data_9BML
# 
_entry.id   9BML 
# 
_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   9BML         pdb_00009bml 10.2210/pdb9bml/pdb 
WWPDB D_1000283529 ?            ?                   
EMDB  EMD-44702    ?            ?                   
# 
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                        9BML 
_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 the motor domain from full-length human dynein-1 in 5mM AMPPNP' 
_pdbx_database_related.db_id          EMD-44702 
_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     1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cytoplasmic dynein heavy chain 1,Dynein heavy chain,cytosolic' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKSALEQMRKFLSDPQVHTVLVE
RSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIKRTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPF
FKSYIRESGKADRDGDKMAPSVEKKIAELEMGLLHLQQNIEIPEISLPIHPMITNVAKQCYERGEKPKVTDFGDKVEDPT
FLNQLQSGVNRWIREIQKVTKLDRDPASGTALQEISFWLNLERALYRIQEKRESPEVLLTLDILKHGKRFHATVSFDTDT
GLKQALETVNDYNPLMKDFPLNDLLSATELDKIRQALVAIFTHLRKIRNTKYPIQRALRLVEAISRDLSSQLLKVLGTRK
LMHVAYEEFEKVMVACFEVFQTWDDEYEKLQVLLRDIVKRKREENLKMVWRINPAHRKLQARLDQMRKFRRQHEQLRAVI
VRVLRPQVTAVAQQNQGEVPEPQDMKVAEVLFDAADANAIEEVNLAYENVKEVDGLDVSKEGTEAWEAAMKRYDERIDRV
ETRITARLRDQLGTAKNANEMFRIFSRFNALFVRPHIRGAIREYQTQLIQRVKDDIESLHDKFKVQYPQSQACKMSHVRD
LPPVSGSIIWAKQIDRQLTAYMKRVEDVLGKGWENHVEGQKLKQDGDSFRMKLNTQEIFDDWARKVQQRNLGVSGRIFTI
ESTRVRGRTGNVLKLKVNFLPEIITLSKEVRNLKWLGFRVPLAIVNKAHQANQLYPFAISLIESVRTYERTCEKVEERNT
ISLLVAGLKKEVQALIAEGIALVWESYKLDPYVQRLAETVFNFQEKVDDLLIIEEKIDLEVRSLETCMYDHKTFSEILNR
VQKAVDDLNLHSYSNLPIWVNKLDMEIERILGVRLQAGLRAWTQVLLGQAEDKAEVDMDTDAPQVSHKPGGEPKIKNVVH
ELRITNQVIYLNPPIEECRYKLYQEMFAWKMVVLSLPRIQSQRYQVGVHYELTEEEKFYRNALTRMPDGPVALEESYSAV
MGIVSEVEQYVKVWLQYQCLWDMQAENIYNRLGEDLNKWQALLVQIRKARGTFDNAETKKEFGPVVIDYGKVQSKVNLKY
DSWHKEVLSKFGQMLGSNMTEFHSQISKSRQELEQHSVDTASTSDAVTFITYVQSLKRKIKQFEKQVELYRNGQRLLEKQ
RFQFPPSWLYIDNIEGEWGAFNDIMRRKDSAIQQQVANLQMKIVQEDRAVESRTTDLLTDWEKTKPVTGNLRPEEALQAL
TIYEGKFGRLKDDREKCAKAKEALELTDTGLLSGSEERVQVALEELQDLKGVWSELSKVWEQIDQMKEQPWVSVQPRKLR
QNLDALLNQLKSFPARLRQYASYEFVQRLLKGYMKINMLVIELKSEALKDRHWKQLMKRLHVNWVVSELTLGQIWDVDLQ
KNEAIVKDVLLVAQGEMALEEFLKQIREVWNTYELDLVNYQNKCRLIRGWDDLFNKVKEHINSVSAMKLSPYYKVFEEDA
LSWEDKLNRIMALFDVWIDVQRRWVYLEGIFTGSADIKHLLPVETQRFQSISTEFLALMKKVSKSPLVMDVLNIQGVQRS
LERLADLLGKIQKALGEYLERERSSFPRFYFVGDEDLLEIIGNSKNVAKLQKHFKKMFAGVSSIILNEDNSVVLGISSRE
GEEVMFKTPVSITEHPKINEWLTLVEKEMRVTLAKLLAESVTEVEIFGKATSIDPNTYITWIDKYQAQLVVLSAQIAWSE
NVETALSSMGGGGDAAPLHSVLSNVEVTLNVLADSVLMEQPPLRRRKLEHLITELVHQRDVTRSLIKSKIDNAKSFEWLS
QMRFYFDPKQTDVLQQLSIQMANAKFNYGFEYLGVQDKLVQTPLTDRCYLTMTQALEARLGGSPFGPAGTGKTESVKALG
HQLGRFVLVFNCDETFDFQAMGRIFVGLCQVGAWGCFDEFNRLEERMLSAVSQQVQCIQEALREHSNPNYDKTSAPITCE
LLNKQVKVSPDMAIFITMNPGYAGRSNLPDNLKKLFRSLAMTKPDRQLIAQVMLYSQGFRTAEVLANKIVPFFKLCDEQL
SSQSHYDFGLRALKSVLVSAGNVKRERIQKIKREKEERGEAVDEGEIAENLPEQEILIQSVCETMVPKLVAEDIPLLFSL
LSDVFPGVQYHRGEMTALREELKKVCQEMYLTYGDGEEVGGMWVEKVLQLYQITQINHGLMMVGPSGSGKSMAWRVLLKA
LERLEGVEGVAHIIDPKAISKDHLYGTLDPNTREWTDGLFTHVLRKIIDSVRGELQKRQWIVFDGDVDPEWVENLNSVLD
DNKLLTLPNGERLSLPPNVRIMFEVQDLKYATLATVSRCGMVWFSEDVLSTDMIFNNFLARLRSIPLDEGEDEAQRRRKG
KEDEGEEAASPMLQIQRDAATIMQPYFTSNGLVTKALEHAFQLEHIMDLTRLRCLGSLFSMLHQACRNVAQYNANHPDFP
MQIEQLERYIQRYLVYAILWSLSGDSRLKMRAELGEYIRRITTVPLPTAPNIPIIDYEVSISGEWSPWQAKVPQIEVETH
KVAAPDVVVPTLDTVRHEALLYTWLAEHKPLVLCGPPGSGKTMTLFSALRALPDMEVVGLNFSSATTPELLLKTFDHYCE
YRRTPNGVVLAPVQLGKWLVLFCDEINLPDMDKYGTQRVISFIRQMVEHGGFYRTSDQTWVKLERIQFVGACNPPTDPGR
KPLSHRFLRHVPVVYVDYPGPASLTQIYGTFNRAMLRLIPSLRTYAEPLTAAMVEFYTMSQERFTQDTQPHYIYSPREMT
RWVRGIFEALRPLETLPVEGLIRIWAHEALRLFQDRLVEDEERRWTDENIDTVALKHFPNIDREKAMSRPILYSNWLSKD
YIPVDQEELRDYVKARLKVFYEEELDVPLVLFNEVLDHVLRIDRIFRQPQGHLLLIGVSGAGKTTLSRFVAWMNGLSVYQ
IKVHRKYTGEDFDEDLRTVLRRSGCKNEKIAFIMDESNVLDSGFLERMNTLLANGEVPGLFEGDEYATLMTQCKEGAQKE
GLMLDSHEELYKWFTSQVIRNLHVVFTMNPSSEGLKDRAATSPALFNRCVLNWFGDWSTEALYQVGKEFTSKMDLEKPNY
IVPDYMPVVYDKLPQPPSHREAIVNSCVFVHQTLHQANARLAKRGGRTMAITPRHYLDFINHYANLFHEKRSELEEQQMH
LNVGLRKIKETVDQVEELRRDLRIKSQELEVKNAAANDKLKKMVKDQQEAEKKKVMSQEIQEQLHKQQEVIADKQMSVKE
DLDKVEPAVIEAQNAVKSIKKQHLVEVRSMANPPAAVKLALESICLLLGESTTDWKQIRSIIMRENFIPTIVNFSAEEIS
DAIREKMKKNYMSNPSYNYEIVNRASLACGPMVKWAIAQLNYADMLKRVEPLRNELQKLEDDAKDNQQKANEVEQMIRDL
EASIARYKEEYAVLISEAQAIKADLAAVEAKVNRSTALLKSLSAERERWEKTSETFKNQMSTIAGDCLLSAAFIAYAGYF
DQQMRQNLFTTWSHHLQQANIQFRTDIARTEYLSNADERLRWQASSLPADDLCTENAIMLKRFNRYPLIIDPSGQATEFI
MNEYKDRKITRTSFLDDAFRKNLESALRFGNPLLVQDVESYDPVLNPVLNREVRRTGGRVLITLGDQDIDLSPSFVIFLS
TRDPTVEFPPDLCSRVTFVNFTVTRSSLQSQCLNEVLKAERPDVDEKRSDLLKLQGEFQLRLRQLEKSLLQALNEVKGRI
LDDDTIITTLENLKREAAEVTRKVEETDIVMQEVETVSQQYLPLSTACSSIYFTMESLKQIHFLYQYSLQFFLDIYHNVL
YENPNLKGVTDHTQRLSIITKDLFQVAFNRVARGMLHQDHITFAMLLARIKLKGTVGEPTYDAEFQHFLRGNEIVLSAGS
TPRIQGLTVEQAEAVVRLSCLPAFKDLIAKVQADEQFGIWLDSSSPEQTVPYLWSEETPATPIGQAIHRLLLIQAFRPDR
LLAMAHMFVSTNLGESFMSIMEQPLDLTHIVGTEVKPNTPVLMCSVPGYDASGHVEDLAAEQNTQITSIAIGSAEGFNQA
DKAINTAVKSGRWVMLKNVHLAPGWLMQLEKKLHSLQPHACFRLFLTMEINPKVPVNLLRAGRIFVFEPPPGVKANMLRT
FSSIPVSRICKSPNERARLYFLLAWFHAIIQERLRYAPLGWSKKYEFGESDLRSACDTVDTWLDDTAKGRQNISPDKIPW
SALKTLMAQSIYGGRVDNEFDQRLLNTFLERLFTTRSFDSEFKLACKVDGHKDIQMPDGIRREEFVQWVELLPDTQTPSW
LGLPNNAERVLLTTQGVDMISKMLKMQMLEDEDDLAYAETEKKTRTDSTSDGRPAWMRTLHTTASNWLHLIPQTLSHLKR
TVENIKDPLFRFFEREVKMGAKLLQDVRQDLADVVQVCEGKKKQTNYLRTLINELVKGILPRSWSHYTVPAGMTVIQWVS
DFSERIKQLQNISLAAASGGAKELKNIHVCLGGLFVPEAYITATRQYVAQANSWSLEELCLEVNVTTSQGATLDACSFGV
TGLKLQGATCNNNKLSLSNAISTALPLTQLRWVKQTNTEKKASVVTLPVYLNFTRADLIFTVDFEIATKEDPRSFYERGV
AVLCTE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
3 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
4 'MAGNESIUM ION'             MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    PRO n 
1 5    GLY n 
1 6    GLY n 
1 7    GLY n 
1 8    GLY n 
1 9    GLY n 
1 10   GLU n 
1 11   ASP n 
1 12   GLY n 
1 13   SER n 
1 14   ALA n 
1 15   GLY n 
1 16   LEU n 
1 17   GLU n 
1 18   VAL n 
1 19   SER n 
1 20   ALA n 
1 21   VAL n 
1 22   GLN n 
1 23   ASN n 
1 24   VAL n 
1 25   ALA n 
1 26   ASP n 
1 27   VAL n 
1 28   SER n 
1 29   VAL n 
1 30   LEU n 
1 31   GLN n 
1 32   LYS n 
1 33   HIS n 
1 34   LEU n 
1 35   ARG n 
1 36   LYS n 
1 37   LEU n 
1 38   VAL n 
1 39   PRO n 
1 40   LEU n 
1 41   LEU n 
1 42   LEU n 
1 43   GLU n 
1 44   ASP n 
1 45   GLY n 
1 46   GLY n 
1 47   GLU n 
1 48   ALA n 
1 49   PRO n 
1 50   ALA n 
1 51   ALA n 
1 52   LEU n 
1 53   GLU n 
1 54   ALA n 
1 55   ALA n 
1 56   LEU n 
1 57   GLU n 
1 58   GLU n 
1 59   LYS n 
1 60   SER n 
1 61   ALA n 
1 62   LEU n 
1 63   GLU n 
1 64   GLN n 
1 65   MET n 
1 66   ARG n 
1 67   LYS n 
1 68   PHE n 
1 69   LEU n 
1 70   SER n 
1 71   ASP n 
1 72   PRO n 
1 73   GLN n 
1 74   VAL n 
1 75   HIS n 
1 76   THR n 
1 77   VAL n 
1 78   LEU n 
1 79   VAL n 
1 80   GLU n 
1 81   ARG n 
1 82   SER n 
1 83   THR n 
1 84   LEU n 
1 85   LYS n 
1 86   GLU n 
1 87   ASP n 
1 88   VAL n 
1 89   GLY n 
1 90   ASP n 
1 91   GLU n 
1 92   GLY n 
1 93   GLU n 
1 94   GLU n 
1 95   GLU n 
1 96   LYS n 
1 97   GLU n 
1 98   PHE n 
1 99   ILE n 
1 100  SER n 
1 101  TYR n 
1 102  ASN n 
1 103  ILE n 
1 104  ASN n 
1 105  ILE n 
1 106  ASP n 
1 107  ILE n 
1 108  HIS n 
1 109  TYR n 
1 110  GLY n 
1 111  VAL n 
1 112  LYS n 
1 113  SER n 
1 114  ASN n 
1 115  SER n 
1 116  LEU n 
1 117  ALA n 
1 118  PHE n 
1 119  ILE n 
1 120  LYS n 
1 121  ARG n 
1 122  THR n 
1 123  PRO n 
1 124  VAL n 
1 125  ILE n 
1 126  ASP n 
1 127  ALA n 
1 128  ASP n 
1 129  LYS n 
1 130  PRO n 
1 131  VAL n 
1 132  SER n 
1 133  SER n 
1 134  GLN n 
1 135  LEU n 
1 136  ARG n 
1 137  VAL n 
1 138  LEU n 
1 139  THR n 
1 140  LEU n 
1 141  SER n 
1 142  GLU n 
1 143  ASP n 
1 144  SER n 
1 145  PRO n 
1 146  TYR n 
1 147  GLU n 
1 148  THR n 
1 149  LEU n 
1 150  HIS n 
1 151  SER n 
1 152  PHE n 
1 153  ILE n 
1 154  SER n 
1 155  ASN n 
1 156  ALA n 
1 157  VAL n 
1 158  ALA n 
1 159  PRO n 
1 160  PHE n 
1 161  PHE n 
1 162  LYS n 
1 163  SER n 
1 164  TYR n 
1 165  ILE n 
1 166  ARG n 
1 167  GLU n 
1 168  SER n 
1 169  GLY n 
1 170  LYS n 
1 171  ALA n 
1 172  ASP n 
1 173  ARG n 
1 174  ASP n 
1 175  GLY n 
1 176  ASP n 
1 177  LYS n 
1 178  MET n 
1 179  ALA n 
1 180  PRO n 
1 181  SER n 
1 182  VAL n 
1 183  GLU n 
1 184  LYS n 
1 185  LYS n 
1 186  ILE n 
1 187  ALA n 
1 188  GLU n 
1 189  LEU n 
1 190  GLU n 
1 191  MET n 
1 192  GLY n 
1 193  LEU n 
1 194  LEU n 
1 195  HIS n 
1 196  LEU n 
1 197  GLN n 
1 198  GLN n 
1 199  ASN n 
1 200  ILE n 
1 201  GLU n 
1 202  ILE n 
1 203  PRO n 
1 204  GLU n 
1 205  ILE n 
1 206  SER n 
1 207  LEU n 
1 208  PRO n 
1 209  ILE n 
1 210  HIS n 
1 211  PRO n 
1 212  MET n 
1 213  ILE n 
1 214  THR n 
1 215  ASN n 
1 216  VAL n 
1 217  ALA n 
1 218  LYS n 
1 219  GLN n 
1 220  CYS n 
1 221  TYR n 
1 222  GLU n 
1 223  ARG n 
1 224  GLY n 
1 225  GLU n 
1 226  LYS n 
1 227  PRO n 
1 228  LYS n 
1 229  VAL n 
1 230  THR n 
1 231  ASP n 
1 232  PHE n 
1 233  GLY n 
1 234  ASP n 
1 235  LYS n 
1 236  VAL n 
1 237  GLU n 
1 238  ASP n 
1 239  PRO n 
1 240  THR n 
1 241  PHE n 
1 242  LEU n 
1 243  ASN n 
1 244  GLN n 
1 245  LEU n 
1 246  GLN n 
1 247  SER n 
1 248  GLY n 
1 249  VAL n 
1 250  ASN n 
1 251  ARG n 
1 252  TRP n 
1 253  ILE n 
1 254  ARG n 
1 255  GLU n 
1 256  ILE n 
1 257  GLN n 
1 258  LYS n 
1 259  VAL n 
1 260  THR n 
1 261  LYS n 
1 262  LEU n 
1 263  ASP n 
1 264  ARG n 
1 265  ASP n 
1 266  PRO n 
1 267  ALA n 
1 268  SER n 
1 269  GLY n 
1 270  THR n 
1 271  ALA n 
1 272  LEU n 
1 273  GLN n 
1 274  GLU n 
1 275  ILE n 
1 276  SER n 
1 277  PHE n 
1 278  TRP n 
1 279  LEU n 
1 280  ASN n 
1 281  LEU n 
1 282  GLU n 
1 283  ARG n 
1 284  ALA n 
1 285  LEU n 
1 286  TYR n 
1 287  ARG n 
1 288  ILE n 
1 289  GLN n 
1 290  GLU n 
1 291  LYS n 
1 292  ARG n 
1 293  GLU n 
1 294  SER n 
1 295  PRO n 
1 296  GLU n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  THR n 
1 301  LEU n 
1 302  ASP n 
1 303  ILE n 
1 304  LEU n 
1 305  LYS n 
1 306  HIS n 
1 307  GLY n 
1 308  LYS n 
1 309  ARG n 
1 310  PHE n 
1 311  HIS n 
1 312  ALA n 
1 313  THR n 
1 314  VAL n 
1 315  SER n 
1 316  PHE n 
1 317  ASP n 
1 318  THR n 
1 319  ASP n 
1 320  THR n 
1 321  GLY n 
1 322  LEU n 
1 323  LYS n 
1 324  GLN n 
1 325  ALA n 
1 326  LEU n 
1 327  GLU n 
1 328  THR n 
1 329  VAL n 
1 330  ASN n 
1 331  ASP n 
1 332  TYR n 
1 333  ASN n 
1 334  PRO n 
1 335  LEU n 
1 336  MET n 
1 337  LYS n 
1 338  ASP n 
1 339  PHE n 
1 340  PRO n 
1 341  LEU n 
1 342  ASN n 
1 343  ASP n 
1 344  LEU n 
1 345  LEU n 
1 346  SER n 
1 347  ALA n 
1 348  THR n 
1 349  GLU n 
1 350  LEU n 
1 351  ASP n 
1 352  LYS n 
1 353  ILE n 
1 354  ARG n 
1 355  GLN n 
1 356  ALA n 
1 357  LEU n 
1 358  VAL n 
1 359  ALA n 
1 360  ILE n 
1 361  PHE n 
1 362  THR n 
1 363  HIS n 
1 364  LEU n 
1 365  ARG n 
1 366  LYS n 
1 367  ILE n 
1 368  ARG n 
1 369  ASN n 
1 370  THR n 
1 371  LYS n 
1 372  TYR n 
1 373  PRO n 
1 374  ILE n 
1 375  GLN n 
1 376  ARG n 
1 377  ALA n 
1 378  LEU n 
1 379  ARG n 
1 380  LEU n 
1 381  VAL n 
1 382  GLU n 
1 383  ALA n 
1 384  ILE n 
1 385  SER n 
1 386  ARG n 
1 387  ASP n 
1 388  LEU n 
1 389  SER n 
1 390  SER n 
1 391  GLN n 
1 392  LEU n 
1 393  LEU n 
1 394  LYS n 
1 395  VAL n 
1 396  LEU n 
1 397  GLY n 
1 398  THR n 
1 399  ARG n 
1 400  LYS n 
1 401  LEU n 
1 402  MET n 
1 403  HIS n 
1 404  VAL n 
1 405  ALA n 
1 406  TYR n 
1 407  GLU n 
1 408  GLU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  VAL n 
1 413  MET n 
1 414  VAL n 
1 415  ALA n 
1 416  CYS n 
1 417  PHE n 
1 418  GLU n 
1 419  VAL n 
1 420  PHE n 
1 421  GLN n 
1 422  THR n 
1 423  TRP n 
1 424  ASP n 
1 425  ASP n 
1 426  GLU n 
1 427  TYR n 
1 428  GLU n 
1 429  LYS n 
1 430  LEU n 
1 431  GLN n 
1 432  VAL n 
1 433  LEU n 
1 434  LEU n 
1 435  ARG n 
1 436  ASP n 
1 437  ILE n 
1 438  VAL n 
1 439  LYS n 
1 440  ARG n 
1 441  LYS n 
1 442  ARG n 
1 443  GLU n 
1 444  GLU n 
1 445  ASN n 
1 446  LEU n 
1 447  LYS n 
1 448  MET n 
1 449  VAL n 
1 450  TRP n 
1 451  ARG n 
1 452  ILE n 
1 453  ASN n 
1 454  PRO n 
1 455  ALA n 
1 456  HIS n 
1 457  ARG n 
1 458  LYS n 
1 459  LEU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  LEU n 
1 464  ASP n 
1 465  GLN n 
1 466  MET n 
1 467  ARG n 
1 468  LYS n 
1 469  PHE n 
1 470  ARG n 
1 471  ARG n 
1 472  GLN n 
1 473  HIS n 
1 474  GLU n 
1 475  GLN n 
1 476  LEU n 
1 477  ARG n 
1 478  ALA n 
1 479  VAL n 
1 480  ILE n 
1 481  VAL n 
1 482  ARG n 
1 483  VAL n 
1 484  LEU n 
1 485  ARG n 
1 486  PRO n 
1 487  GLN n 
1 488  VAL n 
1 489  THR n 
1 490  ALA n 
1 491  VAL n 
1 492  ALA n 
1 493  GLN n 
1 494  GLN n 
1 495  ASN n 
1 496  GLN n 
1 497  GLY n 
1 498  GLU n 
1 499  VAL n 
1 500  PRO n 
1 501  GLU n 
1 502  PRO n 
1 503  GLN n 
1 504  ASP n 
1 505  MET n 
1 506  LYS n 
1 507  VAL n 
1 508  ALA n 
1 509  GLU n 
1 510  VAL n 
1 511  LEU n 
1 512  PHE n 
1 513  ASP n 
1 514  ALA n 
1 515  ALA n 
1 516  ASP n 
1 517  ALA n 
1 518  ASN n 
1 519  ALA n 
1 520  ILE n 
1 521  GLU n 
1 522  GLU n 
1 523  VAL n 
1 524  ASN n 
1 525  LEU n 
1 526  ALA n 
1 527  TYR n 
1 528  GLU n 
1 529  ASN n 
1 530  VAL n 
1 531  LYS n 
1 532  GLU n 
1 533  VAL n 
1 534  ASP n 
1 535  GLY n 
1 536  LEU n 
1 537  ASP n 
1 538  VAL n 
1 539  SER n 
1 540  LYS n 
1 541  GLU n 
1 542  GLY n 
1 543  THR n 
1 544  GLU n 
1 545  ALA n 
1 546  TRP n 
1 547  GLU n 
1 548  ALA n 
1 549  ALA n 
1 550  MET n 
1 551  LYS n 
1 552  ARG n 
1 553  TYR n 
1 554  ASP n 
1 555  GLU n 
1 556  ARG n 
1 557  ILE n 
1 558  ASP n 
1 559  ARG n 
1 560  VAL n 
1 561  GLU n 
1 562  THR n 
1 563  ARG n 
1 564  ILE n 
1 565  THR n 
1 566  ALA n 
1 567  ARG n 
1 568  LEU n 
1 569  ARG n 
1 570  ASP n 
1 571  GLN n 
1 572  LEU n 
1 573  GLY n 
1 574  THR n 
1 575  ALA n 
1 576  LYS n 
1 577  ASN n 
1 578  ALA n 
1 579  ASN n 
1 580  GLU n 
1 581  MET n 
1 582  PHE n 
1 583  ARG n 
1 584  ILE n 
1 585  PHE n 
1 586  SER n 
1 587  ARG n 
1 588  PHE n 
1 589  ASN n 
1 590  ALA n 
1 591  LEU n 
1 592  PHE n 
1 593  VAL n 
1 594  ARG n 
1 595  PRO n 
1 596  HIS n 
1 597  ILE n 
1 598  ARG n 
1 599  GLY n 
1 600  ALA n 
1 601  ILE n 
1 602  ARG n 
1 603  GLU n 
1 604  TYR n 
1 605  GLN n 
1 606  THR n 
1 607  GLN n 
1 608  LEU n 
1 609  ILE n 
1 610  GLN n 
1 611  ARG n 
1 612  VAL n 
1 613  LYS n 
1 614  ASP n 
1 615  ASP n 
1 616  ILE n 
1 617  GLU n 
1 618  SER n 
1 619  LEU n 
1 620  HIS n 
1 621  ASP n 
1 622  LYS n 
1 623  PHE n 
1 624  LYS n 
1 625  VAL n 
1 626  GLN n 
1 627  TYR n 
1 628  PRO n 
1 629  GLN n 
1 630  SER n 
1 631  GLN n 
1 632  ALA n 
1 633  CYS n 
1 634  LYS n 
1 635  MET n 
1 636  SER n 
1 637  HIS n 
1 638  VAL n 
1 639  ARG n 
1 640  ASP n 
1 641  LEU n 
1 642  PRO n 
1 643  PRO n 
1 644  VAL n 
1 645  SER n 
1 646  GLY n 
1 647  SER n 
1 648  ILE n 
1 649  ILE n 
1 650  TRP n 
1 651  ALA n 
1 652  LYS n 
1 653  GLN n 
1 654  ILE n 
1 655  ASP n 
1 656  ARG n 
1 657  GLN n 
1 658  LEU n 
1 659  THR n 
1 660  ALA n 
1 661  TYR n 
1 662  MET n 
1 663  LYS n 
1 664  ARG n 
1 665  VAL n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LEU n 
1 670  GLY n 
1 671  LYS n 
1 672  GLY n 
1 673  TRP n 
1 674  GLU n 
1 675  ASN n 
1 676  HIS n 
1 677  VAL n 
1 678  GLU n 
1 679  GLY n 
1 680  GLN n 
1 681  LYS n 
1 682  LEU n 
1 683  LYS n 
1 684  GLN n 
1 685  ASP n 
1 686  GLY n 
1 687  ASP n 
1 688  SER n 
1 689  PHE n 
1 690  ARG n 
1 691  MET n 
1 692  LYS n 
1 693  LEU n 
1 694  ASN n 
1 695  THR n 
1 696  GLN n 
1 697  GLU n 
1 698  ILE n 
1 699  PHE n 
1 700  ASP n 
1 701  ASP n 
1 702  TRP n 
1 703  ALA n 
1 704  ARG n 
1 705  LYS n 
1 706  VAL n 
1 707  GLN n 
1 708  GLN n 
1 709  ARG n 
1 710  ASN n 
1 711  LEU n 
1 712  GLY n 
1 713  VAL n 
1 714  SER n 
1 715  GLY n 
1 716  ARG n 
1 717  ILE n 
1 718  PHE n 
1 719  THR n 
1 720  ILE n 
1 721  GLU n 
1 722  SER n 
1 723  THR n 
1 724  ARG n 
1 725  VAL n 
1 726  ARG n 
1 727  GLY n 
1 728  ARG n 
1 729  THR n 
1 730  GLY n 
1 731  ASN n 
1 732  VAL n 
1 733  LEU n 
1 734  LYS n 
1 735  LEU n 
1 736  LYS n 
1 737  VAL n 
1 738  ASN n 
1 739  PHE n 
1 740  LEU n 
1 741  PRO n 
1 742  GLU n 
1 743  ILE n 
1 744  ILE n 
1 745  THR n 
1 746  LEU n 
1 747  SER n 
1 748  LYS n 
1 749  GLU n 
1 750  VAL n 
1 751  ARG n 
1 752  ASN n 
1 753  LEU n 
1 754  LYS n 
1 755  TRP n 
1 756  LEU n 
1 757  GLY n 
1 758  PHE n 
1 759  ARG n 
1 760  VAL n 
1 761  PRO n 
1 762  LEU n 
1 763  ALA n 
1 764  ILE n 
1 765  VAL n 
1 766  ASN n 
1 767  LYS n 
1 768  ALA n 
1 769  HIS n 
1 770  GLN n 
1 771  ALA n 
1 772  ASN n 
1 773  GLN n 
1 774  LEU n 
1 775  TYR n 
1 776  PRO n 
1 777  PHE n 
1 778  ALA n 
1 779  ILE n 
1 780  SER n 
1 781  LEU n 
1 782  ILE n 
1 783  GLU n 
1 784  SER n 
1 785  VAL n 
1 786  ARG n 
1 787  THR n 
1 788  TYR n 
1 789  GLU n 
1 790  ARG n 
1 791  THR n 
1 792  CYS n 
1 793  GLU n 
1 794  LYS n 
1 795  VAL n 
1 796  GLU n 
1 797  GLU n 
1 798  ARG n 
1 799  ASN n 
1 800  THR n 
1 801  ILE n 
1 802  SER n 
1 803  LEU n 
1 804  LEU n 
1 805  VAL n 
1 806  ALA n 
1 807  GLY n 
1 808  LEU n 
1 809  LYS n 
1 810  LYS n 
1 811  GLU n 
1 812  VAL n 
1 813  GLN n 
1 814  ALA n 
1 815  LEU n 
1 816  ILE n 
1 817  ALA n 
1 818  GLU n 
1 819  GLY n 
1 820  ILE n 
1 821  ALA n 
1 822  LEU n 
1 823  VAL n 
1 824  TRP n 
1 825  GLU n 
1 826  SER n 
1 827  TYR n 
1 828  LYS n 
1 829  LEU n 
1 830  ASP n 
1 831  PRO n 
1 832  TYR n 
1 833  VAL n 
1 834  GLN n 
1 835  ARG n 
1 836  LEU n 
1 837  ALA n 
1 838  GLU n 
1 839  THR n 
1 840  VAL n 
1 841  PHE n 
1 842  ASN n 
1 843  PHE n 
1 844  GLN n 
1 845  GLU n 
1 846  LYS n 
1 847  VAL n 
1 848  ASP n 
1 849  ASP n 
1 850  LEU n 
1 851  LEU n 
1 852  ILE n 
1 853  ILE n 
1 854  GLU n 
1 855  GLU n 
1 856  LYS n 
1 857  ILE n 
1 858  ASP n 
1 859  LEU n 
1 860  GLU n 
1 861  VAL n 
1 862  ARG n 
1 863  SER n 
1 864  LEU n 
1 865  GLU n 
1 866  THR n 
1 867  CYS n 
1 868  MET n 
1 869  TYR n 
1 870  ASP n 
1 871  HIS n 
1 872  LYS n 
1 873  THR n 
1 874  PHE n 
1 875  SER n 
1 876  GLU n 
1 877  ILE n 
1 878  LEU n 
1 879  ASN n 
1 880  ARG n 
1 881  VAL n 
1 882  GLN n 
1 883  LYS n 
1 884  ALA n 
1 885  VAL n 
1 886  ASP n 
1 887  ASP n 
1 888  LEU n 
1 889  ASN n 
1 890  LEU n 
1 891  HIS n 
1 892  SER n 
1 893  TYR n 
1 894  SER n 
1 895  ASN n 
1 896  LEU n 
1 897  PRO n 
1 898  ILE n 
1 899  TRP n 
1 900  VAL n 
1 901  ASN n 
1 902  LYS n 
1 903  LEU n 
1 904  ASP n 
1 905  MET n 
1 906  GLU n 
1 907  ILE n 
1 908  GLU n 
1 909  ARG n 
1 910  ILE n 
1 911  LEU n 
1 912  GLY n 
1 913  VAL n 
1 914  ARG n 
1 915  LEU n 
1 916  GLN n 
1 917  ALA n 
1 918  GLY n 
1 919  LEU n 
1 920  ARG n 
1 921  ALA n 
1 922  TRP n 
1 923  THR n 
1 924  GLN n 
1 925  VAL n 
1 926  LEU n 
1 927  LEU n 
1 928  GLY n 
1 929  GLN n 
1 930  ALA n 
1 931  GLU n 
1 932  ASP n 
1 933  LYS n 
1 934  ALA n 
1 935  GLU n 
1 936  VAL n 
1 937  ASP n 
1 938  MET n 
1 939  ASP n 
1 940  THR n 
1 941  ASP n 
1 942  ALA n 
1 943  PRO n 
1 944  GLN n 
1 945  VAL n 
1 946  SER n 
1 947  HIS n 
1 948  LYS n 
1 949  PRO n 
1 950  GLY n 
1 951  GLY n 
1 952  GLU n 
1 953  PRO n 
1 954  LYS n 
1 955  ILE n 
1 956  LYS n 
1 957  ASN n 
1 958  VAL n 
1 959  VAL n 
1 960  HIS n 
1 961  GLU n 
1 962  LEU n 
1 963  ARG n 
1 964  ILE n 
1 965  THR n 
1 966  ASN n 
1 967  GLN n 
1 968  VAL n 
1 969  ILE n 
1 970  TYR n 
1 971  LEU n 
1 972  ASN n 
1 973  PRO n 
1 974  PRO n 
1 975  ILE n 
1 976  GLU n 
1 977  GLU n 
1 978  CYS n 
1 979  ARG n 
1 980  TYR n 
1 981  LYS n 
1 982  LEU n 
1 983  TYR n 
1 984  GLN n 
1 985  GLU n 
1 986  MET n 
1 987  PHE n 
1 988  ALA n 
1 989  TRP n 
1 990  LYS n 
1 991  MET n 
1 992  VAL n 
1 993  VAL n 
1 994  LEU n 
1 995  SER n 
1 996  LEU n 
1 997  PRO n 
1 998  ARG n 
1 999  ILE n 
1 1000 GLN n 
1 1001 SER n 
1 1002 GLN n 
1 1003 ARG n 
1 1004 TYR n 
1 1005 GLN n 
1 1006 VAL n 
1 1007 GLY n 
1 1008 VAL n 
1 1009 HIS n 
1 1010 TYR n 
1 1011 GLU n 
1 1012 LEU n 
1 1013 THR n 
1 1014 GLU n 
1 1015 GLU n 
1 1016 GLU n 
1 1017 LYS n 
1 1018 PHE n 
1 1019 TYR n 
1 1020 ARG n 
1 1021 ASN n 
1 1022 ALA n 
1 1023 LEU n 
1 1024 THR n 
1 1025 ARG n 
1 1026 MET n 
1 1027 PRO n 
1 1028 ASP n 
1 1029 GLY n 
1 1030 PRO n 
1 1031 VAL n 
1 1032 ALA n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLU n 
1 1036 SER n 
1 1037 TYR n 
1 1038 SER n 
1 1039 ALA n 
1 1040 VAL n 
1 1041 MET n 
1 1042 GLY n 
1 1043 ILE n 
1 1044 VAL n 
1 1045 SER n 
1 1046 GLU n 
1 1047 VAL n 
1 1048 GLU n 
1 1049 GLN n 
1 1050 TYR n 
1 1051 VAL n 
1 1052 LYS n 
1 1053 VAL n 
1 1054 TRP n 
1 1055 LEU n 
1 1056 GLN n 
1 1057 TYR n 
1 1058 GLN n 
1 1059 CYS n 
1 1060 LEU n 
1 1061 TRP n 
1 1062 ASP n 
1 1063 MET n 
1 1064 GLN n 
1 1065 ALA n 
1 1066 GLU n 
1 1067 ASN n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 ASN n 
1 1071 ARG n 
1 1072 LEU n 
1 1073 GLY n 
1 1074 GLU n 
1 1075 ASP n 
1 1076 LEU n 
1 1077 ASN n 
1 1078 LYS n 
1 1079 TRP n 
1 1080 GLN n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 LEU n 
1 1084 VAL n 
1 1085 GLN n 
1 1086 ILE n 
1 1087 ARG n 
1 1088 LYS n 
1 1089 ALA n 
1 1090 ARG n 
1 1091 GLY n 
1 1092 THR n 
1 1093 PHE n 
1 1094 ASP n 
1 1095 ASN n 
1 1096 ALA n 
1 1097 GLU n 
1 1098 THR n 
1 1099 LYS n 
1 1100 LYS n 
1 1101 GLU n 
1 1102 PHE n 
1 1103 GLY n 
1 1104 PRO n 
1 1105 VAL n 
1 1106 VAL n 
1 1107 ILE n 
1 1108 ASP n 
1 1109 TYR n 
1 1110 GLY n 
1 1111 LYS n 
1 1112 VAL n 
1 1113 GLN n 
1 1114 SER n 
1 1115 LYS n 
1 1116 VAL n 
1 1117 ASN n 
1 1118 LEU n 
1 1119 LYS n 
1 1120 TYR n 
1 1121 ASP n 
1 1122 SER n 
1 1123 TRP n 
1 1124 HIS n 
1 1125 LYS n 
1 1126 GLU n 
1 1127 VAL n 
1 1128 LEU n 
1 1129 SER n 
1 1130 LYS n 
1 1131 PHE n 
1 1132 GLY n 
1 1133 GLN n 
1 1134 MET n 
1 1135 LEU n 
1 1136 GLY n 
1 1137 SER n 
1 1138 ASN n 
1 1139 MET n 
1 1140 THR n 
1 1141 GLU n 
1 1142 PHE n 
1 1143 HIS n 
1 1144 SER n 
1 1145 GLN n 
1 1146 ILE n 
1 1147 SER n 
1 1148 LYS n 
1 1149 SER n 
1 1150 ARG n 
1 1151 GLN n 
1 1152 GLU n 
1 1153 LEU n 
1 1154 GLU n 
1 1155 GLN n 
1 1156 HIS n 
1 1157 SER n 
1 1158 VAL n 
1 1159 ASP n 
1 1160 THR n 
1 1161 ALA n 
1 1162 SER n 
1 1163 THR n 
1 1164 SER n 
1 1165 ASP n 
1 1166 ALA n 
1 1167 VAL n 
1 1168 THR n 
1 1169 PHE n 
1 1170 ILE n 
1 1171 THR n 
1 1172 TYR n 
1 1173 VAL n 
1 1174 GLN n 
1 1175 SER n 
1 1176 LEU n 
1 1177 LYS n 
1 1178 ARG n 
1 1179 LYS n 
1 1180 ILE n 
1 1181 LYS n 
1 1182 GLN n 
1 1183 PHE n 
1 1184 GLU n 
1 1185 LYS n 
1 1186 GLN n 
1 1187 VAL n 
1 1188 GLU n 
1 1189 LEU n 
1 1190 TYR n 
1 1191 ARG n 
1 1192 ASN n 
1 1193 GLY n 
1 1194 GLN n 
1 1195 ARG n 
1 1196 LEU n 
1 1197 LEU n 
1 1198 GLU n 
1 1199 LYS n 
1 1200 GLN n 
1 1201 ARG n 
1 1202 PHE n 
1 1203 GLN n 
1 1204 PHE n 
1 1205 PRO n 
1 1206 PRO n 
1 1207 SER n 
1 1208 TRP n 
1 1209 LEU n 
1 1210 TYR n 
1 1211 ILE n 
1 1212 ASP n 
1 1213 ASN n 
1 1214 ILE n 
1 1215 GLU n 
1 1216 GLY n 
1 1217 GLU n 
1 1218 TRP n 
1 1219 GLY n 
1 1220 ALA n 
1 1221 PHE n 
1 1222 ASN n 
1 1223 ASP n 
1 1224 ILE n 
1 1225 MET n 
1 1226 ARG n 
1 1227 ARG n 
1 1228 LYS n 
1 1229 ASP n 
1 1230 SER n 
1 1231 ALA n 
1 1232 ILE n 
1 1233 GLN n 
1 1234 GLN n 
1 1235 GLN n 
1 1236 VAL n 
1 1237 ALA n 
1 1238 ASN n 
1 1239 LEU n 
1 1240 GLN n 
1 1241 MET n 
1 1242 LYS n 
1 1243 ILE n 
1 1244 VAL n 
1 1245 GLN n 
1 1246 GLU n 
1 1247 ASP n 
1 1248 ARG n 
1 1249 ALA n 
1 1250 VAL n 
1 1251 GLU n 
1 1252 SER n 
1 1253 ARG n 
1 1254 THR n 
1 1255 THR n 
1 1256 ASP n 
1 1257 LEU n 
1 1258 LEU n 
1 1259 THR n 
1 1260 ASP n 
1 1261 TRP n 
1 1262 GLU n 
1 1263 LYS n 
1 1264 THR n 
1 1265 LYS n 
1 1266 PRO n 
1 1267 VAL n 
1 1268 THR n 
1 1269 GLY n 
1 1270 ASN n 
1 1271 LEU n 
1 1272 ARG n 
1 1273 PRO n 
1 1274 GLU n 
1 1275 GLU n 
1 1276 ALA n 
1 1277 LEU n 
1 1278 GLN n 
1 1279 ALA n 
1 1280 LEU n 
1 1281 THR n 
1 1282 ILE n 
1 1283 TYR n 
1 1284 GLU n 
1 1285 GLY n 
1 1286 LYS n 
1 1287 PHE n 
1 1288 GLY n 
1 1289 ARG n 
1 1290 LEU n 
1 1291 LYS n 
1 1292 ASP n 
1 1293 ASP n 
1 1294 ARG n 
1 1295 GLU n 
1 1296 LYS n 
1 1297 CYS n 
1 1298 ALA n 
1 1299 LYS n 
1 1300 ALA n 
1 1301 LYS n 
1 1302 GLU n 
1 1303 ALA n 
1 1304 LEU n 
1 1305 GLU n 
1 1306 LEU n 
1 1307 THR n 
1 1308 ASP n 
1 1309 THR n 
1 1310 GLY n 
1 1311 LEU n 
1 1312 LEU n 
1 1313 SER n 
1 1314 GLY n 
1 1315 SER n 
1 1316 GLU n 
1 1317 GLU n 
1 1318 ARG n 
1 1319 VAL n 
1 1320 GLN n 
1 1321 VAL n 
1 1322 ALA n 
1 1323 LEU n 
1 1324 GLU n 
1 1325 GLU n 
1 1326 LEU n 
1 1327 GLN n 
1 1328 ASP n 
1 1329 LEU n 
1 1330 LYS n 
1 1331 GLY n 
1 1332 VAL n 
1 1333 TRP n 
1 1334 SER n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 SER n 
1 1338 LYS n 
1 1339 VAL n 
1 1340 TRP n 
1 1341 GLU n 
1 1342 GLN n 
1 1343 ILE n 
1 1344 ASP n 
1 1345 GLN n 
1 1346 MET n 
1 1347 LYS n 
1 1348 GLU n 
1 1349 GLN n 
1 1350 PRO n 
1 1351 TRP n 
1 1352 VAL n 
1 1353 SER n 
1 1354 VAL n 
1 1355 GLN n 
1 1356 PRO n 
1 1357 ARG n 
1 1358 LYS n 
1 1359 LEU n 
1 1360 ARG n 
1 1361 GLN n 
1 1362 ASN n 
1 1363 LEU n 
1 1364 ASP n 
1 1365 ALA n 
1 1366 LEU n 
1 1367 LEU n 
1 1368 ASN n 
1 1369 GLN n 
1 1370 LEU n 
1 1371 LYS n 
1 1372 SER n 
1 1373 PHE n 
1 1374 PRO n 
1 1375 ALA n 
1 1376 ARG n 
1 1377 LEU n 
1 1378 ARG n 
1 1379 GLN n 
1 1380 TYR n 
1 1381 ALA n 
1 1382 SER n 
1 1383 TYR n 
1 1384 GLU n 
1 1385 PHE n 
1 1386 VAL n 
1 1387 GLN n 
1 1388 ARG n 
1 1389 LEU n 
1 1390 LEU n 
1 1391 LYS n 
1 1392 GLY n 
1 1393 TYR n 
1 1394 MET n 
1 1395 LYS n 
1 1396 ILE n 
1 1397 ASN n 
1 1398 MET n 
1 1399 LEU n 
1 1400 VAL n 
1 1401 ILE n 
1 1402 GLU n 
1 1403 LEU n 
1 1404 LYS n 
1 1405 SER n 
1 1406 GLU n 
1 1407 ALA n 
1 1408 LEU n 
1 1409 LYS n 
1 1410 ASP n 
1 1411 ARG n 
1 1412 HIS n 
1 1413 TRP n 
1 1414 LYS n 
1 1415 GLN n 
1 1416 LEU n 
1 1417 MET n 
1 1418 LYS n 
1 1419 ARG n 
1 1420 LEU n 
1 1421 HIS n 
1 1422 VAL n 
1 1423 ASN n 
1 1424 TRP n 
1 1425 VAL n 
1 1426 VAL n 
1 1427 SER n 
1 1428 GLU n 
1 1429 LEU n 
1 1430 THR n 
1 1431 LEU n 
1 1432 GLY n 
1 1433 GLN n 
1 1434 ILE n 
1 1435 TRP n 
1 1436 ASP n 
1 1437 VAL n 
1 1438 ASP n 
1 1439 LEU n 
1 1440 GLN n 
1 1441 LYS n 
1 1442 ASN n 
1 1443 GLU n 
1 1444 ALA n 
1 1445 ILE n 
1 1446 VAL n 
1 1447 LYS n 
1 1448 ASP n 
1 1449 VAL n 
1 1450 LEU n 
1 1451 LEU n 
1 1452 VAL n 
1 1453 ALA n 
1 1454 GLN n 
1 1455 GLY n 
1 1456 GLU n 
1 1457 MET n 
1 1458 ALA n 
1 1459 LEU n 
1 1460 GLU n 
1 1461 GLU n 
1 1462 PHE n 
1 1463 LEU n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 ARG n 
1 1468 GLU n 
1 1469 VAL n 
1 1470 TRP n 
1 1471 ASN n 
1 1472 THR n 
1 1473 TYR n 
1 1474 GLU n 
1 1475 LEU n 
