190.416 159.473 139.905 1.00 31.28  ? 4641 ALA A C     1 
ATOM   23564 O  O     . ALA A 1 4641 ? 191.290 158.649 140.193 1.00 33.67  ? 4641 ALA A O     1 
ATOM   23565 C  CB    . ALA A 1 4641 ? 187.884 159.358 140.018 1.00 23.48  ? 4641 ALA A CB    1 
ATOM   23566 N  N     . VAL A 1 4642 ? 190.523 160.768 140.190 1.00 27.19  ? 4642 VAL A N     1 
ATOM   23567 C  CA    . VAL A 1 4642 ? 191.668 161.344 140.883 1.00 22.86  ? 4642 VAL A CA    1 
ATOM   23568 C  C     . VAL A 1 4642 ? 191.173 161.998 142.164 1.00 28.34  ? 4642 VAL A C     1 
ATOM   23569 O  O     . VAL A 1 4642 ? 190.141 162.679 142.164 1.00 30.77  ? 4642 VAL A O     1 
ATOM   23570 C  CB    . VAL A 1 4642 ? 192.414 162.368 140.000 1.00 28.54  ? 4642 VAL A CB    1 
ATOM   23571 C  CG1   . VAL A 1 4642 ? 193.621 162.936 140.734 1.00 30.45  ? 4642 VAL A CG1   1 
ATOM   23572 C  CG2   . VAL A 1 4642 ? 192.833 161.734 138.685 1.00 30.43  ? 4642 VAL A CG2   1 
ATOM   23573 N  N     . LEU A 1 4643 ? 191.899 161.785 143.259 1.00 29.43  ? 4643 LEU A N     1 
ATOM   23574 C  CA    . LEU A 1 4643 ? 191.567 162.375 144.547 1.00 31.00  ? 4643 LEU A CA    1 
ATOM   23575 C  C     . LEU A 1 4643 ? 192.616 163.410 144.925 1.00 31.52  ? 4643 LEU A C     1 
ATOM   23576 O  O     . LEU A 1 4643 ? 193.810 163.217 144.678 1.00 35.67  ? 4643 LEU A O     1 
ATOM   23577 C  CB    . LEU A 1 4643 ? 191.467 161.307 145.641 1.00 32.01  ? 4643 LEU A CB    1 
ATOM   23578 C  CG    . LEU A 1 4643 ? 190.465 160.177 145.396 1.00 28.47  ? 4643 LEU A CG    1 
ATOM   23579 C  CD1   . LEU A 1 4643 ? 190.447 159.215 146.573 1.00 24.47  ? 4643 LEU A CD1   1 
ATOM   23580 C  CD2   . LEU A 1 4643 ? 189.077 160.738 145.133 1.00 31.06  ? 4643 LEU A CD2   1 
ATOM   23581 N  N     . CYS A 1 4644 ? 192.161 164.513 145.523 1.00 31.99  ? 4644 CYS A N     1 
ATOM   23582 C  CA    . CYS A 1 4644 ? 193.078 165.570 145.933 1.00 36.44  ? 4644 CYS A CA    1 
ATOM   23583 C  C     . CYS A 1 4644 ? 193.882 165.194 147.170 1.00 40.68  ? 4644 CYS A C     1 
ATOM   23584 O  O     . CYS A 1 4644 ? 194.981 165.724 147.362 1.00 45.68  ? 4644 CYS A O     1 
ATOM   23585 C  CB    . CYS A 1 4644 ? 192.307 166.866 146.188 1.00 39.53  ? 4644 CYS A CB    1 
ATOM   23586 S  SG    . CYS A 1 4644 ? 191.725 167.694 144.690 1.00 57.13  ? 4644 CYS A SG    1 
ATOM   23587 N  N     . THR A 1 4645 ? 193.365 164.300 148.007 1.00 40.01  ? 4645 THR A N     1 