1 1476 ASP n 
1 1477 LEU n 
1 1478 VAL n 
1 1479 ASN n 
1 1480 TYR n 
1 1481 GLN n 
1 1482 ASN n 
1 1483 LYS n 
1 1484 CYS n 
1 1485 ARG n 
1 1486 LEU n 
1 1487 ILE n 
1 1488 ARG n 
1 1489 GLY n 
1 1490 TRP n 
1 1491 ASP n 
1 1492 ASP n 
1 1493 LEU n 
1 1494 PHE n 
1 1495 ASN n 
1 1496 LYS n 
1 1497 VAL n 
1 1498 LYS n 
1 1499 GLU n 
1 1500 HIS n 
1 1501 ILE n 
1 1502 ASN n 
1 1503 SER n 
1 1504 VAL n 
1 1505 SER n 
1 1506 ALA n 
1 1507 MET n 
1 1508 LYS n 
1 1509 LEU n 
1 1510 SER n 
1 1511 PRO n 
1 1512 TYR n 
1 1513 TYR n 
1 1514 LYS n 
1 1515 VAL n 
1 1516 PHE n 
1 1517 GLU n 
1 1518 GLU n 
1 1519 ASP n 
1 1520 ALA n 
1 1521 LEU n 
1 1522 SER n 
1 1523 TRP n 
1 1524 GLU n 
1 1525 ASP n 
1 1526 LYS n 
1 1527 LEU n 
1 1528 ASN n 
1 1529 ARG n 
1 1530 ILE n 
1 1531 MET n 
1 1532 ALA n 
1 1533 LEU n 
1 1534 PHE n 
1 1535 ASP n 
1 1536 VAL n 
1 1537 TRP n 
1 1538 ILE n 
1 1539 ASP n 
1 1540 VAL n 
1 1541 GLN n 
1 1542 ARG n 
1 1543 ARG n 
1 1544 TRP n 
1 1545 VAL n 
1 1546 TYR n 
1 1547 LEU n 
1 1548 GLU n 
1 1549 GLY n 
1 1550 ILE n 
1 1551 PHE n 
1 1552 THR n 
1 1553 GLY n 
1 1554 SER n 
1 1555 ALA n 
1 1556 ASP n 
1 1557 ILE n 
1 1558 LYS n 
1 1559 HIS n 
1 1560 LEU n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 VAL n 
1 1564 GLU n 
1 1565 THR n 
1 1566 GLN n 
1 1567 ARG n 
1 1568 PHE n 
1 1569 GLN n 
1 1570 SER n 
1 1571 ILE n 
1 1572 SER n 
1 1573 THR n 
1 1574 GLU n 
1 1575 PHE n 
1 1576 LEU n 
1 1577 ALA n 
1 1578 LEU n 
1 1579 MET n 
1 1580 LYS n 
1 1581 LYS n 
1 1582 VAL n 
1 1583 SER n 
1 1584 LYS n 
1 1585 SER n 
1 1586 PRO n 
1 1587 LEU n 
1 1588 VAL n 
1 1589 MET n 
1 1590 ASP n 
1 1591 VAL n 
1 1592 LEU n 
1 1593 ASN n 
1 1594 ILE n 
1 1595 GLN n 
1 1596 GLY n 
1 1597 VAL n 
1 1598 GLN n 
1 1599 ARG n 
1 1600 SER n 
1 1601 LEU n 
1 1602 GLU n 
1 1603 ARG n 
1 1604 LEU n 
1 1605 ALA n 
1 1606 ASP n 
1 1607 LEU n 
1 1608 LEU n 
1 1609 GLY n 
1 1610 LYS n 
1 1611 ILE n 
1 1612 GLN n 
1 1613 LYS n 
1 1614 ALA n 
1 1615 LEU n 
1 1616 GLY n 
1 1617 GLU n 
1 1618 TYR n 
1 1619 LEU n 
1 1620 GLU n 
1 1621 ARG n 
1 1622 GLU n 
1 1623 ARG n 
1 1624 SER n 
1 1625 SER n 
1 1626 PHE n 
1 1627 PRO n 
1 1628 ARG n 
1 1629 PHE n 
1 1630 TYR n 
1 1631 PHE n 
1 1632 VAL n 
1 1633 GLY n 
1 1634 ASP n 
1 1635 GLU n 
1 1636 ASP n 
1 1637 LEU n 
1 1638 LEU n 
1 1639 GLU n 
1 1640 ILE n 
1 1641 ILE n 
1 1642 GLY n 
1 1643 ASN n 
1 1644 SER n 
1 1645 LYS n 
1 1646 ASN n 
1 1647 VAL n 
1 1648 ALA n 
1 1649 LYS n 
1 1650 LEU n 
1 1651 GLN n 
1 1652 LYS n 
1 1653 HIS n 
1 1654 PHE n 
1 1655 LYS n 
1 1656 LYS n 
1 1657 MET n 
1 1658 PHE n 
1 1659 ALA n 
1 1660 GLY n 
1 1661 VAL n 
1 1662 SER n 
1 1663 SER n 
1 1664 ILE n 
1 1665 ILE n 
1 1666 LEU n 
1 1667 ASN n 
1 1668 GLU n 
1 1669 ASP n 
1 1670 ASN n 
1 1671 SER n 
1 1672 VAL n 
1 1673 VAL n 
1 1674 LEU n 
1 1675 GLY n 
1 1676 ILE n 
1 1677 SER n 
1 1678 SER n 
1 1679 ARG n 
1 1680 GLU n 
1 1681 GLY n 
1 1682 GLU n 
1 1683 GLU n 
1 1684 VAL n 
1 1685 MET n 
1 1686 PHE n 
1 1687 LYS n 
1 1688 THR n 
1 1689 PRO n 
1 1690 VAL n 
1 1691 SER n 
1 1692 ILE n 
1 1693 THR n 
1 1694 GLU n 
1 1695 HIS n 
1 1696 PRO n 
1 1697 LYS n 
1 1698 ILE n 
1 1699 ASN n 
1 1700 GLU n 
1 1701 TRP n 
1 1702 LEU n 
1 1703 THR n 
1 1704 LEU n 
1 1705 VAL n 
1 1706 GLU n 
1 1707 LYS n 
1 1708 GLU n 
1 1709 MET n 
1 1710 ARG n 
1 1711 VAL n 
1 1712 THR n 
1 1713 LEU n 
1 1714 ALA n 
1 1715 LYS n 
1 1716 LEU n 
1 1717 LEU n 
1 1718 ALA n 
1 1719 GLU n 
1 1720 SER n 
1 1721 VAL n 
1 1722 THR n 
1 1723 GLU n 
1 1724 VAL n 
1 1725 GLU n 
1 1726 ILE n 
1 1727 PHE n 
1 1728 GLY n 
1 1729 LYS n 
1 1730 ALA n 
1 1731 THR n 
1 1732 SER n 
1 1733 ILE n 
1 1734 ASP n 
1 1735 PRO n 
1 1736 ASN n 
1 1737 THR n 
1 1738 TYR n 
1 1739 ILE n 
1 1740 THR n 
1 1741 TRP n 
1 1742 ILE n 
1 1743 ASP n 
1 1744 LYS n 
1 1745 TYR n 
1 1746 GLN n 
1 1747 ALA n 
1 1748 GLN n 
1 1749 LEU n 
1 1750 VAL n 
1 1751 VAL n 
1 1752 LEU n 
1 1753 SER n 
1 1754 ALA n 
1 1755 GLN n 
1 1756 ILE n 
1 1757 ALA n 
1 1758 TRP n 
1 1759 SER n 
1 1760 GLU n 
1 1761 ASN n 
1 1762 VAL n 
1 1763 GLU n 
1 1764 THR n 
1 1765 ALA n 
1 1766 LEU n 
1 1767 SER n 
1 1768 SER n 
1 1769 MET n 
1 1770 GLY n 
1 1771 GLY n 
1 1772 GLY n 
1 1773 GLY n 
1 1774 ASP n 
1 1775 ALA n 
1 1776 ALA n 
1 1777 PRO n 
1 1778 LEU n 
1 1779 HIS n 
1 1780 SER n 
1 1781 VAL n 
1 1782 LEU n 
1 1783 SER n 
1 1784 ASN n 
1 1785 VAL n 
1 1786 GLU n 
1 1787 VAL n 
1 1788 THR n 
1 1789 LEU n 
1 1790 ASN n 
1 1791 VAL n 
1 1792 LEU n 
1 1793 ALA n 
1 1794 ASP n 
1 1795 SER n 
1 1796 VAL n 
1 1797 LEU n 
1 1798 MET n 
1 1799 GLU n 
1 1800 GLN n 
1 1801 PRO n 
1 1802 PRO n 
1 1803 LEU n 
1 1804 ARG n 
1 1805 ARG n 
1 1806 ARG n 
1 1807 LYS n 
1 1808 LEU n 
1 1809 GLU n 
1 1810 HIS n 
1 1811 LEU n 
1 1812 ILE n 
1 1813 THR n 
1 1814 GLU n 
1 1815 LEU n 
1 1816 VAL n 
1 1817 HIS n 
1 1818 GLN n 
1 1819 ARG n 
1 1820 ASP n 
1 1821 VAL n 
1 1822 THR n 
1 1823 ARG n 
1 1824 SER n 
1 1825 LEU n 
1 1826 ILE n 
1 1827 LYS n 
1 1828 SER n 
1 1829 LYS n 
1 1830 ILE n 
1 1831 ASP n 
1 1832 ASN n 
1 1833 ALA n 
1 1834 LYS n 
1 1835 SER n 
1 1836 PHE n 
1 1837 GLU n 
1 1838 TRP n 
1 1839 LEU n 
1 1840 SER n 
1 1841 GLN n 
1 1842 MET n 
1 1843 ARG n 
1 1844 PHE n 
1 1845 TYR n 
1 1846 PHE n 
1 1847 ASP n 
1 1848 PRO n 
1 1849 LYS n 
1 1850 GLN n 
1 1851 THR n 
1 1852 ASP n 
1 1853 VAL n 
1 1854 LEU n 
1 1855 GLN n 
1 1856 GLN n 
1 1857 LEU n 
1 1858 SER n 
1 1859 ILE n 
1 1860 GLN n 
1 1861 MET n 
1 1862 ALA n 
1 1863 ASN n 
1 1864 ALA n 
1 1865 LYS n 
1 1866 PHE n 
1 1867 ASN n 
1 1868 TYR n 
1 1869 GLY n 
1 1870 PHE n 
1 1871 GLU n 
1 1872 TYR n 
1 1873 LEU n 
1 1874 GLY n 
1 1875 VAL n 
1 1876 GLN n 
1 1877 ASP n 
1 1878 LYS n 
1 1879 LEU n 
1 1880 VAL n 
1 1881 GLN n 
1 1882 THR n 
1 1883 PRO n 
1 1884 LEU n 
1 1885 THR n 
1 1886 ASP n 
1 1887 ARG n 
1 1888 CYS n 
1 1889 TYR n 
1 1890 LEU n 
1 1891 THR n 
1 1892 MET n 
1 1893 THR n 
1 1894 GLN n 
1 1895 ALA n 
1 1896 LEU n 
1 1897 GLU n 
1 1898 ALA n 
1 1899 ARG n 
1 1900 LEU n 
1 1901 GLY n 
1 1902 GLY n 
1 1903 SER n 
1 1904 PRO n 
1 1905 PHE n 
1 1906 GLY n 
1 1907 PRO n 
1 1908 ALA n 
1 1909 GLY n 
1 1910 THR n 
1 1911 GLY n 
1 1912 LYS n 
1 1913 THR n 
1 1914 GLU n 
1 1915 SER n 
1 1916 VAL n 
1 1917 LYS n 
1 1918 ALA n 
1 1919 LEU n 
1 1920 GLY n 
1 1921 HIS n 
1 1922 GLN n 
1 1923 LEU n 
1 1924 GLY n 
1 1925 ARG n 
1 1926 PHE n 
1 1927 VAL n 
1 1928 LEU n 
1 1929 VAL n 
1 1930 PHE n 
1 1931 ASN n 
1 1932 CYS n 
1 1933 ASP n 
1 1934 GLU n 
1 1935 THR n 
1 1936 PHE n 
1 1937 ASP n 
1 1938 PHE n 
1 1939 GLN n 
1 1940 ALA n 
1 1941 MET n 
1 1942 GLY n 
1 1943 ARG n 
1 1944 ILE n 
1 1945 PHE n 
1 1946 VAL n 
1 1947 GLY n 
1 1948 LEU n 
1 1949 CYS n 
1 1950 GLN n 
1 1951 VAL n 
1 1952 GLY n 
1 1953 ALA n 
1 1954 TRP n 
1 1955 GLY n 
1 1956 CYS n 
1 1957 PHE n 
1 1958 ASP n 
1 1959 GLU n 
1 1960 PHE n 
1 1961 ASN n 
1 1962 ARG n 
1 1963 LEU n 
1 1964 GLU n 
1 1965 GLU n 
1 1966 ARG n 
1 1967 MET n 
1 1968 LEU n 
1 1969 SER n 
1 1970 ALA n 
1 1971 VAL n 
1 1972 SER n 
1 1973 GLN n 
1 1974 GLN n 
1 1975 VAL n 
1 1976 GLN n 
1 1977 CYS n 
1 1978 ILE n 
1 1979 GLN n 
1 1980 GLU n 
1 1981 ALA n 
1 1982 LEU n 
1 1983 ARG n 
1 1984 GLU n 
1 1985 HIS n 
1 1986 SER n 
1 1987 ASN n 
1 1988 PRO n 
1 1989 ASN n 
1 1990 TYR n 
1 1991 ASP n 
1 1992 LYS n 
1 1993 THR n 
1 1994 SER n 
1 1995 ALA n 
1 1996 PRO n 
1 1997 ILE n 
1 1998 THR n 
1 1999 CYS n 
1 2000 GLU n 
1 2001 LEU n 
1 2002 LEU n 
1 2003 ASN n 
1 2004 LYS n 
1 2005 GLN n 
1 2006 VAL n 
1 2007 LYS n 
1 2008 VAL n 
1 2009 SER n 
1 2010 PRO n 
1 2011 ASP n 
1 2012 MET n 
1 2013 ALA n 
1 2014 ILE n 
1 2015 PHE n 
1 2016 ILE n 
1 2017 THR n 
1 2018 MET n 
1 2019 ASN n 
1 2020 PRO n 
1 2021 GLY n 
1 2022 TYR n 
1 2023 ALA n 
1 2024 GLY n 
1 2025 ARG n 
1 2026 SER n 
1 2027 ASN n 
1 2028 LEU n 
1 2029 PRO n 
1 2030 ASP n 
1 2031 ASN n 
1 2032 LEU n 
1 2033 LYS n 
1 2034 LYS n 
1 2035 LEU n 
1 2036 PHE n 
1 2037 ARG n 
1 2038 SER n 
1 2039 LEU n 
1 2040 ALA n 
1 2041 MET n 
1 2042 THR n 
1 2043 LYS n 
1 2044 PRO n 
1 2045 ASP n 
1 2046 ARG n 
1 2047 GLN n 
1 2048 LEU n 
1 2049 ILE n 
1 2050 ALA n 
1 2051 GLN n 
1 2052 VAL n 
1 2053 MET n 
1 2054 LEU n 
1 2055 TYR n 
1 2056 SER n 
1 2057 GLN n 
1 2058 GLY n 
1 2059 PHE n 
1 2060 ARG n 
1 2061 THR n 
1 2062 ALA n 
1 2063 GLU n 
1 2064 VAL n 
1 2065 LEU n 
1 2066 ALA n 
1 2067 ASN n 
1 2068 LYS n 
1 2069 ILE n 
1 2070 VAL n 
1 2071 PRO n 
1 2072 PHE n 
1 2073 PHE n 
1 2074 LYS n 
1 2075 LEU n 
1 2076 CYS n 
1 2077 ASP n 
1 2078 GLU n 
1 2079 GLN n 
1 2080 LEU n 
1 2081 SER n 
1 2082 SER n 
1 2083 GLN n 
1 2084 SER n 
1 2085 HIS n 
1 2086 TYR n 
1 2087 ASP n 
1 2088 PHE n 
1 2089 GLY n 
1 2090 LEU n 
1 2091 ARG n 
1 2092 ALA n 
1 2093 LEU n 
1 2094 LYS n 
1 2095 SER n 
1 2096 VAL n 
1 2097 LEU n 
1 2098 VAL n 
1 2099 SER n 
1 2100 ALA n 
1 2101 GLY n 
1 2102 ASN n 
1 2103 VAL n 
1 2104 LYS n 
1 2105 ARG n 
1 2106 GLU n 
1 2107 ARG n 
1 2108 ILE n 
1 2109 GLN n 
1 2110 LYS n 
1 2111 ILE n 
1 2112 LYS n 
1 2113 ARG n 
1 2114 GLU n 
1 2115 LYS n 
1 2116 GLU n 
1 2117 GLU n 
1 2118 ARG n 
1 2119 GLY n 
1 2120 GLU n 
1 2121 ALA n 
1 2122 VAL n 
1 2123 ASP n 
1 2124 GLU n 
1 2125 GLY n 
1 2126 GLU n 
1 2127 ILE n 
1 2128 ALA n 
1 2129 GLU n 
1 2130 ASN n 
1 2131 LEU n 
1 2132 PRO n 
1 2133 GLU n 
1 2134 GLN n 
1 2135 GLU n 
1 2136 ILE n 
1 2137 LEU n 
1 2138 ILE n 
1 2139 GLN n 
1 2140 SER n 
1 2141 VAL n 
1 2142 CYS n 
1 2143 GLU n 
1 2144 THR n 
1 2145 MET n 
1 2146 VAL n 
1 2147 PRO n 
1 2148 LYS n 
1 2149 LEU n 
1 2150 VAL n 
1 2151 ALA n 
1 2152 GLU n 
1 2153 ASP n 
1 2154 ILE n 
1 2155 PRO n 
1 2156 LEU n 
1 2157 LEU n 
1 2158 PHE n 
1 2159 SER n 
1 2160 LEU n 
1 2161 LEU n 
1 2162 SER n 
1 2163 ASP n 
1 2164 VAL n 
1 2165 PHE n 
1 2166 PRO n 
1 2167 GLY n 
1 2168 VAL n 
1 2169 GLN n 
1 2170 TYR n 
1 2171 HIS n 
1 2172 ARG n 
1 2173 GLY n 
1 2174 GLU n 
1 2175 MET n 
1 2176 THR n 
1 2177 ALA n 
1 2178 LEU n 
1 2179 ARG n 
1 2180 GLU n 
1 2181 GLU n 
1 2182 LEU n 
1 2183 LYS n 
1 2184 LYS n 
1 2185 VAL n 
1 2186 CYS n 
1 2187 GLN n 
1 2188 GLU n 
1 2189 MET n 
1 2190 TYR n 
1 2191 LEU n 
1 2192 THR n 
1 2193 TYR n 
1 2194 GLY n 
1 2195 ASP n 
1 2196 GLY n 
1 2197 GLU n 
1 2198 GLU n 
1 2199 VAL n 
1 2200 GLY n 
1 2201 GLY n 
1 2202 MET n 
1 2203 TRP n 
1 2204 VAL n 
1 2205 GLU n 
1 2206 LYS n 
1 2207 VAL n 
1 2208 LEU n 
1 2209 GLN n 
1 2210 LEU n 
1 2211 TYR n 
1 2212 GLN n 
1 2213 ILE n 
1 2214 THR n 
1 2215 GLN n 
1 2216 ILE n 
1 2217 ASN n 
1 2218 HIS n 
1 2219 GLY n 
1 2220 LEU n 
1 2221 MET n 
1 2222 MET n 
1 2223 VAL n 
1 2224 GLY n 
1 2225 PRO n 
1 2226 SER n 
1 2227 GLY n 
1 2228 SER n 
1 2229 GLY n 
1 2230 LYS n 
1 2231 SER n 
1 2232 MET n 
1 2233 ALA n 
1 2234 TRP n 
1 2235 ARG n 
1 2236 VAL n 
1 2237 LEU n 
1 2238 LEU n 
1 2239 LYS n 
1 2240 ALA n 
1 2241 LEU n 
1 2242 GLU n 
1 2243 ARG n 
1 2244 LEU n 
1 2245 GLU n 
1 2246 GLY n 
1 2247 VAL n 
1 2248 GLU n 
1 2249 GLY n 
1 2250 VAL n 
1 2251 ALA n 
1 2252 HIS n 
1 2253 ILE n 
1 2254 ILE n 
1 2255 ASP n 
1 2256 PRO n 
1 2257 LYS n 
1 2258 ALA n 
1 2259 ILE n 
1 2260 SER n 
1 2261 LYS n 
1 2262 ASP n 
1 2263 HIS n 
1 2264 LEU n 
1 2265 TYR n 
1 2266 GLY n 
1 2267 THR n 
1 2268 LEU n 
1 2269 ASP n 
1 2270 PRO n 
1 2271 ASN n 
1 2272 THR n 
1 2273 ARG n 
1 2274 GLU n 
1 2275 TRP n 
1 2276 THR n 
1 2277 ASP n 
1 2278 GLY n 
1 2279 LEU n 
1 2280 PHE n 
1 2281 THR n 
1 2282 HIS n 
1 2283 VAL n 
1 2284 LEU n 
1 2285 ARG n 
1 2286 LYS n 
1 2287 ILE n 
1 2288 ILE n 
1 2289 ASP n 
1 2290 SER n 
1 2291 VAL n 
1 2292 ARG n 
1 2293 GLY n 
1 2294 GLU n 
1 2295 LEU n 
1 2296 GLN n 
1 2297 LYS n 
1 2298 ARG n 
1 2299 GLN n 
1 2300 TRP n 
1 2301 ILE n 
1 2302 VAL n 
1 2303 PHE n 
1 2304 ASP n 
1 2305 GLY n 
1 2306 ASP n 
1 2307 VAL n 
1 2308 ASP n 
1 2309 PRO n 
1 2310 GLU n 
1 2311 TRP n 
1 2312 VAL n 
1 2313 GLU n 
1 2314 ASN n 
1 2315 LEU n 
1 2316 ASN n 
1 2317 SER n 
1 2318 VAL n 
1 2319 LEU n 
1 2320 ASP n 
1 2321 ASP n 
1 2322 ASN n 
1 2323 LYS n 
1 2324 LEU n 
1 2325 LEU n 
1 2326 THR n 
1 2327 LEU n 
1 2328 PRO n 
1 2329 ASN n 
1 2330 GLY n 
1 2331 GLU n 
1 2332 ARG n 
1 2333 LEU n 
1 2334 SER n 
1 2335 LEU n 
1 2336 PRO n 
1 2337 PRO n 
1 2338 ASN n 
1 2339 VAL n 
1 2340 ARG n 
1 2341 ILE n 
1 2342 MET n 
1 2343 PHE n 
1 2344 GLU n 
1 2345 VAL n 
1 2346 GLN n 
1 2347 ASP n 
1 2348 LEU n 
1 2349 LYS n 
1 2350 TYR n 
1 2351 ALA n 
1 2352 THR n 
1 2353 LEU n 
1 2354 ALA n 
1 2355 THR n 
1 2356 VAL n 
1 2357 SER n 
1 2358 ARG n 
1 2359 CYS n 
1 2360 GLY n 
1 2361 MET n 
1 2362 VAL n 
1 2363 TRP n 
1 2364 PHE n 
1 2365 SER n 
1 2366 GLU n 
1 2367 ASP n 
1 2368 VAL n 
1 2369 LEU n 
1 2370 SER n 
1 2371 THR n 
1 2372 ASP n 
1 2373 MET n 
1 2374 ILE n 
1 2375 PHE n 
1 2376 ASN n 
1 2377 ASN n 
1 2378 PHE n 
1 2379 LEU n 
1 2380 ALA n 
1 2381 ARG n 
1 2382 LEU n 
1 2383 ARG n 
1 2384 SER n 
1 2385 ILE n 
1 2386 PRO n 
1 2387 LEU n 
1 2388 ASP n 
1 2389 GLU n 
1 2390 GLY n 
1 2391 GLU n 
1 2392 ASP n 
1 2393 GLU n 
1 2394 ALA n 
1 2395 GLN n 
1 2396 ARG n 
1 2397 ARG n 
1 2398 ARG n 
1 2399 LYS n 
1 2400 GLY n 
1 2401 LYS n 
1 2402 GLU n 
1 2403 ASP n 
1 2404 GLU n 
1 2405 GLY n 
1 2406 GLU n 
1 2407 GLU n 
1 2408 ALA n 
1 2409 ALA n 
1 2410 SER n 
1 2411 PRO n 
1 2412 MET n 
1 2413 LEU n 
1 2414 GLN n 
1 2415 ILE n 
1 2416 GLN n 
1 2417 ARG n 
1 2418 ASP n 
1 2419 ALA n 
1 2420 ALA n 
1 2421 THR n 
1 2422 ILE n 
1 2423 MET n 
1 2424 GLN n 
1 2425 PRO n 
1 2426 TYR n 
1 2427 PHE n 
1 2428 THR n 
1 2429 SER n 
1 2430 ASN n 
1 2431 GLY n 
1 2432 LEU n 
1 2433 VAL n 
1 2434 THR n 
1 2435 LYS n 
1 2436 ALA n 
1 2437 LEU n 
1 2438 GLU n 
1 2439 HIS n 
1 2440 ALA n 
1 2441 PHE n 
1 2442 GLN n 
1 2443 LEU n 
1 2444 GLU n 
1 2445 HIS n 
1 2446 ILE n 
1 2447 MET n 
1 2448 ASP n 
1 2449 LEU n 
1 2450 THR n 
1 2451 ARG n 
1 2452 LEU n 
1 2453 ARG n 
1 2454 CYS n 
1 2455 LEU n 
1 2456 GLY n 
1 2457 SER n 
1 2458 LEU n 
1 2459 PHE n 
1 2460 SER n 
1 2461 MET n 
1 2462 LEU n 
1 2463 HIS n 
1 2464 GLN n 
1 2465 ALA n 
1 2466 CYS n 
1 2467 ARG n 
1 2468 ASN n 
1 2469 VAL n 
1 2470 ALA n 
1 2471 GLN n 
1 2472 TYR n 
1 2473 ASN n 
1 2474 ALA n 
1 2475 ASN n 
1 2476 HIS n 
1 2477 PRO n 
1 2478 ASP n 
1 2479 PHE n 
1 2480 PRO n 
1 2481 MET n 
1 2482 GLN n 
1 2483 ILE n 
1 2484 GLU n 
1 2485 GLN n 
1 2486 LEU n 
1 2487 GLU n 
1 2488 ARG n 
1 2489 TYR n 
1 2490 ILE n 
1 2491 GLN n 
1 2492 ARG n 
1 2493 TYR n 
1 2494 LEU n 
1 2495 VAL n 
1 2496 TYR n 
1 2497 ALA n 
1 2498 ILE n 
1 2499 LEU n 
1 2500 TRP n 
1 2501 SER n 
1 2502 LEU n 
1 2503 SER n 
1 2504 GLY n 
1 2505 ASP n 
1 2506 SER n 
1 2507 ARG n 
1 2508 LEU n 
1 2509 LYS n 
1 2510 MET n 
1 2511 ARG n 
1 2512 ALA n 
1 2513 GLU n 
1 2514 LEU n 
1 2515 GLY n 
1 2516 GLU n 
1 2517 TYR n 
1 2518 ILE n 
1 2519 ARG n 
1 2520 ARG n 
1 2521 ILE n 
1 2522 THR n 
1 2523 THR n 
1 2524 VAL n 
1 2525 PRO n 
1 2526 LEU n 
1 2527 PRO n 
1 2528 THR n 
1 2529 ALA n 
1 2530 PRO n 
1 2531 ASN n 
1 2532 ILE n 
1 2533 PRO n 
1 2534 ILE n 
1 2535 ILE n 
1 2536 ASP n 
1 2537 TYR n 
1 2538 GLU n 
1 2539 VAL n 
1 2540 SER n 
1 2541 ILE n 
1 2542 SER n 
1 2543 GLY n 
1 2544 GLU n 
1 2545 TRP n 
1 2546 SER n 
1 2547 PRO n 
1 2548 TRP n 
1 2549 GLN n 
1 2550 ALA n 
1 2551 LYS n 
1 2552 VAL n 
1 2553 PRO n 
1 2554 GLN n 
1 2555 ILE n 
1 2556 GLU n 
1 2557 VAL n 
1 2558 GLU n 
1 2559 THR n 
1 2560 HIS n 
1 2561 LYS n 
1 2562 VAL n 
1 2563 ALA n 
1 2564 ALA n 
1 2565 PRO n 
1 2566 ASP n 
1 2567 VAL n 
1 2568 VAL n 
1 2569 VAL n 
1 2570 PRO n 
1 2571 THR n 
1 2572 LEU n 
1 2573 ASP n 
1 2574 THR n 
1 2575 VAL n 
1 2576 ARG n 
1 2577 HIS n 
1 2578 GLU n 
1 2579 ALA n 
1 2580 LEU n 
1 2581 LEU n 
1 2582 TYR n 
1 2583 THR n 
1 2584 TRP n 
1 2585 LEU n 
1 2586 ALA n 
1 2587 GLU n 
1 2588 HIS n 
1 2589 LYS n 
1 2590 PRO n 
1 2591 LEU n 
1 2592 VAL n 
1 2593 LEU n 
1 2594 CYS n 
1 2595 GLY n 
1 2596 PRO n 
1 2597 PRO n 
1 2598 GLY n 
1 2599 SER n 
1 2600 GLY n 
1 2601 LYS n 
1 2602 THR n 
1 2603 MET n 
1 2604 THR n 
1 2605 LEU n 
1 2606 PHE n 
1 2607 SER n 
1 2608 ALA n 
1 2609 LEU n 
1 2610 ARG n 
1 2611 ALA n 
1 2612 LEU n 
1 2613 PRO n 
1 2614 ASP n 
1 2615 MET n 
1 2616 GLU n 
1 2617 VAL n 
1 2618 VAL n 
1 2619 GLY n 
1 2620 LEU n 
1 2621 ASN n 
1 2622 PHE n 
1 2623 SER n 
1 2624 SER n 
1 2625 ALA n 
1 2626 THR n 
1 2627 THR n 
1 2628 PRO n 
1 2629 GLU n 
1 2630 LEU n 
1 2631 LEU n 
1 2632 LEU n 
1 2633 LYS n 
1 2634 THR n 
1 2635 PHE n 
1 2636 ASP n 
1 2637 HIS n 
1 2638 TYR n 
1 2639 CYS n 
1 2640 GLU n 
1 2641 TYR n 
1 2642 ARG n 
1 2643 ARG n 
1 2644 THR n 
1 2645 PRO n 
1 2646 ASN n 
1 2647 GLY n 
1 2648 VAL n 
1 2649 VAL n 
1 2650 LEU n 
1 2651 ALA n 
1 2652 PRO n 
1 2653 VAL n 
1 2654 GLN n 
1 2655 LEU n 
1 2656 GLY n 
1 2657 LYS n 
1 2658 TRP n 
1 2659 LEU n 
1 2660 VAL n 
1 2661 LEU n 
1 2662 PHE n 
1 2663 CYS n 
1 2664 ASP n 
1 2665 GLU n 
1 2666 ILE n 
1 2667 ASN n 
1 2668 LEU n 
1 2669 PRO n 
1 2670 ASP n 
1 2671 MET n 
1 2672 ASP n 
1 2673 LYS n 
1 2674 TYR n 
1 2675 GLY n 
1 2676 THR n 
1 2677 GLN n 
1 2678 ARG n 
1 2679 VAL n 
1 2680 ILE n 
1 2681 SER n 
1 2682 PHE n 
1 2683 ILE n 
1 2684 ARG n 
1 2685 GLN n 
1 2686 MET n 
1 2687 VAL n 
1 2688 GLU n 
1 2689 HIS n 
1 2690 GLY n 
1 2691 GLY n 
1 2692 PHE n 
1 2693 TYR n 
1 2694 ARG n 
1 2695 THR n 
1 2696 SER n 
1 2697 ASP n 
1 2698 GLN n 
1 2699 THR n 
1 2700 TRP n 
1 2701 VAL n 
1 2702 LYS n 
1 2703 LEU n 
1 2704 GLU n 
1 2705 ARG n 
1 2706 ILE n 
1 2707 GLN n 
1 2708 PHE n 
1 2709 VAL n 
1 2710 GLY n 
1 2711 ALA n 
1 2712 CYS n 
1 2713 ASN n 
1 2714 PRO n 
1 2715 PRO n 
1 2716 THR n 
1 2717 ASP n 
1 2718 PRO n 
1 2719 GLY n 
1 2720 ARG n 
1 2721 LYS n 
1 2722 PRO n 
1 2723 LEU n 
1 2724 SER n 
1 2725 HIS n 
1 2726 ARG n 
1 2727 PHE n 
1 2728 LEU n 
1 2729 ARG n 
1 2730 HIS n 
1 2731 VAL n 
1 2732 PRO n 
1 2733 VAL n 
1 2734 VAL n 
1 2735 TYR n 
1 2736 VAL n 
1 2737 ASP n 
1 2738 TYR n 
1 2739 PRO n 
1 2740 GLY n 
1 2741 PRO n 
1 2742 ALA n 
1 2743 SER n 
1 2744 LEU n 
1 2745 THR n 
1 2746 GLN n 
1 2747 ILE n 
1 2748 TYR n 
1 2749 GLY n 
1 2750 THR n 
1 2751 PHE n 
1 2752 ASN n 
1 2753 ARG n 
1 2754 ALA n 
1 2755 MET n 
1 2756 LEU n 
1 2757 ARG n 
1 2758 LEU n 
1 2759 ILE n 
1 2760 PRO n 
1 2761 SER n 
1 2762 LEU n 
1 2763 ARG n 
1 2764 THR n 
1 2765 TYR n 
1 2766 ALA n 
1 2767 GLU n 
1 2768 PRO n 
1 2769 LEU n 
1 2770 THR n 
1 2771 ALA n 
1 2772 ALA n 
1 2773 MET n 
1 2774 VAL n 
1 2775 GLU n 
1 2776 PHE n 
1 2777 TYR n 
1 2778 THR n 
1 2779 MET n 
1 2780 SER n 
1 2781 GLN n 
1 2782 GLU n 
1 2783 ARG n 
1 2784 PHE n 
1 2785 THR n 
1 2786 GLN n 
1 2787 ASP n 
1 2788 THR n 
1 2789 GLN n 
1 2790 PRO n 
1 2791 HIS n 
1 2792 TYR n 
1 2793 ILE n 
1 2794 TYR n 
1 2795 SER n 
1 2796 PRO n 
1 2797 ARG n 
1 2798 GLU n 
1 2799 MET n 
1 2800 THR n 
1 2801 ARG n 
1 2802 TRP n 
1 2803 VAL n 
1 2804 ARG n 
1 2805 GLY n 
1 2806 ILE n 
1 2807 PHE n 
1 2808 GLU n 
1 2809 ALA n 
1 2810 LEU n 
1 2811 ARG n 
1 2812 PRO n 
1 2813 LEU n 
1 2814 GLU n 
1 2815 THR n 
1 2816 LEU n 
1 2817 PRO n 
1 2818 VAL n 
1 2819 GLU n 
1 2820 GLY n 
1 2821 LEU n 
1 2822 ILE n 
1 2823 ARG n 
1 2824 ILE n 
1 2825 TRP n 
1 2826 ALA n 
1 2827 HIS n 
1 2828 GLU n 
1 2829 ALA n 
1 2830 LEU n 
1 2831 ARG n 
1 2832 LEU n 
1 2833 PHE n 
1 2834 GLN n 
1 2835 ASP n 
1 2836 ARG n 
1 2837 LEU n 
1 2838 VAL n 
1 2839 GLU n 
1 2840 ASP n 
1 2841 GLU n 
1 2842 GLU n 
1 2843 ARG n 
1 2844 ARG n 
1 2845 TRP n 
1 2846 THR n 
1 2847 ASP n 
1 2848 GLU n 
1 2849 ASN n 
1 2850 ILE n 
1 2851 ASP n 
1 2852 THR n 
1 2853 VAL n 
1 2854 ALA n 
1 2855 LEU n 
1 2856 LYS n 
1 2857 HIS n 
1 2858 PHE n 
1 2859 PRO n 
1 2860 ASN n 
1 2861 ILE n 
1 2862 ASP n 
1 2863 ARG n 
1 2864 GLU n 
1 2865 LYS n 
1 2866 ALA n 
1 2867 MET n 
1 2868 SER n 
1 2869 ARG n 
1 2870 PRO n 
1 2871 ILE n 
1 2872 LEU n 
1 2873 TYR n 
1 2874 SER n 
1 2875 ASN n 
1 2876 TRP n 
1 2877 LEU n 
1 2878 SER n 
1 2879 LYS n 
1 2880 ASP n 
1 2881 TYR n 
1 2882 ILE n 
1 2883 PRO n 
1 2884 VAL n 
1 2885 ASP n 
1 2886 GLN n 
1 2887 GLU n 
1 2888 GLU n 
1 2889 LEU n 
1 2890 ARG n 
1 2891 ASP n 
1 2892 TYR n 
1 2893 VAL n 
1 2894 LYS n 
1 2895 ALA n 
1 2896 ARG n 
1 2897 LEU n 
1 2898 LYS n 
1 2899 VAL n 
1 2900 PHE n 
1 2901 TYR n 
1 2902 GLU n 
1 2903 GLU n 
1 2904 GLU n 
1 2905 LEU n 
1 2906 ASP n 
1 2907 VAL n 
1 2908 PRO n 
1 2909 LEU n 
1 2910 VAL n 
1 2911 LEU n 
1 2912 PHE n 
1 2913 ASN n 
1 2914 GLU n 
1 2915 VAL n 
1 2916 LEU n 
1 2917 ASP n 
1 2918 HIS n 
1 2919 VAL n 
1 2920 LEU n 
1 2921 ARG n 
1 2922 ILE n 
1 2923 ASP n 
1 2924 ARG n 
1 2925 ILE n 
1 2926 PHE n 
1 2927 ARG n 
1 2928 GLN n 
1 2929 PRO n 
1 2930 GLN n 
1 2931 GLY n 
1 2932 HIS n 
1 2933 LEU n 
1 2934 LEU n 
1 2935 LEU n 
1 2936 ILE n 
1 2937 GLY n 
1 2938 VAL n 
1 2939 SER n 
1 2940 GLY n 
1 2941 ALA n 
1 2942 GLY n 
1 2943 LYS n 
1 2944 THR n 
1 2945 THR n 
1 2946 LEU n 
1 2947 SER n 
1 2948 ARG n 
1 2949 PHE n 
1 2950 VAL n 
1 2951 ALA n 
1 2952 TRP n 
1 2953 MET n 
1 2954 ASN n 
1 2955 GLY n 
1 2956 LEU n 
1 2957 SER n 
1 2958 VAL n 
1 2959 TYR n 
1 2960 GLN n 
1 2961 ILE n 
1 2962 LYS n 
1 2963 VAL n 
1 2964 HIS n 
1 2965 ARG n 
1 2966 LYS n 
1 2967 TYR n 
1 2968 THR n 
1 2969 GLY n 
1 2970 GLU n 
1 2971 ASP n 
1 2972 PHE n 
1 2973 ASP n 
1 2974 GLU n 
1 2975 ASP n 
1 2976 LEU n 
1 2977 ARG n 
1 2978 THR n 
1 2979 VAL n 
1 2980 LEU n 
1 2981 ARG n 
1 2982 ARG n 
1 2983 SER n 
1 2984 GLY n 
1 2985 CYS n 
1 2986 LYS n 
1 2987 ASN n 
1 2988 GLU n 
1 2989 LYS n 
1 2990 ILE n 
1 2991 ALA n 
1 2992 PHE n 
1 2993 ILE n 
1 2994 MET n 
1 2995 ASP n 
1 2996 GLU n 
1 2997 SER n 
1 2998 ASN n 
1 2999 VAL n 
1 3000 LEU n 
1 3001 ASP n 
1 3002 SER n 
1 3003 GLY n 
1 3004 PHE n 
1 3005 LEU n 
1 3006 GLU n 
1 3007 ARG n 
1 3008 MET n 
1 3009 ASN n 
1 3010 THR n 
1 3011 LEU n 
1 3012 LEU n 
1 3013 ALA n 
1 3014 ASN n 
1 3015 GLY n 
1 3016 GLU n 
1 3017 VAL n 
1 3018 PRO n 
1 3019 GLY n 
1 3020 LEU n 
1 3021 PHE n 
1 3022 GLU n 
1 3023 GLY n 
1 3024 ASP n 
1 3025 GLU n 
1 3026 TYR n 
1 3027 ALA n 
1 3028 THR n 
1 3029 LEU n 
1 3030 MET n 
1 3031 THR n 
1 3032 GLN n 
1 3033 CYS n 
1 3034 LYS n 
1 3035 GLU n 
1 3036 GLY n 
1 3037 ALA n 
1 3038 GLN n 
1 3039 LYS n 
1 3040 GLU n 
1 3041 GLY n 
1 3042 LEU n 
1 3043 MET n 
1 3044 LEU n 
1 3045 ASP n 
1 3046 SER n 
1 3047 HIS n 
1 3048 GLU n 
1 3049 GLU n 
1 3050 LEU n 
1 3051 TYR n 
1 3052 LYS n 
1 3053 TRP n 
1 3054 PHE n 
1 3055 THR n 
1 3056 SER n 
1 3057 GLN n 
1 3058 VAL n 
1 3059 ILE n 
1 3060 ARG n 
1 3061 ASN n 
1 3062 LEU n 
1 3063 HIS n 
1 3064 VAL n 
1 3065 VAL n 
1 3066 PHE n 
1 3067 THR n 
1 3068 MET n 
1 3069 ASN n 
1 3070 PRO n 
1 3071 SER n 
1 3072 SER n 
1 3073 GLU n 
1 3074 GLY n 
1 3075 LEU n 
1 3076 LYS n 
1 3077 ASP n 
1 3078 ARG n 
1 3079 ALA n 
1 3080 ALA n 
1 3081 THR n 
1 3082 SER n 
1 3083 PRO n 
1 3084 ALA n 
1 3085 LEU n 
1 3086 PHE n 
1 3087 ASN n 
1 3088 ARG n 
1 3089 CYS n 
1 3090 VAL n 
1 3091 LEU n 
1 3092 ASN n 
1 3093 TRP n 
1 3094 PHE n 
1 3095 GLY n 
1 3096 ASP n 
1 3097 TRP n 
1 3098 SER n 
1 3099 THR n 
1 3100 GLU n 
1 3101 ALA n 
1 3102 LEU n 
1 3103 TYR n 
1 3104 GLN n 
1 3105 VAL n 
1 3106 GLY n 
1 3107 LYS n 
1 3108 GLU n 
1 3109 PHE n 
1 3110 THR n 
1 3111 SER n 
1 3112 LYS n 
1 3113 MET n 
1 3114 ASP n 
1 3115 LEU n 
1 3116 GLU n 
1 3117 LYS n 
1 3118 PRO n 
1 3119 ASN n 
1 3120 TYR n 
1 3121 ILE n 
1 3122 VAL n 
1 3123 PRO n 
1 3124 ASP n 
1 3125 TYR n 
1 3126 MET n 
1 3127 PRO n 
1 3128 VAL n 
1 3129 VAL n 
1 3130 TYR n 
1 3131 ASP n 
1 3132 LYS n 
1 3133 LEU n 
1 3134 PRO n 
1 3135 GLN n 
1 3136 PRO n 
1 3137 PRO n 
1 3138 SER n 
1 3139 HIS n 
1 3140 ARG n 
1 3141 GLU n 
1 3142 ALA n 
1 3143 ILE n 
1 3144 VAL n 
1 3145 ASN n 
1 3146 SER n 
1 3147 CYS n 
1 3148 VAL n 
1 3149 PHE n 
1 3150 VAL n 
1 3151 HIS n 
1 3152 GLN n 
1 3153 THR n 
1 3154 LEU n 
1 3155 HIS n 
1 3156 GLN n 
1 3157 ALA n 
1 3158 ASN n 
1 3159 ALA n 
1 3160 ARG n 
1 3161 LEU n 
1 3162 ALA n 
1 3163 LYS n 
1 3164 ARG n 
1 3165 GLY n 
1 3166 GLY n 
1 3167 ARG n 
1 3168 THR n 
1 3169 MET n 
1 3170 ALA n 
1 3171 ILE n 
1 3172 THR n 
1 3173 PRO n 
1 3174 ARG n 
1 3175 HIS n 
1 3176 TYR n 
1 3177 LEU n 
1 3178 ASP n 
1 3179 PHE n 
1 3180 ILE n 
1 3181 ASN n 
1 3182 HIS n 
1 3183 TYR n 
1 3184 ALA n 
1 3185 ASN n 
1 3186 LEU n 
1 3187 PHE n 
1 3188 HIS n 
1 3189 GLU n 
1 3190 LYS n 
1 3191 ARG n 
1 3192 SER n 
1 3193 GLU n 
1 3194 LEU n 
1 3195 GLU n 
1 3196 GLU n 
1 3197 GLN n 
1 3198 GLN n 
1 3199 MET n 
1 3200 HIS n 
1 3201 LEU n 
1 3202 ASN n 
1 3203 VAL n 
1 3204 GLY n 
1 3205 LEU n 
1 3206 ARG n 
1 3207 LYS n 
1 3208 ILE n 
1 3209 LYS n 
1 3210 GLU n 
1 3211 THR n 
1 3212 VAL n 
1 3213 ASP n 
1 3214 GLN n 
1 3215 VAL n 
1 3216 GLU n 
1 3217 GLU n 
1 3218 LEU n 
1 3219 ARG n 
1 3220 ARG n 
1 3221 ASP n 
1 3222 LEU n 
1 3223 ARG n 
1 3224 ILE n 
1 3225 LYS n 
1 3226 SER n 
1 3227 GLN n 
1 3228 GLU n 
1 3229 LEU n 
1 3230 GLU n 
1 3231 VAL n 
1 3232 LYS n 
1 3233 ASN n 
1 3234 ALA n 
1 3235 ALA n 
1 3236 ALA n 
1 3237 ASN n 
1 3238 ASP n 
1 3239 LYS n 
1 3240 LEU n 
1 3241 LYS n 
1 3242 LYS n 
1 3243 MET n 
1 3244 VAL n 
1 3245 LYS n 
1 3246 ASP n 
1 3247 GLN n 
1 3248 GLN n 
1 3249 GLU n 
1 3250 ALA n 
1 3251 GLU n 
1 3252 LYS n 
1 3253 LYS n 
1 3254 LYS n 
1 3255 VAL n 
1 3256 MET n 
1 3257 SER n 
1 3258 GLN n 
1 3259 GLU n 
1 3260 ILE n 
1 3261 GLN n 
1 3262 GLU n 
1 3263 GLN n 
1 3264 LEU n 
1 3265 HIS n 
1 3266 LYS n 
1 3267 GLN n 
1 3268 GLN n 
1 3269 GLU n 
1 3270 VAL n 
1 3271 ILE n 
1 3272 ALA n 
1 3273 ASP n 
1 3274 LYS n 
1 3275 GLN n 
1 3276 MET n 
1 3277 SER n 
1 3278 VAL n 
1 3279 LYS n 
1 3280 GLU n 
1 3281 ASP n 
1 3282 LEU n 
1 3283 ASP n 
1 3284 LYS n 
1 3285 VAL n 
1 3286 GLU n 
1 3287 PRO n 
1 3288 ALA n 
1 3289 VAL n 
1 3290 ILE n 
1 3291 GLU n 
1 3292 ALA n 
1 3293 GLN n 
1 3294 ASN n 
1 3295 ALA n 
1 3296 VAL n 
1 3297 LYS n 
1 3298 SER n 
1 3299 ILE n 
1 3300 LYS n 
1 3301 LYS n 
1 3302 GLN n 
1 3303 HIS n 
1 3304 LEU n 
1 3305 VAL n 
1 3306 GLU n 
1 3307 VAL n 
1 3308 ARG n 
1 3309 SER n 
1 3310 MET n 
1 3311 ALA n 
1 3312 ASN n 
1 3313 PRO n 
1 3314 PRO n 
1 3315 ALA n 
1 3316 ALA n 
1 3317 VAL n 
1 3318 LYS n 
1 3319 LEU n 
1 3320 ALA n 
1 3321 LEU n 
1 3322 GLU n 
1 3323 SER n 
1 3324 ILE n 
1 3325 CYS n 
1 3326 LEU n 
1 3327 LEU n 
1 3328 LEU n 
1 3329 GLY n 
1 3330 GLU n 
1 3331 SER n 
1 3332 THR n 
1 3333 THR n 
1 3334 ASP n 
1 3335 TRP n 
1 3336 LYS n 
1 3337 GLN n 
1 3338 ILE n 
1 3339 ARG n 
1 3340 SER n 
1 3341 ILE n 
1 3342 ILE n 
1 3343 MET n 
1 3344 ARG n 
1 3345 GLU n 
1 3346 ASN n 
1 3347 PHE n 
1 3348 ILE n 
1 3349 PRO n 
1 3350 THR n 
1 3351 ILE n 
1 3352 VAL n 
1 3353 ASN n 
1 3354 PHE n 
1 3355 SER n 
1 3356 ALA n 
1 3357 GLU n 
1 3358 GLU n 
1 3359 ILE n 
1 3360 SER n 
1 3361 ASP n 
1 3362 ALA n 
1 3363 ILE n 
1 3364 ARG n 
1 3365 GLU n 
1 3366 LYS n 
1 3367 MET n 
1 3368 LYS n 
1 3369 LYS n 
1 3370 ASN n 
1 3371 TYR n 
1 3372 MET n 
1 3373 SER n 
1 3374 ASN n 
1 3375 PRO n 
1 3376 SER n 
1 3377 TYR n 
1 3378 ASN n 
1 3379 TYR n 
1 3380 GLU n 
1 3381 ILE n 
1 3382 VAL n 
1 3383 ASN n 
1 3384 ARG n 
1 3385 ALA n 
1 3386 SER n 
1 3387 LEU n 
1 3388 ALA n 
1 3389 CYS n 
1 3390 GLY n 
1 3391 PRO n 
1 3392 MET n 
1 3393 VAL n 
1 3394 LYS n 
1 3395 TRP n 
1 3396 ALA n 
1 3397 ILE n 
1 3398 ALA n 
1 3399 GLN n 
1 3400 LEU n 
1 3401 ASN n 
1 3402 TYR n 
1 3403 ALA n 
1 3404 ASP n 
1 3405 MET n 
1 3406 LEU n 
1 3407 LYS n 
1 3408 ARG n 
1 3409 VAL n 
1 3410 GLU n 
1 3411 PRO n 
1 3412 LEU n 
1 3413 ARG n 
1 3414 ASN n 
1 3415 GLU n 
1 3416 LEU n 
1 3417 GLN n 
1 3418 LYS n 
1 3419 LEU n 
1 3420 GLU n 
1 3421 ASP n 
1 3422 ASP n 
1 3423 ALA n 
1 3424 LYS n 
1 3425 ASP n 
1 3426 ASN n 
1 3427 GLN n 
1 3428 GLN n 
1 3429 LYS n 
1 3430 ALA n 
1 3431 ASN n 
1 3432 GLU n 
1 3433 VAL n 
1 3434 GLU n 
1 3435 GLN n 
1 3436 MET n 
1 3437 ILE n 
1 3438 ARG n 
1 3439 ASP n 
1 3440 LEU n 
1 3441 GLU n 
1 3442 ALA n 
1 3443 SER n 
1 3444 ILE n 
1 3445 ALA n 
1 3446 ARG n 
1 3447 TYR n 
1 3448 LYS n 
1 3449 GLU n 
1 3450 GLU n 
1 3451 TYR n 
1 3452 ALA n 
1 3453 VAL n 
1 3454 LEU n 
1 3455 ILE n 
1 3456 SER n 
1 3457 GLU n 
1 3458 ALA n 
1 3459 GLN n 
1 3460 ALA n 
1 3461 ILE n 
1 3462 LYS n 
1 3463 ALA n 
1 3464 ASP n 
1 3465 LEU n 
1 3466 ALA n 
1 3467 ALA n 
1 3468 VAL n 
1 3469 GLU n 
1 3470 ALA n 
1 3471 LYS n 
1 3472 VAL n 
1 3473 ASN n 
1 3474 ARG n 
1 3475 SER n 
1 3476 THR n 
1 3477 ALA n 
1 3478 LEU n 
1 3479 LEU n 
1 3480 LYS n 
1 3481 SER n 
1 3482 LEU n 
1 3483 SER n 
1 3484 ALA n 
1 3485 GLU n 
1 3486 ARG n 
1 3487 GLU n 
1 3488 ARG n 
1 3489 TRP n 
1 3490 GLU n 
1 3491 LYS n 
1 3492 THR n 
1 3493 SER n 
1 3494 GLU n 
1 3495 THR n 
1 3496 PHE n 
1 3497 LYS n 
1 3498 ASN n 
1 3499 GLN n 
1 3500 MET n 
1 3501 SER n 
1 3502 THR n 
1 3503 ILE n 
1 3504 ALA n 
1 3505 GLY n 
1 3506 ASP n 
1 3507 CYS n 
1 3508 LEU n 
1 3509 LEU n 
1 3510 SER n 
1 3511 ALA n 
1 3512 ALA n 
1 3513 PHE n 
1 3514 ILE n 
1 3515 ALA n 
1 3516 TYR n 
1 3517 ALA n 
1 3518 GLY n 
1 3519 TYR n 
1 3520 PHE n 
1 3521 ASP n 
1 3522 GLN n 
1 3523 GLN n 
1 3524 MET n 
1 3525 ARG n 
1 3526 GLN n 
1 3527 ASN n 
1 3528 LEU n 
1 3529 PHE n 
1 3530 THR n 
1 3531 THR n 
1 3532 TRP n 
1 3533 SER n 
1 3534 HIS n 
1 3535 HIS n 
1 3536 LEU n 
1 3537 GLN n 
1 3538 GLN n 
1 3539 ALA n 
1 3540 ASN n 
1 3541 ILE n 
1 3542 GLN n 
1 3543 PHE n 
1 3544 ARG n 
1 3545 THR n 
1 3546 ASP n 
1 3547 ILE n 
1 3548 ALA n 
1 3549 ARG n 
1 3550 THR n 
1 3551 GLU n 
1 3552 TYR n 
1 3553 LEU n 
1 3554 SER n 
1 3555 ASN n 
1 3556 ALA n 
1 3557 ASP n 
1 3558 GLU n 
1 3559 ARG n 
1 3560 LEU n 
1 3561 ARG n 
1 3562 TRP n 
1 3563 GLN n 
1 3564 ALA n 
1 3565 SER n 
1 3566 SER n 
1 3567 LEU n 
1 3568 PRO n 
1 3569 ALA n 
1 3570 ASP n 
1 3571 ASP n 
1 3572 LEU n 
1 3573 CYS n 
1 3574 THR n 
1 3575 GLU n 
1 3576 ASN n 
1 3577 ALA n 
1 3578 ILE n 
1 3579 MET n 
1 3580 LEU n 
1 3581 LYS n 
1 3582 ARG n 
1 3583 PHE n 
1 3584 ASN n 
1 3585 ARG n 
1 3586 TYR n 
1 3587 PRO n 
1 3588 LEU n 
1 3589 ILE n 
1 3590 ILE n 
1 3591 ASP n 
1 3592 PRO n 
1 3593 SER n 
1 3594 GLY n 
1 3595 GLN n 
1 3596 ALA n 
1 3597 THR n 
1 3598 GLU n 
1 3599 PHE n 
1 3600 ILE n 
1 3601 MET n 
1 3602 ASN n 
1 3603 GLU n 
1 3604 TYR n 
1 3605 LYS n 
1 3606 ASP n 
1 3607 ARG n 
1 3608 LYS n 
1 3609 ILE n 
1 3610 THR n 
1 3611 ARG n 
1 3612 THR n 
1 3613 SER n 
1 3614 PHE n 
1 3615 LEU n 
1 3616 ASP n 
1 3617 ASP n 
1 3618 ALA n 
1 3619 PHE n 
1 3620 ARG n 
1 3621 LYS n 
1 3622 ASN n 
1 3623 LEU n 
1 3624 GLU n 
1 3625 SER n 
1 3626 ALA n 
1 3627 LEU n 
1 3628 ARG n 
1 3629 PHE n 
1 3630 GLY n 
1 3631 ASN n 
1 3632 PRO n 
1 3633 LEU n 
1 3634 LEU n 
1 3635 VAL n 
1 3636 GLN n 
1 3637 ASP n 
1 3638 VAL n 
1 3639 GLU n 
1 3640 SER n 
1 3641 TYR n 
1 3642 ASP n 
1 3643 PRO n 
1 3644 VAL n 
1 3645 LEU n 
1 3646 ASN n 
1 3647 PRO n 
1 3648 VAL n 
1 3649 LEU n 
1 3650 ASN n 
1 3651 ARG n 
1 3652 GLU n 
1 3653 VAL n 
1 3654 ARG n 
1 3655 ARG n 
1 3656 THR n 
1 3657 GLY n 
1 3658 GLY n 
1 3659 ARG n 
1 3660 VAL n 
1 3661 LEU n 
1 3662 ILE n 
1 3663 THR n 
1 3664 LEU n 
1 3665 GLY n 
1 3666 ASP n 
1 3667 GLN n 
1 3668 ASP n 
1 3669 ILE n 
1 3670 ASP n 
1 3671 LEU n 
1 3672 SER n 
1 3673 PRO n 
1 3674 SER n 
1 3675 PHE n 
1 3676 VAL n 
1 3677 ILE n 
1 3678 PHE n 
1 3679 LEU n 
1 3680 SER n 
1 3681 THR n 
1 3682 ARG n 
1 3683 ASP n 
1 3684 PRO n 
1 3685 THR n 
1 3686 VAL n 
1 3687 GLU n 
1 3688 PHE n 
1 3689 PRO n 
1 3690 PRO n 
1 3691 ASP n 
1 3692 LEU n 
1 3693 CYS n 
1 3694 SER n 
1 3695 ARG n 
1 3696 VAL n 
1 3697 THR n 
1 3698 PHE n 
1 3699 VAL n 
1 3700 ASN n 
1 3701 PHE n 
1 3702 THR n 
1 3703 VAL n 
1 3704 THR n 
1 3705 ARG n 
1 3706 SER n 
1 3707 SER n 
1 3708 LEU n 
1 3709 GLN n 
1 3710 SER n 
1 3711 GLN n 
1 3712 CYS n 
1 3713 LEU n 
1 3714 ASN n 
1 3715 GLU n 
1 3716 VAL n 
1 3717 LEU n 
1 3718 LYS n 
1 3719 ALA n 
1 3720 GLU n 
1 3721 ARG n 
1 3722 PRO n 
1 3723 ASP n 
1 3724 VAL n 
1 3725 ASP n 
1 3726 GLU n 
1 3727 LYS n 
1 3728 ARG n 
1 3729 SER n 
1 3730 ASP n 
1 3731 LEU n 
1 3732 LEU n 
1 3733 LYS n 
1 3734 LEU n 
1 3735 GLN n 
1 3736 GLY n 
1 3737 GLU n 
1 3738 PHE n 
1 3739 GLN n 
1 3740 LEU n 
1 3741 ARG n 
1 3742 LEU n 
1 3743 ARG n 
1 3744 GLN n 
1 3745 LEU n 
1 3746 GLU n 
1 3747 LYS n 
1 3748 SER n 
1 3749 LEU n 
1 3750 LEU n 
1 3751 GLN n 
1 3752 ALA n 
1 3753 LEU n 
1 3754 ASN n 
1 3755 GLU n 
1 3756 VAL n 
1 3757 LYS n 
1 3758 GLY n 
1 3759 ARG n 
1 3760 ILE n 
1 3761 LEU n 
1 3762 ASP n 
1 3763 ASP n 
1 3764 ASP n 
1 3765 THR n 
1 3766 ILE n 
1 3767 ILE n 
1 3768 THR n 
1 3769 THR n 
1 3770 LEU n 
1 3771 GLU n 
1 3772 ASN n 
1 3773 LEU n 
1 3774 LYS n 
1 3775 ARG n 
1 3776 GLU n 
1 3777 ALA n 
1 3778 ALA n 
1 3779 GLU n 
1 3780 VAL n 
1 3781 THR n 
1 3782 ARG n 
1 3783 LYS n 
1 3784 VAL n 
1 3785 GLU n 
1 3786 GLU n 
1 3787 THR n 
1 3788 ASP n 
1 3789 ILE n 
1 3790 VAL n 
1 3791 MET n 
1 3792 GLN n 
1 3793 GLU n 
1 3794 VAL n 
1 3795 GLU n 
1 3796 THR n 
1 3797 VAL n 
1 3798 SER n 
1 3799 GLN n 
1 3800 GLN n 
1 3801 TYR n 
1 3802 LEU n 
1 3803 PRO n 
1 3804 LEU n 
1 3805 SER n 
1 3806 THR n 
1 3807 ALA n 
1 3808 CYS n 
1 3809 SER n 
1 3810 SER n 
1 3811 ILE n 
1 3812 TYR n 
1 3813 PHE n 
1 3814 THR n 
1 3815 MET n 
1 3816 GLU n 
1 3817 SER n 
1 3818 LEU n 
1 3819 LYS n 
1 3820 GLN n 
1 3821 ILE n 
1 3822 HIS n 
1 3823 PHE n 
1 3824 LEU n 
1 3825 TYR n 
1 3826 GLN n 
1 3827 TYR n 
1 3828 SER n 
1 3829 LEU n 
1 3830 GLN n 
1 3831 PHE n 
1 3832 PHE n 
1 3833 LEU n 
1 3834 ASP n 
1 3835 ILE n 
1 3836 TYR n 
1 3837 HIS n 
1 3838 ASN n 
1 3839 VAL n 
1 3840 LEU n 
1 3841 TYR n 
1 3842 GLU n 
1 3843 ASN n 
1 3844 PRO n 
1 3845 ASN n 
1 3846 LEU n 
1 3847 LYS n 
1 3848 GLY n 
1 3849 VAL n 
1 3850 THR n 
1 3851 ASP n 
1 3852 HIS n 
1 3853 THR n 
1 3854 GLN n 
1 3855 ARG n 
1 3856 LEU n 
1 3857 SER n 
1 3858 ILE n 
1 3859 ILE n 
1 3860 THR n 
1 3861 LYS n 
1 3862 ASP n 
1 3863 LEU n 
1 3864 PHE n 
1 3865 GLN n 
1 3866 VAL n 
1 3867 ALA n 
1 3868 PHE n 
1 3869 ASN n 
1 3870 ARG n 
1 3871 VAL n 
1 3872 ALA n 
1 3873 ARG n 
1 3874 GLY n 
1 3875 MET n 
1 3876 LEU n 
1 3877 HIS n 
1 3878 GLN n 
1 3879 ASP n 
1 3880 HIS n 
1 3881 ILE n 
1 3882 THR n 
1 3883 PHE n 
1 3884 ALA n 
1 3885 MET n 
1 3886 LEU n 
1 3887 LEU n 
1 3888 ALA n 
1 3889 ARG n 
1 3890 ILE n 
1 3891 LYS n 
1 3892 LEU n 
1 3893 LYS n 
1 3894 GLY n 
1 3895 THR n 
1 3896 VAL n 
1 3897 GLY n 
1 3898 GLU n 
1 3899 PRO n 
1 3900 THR n 
1 3901 TYR n 
1 3902 ASP n 
1 3903 ALA n 
1 3904 GLU n 
1 3905 PHE n 
1 3906 GLN n 
1 3907 HIS n 
1 3908 PHE n 
1 3909 LEU n 
1 3910 ARG n 
1 3911 GLY n 
1 3912 ASN n 
1 3913 GLU n 
1 3914 ILE n 
1 3915 VAL n 
1 3916 LEU n 
1 3917 SER n 
1 3918 ALA n 
1 3919 GLY n 
1 3920 SER n 
1 3921 THR n 
1 3922 PRO n 
1 3923 ARG n 
1 3924 ILE n 
1 3925 GLN n 
1 3926 GLY n 
1 3927 LEU n 
1 3928 THR n 
1 3929 VAL n 
1 3930 GLU n 
1 3931 GLN n 
1 3932 ALA n 
1 3933 GLU n 
1 3934 ALA n 
1 3935 VAL n 
1 3936 VAL n 
1 3937 ARG n 
1 3938 LEU n 
1 3939 SER n 
1 3940 CYS n 
1 3941 LEU n 
1 3942 PRO n 
1 3943 ALA n 
1 3944 PHE n 
1 3945 LYS n 
1 3946 ASP n 
1 3947 LEU n 
1 3948 ILE n 
1 3949 ALA n 
1 3950 LYS n 
1 3951 VAL n 
1 3952 GLN n 
1 3953 ALA n 
1 3954 ASP n 
1 3955 GLU n 
1 3956 GLN n 
1 3957 PHE n 
1 3958 GLY n 
1 3959 ILE n 
1 3960 TRP n 
1 3961 LEU n 
1 3962 ASP n 
1 3963 SER n 
1 3964 SER n 
1 3965 SER n 
1 3966 PRO n 
1 3967 GLU n 
1 3968 GLN n 
1 3969 THR n 
1 3970 VAL n 
1 3971 PRO n 
1 3972 TYR n 
1 3973 LEU n 
1 3974 TRP n 
1 3975 SER n 
1 3976 GLU n 
1 3977 GLU n 
1 3978 THR n 
1 3979 PRO n 
1 3980 ALA n 
1 3981 THR n 
1 3982 PRO n 
1 3983 ILE n 
1 3984 GLY n 
1 3985 GLN n 
1 3986 ALA n 
1 3987 ILE n 
1 3988 HIS n 
1 3989 ARG n 
1 3990 LEU n 
1 3991 LEU n 
1 3992 LEU n 
1 3993 ILE n 
1 3994 GLN n 
1 3995 ALA n 
1 3996 PHE n 
1 3997 ARG n 
1 3998 PRO n 
1 3999 ASP n 
1 4000 ARG n 
1 4001 LEU n 
1 4002 LEU n 
1 4003 ALA n 
1 4004 MET n 
1 4005 ALA n 
1 4006 HIS n 
1 4007 MET n 
1 4008 PHE n 
1 4009 VAL n 
1 4010 SER n 
1 4011 THR n 
1 4012 ASN n 
1 4013 LEU n 
1 4014 GLY n 
1 4015 GLU n 
1 4016 SER n 
1 4017 PHE n 
1 4018 MET n 
1 4019 SER n 
1 4020 ILE n 
1 4021 MET n 
1 4022 GLU n 
1 4023 GLN n 
1 4024 PRO n 
1 4025 LEU n 
1 4026 ASP n 
1 4027 LEU n 
1 4028 THR n 
1 4029 HIS n 
1 4030 ILE n 
1 4031 VAL n 
1 4032 GLY n 
1 4033 THR n 
1 4034 GLU n 
1 4035 VAL n 
1 4036 LYS n 
1 4037 PRO n 
1 4038 ASN n 
1 4039 THR n 
1 4040 PRO n 
1 4041 VAL n 
1 4042 LEU n 
1 4043 MET n 
1 4044 CYS n 
1 4045 SER n 
1 4046 VAL n 
1 4047 PRO n 
1 4048 GLY n 
1 4049 TYR n 
1 4050 ASP n 
1 4051 ALA n 
1 4052 SER n 
1 4053 GLY n 
1 4054 HIS n 
1 4055 VAL n 
1 4056 GLU n 
1 4057 ASP n 
1 4058 LEU n 
1 4059 ALA n 
1 4060 ALA n 
1 4061 GLU n 
1 4062 GLN n 
1 4063 ASN n 
1 4064 THR n 
1 4065 GLN n 
1 4066 ILE n 
1 4067 THR n 
1 4068 SER n 
1 4069 ILE n 
1 4070 ALA n 
1 4071 ILE n 
1 4072 GLY n 
1 4073 SER n 
1 4074 ALA n 
1 4075 GLU n 
1 4076 GLY n 
1 4077 PHE n 
1 4078 ASN n 
1 4079 GLN n 
1 4080 ALA n 
1 4081 ASP n 
1 4082 LYS n 
1 4083 ALA n 
1 4084 ILE n 
1 4085 ASN n 
1 4086 THR n 
1 4087 ALA n 
1 4088 VAL n 
1 4089 LYS n 
1 4090 SER n 
1 4091 GLY n 
1 4092 ARG n 
1 4093 TRP n 
1 4094 VAL n 
1 4095 MET n 
1 4096 LEU n 
1 4097 LYS n 
1 4098 ASN n 
1 4099 VAL n 
1 4100 HIS n 
1 4101 LEU n 
1 4102 ALA n 
1 4103 PRO n 
1 4104 GLY n 
1 4105 TRP n 
1 4106 LEU n 
1 4107 MET n 
1 4108 GLN n 
1 4109 LEU n 
1 4110 GLU n 
1 4111 LYS n 
1 4112 LYS n 
1 4113 LEU n 
1 4114 HIS n 
1 4115 SER n 
1 4116 LEU n 
1 4117 GLN n 
1 4118 PRO n 
1 4119 HIS n 
1 4120 ALA n 
1 4121 CYS n 
1 4122 PHE n 
1 4123 ARG n 
1 4124 LEU n 
1 4125 PHE n 
1 4126 LEU n 
1 4127 THR n 
1 4128 MET n 
1 4129 GLU n 
1 4130 ILE n 
1 4131 ASN n 
1 4132 PRO n 
1 4133 LYS n 
1 4134 VAL n 
1 4135 PRO n 
1 4136 VAL n 
1 4137 ASN n 
1 4138 LEU n 
1 4139 LEU n 
1 4140 ARG n 
1 4141 ALA n 
1 4142 GLY n 
1 4143 ARG n 
1 4144 ILE n 
1 4145 PHE n 
1 4146 VAL n 
1 4147 PHE n 
1 4148 GLU n 
1 4149 PRO n 
1 4150 PRO n 
1 4151 PRO n 
1 4152 GLY n 
1 4153 VAL n 
1 4154 LYS n 
1 4155 ALA n 
1 4156 ASN n 
1 4157 MET n 
1 4158 LEU n 
1 4159 ARG n 
1 4160 THR n 
1 4161 PHE n 
1 4162 SER n 
1 4163 SER n 
1 4164 ILE n 
1 4165 PRO n 
1 4166 VAL n 
1 4167 SER n 
1 4168 ARG n 
1 4169 ILE n 
1 4170 CYS n 
1 4171 LYS n 
1 4172 SER n 
1 4173 PRO n 
1 4174 ASN n 
1 4175 GLU n 
1 4176 ARG n 
1 4177 ALA n 
1 4178 ARG n 
1 4179 LEU n 
1 4180 TYR n 
1 4181 PHE n 
1 4182 LEU n 
1 4183 LEU n 
1 4184 ALA n 
1 4185 TRP n 
1 4186 PHE n 
1 4187 HIS n 
1 4188 ALA n 
1 4189 ILE n 
1 4190 ILE n 
1 4191 GLN n 
1 4192 GLU n 
1 4193 ARG n 
1 4194 LEU n 
1 4195 ARG n 
1 4196 TYR n 
1 4197 ALA n 
1 4198 PRO n 
1 4199 LEU n 
1 4200 GLY n 
1 4201 TRP n 
1 4202 SER n 
1 4203 LYS n 
1 4204 LYS n 
1 4205 TYR n 
1 4206 GLU n 
1 4207 PHE n 
1 4208 GLY n 
1 4209 GLU n 
1 4210 SER n 
1 4211 ASP n 
1 4212 LEU n 
1 4213 ARG n 
1 4214 SER n 
1 4215 ALA n 
1 4216 CYS n 
1 4217 ASP n 
1 4218 THR n 
1 4219 VAL n 
1 4220 ASP n 
1 4221 THR n 
1 4222 TRP n 
1 4223 LEU n 
1 4224 ASP n 
1 4225 ASP n 
1 4226 THR n 
1 4227 ALA n 
1 4228 LYS n 
1 4229 GLY n 
1 4230 ARG n 
1 4231 GLN n 
1 4232 ASN n 
1 4233 ILE n 
1 4234 SER n 
1 4235 PRO n 
1 4236 ASP n 
1 4237 LYS n 
1 4238 ILE n 
1 4239 PRO n 
1 4240 TRP n 
1 4241 SER n 
1 4242 ALA n 
1 4243 LEU n 
1 4244 LYS n 
1 4245 THR n 
1 4246 LEU n 
1 4247 MET n 
1 4248 ALA n 
1 4249 GLN n 
1 4250 SER n 
1 4251 ILE n 
1 4252 TYR n 
1 4253 GLY n 
1 4254 GLY n 
1 4255 ARG n 
1 4256 VAL n 
1 4257 ASP n 
1 4258 ASN n 
1 4259 GLU n 
1 4260 PHE n 
1 4261 ASP n 
1 4262 GLN n 
1 4263 ARG n 
1 4264 LEU n 
1 4265 LEU n 
1 4266 ASN n 
1 4267 THR n 
1 4268 PHE n 
1 4269 LEU n 
1 4270 GLU n 
1 4271 ARG n 
1 4272 LEU n 
1 4273 PHE n 
1 4274 THR n 
1 4275 THR n 
1 4276 ARG n 
1 4277 SER n 
1 4278 PHE n 
1 4279 ASP n 
1 4280 SER n 
1 4281 GLU n 
1 4282 PHE n 
1 4283 LYS n 
1 4284 LEU n 
1 4285 ALA n 
1 4286 CYS n 
1 4287 LYS n 
1 4288 VAL n 
1 4289 ASP n 
1 4290 GLY n 
1 4291 HIS n 
1 4292 LYS n 
1 4293 ASP n 
1 4294 ILE n 
1 4295 GLN n 
1 4296 MET n 
1 4297 PRO n 
1 4298 ASP n 
1 4299 GLY n 
1 4300 ILE n 
1 4301 ARG n 
1 4302 ARG n 
1 4303 GLU n 
1 4304 GLU n 
1 4305 PHE n 
1 4306 VAL n 
1 4307 GLN n 
1 4308 TRP n 
1 4309 VAL n 
1 4310 GLU n 
1 4311 LEU n 
1 4312 LEU n 
1 4313 PRO n 
1 4314 ASP n 
1 4315 THR n 
1 4316 GLN n 
1 4317 THR n 
1 4318 PRO n 
1 4319 SER n 
1 4320 TRP n 
1 4321 LEU n 
1 4322 GLY n 
1 4323 LEU n 
1 4324 PRO n 
1 4325 ASN n 
1 4326 ASN n 
1 4327 ALA n 
1 4328 GLU n 
1 4329 ARG n 
1 4330 VAL n 
1 4331 LEU n 
1 4332 LEU n 
1 4333 THR n 
1 4334 THR n 
1 4335 GLN n 
1 4336 GLY n 
1 4337 VAL n 
1 4338 ASP n 
1 4339 MET n 
1 4340 ILE n 
1 4341 SER n 
1 4342 LYS n 
1 4343 MET n 
1 4344 LEU n 
1 4345 LYS n 
1 4346 MET n 
1 4347 GLN n 
1 4348 MET n 
1 4349 LEU n 
1 4350 GLU n 
1 4351 ASP n 
1 4352 GLU n 
1 4353 ASP n 
1 4354 ASP n 
1 4355 LEU n 
1 4356 ALA n 
1 4357 TYR n 
1 4358 ALA n 
1 4359 GLU n 
1 4360 THR n 
1 4361 GLU n 
1 4362 LYS n 
1 4363 LYS n 
1 4364 THR n 
1 4365 ARG n 
1 4366 THR n 
1 4367 ASP n 
1 4368 SER n 
1 4369 THR n 
1 4370 SER n 
1 4371 ASP n 
1 4372 GLY n 
1 4373 ARG n 
1 4374 PRO n 
1 4375 ALA n 
1 4376 TRP n 
1 4377 MET n 
1 4378 ARG n 
1 4379 THR n 
1 4380 LEU n 
1 4381 HIS n 
1 4382 THR n 
1 4383 THR n 
1 4384 ALA n 
1 4385 SER n 
1 4386 ASN n 
1 4387 TRP n 
1 4388 LEU n 
1 4389 HIS n 
1 4390 LEU n 
1 4391 ILE n 
1 4392 PRO n 
1 4393 GLN n 
1 4394 THR n 
1 4395 LEU n 
1 4396 SER n 
1 4397 HIS n 
1 4398 LEU n 
1 4399 LYS n 
1 4400 ARG n 
1 4401 THR n 
1 4402 VAL n 
1 4403 GLU n 
1 4404 ASN n 
1 4405 ILE n 
1 4406 LYS n 
1 4407 ASP n 
1 4408 PRO n 
1 4409 LEU n 
1 4410 PHE n 
1 4411 ARG n 
1 4412 PHE n 
1 4413 PHE n 
1 4414 GLU n 
1 4415 ARG n 
1 4416 GLU n 
1 4417 VAL n 
1 4418 LYS n 
1 4419 MET n 
1 4420 GLY n 
1 4421 ALA n 
1 4422 LYS n 
1 4423 LEU n 
1 4424 LEU n 
1 4425 GLN n 
1 4426 ASP n 
1 4427 VAL n 
1 4428 ARG n 
1 4429 GLN n 
1 4430 ASP n 
1 4431 LEU n 
1 4432 ALA n 
1 4433 ASP n 
1 4434 VAL n 
1 4435 VAL n 
1 4436 GLN n 
1 4437 VAL n 
1 4438 CYS n 
1 4439 GLU n 
1 4440 GLY n 
1 4441 LYS n 
1 4442 LYS n 
1 4443 LYS n 
1 4444 GLN n 
1 4445 THR n 
1 4446 ASN n 
1 4447 TYR n 
1 4448 LEU n 
1 4449 ARG n 
1 4450 THR n 
1 4451 LEU n 
1 4452 ILE n 
1 4453 ASN n 
1 4454 GLU n 
1 4455 LEU n 
1 4456 VAL n 
1 4457 LYS n 
1 4458 GLY n 
1 4459 ILE n 
1 4460 LEU n 
1 4461 PRO n 
1 4462 ARG n 
1 4463 SER n 
1 4464 TRP n 
1 4465 SER n 
1 4466 HIS n 
1 4467 TYR n 
1 4468 THR n 
1 4469 VAL n 
1 4470 PRO n 
1 4471 ALA n 
1 4472 GLY n 
1 4473 MET n 
1 4474 THR n 
1 4475 VAL n 
1 4476 ILE n 
1 4477 GLN n 
1 4478 TRP n 
1 4479 VAL n 
1 4480 SER n 
1 4481 ASP n 
1 4482 PHE n 
1 4483 SER n 
1 4484 GLU n 
1 4485 ARG n 
1 4486 ILE n 
1 4487 LYS n 
1 4488 GLN n 
1 4489 LEU n 
1 4490 GLN n 
1 4491 ASN n 
1 4492 ILE n 
1 4493 SER n 
1 4494 LEU n 
1 4495 ALA n 
1 4496 ALA n 
1 4497 ALA n 
1 4498 SER n 
1 4499 GLY n 
1 4500 GLY n 
1 4501 ALA n 
1 4502 LYS n 
1 4503 GLU n 
1 4504 LEU n 
1 4505 LYS n 
1 4506 ASN n 
1 4507 ILE n 
1 4508 HIS n 
1 4509 VAL n 
1 4510 CYS n 
1 4511 LEU n 
1 4512 GLY n 
1 4513 GLY n 
1 4514 LEU n 
1 4515 PHE n 
1 4516 VAL n 
1 4517 PRO n 
1 4518 GLU n 
1 4519 ALA n 
1 4520 TYR n 
1 4521 ILE n 
1 4522 THR n 
1 4523 ALA n 
1 4524 THR n 
1 4525 ARG n 
1 4526 GLN n 
1 4527 TYR n 
1 4528 VAL n 
1 4529 ALA n 
1 4530 GLN n 
1 4531 ALA n 
1 4532 ASN n 
1 4533 SER n 
1 4534 TRP n 
1 4535 SER n 
1 4536 LEU n 
1 4537 GLU n 
1 4538 GLU n 
1 4539 LEU n 
1 4540 CYS n 
1 4541 LEU n 
1 4542 GLU n 
1 4543 VAL n 
1 4544 ASN n 
1 4545 VAL n 
1 4546 THR n 
1 4547 THR n 
1 4548 SER n 
1 4549 GLN n 
1 4550 GLY n 
1 4551 ALA n 
1 4552 THR n 
1 4553 LEU n 
1 4554 ASP n 
1 4555 ALA n 
1 4556 CYS n 
1 4557 SER n 
1 4558 PHE n 
1 4559 GLY n 
1 4560 VAL n 
1 4561 THR n 
1 4562 GLY n 
1 4563 LEU n 
1 4564 LYS n 
1 4565 LEU n 
1 4566 GLN n 
1 4567 GLY n 
1 4568 ALA n 
1 4569 THR n 
1 4570 CYS n 
1 4571 ASN n 
1 4572 ASN n 
1 4573 ASN n 
1 4574 LYS n 
1 4575 LEU n 
1 4576 SER n 
1 4577 LEU n 
1 4578 SER n 
1 4579 ASN n 
1 4580 ALA n 
1 4581 ILE n 
1 4582 SER n 
1 4583 THR n 
1 4584 ALA n 
1 4585 LEU n 
1 4586 PRO n 
1 4587 LEU n 
1 4588 THR n 
1 4589 GLN n 
1 4590 LEU n 
1 4591 ARG n 
1 4592 TRP n 
1 4593 VAL n 
1 4594 LYS n 
1 4595 GLN n 
1 4596 THR n 
1 4597 ASN n 
1 4598 THR n 
1 4599 GLU n 
1 4600 LYS n 
1 4601 LYS n 
1 4602 ALA n 
1 4603 SER n 
1 4604 VAL n 
1 4605 VAL n 
1 4606 THR n 
1 4607 LEU n 
1 4608 PRO n 
1 4609 VAL n 
1 4610 TYR n 
1 4611 LEU n 
1 4612 ASN n 
1 4613 PHE n 
1 4614 THR n 
1 4615 ARG n 
1 4616 ALA n 
1 4617 ASP n 
1 4618 LEU n 
1 4619 ILE n 
1 4620 PHE n 
1 4621 THR n 
1 4622 VAL n 
1 4623 ASP n 
1 4624 PHE n 
1 4625 GLU n 
1 4626 ILE n 
1 4627 ALA n 
1 4628 THR n 
1 4629 LYS n 
1 4630 GLU n 
1 4631 ASP n 
1 4632 PRO n 
1 4633 ARG n 
1 4634 SER n 
1 4635 PHE n 
1 4636 TYR n 
1 4637 GLU n 
1 4638 ARG n 
1 4639 GLY n 
1 4640 VAL n 
1 4641 ALA n 
1 4642 VAL n 
1 4643 LEU n 
1 4644 CYS n 
1 4645 THR n 
1 4646 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   4646 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ? 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                      ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    PRO 4    4    ?    ?   ?   A . n 
A 1 5    GLY 5    5    ?    ?   ?   A . n 
A 1 6    GLY 6    6    ?    ?   ?   A . n 
A 1 7    GLY 7    7    ?    ?   ?   A . n 
A 1 8    GLY 8    8    ?    ?   ?   A . n 
A 1 9    GLY 9    9    ?    ?   ?   A . n 
A 1 10   GLU 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   SER 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLY 15   15   ?    ?   ?   A . n 
A 1 16   LEU 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   SER 19   19   ?    ?   ?   A . n 
A 1 20   ALA 20   20   ?    ?   ?   A . n 
A 1 21   VAL 21   21   ?    ?   ?   A . n 
A 1 22   GLN 22   22   ?    ?   ?   A . n 
A 1 23   ASN 23   23   ?    ?   ?   A . n 
A 1 24   VAL 24   24   ?    ?   ?   A . n 
A 1 25   ALA 25   25   ?    ?   ?   A . n 
A 1 26   ASP 26   26   ?    ?   ?   A . n 
A 1 27   VAL 27   27   ?    ?   ?   A . n 
A 1 28   SER 28   28   ?    ?   ?   A . n 
A 1 29   VAL 29   29   ?    ?   ?   A . n 
A 1 30   LEU 30   30   ?    ?   ?   A . n 
A 1 31   GLN 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   HIS 33   33   ?    ?   ?   A . n 
A 1 34   LEU 34   34   ?    ?   ?   A . n 
A 1 35   ARG 35   35   ?    ?   ?   A . n 
A 1 36   LYS 36   36   ?    ?   ?   A . n 
A 1 37   LEU 37   37   ?    ?   ?   A . n 
A 1 38   VAL 38   38   ?    ?   ?   A . n 
A 1 39   PRO 39   39   ?    ?   ?   A . n 
A 1 40   LEU 40   40   ?    ?   ?   A . n 
A 1 41   LEU 41   41   ?    ?   ?   A . n 
A 1 42   LEU 42   42   ?    ?   ?   A . n 
A 1 43   GLU 43   43   ?    ?   ?   A . n 
A 1 44   ASP 44   44   ?    ?   ?   A . n 
A 1 45   GLY 45   45   ?    ?   ?   A . n 
A 1 46   GLY 46   46   ?    ?   ?   A . n 
A 1 47   GLU 47   47   ?    ?   ?   A . n 
A 1 48   ALA 48   48   ?    ?   ?   A . n 
A 1 49   PRO 49   49   ?    ?   ?   A . n 
A 1 50   ALA 50   50   ?    ?   ?   A . n 
A 1 51   ALA 51   51   ?    ?   ?   A . n 
A 1 52   LEU 52   52   ?    ?   ?   A . n 
A 1 53   GLU 53   53   ?    ?   ?   A . n 
A 1 54   ALA 54   54   ?    ?   ?   A . n 
A 1 55   ALA 55   55   ?    ?   ?   A . n 
A 1 56   LEU 56   56   ?    ?   ?   A . n 
A 1 57   GLU 57   57   ?    ?   ?   A . n 
A 1 58   GLU 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   SER 60   60   ?    ?   ?   A . n 
A 1 61   ALA 61   61   ?    ?   ?   A . n 
A 1 62   LEU 62   62   ?    ?   ?   A . n 
A 1 63   GLU 63   63   ?    ?   ?   A . n 
A 1 64   GLN 64   64   ?    ?   ?   A . n 
A 1 65   MET 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   LYS 67   67   ?    ?   ?   A . n 
A 1 68   PHE 68   68   ?    ?   ?   A . n 
A 1 69   LEU 69   69   ?    ?   ?   A . n 
A 1 70   SER 70   70   ?    ?   ?   A . n 
A 1 71   ASP 71   71   ?    ?   ?   A . n 
A 1 72   PRO 72   72   ?    ?   ?   A . n 
A 1 73   GLN 73   73   ?    ?   ?   A . n 
A 1 74   VAL 74   74   ?    ?   ?   A . n 
A 1 75   HIS 75   75   ?    ?   ?   A . n 
A 1 76   THR 76   76   ?    ?   ?   A . n 
A 1 77   VAL 77   77   ?    ?   ?   A . n 
A 1 78   LEU 78   78   ?    ?   ?   A . n 
A 1 79   VAL 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   ARG 81   81   ?    ?   ?   A . n 
A 1 82   SER 82   82   ?    ?   ?   A . n 
A 1 83   THR 83   83   ?    ?   ?   A . n 
A 1 84   LEU 84   84   ?    ?   ?   A . n 
A 1 85   LYS 85   85   ?    ?   ?   A . n 
A 1 86   GLU 86   86   ?    ?   ?   A . n 
A 1 87   ASP 87   87   ?    ?   ?   A . n 
A 1 88   VAL 88   88   ?    ?   ?   A . n 
A 1 89   GLY 89   89   ?    ?   ?   A . n 
A 1 90   ASP 90   90   ?    ?   ?   A . n 
A 1 91   GLU 91   91   ?    ?   ?   A . n 
A 1 92   GLY 92   92   ?    ?   ?   A . n 
A 1 93   GLU 93   93   ?    ?   ?   A . n 
A 1 94   GLU 94   94   ?    ?   ?   A . n 
A 1 95   GLU 95   95   ?    ?   ?   A . n 
A 1 96   LYS 96   96   ?    ?   ?   A . n 
A 1 97   GLU 97   97   ?    ?   ?   A . n 
A 1 98   PHE 98   98   ?    ?   ?   A . n 
A 1 99   ILE 99   99   ?    ?   ?   A . n 
A 1 100  SER 100  100  ?    ?   ?   A . n 
A 1 101  TYR 101  101  ?    ?   ?   A . n 
A 1 102  ASN 102  102  ?    ?   ?   A . n 
A 1 103  ILE 103  103  ?    ?   ?   A . n 
A 1 104  ASN 104  104  ?    ?   ?   A . n 
A 1 105  ILE 105  105  ?    ?   ?   A . n 
A 1 106  ASP 106  106  ?    ?   ?   A . n 
A 1 107  ILE 107  107  ?    ?   ?   A . n 
A 1 108  HIS 108  108  ?    ?   ?   A . n 
A 1 109  TYR 109  109  ?    ?   ?   A . n 
A 1 110  GLY 110  110  ?    ?   ?   A . n 
A 1 111  VAL 111  111  ?    ?   ?   A . n 
A 1 112  LYS 112  112  ?    ?   ?   A . n 
A 1 113  SER 113  113  ?    ?   ?   A . n 
A 1 114  ASN 114  114  ?    ?   ?   A . n 
A 1 115  SER 115  115  ?    ?   ?   A . n 
A 1 116  LEU 116  116  ?    ?   ?   A . n 
A 1 117  ALA 117  117  ?    ?   ?   A . n 
A 1 118  PHE 118  118  ?    ?   ?   A . n 
A 1 119  ILE 119  119  ?    ?   ?   A . n 
A 1 120  LYS 120  120  ?    ?   ?   A . n 
A 1 121  ARG 121  121  ?    ?   ?   A . n 
A 1 122  THR 122  122  ?    ?   ?   A . n 
A 1 123  PRO 123  123  ?    ?   ?   A . n 
A 1 124  VAL 124  124  ?    ?   ?   A . n 
A 1 125  ILE 125  125  ?    ?   ?   A . n 
A 1 126  ASP 126  126  ?    ?   ?   A . n 
A 1 127  ALA 127  127  ?    ?   ?   A . n 
A 1 128  ASP 128  128  ?    ?   ?   A . n 
A 1 129  LYS 129  129  ?    ?   ?   A . n 
A 1 130  PRO 130  130  ?    ?   ?   A . n 
A 1 131  VAL 131  131  ?    ?   ?   A . n 
A 1 132  SER 132  132  ?    ?   ?   A . n 
A 1 133  SER 133  133  ?    ?   ?   A . n 
A 1 134  GLN 134  134  ?    ?   ?   A . n 
A 1 135  LEU 135  135  ?    ?   ?   A . n 
A 1 136  ARG 136  136  ?    ?   ?   A . n 
A 1 137  VAL 137  137  ?    ?   ?   A . n 
A 1 138  LEU 138  138  ?    ?   ?   A . n 
A 1 139  THR 139  139  ?    ?   ?   A . n 
A 1 140  LEU 140  140  ?    ?   ?   A . n 
A 1 141  SER 141  141  ?    ?   ?   A . n 
A 1 142  GLU 142  142  ?    ?   ?   A . n 
A 1 143  ASP 143  143  ?    ?   ?   A . n 
A 1 144  SER 144  144  ?    ?   ?   A . n 
A 1 145  PRO 145  145  ?    ?   ?   A . n 
A 1 146  TYR 146  146  ?    ?   ?   A . n 
A 1 147  GLU 147  147  ?    ?   ?   A . n 
A 1 148  THR 148  148  ?    ?   ?   A . n 
A 1 149  LEU 149  149  ?    ?   ?   A . n 
A 1 150  HIS 150  150  ?    ?   ?   A . n 
A 1 151  SER 151  151  ?    ?   ?   A . n 
A 1 152  PHE 152  152  ?    ?   ?   A . n 
A 1 153  ILE 153  153  ?    ?   ?   A . n 
A 1 154  SER 154  154  ?    ?   ?   A . n 
A 1 155  ASN 155  155  ?    ?   ?   A . n 
A 1 156  ALA 156  156  ?    ?   ?   A . n 
A 1 157  VAL 157  157  ?    ?   ?   A . n 
A 1 158  ALA 158  158  ?    ?   ?   A . n 
A 1 159  PRO 159  159  ?    ?   ?   A . n 
A 1 160  PHE 160  160  ?    ?   ?   A . n 
A 1 161  PHE 161  161  ?    ?   ?   A . n 
A 1 162  LYS 162  162  ?    ?   ?   A . n 
A 1 163  SER 163  163  ?    ?   ?   A . n 
A 1 164  TYR 164  164  ?    ?   ?   A . n 
A 1 165  ILE 165  165  ?    ?   ?   A . n 
A 1 166  ARG 166  166  ?    ?   ?   A . n 
A 1 167  GLU 167  167  ?    ?   ?   A . n 
A 1 168  SER 168  168  ?    ?   ?   A . n 
A 1 169  GLY 169  169  ?    ?   ?   A . n 
A 1 170  LYS 170  170  ?    ?   ?   A . n 
A 1 171  ALA 171  171  ?    ?   ?   A . n 
A 1 172  ASP 172  172  ?    ?   ?   A . n 
A 1 173  ARG 173  173  ?    ?   ?   A . n 
A 1 174  ASP 174  174  ?    ?   ?   A . n 
A 1 175  GLY 175  175  ?    ?   ?   A . n 
A 1 176  ASP 176  176  ?    ?   ?   A . n 
A 1 177  LYS 177  177  ?    ?   ?   A . n 
A 1 178  MET 178  178  ?    ?   ?   A . n 
A 1 179  ALA 179  179  ?    ?   ?   A . n 
A 1 180  PRO 180  180  ?    ?   ?   A . n 
A 1 181  SER 181  181  ?    ?   ?   A . n 
A 1 182  VAL 182  182  ?    ?   ?   A . n 
A 1 183  GLU 183  183  ?    ?   ?   A . n 
A 1 184  LYS 184  184  ?    ?   ?   A . n 
A 1 185  LYS 185  185  ?    ?   ?   A . n 
A 1 186  ILE 186  186  ?    ?   ?   A . n 
A 1 187  ALA 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  LEU 189  189  ?    ?   ?   A . n 
A 1 190  GLU 190  190  ?    ?   ?   A . n 
A 1 191  MET 191  191  ?    ?   ?   A . n 
A 1 192  GLY 192  192  ?    ?   ?   A . n 
A 1 193  LEU 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  HIS 195  195  ?    ?   ?   A . n 