ATOM   23588 C  CA    . THR A 1 4645 ? 194.070 163.885 149.214 1.00 40.33  ? 4645 THR A CA    1 
ATOM   23589 C  C     . THR A 1 4645 ? 193.717 162.452 149.596 1.00 34.60  ? 4645 THR A C     1 
ATOM   23590 O  O     . THR A 1 4645 ? 192.736 161.892 149.108 1.00 36.70  ? 4645 THR A O     1 
ATOM   23591 C  CB    . THR A 1 4645 ? 193.752 164.815 150.401 1.00 47.96  ? 4645 THR A CB    1 
ATOM   23592 O  OG1   . THR A 1 4645 ? 194.542 164.434 151.534 1.00 53.68  ? 4645 THR A OG1   1 
ATOM   23593 C  CG2   . THR A 1 4645 ? 192.279 164.733 150.765 1.00 41.50  ? 4645 THR A CG2   1 
HETATM 23594 P  PB    . ADP B 2 .    ? 163.957 176.916 142.426 1.00 4.73   ? 4701 ADP A PB    1 
HETATM 23595 O  O1B   . ADP B 2 .    ? 163.989 177.897 143.574 1.00 11.03  ? 4701 ADP A O1B   1 
HETATM 23596 O  O2B   . ADP B 2 .    ? 165.139 175.980 142.372 1.00 7.74   ? 4701 ADP A O2B   1 
HETATM 23597 O  O3B   . ADP B 2 .    ? 162.618 176.244 142.241 1.00 10.12  ? 4701 ADP A O3B   1 
HETATM 23598 P  PA    . ADP B 2 .    ? 163.375 179.197 140.834 1.00 4.60   ? 4701 ADP A PA    1 
HETATM 23599 O  O1A   . ADP B 2 .    ? 162.063 178.900 140.151 1.00 6.31   ? 4701 ADP A O1A   1 
HETATM 23600 O  O2A   . ADP B 2 .    ? 163.408 180.026 142.095 1.00 20.74  ? 4701 ADP A O2A   1 
HETATM 23601 O  O3A   . ADP B 2 .    ? 164.128 177.794 141.086 1.00 7.36   ? 4701 ADP A O3A   1 
HETATM 23602 O  "O5'" . ADP B 2 .    ? 164.363 179.903 139.778 1.00 5.32   ? 4701 ADP A "O5'" 1 
HETATM 23603 C  "C5'" . ADP B 2 .    ? 165.033 181.108 140.143 1.00 7.20   ? 4701 ADP A "C5'" 1 
HETATM 23604 C  "C4'" . ADP B 2 .    ? 165.112 182.051 138.950 1.00 7.69   ? 4701 ADP A "C4'" 1 
HETATM 23605 O  "O4'" . ADP B 2 .    ? 165.827 181.454 137.867 1.00 9.40   ? 4701 ADP A "O4'" 1 
HETATM 23606 C  "C3'" . ADP B 2 .    ? 163.725 182.390 138.433 1.00 10.82  ? 4701 ADP A "C3'" 1 
HETATM 23607 O  "O3'" . ADP B 2 .    ? 163.445 183.772 138.669 1.00 21.91  ? 4701 ADP A "O3'" 1 
HETATM 23608 C  "C2'" . ADP B 2 .    ? 163.767 182.122 136.945 1.00 11.37  ? 4701 ADP A "C2'" 1 
HETATM 23609 O  "O2'" . ADP B 2 .    ? 163.312 183.268 136.225 1.00 17.75  ? 4701 ADP A "O2'" 1 
HETATM 23610 C  "C1'" . ADP B 2 .    ? 165.223 181.834 136.630 1.00 10.51  ? 4701 ADP A "C1'" 1 
HETATM 23611 N  N9    . ADP B 2 .    ? 165.322 180.737 135.639 1.00 5.68   ? 4701 ADP A N9    1 
HETATM 23612 C  C8    . ADP B 2 .    ? 165.463 179.430 135.917 1.00 5.78   ? 4701 ADP A C8    1 