A 1 196  LEU 196  196  ?    ?   ?   A . n 
A 1 197  GLN 197  197  ?    ?   ?   A . n 
A 1 198  GLN 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  ILE 200  200  ?    ?   ?   A . n 
A 1 201  GLU 201  201  ?    ?   ?   A . n 
A 1 202  ILE 202  202  ?    ?   ?   A . n 
A 1 203  PRO 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  ILE 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  LEU 207  207  ?    ?   ?   A . n 
A 1 208  PRO 208  208  ?    ?   ?   A . n 
A 1 209  ILE 209  209  ?    ?   ?   A . n 
A 1 210  HIS 210  210  ?    ?   ?   A . n 
A 1 211  PRO 211  211  ?    ?   ?   A . n 
A 1 212  MET 212  212  ?    ?   ?   A . n 
A 1 213  ILE 213  213  ?    ?   ?   A . n 
A 1 214  THR 214  214  ?    ?   ?   A . n 
A 1 215  ASN 215  215  ?    ?   ?   A . n 
A 1 216  VAL 216  216  ?    ?   ?   A . n 
A 1 217  ALA 217  217  ?    ?   ?   A . n 
A 1 218  LYS 218  218  ?    ?   ?   A . n 
A 1 219  GLN 219  219  ?    ?   ?   A . n 
A 1 220  CYS 220  220  ?    ?   ?   A . n 
A 1 221  TYR 221  221  ?    ?   ?   A . n 
A 1 222  GLU 222  222  ?    ?   ?   A . n 
A 1 223  ARG 223  223  ?    ?   ?   A . n 
A 1 224  GLY 224  224  ?    ?   ?   A . n 
A 1 225  GLU 225  225  ?    ?   ?   A . n 
A 1 226  LYS 226  226  ?    ?   ?   A . n 
A 1 227  PRO 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  VAL 229  229  ?    ?   ?   A . n 
A 1 230  THR 230  230  ?    ?   ?   A . n 
A 1 231  ASP 231  231  ?    ?   ?   A . n 
A 1 232  PHE 232  232  ?    ?   ?   A . n 
A 1 233  GLY 233  233  ?    ?   ?   A . n 
A 1 234  ASP 234  234  ?    ?   ?   A . n 
A 1 235  LYS 235  235  ?    ?   ?   A . n 
A 1 236  VAL 236  236  ?    ?   ?   A . n 
A 1 237  GLU 237  237  ?    ?   ?   A . n 
A 1 238  ASP 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  THR 240  240  ?    ?   ?   A . n 
A 1 241  PHE 241  241  ?    ?   ?   A . n 
A 1 242  LEU 242  242  ?    ?   ?   A . n 
A 1 243  ASN 243  243  ?    ?   ?   A . n 
A 1 244  GLN 244  244  ?    ?   ?   A . n 
A 1 245  LEU 245  245  ?    ?   ?   A . n 
A 1 246  GLN 246  246  ?    ?   ?   A . n 
A 1 247  SER 247  247  ?    ?   ?   A . n 
A 1 248  GLY 248  248  ?    ?   ?   A . n 
A 1 249  VAL 249  249  ?    ?   ?   A . n 
A 1 250  ASN 250  250  ?    ?   ?   A . n 
A 1 251  ARG 251  251  ?    ?   ?   A . n 
A 1 252  TRP 252  252  ?    ?   ?   A . n 
A 1 253  ILE 253  253  ?    ?   ?   A . n 
A 1 254  ARG 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  ILE 256  256  ?    ?   ?   A . n 
A 1 257  GLN 257  257  ?    ?   ?   A . n 
A 1 258  LYS 258  258  ?    ?   ?   A . n 
A 1 259  VAL 259  259  ?    ?   ?   A . n 
A 1 260  THR 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  LEU 262  262  ?    ?   ?   A . n 
A 1 263  ASP 263  263  ?    ?   ?   A . n 
A 1 264  ARG 264  264  ?    ?   ?   A . n 
A 1 265  ASP 265  265  ?    ?   ?   A . n 
A 1 266  PRO 266  266  ?    ?   ?   A . n 
A 1 267  ALA 267  267  ?    ?   ?   A . n 
A 1 268  SER 268  268  ?    ?   ?   A . n 
A 1 269  GLY 269  269  ?    ?   ?   A . n 
A 1 270  THR 270  270  ?    ?   ?   A . n 
A 1 271  ALA 271  271  ?    ?   ?   A . n 
A 1 272  LEU 272  272  ?    ?   ?   A . n 
A 1 273  GLN 273  273  ?    ?   ?   A . n 
A 1 274  GLU 274  274  ?    ?   ?   A . n 
A 1 275  ILE 275  275  ?    ?   ?   A . n 
A 1 276  SER 276  276  ?    ?   ?   A . n 
A 1 277  PHE 277  277  ?    ?   ?   A . n 
A 1 278  TRP 278  278  ?    ?   ?   A . n 
A 1 279  LEU 279  279  ?    ?   ?   A . n 
A 1 280  ASN 280  280  ?    ?   ?   A . n 
A 1 281  LEU 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ARG 283  283  ?    ?   ?   A . n 
A 1 284  ALA 284  284  ?    ?   ?   A . n 
A 1 285  LEU 285  285  ?    ?   ?   A . n 
A 1 286  TYR 286  286  ?    ?   ?   A . n 
A 1 287  ARG 287  287  ?    ?   ?   A . n 
A 1 288  ILE 288  288  ?    ?   ?   A . n 
A 1 289  GLN 289  289  ?    ?   ?   A . n 
A 1 290  GLU 290  290  ?    ?   ?   A . n 
A 1 291  LYS 291  291  ?    ?   ?   A . n 
A 1 292  ARG 292  292  ?    ?   ?   A . n 
A 1 293  GLU 293  293  ?    ?   ?   A . n 
A 1 294  SER 294  294  ?    ?   ?   A . n 
A 1 295  PRO 295  295  ?    ?   ?   A . n 
A 1 296  GLU 296  296  ?    ?   ?   A . n 
A 1 297  VAL 297  297  ?    ?   ?   A . n 
A 1 298  LEU 298  298  ?    ?   ?   A . n 
A 1 299  LEU 299  299  ?    ?   ?   A . n 
A 1 300  THR 300  300  ?    ?   ?   A . n 
A 1 301  LEU 301  301  ?    ?   ?   A . n 
A 1 302  ASP 302  302  ?    ?   ?   A . n 
A 1 303  ILE 303  303  ?    ?   ?   A . n 
A 1 304  LEU 304  304  ?    ?   ?   A . n 
A 1 305  LYS 305  305  ?    ?   ?   A . n 
A 1 306  HIS 306  306  ?    ?   ?   A . n 
A 1 307  GLY 307  307  ?    ?   ?   A . n 
A 1 308  LYS 308  308  ?    ?   ?   A . n 
A 1 309  ARG 309  309  ?    ?   ?   A . n 
A 1 310  PHE 310  310  ?    ?   ?   A . n 
A 1 311  HIS 311  311  ?    ?   ?   A . n 
A 1 312  ALA 312  312  ?    ?   ?   A . n 
A 1 313  THR 313  313  ?    ?   ?   A . n 
A 1 314  VAL 314  314  ?    ?   ?   A . n 
A 1 315  SER 315  315  ?    ?   ?   A . n 
A 1 316  PHE 316  316  ?    ?   ?   A . n 
A 1 317  ASP 317  317  ?    ?   ?   A . n 
A 1 318  THR 318  318  ?    ?   ?   A . n 
A 1 319  ASP 319  319  ?    ?   ?   A . n 
A 1 320  THR 320  320  ?    ?   ?   A . n 
A 1 321  GLY 321  321  ?    ?   ?   A . n 
A 1 322  LEU 322  322  ?    ?   ?   A . n 
A 1 323  LYS 323  323  ?    ?   ?   A . n 
A 1 324  GLN 324  324  ?    ?   ?   A . n 
A 1 325  ALA 325  325  ?    ?   ?   A . n 
A 1 326  LEU 326  326  ?    ?   ?   A . n 
A 1 327  GLU 327  327  ?    ?   ?   A . n 
A 1 328  THR 328  328  ?    ?   ?   A . n 
A 1 329  VAL 329  329  ?    ?   ?   A . n 
A 1 330  ASN 330  330  ?    ?   ?   A . n 
A 1 331  ASP 331  331  ?    ?   ?   A . n 
A 1 332  TYR 332  332  ?    ?   ?   A . n 
A 1 333  ASN 333  333  ?    ?   ?   A . n 
A 1 334  PRO 334  334  ?    ?   ?   A . n 
A 1 335  LEU 335  335  ?    ?   ?   A . n 
A 1 336  MET 336  336  ?    ?   ?   A . n 
A 1 337  LYS 337  337  ?    ?   ?   A . n 
A 1 338  ASP 338  338  ?    ?   ?   A . n 
A 1 339  PHE 339  339  ?    ?   ?   A . n 
A 1 340  PRO 340  340  ?    ?   ?   A . n 
A 1 341  LEU 341  341  ?    ?   ?   A . n 
A 1 342  ASN 342  342  ?    ?   ?   A . n 
A 1 343  ASP 343  343  ?    ?   ?   A . n 
A 1 344  LEU 344  344  ?    ?   ?   A . n 
A 1 345  LEU 345  345  ?    ?   ?   A . n 
A 1 346  SER 346  346  ?    ?   ?   A . n 
A 1 347  ALA 347  347  ?    ?   ?   A . n 
A 1 348  THR 348  348  ?    ?   ?   A . n 
A 1 349  GLU 349  349  ?    ?   ?   A . n 
A 1 350  LEU 350  350  ?    ?   ?   A . n 
A 1 351  ASP 351  351  ?    ?   ?   A . n 
A 1 352  LYS 352  352  ?    ?   ?   A . n 
A 1 353  ILE 353  353  ?    ?   ?   A . n 
A 1 354  ARG 354  354  ?    ?   ?   A . n 
A 1 355  GLN 355  355  ?    ?   ?   A . n 
A 1 356  ALA 356  356  ?    ?   ?   A . n 
A 1 357  LEU 357  357  ?    ?   ?   A . n 
A 1 358  VAL 358  358  ?    ?   ?   A . n 
A 1 359  ALA 359  359  ?    ?   ?   A . n 
A 1 360  ILE 360  360  ?    ?   ?   A . n 
A 1 361  PHE 361  361  ?    ?   ?   A . n 
A 1 362  THR 362  362  ?    ?   ?   A . n 
A 1 363  HIS 363  363  ?    ?   ?   A . n 
A 1 364  LEU 364  364  ?    ?   ?   A . n 
A 1 365  ARG 365  365  ?    ?   ?   A . n 
A 1 366  LYS 366  366  ?    ?   ?   A . n 
A 1 367  ILE 367  367  ?    ?   ?   A . n 
A 1 368  ARG 368  368  ?    ?   ?   A . n 
A 1 369  ASN 369  369  ?    ?   ?   A . n 
A 1 370  THR 370  370  ?    ?   ?   A . n 
A 1 371  LYS 371  371  ?    ?   ?   A . n 
A 1 372  TYR 372  372  ?    ?   ?   A . n 
A 1 373  PRO 373  373  ?    ?   ?   A . n 
A 1 374  ILE 374  374  ?    ?   ?   A . n 
A 1 375  GLN 375  375  ?    ?   ?   A . n 
A 1 376  ARG 376  376  ?    ?   ?   A . n 
A 1 377  ALA 377  377  ?    ?   ?   A . n 
A 1 378  LEU 378  378  ?    ?   ?   A . n 
A 1 379  ARG 379  379  ?    ?   ?   A . n 
A 1 380  LEU 380  380  ?    ?   ?   A . n 
A 1 381  VAL 381  381  ?    ?   ?   A . n 
A 1 382  GLU 382  382  ?    ?   ?   A . n 
A 1 383  ALA 383  383  ?    ?   ?   A . n 
A 1 384  ILE 384  384  ?    ?   ?   A . n 
A 1 385  SER 385  385  ?    ?   ?   A . n 
A 1 386  ARG 386  386  ?    ?   ?   A . n 
A 1 387  ASP 387  387  ?    ?   ?   A . n 
A 1 388  LEU 388  388  ?    ?   ?   A . n 
A 1 389  SER 389  389  ?    ?   ?   A . n 
A 1 390  SER 390  390  ?    ?   ?   A . n 
A 1 391  GLN 391  391  ?    ?   ?   A . n 
A 1 392  LEU 392  392  ?    ?   ?   A . n 
A 1 393  LEU 393  393  ?    ?   ?   A . n 
A 1 394  LYS 394  394  ?    ?   ?   A . n 
A 1 395  VAL 395  395  ?    ?   ?   A . n 
A 1 396  LEU 396  396  ?    ?   ?   A . n 
A 1 397  GLY 397  397  ?    ?   ?   A . n 
A 1 398  THR 398  398  ?    ?   ?   A . n 
A 1 399  ARG 399  399  ?    ?   ?   A . n 
A 1 400  LYS 400  400  ?    ?   ?   A . n 
A 1 401  LEU 401  401  ?    ?   ?   A . n 
A 1 402  MET 402  402  ?    ?   ?   A . n 
A 1 403  HIS 403  403  ?    ?   ?   A . n 
A 1 404  VAL 404  404  ?    ?   ?   A . n 
A 1 405  ALA 405  405  ?    ?   ?   A . n 
A 1 406  TYR 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  GLU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  VAL 412  412  ?    ?   ?   A . n 
A 1 413  MET 413  413  ?    ?   ?   A . n 
A 1 414  VAL 414  414  ?    ?   ?   A . n 
A 1 415  ALA 415  415  ?    ?   ?   A . n 
A 1 416  CYS 416  416  ?    ?   ?   A . n 
A 1 417  PHE 417  417  ?    ?   ?   A . n 
A 1 418  GLU 418  418  ?    ?   ?   A . n 
A 1 419  VAL 419  419  ?    ?   ?   A . n 
A 1 420  PHE 420  420  ?    ?   ?   A . n 
A 1 421  GLN 421  421  ?    ?   ?   A . n 
A 1 422  THR 422  422  ?    ?   ?   A . n 
A 1 423  TRP 423  423  ?    ?   ?   A . n 
A 1 424  ASP 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  GLU 426  426  ?    ?   ?   A . n 
A 1 427  TYR 427  427  ?    ?   ?   A . n 
A 1 428  GLU 428  428  ?    ?   ?   A . n 
A 1 429  LYS 429  429  ?    ?   ?   A . n 
A 1 430  LEU 430  430  ?    ?   ?   A . n 
A 1 431  GLN 431  431  ?    ?   ?   A . n 
A 1 432  VAL 432  432  ?    ?   ?   A . n 
A 1 433  LEU 433  433  ?    ?   ?   A . n 
A 1 434  LEU 434  434  ?    ?   ?   A . n 
A 1 435  ARG 435  435  ?    ?   ?   A . n 
A 1 436  ASP 436  436  ?    ?   ?   A . n 
A 1 437  ILE 437  437  ?    ?   ?   A . n 
A 1 438  VAL 438  438  ?    ?   ?   A . n 
A 1 439  LYS 439  439  ?    ?   ?   A . n 
A 1 440  ARG 440  440  ?    ?   ?   A . n 
A 1 441  LYS 441  441  ?    ?   ?   A . n 
A 1 442  ARG 442  442  ?    ?   ?   A . n 
A 1 443  GLU 443  443  ?    ?   ?   A . n 
A 1 444  GLU 444  444  ?    ?   ?   A . n 
A 1 445  ASN 445  445  ?    ?   ?   A . n 
A 1 446  LEU 446  446  ?    ?   ?   A . n 
A 1 447  LYS 447  447  ?    ?   ?   A . n 
A 1 448  MET 448  448  ?    ?   ?   A . n 
A 1 449  VAL 449  449  ?    ?   ?   A . n 
A 1 450  TRP 450  450  ?    ?   ?   A . n 
A 1 451  ARG 451  451  ?    ?   ?   A . n 
A 1 452  ILE 452  452  ?    ?   ?   A . n 
A 1 453  ASN 453  453  ?    ?   ?   A . n 
A 1 454  PRO 454  454  ?    ?   ?   A . n 
A 1 455  ALA 455  455  ?    ?   ?   A . n 
A 1 456  HIS 456  456  ?    ?   ?   A . n 
A 1 457  ARG 457  457  ?    ?   ?   A . n 
A 1 458  LYS 458  458  ?    ?   ?   A . n 
A 1 459  LEU 459  459  ?    ?   ?   A . n 
A 1 460  GLN 460  460  ?    ?   ?   A . n 
A 1 461  ALA 461  461  ?    ?   ?   A . n 
A 1 462  ARG 462  462  ?    ?   ?   A . n 
A 1 463  LEU 463  463  ?    ?   ?   A . n 
A 1 464  ASP 464  464  ?    ?   ?   A . n 
A 1 465  GLN 465  465  ?    ?   ?   A . n 
A 1 466  MET 466  466  ?    ?   ?   A . n 
A 1 467  ARG 467  467  ?    ?   ?   A . n 
A 1 468  LYS 468  468  ?    ?   ?   A . n 
A 1 469  PHE 469  469  ?    ?   ?   A . n 
A 1 470  ARG 470  470  ?    ?   ?   A . n 
A 1 471  ARG 471  471  ?    ?   ?   A . n 
A 1 472  GLN 472  472  ?    ?   ?   A . n 
A 1 473  HIS 473  473  ?    ?   ?   A . n 
A 1 474  GLU 474  474  ?    ?   ?   A . n 
A 1 475  GLN 475  475  ?    ?   ?   A . n 
A 1 476  LEU 476  476  ?    ?   ?   A . n 
A 1 477  ARG 477  477  ?    ?   ?   A . n 
A 1 478  ALA 478  478  ?    ?   ?   A . n 
A 1 479  VAL 479  479  ?    ?   ?   A . n 
A 1 480  ILE 480  480  ?    ?   ?   A . n 
A 1 481  VAL 481  481  ?    ?   ?   A . n 
A 1 482  ARG 482  482  ?    ?   ?   A . n 
A 1 483  VAL 483  483  ?    ?   ?   A . n 
A 1 484  LEU 484  484  ?    ?   ?   A . n 
A 1 485  ARG 485  485  ?    ?   ?   A . n 
A 1 486  PRO 486  486  ?    ?   ?   A . n 
A 1 487  GLN 487  487  ?    ?   ?   A . n 
A 1 488  VAL 488  488  ?    ?   ?   A . n 
A 1 489  THR 489  489  ?    ?   ?   A . n 
A 1 490  ALA 490  490  ?    ?   ?   A . n 
A 1 491  VAL 491  491  ?    ?   ?   A . n 
A 1 492  ALA 492  492  ?    ?   ?   A . n 
A 1 493  GLN 493  493  ?    ?   ?   A . n 
A 1 494  GLN 494  494  ?    ?   ?   A . n 
A 1 495  ASN 495  495  ?    ?   ?   A . n 
A 1 496  GLN 496  496  ?    ?   ?   A . n 
A 1 497  GLY 497  497  ?    ?   ?   A . n 
A 1 498  GLU 498  498  ?    ?   ?   A . n 
A 1 499  VAL 499  499  ?    ?   ?   A . n 
A 1 500  PRO 500  500  ?    ?   ?   A . n 
A 1 501  GLU 501  501  ?    ?   ?   A . n 
A 1 502  PRO 502  502  ?    ?   ?   A . n 
A 1 503  GLN 503  503  ?    ?   ?   A . n 
A 1 504  ASP 504  504  ?    ?   ?   A . n 
A 1 505  MET 505  505  ?    ?   ?   A . n 
A 1 506  LYS 506  506  ?    ?   ?   A . n 
A 1 507  VAL 507  507  ?    ?   ?   A . n 
A 1 508  ALA 508  508  ?    ?   ?   A . n 
A 1 509  GLU 509  509  ?    ?   ?   A . n 
A 1 510  VAL 510  510  ?    ?   ?   A . n 
A 1 511  LEU 511  511  ?    ?   ?   A . n 
A 1 512  PHE 512  512  ?    ?   ?   A . n 
A 1 513  ASP 513  513  ?    ?   ?   A . n 
A 1 514  ALA 514  514  ?    ?   ?   A . n 
A 1 515  ALA 515  515  ?    ?   ?   A . n 
A 1 516  ASP 516  516  ?    ?   ?   A . n 
A 1 517  ALA 517  517  ?    ?   ?   A . n 
A 1 518  ASN 518  518  ?    ?   ?   A . n 
A 1 519  ALA 519  519  ?    ?   ?   A . n 
A 1 520  ILE 520  520  ?    ?   ?   A . n 
A 1 521  GLU 521  521  ?    ?   ?   A . n 
A 1 522  GLU 522  522  ?    ?   ?   A . n 
A 1 523  VAL 523  523  ?    ?   ?   A . n 
A 1 524  ASN 524  524  ?    ?   ?   A . n 
A 1 525  LEU 525  525  ?    ?   ?   A . n 
A 1 526  ALA 526  526  ?    ?   ?   A . n 
A 1 527  TYR 527  527  ?    ?   ?   A . n 
A 1 528  GLU 528  528  ?    ?   ?   A . n 
A 1 529  ASN 529  529  ?    ?   ?   A . n 
A 1 530  VAL 530  530  ?    ?   ?   A . n 
A 1 531  LYS 531  531  ?    ?   ?   A . n 
A 1 532  GLU 532  532  ?    ?   ?   A . n 
A 1 533  VAL 533  533  ?    ?   ?   A . n 
A 1 534  ASP 534  534  ?    ?   ?   A . n 
A 1 535  GLY 535  535  ?    ?   ?   A . n 
A 1 536  LEU 536  536  ?    ?   ?   A . n 
A 1 537  ASP 537  537  ?    ?   ?   A . n 
A 1 538  VAL 538  538  ?    ?   ?   A . n 
A 1 539  SER 539  539  ?    ?   ?   A . n 
A 1 540  LYS 540  540  ?    ?   ?   A . n 
A 1 541  GLU 541  541  ?    ?   ?   A . n 
A 1 542  GLY 542  542  ?    ?   ?   A . n 
A 1 543  THR 543  543  ?    ?   ?   A . n 
A 1 544  GLU 544  544  ?    ?   ?   A . n 
A 1 545  ALA 545  545  ?    ?   ?   A . n 
A 1 546  TRP 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  ALA 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  MET 550  550  ?    ?   ?   A . n 
A 1 551  LYS 551  551  ?    ?   ?   A . n 
A 1 552  ARG 552  552  ?    ?   ?   A . n 
A 1 553  TYR 553  553  ?    ?   ?   A . n 
A 1 554  ASP 554  554  ?    ?   ?   A . n 
A 1 555  GLU 555  555  ?    ?   ?   A . n 
A 1 556  ARG 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASP 558  558  ?    ?   ?   A . n 
A 1 559  ARG 559  559  ?    ?   ?   A . n 
A 1 560  VAL 560  560  ?    ?   ?   A . n 
A 1 561  GLU 561  561  ?    ?   ?   A . n 
A 1 562  THR 562  562  ?    ?   ?   A . n 
A 1 563  ARG 563  563  ?    ?   ?   A . n 
A 1 564  ILE 564  564  ?    ?   ?   A . n 
A 1 565  THR 565  565  ?    ?   ?   A . n 
A 1 566  ALA 566  566  ?    ?   ?   A . n 
A 1 567  ARG 567  567  ?    ?   ?   A . n 
A 1 568  LEU 568  568  ?    ?   ?   A . n 
A 1 569  ARG 569  569  ?    ?   ?   A . n 
A 1 570  ASP 570  570  ?    ?   ?   A . n 
A 1 571  GLN 571  571  ?    ?   ?   A . n 
A 1 572  LEU 572  572  ?    ?   ?   A . n 
A 1 573  GLY 573  573  ?    ?   ?   A . n 
A 1 574  THR 574  574  ?    ?   ?   A . n 
A 1 575  ALA 575  575  ?    ?   ?   A . n 
A 1 576  LYS 576  576  ?    ?   ?   A . n 
A 1 577  ASN 577  577  ?    ?   ?   A . n 
A 1 578  ALA 578  578  ?    ?   ?   A . n 
A 1 579  ASN 579  579  ?    ?   ?   A . n 
A 1 580  GLU 580  580  ?    ?   ?   A . n 
A 1 581  MET 581  581  ?    ?   ?   A . n 
A 1 582  PHE 582  582  ?    ?   ?   A . n 
A 1 583  ARG 583  583  ?    ?   ?   A . n 
A 1 584  ILE 584  584  ?    ?   ?   A . n 
A 1 585  PHE 585  585  ?    ?   ?   A . n 
A 1 586  SER 586  586  ?    ?   ?   A . n 
A 1 587  ARG 587  587  ?    ?   ?   A . n 
A 1 588  PHE 588  588  ?    ?   ?   A . n 
A 1 589  ASN 589  589  ?    ?   ?   A . n 
A 1 590  ALA 590  590  ?    ?   ?   A . n 
A 1 591  LEU 591  591  ?    ?   ?   A . n 
A 1 592  PHE 592  592  ?    ?   ?   A . n 
A 1 593  VAL 593  593  ?    ?   ?   A . n 
A 1 594  ARG 594  594  ?    ?   ?   A . n 
A 1 595  PRO 595  595  ?    ?   ?   A . n 
A 1 596  HIS 596  596  ?    ?   ?   A . n 
A 1 597  ILE 597  597  ?    ?   ?   A . n 
A 1 598  ARG 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  ALA 600  600  ?    ?   ?   A . n 
A 1 601  ILE 601  601  ?    ?   ?   A . n 
A 1 602  ARG 602  602  ?    ?   ?   A . n 
A 1 603  GLU 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  GLN 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  GLN 607  607  ?    ?   ?   A . n 
A 1 608  LEU 608  608  ?    ?   ?   A . n 
A 1 609  ILE 609  609  ?    ?   ?   A . n 
A 1 610  GLN 610  610  ?    ?   ?   A . n 
A 1 611  ARG 611  611  ?    ?   ?   A . n 
A 1 612  VAL 612  612  ?    ?   ?   A . n 
A 1 613  LYS 613  613  ?    ?   ?   A . n 
A 1 614  ASP 614  614  ?    ?   ?   A . n 
A 1 615  ASP 615  615  ?    ?   ?   A . n 
A 1 616  ILE 616  616  ?    ?   ?   A . n 
A 1 617  GLU 617  617  ?    ?   ?   A . n 
A 1 618  SER 618  618  ?    ?   ?   A . n 
A 1 619  LEU 619  619  ?    ?   ?   A . n 
A 1 620  HIS 620  620  ?    ?   ?   A . n 
A 1 621  ASP 621  621  ?    ?   ?   A . n 
A 1 622  LYS 622  622  ?    ?   ?   A . n 
A 1 623  PHE 623  623  ?    ?   ?   A . n 
A 1 624  LYS 624  624  ?    ?   ?   A . n 
A 1 625  VAL 625  625  ?    ?   ?   A . n 
A 1 626  GLN 626  626  ?    ?   ?   A . n 
A 1 627  TYR 627  627  ?    ?   ?   A . n 
A 1 628  PRO 628  628  ?    ?   ?   A . n 
A 1 629  GLN 629  629  ?    ?   ?   A . n 
A 1 630  SER 630  630  ?    ?   ?   A . n 
A 1 631  GLN 631  631  ?    ?   ?   A . n 
A 1 632  ALA 632  632  ?    ?   ?   A . n 
A 1 633  CYS 633  633  ?    ?   ?   A . n 
A 1 634  LYS 634  634  ?    ?   ?   A . n 
A 1 635  MET 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  HIS 637  637  ?    ?   ?   A . n 
A 1 638  VAL 638  638  ?    ?   ?   A . n 
A 1 639  ARG 639  639  ?    ?   ?   A . n 
A 1 640  ASP 640  640  ?    ?   ?   A . n 
A 1 641  LEU 641  641  ?    ?   ?   A . n 
A 1 642  PRO 642  642  ?    ?   ?   A . n 
A 1 643  PRO 643  643  ?    ?   ?   A . n 
A 1 644  VAL 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  ILE 648  648  ?    ?   ?   A . n 
A 1 649  ILE 649  649  ?    ?   ?   A . n 
A 1 650  TRP 650  650  ?    ?   ?   A . n 
A 1 651  ALA 651  651  ?    ?   ?   A . n 
A 1 652  LYS 652  652  ?    ?   ?   A . n 
A 1 653  GLN 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  ASP 655  655  ?    ?   ?   A . n 
A 1 656  ARG 656  656  ?    ?   ?   A . n 
A 1 657  GLN 657  657  ?    ?   ?   A . n 
A 1 658  LEU 658  658  ?    ?   ?   A . n 
A 1 659  THR 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  TYR 661  661  ?    ?   ?   A . n 
A 1 662  MET 662  662  ?    ?   ?   A . n 
A 1 663  LYS 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  VAL 665  665  ?    ?   ?   A . n 
A 1 666  GLU 666  666  ?    ?   ?   A . n 
A 1 667  ASP 667  667  ?    ?   ?   A . n 
A 1 668  VAL 668  668  ?    ?   ?   A . n 
A 1 669  LEU 669  669  ?    ?   ?   A . n 
A 1 670  GLY 670  670  ?    ?   ?   A . n 
A 1 671  LYS 671  671  ?    ?   ?   A . n 
A 1 672  GLY 672  672  ?    ?   ?   A . n 
A 1 673  TRP 673  673  ?    ?   ?   A . n 
A 1 674  GLU 674  674  ?    ?   ?   A . n 
A 1 675  ASN 675  675  ?    ?   ?   A . n 
A 1 676  HIS 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  GLU 678  678  ?    ?   ?   A . n 
A 1 679  GLY 679  679  ?    ?   ?   A . n 
A 1 680  GLN 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LEU 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  GLN 684  684  ?    ?   ?   A . n 
A 1 685  ASP 685  685  ?    ?   ?   A . n 
A 1 686  GLY 686  686  ?    ?   ?   A . n 
A 1 687  ASP 687  687  ?    ?   ?   A . n 
A 1 688  SER 688  688  ?    ?   ?   A . n 
A 1 689  PHE 689  689  ?    ?   ?   A . n 
A 1 690  ARG 690  690  ?    ?   ?   A . n 
A 1 691  MET 691  691  ?    ?   ?   A . n 
A 1 692  LYS 692  692  ?    ?   ?   A . n 
A 1 693  LEU 693  693  ?    ?   ?   A . n 
A 1 694  ASN 694  694  ?    ?   ?   A . n 
A 1 695  THR 695  695  ?    ?   ?   A . n 
A 1 696  GLN 696  696  ?    ?   ?   A . n 
A 1 697  GLU 697  697  ?    ?   ?   A . n 
A 1 698  ILE 698  698  ?    ?   ?   A . n 
A 1 699  PHE 699  699  ?    ?   ?   A . n 
A 1 700  ASP 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  TRP 702  702  ?    ?   ?   A . n 
A 1 703  ALA 703  703  ?    ?   ?   A . n 
A 1 704  ARG 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  VAL 706  706  ?    ?   ?   A . n 
A 1 707  GLN 707  707  ?    ?   ?   A . n 
A 1 708  GLN 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  ASN 710  710  ?    ?   ?   A . n 
A 1 711  LEU 711  711  ?    ?   ?   A . n 
A 1 712  GLY 712  712  ?    ?   ?   A . n 
A 1 713  VAL 713  713  ?    ?   ?   A . n 
A 1 714  SER 714  714  ?    ?   ?   A . n 
A 1 715  GLY 715  715  ?    ?   ?   A . n 
A 1 716  ARG 716  716  ?    ?   ?   A . n 
A 1 717  ILE 717  717  ?    ?   ?   A . n 
A 1 718  PHE 718  718  ?    ?   ?   A . n 
A 1 719  THR 719  719  ?    ?   ?   A . n 
A 1 720  ILE 720  720  ?    ?   ?   A . n 
A 1 721  GLU 721  721  ?    ?   ?   A . n 
A 1 722  SER 722  722  ?    ?   ?   A . n 
A 1 723  THR 723  723  ?    ?   ?   A . n 
A 1 724  ARG 724  724  ?    ?   ?   A . n 
A 1 725  VAL 725  725  ?    ?   ?   A . n 
A 1 726  ARG 726  726  ?    ?   ?   A . n 
A 1 727  GLY 727  727  ?    ?   ?   A . n 
A 1 728  ARG 728  728  ?    ?   ?   A . n 
A 1 729  THR 729  729  ?    ?   ?   A . n 
A 1 730  GLY 730  730  ?    ?   ?   A . n 
A 1 731  ASN 731  731  ?    ?   ?   A . n 
A 1 732  VAL 732  732  ?    ?   ?   A . n 
A 1 733  LEU 733  733  ?    ?   ?   A . n 
A 1 734  LYS 734  734  ?    ?   ?   A . n 
A 1 735  LEU 735  735  ?    ?   ?   A . n 
A 1 736  LYS 736  736  ?    ?   ?   A . n 
A 1 737  VAL 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  PHE 739  739  ?    ?   ?   A . n 
A 1 740  LEU 740  740  ?    ?   ?   A . n 
A 1 741  PRO 741  741  ?    ?   ?   A . n 
A 1 742  GLU 742  742  ?    ?   ?   A . n 
A 1 743  ILE 743  743  ?    ?   ?   A . n 
A 1 744  ILE 744  744  ?    ?   ?   A . n 
A 1 745  THR 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  SER 747  747  ?    ?   ?   A . n 
A 1 748  LYS 748  748  ?    ?   ?   A . n 
A 1 749  GLU 749  749  ?    ?   ?   A . n 
A 1 750  VAL 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  LYS 754  754  ?    ?   ?   A . n 
A 1 755  TRP 755  755  ?    ?   ?   A . n 
A 1 756  LEU 756  756  ?    ?   ?   A . n 
A 1 757  GLY 757  757  ?    ?   ?   A . n 
A 1 758  PHE 758  758  ?    ?   ?   A . n 
A 1 759  ARG 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  PRO 761  761  ?    ?   ?   A . n 
A 1 762  LEU 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ILE 764  764  ?    ?   ?   A . n 
A 1 765  VAL 765  765  ?    ?   ?   A . n 
A 1 766  ASN 766  766  ?    ?   ?   A . n 
A 1 767  LYS 767  767  ?    ?   ?   A . n 
A 1 768  ALA 768  768  ?    ?   ?   A . n 
A 1 769  HIS 769  769  ?    ?   ?   A . n 
A 1 770  GLN 770  770  ?    ?   ?   A . n 
A 1 771  ALA 771  771  ?    ?   ?   A . n 
A 1 772  ASN 772  772  ?    ?   ?   A . n 
A 1 773  GLN 773  773  ?    ?   ?   A . n 
A 1 774  LEU 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  PRO 776  776  ?    ?   ?   A . n 
A 1 777  PHE 777  777  ?    ?   ?   A . n 
A 1 778  ALA 778  778  ?    ?   ?   A . n 
A 1 779  ILE 779  779  ?    ?   ?   A . n 
A 1 780  SER 780  780  ?    ?   ?   A . n 
A 1 781  LEU 781  781  ?    ?   ?   A . n 
A 1 782  ILE 782  782  ?    ?   ?   A . n 
A 1 783  GLU 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  VAL 785  785  ?    ?   ?   A . n 
A 1 786  ARG 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  TYR 788  788  ?    ?   ?   A . n 
A 1 789  GLU 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  CYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  LYS 794  794  ?    ?   ?   A . n 
A 1 795  VAL 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  ARG 798  798  ?    ?   ?   A . n 
A 1 799  ASN 799  799  ?    ?   ?   A . n 
A 1 800  THR 800  800  ?    ?   ?   A . n 
A 1 801  ILE 801  801  ?    ?   ?   A . n 
A 1 802  SER 802  802  ?    ?   ?   A . n 
A 1 803  LEU 803  803  ?    ?   ?   A . n 
A 1 804  LEU 804  804  ?    ?   ?   A . n 
A 1 805  VAL 805  805  ?    ?   ?   A . n 
A 1 806  ALA 806  806  ?    ?   ?   A . n 
A 1 807  GLY 807  807  ?    ?   ?   A . n 
A 1 808  LEU 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  LYS 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  VAL 812  812  ?    ?   ?   A . n 
A 1 813  GLN 813  813  ?    ?   ?   A . n 
A 1 814  ALA 814  814  ?    ?   ?   A . n 
A 1 815  LEU 815  815  ?    ?   ?   A . n 
A 1 816  ILE 816  816  ?    ?   ?   A . n 
A 1 817  ALA 817  817  ?    ?   ?   A . n 
A 1 818  GLU 818  818  ?    ?   ?   A . n 
A 1 819  GLY 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  ?    ?   ?   A . n 
A 1 821  ALA 821  821  ?    ?   ?   A . n 
A 1 822  LEU 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  TRP 824  824  ?    ?   ?   A . n 
A 1 825  GLU 825  825  ?    ?   ?   A . n 
A 1 826  SER 826  826  ?    ?   ?   A . n 
A 1 827  TYR 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LEU 829  829  ?    ?   ?   A . n 
A 1 830  ASP 830  830  ?    ?   ?   A . n 
A 1 831  PRO 831  831  ?    ?   ?   A . n 
A 1 832  TYR 832  832  ?    ?   ?   A . n 
A 1 833  VAL 833  833  ?    ?   ?   A . n 
A 1 834  GLN 834  834  ?    ?   ?   A . n 
A 1 835  ARG 835  835  ?    ?   ?   A . n 
A 1 836  LEU 836  836  ?    ?   ?   A . n 
A 1 837  ALA 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  THR 839  839  ?    ?   ?   A . n 
A 1 840  VAL 840  840  ?    ?   ?   A . n 
A 1 841  PHE 841  841  ?    ?   ?   A . n 
A 1 842  ASN 842  842  ?    ?   ?   A . n 
A 1 843  PHE 843  843  ?    ?   ?   A . n 
A 1 844  GLN 844  844  ?    ?   ?   A . n 
A 1 845  GLU 845  845  ?    ?   ?   A . n 
A 1 846  LYS 846  846  ?    ?   ?   A . n 
A 1 847  VAL 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  ASP 849  849  ?    ?   ?   A . n 
A 1 850  LEU 850  850  ?    ?   ?   A . n 
A 1 851  LEU 851  851  ?    ?   ?   A . n 
A 1 852  ILE 852  852  ?    ?   ?   A . n 
A 1 853  ILE 853  853  ?    ?   ?   A . n 
A 1 854  GLU 854  854  ?    ?   ?   A . n 
A 1 855  GLU 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  ILE 857  857  ?    ?   ?   A . n 
A 1 858  ASP 858  858  ?    ?   ?   A . n 
A 1 859  LEU 859  859  ?    ?   ?   A . n 
A 1 860  GLU 860  860  ?    ?   ?   A . n 
A 1 861  VAL 861  861  ?    ?   ?   A . n 
A 1 862  ARG 862  862  ?    ?   ?   A . n 
A 1 863  SER 863  863  ?    ?   ?   A . n 
A 1 864  LEU 864  864  ?    ?   ?   A . n 
A 1 865  GLU 865  865  ?    ?   ?   A . n 
A 1 866  THR 866  866  ?    ?   ?   A . n 
A 1 867  CYS 867  867  ?    ?   ?   A . n 
A 1 868  MET 868  868  ?    ?   ?   A . n 
A 1 869  TYR 869  869  ?    ?   ?   A . n 
A 1 870  ASP 870  870  ?    ?   ?   A . n 
A 1 871  HIS 871  871  ?    ?   ?   A . n 
A 1 872  LYS 872  872  ?    ?   ?   A . n 
A 1 873  THR 873  873  ?    ?   ?   A . n 
A 1 874  PHE 874  874  ?    ?   ?   A . n 
A 1 875  SER 875  875  ?    ?   ?   A . n 
A 1 876  GLU 876  876  ?    ?   ?   A . n 
A 1 877  ILE 877  877  ?    ?   ?   A . n 
A 1 878  LEU 878  878  ?    ?   ?   A . n 
A 1 879  ASN 879  879  ?    ?   ?   A . n 
A 1 880  ARG 880  880  ?    ?   ?   A . n 
A 1 881  VAL 881  881  ?    ?   ?   A . n 
A 1 882  GLN 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  ALA 884  884  ?    ?   ?   A . n 
A 1 885  VAL 885  885  ?    ?   ?   A . n 
A 1 886  ASP 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LEU 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LEU 890  890  ?    ?   ?   A . n 
A 1 891  HIS 891  891  ?    ?   ?   A . n 
A 1 892  SER 892  892  ?    ?   ?   A . n 
A 1 893  TYR 893  893  ?    ?   ?   A . n 
A 1 894  SER 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  LEU 896  896  ?    ?   ?   A . n 
A 1 897  PRO 897  897  ?    ?   ?   A . n 
A 1 898  ILE 898  898  ?    ?   ?   A . n 
A 1 899  TRP 899  899  ?    ?   ?   A . n 
A 1 900  VAL 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  LYS 902  902  ?    ?   ?   A . n 
A 1 903  LEU 903  903  ?    ?   ?   A . n 
A 1 904  ASP 904  904  ?    ?   ?   A . n 
A 1 905  MET 905  905  ?    ?   ?   A . n 
A 1 906  GLU 906  906  ?    ?   ?   A . n 
A 1 907  ILE 907  907  ?    ?   ?   A . n 
A 1 908  GLU 908  908  ?    ?   ?   A . n 
A 1 909  ARG 909  909  ?    ?   ?   A . n 
A 1 910  ILE 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  GLY 912  912  ?    ?   ?   A . n 
A 1 913  VAL 913  913  ?    ?   ?   A . n 
A 1 914  ARG 914  914  ?    ?   ?   A . n 
A 1 915  LEU 915  915  ?    ?   ?   A . n 
A 1 916  GLN 916  916  ?    ?   ?   A . n 
A 1 917  ALA 917  917  ?    ?   ?   A . n 
A 1 918  GLY 918  918  ?    ?   ?   A . n 
A 1 919  LEU 919  919  ?    ?   ?   A . n 
A 1 920  ARG 920  920  ?    ?   ?   A . n 
A 1 921  ALA 921  921  ?    ?   ?   A . n 
A 1 922  TRP 922  922  ?    ?   ?   A . n 
A 1 923  THR 923  923  ?    ?   ?   A . n 
A 1 924  GLN 924  924  ?    ?   ?   A . n 
A 1 925  VAL 925  925  ?    ?   ?   A . n 
A 1 926  LEU 926  926  ?    ?   ?   A . n 
A 1 927  LEU 927  927  ?    ?   ?   A . n 
A 1 928  GLY 928  928  ?    ?   ?   A . n 
A 1 929  GLN 929  929  ?    ?   ?   A . n 
A 1 930  ALA 930  930  ?    ?   ?   A . n 
A 1 931  GLU 931  931  ?    ?   ?   A . n 
A 1 932  ASP 932  932  ?    ?   ?   A . n 
A 1 933  LYS 933  933  ?    ?   ?   A . n 
A 1 934  ALA 934  934  ?    ?   ?   A . n 
A 1 935  GLU 935  935  ?    ?   ?   A . n 
A 1 936  VAL 936  936  ?    ?   ?   A . n 
A 1 937  ASP 937  937  ?    ?   ?   A . n 
A 1 938  MET 938  938  ?    ?   ?   A . n 
A 1 939  ASP 939  939  ?    ?   ?   A . n 
A 1 940  THR 940  940  ?    ?   ?   A . n 
A 1 941  ASP 941  941  ?    ?   ?   A . n 
A 1 942  ALA 942  942  ?    ?   ?   A . n 
A 1 943  PRO 943  943  ?    ?   ?   A . n 
A 1 944  GLN 944  944  ?    ?   ?   A . n 
A 1 945  VAL 945  945  ?    ?   ?   A . n 
A 1 946  SER 946  946  ?    ?   ?   A . n 
A 1 947  HIS 947  947  ?    ?   ?   A . n 
A 1 948  LYS 948  948  ?    ?   ?   A . n 
A 1 949  PRO 949  949  ?    ?   ?   A . n 
A 1 950  GLY 950  950  ?    ?   ?   A . n 
A 1 951  GLY 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  PRO 953  953  ?    ?   ?   A . n 
A 1 954  LYS 954  954  ?    ?   ?   A . n 
A 1 955  ILE 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASN 957  957  ?    ?   ?   A . n 
A 1 958  VAL 958  958  ?    ?   ?   A . n 
A 1 959  VAL 959  959  ?    ?   ?   A . n 
A 1 960  HIS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  LEU 962  962  ?    ?   ?   A . n 
A 1 963  ARG 963  963  ?    ?   ?   A . n 
A 1 964  ILE 964  964  ?    ?   ?   A . n 
A 1 965  THR 965  965  ?    ?   ?   A . n 
A 1 966  ASN 966  966  ?    ?   ?   A . n 
A 1 967  GLN 967  967  ?    ?   ?   A . n 
A 1 968  VAL 968  968  ?    ?   ?   A . n 
A 1 969  ILE 969  969  ?    ?   ?   A . n 
A 1 970  TYR 970  970  ?    ?   ?   A . n 
A 1 971  LEU 971  971  ?    ?   ?   A . n 
A 1 972  ASN 972  972  ?    ?   ?   A . n 
A 1 973  PRO 973  973  ?    ?   ?   A . n 
A 1 974  PRO 974  974  ?    ?   ?   A . n 
A 1 975  ILE 975  975  ?    ?   ?   A . n 
A 1 976  GLU 976  976  ?    ?   ?   A . n 
A 1 977  GLU 977  977  ?    ?   ?   A . n 
A 1 978  CYS 978  978  ?    ?   ?   A . n 
A 1 979  ARG 979  979  ?    ?   ?   A . n 
A 1 980  TYR 980  980  ?    ?   ?   A . n 
A 1 981  LYS 981  981  ?    ?   ?   A . n 
A 1 982  LEU 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  GLN 984  984  ?    ?   ?   A . n 
A 1 985  GLU 985  985  ?    ?   ?   A . n 
A 1 986  MET 986  986  ?    ?   ?   A . n 
A 1 987  PHE 987  987  ?    ?   ?   A . n 
A 1 988  ALA 988  988  ?    ?   ?   A . n 
A 1 989  TRP 989  989  ?    ?   ?   A . n 
A 1 990  LYS 990  990  ?    ?   ?   A . n 
A 1 991  MET 991  991  ?    ?   ?   A . n 
A 1 992  VAL 992  992  ?    ?   ?   A . n 
A 1 993  VAL 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  SER 995  995  ?    ?   ?   A . n 
A 1 996  LEU 996  996  ?    ?   ?   A . n 
A 1 997  PRO 997  997  ?    ?   ?   A . n 
A 1 998  ARG 998  998  ?    ?   ?   A . n 
A 1 999  ILE 999  999  ?    ?   ?   A . n 
A 1 1000 GLN 1000 1000 ?    ?   ?   A . n 
A 1 1001 SER 1001 1001 ?    ?   ?   A . n 
A 1 1002 GLN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ARG 1003 1003 ?    ?   ?   A . n 
A 1 1004 TYR 1004 1004 ?    ?   ?   A . n 
A 1 1005 GLN 1005 1005 ?    ?   ?   A . n 
A 1 1006 VAL 1006 1006 ?    ?   ?   A . n 
A 1 1007 GLY 1007 1007 ?    ?   ?   A . n 
A 1 1008 VAL 1008 1008 ?    ?   ?   A . n 
A 1 1009 HIS 1009 1009 ?    ?   ?   A . n 
A 1 1010 TYR 1010 1010 ?    ?   ?   A . n 
A 1 1011 GLU 1011 1011 ?    ?   ?   A . n 
A 1 1012 LEU 1012 1012 ?    ?   ?   A . n 
A 1 1013 THR 1013 1013 ?    ?   ?   A . n 
A 1 1014 GLU 1014 1014 ?    ?   ?   A . n 
A 1 1015 GLU 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LYS 1017 1017 ?    ?   ?   A . n 
A 1 1018 PHE 1018 1018 ?    ?   ?   A . n 
A 1 1019 TYR 1019 1019 ?    ?   ?   A . n 
A 1 1020 ARG 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASN 1021 1021 ?    ?   ?   A . n 
A 1 1022 ALA 1022 1022 ?    ?   ?   A . n 
A 1 1023 LEU 1023 1023 ?    ?   ?   A . n 
A 1 1024 THR 1024 1024 ?    ?   ?   A . n 
A 1 1025 ARG 1025 1025 ?    ?   ?   A . n 
A 1 1026 MET 1026 1026 ?    ?   ?   A . n 
A 1 1027 PRO 1027 1027 ?    ?   ?   A . n 
A 1 1028 ASP 1028 1028 ?    ?   ?   A . n 
A 1 1029 GLY 1029 1029 ?    ?   ?   A . n 
A 1 1030 PRO 1030 1030 ?    ?   ?   A . n 
A 1 1031 VAL 1031 1031 ?    ?   ?   A . n 
A 1 1032 ALA 1032 1032 ?    ?   ?   A . n 
A 1 1033 LEU 1033 1033 ?    ?   ?   A . n 
A 1 1034 GLU 1034 1034 ?    ?   ?   A . n 
A 1 1035 GLU 1035 1035 ?    ?   ?   A . n 
A 1 1036 SER 1036 1036 ?    ?   ?   A . n 
A 1 1037 TYR 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 ALA 1039 1039 ?    ?   ?   A . n 
A 1 1040 VAL 1040 1040 ?    ?   ?   A . n 
A 1 1041 MET 1041 1041 ?    ?   ?   A . n 
A 1 1042 GLY 1042 1042 ?    ?   ?   A . n 
A 1 1043 ILE 1043 1043 ?    ?   ?   A . n 
A 1 1044 VAL 1044 1044 ?    ?   ?   A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   A . n 
A 1 1046 GLU 1046 1046 ?    ?   ?   A . n 
A 1 1047 VAL 1047 1047 ?    ?   ?   A . n 
A 1 1048 GLU 1048 1048 ?    ?   ?   A . n 
A 1 1049 GLN 1049 1049 ?    ?   ?   A . n 
A 1 1050 TYR 1050 1050 ?    ?   ?   A . n 
A 1 1051 VAL 1051 1051 ?    ?   ?   A . n 
A 1 1052 LYS 1052 1052 ?    ?   ?   A . n 
A 1 1053 VAL 1053 1053 ?    ?   ?   A . n 
A 1 1054 TRP 1054 1054 ?    ?   ?   A . n 
A 1 1055 LEU 1055 1055 ?    ?   ?   A . n 
A 1 1056 GLN 1056 1056 ?    ?   ?   A . n 
A 1 1057 TYR 1057 1057 ?    ?   ?   A . n 
A 1 1058 GLN 1058 1058 ?    ?   ?   A . n 
A 1 1059 CYS 1059 1059 ?    ?   ?   A . n 
A 1 1060 LEU 1060 1060 ?    ?   ?   A . n 
A 1 1061 TRP 1061 1061 ?    ?   ?   A . n 
A 1 1062 ASP 1062 1062 ?    ?   ?   A . n 
A 1 1063 MET 1063 1063 ?    ?   ?   A . n 
A 1 1064 GLN 1064 1064 ?    ?   ?   A . n 
A 1 1065 ALA 1065 1065 ?    ?   ?   A . n 
A 1 1066 GLU 1066 1066 ?    ?   ?   A . n 
A 1 1067 ASN 1067 1067 ?    ?   ?   A . n 
A 1 1068 ILE 1068 1068 ?    ?   ?   A . n 
A 1 1069 TYR 1069 1069 ?    ?   ?   A . n 
A 1 1070 ASN 1070 1070 ?    ?   ?   A . n 
A 1 1071 ARG 1071 1071 ?    ?   ?   A . n 
A 1 1072 LEU 1072 1072 ?    ?   ?   A . n 
A 1 1073 GLY 1073 1073 ?    ?   ?   A . n 
A 1 1074 GLU 1074 1074 ?    ?   ?   A . n 
A 1 1075 ASP 1075 1075 ?    ?   ?   A . n 
A 1 1076 LEU 1076 1076 ?    ?   ?   A . n 
A 1 1077 ASN 1077 1077 ?    ?   ?   A . n 
A 1 1078 LYS 1078 1078 ?    ?   ?   A . n 
A 1 1079 TRP 1079 1079 ?    ?   ?   A . n 
A 1 1080 GLN 1080 1080 ?    ?   ?   A . n 
A 1 1081 ALA 1081 1081 ?    ?   ?   A . n 
A 1 1082 LEU 1082 1082 ?    ?   ?   A . n 
A 1 1083 LEU 1083 1083 ?    ?   ?   A . n 
A 1 1084 VAL 1084 1084 ?    ?   ?   A . n 
A 1 1085 GLN 1085 1085 ?    ?   ?   A . n 
A 1 1086 ILE 1086 1086 ?    ?   ?   A . n 
A 1 1087 ARG 1087 1087 ?    ?   ?   A . n 
A 1 1088 LYS 1088 1088 ?    ?   ?   A . n 
A 1 1089 ALA 1089 1089 ?    ?   ?   A . n 
A 1 1090 ARG 1090 1090 ?    ?   ?   A . n 
A 1 1091 GLY 1091 1091 ?    ?   ?   A . n 
A 1 1092 THR 1092 1092 ?    ?   ?   A . n 
A 1 1093 PHE 1093 1093 ?    ?   ?   A . n 
A 1 1094 ASP 1094 1094 ?    ?   ?   A . n 
A 1 1095 ASN 1095 1095 ?    ?   ?   A . n 
A 1 1096 ALA 1096 1096 ?    ?   ?   A . n 
A 1 1097 GLU 1097 1097 ?    ?   ?   A . n 
A 1 1098 THR 1098 1098 ?    ?   ?   A . n 
A 1 1099 LYS 1099 1099 ?    ?   ?   A . n 
A 1 1100 LYS 1100 1100 ?    ?   ?   A . n 
A 1 1101 GLU 1101 1101 ?    ?   ?   A . n 
A 1 1102 PHE 1102 1102 ?    ?   ?   A . n 
A 1 1103 GLY 1103 1103 ?    ?   ?   A . n 
A 1 1104 PRO 1104 1104 ?    ?   ?   A . n 
A 1 1105 VAL 1105 1105 ?    ?   ?   A . n 
A 1 1106 VAL 1106 1106 ?    ?   ?   A . n 
A 1 1107 ILE 1107 1107 ?    ?   ?   A . n 
A 1 1108 ASP 1108 1108 ?    ?   ?   A . n 
A 1 1109 TYR 1109 1109 ?    ?   ?   A . n 
A 1 1110 GLY 1110 1110 ?    ?   ?   A . n 
A 1 1111 LYS 1111 1111 ?    ?   ?   A . n 
A 1 1112 VAL 1112 1112 ?    ?   ?   A . n 
A 1 1113 GLN 1113 1113 ?    ?   ?   A . n 
A 1 1114 SER 1114 1114 ?    ?   ?   A . n 
A 1 1115 LYS 1115 1115 ?    ?   ?   A . n 
A 1 1116 VAL 1116 1116 ?    ?   ?   A . n 
A 1 1117 ASN 1117 1117 ?    ?   ?   A . n 
A 1 1118 LEU 1118 1118 ?    ?   ?   A . n 
A 1 1119 LYS 1119 1119 ?    ?   ?   A . n 
A 1 1120 TYR 1120 1120 ?    ?   ?   A . n 
A 1 1121 ASP 1121 1121 ?    ?   ?   A . n 
A 1 1122 SER 1122 1122 ?    ?   ?   A . n 
A 1 1123 TRP 1123 1123 ?    ?   ?   A . n 
A 1 1124 HIS 1124 1124 ?    ?   ?   A . n 
A 1 1125 LYS 1125 1125 ?    ?   ?   A . n 
A 1 1126 GLU 1126 1126 ?    ?   ?   A . n 
A 1 1127 VAL 1127 1127 ?    ?   ?   A . n 
A 1 1128 LEU 1128 1128 ?    ?   ?   A . n 
A 1 1129 SER 1129 1129 ?    ?   ?   A . n 
A 1 1130 LYS 1130 1130 ?    ?   ?   A . n 
A 1 1131 PHE 1131 1131 ?    ?   ?   A . n 
A 1 1132 GLY 1132 1132 ?    ?   ?   A . n 
A 1 1133 GLN 1133 1133 ?    ?   ?   A . n 
A 1 1134 MET 1134 1134 ?    ?   ?   A . n 
A 1 1135 LEU 1135 1135 ?    ?   ?   A . n 
A 1 1136 GLY 1136 1136 ?    ?   ?   A . n 
A 1 1137 SER 1137 1137 ?    ?   ?   A . n 
A 1 1138 ASN 1138 1138 ?    ?   ?   A . n 
A 1 1139 MET 1139 1139 ?    ?   ?   A . n 
A 1 1140 THR 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLU 1141 1141 ?    ?   ?   A . n 
A 1 1142 PHE 1142 1142 ?    ?   ?   A . n 
A 1 1143 HIS 1143 1143 ?    ?   ?   A . n 
A 1 1144 SER 1144 1144 ?    ?   ?   A . n 
A 1 1145 GLN 1145 1145 ?    ?   ?   A . n 
A 1 1146 ILE 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 LYS 1148 1148 ?    ?   ?   A . n 
A 1 1149 SER 1149 1149 ?    ?   ?   A . n 
A 1 1150 ARG 1150 1150 ?    ?   ?   A . n 
A 1 1151 GLN 1151 1151 ?    ?   ?   A . n 
A 1 1152 GLU 1152 1152 ?    ?   ?   A . n 
A 1 1153 LEU 1153 1153 ?    ?   ?   A . n 
A 1 1154 GLU 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLN 1155 1155 ?    ?   ?   A . n 
A 1 1156 HIS 1156 1156 ?    ?   ?   A . n 
A 1 1157 SER 1157 1157 ?    ?   ?   A . n 
A 1 1158 VAL 1158 1158 ?    ?   ?   A . n 
A 1 1159 ASP 1159 1159 ?    ?   ?   A . n 
A 1 1160 THR 1160 1160 ?    ?   ?   A . n 
A 1 1161 ALA 1161 1161 ?    ?   ?   A . n 
A 1 1162 SER 1162 1162 ?    ?   ?   A . n 
A 1 1163 THR 1163 1163 ?    ?   ?   A . n 
A 1 1164 SER 1164 1164 ?    ?   ?   A . n 
A 1 1165 ASP 1165 1165 ?    ?   ?   A . n 
A 1 1166 ALA 1166 1166 ?    ?   ?   A . n 
A 1 1167 VAL 1167 1167 ?    ?   ?   A . n 
A 1 1168 THR 1168 1168 ?    ?   ?   A . n 
A 1 1169 PHE 1169 1169 ?    ?   ?   A . n 
A 1 1170 ILE 1170 1170 ?    ?   ?   A . n 
A 1 1171 THR 1171 1171 ?    ?   ?   A . n 
A 1 1172 TYR 1172 1172 ?    ?   ?   A . n 
A 1 1173 VAL 1173 1173 ?    ?   ?   A . n 
A 1 1174 GLN 1174 1174 ?    ?   ?   A . n 
A 1 1175 SER 1175 1175 ?    ?   ?   A . n 
A 1 1176 LEU 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 ARG 1178 1178 ?    ?   ?   A . n 
A 1 1179 LYS 1179 1179 ?    ?   ?   A . n 
A 1 1180 ILE 1180 1180 ?    ?   ?   A . n 
A 1 1181 LYS 1181 1181 ?    ?   ?   A . n 
A 1 1182 GLN 1182 1182 ?    ?   ?   A . n 
A 1 1183 PHE 1183 1183 ?    ?   ?   A . n 
A 1 1184 GLU 1184 1184 ?    ?   ?   A . n 
A 1 1185 LYS 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 VAL 1187 1187 ?    ?   ?   A . n 
A 1 1188 GLU 1188 1188 ?    ?   ?   A . n 
A 1 1189 LEU 1189 1189 ?    ?   ?   A . n 
A 1 1190 TYR 1190 1190 ?    ?   ?   A . n 
A 1 1191 ARG 1191 1191 ?    ?   ?   A . n 
A 1 1192 ASN 1192 1192 ?    ?   ?   A . n 
A 1 1193 GLY 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLN 1194 1194 ?    ?   ?   A . n 
A 1 1195 ARG 1195 1195 ?    ?   ?   A . n 
A 1 1196 LEU 1196 1196 ?    ?   ?   A . n 
A 1 1197 LEU 1197 1197 ?    ?   ?   A . n 
A 1 1198 GLU 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 GLN 1200 1200 ?    ?   ?   A . n 
A 1 1201 ARG 1201 1201 ?    ?   ?   A . n 
A 1 1202 PHE 1202 1202 ?    ?   ?   A . n 
A 1 1203 GLN 1203 1203 ?    ?   ?   A . n 
A 1 1204 PHE 1204 1204 ?    ?   ?   A . n 
A 1 1205 PRO 1205 1205 ?    ?   ?   A . n 
A 1 1206 PRO 1206 1206 ?    ?   ?   A . n 
A 1 1207 SER 1207 1207 ?    ?   ?   A . n 
A 1 1208 TRP 1208 1208 ?    ?   ?   A . n 
A 1 1209 LEU 1209 1209 ?    ?   ?   A . n 
A 1 1210 TYR 1210 1210 ?    ?   ?   A . n 
A 1 1211 ILE 1211 1211 ?    ?   ?   A . n 
A 1 1212 ASP 1212 1212 ?    ?   ?   A . n 
A 1 1213 ASN 1213 1213 ?    ?   ?   A . n 
A 1 1214 ILE 1214 1214 ?    ?   ?   A . n 
A 1 1215 GLU 1215 1215 ?    ?   ?   A . n 
A 1 1216 GLY 1216 1216 ?    ?   ?   A . n 
A 1 1217 GLU 1217 1217 ?    ?   ?   A . n 
A 1 1218 TRP 1218 1218 ?    ?   ?   A . n 
A 1 1219 GLY 1219 1219 ?    ?   ?   A . n 
A 1 1220 ALA 1220 1220 ?    ?   ?   A . n 
A 1 1221 PHE 1221 1221 ?    ?   ?   A . n 
A 1 1222 ASN 1222 1222 ?    ?   ?   A . n 
A 1 1223 ASP 1223 1223 ?    ?   ?   A . n 
A 1 1224 ILE 1224 1224 ?    ?   ?   A . n 
A 1 1225 MET 1225 1225 ?    ?   ?   A . n 
A 1 1226 ARG 1226 1226 ?    ?   ?   A . n 
A 1 1227 ARG 1227 1227 ?    ?   ?   A . n 
A 1 1228 LYS 1228 1228 ?    ?   ?   A . n 
A 1 1229 ASP 1229 1229 ?    ?   ?   A . n 
A 1 1230 SER 1230 1230 ?    ?   ?   A . n 
A 1 1231 ALA 1231 1231 ?    ?   ?   A . n 
A 1 1232 ILE 1232 1232 ?    ?   ?   A . n 
A 1 1233 GLN 1233 1233 ?    ?   ?   A . n 
A 1 1234 GLN 1234 1234 ?    ?   ?   A . n 
A 1 1235 GLN 1235 1235 ?    ?   ?   A . n 
A 1 1236 VAL 1236 1236 ?    ?   ?   A . n 
A 1 1237 ALA 1237 1237 ?    ?   ?   A . n 
A 1 1238 ASN 1238 1238 ?    ?   ?   A . n 
A 1 1239 LEU 1239 1239 ?    ?   ?   A . n 
A 1 1240 GLN 1240 1240 ?    ?   ?   A . n 
A 1 1241 MET 1241 1241 ?    ?   ?   A . n 
A 1 1242 LYS 1242 1242 ?    ?   ?   A . n 
A 1 1243 ILE 1243 1243 ?    ?   ?   A . n 
A 1 1244 VAL 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLN 1245 1245 ?    ?   ?   A . n 
A 1 1246 GLU 1246 1246 ?    ?   ?   A . n 
A 1 1247 ASP 1247 1247 ?    ?   ?   A . n 
A 1 1248 ARG 1248 1248 ?    ?   ?   A . n 
A 1 1249 ALA 1249 1249 ?    ?   ?   A . n 
A 1 1250 VAL 1250 1250 ?    ?   ?   A . n 
A 1 1251 GLU 1251 1251 ?    ?   ?   A . n 
A 1 1252 SER 1252 1252 ?    ?   ?   A . n 
A 1 1253 ARG 1253 1253 ?    ?   ?   A . n 
A 1 1254 THR 1254 1254 ?    ?   ?   A . n 
A 1 1255 THR 1255 1255 ?    ?   ?   A . n 
A 1 1256 ASP 1256 1256 ?    ?   ?   A . n 
A 1 1257 LEU 1257 1257 ?    ?   ?   A . n 
A 1 1258 LEU 1258 1258 ?    ?   ?   A . n 
A 1 1259 THR 1259 1259 ?    ?   ?   A . n 
A 1 1260 ASP 1260 1260 ?    ?   ?   A . n 
A 1 1261 TRP 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLU 1262 1262 ?    ?   ?   A . n 
A 1 1263 LYS 1263 1263 ?    ?   ?   A . n 
A 1 1264 THR 1264 1264 ?    ?   ?   A . n 
A 1 1265 LYS 1265 1265 ?    ?   ?   A . n 
A 1 1266 PRO 1266 1266 ?    ?   ?   A . n 
A 1 1267 VAL 1267 1267 ?    ?   ?   A . n 
A 1 1268 THR 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLY 1269 1269 ?    ?   ?   A . n 
A 1 1270 ASN 1270 1270 ?    ?   ?   A . n 
A 1 1271 LEU 1271 1271 ?    ?   ?   A . n 
A 1 1272 ARG 1272 1272 ?    ?   ?   A . n 
A 1 1273 PRO 1273 1273 ?    ?   ?   A . n 
A 1 1274 GLU 1274 1274 ?    ?   ?   A . n 
A 1 1275 GLU 1275 1275 ?    ?   ?   A . n 
A 1 1276 ALA 1276 1276 ?    ?   ?   A . n 
A 1 1277 LEU 1277 1277 ?    ?   ?   A . n 
A 1 1278 GLN 1278 1278 ?    ?   ?   A . n 
A 1 1279 ALA 1279 1279 ?    ?   ?   A . n 
A 1 1280 LEU 1280 1280 ?    ?   ?   A . n 
A 1 1281 THR 1281 1281 ?    ?   ?   A . n 
A 1 1282 ILE 1282 1282 ?    ?   ?   A . n 
A 1 1283 TYR 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLU 1284 1284 ?    ?   ?   A . n 
A 1 1285 GLY 1285 1285 ?    ?   ?   A . n 
A 1 1286 LYS 1286 1286 ?    ?   ?   A . n 
A 1 1287 PHE 1287 1287 ?    ?   ?   A . n 
A 1 1288 GLY 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 LEU 1290 1290 ?    ?   ?   A . n 
A 1 1291 LYS 1291 1291 ?    ?   ?   A . n 
A 1 1292 ASP 1292 1292 ?    ?   ?   A . n 
A 1 1293 ASP 1293 1293 ?    ?   ?   A . n 
A 1 1294 ARG 1294 1294 ?    ?   ?   A . n 
A 1 1295 GLU 1295 1295 ?    ?   ?   A . n 
A 1 1296 LYS 1296 1296 ?    ?   ?   A . n 
A 1 1297 CYS 1297 1297 ?    ?   ?   A . n 
A 1 1298 ALA 1298 1298 ?    ?   ?   A . n 
A 1 1299 LYS 1299 1299 ?    ?   ?   A . n 
A 1 1300 ALA 1300 1300 ?    ?   ?   A . n 
A 1 1301 LYS 1301 1301 ?    ?   ?   A . n 
A 1 1302 GLU 1302 1302 ?    ?   ?   A . n 
A 1 1303 ALA 1303 1303 ?    ?   ?   A . n 
A 1 1304 LEU 1304 1304 ?    ?   ?   A . n 
A 1 1305 GLU 1305 1305 ?    ?   ?   A . n 
A 1 1306 LEU 1306 1306 ?    ?   ?   A . n 
A 1 1307 THR 1307 1307 ?    ?   ?   A . n 
A 1 1308 ASP 1308 1308 ?    ?   ?   A . n 
A 1 1309 THR 1309 1309 ?    ?   ?   A . n 
A 1 1310 GLY 1310 1310 ?    ?   ?   A . n 
A 1 1311 LEU 1311 1311 ?    ?   ?   A . n 
A 1 1312 LEU 1312 1312 ?    ?   ?   A . n 
A 1 1313 SER 1313 1313 ?    ?   ?   A . n 
A 1 1314 GLY 1314 1314 ?    ?   ?   A . n 
A 1 1315 SER 1315 1315 ?    ?   ?   A . n 
A 1 1316 GLU 1316 1316 ?    ?   ?   A . n 
A 1 1317 GLU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ARG 1318 1318 ?    ?   ?   A . n 
A 1 1319 VAL 1319 1319 ?    ?   ?   A . n 
A 1 1320 GLN 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 ALA 1322 1322 ?    ?   ?   A . n 
A 1 1323 LEU 1323 1323 ?    ?   ?   A . n 
A 1 1324 GLU 1324 1324 ?    ?   ?   A . n 
A 1 1325 GLU 1325 1325 ?    ?   ?   A . n 
A 1 1326 LEU 1326 1326 ?    ?   ?   A . n 
A 1 1327 GLN 1327 1327 ?    ?   ?   A . n 
A 1 1328 ASP 1328 1328 ?    ?   ?   A . n 
A 1 1329 LEU 1329 1329 ?    ?   ?   A . n 
A 1 1330 LYS 1330 1330 ?    ?   ?   A . n 
A 1 1331 GLY 1331 1331 ?    ?   ?   A . n 
A 1 1332 VAL 1332 1332 ?    ?   ?   A . n 
A 1 1333 TRP 1333 1333 ?    ?   ?   A . n 
A 1 1334 SER 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 SER 1337 1337 ?    ?   ?   A . n 
A 1 1338 LYS 1338 1338 ?    ?   ?   A . n 
A 1 1339 VAL 1339 1339 ?    ?   ?   A . n 
A 1 1340 TRP 1340 1340 ?    ?   ?   A . n 
A 1 1341 GLU 1341 1341 ?    ?   ?   A . n 
A 1 1342 GLN 1342 1342 ?    ?   ?   A . n 
A 1 1343 ILE 1343 1343 ?    ?   ?   A . n 
A 1 1344 ASP 1344 1344 ?    ?   ?   A . n 
A 1 1345 GLN 1345 1345 ?    ?   ?   A . n 
A 1 1346 MET 1346 1346 ?    ?   ?   A . n 
A 1 1347 LYS 1347 1347 ?    ?   ?   A . n 
A 1 1348 GLU 1348 1348 ?    ?   ?   A . n 
A 1 1349 GLN 1349 1349 ?    ?   ?   A . n 
A 1 1350 PRO 1350 1350 ?    ?   ?   A . n 
A 1 1351 TRP 1351 1351 ?    ?   ?   A . n 
A 1 1352 VAL 1352 1352 ?    ?   ?   A . n 
A 1 1353 SER 1353 1353 ?    ?   ?   A . n 
A 1 1354 VAL 1354 1354 ?    ?   ?   A . n 
A 1 1355 GLN 1355 1355 ?    ?   ?   A . n 
A 1 1356 PRO 1356 1356 ?    ?   ?   A . n 
A 1 1357 ARG 1357 1357 ?    ?   ?   A . n 
A 1 1358 LYS 1358 1358 ?    ?   ?   A . n 
A 1 1359 LEU 1359 1359 ?    ?   ?   A . n 
A 1 1360 ARG 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLN 1361 1361 ?    ?   ?   A . n 
A 1 1362 ASN 1362 1362 ?    ?   ?   A . n 
A 1 1363 LEU 1363 1363 ?    ?   ?   A . n 
A 1 1364 ASP 1364 1364 ?    ?   ?   A . n 
A 1 1365 ALA 1365 1365 ?    ?   ?   A . n 
A 1 1366 LEU 1366 1366 ?    ?   ?   A . n 
A 1 1367 LEU 1367 1367 ?    ?   ?   A . n 
A 1 1368 ASN 1368 1368 ?    ?   ?   A . n 
A 1 1369 GLN 1369 1369 ?    ?   ?   A . n 
A 1 1370 LEU 1370 1370 ?    ?   ?   A . n 
A 1 1371 LYS 1371 1371 ?    ?   ?   A . n 
A 1 1372 SER 1372 1372 ?    ?   ?   A . n 
A 1 1373 PHE 1373 1373 ?    ?   ?   A . n 
A 1 1374 PRO 1374 1374 ?    ?   ?   A . n 
A 1 1375 ALA 1375 1375 ?    ?   ?   A . n 
A 1 1376 ARG 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 ARG 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLN 1379 1379 ?    ?   ?   A . n 
A 1 1380 TYR 1380 1380 ?    ?   ?   A . n 
A 1 1381 ALA 1381 1381 ?    ?   ?   A . n 
A 1 1382 SER 1382 1382 ?    ?   ?   A . n 
A 1 1383 TYR 1383 1383 ?    ?   ?   A . n 
A 1 1384 GLU 1384 1384 ?    ?   ?   A . n 
A 1 1385 PHE 1385 1385 ?    ?   ?   A . n 
A 1 1386 VAL 1386 1386 ?    ?   ?   A . n 
A 1 1387 GLN 1387 1387 ?    ?   ?   A . n 
A 1 1388 ARG 1388 1388 ?    ?   ?   A . n 
A 1 1389 LEU 1389 1389 ?    ?   ?   A . n 
A 1 1390 LEU 1390 1390 ?    ?   ?   A . n 
A 1 1391 LYS 1391 1391 ?    ?   ?   A . n 
A 1 1392 GLY 1392 1392 ?    ?   ?   A . n 
A 1 1393 TYR 1393 1393 ?    ?   ?   A . n 
A 1 1394 MET 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ILE 1396 1396 ?    ?   ?   A . n 
A 1 1397 ASN 1397 1397 ?    ?   ?   A . n 
A 1 1398 MET 1398 1398 ?    ?   ?   A . n 
A 1 1399 LEU 1399 1399 ?    ?   ?   A . n 
A 1 1400 VAL 1400 1400 ?    ?   ?   A . n 
A 1 1401 ILE 1401 1401 ?    ?   ?   A . n 
A 1 1402 GLU 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 LYS 1404 1404 ?    ?   ?   A . n 
A 1 1405 SER 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLU 1406 1406 ?    ?   ?   A . n 
A 1 1407 ALA 1407 1407 ?    ?   ?   A . n 
A 1 1408 LEU 1408 1408 ?    ?   ?   A . n 
A 1 1409 LYS 1409 1409 ?    ?   ?   A . n 
A 1 1410 ASP 1410 1410 ?    ?   ?   A . n 
A 1 1411 ARG 1411 1411 ?    ?   ?   A . n 
A 1 1412 HIS 1412 1412 ?    ?   ?   A . n 
A 1 1413 TRP 1413 1413 ?    ?   ?   A . n 
A 1 1414 LYS 1414 1414 ?    ?   ?   A . n 
A 1 1415 GLN 1415 1415 ?    ?   ?   A . n 
A 1 1416 LEU 1416 1416 ?    ?   ?   A . n 
A 1 1417 MET 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ARG 1419 1419 ?    ?   ?   A . n 
A 1 1420 LEU 1420 1420 ?    ?   ?   A . n 
A 1 1421 HIS 1421 1421 ?    ?   ?   A . n 
A 1 1422 VAL 1422 1422 ?    ?   ?   A . n 
A 1 1423 ASN 1423 1423 ?    ?   ?   A . n 
A 1 1424 TRP 1424 1424 ?    ?   ?   A . n 
A 1 1425 VAL 1425 1425 ?    ?   ?   A . n 
A 1 1426 VAL 1426 1426 ?    ?   ?   A . n 
A 1 1427 SER 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLU 1428 1428 ?    ?   ?   A . n 
A 1 1429 LEU 1429 1429 ?    ?   ?   A . n 
A 1 1430 THR 1430 1430 ?    ?   ?   A . n 
A 1 1431 LEU 1431 1431 ?    ?   ?   A . n 
A 1 1432 GLY 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLN 1433 1433 ?    ?   ?   A . n 
A 1 1434 ILE 1434 1434 ?    ?   ?   A . n 
A 1 1435 TRP 1435 1435 ?    ?   ?   A . n 
A 1 1436 ASP 1436 1436 ?    ?   ?   A . n 
A 1 1437 VAL 1437 1437 ?    ?   ?   A . n 
A 1 1438 ASP 1438 1438 ?    ?   ?   A . n 
A 1 1439 LEU 1439 1439 ?    ?   ?   A . n 
A 1 1440 GLN 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ASN 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 ALA 1444 1444 ?    ?   ?   A . n 
A 1 1445 ILE 1445 1445 ?    ?   ?   A . n 
A 1 1446 VAL 1446 1446 ?    ?   ?   A . n 
A 1 1447 LYS 1447 1447 ?    ?   ?   A . n 
A 1 1448 ASP 1448 1448 ?    ?   ?   A . n 
A 1 1449 VAL 1449 1449 ?    ?   ?   A . n 
A 1 1450 LEU 1450 1450 ?    ?   ?   A . n 
A 1 1451 LEU 1451 1451 ?    ?   ?   A . n 
A 1 1452 VAL 1452 1452 ?    ?   ?   A . n 
A 1 1453 ALA 1453 1453 ?    ?   ?   A . n 
A 1 1454 GLN 1454 1454 ?    ?   ?   A . n 
A 1 1455 GLY 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLU 1456 1456 ?    ?   ?   A . n 
A 1 1457 MET 1457 1457 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 . 
# 
_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                   9BML 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BML 
_struct.title                        'State-2 of the motor domain from full-length human dynein-1 in 5mM AMPPNP' 
_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        9BML 
_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 ? 