HETATM 23613 N  N7    . ADP B 2 .    ? 165.522 178.690 134.782 1.00 6.42   ? 4701 ADP A N7    1 
HETATM 23614 C  C5    . ADP B 2 .    ? 165.416 179.539 133.746 1.00 5.18   ? 4701 ADP A C5    1 
HETATM 23615 C  C6    . ADP B 2 .    ? 165.403 179.423 132.271 1.00 4.74   ? 4701 ADP A C6    1 
HETATM 23616 N  N6    . ADP B 2 .    ? 165.520 178.220 131.662 1.00 6.23   ? 4701 ADP A N6    1 
HETATM 23617 N  N1    . ADP B 2 .    ? 165.274 180.557 131.553 1.00 5.21   ? 4701 ADP A N1    1 
HETATM 23618 C  C2    . ADP B 2 .    ? 165.158 181.759 132.143 1.00 5.78   ? 4701 ADP A C2    1 
HETATM 23619 N  N3    . ADP B 2 .    ? 165.161 181.938 133.474 1.00 5.89   ? 4701 ADP A N3    1 
HETATM 23620 C  C4    . ADP B 2 .    ? 165.285 180.886 134.315 1.00 4.64   ? 4701 ADP A C4    1 
HETATM 23621 P  PG    . ATP C 3 .    ? 170.556 197.228 165.641 1.00 3.78   ? 4702 ATP A PG    1 
HETATM 23622 O  O1G   . ATP C 3 .    ? 171.144 196.144 164.809 1.00 4.89   ? 4702 ATP A O1G   1 
HETATM 23623 O  O2G   . ATP C 3 .    ? 169.040 197.332 165.527 1.00 7.88   ? 4702 ATP A O2G   1 
HETATM 23624 O  O3G   . ATP C 3 .    ? 170.943 197.141 167.115 1.00 3.53   ? 4702 ATP A O3G   1 
HETATM 23625 P  PB    . ATP C 3 .    ? 171.224 199.533 163.851 1.00 0.50   ? 4702 ATP A PB    1 
HETATM 23626 O  O1B   . ATP C 3 .    ? 172.375 199.123 163.024 1.00 2.41   ? 4702 ATP A O1B   1 
HETATM 23627 O  O2B   . ATP C 3 .    ? 169.865 199.508 163.159 1.00 2.00   ? 4702 ATP A O2B   1 
HETATM 23628 O  O3B   . ATP C 3 .    ? 171.092 198.657 165.171 1.00 4.86   ? 4702 ATP A O3B   1 
HETATM 23629 P  PA    . ATP C 3 .    ? 170.503 202.243 164.773 1.00 3.80   ? 4702 ATP A PA    1 
HETATM 23630 O  O1A   . ATP C 3 .    ? 169.139 201.834 165.165 1.00 13.69  ? 4702 ATP A O1A   1 
HETATM 23631 O  O2A   . ATP C 3 .    ? 170.579 203.176 163.571 1.00 2.99   ? 4702 ATP A O2A   1 
HETATM 23632 O  O3A   . ATP C 3 .    ? 171.420 200.993 164.453 1.00 2.15   ? 4702 ATP A O3A   1 
HETATM 23633 O  "O5'" . ATP C 3 .    ? 171.239 202.926 165.990 1.00 10.43  ? 4702 ATP A "O5'" 1 
HETATM 23634 C  "C5'" . ATP C 3 .    ? 172.517 203.574 165.825 1.00 6.15   ? 4702 ATP A "C5'" 1 
HETATM 23635 C  "C4'" . ATP C 3 .    ? 172.623 204.678 166.846 1.00 6.32   ? 4702 ATP A "C4'" 1 
HETATM 23636 O  "O4'" . ATP C 3 .    ? 173.384 205.769 166.292 1.00 10.95  ? 4702 ATP A "O4'" 1 