# 
_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              9BML 
_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 
# 
_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 ? LYS A 1613 ? GLY A 1596 LYS A 1613 1 ? 18 
HELX_P HELX_P9   AA9 LEU A 1615 ? PHE A 1626 ? LEU A 1615 PHE A 1626 1 ? 12 
HELX_P HELX_P10  AB1 PRO A 1627 ? VAL A 1632 ? PRO A 1627 VAL A 1632 5 ? 6  
HELX_P HELX_P11  AB2 GLY A 1633 ? ASN A 1643 ? GLY A 1633 ASN A 1643 1 ? 11 
HELX_P HELX_P12  AB3 ASN A 1646 ? PHE A 1654 ? ASN A 1646 PHE A 1654 5 ? 9  
HELX_P HELX_P13  AB4 LYS A 1697 ? GLY A 1728 ? LYS A 1697 GLY A 1728 1 ? 32 
HELX_P HELX_P14  AB5 ASP A 1734 ? TYR A 1745 ? ASP A 1734 TYR A 1745 1 ? 12 
HELX_P HELX_P15  AB6 GLN A 1746 ? MET A 1769 ? GLN A 1746 MET A 1769 1 ? 24 
HELX_P HELX_P16  AB7 GLY A 1770 ? GLY A 1772 ? GLY A 1770 GLY A 1772 5 ? 3  
HELX_P HELX_P17  AB8 PRO A 1777 ? LEU A 1797 ? PRO A 1777 LEU A 1797 1 ? 21 
HELX_P HELX_P18  AB9 PRO A 1801 ? SER A 1828 ? PRO A 1801 SER A 1828 1 ? 28 
HELX_P HELX_P19  AC1 SER A 1835 ? SER A 1840 ? SER A 1835 SER A 1840 1 ? 6  
HELX_P HELX_P20  AC2 ASP A 1852 ? GLN A 1855 ? ASP A 1852 GLN A 1855 5 ? 4  
HELX_P HELX_P21  AC3 THR A 1882 ? ALA A 1898 ? THR A 1882 ALA A 1898 1 ? 17 
HELX_P HELX_P22  AC4 LYS A 1912 ? LEU A 1923 ? LYS A 1912 LEU A 1923 1 ? 12 
HELX_P HELX_P23  AC5 ASP A 1937 ? GLY A 1952 ? ASP A 1937 GLY A 1952 1 ? 16 
HELX_P HELX_P24  AC6 PHE A 1960 ? LEU A 1963 ? PHE A 1960 LEU A 1963 5 ? 4  
HELX_P HELX_P25  AC7 GLU A 1964 ? ASN A 1987 ? GLU A 1964 ASN A 1987 1 ? 24 
HELX_P HELX_P26  AC8 PRO A 2029 ? LYS A 2034 ? PRO A 2029 LYS A 2034 1 ? 6  
HELX_P HELX_P27  AC9 ASP A 2045 ? GLN A 2057 ? ASP A 2045 GLN A 2057 1 ? 13 
HELX_P HELX_P28  AD1 THR A 2061 ? LEU A 2080 ? THR A 2061 LEU A 2080 1 ? 20 
HELX_P HELX_P29  AD2 GLY A 2089 ? ARG A 2118 ? GLY A 2089 ARG A 2118 1 ? 30 
HELX_P HELX_P30  AD3 ASP A 2123 ? ASN A 2130 ? ASP A 2123 ASN A 2130 1 ? 8  
HELX_P HELX_P31  AD4 PRO A 2132 ? VAL A 2146 ? PRO A 2132 VAL A 2146 1 ? 15 
HELX_P HELX_P32  AD5 PRO A 2147 ? LEU A 2149 ? PRO A 2147 LEU A 2149 5 ? 3  
HELX_P HELX_P33  AD6 ASP A 2153 ? PHE A 2165 ? ASP A 2153 PHE A 2165 1 ? 13 
HELX_P HELX_P34  AD7 MET A 2175 ? MET A 2189 ? MET A 2175 MET A 2189 1 ? 15 
HELX_P HELX_P35  AD8 GLY A 2200 ? ASN A 2217 ? GLY A 2200 ASN A 2217 1 ? 18 
HELX_P HELX_P36  AD9 GLY A 2229 ? GLY A 2246 ? GLY A 2229 GLY A 2246 1 ? 18 
HELX_P HELX_P37  AE1 ASP A 2255 ? ILE A 2259 ? ASP A 2255 ILE A 2259 5 ? 5  
HELX_P HELX_P38  AE2 SER A 2260 ? TYR A 2265 ? SER A 2260 TYR A 2265 1 ? 6  
HELX_P HELX_P39  AE3 LEU A 2279 ? SER A 2290 ? LEU A 2279 SER A 2290 1 ? 12 
HELX_P HELX_P40  AE4 GLY A 2293 ? LYS A 2297 ? GLY A 2293 LYS A 2297 5 ? 5  
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 ? CYS A 2359 ? THR A 2352 CYS A 2359 1 ? 8  
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 ? SER A 2503 ? GLN A 2482 SER A 2503 1 ? 22 
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 ? GLY A 3165 ? SER A 3138 GLY A 3165 1 ? 28 
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 ? THR A 3495 ? GLU A 3450 THR A 3495 1 ? 46 
HELX_P HELX_P80  AI8 THR A 3495 ? ALA A 3517 ? THR A 3495 ALA A 3517 1 ? 23 
HELX_P HELX_P81  AI9 ASP A 3521 ? ALA A 3539 ? ASP A 3521 ALA A 3539 1 ? 19 
HELX_P HELX_P82  AJ1 ALA A 3548 ? SER A 3554 ? ALA A 3548 SER A 3554 1 ? 7  
HELX_P HELX_P83  AJ2 ASN A 3555 ? SER A 3565 ? ASN A 3555 SER A 3565 1 ? 11 
HELX_P HELX_P84  AJ3 ASP A 3570 ? ARG A 3582 ? ASP A 3570 ARG A 3582 1 ? 13 
HELX_P HELX_P85  AJ4 GLY A 3594 ? TYR A 3604 ? GLY A 3594 TYR A 3604 1 ? 11 
HELX_P HELX_P86  AJ5 LYS A 3605 ? LYS A 3608 ? LYS A 3605 LYS A 3608 5 ? 4  
HELX_P HELX_P87  AJ6 ALA A 3618 ? GLY A 3630 ? ALA A 3618 GLY A 3630 1 ? 13 
HELX_P HELX_P88  AJ7 VAL A 3638 ? TYR A 3641 ? VAL A 3638 TYR A 3641 5 ? 4  
HELX_P HELX_P89  AJ8 ASP A 3642 ? VAL A 3644 ? ASP A 3642 VAL A 3644 5 ? 3  
HELX_P HELX_P90  AJ9 LEU A 3645 ? ARG A 3651 ? LEU A 3645 ARG A 3651 1 ? 7  
HELX_P HELX_P91  AK1 PRO A 3689 ? VAL A 3696 ? PRO A 3689 VAL A 3696 1 ? 8  
HELX_P HELX_P92  AK2 THR A 3704 ? ARG A 3721 ? THR A 3704 ARG A 3721 1 ? 18 
HELX_P HELX_P93  AK3 ARG A 3721 ? VAL A 3756 ? ARG A 3721 VAL A 3756 1 ? 36 
HELX_P HELX_P94  AK4 ARG A 3759 ? ASP A 3762 ? ARG A 3759 ASP A 3762 5 ? 4  
HELX_P HELX_P95  AK5 ASP A 3763 ? SER A 3817 ? ASP A 3763 SER A 3817 1 ? 55 
HELX_P HELX_P96  AK6 LEU A 3818 ? ILE A 3821 ? LEU A 3818 ILE A 3821 5 ? 4  
HELX_P HELX_P97  AK7 SER A 3828 ? GLU A 3842 ? SER A 3828 GLU A 3842 1 ? 15 
HELX_P HELX_P98  AK8 ASN A 3843 ? LYS A 3847 ? ASN A 3843 LYS A 3847 5 ? 5  
HELX_P HELX_P99  AK9 ASP A 3851 ? ARG A 3873 ? ASP A 3851 ARG A 3873 1 ? 23 
HELX_P HELX_P100 AL1 LEU A 3876 ? GLY A 3894 ? LEU A 3876 GLY A 3894 1 ? 19 
HELX_P HELX_P101 AL2 TYR A 3901 ? GLY A 3911 ? TYR A 3901 GLY A 3911 1 ? 11 
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 ? ASP A 3954 ? ASP A 3946 ASP A 3954 1 ? 9  
HELX_P HELX_P106 AL7 GLN A 3956 ? ASP A 3962 ? GLN A 3956 ASP A 3962 1 ? 7  
HELX_P HELX_P107 AL8 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 ? GLY A 4014 ? ARG A 4000 GLY A 4014 1 ? 15 
HELX_P HELX_P110 AM2 GLU A 4015 ? GLN A 4023 ? GLU A 4015 GLN A 4023 5 ? 9  
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 ? ASN A 4063 ? ALA A 4051 ASN A 4063 1 ? 13 
HELX_P HELX_P113 AM5 SER A 4073 ? GLY A 4091 ? SER A 4073 GLY A 4091 1 ? 19 
HELX_P HELX_P114 AM6 VAL A 4099 ? LEU A 4101 ? VAL A 4099 LEU A 4101 5 ? 3  
HELX_P HELX_P115 AM7 ALA A 4102 ? 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 ? LEU A 4194 ? GLU A 4175 LEU A 4194 1 ? 20 
HELX_P HELX_P120 AN3 TYR A 4196 ? TRP A 4201 ? TYR A 4196 TRP A 4201 1 ? 6  
HELX_P HELX_P121 AN4 GLY A 4208 ? ALA A 4227 ? GLY A 4208 ALA A 4227 1 ? 20 
HELX_P HELX_P122 AN5 SER A 4234 ? ILE A 4238 ? SER A 4234 ILE A 4238 5 ? 5  
HELX_P HELX_P123 AN6 PRO A 4239 ? SER A 4250 ? PRO A 4239 SER A 4250 1 ? 12 
HELX_P HELX_P124 AN7 ASN A 4258 ? PHE A 4273 ? ASN A 4258 PHE A 4273 1 ? 16 
HELX_P HELX_P125 AN8 THR A 4274 ? ASP A 4279 ? THR A 4274 ASP A 4279 5 ? 6  
HELX_P HELX_P126 AN9 ARG A 4301 ? LEU A 4311 ? ARG A 4301 LEU A 4311 1 ? 11 
HELX_P HELX_P127 AO1 THR A 4317 ? GLY A 4322 ? THR A 4317 GLY A 4322 5 ? 6  
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 THR A 4401 ? LYS A 4406 ? THR A 4401 LYS A 4406 1 ? 6  
HELX_P HELX_P131 AO5 ASP A 4407 ? GLU A 4439 ? ASP A 4407 GLU A 4439 1 ? 33 
HELX_P HELX_P132 AO6 THR A 4445 ? LYS A 4457 ? THR A 4445 LYS A 4457 1 ? 13 
HELX_P HELX_P133 AO7 THR A 4474 ? SER A 4498 ? THR A 4474 SER A 4498 1 ? 25 
HELX_P HELX_P134 AO8 GLY A 4500 ? ILE A 4507 ? GLY A 4500 ILE A 4507 1 ? 8  
HELX_P HELX_P135 AO9 VAL A 4516 ? SER A 4533 ? VAL A 4516 SER A 4533 1 ? 18 
HELX_P HELX_P136 AP1 SER A 4535 ? GLU A 4537 ? SER A 4535 GLU A 4537 5 ? 3  
HELX_P HELX_P137 AP2 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 SER 2231 OG  ? ? ? 1_555 F MG . MG ? ? A SER 2231 A MG 4705 1_555 ? ? ? ? ? ? ? 1.975 ? ? 
metalc2 metalc ? ? A GLU 2344 OE2 ? ? ? 1_555 F MG . MG ? ? A GLU 2344 A MG 4705 1_555 ? ? ? ? ? ? ? 2.518 ? ? 
metalc3 metalc ? ? C ATP .    O2G ? ? ? 1_555 F MG . MG ? ? A ATP 4702 A MG 4705 1_555 ? ? ? ? ? ? ? 1.949 ? ? 
metalc4 metalc ? ? C ATP .    O2B ? ? ? 1_555 F MG . MG ? ? A ATP 4702 A MG 4705 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
# 
_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 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 64.9  ? 
2 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 145.7 ? 
3 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2G ? C ATP .    ? A ATP 4702 ? 1_555 81.3  ? 
4 OG  ? A SER 2231 ? A SER 2231 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 85.7  ? 
5 OE2 ? A GLU 2344 ? A GLU 2344 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 98.0  ? 
6 O2G ? C ATP .    ? A ATP 4702 ? 1_555 MG ? F MG . ? A MG 4705 ? 1_555 O2B ? C ATP .    ? A ATP 4702 ? 1_555 93.7  ? 
# 
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 ? ASN A 1479 ? ASP A 1476 ASN A 1479 
AA1 2 ARG A 1485 ? ARG A 1488 ? ARG A 1485 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 ARG A 1843 ? PHE A 1846 ? ARG A 1843 PHE A 1846 
AA3 2 LEU A 1857 ? MET A 1861 ? LEU A 1857 MET A 1861 
AA3 3 ALA A 1864 ? ASN A 1867 ? ALA A 1864 ASN A 1867 
AA4 1 GLY A 1901 ? PHE A 1905 ? GLY A 1901 PHE A 1905 
AA4 2 PHE A 2036 ? ALA A 2040 ? PHE A 2036 ALA A 2040 
AA5 1 VAL A 1927 ? VAL A 1929 ? VAL A 1927 VAL A 1929 
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 ? GLU A 2000 ? THR A 1998 GLU A 2000 
AA6 2 GLN A 2005 ? LYS A 2007 ? GLN A 2005 LYS A 2007 
AA7 1 GLY A 2249 ? ILE A 2253 ? GLY A 2249 ILE A 2253 
AA7 2 ARG A 2298 ? ASP A 2304 ? ARG A 2298 ASP A 2304 
AA7 3 VAL A 2339 ? VAL A 2345 ? VAL A 2339 VAL A 2345 
AA7 4 GLY A 2219 ? VAL A 2223 ? GLY A 2219 VAL A 2223 
AA7 5 GLY A 2360 ? TRP A 2363 ? GLY A 2360 TRP A 2363 
AA8 1 GLY A 2266 ? LEU A 2268 ? GLY A 2266 LEU A 2268 
AA8 2 TRP A 2275 ? ASP A 2277 ? TRP A 2275 ASP A 2277 
AA9 1 LEU A 2324 ? THR A 2326 ? LEU A 2324 THR A 2326 
AA9 2 ARG A 2332 ? SER A 2334 ? ARG A 2332 SER A 2334 
AB1 1 TYR A 2537 ? VAL A 2539 ? TYR A 2537 VAL A 2539 
AB1 2 TRP A 2545 ? PRO A 2547 ? TRP A 2545 PRO A 2547 
AB2 1 MET A 2615 ? LEU A 2620 ? MET A 2615 LEU A 2620 
AB2 2 TRP A 2658 ? CYS A 2663 ? TRP A 2658 CYS A 2663 
AB2 3 ILE A 2706 ? CYS A 2712 ? ILE A 2706 CYS A 2712 
AB2 4 LEU A 2591 ? CYS A 2594 ? LEU A 2591 CYS A 2594 
AB2 5 VAL A 2733 ? TYR A 2735 ? VAL A 2733 TYR A 2735 
AB3 1 CYS A 2639 ? THR A 2644 ? CYS A 2639 THR A 2644 
AB3 2 GLY A 2647 ? PRO A 2652 ? GLY A 2647 PRO A 2652 
AB3 3 THR A 2699 ? LEU A 2703 ? THR A 2699 LEU A 2703 
AB3 4 GLY A 2691 ? ARG A 2694 ? GLY A 2691 ARG A 2694 
AB4 1 TYR A 2873 ? SER A 2874 ? TYR A 2873 SER A 2874 
AB4 2 ILE A 2882 ? PRO A 2883 ? ILE A 2882 PRO A 2883 
AB5 1 SER A 2957 ? TYR A 2959 ? SER A 2957 TYR A 2959 
AB5 2 ILE A 2990 ? ASP A 2995 ? ILE A 2990 ASP A 2995 
AB5 3 LEU A 3062 ? MET A 3068 ? LEU A 3062 MET A 3068 
AB5 4 HIS A 2932 ? ILE A 2936 ? HIS A 2932 ILE A 2936 
AB5 5 CYS A 3089 ? TRP A 3093 ? CYS A 3089 TRP A 3093 
AB6 1 THR A 3610 ? SER A 3613 ? THR A 3610 SER A 3613 
AB6 2 LEU A 3633 ? GLN A 3636 ? LEU A 3633 GLN A 3636 
AB6 3 ILE A 3677 ? THR A 3681 ? ILE A 3677 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 HIS A 4508 ? CYS A 4510 ? HIS A 4508 CYS A 4510 
AC1 2 PHE A 4558 ? THR A 4561 ? PHE A 4558 THR A 4561 
AC1 3 LEU A 4587 ? LYS A 4594 ? LEU A 4587 LYS A 4594 
AC1 4 LEU A 4539 ? THR A 4546 ? LEU A 4539 THR A 4546 
AC2 1 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
AC2 2 LYS A 4574 ? ALA A 4584 ? LYS A 4574 ALA A 4584 
AC2 3 LEU A 4618 ? ILE A 4626 ? LEU A 4618 ILE A 4626 
AC2 4 VAL A 4604 ? TYR A 4610 ? VAL A 4604 TYR A 4610 
AC2 5 ALA A 4641 ? LEU A 4643 ? ALA A 4641 LEU A 4643 
AC2 6 LYS A 4564 ? ASN A 4571 ? LYS A 4564 ASN A 4571 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 1478 ? N VAL A 1478 O LEU A 1486 ? O LEU A 1486 
AA2 1 2 N SER A 1663 ? N SER A 1663 O SER A 1677 ? O SER A 1677 
AA2 2 3 N VAL A 1673 ? N VAL A 1673 O VAL A 1690 ? O VAL A 1690 
AA3 1 2 N TYR A 1845 ? N TYR A 1845 O SER A 1858 ? O SER A 1858 
AA3 2 3 N ILE A 1859 ? N ILE A 1859 O PHE A 1866 ? O PHE A 1866 
AA4 1 2 N PHE A 1905 ? N PHE A 1905 O LEU A 2039 ? O LEU A 2039 
AA5 1 2 N LEU A 1928 ? N LEU A 1928 O CYS A 1956 ? O CYS A 1956 
AA5 2 3 N PHE A 1957 ? N PHE A 1957 O PHE A 2015 ? O PHE A 2015 
AA6 1 2 N CYS A 1999 ? N CYS A 1999 O VAL A 2006 ? O VAL A 2006 
AA7 1 2 N 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 PHE A 2343 ? O PHE A 2343 N MET A 2222 ? N MET A 2222 
AA7 4 5 N MET A 2221 ? N MET A 2221 O VAL A 2362 ? O VAL A 2362 
AA8 1 2 N THR A 2267 ? N THR A 2267 O THR A 2276 ? O THR A 2276 
AA9 1 2 N LEU A 2325 ? N LEU A 2325 O LEU A 2333 ? O LEU A 2333 
AB1 1 2 N GLU A 2538 ? N GLU A 2538 O SER A 2546 ? O SER A 2546 
AB2 1 2 N LEU A 2620 ? N LEU A 2620 O PHE A 2662 ? O PHE A 2662 
AB2 2 3 N LEU A 2659 ? N LEU A 2659 O GLN A 2707 ? O GLN A 2707 
AB2 3 4 O GLY A 2710 ? O GLY A 2710 N LEU A 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 GLU A 2640 ? N GLU A 2640 O ALA A 2651 ? O ALA A 2651 
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 HIS A 3063 ? O HIS A 3063 
AB5 3 4 O PHE A 3066 ? O PHE A 3066 N LEU A 2933 ? N LEU A 2933 
AB5 4 5 N HIS A 2932 ? N HIS A 2932 O VAL A 3090 ? O VAL A 3090 
AB6 1 2 N THR A 3612 ? N THR A 3612 O LEU A 3634 ? O LEU A 3634 
AB6 2 3 N VAL A 3635 ? N VAL A 3635 O PHE A 3678 ? O PHE A 3678 
AB6 3 4 O LEU A 3679 ? O LEU A 3679 N ILE A 3589 ? N ILE A 3589 
AB6 4 5 N LEU A 3588 ? N LEU A 3588 O THR A 3697 ? O THR A 3697 
AB7 1 2 N ARG A 3654 ? N ARG A 3654 O LEU A 3661 ? O LEU A 3661 
AB7 2 3 N ILE A 3662 ? N ILE A 3662 O ILE A 3669 ? O ILE A 3669 
AB8 1 2 N ILE A 4069 ? N ILE A 4069 O MET A 4095 ? O MET A 4095 
AB8 2 3 N LEU A 4096 ? N LEU A 4096 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 GLY A 4559 ? O GLY A 4559 
AC1 2 3 N VAL A 4560 ? N VAL A 4560 O THR A 4588 ? O THR A 4588 
AC1 3 4 O GLN A 4589 ? O GLN A 4589 N ASN A 4544 ? N ASN A 4544 
AC2 1 2 N LEU A 4565 ? N LEU A 4565 O THR A 4583 ? O THR A 4583 
AC2 2 3 N LEU A 4575 ? N LEU A 4575 O GLU A 4625 ? O GLU A 4625 
AC2 3 4 O ILE A 4619 ? O ILE A 4619 N VAL A 4609 ? N VAL A 4609 
AC2 4 5 N TYR A 4610 ? N TYR A 4610 O VAL A 4642 ? O VAL A 4642 
AC2 5 6 O LEU A 4643 ? O LEU A 4643 N LYS A 4564 ? N LYS A 4564 
# 
_pdbx_entry_details.entry_id                   9BML 
_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_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 ? ? -95.68  32.00   
2  1 ALA A 1862 ? ? 59.38   -121.09 
3  1 THR A 2061 ? ? -104.00 41.60   
4  1 VAL A 2838 ? ? -98.27  -60.48  
5  1 SER A 3640 ? ? -109.86 42.07   
6  1 GLU A 4206 ? ? -93.48  54.69   
7  1 LEU A 4395 ? ? -161.79 117.68  
8  1 ASN A 4597 ? ? 39.38   48.70   
9  1 GLU A 4599 ? ? 62.10   -140.95 
10 1 SER A 4603 ? ? -141.44 30.97   
11 1 THR A 4628 ? ? 47.61   -131.76 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     4633 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.137 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BML 
_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                    9BML 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.3 
_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               40850 
_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 AMPPNP' 
_em_buffer.pH            7.2 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'State-2 of the motor domain from full-length human dynein-1 in 5mM AMPPNP' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BML 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS GLACIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             3000 
_em_imaging.calibrated_defocus_min          1200 
_em_imaging.calibrated_defocus_max          3000 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           45000 
_em_imaging.calibrated_magnification        45000 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            30 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              9BML 
_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                9BML 
_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 
ILE N      N  N N 247 
ILE CA     C  N S 248 
ILE C      C  N N 249 
ILE O      O  N N 250 
ILE CB     C  N S 251 
ILE CG1    C  N N 252 
ILE CG2    C  N N 253 
ILE CD1    C  N N 254 
ILE OXT    O  N N 255 
ILE H      H  N N 256 
ILE H2     H  N N 257 
ILE HA     H  N N 258 
ILE HB     H  N N 259 
ILE HG12   H  N N 260 
ILE HG13   H  N N 261 
ILE HG21   H  N N 262 
ILE HG22   H  N N 263 
ILE HG23   H  N N 264 
ILE HD11   H  N N 265 
ILE HD12   H  N N 266 
ILE HD13   H  N N 267 
ILE HXT    H  N N 268 
LEU N      N  N N 269 
LEU CA     C  N S 270 
LEU C      C  N N 271 
LEU O      O  N N 272 
LEU CB     C  N N 273 
LEU CG     C  N N 274 
LEU CD1    C  N N 275 
LEU CD2    C  N N 276 
LEU OXT    O  N N 277 
LEU H      H  N N 278 
LEU H2     H  N N 279 
LEU HA     H  N N 280 
LEU HB2    H  N N 281 
LEU HB3    H  N N 282 
LEU HG     H  N N 283 
LEU HD11   H  N N 284 
LEU HD12   H  N N 285 
LEU HD13   H  N N 286 
LEU HD21   H  N N 287 
LEU HD22   H  N N 288 
LEU HD23   H  N N 289 
LEU HXT    H  N N 290 
LYS N      N  N N 291 
LYS CA     C  N S 292 
LYS C      C  N N 293 
LYS O      O  N N 294 
LYS CB     C  N N 295 
LYS CG     C  N N 296 
LYS CD     C  N N 297 
LYS CE     C  N N 298 
LYS NZ     N  N N 299 
LYS OXT    O  N N 300 
LYS H      H  N N 301 
LYS H2     H  N N 302 
LYS HA     H  N N 303 
LYS HB2    H  N N 304 
LYS HB3    H  N N 305 
LYS HG2    H  N N 306 
LYS HG3    H  N N 307 
LYS HD2    H  N N 308 
LYS HD3    H  N N 309 
LYS HE2    H  N N 310 
LYS HE3    H  N N 311 
LYS HZ1    H  N N 312 
LYS HZ2    H  N N 313 
LYS HZ3    H  N N 314 
LYS HXT    H  N N 315 
MET N      N  N N 316 
MET CA     C  N S 317 
MET C      C  N N 318 
MET O      O  N N 319 
MET CB     C  N N 320 
MET CG     C  N N 321 
MET SD     S  N N 322 
MET CE     C  N N 323 
MET OXT    O  N N 324 
MET H      H  N N 325 
MET H2     H  N N 326 
MET HA     H  N N 327 
MET HB2    H  N N 328 
MET HB3    H  N N 329 
MET HG2    H  N N 330 
MET HG3    H  N N 331 
MET HE1    H  N N 332 
MET HE2    H  N N 333 
MET HE3    H  N N 334 
MET HXT    H  N N 335 
MG  MG     MG N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
ATP PG    O1G    doub N N 114 
ATP PG    O2G    sing N N 115 
ATP PG    O3G    sing N N 116 
ATP PG    O3B    sing N N 117 
ATP O2G   HOG2   sing N N 118 
ATP O3G   HOG3   sing N N 119 
ATP PB    O1B    doub N N 120 
ATP PB    O2B    sing N N 121 
ATP PB    O3B    sing N N 122 
ATP PB    O3A    sing N N 123 
ATP O2B   HOB2   sing N N 124 
ATP PA    O1A    doub N N 125 
ATP PA    O2A    sing N N 126 
ATP PA    O3A    sing N N 127 
ATP PA    "O5'"  sing N N 128 
ATP O2A   HOA2   sing N N 129 
ATP "O5'" "C5'"  sing N N 130 
ATP "C5'" "C4'"  sing N N 131 
ATP "C5'" "H5'1" sing N N 132 
ATP "C5'" "H5'2" sing N N 133 
ATP "C4'" "O4'"  sing N N 134 
ATP "C4'" "C3'"  sing N N 135 
ATP "C4'" "H4'"  sing N N 136 
ATP "O4'" "C1'"  sing N N 137 
ATP "C3'" "O3'"  sing N N 138 
ATP "C3'" "C2'"  sing N N 139 
ATP "C3'" "H3'"  sing N N 140 
ATP "O3'" "HO3'" sing N N 141 
ATP "C2'" "O2'"  sing N N 142 
ATP "C2'" "C1'"  sing N N 143 
ATP "C2'" "H2'"  sing N N 144 
ATP "O2'" "HO2'" sing N N 145 
ATP "C1'" N9     sing N N 146 
ATP "C1'" "H1'"  sing N N 147 
ATP N9    C8     sing Y N 148 
ATP N9    C4     sing Y N 149 
ATP C8    N7     doub Y N 150 
ATP C8    H8     sing N N 151 
ATP N7    C5     sing Y N 152 
ATP C5    C6     sing Y N 153 
ATP C5    C4     doub Y N 154 
ATP C6    N6     sing N N 155 
ATP C6    N1     doub Y N 156 
ATP N6    HN61   sing N N 157 
ATP N6    HN62   sing N N 158 
ATP N1    C2     sing Y N 159 
ATP C2    N3     doub Y N 160 
ATP C2    H2     sing N N 161 
ATP N3    C4     sing Y N 162 
CYS N     CA     sing N N 163 
CYS N     H      sing N N 164 
CYS N     H2     sing N N 165 
CYS CA    C      sing N N 166 
CYS CA    CB     sing N N 167 
CYS CA    HA     sing N N 168 
CYS C     O      doub N N 169 
CYS C     OXT    sing N N 170 
CYS CB    SG     sing N N 171 
CYS CB    HB2    sing N N 172 
CYS CB    HB3    sing N N 173 
CYS SG    HG     sing N N 174 
CYS OXT   HXT    sing N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-02 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BML 
_em_admin.last_update        2025-04-30 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'State-2 of the motor domain from full-length human dynein-1 in 5mM AMPPNP' 
# 
_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                    9BML 
_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 ? 150.370 233.958 172.608 1.00 233.70 ? 1457 MET A N     1 
ATOM   2     C  CA    . MET A 1 1457 ? 150.461 233.967 171.153 1.00 234.10 ? 1457 MET A CA    1 
ATOM   3     C  C     . MET A 1 1457 ? 151.852 233.556 170.684 1.00 234.50 ? 1457 MET A C     1 
ATOM   4     O  O     . MET A 1 1457 ? 152.257 233.873 169.565 1.00 234.64 ? 1457 MET A O     1 
ATOM   5     C  CB    . MET A 1 1457 ? 150.108 235.353 170.600 1.00 233.88 ? 1457 MET A CB    1 
ATOM   6     C  CG    . MET A 1 1457 ? 148.974 236.091 171.323 1.00 233.38 ? 1457 MET A CG    1 
ATOM   7     S  SD    . MET A 1 1457 ? 147.549 235.154 171.943 1.00 232.51 ? 1457 MET A SD    1 
ATOM   8     C  CE    . MET A 1 1457 ? 147.134 234.068 170.572 1.00 232.77 ? 1457 MET A CE    1 
ATOM   9     N  N     . ALA A 1 1458 ? 152.582 232.849 171.550 1.00 237.77 ? 1458 ALA A N     1 
ATOM   10    C  CA    . ALA A 1 1458 ? 153.919 232.391 171.185 1.00 237.31 ? 1458 ALA A CA    1 
ATOM   11    C  C     . ALA A 1 1458 ? 153.873 231.352 170.074 1.00 238.10 ? 1458 ALA A C     1 
ATOM   12    O  O     . ALA A 1 1458 ? 154.865 231.165 169.357 1.00 238.64 ? 1458 ALA A O     1 
ATOM   13    C  CB    . ALA A 1 1458 ? 154.634 231.825 172.412 1.00 236.60 ? 1458 ALA A CB    1 
ATOM   14    N  N     . LEU A 1 1459 ? 152.738 230.665 169.919 1.00 240.96 ? 1459 LEU A N     1 
ATOM   15    C  CA    . LEU A 1 1459 ? 152.613 229.672 168.858 1.00 241.20 ? 1459 LEU A CA    1 
ATOM   16    C  C     . LEU A 1 1459 ? 152.789 230.308 167.486 1.00 241.15 ? 1459 LEU A C     1 
ATOM   17    O  O     . LEU A 1 1459 ? 153.566 229.814 166.660 1.00 241.19 ? 1459 LEU A O     1 
ATOM   18    C  CB    . LEU A 1 1459 ? 151.262 228.961 168.950 1.00 241.11 ? 1459 LEU A CB    1 
ATOM   19    C  CG    . LEU A 1 1459 ? 151.093 227.900 170.041 1.00 241.37 ? 1459 LEU A CG    1 
ATOM   20    C  CD1   . LEU A 1 1459 ? 150.682 228.529 171.365 1.00 240.37 ? 1459 LEU A CD1   1 
ATOM   21    C  CD2   . LEU A 1 1459 ? 150.086 226.842 169.609 1.00 241.17 ? 1459 LEU A CD2   1 
ATOM   22    N  N     . GLU A 1 1460 ? 152.091 231.417 167.235 1.00 239.13 ? 1460 GLU A N     1 
ATOM   23    C  CA    . GLU A 1 1460 ? 152.219 232.097 165.951 1.00 238.81 ? 1460 GLU A CA    1 
ATOM   24    C  C     . GLU A 1 1460 ? 153.625 232.651 165.758 1.00 239.38 ? 1460 GLU A C     1 
ATOM   25    O  O     . GLU A 1 1460 ? 154.157 232.641 164.642 1.00 239.18 ? 1460 GLU A O     1 
ATOM   26    C  CB    . GLU A 1 1460 ? 151.178 233.212 165.844 1.00 238.37 ? 1460 GLU A CB    1 
ATOM   27    C  CG    . GLU A 1 1460 ? 151.211 233.974 164.529 1.00 238.40 ? 1460 GLU A CG    1 
ATOM   28    C  CD    . GLU A 1 1460 ? 150.263 235.157 164.519 1.00 238.45 ? 1460 GLU A CD    1 
ATOM   29    O  OE1   . GLU A 1 1460 ? 150.481 236.102 165.306 1.00 238.33 ? 1460 GLU A OE1   1 
ATOM   30    O  OE2   . GLU A 1 1460 ? 149.301 235.143 163.723 1.00 238.26 ? 1460 GLU A OE2   1 
ATOM   31    N  N     . GLU A 1 1461 ? 154.245 233.139 166.836 1.00 241.19 ? 1461 GLU A N     1 
ATOM   32    C  CA    . GLU A 1 1461 ? 155.601 233.669 166.732 1.00 240.54 ? 1461 GLU A CA    1 
ATOM   33    C  C     . GLU A 1 1461 ? 156.590 232.587 166.315 1.00 240.21 ? 1461 GLU A C     1 
ATOM   34    O  O     . GLU A 1 1461 ? 157.400 232.793 165.404 1.00 240.07 ? 1461 GLU A O     1 
ATOM   35    C  CB    . GLU A 1 1461 ? 156.024 234.298 168.059 1.00 239.77 ? 1461 GLU A CB    1 
ATOM   36    C  CG    . GLU A 1 1461 ? 155.019 235.284 168.634 1.00 239.70 ? 1461 GLU A CG    1 
ATOM   37    C  CD    . GLU A 1 1461 ? 154.396 236.171 167.573 1.00 239.82 ? 1461 GLU A CD    1 
ATOM   38    O  OE1   . GLU A 1 1461 ? 155.143 236.911 166.899 1.00 239.53 ? 1461 GLU A OE1   1 
ATOM   39    O  OE2   . GLU A 1 1461 ? 153.158 236.126 167.412 1.00 239.85 ? 1461 GLU A OE2   1 
ATOM   40    N  N     . PHE A 1 1462 ? 156.533 231.420 166.961 1.00 239.20 ? 1462 PHE A N     1 
ATOM   41    C  CA    . PHE A 1 1462 ? 157.451 230.349 166.587 1.00 239.28 ? 1462 PHE A CA    1 
ATOM   42    C  C     . PHE A 1 1462 ? 157.114 229.782 165.213 1.00 238.72 ? 1462 PHE A C     1 
ATOM   43    O  O     . PHE A 1 1462 ? 158.009 229.334 164.487 1.00 238.07 ? 1462 PHE A O     1 
ATOM   44    C  CB    . PHE A 1 1462 ? 157.447 229.246 167.643 1.00 238.47 ? 1462 PHE A CB    1 
ATOM   45    C  CG    . PHE A 1 1462 ? 158.350 229.514 168.813 1.00 238.72 ? 1462 PHE A CG    1 
ATOM   46    C  CD1   . PHE A 1 1462 ? 158.182 230.643 169.597 1.00 238.83 ? 1462 PHE A CD1   1 
ATOM   47    C  CD2   . PHE A 1 1462 ? 159.367 228.628 169.133 1.00 237.91 ? 1462 PHE A CD2   1 
ATOM   48    C  CE1   . PHE A 1 1462 ? 159.014 230.886 170.675 1.00 238.13 ? 1462 PHE A CE1   1 
ATOM   49    C  CE2   . PHE A 1 1462 ? 160.201 228.864 170.209 1.00 237.37 ? 1462 PHE A CE2   1 
ATOM   50    C  CZ    . PHE A 1 1462 ? 160.024 229.995 170.981 1.00 237.40 ? 1462 PHE A CZ    1 
ATOM   51    N  N     . LEU A 1 1463 ? 155.833 229.791 164.830 1.00 237.12 ? 1463 LEU A N     1 
ATOM   52    C  CA    . LEU A 1 1463 ? 155.483 229.388 163.471 1.00 236.76 ? 1463 LEU A CA    1 
ATOM   53    C  C     . LEU A 1 1463 ? 156.103 230.329 162.446 1.00 236.36 ? 1463 LEU A C     1 
ATOM   54    O  O     . LEU A 1 1463 ? 156.640 229.883 161.426 1.00 235.93 ? 1463 LEU A O     1 
ATOM   55    C  CB    . LEU A 1 1463 ? 153.964 229.332 163.303 1.00 236.24 ? 1463 LEU A CB    1 
ATOM   56    C  CG    . LEU A 1 1463 ? 153.224 228.172 163.975 1.00 236.20 ? 1463 LEU A CG    1 
ATOM   57    C  CD1   . LEU A 1 1463 ? 151.895 227.910 163.283 1.00 235.24 ? 1463 LEU A CD1   1 
ATOM   58    C  CD2   . LEU A 1 1463 ? 154.079 226.912 163.997 1.00 236.29 ? 1463 LEU A CD2   1 
ATOM   59    N  N     . LYS A 1 1464 ? 156.050 231.637 162.705 1.00 234.35 ? 1464 LYS A N     1 
ATOM   60    C  CA    . LYS A 1 1464 ? 156.706 232.593 161.819 1.00 234.03 ? 1464 LYS A CA    1 
ATOM   61    C  C     . LYS A 1 1464 ? 158.213 232.370 161.797 1.00 234.41 ? 1464 LYS A C     1 
ATOM   62    O  O     . LYS A 1 1464 ? 158.854 232.494 160.745 1.00 234.50 ? 1464 LYS A O     1 
ATOM   63    C  CB    . LYS A 1 1464 ? 156.380 234.022 162.256 1.00 233.89 ? 1464 LYS A CB    1 
ATOM   64    C  CG    . LYS A 1 1464 ? 156.787 235.091 161.254 1.00 233.81 ? 1464 LYS A CG    1 
ATOM   65    C  CD    . LYS A 1 1464 ? 156.326 234.737 159.851 1.00 233.61 ? 1464 LYS A CD    1 
ATOM   66    C  CE    . LYS A 1 1464 ? 156.875 235.711 158.823 1.00 233.61 ? 1464 LYS A CE    1 
ATOM   67    N  NZ    . LYS A 1 1464 ? 156.590 235.264 157.431 1.00 233.60 ? 1464 LYS A NZ    1 
ATOM   68    N  N     . GLN A 1 1465 ? 158.794 232.043 162.954 1.00 233.80 ? 1465 GLN A N     1 
ATOM   69    C  CA    . GLN A 1 1465 ? 160.224 231.752 163.013 1.00 233.30 ? 1465 GLN A CA    1 
ATOM   70    C  C     . GLN A 1 1465 ? 160.578 230.562 162.129 1.00 233.54 ? 1465 GLN A C     1 
ATOM   71    O  O     . GLN A 1 1465 ? 161.559 230.602 161.378 1.00 234.04 ? 1465 GLN A O     1 
ATOM   72    C  CB    . GLN A 1 1465 ? 160.645 231.487 164.459 1.00 232.64 ? 1465 GLN A CB    1 
ATOM   73    C  CG    . GLN A 1 1465 ? 160.599 232.706 165.361 1.00 232.87 ? 1465 GLN A CG    1 
ATOM   74    C  CD    . GLN A 1 1465 ? 160.609 232.338 166.832 1.00 233.21 ? 1465 GLN A CD    1 
ATOM   75    O  OE1   . GLN A 1 1465 ? 159.724 232.734 167.589 1.00 233.55 ? 1465 GLN A OE1   1 
ATOM   76    N  NE2   . GLN A 1 1465 ? 161.614 231.573 167.243 1.00 233.15 ? 1465 GLN A NE2   1 
ATOM   77    N  N     . ILE A 1 1466 ? 159.782 229.493 162.202 1.00 230.97 ? 1466 ILE A N     1 
ATOM   78    C  CA    . ILE A 1 1466 ? 160.054 228.307 161.393 1.00 230.85 ? 1466 ILE A CA    1 
ATOM   79    C  C     . ILE A 1 1466 ? 159.847 228.611 159.914 1.00 231.00 ? 1466 ILE A C     1 
ATOM   80    O  O     . ILE A 1 1466 ? 160.596 228.127 159.054 1.00 230.87 ? 1466 ILE A O     1 
ATOM   81    C  CB    . ILE A 1 1466 ? 159.183 227.125 161.861 1.00 230.68 ? 1466 ILE A CB    1 
ATOM   82    C  CG1   . ILE A 1 1466 ? 159.473 226.793 163.325 1.00 230.24 ? 1466 ILE A CG1   1 
ATOM   83    C  CG2   . ILE A 1 1466 ? 159.432 225.899 160.997 1.00 230.40 ? 1466 ILE A CG2   1 
ATOM   84    C  CD1   . ILE A 1 1466 ? 158.338 226.074 164.022 1.00 230.05 ? 1466 ILE A CD1   1 
ATOM   85    N  N     . ARG A 1 1467 ? 158.829 229.416 159.592 1.00 233.13 ? 1467 ARG A N     1 
ATOM   86    C  CA    . ARG A 1 1467 ? 158.619 229.827 158.207 1.00 232.85 ? 1467 ARG A CA    1 
ATOM   87    C  C     . ARG A 1 1467 ? 159.835 230.566 157.667 1.00 233.12 ? 1467 ARG A C     1 
ATOM   88    O  O     . ARG A 1 1467 ? 160.303 230.282 156.558 1.00 232.93 ? 1467 ARG A O     1 
ATOM   89    C  CB    . ARG A 1 1467 ? 157.378 230.715 158.094 1.00 233.05 ? 1467 ARG A CB    1 
ATOM   90    C  CG    . ARG A 1 1467 ? 157.153 231.274 156.694 1.00 232.35 ? 1467 ARG A CG    1 
ATOM   91    C  CD    . ARG A 1 1467 ? 155.831 232.029 156.541 1.00 232.31 ? 1467 ARG A CD    1 
ATOM   92    N  NE    . ARG A 1 1467 ? 154.651 231.257 156.921 1.00 232.90 ? 1467 ARG A NE    1 
ATOM   93    C  CZ    . ARG A 1 1467 ? 154.048 231.334 158.100 1.00 233.40 ? 1467 ARG A CZ    1 
ATOM   94    N  NH1   . ARG A 1 1467 ? 154.504 232.120 159.061 1.00 233.31 ? 1467 ARG A NH1   1 
ATOM   95    N  NH2   . ARG A 1 1467 ? 152.954 230.610 158.317 1.00 232.90 ? 1467 ARG A NH2   1 
ATOM   96    N  N     . GLU A 1 1468 ? 160.358 231.519 158.441 1.00 234.92 ? 1468 GLU A N     1 
ATOM   97    C  CA    . GLU A 1 1468 ? 161.532 232.267 158.005 1.00 234.50 ? 1468 GLU A CA    1 
ATOM   98    C  C     . GLU A 1 1468 ? 162.752 231.362 157.883 1.00 234.23 ? 1468 GLU A C     1 
ATOM   99    O  O     . GLU A 1 1468 ? 163.532 231.490 156.932 1.00 234.59 ? 1468 GLU A O     1 
ATOM   100   C  CB    . GLU A 1 1468 ? 161.809 233.420 158.969 1.00 234.29 ? 1468 GLU A CB    1 
ATOM   101   C  CG    . GLU A 1 1468 ? 160.799 234.557 158.884 1.00 234.45 ? 1468 GLU A CG    1 
ATOM   102   C  CD    . GLU A 1 1468 ? 160.944 235.384 157.618 1.00 234.82 ? 1468 GLU A CD    1 
ATOM   103   O  OE1   . GLU A 1 1468 ? 161.946 235.207 156.894 1.00 234.92 ? 1468 GLU A OE1   1 
ATOM   104   O  OE2   . GLU A 1 1468 ? 160.050 236.213 157.345 1.00 234.89 ? 1468 GLU A OE2   1 
ATOM   105   N  N     . VAL A 1 1469 ? 162.930 230.440 158.832 1.00 228.44 ? 1469 VAL A N     1 
ATOM   106   C  CA    . VAL A 1 1469 ? 164.072 229.531 158.782 1.00 228.33 ? 1469 VAL A CA    1 
ATOM   107   C  C     . VAL A 1 1469 ? 164.022 228.678 157.521 1.00 228.64 ? 1469 VAL A C     1 
ATOM   108   O  O     . VAL A 1 1469 ? 165.032 228.515 156.825 1.00 228.70 ? 1469 VAL A O     1 
ATOM   109   C  CB    . VAL A 1 1469 ? 164.124 228.662 160.053 1.00 227.73 ? 1469 VAL A CB    1 
ATOM   110   C  CG1   . VAL A 1 1469 ? 165.109 227.518 159.875 1.00 227.55 ? 1469 VAL A CG1   1 
ATOM   111   C  CG2   . VAL A 1 1469 ? 164.516 229.507 161.253 1.00 227.25 ? 1469 VAL A CG2   1 
ATOM   112   N  N     . TRP A 1 1470 ? 162.848 228.130 157.198 1.00 224.60 ? 1470 TRP A N     1 
ATOM   113   C  CA    . TRP A 1 1470 ? 162.745 227.293 156.008 1.00 223.98 ? 1470 TRP A CA    1 
ATOM   114   C  C     . TRP A 1 1470 ? 162.869 228.104 154.724 1.00 224.13 ? 1470 TRP A C     1 
ATOM   115   O  O     . TRP A 1 1470 ? 163.509 227.647 153.770 1.00 224.11 ? 1470 TRP A O     1 
ATOM   116   C  CB    . TRP A 1 1470 ? 161.438 226.501 156.021 1.00 223.52 ? 1470 TRP A CB    1 
ATOM   117   C  CG    . TRP A 1 1470 ? 161.511 225.263 156.865 1.00 224.37 ? 1470 TRP A CG    1 
ATOM   118   C  CD1   . TRP A 1 1470 ? 160.660 224.904 157.869 1.00 224.10 ? 1470 TRP A CD1   1 
ATOM   119   C  CD2   . TRP A 1 1470 ? 162.493 224.221 156.779 1.00 223.88 ? 1470 TRP A CD2   1 
ATOM   120   N  NE1   . TRP A 1 1470 ? 161.050 223.704 158.412 1.00 223.62 ? 1470 TRP A NE1   1 
ATOM   121   C  CE2   . TRP A 1 1470 ? 162.172 223.264 157.761 1.00 223.43 ? 1470 TRP A CE2   1 
ATOM   122   C  CE3   . TRP A 1 1470 ? 163.610 224.003 155.965 1.00 223.21 ? 1470 TRP A CE3   1 
ATOM   123   C  CZ2   . TRP A 1 1470 ? 162.929 222.111 157.952 1.00 223.27 ? 1470 TRP A CZ2   1 
ATOM   124   C  CZ3   . TRP A 1 1470 ? 164.359 222.859 156.158 1.00 222.84 ? 1470 TRP A CZ3   1 
ATOM   125   C  CH2   . TRP A 1 1470 ? 164.015 221.928 157.142 1.00 222.89 ? 1470 TRP A CH2   1 
ATOM   126   N  N     . ASN A 1 1471 ? 162.279 229.302 154.676 1.00 228.24 ? 1471 ASN A N     1 
ATOM   127   C  CA    . ASN A 1 1471 ? 162.393 230.121 153.474 1.00 227.84 ? 1471 ASN A CA    1 
ATOM   128   C  C     . ASN A 1 1471 ? 163.823 230.594 153.251 1.00 227.67 ? 1471 ASN A C     1 
ATOM   129   O  O     . ASN A 1 1471 ? 164.232 230.805 152.104 1.00 227.12 ? 1471 ASN A O     1 
ATOM   130   C  CB    . ASN A 1 1471 ? 161.441 231.314 153.556 1.00 227.62 ? 1471 ASN A CB    1 
ATOM   131   C  CG    . ASN A 1 1471 ? 159.985 230.903 153.457 1.00 227.54 ? 1471 ASN A CG    1 
ATOM   132   O  OD1   . ASN A 1 1471 ? 159.665 229.716 153.396 1.00 227.26 ? 1471 ASN A OD1   1 
ATOM   133   N  ND2   . ASN A 1 1471 ? 159.093 231.887 153.439 1.00 227.62 ? 1471 ASN A ND2   1 
ATOM   134   N  N     . THR A 1 1472 ? 164.595 230.763 154.324 1.00 226.05 ? 1472 THR A N     1 
ATOM   135   C  CA    . THR A 1 1472 ? 165.994 231.148 154.215 1.00 225.40 ? 1472 THR A CA    1 
ATOM   136   C  C     . THR A 1 1472 ? 166.938 229.957 154.124 1.00 224.79 ? 1472 THR A C     1 
ATOM   137   O  O     . THR A 1 1472 ? 168.098 230.137 153.736 1.00 224.40 ? 1472 THR A O     1 
ATOM   138   C  CB    . THR A 1 1472 ? 166.400 232.024 155.407 1.00 225.24 ? 1472 THR A CB    1 
ATOM   139   O  OG1   . THR A 1 1472 ? 166.080 231.349 156.630 1.00 225.80 ? 1472 THR A OG1   1 
ATOM   140   C  CG2   . THR A 1 1472 ? 165.669 233.358 155.362 1.00 224.73 ? 1472 THR A CG2   1 
ATOM   141   N  N     . TYR A 1 1473 ? 166.479 228.756 154.468 1.00 214.21 ? 1473 TYR A N     1 
ATOM   142   C  CA    . TYR A 1 1473 ? 167.337 227.581 154.400 1.00 213.66 ? 1473 TYR A CA    1 
ATOM   143   C  C     . TYR A 1 1473 ? 167.594 227.203 152.948 1.00 213.69 ? 1473 TYR A C     1 
ATOM   144   O  O     . TYR A 1 1473 ? 166.659 227.086 152.149 1.00 213.30 ? 1473 TYR A O     1 
ATOM   145   C  CB    . TYR A 1 1473 ? 166.701 226.411 155.149 1.00 212.77 ? 1473 TYR A CB    1 
ATOM   146   C  CG    . TYR A 1 1473 ? 167.695 225.396 155.669 1.00 213.08 ? 1473 TYR A CG    1 
ATOM   147   C  CD1   . TYR A 1 1473 ? 168.380 224.555 154.802 1.00 212.88 ? 1473 TYR A CD1   1 
ATOM   148   C  CD2   . TYR A 1 1473 ? 167.948 225.278 157.030 1.00 213.23 ? 1473 TYR A CD2   1 
ATOM   149   C  CE1   . TYR A 1 1473 ? 169.289 223.627 155.274 1.00 212.80 ? 1473 TYR A CE1   1 
ATOM   150   C  CE2   . TYR A 1 1473 ? 168.855 224.353 157.511 1.00 212.89 ? 1473 TYR A CE2   1 
ATOM   151   C  CZ    . TYR A 1 1473 ? 169.522 223.530 156.629 1.00 213.07 ? 1473 TYR A CZ    1 
ATOM   152   O  OH    . TYR A 1 1473 ? 170.426 222.608 157.103 1.00 213.75 ? 1473 TYR A OH    1 
ATOM   153   N  N     . GLU A 1 1474 ? 168.865 227.009 152.607 1.00 205.74 ? 1474 GLU A N     1 
ATOM   154   C  CA    . GLU A 1 1474 ? 169.261 226.594 151.271 1.00 204.82 ? 1474 GLU A CA    1 
ATOM   155   C  C     . GLU A 1 1474 ? 170.157 225.369 151.362 1.00 204.39 ? 1474 GLU A C     1 
ATOM   156   O  O     . GLU A 1 1474 ? 170.799 225.119 152.386 1.00 203.89 ? 1474 GLU A O     1 
ATOM   157   C  CB    . GLU A 1 1474 ? 169.983 227.713 150.512 1.00 204.28 ? 1474 GLU A CB    1 
ATOM   158   C  CG    . GLU A 1 1474 ? 169.049 228.679 149.806 1.00 204.64 ? 1474 GLU A CG    1 
ATOM   159   C  CD    . GLU A 1 1474 ? 169.758 229.515 148.760 1.00 204.83 ? 1474 GLU A CD    1 
ATOM   160   O  OE1   . GLU A 1 1474 ? 171.000 229.423 148.667 1.00 204.59 ? 1474 GLU A OE1   1 
ATOM   161   O  OE2   . GLU A 1 1474 ? 169.074 230.260 148.029 1.00 205.04 ? 1474 GLU A OE2   1 
ATOM   162   N  N     . LEU A 1 1475 ? 170.190 224.610 150.273 1.00 196.35 ? 1475 LEU A N     1 
ATOM   163   C  CA    . LEU A 1 1475 ? 170.927 223.355 150.242 1.00 196.07 ? 1475 LEU A CA    1 
ATOM   164   C  C     . LEU A 1 1475 ? 172.401 223.622 149.955 1.00 195.74 ? 1475 LEU A C     1 
ATOM   165   O  O     . LEU A 1 1475 ? 172.752 224.099 148.871 1.00 196.26 ? 1475 LEU A O     1 
ATOM   166   C  CB    . LEU A 1 1475 ? 170.323 222.436 149.186 1.00 196.03 ? 1475 LEU A CB    1 
ATOM   167   C  CG    . LEU A 1 1475 ? 170.240 220.946 149.501 1.00 195.25 ? 1475 LEU A CG    1 
ATOM   168   C  CD1   . LEU A 1 1475 ? 169.132 220.678 150.504 1.00 194.97 ? 1475 LEU A CD1   1 
ATOM   169   C  CD2   . LEU A 1 1475 ? 169.992 220.177 148.222 1.00 195.69 ? 1475 LEU A CD2   1 
ATOM   170   N  N     . ASP A 1 1476 ? 173.260 223.316 150.925 1.00 192.20 ? 1476 ASP A N     1 
ATOM   171   C  CA    . ASP A 1 1476 ? 174.698 223.525 150.777 1.00 192.70 ? 1476 ASP A CA    1 
ATOM   172   C  C     . ASP A 1 1476 ? 175.239 222.583 149.708 1.00 193.68 ? 1476 ASP A C     1 
ATOM   173   O  O     . ASP A 1 1476 ? 175.053 221.365 149.792 1.00 195.35 ? 1476 ASP A O     1 
ATOM   174   C  CB    . ASP A 1 1476 ? 175.401 223.300 152.112 1.00 194.02 ? 1476 ASP A CB    1 
ATOM   175   C  CG    . ASP A 1 1476 ? 176.800 223.881 152.141 1.00 194.08 ? 1476 ASP A CG    1 
ATOM   176   O  OD1   . ASP A 1 1476 ? 177.154 224.627 151.205 1.00 194.91 ? 1476 ASP A OD1   1 
ATOM   177   O  OD2   . ASP A 1 1476 ? 177.547 223.589 153.099 1.00 192.60 ? 1476 ASP A OD2   1 
ATOM   178   N  N     . LEU A 1 1477 ? 175.909 223.140 148.702 1.00 188.66 ? 1477 LEU A N     1 
ATOM   179   C  CA    . LEU A 1 1477 ? 176.384 222.377 147.557 1.00 189.23 ? 1477 LEU A CA    1 
ATOM   180   C  C     . LEU A 1 1477 ? 177.896 222.500 147.416 1.00 189.43 ? 1477 LEU A C     1 
ATOM   181   O  O     . LEU A 1 1477 ? 178.453 223.596 147.531 1.00 189.54 ? 1477 LEU A O     1 
ATOM   182   C  CB    . LEU A 1 1477 ? 175.695 222.847 146.273 1.00 189.29 ? 1477 LEU A CB    1 
ATOM   183   C  CG    . LEU A 1 1477 ? 174.173 222.683 146.241 1.00 188.25 ? 1477 LEU A CG    1 
ATOM   184   C  CD1   . LEU A 1 1477 ? 173.630 222.950 144.847 1.00 188.49 ? 1477 LEU A CD1   1 
ATOM   185   C  CD2   . LEU A 1 1477 ? 173.765 221.298 146.721 1.00 189.21 ? 1477 LEU A CD2   1 
ATOM   186   N  N     . VAL A 1 1478 ? 178.556 221.367 147.163 1.00 186.95 ? 1478 VAL A N     1 
ATOM   187   C  CA    . VAL A 1 1478 ? 180.000 221.309 146.963 1.00 186.37 ? 1478 VAL A CA    1 
ATOM   188   C  C     . VAL A 1 1478 ? 180.292 220.457 145.733 1.00 186.48 ? 1478 VAL A C     1 
ATOM   189   O  O     . VAL A 1 1478 ? 179.613 219.455 145.484 1.00 186.91 ? 1478 VAL A O     1 
ATOM   190   C  CB    . VAL A 1 1478 ? 180.737 220.755 148.204 1.00 185.83 ? 1478 VAL A CB    1 
ATOM   191   C  CG1   . VAL A 1 1478 ? 180.456 221.619 149.420 1.00 185.70 ? 1478 VAL A CG1   1 
ATOM   192   C  CG2   . VAL A 1 1478 ? 180.335 219.312 148.478 1.00 186.05 ? 1478 VAL A CG2   1 
ATOM   193   N  N     . ASN A 1 1479 ? 181.305 220.856 144.967 1.00 189.49 ? 1479 ASN A N     1 
ATOM   194   C  CA    . ASN A 1 1479 ? 181.586 220.215 143.689 1.00 189.98 ? 1479 ASN A CA    1 
ATOM   195   C  C     . ASN A 1 1479 ? 182.200 218.830 143.876 1.00 190.30 ? 1479 ASN A C     1 
ATOM   196   O  O     . ASN A 1 1479 ? 182.700 218.484 144.950 1.00 190.26 ? 1479 ASN A O     1 
ATOM   197   C  CB    . ASN A 1 1479 ? 182.521 221.087 142.851 1.00 190.47 ? 1479 ASN A CB    1 
ATOM   198   C  CG    . ASN A 1 1479 ? 183.918 221.172 143.435 1.00 190.04 ? 1479 ASN A CG    1 
ATOM   199   O  OD1   . ASN A 1 1479 ? 184.103 221.082 144.648 1.00 189.76 ? 1479 ASN A OD1   1 
ATOM   200   N  ND2   . ASN A 1 1479 ? 184.910 221.345 142.569 1.00 189.50 ? 1479 ASN A ND2   1 
ATOM   201   N  N     . TYR A 1 1480 ? 182.155 218.032 142.805 1.00 191.64 ? 1480 TYR A N     1 
ATOM   202   C  CA    . TYR A 1 1480 ? 182.727 216.683 142.771 1.00 191.43 ? 1480 TYR A CA    1 
ATOM   203   C  C     . TYR A 1 1480 ? 183.493 216.525 141.463 1.00 191.71 ? 1480 TYR A C     1 
ATOM   204   O  O     . TYR A 1 1480 ? 182.930 216.058 140.470 1.00 192.83 ? 1480 TYR A O     1 
ATOM   205   C  CB    . TYR A 1 1480 ? 181.643 215.624 142.899 1.00 191.90 ? 1480 TYR A CB    1 
ATOM   206   C  CG    . TYR A 1 1480 ? 182.150 214.201 142.938 1.00 192.17 ? 1480 TYR A CG    1 
ATOM   207   C  CD1   . TYR A 1 1480 ? 182.852 213.724 144.037 1.00 190.83 ? 1480 TYR A CD1   1 
ATOM   208   C  CD2   . TYR A 1 1480 ? 181.912 213.329 141.884 1.00 192.59 ? 1480 TYR A CD2   1 
ATOM   209   C  CE1   . TYR A 1 1480 ? 183.311 212.422 144.081 1.00 190.93 ? 1480 TYR A CE1   1 
ATOM   210   C  CE2   . TYR A 1 1480 ? 182.367 212.024 141.919 1.00 192.02 ? 1480 TYR A CE2   1 
ATOM   211   C  CZ    . TYR A 1 1480 ? 183.066 211.576 143.019 1.00 191.25 ? 1480 TYR A CZ    1 
ATOM   212   O  OH    . TYR A 1 1480 ? 183.521 210.278 143.059 1.00 190.64 ? 1480 TYR A OH    1 
ATOM   213   N  N     . GLN A 1 1481 ? 184.773 216.901 141.472 1.00 189.93 ? 1481 GLN A N     1 
ATOM   214   C  CA    . GLN A 1 1481 ? 185.638 216.767 140.298 1.00 190.80 ? 1481 GLN A CA    1 
ATOM   215   C  C     . GLN A 1 1481 ? 185.016 217.432 139.071 1.00 191.09 ? 1481 GLN A C     1 
ATOM   216   O  O     . GLN A 1 1481 ? 185.094 216.913 137.955 1.00 190.91 ? 1481 GLN A O     1 
ATOM   217   C  CB    . GLN A 1 1481 ? 185.961 215.298 140.018 1.00 190.41 ? 1481 GLN A CB    1 
ATOM   218   C  CG    . GLN A 1 1481 ? 186.409 214.522 141.247 1.00 190.35 ? 1481 GLN A CG    1 
ATOM   219   C  CD    . GLN A 1 1481 ? 186.445 213.024 141.014 1.00 190.10 ? 1481 GLN A CD    1 
ATOM   220   O  OE1   . GLN A 1 1481 ? 186.092 212.542 139.938 1.00 189.68 ? 1481 GLN A OE1   1 
ATOM   221   N  NE2   . GLN A 1 1481 ? 186.876 212.279 142.026 1.00 189.61 ? 1481 GLN A NE2   1 
ATOM   222   N  N     . ASN A 1 1482 ? 184.387 218.590 139.286 1.00 191.29 ? 1482 ASN A N     1 
ATOM   223   C  CA    . ASN A 1 1482 ? 183.721 219.349 138.226 1.00 191.05 ? 1482 ASN A CA    1 
ATOM   224   C  C     . ASN A 1 1482 ? 182.659 218.519 137.509 1.00 192.08 ? 1482 ASN A C     1 
ATOM   225   O  O     . ASN A 1 1482 ? 182.577 218.526 136.278 1.00 193.11 ? 1482 ASN A O     1 
ATOM   226   C  CB    . ASN A 1 1482 ? 184.735 219.905 137.223 1.00 191.96 ? 1482 ASN A CB    1 
ATOM   227   C  CG    . ASN A 1 1482 ? 185.985 220.431 137.895 1.00 191.95 ? 1482 ASN A CG    1 
ATOM   228   O  OD1   . ASN A 1 1482 ? 185.917 221.057 138.953 1.00 191.80 ? 1482 ASN A OD1   1 
ATOM   229   N  ND2   . ASN A 1 1482 ? 187.138 220.178 137.286 1.00 192.24 ? 1482 ASN A ND2   1 
ATOM   230   N  N     . LYS A 1 1483 ? 181.846 217.789 138.274 1.00 188.53 ? 1483 LYS A N     1 
ATOM   231   C  CA    . LYS A 1 1483 ? 180.754 216.984 137.736 1.00 188.00 ? 1483 LYS A CA    1 
ATOM   232   C  C     . LYS A 1 1483 ? 179.389 217.365 138.295 1.00 187.16 ? 1483 LYS A C     1 
ATOM   233   O  O     . LYS A 1 1483 ? 178.428 217.493 137.531 1.00 185.92 ? 1483 LYS A O     1 
ATOM   234   C  CB    . LYS A 1 1483 ? 181.000 215.497 138.012 1.00 188.19 ? 1483 LYS A CB    1 
ATOM   235   C  CG    . LYS A 1 1483 ? 182.279 214.924 137.431 1.00 187.66 ? 1483 LYS A CG    1 
ATOM   236   C  CD    . LYS A 1 1483 ? 182.662 213.654 138.179 1.00 187.61 ? 1483 LYS A CD    1 
ATOM   237   C  CE    . LYS A 1 1483 ? 183.809 212.927 137.505 1.00 187.24 ? 1483 LYS A CE    1 
ATOM   238   N  NZ    . LYS A 1 1483 ? 183.363 212.278 136.243 1.00 187.07 ? 1483 LYS A NZ    1 
ATOM   239   N  N     . CYS A 1 1484 ? 179.284 217.554 139.605 1.00 189.03 ? 1484 CYS A N     1 
ATOM   240   C  CA    . CYS A 1 1484 ? 178.013 217.789 140.290 1.00 188.62 ? 1484 CYS A CA    1 
ATOM   241   C  C     . CYS A 1 1484 ? 178.305 218.576 141.565 1.00 188.32 ? 1484 CYS A C     1 
ATOM   242   O  O     . CYS A 1 1484 ? 179.463 218.709 141.977 1.00 188.24 ? 1484 CYS A O     1 
ATOM   243   C  CB    . CYS A 1 1484 ? 177.297 216.471 140.584 1.00 189.52 ? 1484 CYS A CB    1 
ATOM   244   S  SG    . CYS A 1 1484 ? 177.639 215.824 142.234 1.00 191.85 ? 1484 CYS A SG    1 
ATOM   245   N  N     . ARG A 1 1485 ? 177.251 219.098 142.192 1.00 189.03 ? 1485 ARG A N     1 
ATOM   246   C  CA    . ARG A 1 1485 ? 177.352 219.872 143.429 1.00 189.70 ? 1485 ARG A CA    1 
ATOM   247   C  C     . ARG A 1 1485 ? 176.551 219.142 144.506 1.00 190.49 ? 1485 ARG A C     1 
ATOM   248   O  O     . ARG A 1 1485 ? 175.329 219.299 144.587 1.00 189.91 ? 1485 ARG A O     1 
ATOM   249   C  CB    . ARG A 1 1485 ? 176.841 221.296 143.222 1.00 189.51 ? 1485 ARG A CB    1 
ATOM   250   C  CG    . ARG A 1 1485 ? 177.565 222.073 142.132 1.00 189.40 ? 1485 ARG A CG    1 
ATOM   251   C  CD    . ARG A 1 1485 ? 178.417 223.181 142.723 1.00 189.94 ? 1485 ARG A CD    1 
ATOM   252   N  NE    . ARG A 1 1485 ? 177.636 224.079 143.566 1.00 190.51 ? 1485 ARG A NE    1 
ATOM   253   C  CZ    . ARG A 1 1485 ? 176.763 224.970 143.116 1.00 189.76 ? 1485 ARG A CZ    1 
ATOM   254   N  NH1   . ARG A 1 1485 ? 176.534 225.124 141.822 1.00 189.84 ? 1485 ARG A NH1   1 
ATOM   255   N  NH2   . ARG A 1 1485 ? 176.107 225.732 143.987 1.00 189.18 ? 1485 ARG A NH2   1 
ATOM   256   N  N     . LEU A 1 1486 ? 177.236 218.372 145.351 1.00 187.91 ? 1486 LEU A N     1 
ATOM   257   C  CA    . LEU A 1 1486 ? 176.553 217.467 146.269 1.00 186.20 ? 1486 LEU A CA    1 
ATOM   258   C  C     . LEU A 1 1486 ? 175.936 218.213 147.441 1.00 186.62 ? 1486 LEU A C     1 
ATOM   259   O  O     . LEU A 1 1486 ? 176.373 219.301 147.820 1.00 187.65 ? 1486 LEU A O     1 
ATOM   260   C  CB    . LEU A 1 1486 ? 177.495 216.401 146.832 1.00 185.94 ? 1486 LEU A CB    1 
ATOM   261   C  CG    . LEU A 1 1486 ? 178.341 215.493 145.947 1.00 185.53 ? 1486 LEU A CG    1 
ATOM   262   C  CD1   . LEU A 1 1486 ? 179.507 216.261 145.392 1.00 186.15 ? 1486 LEU A CD1   1 
ATOM   263   C  CD2   . LEU A 1 1486 ? 178.816 214.286 146.736 1.00 185.53 ? 1486 LEU A CD2   1 
ATOM   264   N  N     . ILE A 1 1487 ? 174.919 217.589 148.033 1.00 184.97 ? 1487 ILE A N     1 
ATOM   265   C  CA    . ILE A 1 1487 ? 174.336 218.100 149.264 1.00 185.13 ? 1487 ILE A CA    1 
ATOM   266   C  C     . ILE A 1 1487 ? 175.304 217.863 150.415 1.00 184.70 ? 1487 ILE A C     1 
ATOM   267   O  O     . ILE A 1 1487 ? 175.805 216.748 150.612 1.00 185.26 ? 1487 ILE A O     1 
ATOM   268   C  CB    . ILE A 1 1487 ? 172.982 217.422 149.527 1.00 185.42 ? 1487 ILE A CB    1 
ATOM   269   C  CG1   . ILE A 1 1487 ? 172.171 217.343 148.231 1.00 184.60 ? 1487 ILE A CG1   1 
ATOM   270   C  CG2   . ILE A 1 1487 ? 172.219 218.157 150.618 1.00 184.93 ? 1487 ILE A CG2   1 
ATOM   271   C  CD1   . ILE A 1 1487 ? 170.821 216.681 148.390 1.00 184.44 ? 1487 ILE A CD1   1 
ATOM   272   N  N     . ARG A 1 1488 ? 175.577 218.916 151.180 1.00 185.93 ? 1488 ARG A N     1 
ATOM   273   C  CA    . ARG A 1 1488 ? 176.459 218.829 152.332 1.00 185.72 ? 1488 ARG A CA    1 
ATOM   274   C  C     . ARG A 1 1488 ? 175.750 219.403 153.549 1.00 186.76 ? 1488 ARG A C     1 
ATOM   275   O  O     . ARG A 1 1488 ? 174.923 220.311 153.435 1.00 187.78 ? 1488 ARG A O     1 
ATOM   276   C  CB    . ARG A 1 1488 ? 177.783 219.571 152.093 1.00 186.62 ? 1488 ARG A CB    1 
ATOM   277   C  CG    . ARG A 1 1488 ? 178.878 219.214 153.087 1.00 186.24 ? 1488 ARG A CG    1 
ATOM   278   C  CD    . ARG A 1 1488 ? 180.145 220.020 152.850 1.00 186.76 ? 1488 ARG A CD    1 
ATOM   279   N  NE    . ARG A 1 1488 ? 179.908 221.455 152.947 1.00 187.02 ? 1488 ARG A NE    1 
ATOM   280   C  CZ    . ARG A 1 1488 ? 180.836 222.381 152.751 1.00 187.25 ? 1488 ARG A CZ    1 
ATOM   281   N  NH1   . ARG A 1 1488 ? 182.083 222.056 152.447 1.00 187.06 ? 1488 ARG A NH1   1 
ATOM   282   N  NH2   . ARG A 1 1488 ? 180.506 223.664 152.861 1.00 186.71 ? 1488 ARG A NH2   1 
ATOM   283   N  N     . GLY A 1 1489 ? 176.082 218.863 154.719 1.00 191.16 ? 1489 GLY A N     1 
ATOM   284   C  CA    . GLY A 1 1489 ? 175.429 219.272 155.946 1.00 191.34 ? 1489 GLY A CA    1 
ATOM   285   C  C     . GLY A 1 1489 ? 174.157 218.493 156.205 1.00 191.51 ? 1489 GLY A C     1 
ATOM   286   O  O     . GLY A 1 1489 ? 173.113 219.073 156.517 1.00 190.80 ? 1489 GLY A O     1 
ATOM   287   N  N     . TRP A 1 1490 ? 174.239 217.168 156.067 1.00 186.39 ? 1490 TRP A N     1 
ATOM   288   C  CA    . TRP A 1 1490 ? 173.071 216.319 156.282 1.00 186.56 ? 1490 TRP A CA    1 
ATOM   289   C  C     . TRP A 1 1490 ? 172.586 216.400 157.723 1.00 188.12 ? 1490 TRP A C     1 
ATOM   290   O  O     . TRP A 1 1490 ? 171.376 216.464 157.977 1.00 188.25 ? 1490 TRP A O     1 
ATOM   291   C  CB    . TRP A 1 1490 ? 173.410 214.875 155.919 1.00 186.26 ? 1490 TRP A CB    1 
ATOM   292   C  CG    . TRP A 1 1490 ? 173.679 214.660 154.464 1.00 185.82 ? 1490 TRP A CG    1 
ATOM   293   C  CD1   . TRP A 1 1490 ? 174.894 214.457 153.878 1.00 186.47 ? 1490 TRP A CD1   1 
ATOM   294   C  CD2   . TRP A 1 1490 ? 172.713 214.610 153.409 1.00 186.13 ? 1490 TRP A CD2   1 
ATOM   295   N  NE1   . TRP A 1 1490 ? 174.746 214.291 152.524 1.00 186.88 ? 1490 TRP A NE1   1 
ATOM   296   C  CE2   . TRP A 1 1490 ? 173.415 214.380 152.210 1.00 186.65 ? 1490 TRP A CE2   1 
ATOM   297   C  CE3   . TRP A 1 1490 ? 171.322 214.741 153.362 1.00 186.35 ? 1490 TRP A CE3   1 
ATOM   298   C  CZ2   . TRP A 1 1490 ? 172.775 214.277 150.979 1.00 186.40 ? 1490 TRP A CZ2   1 
ATOM   299   C  CZ3   . TRP A 1 1490 ? 170.690 214.639 152.138 1.00 186.22 ? 1490 TRP A CZ3   1 
ATOM   300   C  CH2   . TRP A 1 1490 ? 171.415 214.411 150.964 1.00 186.11 ? 1490 TRP A CH2   1 
ATOM   301   N  N     . ASP A 1 1491 ? 173.519 216.397 158.678 1.00 193.88 ? 1491 ASP A N     1 
ATOM   302   C  CA    . ASP A 1 1491 ? 173.148 216.401 160.090 1.00 193.61 ? 1491 ASP A CA    1 
ATOM   303   C  C     . ASP A 1 1491 ? 172.397 217.670 160.467 1.00 194.03 ? 1491 ASP A C     1 
ATOM   304   O  O     . ASP A 1 1491 ? 171.439 217.621 161.248 1.00 193.89 ? 1491 ASP A O     1 
ATOM   305   C  CB    . ASP A 1 1491 ? 174.397 216.235 160.955 1.00 192.40 ? 1491 ASP A CB    1 
ATOM   306   C  CG    . ASP A 1 1491 ? 175.500 217.205 160.579 1.00 193.06 ? 1491 ASP A CG    1 
ATOM   307   O  OD1   . ASP A 1 1491 ? 175.325 217.955 159.595 1.00 194.63 ? 1491 ASP A OD1   1 
ATOM   308   O  OD2   . ASP A 1 1491 ? 176.543 217.218 161.265 1.00 193.32 ? 1491 ASP A OD2   1 
ATOM   309   N  N     . ASP A 1 1492 ? 172.827 218.820 159.939 1.00 199.38 ? 1492 ASP A N     1 
ATOM   310   C  CA    . ASP A 1 1492 ? 172.160 220.079 160.262 1.00 198.51 ? 1492 ASP A CA    1 
ATOM   311   C  C     . ASP A 1 1492 ? 170.710 220.070 159.796 1.00 198.86 ? 1492 ASP A C     1 
ATOM   312   O  O     . ASP A 1 1492 ? 169.801 220.420 160.558 1.00 199.79 ? 1492 ASP A O     1 
ATOM   313   C  CB    . ASP A 1 1492 ? 172.917 221.250 159.636 1.00 198.39 ? 1492 ASP A CB    1 
ATOM   314   C  CG    . ASP A 1 1492 ? 174.369 221.302 160.066 1.00 198.31 ? 1492 ASP A CG    1 
ATOM   315   O  OD1   . ASP A 1 1492 ? 174.626 221.399 161.285 1.00 198.47 ? 1492 ASP A OD1   1 
ATOM   316   O  OD2   . ASP A 1 1492 ? 175.253 221.246 159.186 1.00 197.88 ? 1492 ASP A OD2   1 
ATOM   317   N  N     . LEU A 1 1493 ? 170.471 219.654 158.552 1.00 196.08 ? 1493 LEU A N     1 
ATOM   318   C  CA    . LEU A 1 1493 ? 169.100 219.559 158.063 1.00 196.52 ? 1493 LEU A CA    1 
ATOM   319   C  C     . LEU A 1 1493 ? 168.300 218.561 158.890 1.00 197.43 ? 1493 LEU A C     1 
ATOM   320   O  O     . LEU A 1 1493 ? 167.143 218.817 159.247 1.00 196.95 ? 1493 LEU A O     1 
ATOM   321   C  CB    . LEU A 1 1493 ? 169.098 219.168 156.585 1.00 194.97 ? 1493 LEU A CB    1 
ATOM   322   C  CG    . LEU A 1 1493 ? 167.746 218.781 155.984 1.00 194.80 ? 1493 LEU A CG    1 
ATOM   323   C  CD1   . LEU A 1 1493 ? 166.904 220.018 155.719 1.00 195.19 ? 1493 LEU A CD1   1 
ATOM   324   C  CD2   . LEU A 1 1493 ? 167.942 217.979 154.710 1.00 194.46 ? 1493 LEU A CD2   1 
ATOM   325   N  N     . PHE A 1 1494 ? 168.913 217.422 159.224 1.00 191.60 ? 1494 PHE A N     1 
ATOM   326   C  CA    . PHE A 1 1494 ? 168.190 216.385 159.952 1.00 190.66 ? 1494 PHE A CA    1 
ATOM   327   C  C     . PHE A 1 1494 ? 167.746 216.866 161.328 1.00 191.23 ? 1494 PHE A C     1 
ATOM   328   O  O     . PHE A 1 1494 ? 166.569 216.724 161.688 1.00 191.36 ? 1494 PHE A O     1 
ATOM   329   C  CB    . PHE A 1 1494 ? 169.051 215.127 160.069 1.00 189.85 ? 1494 PHE A CB    1 
ATOM   330   C  CG    . PHE A 1 1494 ? 169.082 214.298 158.817 1.00 188.77 ? 1494 PHE A CG    1 
ATOM   331   C  CD1   . PHE A 1 1494 ? 167.993 214.277 157.960 1.00 189.00 ? 1494 PHE A CD1   1 
ATOM   332   C  CD2   . PHE A 1 1494 ? 170.192 213.534 158.500 1.00 188.67 ? 1494 PHE A CD2   1 
ATOM   333   C  CE1   . PHE A 1 1494 ? 168.014 213.515 156.808 1.00 188.62 ? 1494 PHE A CE1   1 
ATOM   334   C  CE2   . PHE A 1 1494 ? 170.218 212.769 157.349 1.00 188.37 ? 1494 PHE A CE2   1 
ATOM   335   C  CZ    . PHE A 1 1494 ? 169.128 212.760 156.502 1.00 188.27 ? 1494 PHE A CZ    1 
ATOM   336   N  N     . ASN A 1 1495 ? 168.657 217.448 162.115 1.00 197.17 ? 1495 ASN A N     1 
ATOM   337   C  CA    . ASN A 1 1495 ? 168.254 217.842 163.462 1.00 196.14 ? 1495 ASN A CA    1 
ATOM   338   C  C     . ASN A 1 1495 ? 167.395 219.100 163.426 1.00 196.90 ? 1495 ASN A C     1 
ATOM   339   O  O     . ASN A 1 1495 ? 166.568 219.311 164.318 1.00 198.07 ? 1495 ASN A O     1 
ATOM   340   C  CB    . ASN A 1 1495 ? 169.457 218.026 164.398 1.00 196.03 ? 1495 ASN A CB    1 
ATOM   341   C  CG    . ASN A 1 1495 ? 170.607 218.759 163.760 1.00 195.85 ? 1495 ASN A CG    1 
ATOM   342   O  OD1   . ASN A 1 1495 ? 170.414 219.592 162.888 1.00 196.41 ? 1495 ASN A OD1   1 
ATOM   343   N  ND2   . ASN A 1 1495 ? 171.822 218.450 164.199 1.00 195.26 ? 1495 ASN A ND2   1 
ATOM   344   N  N     . LYS A 1 1496 ? 167.542 219.932 162.387 1.00 206.89 ? 1496 LYS A N     1 
ATOM   345   C  CA    . LYS A 1 1496 ? 166.609 221.041 162.218 1.00 208.29 ? 1496 LYS A CA    1 
ATOM   346   C  C     . LYS A 1 1496 ? 165.186 220.535 162.013 1.00 208.85 ? 1496 LYS A C     1 
ATOM   347   O  O     . LYS A 1 1496 ? 164.247 221.014 162.665 1.00 209.64 ? 1496 LYS A O     1 
ATOM   348   C  CB    . LYS A 1 1496 ? 167.043 221.918 161.043 1.00 207.88 ? 1496 LYS A CB    1 
ATOM   349   C  CG    . LYS A 1 1496 ? 166.156 223.130 160.808 1.00 208.64 ? 1496 LYS A CG    1 
ATOM   350   C  CD    . LYS A 1 1496 ? 166.155 224.065 162.007 1.00 208.32 ? 1496 LYS A CD    1 
ATOM   351   C  CE    . LYS A 1 1496 ? 167.515 224.712 162.209 1.00 207.44 ? 1496 LYS A CE    1 
ATOM   352   N  NZ    . LYS A 1 1496 ? 167.532 225.601 163.403 1.00 207.35 ? 1496 LYS A NZ    1 
ATOM   353   N  N     . VAL A 1 1497 ? 165.009 219.552 161.126 1.00 207.21 ? 1497 VAL A N     1 
ATOM   354   C  CA    . VAL A 1 1497 ? 163.678 218.992 160.900 1.00 207.41 ? 1497 VAL A CA    1 
ATOM   355   C  C     . VAL A 1 1497 ? 163.161 218.319 162.165 1.00 207.84 ? 1497 VAL A C     1 
ATOM   356   O  O     . VAL A 1 1497 ? 161.978 218.436 162.508 1.00 207.44 ? 1497 VAL A O     1 
ATOM   357   C  CB    . VAL A 1 1497 ? 163.693 218.017 159.708 1.00 206.59 ? 1497 VAL A CB    1 
ATOM   358   C  CG1   . VAL A 1 1497 ? 162.308 217.448 159.487 1.00 207.21 ? 1497 VAL A CG1   1 
ATOM   359   C  CG2   . VAL A 1 1497 ? 164.164 218.720 158.453 1.00 206.25 ? 1497 VAL A CG2   1 
ATOM   360   N  N     . LYS A 1 1498 ? 164.033 217.594 162.871 1.00 210.21 ? 1498 LYS A N     1 
ATOM   361   C  CA    . LYS A 1 1498 ? 163.610 216.926 164.099 1.00 209.31 ? 1498 LYS A CA    1 
ATOM   362   C  C     . LYS A 1 1498 ? 163.136 217.930 165.144 1.00 210.12 ? 1498 LYS A C     1 
ATOM   363   O  O     . LYS A 1 1498 ? 162.082 217.741 165.766 1.00 211.06 ? 1498 LYS A O     1 
ATOM   364   C  CB    . LYS A 1 1498 ? 164.751 216.074 164.653 1.00 208.70 ? 1498 LYS A CB    1 
ATOM   365   C  CG    . LYS A 1 1498 ? 164.995 214.787 163.884 1.00 208.92 ? 1498 LYS A CG    1 
ATOM   366   C  CD    . LYS A 1 1498 ? 166.143 213.994 164.484 1.00 210.25 ? 1498 LYS A CD    1 
ATOM   367   C  CE    . LYS A 1 1498 ? 166.248 212.613 163.855 1.00 210.41 ? 1498 LYS A CE    1 
ATOM   368   N  NZ    . LYS A 1 1498 ? 166.601 212.686 162.410 1.00 209.94 ? 1498 LYS A NZ    1 
ATOM   369   N  N     . GLU A 1 1499 ? 163.898 219.008 165.347 1.00 211.65 ? 1499 GLU A N     1 
ATOM   370   C  CA    . GLU A 1 1499 ? 163.517 220.008 166.338 1.00 211.38 ? 1499 GLU A CA    1 
ATOM   371   C  C     . GLU A 1 1499 ? 162.236 220.726 165.929 1.00 212.82 ? 1499 GLU A C     1 
ATOM   372   O  O     . GLU A 1 1499 ? 161.396 221.036 166.781 1.00 212.84 ? 1499 GLU A O     1 
ATOM   373   C  CB    . GLU A 1 1499 ? 164.668 220.994 166.562 1.00 210.75 ? 1499 GLU A CB    1 
ATOM   374   C  CG    . GLU A 1 1499 ? 164.710 222.189 165.620 1.00 212.03 ? 1499 GLU A CG    1 
ATOM   375   C  CD    . GLU A 1 1499 ? 165.438 223.378 166.215 1.00 211.73 ? 1499 GLU A CD    1 
ATOM   376   O  OE1   . GLU A 1 1499 ? 165.901 223.277 167.370 1.00 211.06 ? 1499 GLU A OE1   1 
ATOM   377   O  OE2   . GLU A 1 1499 ? 165.548 224.414 165.526 1.00 211.67 ? 1499 GLU A OE2   1 
ATOM   378   N  N     . HIS A 1 1500 ? 162.052 220.976 164.629 1.00 217.21 ? 1500 HIS A N     1 
ATOM   379   C  CA    . HIS A 1 1500 ? 160.822 221.622 164.182 1.00 216.93 ? 1500 HIS A CA    1 
ATOM   380   C  C     . HIS A 1 1500 ? 159.612 220.716 164.390 1.00 217.44 ? 1500 HIS A C     1 
ATOM   381   O  O     . HIS A 1 1500 ? 158.551 221.178 164.831 1.00 217.43 ? 1500 HIS A O     1 
ATOM   382   C  CB    . HIS A 1 1500 ? 160.954 222.034 162.717 1.00 216.65 ? 1500 HIS A CB    1 
ATOM   383   C  CG    . HIS A 1 1500 ? 161.769 223.272 162.511 1.00 216.70 ? 1500 HIS A CG    1 
ATOM   384   N  ND1   . HIS A 1 1500 ? 162.037 223.789 161.262 1.00 216.89 ? 1500 HIS A ND1   1 
ATOM   385   C  CD2   . HIS A 1 1500 ? 162.373 224.098 163.398 1.00 216.53 ? 1500 HIS A CD2   1 
ATOM   386   C  CE1   . HIS A 1 1500 ? 162.773 224.879 161.388 1.00 217.13 ? 1500 HIS A CE1   1 
ATOM   387   N  NE2   . HIS A 1 1500 ? 162.990 225.089 162.674 1.00 217.20 ? 1500 HIS A NE2   1 
ATOM   388   N  N     . ILE A 1 1501 ? 159.757 219.422 164.094 1.00 214.29 ? 1501 ILE A N     1 
ATOM   389   C  CA    . ILE A 1 1501 ? 158.665 218.477 164.316 1.00 213.46 ? 1501 ILE A CA    1 
ATOM   390   C  C     . ILE A 1 1501 ? 158.325 218.396 165.799 1.00 214.05 ? 1501 ILE A C     1 
ATOM   391   O  O     . ILE A 1 1501 ? 157.148 218.394 166.186 1.00 214.70 ? 1501 ILE A O     1 
ATOM   392   C  CB    . ILE A 1 1501 ? 159.031 217.094 163.742 1.00 212.51 ? 1501 ILE A CB    1 
ATOM   393   C  CG1   . ILE A 1 1501 ? 158.849 217.077 162.224 1.00 212.57 ? 1501 ILE A CG1   1 
ATOM   394   C  CG2   . ILE A 1 1501 ? 158.193 216.000 164.388 1.00 213.06 ? 1501 ILE A CG2   1 
ATOM   395   C  CD1   . ILE A 1 1501 ? 159.296 215.789 161.570 1.00 212.71 ? 1501 ILE A CD1   1 
ATOM   396   N  N     . ASN A 1 1502 ? 159.350 218.328 166.653 1.00 216.49 ? 1502 ASN A N     1 
ATOM   397   C  CA    . ASN A 1 1502 ? 159.109 218.269 168.091 1.00 216.28 ? 1502 ASN A CA    1 
ATOM   398   C  C     . ASN A 1 1502 ? 158.428 219.538 168.590 1.00 216.67 ? 1502 ASN A C     1 
ATOM   399   O  O     . ASN A 1 1502 ? 157.547 219.478 169.456 1.00 216.57 ? 1502 ASN A O     1 
ATOM   400   C  CB    . ASN A 1 1502 ? 160.424 218.031 168.832 1.00 216.75 ? 1502 ASN A CB    1 
ATOM   401   C  CG    . ASN A 1 1502 ? 161.051 216.694 168.489 1.00 216.16 ? 1502 ASN A CG    1 
ATOM   402   O  OD1   . ASN A 1 1502 ? 160.378 215.788 167.998 1.00 216.31 ? 1502 ASN A OD1   1 
ATOM   403   N  ND2   . ASN A 1 1502 ? 162.348 216.565 168.744 1.00 215.88 ? 1502 ASN A ND2   1 
ATOM   404   N  N     . SER A 1 1503 ? 158.827 220.697 168.060 1.00 222.06 ? 1503 SER A N     1 
ATOM   405   C  CA    . SER A 1 1503 ? 158.177 221.947 168.441 1.00 222.40 ? 1503 SER A CA    1 
ATOM   406   C  C     . SER A 1 1503 ? 156.710 221.954 168.028 1.00 223.65 ? 1503 SER A C     1 
ATOM   407   O  O     . SER A 1 1503 ? 155.844 222.383 168.799 1.00 224.42 ? 1503 SER A O     1 
ATOM   408   C  CB    . SER A 1 1503 ? 158.915 223.133 167.822 1.00 221.37 ? 1503 SER A CB    1 
ATOM   409   O  OG    . SER A 1 1503 ? 158.611 223.259 166.444 1.00 222.39 ? 1503 SER A OG    1 
ATOM   410   N  N     . VAL A 1 1504 ? 156.410 221.476 166.818 1.00 224.41 ? 1504 VAL A N     1 
ATOM   411   C  CA    . VAL A 1 1504 ? 155.019 221.447 166.369 1.00 223.66 ? 1504 VAL A CA    1 
ATOM   412   C  C     . VAL A 1 1504 ? 154.199 220.490 167.228 1.00 224.21 ? 1504 VAL A C     1 
ATOM   413   O  O     . VAL A 1 1504 ? 153.031 220.755 167.538 1.00 224.42 ? 1504 VAL A O     1 
ATOM   414   C  CB    . VAL A 1 1504 ? 154.938 221.086 164.874 1.00 222.83 ? 1504 VAL A CB    1 
ATOM   415   C  CG1   . VAL A 1 1504 ? 153.487 220.979 164.436 1.00 223.08 ? 1504 VAL A CG1   1 
ATOM   416   C  CG2   . VAL A 1 1504 ? 155.657 222.130 164.039 1.00 223.30 ? 1504 VAL A CG2   1 
ATOM   417   N  N     . SER A 1 1505 ? 154.794 219.366 167.634 1.00 227.47 ? 1505 SER A N     1 
ATOM   418   C  CA    . SER A 1 1505 ? 154.080 218.438 168.509 1.00 227.13 ? 1505 SER A CA    1 
ATOM   419   C  C     . SER A 1 1505 ? 153.816 219.058 169.880 1.00 227.29 ? 1505 SER A C     1 
ATOM   420   O  O     . SER A 1 1505 ? 152.701 218.964 170.414 1.00 227.25 ? 1505 SER A O     1 
ATOM   421   C  CB    . SER A 1 1505 ? 154.868 217.136 168.648 1.00 227.15 ? 1505 SER A CB    1 
ATOM   422   O  OG    . SER A 1 1505 ? 155.025 216.501 167.391 1.00 226.76 ? 1505 SER A OG    1 