HETATM 23637 C  "C3'" . ATP C 3 .    ? 171.298 205.305 167.258 1.00 6.26   ? 4702 ATP A "C3'" 1 
HETATM 23638 O  "O3'" . ATP C 3 .    ? 171.394 205.912 168.542 1.00 20.79  ? 4702 ATP A "O3'" 1 
HETATM 23639 C  "C2'" . ATP C 3 .    ? 171.078 206.341 166.155 1.00 8.33   ? 4702 ATP A "C2'" 1 
HETATM 23640 O  "O2'" . ATP C 3 .    ? 170.286 207.436 166.601 1.00 15.41  ? 4702 ATP A "O2'" 1 
HETATM 23641 C  "C1'" . ATP C 3 .    ? 172.511 206.799 165.857 1.00 8.27   ? 4702 ATP A "C1'" 1 
HETATM 23642 N  N9    . ATP C 3 .    ? 172.768 207.047 164.443 1.00 8.74   ? 4702 ATP A N9    1 
HETATM 23643 C  C8    . ATP C 3 .    ? 172.496 206.208 163.394 1.00 8.28   ? 4702 ATP A C8    1 
HETATM 23644 N  N7    . ATP C 3 .    ? 172.830 206.691 162.222 1.00 8.84   ? 4702 ATP A N7    1 
HETATM 23645 C  C5    . ATP C 3 .    ? 173.360 207.937 162.520 1.00 7.25   ? 4702 ATP A C5    1 
HETATM 23646 C  C6    . ATP C 3 .    ? 173.900 208.957 161.714 1.00 8.88   ? 4702 ATP A C6    1 
HETATM 23647 N  N6    . ATP C 3 .    ? 173.999 208.879 160.383 1.00 11.80  ? 4702 ATP A N6    1 
HETATM 23648 N  N1    . ATP C 3 .    ? 174.342 210.076 162.328 1.00 10.79  ? 4702 ATP A N1    1 
HETATM 23649 C  C2    . ATP C 3 .    ? 174.245 210.160 163.657 1.00 9.60   ? 4702 ATP A C2    1 
HETATM 23650 N  N3    . ATP C 3 .    ? 173.757 209.266 164.519 1.00 10.80  ? 4702 ATP A N3    1 
HETATM 23651 C  C4    . ATP C 3 .    ? 173.328 208.170 163.885 1.00 8.65   ? 4702 ATP A C4    1 
HETATM 23652 P  PB    . ADP D 2 .    ? 171.433 188.109 194.307 1.00 3.21   ? 4703 ADP A PB    1 
HETATM 23653 O  O1B   . ADP D 2 .    ? 170.236 188.953 193.947 1.00 6.42   ? 4703 ADP A O1B   1 
HETATM 23654 O  O2B   . ADP D 2 .    ? 171.173 186.622 194.312 1.00 7.27   ? 4703 ADP A O2B   1 
HETATM 23655 O  O3B   . ADP D 2 .    ? 172.707 188.515 193.607 1.00 5.55   ? 4703 ADP A O3B   1 
HETATM 23656 P  PA    . ADP D 2 .    ? 170.571 188.503 196.962 1.00 7.21   ? 4703 ADP A PA    1 
HETATM 23657 O  O1A   . ADP D 2 .    ? 170.141 189.938 197.151 1.00 5.85   ? 4703 ADP A O1A   1 
HETATM 23658 O  O2A   . ADP D 2 .    ? 169.537 187.443 196.668 1.00 12.90  ? 4703 ADP A O2A   1 
HETATM 23659 O  O3A   . ADP D 2 .    ? 171.733 188.460 195.848 1.00 7.01   ? 4703 ADP A O3A   1 
HETATM 23660 O  "O5'" . ADP D 2 .    ? 171.379 188.047 198.277 1.00 13.18  ? 4703 ADP A "O5'" 1 
HETATM 23661 C  "C5'" . ADP D 2 .    ? 172.451 188.850 198.766 1.00 10.86  ? 4703 ADP A "C5'" 1 
HETATM 23662 C  "C4'" . ADP D 2 .    ? 172.746 188.509 200.220 1.00 10.42  ? 4703 ADP A "C4'" 1 
HETATM 23663 O  "O4'" . ADP D 2 .    ? 173.993 189.085 200.616 1.00 13.72  ? 4703 ADP A "O4'" 1 
HETATM 23664 C  "C3'" . ADP D 2 .    ? 171.669 189.077 201.123 1.00 10.29  ? 4703 ADP A "C3'" 1 
HETATM 23665 O  "O3'" . ADP D 2 .    ? 171.068 188.022 201.878 1.00 21.09  ? 4703 ADP A "O3'" 1 
HETATM 23666 C  "C2'" . ADP D 2 .    ? 172.379 190.035 202.053 1.00 8.01   ? 4703 ADP A "C2'" 1 
HETATM 23667 O  "O2'" . ADP D 2 .    ? 172.015 189.762 203.409 1.00 13.04  ? 4703 ADP A "O2'" 1 
HETATM 23668 C  "C1'" . ADP D 2 .    ? 173.866 189.788 201.854 1.00 10.49  ? 4703 ADP A "C1'" 1 
HETATM 23669 N  N9    . ADP D 2 .    ? 174.622 191.064 201.769 1.00 6.87   ? 4703 ADP A N9    1 
HETATM 23670 C  C8    . ADP D 2 .    ? 175.577 191.332 200.859 1.00 9.60   ? 4703 ADP A C8    1 
HETATM 23671 N  N7    . ADP D 2 .    ? 176.095 192.573 201.036 1.00 12.13  ? 4703 ADP A N7    1 
HETATM 23672 C  C5    . ADP D 2 .    ? 175.466 193.123 202.088 1.00 9.04   ? 4703 ADP A C5    1 
HETATM 23673 C  C6    . ADP D 2 .    ? 175.533 194.415 202.809 1.00 11.74  ? 4703 ADP A C6    1 
HETATM 23674 N  N6    . ADP D 2 .    ? 176.394 195.388 202.428 1.00 13.45  ? 4703 ADP A N6    1 
HETATM 23675 N  N1    . ADP D 2 .    ? 174.705 194.594 203.858 1.00 14.42  ? 4703 ADP A N1    1 
HETATM 23676 C  C2    . ADP D 2 .    ? 173.842 193.639 204.248 1.00 13.52  ? 4703 ADP A C2    1 
HETATM 23677 N  N3    . ADP D 2 .    ? 173.732 192.445 203.642 1.00 8.85   ? 4703 ADP A N3    1 
HETATM 23678 C  C4    . ADP D 2 .    ? 174.502 192.125 202.575 1.00 6.49   ? 4703 ADP A C4    1 
HETATM 23679 P  PB    . ADP E 2 .    ? 159.814 158.529 199.994 1.00 17.61  ? 4704 ADP A PB    1 
HETATM 23680 O  O1B   . ADP E 2 .    ? 160.902 158.246 201.001 1.00 18.87  ? 4704 ADP A O1B   1 
HETATM 23681 O  O2B   . ADP E 2 .    ? 159.093 159.836 200.211 1.00 19.56  ? 4704 ADP A O2B   1 
HETATM 23682 O  O3B   . ADP E 2 .    ? 160.223 158.282 198.562 1.00 23.11  ? 4704 ADP A O3B   1 
HETATM 23683 P  PA    . ADP E 2 .    ? 158.111 157.107 201.739 1.00 17.63  ? 4704 ADP A PA    1 
HETATM 23684 O  O1A   . ADP E 2 .    ? 159.250 156.682 202.629 1.00 24.30  ? 4704 ADP A O1A   1 
HETATM 23685 O  O2A   . ADP E 2 .    ? 157.219 158.251 202.151 1.00 14.06  ? 4704 ADP A O2A   1 
HETATM 23686 O  O3A   . ADP E 2 .    ? 158.698 157.395 200.265 1.00 26.75  ? 4704 ADP A O3A   1 
HETATM 23687 O  "O5'" . ADP E 2 .    ? 157.205 155.795 201.525 1.00 27.77  ? 4704 ADP A "O5'" 1 
HETATM 23688 C  "C5'" . ADP E 2 .    ? 156.418 155.303 202.607 1.00 30.90  ? 4704 ADP A "C5'" 1 
HETATM 23689 C  "C4'" . ADP E 2 .    ? 156.871 153.893 202.963 1.00 24.73  ? 4704 ADP A "C4'" 1 
HETATM 23690 O  "O4'" . ADP E 2 .    ? 158.250 153.906 203.342 1.00 21.04  ? 4704 ADP A "O4'" 1 
HETATM 23691 C  "C3'" . ADP E 2 .    ? 156.087 153.343 204.142 1.00 26.50  ? 4704 ADP A "C3'" 1 
HETATM 23692 O  "O3'" . ADP E 2 .    ? 155.280 152.239 203.725 1.00 36.87  ? 4704 ADP A "O3'" 1 
HETATM 23693 C  "C2'" . ADP E 2 .    ? 157.119 152.877 205.149 1.00 26.35  ? 4704 ADP A "C2'" 1 
HETATM 23694 O  "O2'" . ADP E 2 .    ? 156.942 151.486 205.430 1.00 28.61  ? 4704 ADP A "O2'" 1 
HETATM 23695 C  "C1'" . ADP E 2 .    ? 158.475 153.104 204.505 1.00 22.16  ? 4704 ADP A "C1'" 1 
HETATM 23696 N  N9    . ADP E 2 .    ? 159.370 153.830 205.441 1.00 20.53  ? 4704 ADP A N9    1 
HETATM 23697 C  C8    . ADP E 2 .    ? 159.961 155.012 205.191 1.00 22.01  ? 4704 ADP A C8    1 
HETATM 23698 N  N7    . ADP E 2 .    ? 160.723 155.414 206.239 1.00 24.80  ? 4704 ADP A N7    1 
HETATM 23699 C  C5    . ADP E 2 .    ? 160.629 154.470 207.190 1.00 18.60  ? 4704 ADP A C5    1 
HETATM 23700 C  C6    . ADP E 2 .    ? 161.184 154.270 208.549 1.00 18.19  ? 4704 ADP A C6    1 
HETATM 23701 N  N6    . ADP E 2 .    ? 162.012 155.183 209.110 1.00 17.58  ? 4704 ADP A N6    1 
HETATM 23702 N  N1    . ADP E 2 .    ? 160.838 153.146 209.209 1.00 21.39  ? 4704 ADP A N1    1 
HETATM 23703 C  C2    . ADP E 2 .    ? 160.016 152.232 208.665 1.00 21.87  ? 4704 ADP A C2    1 
HETATM 23704 N  N3    . ADP E 2 .    ? 159.476 152.351 207.440 1.00 19.97  ? 4704 ADP A N3    1 
HETATM 23705 C  C4    . ADP E 2 .    ? 159.741 153.425 206.660 1.00 16.94  ? 4704 ADP A C4    1 
HETATM 23706 MG MG    . MG  F 4 .    ? 160.911 177.189 143.550 1.00 15.68  ? 4705 MG  A MG    1 
HETATM 23707 MG MG    . MG  G 4 .    ? 167.635 198.851 164.423 1.00 4.58   ? 4706 MG  A MG    1 
HETATM 23708 O  O     . HOH H 5 .    ? 161.393 175.400 144.192 1.00 13.55  ? 4801 HOH A O     1 
HETATM 23709 O  O     . HOH H 5 .    ? 161.748 177.332 145.347 1.00 8.92   ? 4802 HOH A O     1 
HETATM 23710 O  O     . HOH H 5 .    ? 160.973 179.139 143.873 1.00 12.79  ? 4803 HOH A O     1 
# 