ATOM   423   N  N     . ALA A 1 1506 ? 154.831 219.703 170.462 1.00 231.46 ? 1506 ALA A N     1 
ATOM   424   C  CA    . ALA A 1 1506 ? 154.641 220.378 171.742 1.00 231.77 ? 1506 ALA A CA    1 
ATOM   425   C  C     . ALA A 1 1506 ? 153.601 221.484 171.626 1.00 232.05 ? 1506 ALA A C     1 
ATOM   426   O  O     . ALA A 1 1506 ? 152.918 221.814 172.603 1.00 231.59 ? 1506 ALA A O     1 
ATOM   427   C  CB    . ALA A 1 1506 ? 155.971 220.938 172.245 1.00 231.08 ? 1506 ALA A CB    1 
ATOM   428   N  N     . MET A 1 1507 ? 153.474 222.075 170.438 1.00 236.23 ? 1507 MET A N     1 
ATOM   429   C  CA    . MET A 1 1507 ? 152.404 223.036 170.198 1.00 236.32 ? 1507 MET A CA    1 
ATOM   430   C  C     . MET A 1 1507 ? 151.049 222.344 170.173 1.00 236.91 ? 1507 MET A C     1 
ATOM   431   O  O     . MET A 1 1507 ? 150.071 222.855 170.730 1.00 237.03 ? 1507 MET A O     1 
ATOM   432   C  CB    . MET A 1 1507 ? 152.653 223.761 168.881 1.00 235.15 ? 1507 MET A CB    1 
ATOM   433   C  CG    . MET A 1 1507 ? 153.710 224.820 168.985 1.00 234.82 ? 1507 MET A CG    1 
ATOM   434   S  SD    . MET A 1 1507 ? 153.540 226.115 167.762 1.00 234.43 ? 1507 MET A SD    1 
ATOM   435   C  CE    . MET A 1 1507 ? 154.905 227.132 168.276 1.00 235.28 ? 1507 MET A CE    1 
ATOM   436   N  N     . LYS A 1 1508 ? 150.980 221.181 169.521 1.00 235.09 ? 1508 LYS A N     1 
ATOM   437   C  CA    . LYS A 1 1508 ? 149.763 220.376 169.536 1.00 234.56 ? 1508 LYS A CA    1 
ATOM   438   C  C     . LYS A 1 1508 ? 149.340 220.048 170.961 1.00 235.10 ? 1508 LYS A C     1 
ATOM   439   O  O     . LYS A 1 1508 ? 148.143 219.909 171.240 1.00 235.23 ? 1508 LYS A O     1 
ATOM   440   C  CB    . LYS A 1 1508 ? 149.978 219.098 168.720 1.00 233.86 ? 1508 LYS A CB    1 
ATOM   441   C  CG    . LYS A 1 1508 ? 149.099 217.922 169.118 1.00 234.17 ? 1508 LYS A CG    1 
ATOM   442   C  CD    . LYS A 1 1508 ? 149.055 216.866 168.027 1.00 234.01 ? 1508 LYS A CD    1 
ATOM   443   C  CE    . LYS A 1 1508 ? 148.586 215.528 168.576 1.00 233.39 ? 1508 LYS A CE    1 
ATOM   444   N  NZ    . LYS A 1 1508 ? 149.665 214.831 169.330 1.00 232.86 ? 1508 LYS A NZ    1 
ATOM   445   N  N     . LEU A 1 1509 ? 150.306 219.943 171.877 1.00 236.38 ? 1509 LEU A N     1 
ATOM   446   C  CA    . LEU A 1 1509 ? 149.967 219.762 173.286 1.00 236.23 ? 1509 LEU A CA    1 
ATOM   447   C  C     . LEU A 1 1509 ? 149.147 220.934 173.819 1.00 235.81 ? 1509 LEU A C     1 
ATOM   448   O  O     . LEU A 1 1509 ? 148.204 220.739 174.595 1.00 235.93 ? 1509 LEU A O     1 
ATOM   449   C  CB    . LEU A 1 1509 ? 151.238 219.584 174.117 1.00 236.15 ? 1509 LEU A CB    1 
ATOM   450   C  CG    . LEU A 1 1509 ? 152.105 218.356 173.836 1.00 236.01 ? 1509 LEU A CG    1 
ATOM   451   C  CD1   . LEU A 1 1509 ? 153.213 218.242 174.872 1.00 235.04 ? 1509 LEU A CD1   1 
ATOM   452   C  CD2   . LEU A 1 1509 ? 151.258 217.094 173.813 1.00 235.41 ? 1509 LEU A CD2   1 
ATOM   453   N  N     . SER A 1 1510 ? 149.489 222.157 173.415 1.00 237.23 ? 1510 SER A N     1 
ATOM   454   C  CA    . SER A 1 1510 ? 148.861 223.348 173.968 1.00 237.48 ? 1510 SER A CA    1 
ATOM   455   C  C     . SER A 1 1510 ? 147.396 223.453 173.541 1.00 238.06 ? 1510 SER A C     1 
ATOM   456   O  O     . SER A 1 1510 ? 147.005 222.945 172.488 1.00 238.39 ? 1510 SER A O     1 
ATOM   457   C  CB    . SER A 1 1510 ? 149.621 224.597 173.528 1.00 237.43 ? 1510 SER A CB    1 
ATOM   458   O  OG    . SER A 1 1510 ? 149.106 225.105 172.310 1.00 237.41 ? 1510 SER A OG    1 
ATOM   459   N  N     . PRO A 1 1511 ? 146.562 224.111 174.355 1.00 237.59 ? 1511 PRO A N     1 
ATOM   460   C  CA    . PRO A 1 1511 ? 145.148 224.261 173.969 1.00 237.45 ? 1511 PRO A CA    1 
ATOM   461   C  C     . PRO A 1 1511 ? 144.920 225.330 172.916 1.00 237.47 ? 1511 PRO A C     1 
ATOM   462   O  O     . PRO A 1 1511 ? 143.939 225.251 172.165 1.00 237.04 ? 1511 PRO A O     1 
ATOM   463   C  CB    . PRO A 1 1511 ? 144.464 224.612 175.296 1.00 236.64 ? 1511 PRO A CB    1 
ATOM   464   C  CG    . PRO A 1 1511 ? 145.527 225.291 176.086 1.00 235.99 ? 1511 PRO A CG    1 
ATOM   465   C  CD    . PRO A 1 1511 ? 146.824 224.624 175.711 1.00 236.35 ? 1511 PRO A CD    1 
ATOM   466   N  N     . TYR A 1 1512 ? 145.797 226.335 172.836 1.00 240.18 ? 1512 TYR A N     1 
ATOM   467   C  CA    . TYR A 1 1512 ? 145.658 227.367 171.813 1.00 239.37 ? 1512 TYR A CA    1 
ATOM   468   C  C     . TYR A 1 1512 ? 145.999 226.845 170.425 1.00 239.28 ? 1512 TYR A C     1 
ATOM   469   O  O     . TYR A 1 1512 ? 145.865 227.583 169.442 1.00 238.78 ? 1512 TYR A O     1 
ATOM   470   C  CB    . TYR A 1 1512 ? 146.543 228.570 172.150 1.00 239.64 ? 1512 TYR A CB    1 
ATOM   471   C  CG    . TYR A 1 1512 ? 146.036 229.406 173.303 1.00 239.91 ? 1512 TYR A CG    1 
ATOM   472   C  CD1   . TYR A 1 1512 ? 144.717 229.311 173.730 1.00 239.75 ? 1512 TYR A CD1   1 
ATOM   473   C  CD2   . TYR A 1 1512 ? 146.875 230.294 173.963 1.00 239.54 ? 1512 TYR A CD2   1 
ATOM   474   C  CE1   . TYR A 1 1512 ? 144.250 230.076 174.783 1.00 239.48 ? 1512 TYR A CE1   1 
ATOM   475   C  CE2   . TYR A 1 1512 ? 146.417 231.063 175.017 1.00 239.21 ? 1512 TYR A CE2   1 
ATOM   476   C  CZ    . TYR A 1 1512 ? 145.104 230.950 175.422 1.00 239.29 ? 1512 TYR A CZ    1 
ATOM   477   O  OH    . TYR A 1 1512 ? 144.644 231.713 176.471 1.00 239.05 ? 1512 TYR A OH    1 
ATOM   478   N  N     . TYR A 1 1513 ? 146.442 225.592 170.328 1.00 240.13 ? 1513 TYR A N     1 
ATOM   479   C  CA    . TYR A 1 1513 ? 146.798 224.956 169.067 1.00 240.09 ? 1513 TYR A CA    1 
ATOM   480   C  C     . TYR A 1 1513 ? 145.631 224.935 168.086 1.00 240.07 ? 1513 TYR A C     1 
ATOM   481   O  O     . TYR A 1 1513 ? 145.840 224.889 166.870 1.00 240.46 ? 1513 TYR A O     1 
ATOM   482   C  CB    . TYR A 1 1513 ? 147.293 223.533 169.340 1.00 239.31 ? 1513 TYR A CB    1 
ATOM   483   C  CG    . TYR A 1 1513 ? 147.406 222.648 168.123 1.00 239.58 ? 1513 TYR A CG    1 
ATOM   484   C  CD1   . TYR A 1 1513 ? 148.330 222.918 167.125 1.00 239.73 ? 1513 TYR A CD1   1 
ATOM   485   C  CD2   . TYR A 1 1513 ? 146.591 221.533 167.977 1.00 239.52 ? 1513 TYR A CD2   1 
ATOM   486   C  CE1   . TYR A 1 1513 ? 148.436 222.106 166.014 1.00 239.62 ? 1513 TYR A CE1   1 
ATOM   487   C  CE2   . TYR A 1 1513 ? 146.690 220.715 166.869 1.00 239.55 ? 1513 TYR A CE2   1 
ATOM   488   C  CZ    . TYR A 1 1513 ? 147.614 221.007 165.890 1.00 239.60 ? 1513 TYR A CZ    1 
ATOM   489   O  OH    . TYR A 1 1513 ? 147.719 220.197 164.782 1.00 239.20 ? 1513 TYR A OH    1 
ATOM   490   N  N     . LYS A 1 1514 ? 144.400 224.982 168.604 1.00 238.71 ? 1514 LYS A N     1 
ATOM   491   C  CA    . LYS A 1 1514 ? 143.223 224.843 167.750 1.00 238.41 ? 1514 LYS A CA    1 
ATOM   492   C  C     . LYS A 1 1514 ? 143.136 225.960 166.715 1.00 238.83 ? 1514 LYS A C     1 
ATOM   493   O  O     . LYS A 1 1514 ? 142.809 225.710 165.549 1.00 238.88 ? 1514 LYS A O     1 
ATOM   494   C  CB    . LYS A 1 1514 ? 141.957 224.811 168.608 1.00 238.54 ? 1514 LYS A CB    1 
ATOM   495   C  CG    . LYS A 1 1514 ? 140.678 224.569 167.822 1.00 238.40 ? 1514 LYS A CG    1 
ATOM   496   C  CD    . LYS A 1 1514 ? 140.800 223.349 166.922 1.00 238.43 ? 1514 LYS A CD    1 
ATOM   497   C  CE    . LYS A 1 1514 ? 139.602 223.226 165.994 1.00 238.60 ? 1514 LYS A CE    1 
ATOM   498   N  NZ    . LYS A 1 1514 ? 139.732 222.068 165.068 1.00 238.97 ? 1514 LYS A NZ    1 
ATOM   499   N  N     . VAL A 1 1515 ? 143.418 227.201 167.122 1.00 244.43 ? 1515 VAL A N     1 
ATOM   500   C  CA    . VAL A 1 1515 ? 143.331 228.324 166.195 1.00 244.70 ? 1515 VAL A CA    1 
ATOM   501   C  C     . VAL A 1 1515 ? 144.387 228.232 165.099 1.00 244.40 ? 1515 VAL A C     1 
ATOM   502   O  O     . VAL A 1 1515 ? 144.209 228.804 164.018 1.00 244.04 ? 1515 VAL A O     1 
ATOM   503   C  CB    . VAL A 1 1515 ? 143.427 229.660 166.965 1.00 244.35 ? 1515 VAL A CB    1 
ATOM   504   C  CG1   . VAL A 1 1515 ? 144.851 229.924 167.419 1.00 244.16 ? 1515 VAL A CG1   1 
ATOM   505   C  CG2   . VAL A 1 1515 ? 142.905 230.812 166.115 1.00 243.63 ? 1515 VAL A CG2   1 
ATOM   506   N  N     . PHE A 1 1516 ? 145.485 227.517 165.346 1.00 240.19 ? 1516 PHE A N     1 
ATOM   507   C  CA    . PHE A 1 1516 ? 146.508 227.275 164.338 1.00 239.58 ? 1516 PHE A CA    1 
ATOM   508   C  C     . PHE A 1 1516 ? 146.641 225.804 163.972 1.00 239.54 ? 1516 PHE A C     1 
ATOM   509   O  O     . PHE A 1 1516 ? 147.696 225.399 163.471 1.00 239.35 ? 1516 PHE A O     1 
ATOM   510   C  CB    . PHE A 1 1516 ? 147.867 227.806 164.813 1.00 239.60 ? 1516 PHE A CB    1 
ATOM   511   C  CG    . PHE A 1 1516 ? 147.815 229.192 165.393 1.00 239.60 ? 1516 PHE A CG    1 
ATOM   512   C  CD1   . PHE A 1 1516 ? 147.264 230.240 164.673 1.00 239.68 ? 1516 PHE A CD1   1 
ATOM   513   C  CD2   . PHE A 1 1516 ? 148.332 229.449 166.652 1.00 239.44 ? 1516 PHE A CD2   1 
ATOM   514   C  CE1   . PHE A 1 1516 ? 147.221 231.517 165.203 1.00 239.64 ? 1516 PHE A CE1   1 
ATOM   515   C  CE2   . PHE A 1 1516 ? 148.293 230.724 167.188 1.00 239.68 ? 1516 PHE A CE2   1 
ATOM   516   C  CZ    . PHE A 1 1516 ? 147.736 231.759 166.462 1.00 239.54 ? 1516 PHE A CZ    1 
ATOM   517   N  N     . GLU A 1 1517 ? 145.607 224.994 164.211 1.00 241.72 ? 1517 GLU A N     1 
ATOM   518   C  CA    . GLU A 1 1517 ? 145.719 223.550 164.028 1.00 242.19 ? 1517 GLU A CA    1 
ATOM   519   C  C     . GLU A 1 1517 ? 145.903 223.177 162.561 1.00 242.19 ? 1517 GLU A C     1 
ATOM   520   O  O     . GLU A 1 1517 ? 146.813 222.420 162.208 1.00 242.75 ? 1517 GLU A O     1 
ATOM   521   C  CB    . GLU A 1 1517 ? 144.485 222.861 164.613 1.00 242.16 ? 1517 GLU A CB    1 
ATOM   522   C  CG    . GLU A 1 1517 ? 144.371 221.389 164.264 1.00 241.99 ? 1517 GLU A CG    1 
ATOM   523   C  CD    . GLU A 1 1517 ? 143.177 220.730 164.921 1.00 242.01 ? 1517 GLU A CD    1 
ATOM   524   O  OE1   . GLU A 1 1517 ? 142.035 221.144 164.632 1.00 241.98 ? 1517 GLU A OE1   1 
ATOM   525   O  OE2   . GLU A 1 1517 ? 143.380 219.799 165.729 1.00 242.04 ? 1517 GLU A OE2   1 
ATOM   526   N  N     . GLU A 1 1518 ? 145.039 223.704 161.689 1.00 234.98 ? 1518 GLU A N     1 
ATOM   527   C  CA    . GLU A 1 1518 ? 145.096 223.347 160.274 1.00 234.91 ? 1518 GLU A CA    1 
ATOM   528   C  C     . GLU A 1 1518 ? 146.428 223.755 159.657 1.00 234.70 ? 1518 GLU A C     1 
ATOM   529   O  O     . GLU A 1 1518 ? 147.055 222.981 158.921 1.00 234.31 ? 1518 GLU A O     1 
ATOM   530   C  CB    . GLU A 1 1518 ? 143.930 224.000 159.528 1.00 234.03 ? 1518 GLU A CB    1 
ATOM   531   C  CG    . GLU A 1 1518 ? 144.128 224.109 158.026 1.00 233.75 ? 1518 GLU A CG    1 
ATOM   532   C  CD    . GLU A 1 1518 ? 143.179 225.102 157.387 1.00 233.30 ? 1518 GLU A CD    1 
ATOM   533   O  OE1   . GLU A 1 1518 ? 143.225 226.294 157.758 1.00 233.52 ? 1518 GLU A OE1   1 
ATOM   534   O  OE2   . GLU A 1 1518 ? 142.386 224.691 156.514 1.00 233.46 ? 1518 GLU A OE2   1 
ATOM   535   N  N     . ASP A 1 1519 ? 146.879 224.974 159.959 1.00 234.07 ? 1519 ASP A N     1 
ATOM   536   C  CA    . ASP A 1 1519 ? 148.182 225.420 159.482 1.00 234.30 ? 1519 ASP A CA    1 
ATOM   537   C  C     . ASP A 1 1519 ? 149.287 224.507 159.997 1.00 234.85 ? 1519 ASP A C     1 
ATOM   538   O  O     . ASP A 1 1519 ? 150.123 224.030 159.224 1.00 234.63 ? 1519 ASP A O     1 
ATOM   539   C  CB    . ASP A 1 1519 ? 148.429 226.867 159.908 1.00 233.88 ? 1519 ASP A CB    1 
ATOM   540   C  CG    . ASP A 1 1519 ? 149.743 227.412 159.384 1.00 234.03 ? 1519 ASP A CG    1 
ATOM   541   O  OD1   . ASP A 1 1519 ? 149.894 227.519 158.149 1.00 233.31 ? 1519 ASP A OD1   1 
ATOM   542   O  OD2   . ASP A 1 1519 ? 150.625 227.733 160.208 1.00 234.00 ? 1519 ASP A OD2   1 
ATOM   543   N  N     . ALA A 1 1520 ? 149.290 224.231 161.303 1.00 231.31 ? 1520 ALA A N     1 
ATOM   544   C  CA    . ALA A 1 1520 ? 150.314 223.355 161.864 1.00 230.06 ? 1520 ALA A CA    1 
ATOM   545   C  C     . ALA A 1 1520 ? 150.184 221.936 161.326 1.00 230.67 ? 1520 ALA A C     1 
ATOM   546   O  O     . ALA A 1 1520 ? 151.181 221.212 161.221 1.00 230.28 ? 1520 ALA A O     1 
ATOM   547   C  CB    . ALA A 1 1520 ? 150.237 223.365 163.389 1.00 229.04 ? 1520 ALA A CB    1 
ATOM   548   N  N     . LEU A 1 1521 ? 148.965 221.518 160.975 1.00 231.46 ? 1521 LEU A N     1 
ATOM   549   C  CA    . LEU A 1 1521 ? 148.789 220.214 160.341 1.00 230.81 ? 1521 LEU A CA    1 
ATOM   550   C  C     . LEU A 1 1521 ? 149.494 220.165 158.991 1.00 230.28 ? 1521 LEU A C     1 
ATOM   551   O  O     . LEU A 1 1521 ? 150.246 219.226 158.700 1.00 230.37 ? 1521 LEU A O     1 
ATOM   552   C  CB    . LEU A 1 1521 ? 147.300 219.901 160.184 1.00 230.15 ? 1521 LEU A CB    1 
ATOM   553   C  CG    . LEU A 1 1521 ? 146.590 219.314 161.406 1.00 230.25 ? 1521 LEU A CG    1 
ATOM   554   C  CD1   . LEU A 1 1521 ? 145.208 218.799 161.029 1.00 229.97 ? 1521 LEU A CD1   1 
ATOM   555   C  CD2   . LEU A 1 1521 ? 147.425 218.212 162.039 1.00 230.28 ? 1521 LEU A CD2   1 
ATOM   556   N  N     . SER A 1 1522 ? 149.273 221.183 158.155 1.00 223.18 ? 1522 SER A N     1 
ATOM   557   C  CA    . SER A 1 1522 ? 149.955 221.235 156.864 1.00 222.78 ? 1522 SER A CA    1 
ATOM   558   C  C     . SER A 1 1522 ? 151.463 221.362 157.048 1.00 223.09 ? 1522 SER A C     1 
ATOM   559   O  O     . SER A 1 1522 ? 152.251 220.878 156.226 1.00 223.56 ? 1522 SER A O     1 
ATOM   560   C  CB    . SER A 1 1522 ? 149.413 222.396 156.030 1.00 222.36 ? 1522 SER A CB    1 
ATOM   561   O  OG    . SER A 1 1522 ? 150.075 222.473 154.779 1.00 221.50 ? 1522 SER A OG    1 
ATOM   562   N  N     . TRP A 1 1523 ? 151.882 222.012 158.134 1.00 225.49 ? 1523 TRP A N     1 
ATOM   563   C  CA    . TRP A 1 1523 ? 153.308 222.156 158.409 1.00 225.47 ? 1523 TRP A CA    1 
ATOM   564   C  C     . TRP A 1 1523 ? 153.943 220.821 158.767 1.00 225.17 ? 1523 TRP A C     1 
ATOM   565   O  O     . TRP A 1 1523 ? 155.021 220.482 158.266 1.00 224.53 ? 1523 TRP A O     1 
ATOM   566   C  CB    . TRP A 1 1523 ? 153.524 223.185 159.514 1.00 225.36 ? 1523 TRP A CB    1 
ATOM   567   C  CG    . TRP A 1 1523 ? 153.448 224.583 159.006 1.00 225.58 ? 1523 TRP A CG    1 
ATOM   568   C  CD1   . TRP A 1 1523 ? 152.489 225.111 158.194 1.00 225.98 ? 1523 TRP A CD1   1 
ATOM   569   C  CD2   . TRP A 1 1523 ? 154.381 225.633 159.259 1.00 225.80 ? 1523 TRP A CD2   1 
ATOM   570   N  NE1   . TRP A 1 1523 ? 152.761 226.429 157.933 1.00 226.41 ? 1523 TRP A NE1   1 
ATOM   571   C  CE2   . TRP A 1 1523 ? 153.919 226.774 158.576 1.00 226.45 ? 1523 TRP A CE2   1 
ATOM   572   C  CE3   . TRP A 1 1523 ? 155.560 225.722 160.001 1.00 225.44 ? 1523 TRP A CE3   1 
ATOM   573   C  CZ2   . TRP A 1 1523 ? 154.595 227.984 158.612 1.00 226.38 ? 1523 TRP A CZ2   1 
ATOM   574   C  CZ3   . TRP A 1 1523 ? 156.225 226.924 160.035 1.00 225.59 ? 1523 TRP A CZ3   1 
ATOM   575   C  CH2   . TRP A 1 1523 ? 155.743 228.037 159.345 1.00 225.69 ? 1523 TRP A CH2   1 
ATOM   576   N  N     . GLU A 1 1524 ? 153.291 220.050 159.640 1.00 219.21 ? 1524 GLU A N     1 
ATOM   577   C  CA    . GLU A 1 1524 ? 153.753 218.691 159.900 1.00 219.32 ? 1524 GLU A CA    1 
ATOM   578   C  C     . GLU A 1 1524 ? 153.762 217.870 158.621 1.00 219.09 ? 1524 GLU A C     1 
ATOM   579   O  O     . GLU A 1 1524 ? 154.663 217.053 158.405 1.00 219.91 ? 1524 GLU A O     1 
ATOM   580   C  CB    . GLU A 1 1524 ? 152.881 218.019 160.960 1.00 219.33 ? 1524 GLU A CB    1 
ATOM   581   C  CG    . GLU A 1 1524 ? 153.438 218.106 162.369 1.00 218.50 ? 1524 GLU A CG    1 
ATOM   582   C  CD    . GLU A 1 1524 ? 152.789 217.116 163.318 1.00 218.33 ? 1524 GLU A CD    1 
ATOM   583   O  OE1   . GLU A 1 1524 ? 151.711 216.584 162.979 1.00 218.82 ? 1524 GLU A OE1   1 
ATOM   584   O  OE2   . GLU A 1 1524 ? 153.359 216.866 164.401 1.00 218.16 ? 1524 GLU A OE2   1 
ATOM   585   N  N     . ASP A 1 1525 ? 152.775 218.090 157.749 1.00 212.03 ? 1525 ASP A N     1 
ATOM   586   C  CA    . ASP A 1 1525 ? 152.726 217.360 156.487 1.00 211.91 ? 1525 ASP A CA    1 
ATOM   587   C  C     . ASP A 1 1525 ? 153.966 217.647 155.643 1.00 212.63 ? 1525 ASP A C     1 
ATOM   588   O  O     . ASP A 1 1525 ? 154.656 216.719 155.197 1.00 213.45 ? 1525 ASP A O     1 
ATOM   589   C  CB    . ASP A 1 1525 ? 151.443 217.727 155.733 1.00 211.89 ? 1525 ASP A CB    1 
ATOM   590   C  CG    . ASP A 1 1525 ? 151.570 217.579 154.224 1.00 211.60 ? 1525 ASP A CG    1 
ATOM   591   O  OD1   . ASP A 1 1525 ? 151.010 218.429 153.500 1.00 210.92 ? 1525 ASP A OD1   1 
ATOM   592   O  OD2   . ASP A 1 1525 ? 152.169 216.587 153.755 1.00 212.41 ? 1525 ASP A OD2   1 
ATOM   593   N  N     . LYS A 1 1526 ? 154.278 218.928 155.423 1.00 209.82 ? 1526 LYS A N     1 
ATOM   594   C  CA    . LYS A 1 1526 ? 155.413 219.236 154.557 1.00 209.08 ? 1526 LYS A CA    1 
ATOM   595   C  C     . LYS A 1 1526 ? 156.726 218.855 155.229 1.00 209.12 ? 1526 LYS A C     1 
ATOM   596   O  O     . LYS A 1 1526 ? 157.686 218.464 154.558 1.00 209.13 ? 1526 LYS A O     1 
ATOM   597   C  CB    . LYS A 1 1526 ? 155.436 220.709 154.132 1.00 208.53 ? 1526 LYS A CB    1 
ATOM   598   C  CG    . LYS A 1 1526 ? 155.640 221.755 155.212 1.00 209.11 ? 1526 LYS A CG    1 
ATOM   599   C  CD    . LYS A 1 1526 ? 154.896 223.031 154.844 1.00 208.75 ? 1526 LYS A CD    1 
ATOM   600   C  CE    . LYS A 1 1526 ? 154.893 224.034 155.977 1.00 208.75 ? 1526 LYS A CE    1 
ATOM   601   N  NZ    . LYS A 1 1526 ? 156.152 224.829 156.005 1.00 208.20 ? 1526 LYS A NZ    1 
ATOM   602   N  N     . LEU A 1 1527 ? 156.785 218.948 156.559 1.00 205.96 ? 1527 LEU A N     1 
ATOM   603   C  CA    . LEU A 1 1527 ? 157.981 218.526 157.279 1.00 205.63 ? 1527 LEU A CA    1 
ATOM   604   C  C     . LEU A 1 1527 ? 158.216 217.030 157.108 1.00 205.73 ? 1527 LEU A C     1 
ATOM   605   O  O     . LEU A 1 1527 ? 159.353 216.578 156.920 1.00 205.04 ? 1527 LEU A O     1 
ATOM   606   C  CB    . LEU A 1 1527 ? 157.846 218.896 158.756 1.00 204.63 ? 1527 LEU A CB    1 
ATOM   607   C  CG    . LEU A 1 1527 ? 158.591 220.160 159.185 1.00 204.70 ? 1527 LEU A CG    1 
ATOM   608   C  CD1   . LEU A 1 1527 ? 158.569 220.310 160.694 1.00 205.61 ? 1527 LEU A CD1   1 
ATOM   609   C  CD2   . LEU A 1 1527 ? 160.017 220.151 158.663 1.00 205.63 ? 1527 LEU A CD2   1 
ATOM   610   N  N     . ASN A 1 1528 ? 157.139 216.243 157.162 1.00 202.28 ? 1528 ASN A N     1 
ATOM   611   C  CA    . ASN A 1 1528 ? 157.248 214.811 156.909 1.00 201.64 ? 1528 ASN A CA    1 
ATOM   612   C  C     . ASN A 1 1528 ? 157.690 214.542 155.476 1.00 201.30 ? 1528 ASN A C     1 
ATOM   613   O  O     . ASN A 1 1528 ? 158.463 213.612 155.219 1.00 202.63 ? 1528 ASN A O     1 
ATOM   614   C  CB    . ASN A 1 1528 ? 155.917 214.121 157.208 1.00 200.79 ? 1528 ASN A CB    1 
ATOM   615   C  CG    . ASN A 1 1528 ? 155.561 214.157 158.681 1.00 200.25 ? 1528 ASN A CG    1 
ATOM   616   O  OD1   . ASN A 1 1528 ? 156.436 214.248 159.541 1.00 200.31 ? 1528 ASN A OD1   1 
ATOM   617   N  ND2   . ASN A 1 1528 ? 154.269 214.085 158.979 1.00 199.52 ? 1528 ASN A ND2   1 
ATOM   618   N  N     . ARG A 1 1529 ? 157.196 215.337 154.522 1.00 196.22 ? 1529 ARG A N     1 
ATOM   619   C  CA    . ARG A 1 1529 ? 157.656 215.179 153.143 1.00 196.09 ? 1529 ARG A CA    1 
ATOM   620   C  C     . ARG A 1 1529 ? 159.151 215.464 153.019 1.00 196.20 ? 1529 ARG A C     1 
ATOM   621   O  O     . ARG A 1 1529 ? 159.869 214.766 152.294 1.00 195.64 ? 1529 ARG A O     1 
ATOM   622   C  CB    . ARG A 1 1529 ? 156.860 216.071 152.188 1.00 196.94 ? 1529 ARG A CB    1 
ATOM   623   C  CG    . ARG A 1 1529 ? 155.353 215.921 152.270 1.00 197.14 ? 1529 ARG A CG    1 
ATOM   624   C  CD    . ARG A 1 1529 ? 154.656 217.194 151.825 1.00 197.46 ? 1529 ARG A CD    1 
ATOM   625   N  NE    . ARG A 1 1529 ? 154.920 217.499 150.424 1.00 197.18 ? 1529 ARG A NE    1 
ATOM   626   C  CZ    . ARG A 1 1529 ? 154.740 218.690 149.870 1.00 196.79 ? 1529 ARG A CZ    1 
ATOM   627   N  NH1   . ARG A 1 1529 ? 154.290 219.718 150.571 1.00 196.99 ? 1529 ARG A NH1   1 
ATOM   628   N  NH2   . ARG A 1 1529 ? 155.017 218.853 148.579 1.00 195.61 ? 1529 ARG A NH2   1 
ATOM   629   N  N     . ILE A 1 1530 ? 159.636 216.497 153.714 1.00 195.17 ? 1530 ILE A N     1 
ATOM   630   C  CA    . ILE A 1 1530 ? 161.071 216.793 153.704 1.00 195.03 ? 1530 ILE A CA    1 
ATOM   631   C  C     . ILE A 1 1530 ? 161.855 215.631 154.301 1.00 194.50 ? 1530 ILE A C     1 
ATOM   632   O  O     . ILE A 1 1530 ? 162.910 215.237 153.788 1.00 193.87 ? 1530 ILE A O     1 
ATOM   633   C  CB    . ILE A 1 1530 ? 161.372 218.108 154.446 1.00 195.04 ? 1530 ILE A CB    1 
ATOM   634   C  CG1   . ILE A 1 1530 ? 160.508 219.249 153.912 1.00 195.21 ? 1530 ILE A CG1   1 
ATOM   635   C  CG2   . ILE A 1 1530 ? 162.847 218.459 154.330 1.00 194.86 ? 1530 ILE A CG2   1 
ATOM   636   C  CD1   . ILE A 1 1530 ? 160.411 220.429 154.853 1.00 194.91 ? 1530 ILE A CD1   1 
ATOM   637   N  N     . MET A 1 1531 ? 161.354 215.073 155.405 1.00 189.81 ? 1531 MET A N     1 
ATOM   638   C  CA    . MET A 1 1531 ? 162.027 213.933 156.024 1.00 188.84 ? 1531 MET A CA    1 
ATOM   639   C  C     . MET A 1 1531 ? 162.093 212.744 155.074 1.00 188.74 ? 1531 MET A C     1 
ATOM   640   O  O     . MET A 1 1531 ? 163.145 212.113 154.921 1.00 189.89 ? 1531 MET A O     1 
ATOM   641   C  CB    . MET A 1 1531 ? 161.320 213.536 157.320 1.00 188.83 ? 1531 MET A CB    1 
ATOM   642   C  CG    . MET A 1 1531 ? 161.983 214.072 158.571 1.00 189.08 ? 1531 MET A CG    1 
ATOM   643   S  SD    . MET A 1 1531 ? 163.631 213.378 158.807 1.00 188.63 ? 1531 MET A SD    1 
ATOM   644   C  CE    . MET A 1 1531 ? 164.035 214.002 160.435 1.00 188.60 ? 1531 MET A CE    1 
ATOM   645   N  N     . ALA A 1 1532 ? 160.975 212.429 154.418 1.00 188.02 ? 1532 ALA A N     1 
ATOM   646   C  CA    . ALA A 1 1532 ? 160.932 211.275 153.527 1.00 188.31 ? 1532 ALA A CA    1 
ATOM   647   C  C     . ALA A 1 1532 ? 161.851 211.467 152.327 1.00 189.25 ? 1532 ALA A C     1 
ATOM   648   O  O     . ALA A 1 1532 ? 162.527 210.529 151.888 1.00 188.66 ? 1532 ALA A O     1 
ATOM   649   C  CB    . ALA A 1 1532 ? 159.495 211.020 153.072 1.00 187.66 ? 1532 ALA A CB    1 
ATOM   650   N  N     . LEU A 1 1533 ? 161.881 212.683 151.777 1.00 189.70 ? 1533 LEU A N     1 
ATOM   651   C  CA    . LEU A 1 1533 ? 162.698 212.946 150.597 1.00 189.00 ? 1533 LEU A CA    1 
ATOM   652   C  C     . LEU A 1 1533 ? 164.183 212.798 150.906 1.00 188.92 ? 1533 LEU A C     1 
ATOM   653   O  O     . LEU A 1 1533 ? 164.943 212.243 150.105 1.00 189.19 ? 1533 LEU A O     1 
ATOM   654   C  CB    . LEU A 1 1533 ? 162.396 214.343 150.054 1.00 187.92 ? 1533 LEU A CB    1 
ATOM   655   C  CG    . LEU A 1 1533 ? 163.108 214.752 148.763 1.00 186.64 ? 1533 LEU A CG    1 
ATOM   656   C  CD1   . LEU A 1 1533 ? 163.064 213.629 147.737 1.00 187.90 ? 1533 LEU A CD1   1 
ATOM   657   C  CD2   . LEU A 1 1533 ? 162.501 216.025 148.195 1.00 186.99 ? 1533 LEU A CD2   1 
ATOM   658   N  N     . PHE A 1 1534 ? 164.616 213.293 152.064 1.00 184.43 ? 1534 PHE A N     1 
ATOM   659   C  CA    . PHE A 1 1534 ? 166.035 213.286 152.396 1.00 183.10 ? 1534 PHE A CA    1 
ATOM   660   C  C     . PHE A 1 1534 ? 166.463 212.057 153.189 1.00 182.47 ? 1534 PHE A C     1 
ATOM   661   O  O     . PHE A 1 1534 ? 167.664 211.880 153.416 1.00 182.32 ? 1534 PHE A O     1 
ATOM   662   C  CB    . PHE A 1 1534 ? 166.396 214.557 153.166 1.00 182.98 ? 1534 PHE A CB    1 
ATOM   663   C  CG    . PHE A 1 1534 ? 166.502 215.775 152.295 1.00 183.76 ? 1534 PHE A CG    1 
ATOM   664   C  CD1   . PHE A 1 1534 ? 165.396 216.575 152.064 1.00 183.73 ? 1534 PHE A CD1   1 
ATOM   665   C  CD2   . PHE A 1 1534 ? 167.702 216.109 151.691 1.00 183.60 ? 1534 PHE A CD2   1 
ATOM   666   C  CE1   . PHE A 1 1534 ? 165.488 217.693 151.258 1.00 183.42 ? 1534 PHE A CE1   1 
ATOM   667   C  CE2   . PHE A 1 1534 ? 167.801 217.225 150.883 1.00 183.67 ? 1534 PHE A CE2   1 
ATOM   668   C  CZ    . PHE A 1 1534 ? 166.693 218.018 150.667 1.00 183.44 ? 1534 PHE A CZ    1 
ATOM   669   N  N     . ASP A 1 1535 ? 165.525 211.207 153.611 1.00 177.56 ? 1535 ASP A N     1 
ATOM   670   C  CA    . ASP A 1 1535 ? 165.901 209.920 154.182 1.00 177.70 ? 1535 ASP A CA    1 
ATOM   671   C  C     . ASP A 1 1535 ? 166.379 208.943 153.120 1.00 177.53 ? 1535 ASP A C     1 
ATOM   672   O  O     . ASP A 1 1535 ? 166.978 207.917 153.461 1.00 177.63 ? 1535 ASP A O     1 
ATOM   673   C  CB    . ASP A 1 1535 ? 164.729 209.307 154.953 1.00 177.32 ? 1535 ASP A CB    1 
ATOM   674   C  CG    . ASP A 1 1535 ? 164.586 209.878 156.350 1.00 176.98 ? 1535 ASP A CG    1 
ATOM   675   O  OD1   . ASP A 1 1535 ? 165.612 210.281 156.937 1.00 176.61 ? 1535 ASP A OD1   1 
ATOM   676   O  OD2   . ASP A 1 1535 ? 163.448 209.920 156.863 1.00 177.59 ? 1535 ASP A OD2   1 
ATOM   677   N  N     . VAL A 1 1536 ? 166.123 209.237 151.851 1.00 177.04 ? 1536 VAL A N     1 
ATOM   678   C  CA    . VAL A 1 1536 ? 166.582 208.414 150.742 1.00 177.32 ? 1536 VAL A CA    1 
ATOM   679   C  C     . VAL A 1 1536 ? 167.601 209.158 149.890 1.00 176.60 ? 1536 VAL A C     1 
ATOM   680   O  O     . VAL A 1 1536 ? 168.465 208.543 149.267 1.00 176.90 ? 1536 VAL A O     1 
ATOM   681   C  CB    . VAL A 1 1536 ? 165.376 207.938 149.899 1.00 175.95 ? 1536 VAL A CB    1 
ATOM   682   C  CG1   . VAL A 1 1536 ? 164.484 209.112 149.531 1.00 175.49 ? 1536 VAL A CG1   1 
ATOM   683   C  CG2   . VAL A 1 1536 ? 165.828 207.180 148.654 1.00 175.90 ? 1536 VAL A CG2   1 
ATOM   684   N  N     . TRP A 1 1537 ? 167.530 210.491 149.870 1.00 178.26 ? 1537 TRP A N     1 
ATOM   685   C  CA    . TRP A 1 1537 ? 168.432 211.266 149.023 1.00 178.53 ? 1537 TRP A CA    1 
ATOM   686   C  C     . TRP A 1 1537 ? 169.886 211.087 149.443 1.00 178.53 ? 1537 TRP A C     1 
ATOM   687   O  O     . TRP A 1 1537 ? 170.774 210.978 148.595 1.00 180.01 ? 1537 TRP A O     1 
ATOM   688   C  CB    . TRP A 1 1537 ? 168.038 212.744 149.040 1.00 181.14 ? 1537 TRP A CB    1 
ATOM   689   C  CG    . TRP A 1 1537 ? 168.543 213.504 147.844 1.00 181.27 ? 1537 TRP A CG    1 
ATOM   690   C  CD1   . TRP A 1 1537 ? 169.798 213.458 147.308 1.00 180.84 ? 1537 TRP A CD1   1 
ATOM   691   C  CD2   . TRP A 1 1537 ? 167.786 214.387 147.010 1.00 180.11 ? 1537 TRP A CD2   1 
ATOM   692   N  NE1   . TRP A 1 1537 ? 169.876 214.276 146.208 1.00 179.04 ? 1537 TRP A NE1   1 
ATOM   693   C  CE2   . TRP A 1 1537 ? 168.652 214.857 146.002 1.00 180.12 ? 1537 TRP A CE2   1 
ATOM   694   C  CE3   . TRP A 1 1537 ? 166.462 214.834 147.024 1.00 180.09 ? 1537 TRP A CE3   1 
ATOM   695   C  CZ2   . TRP A 1 1537 ? 168.236 215.751 145.019 1.00 180.76 ? 1537 TRP A CZ2   1 
ATOM   696   C  CZ3   . TRP A 1 1537 ? 166.052 215.720 146.048 1.00 181.57 ? 1537 TRP A CZ3   1 
ATOM   697   C  CH2   . TRP A 1 1537 ? 166.934 216.170 145.059 1.00 181.25 ? 1537 TRP A CH2   1 
ATOM   698   N  N     . ILE A 1 1538 ? 170.152 211.059 150.750 1.00 173.16 ? 1538 ILE A N     1 
ATOM   699   C  CA    . ILE A 1 1538 ? 171.525 210.887 151.227 1.00 174.40 ? 1538 ILE A CA    1 
ATOM   700   C  C     . ILE A 1 1538 ? 172.071 209.523 150.808 1.00 174.27 ? 1538 ILE A C     1 
ATOM   701   O  O     . ILE A 1 1538 ? 173.222 209.395 150.364 1.00 175.27 ? 1538 ILE A O     1 
ATOM   702   C  CB    . ILE A 1 1538 ? 171.595 211.088 152.752 1.00 173.16 ? 1538 ILE A CB    1 
ATOM   703   C  CG1   . ILE A 1 1538 ? 173.040 210.983 153.238 1.00 172.88 ? 1538 ILE A CG1   1 
ATOM   704   C  CG2   . ILE A 1 1538 ? 170.659 210.131 153.486 1.00 171.79 ? 1538 ILE A CG2   1 
ATOM   705   C  CD1   . ILE A 1 1538 ? 173.210 211.325 154.693 1.00 172.06 ? 1538 ILE A CD1   1 
ATOM   706   N  N     . ASP A 1 1539 ? 171.242 208.483 150.940 1.00 172.97 ? 1539 ASP A N     1 
ATOM   707   C  CA    . ASP A 1 1539 ? 171.649 207.137 150.549 1.00 172.80 ? 1539 ASP A CA    1 
ATOM   708   C  C     . ASP A 1 1539 ? 171.895 207.082 149.046 1.00 173.17 ? 1539 ASP A C     1 
ATOM   709   O  O     . ASP A 1 1539 ? 172.888 206.509 148.589 1.00 173.29 ? 1539 ASP A O     1 
ATOM   710   C  CB    . ASP A 1 1539 ? 170.577 206.128 151.010 1.00 172.05 ? 1539 ASP A CB    1 
ATOM   711   C  CG    . ASP A 1 1539 ? 170.763 204.700 150.441 1.00 173.00 ? 1539 ASP A CG    1 
ATOM   712   O  OD1   . ASP A 1 1539 ? 170.592 203.722 151.205 1.00 172.60 ? 1539 ASP A OD1   1 
ATOM   713   O  OD2   . ASP A 1 1539 ? 171.025 204.523 149.233 1.00 174.54 ? 1539 ASP A OD2   1 
ATOM   714   N  N     . VAL A 1 1540 ? 171.009 207.705 148.267 1.00 168.40 ? 1540 VAL A N     1 
ATOM   715   C  CA    . VAL A 1 1540 ? 171.154 207.719 146.811 1.00 167.00 ? 1540 VAL A CA    1 
ATOM   716   C  C     . VAL A 1 1540 ? 172.429 208.450 146.411 1.00 166.58 ? 1540 VAL A C     1 
ATOM   717   O  O     . VAL A 1 1540 ? 173.165 208.013 145.520 1.00 165.32 ? 1540 VAL A O     1 
ATOM   718   C  CB    . VAL A 1 1540 ? 169.918 208.349 146.147 1.00 167.25 ? 1540 VAL A CB    1 
ATOM   719   C  CG1   . VAL A 1 1540 ? 170.178 208.586 144.668 1.00 166.98 ? 1540 VAL A CG1   1 
ATOM   720   C  CG2   . VAL A 1 1540 ? 168.715 207.450 146.323 1.00 168.37 ? 1540 VAL A CG2   1 
ATOM   721   N  N     . GLN A 1 1541 ? 172.697 209.588 147.053 1.00 171.12 ? 1541 GLN A N     1 
ATOM   722   C  CA    . GLN A 1 1541 ? 173.898 210.351 146.740 1.00 169.52 ? 1541 GLN A CA    1 
ATOM   723   C  C     . GLN A 1 1541 ? 175.147 209.541 147.047 1.00 169.25 ? 1541 GLN A C     1 
ATOM   724   O  O     . GLN A 1 1541 ? 176.083 209.493 146.242 1.00 169.63 ? 1541 GLN A O     1 
ATOM   725   C  CB    . GLN A 1 1541 ? 173.908 211.672 147.512 1.00 169.40 ? 1541 GLN A CB    1 
ATOM   726   C  CG    . GLN A 1 1541 ? 175.202 212.457 147.361 1.00 169.71 ? 1541 GLN A CG    1 
ATOM   727   C  CD    . GLN A 1 1541 ? 175.095 213.873 147.886 1.00 170.31 ? 1541 GLN A CD    1 
ATOM   728   O  OE1   . GLN A 1 1541 ? 174.320 214.679 147.374 1.00 171.21 ? 1541 GLN A OE1   1 
ATOM   729   N  NE2   . GLN A 1 1541 ? 175.886 214.187 148.904 1.00 170.71 ? 1541 GLN A NE2   1 
ATOM   730   N  N     . ARG A 1 1542 ? 175.174 208.874 148.203 1.00 164.11 ? 1542 ARG A N     1 
ATOM   731   C  CA    . ARG A 1 1542 ? 176.338 208.058 148.529 1.00 163.33 ? 1542 ARG A CA    1 
ATOM   732   C  C     . ARG A 1 1542 ? 176.485 206.905 147.540 1.00 163.32 ? 1542 ARG A C     1 
ATOM   733   O  O     . ARG A 1 1542 ? 177.598 206.594 147.090 1.00 164.46 ? 1542 ARG A O     1 
ATOM   734   C  CB    . ARG A 1 1542 ? 176.245 207.550 149.969 1.00 164.20 ? 1542 ARG A CB    1 
ATOM   735   C  CG    . ARG A 1 1542 ? 177.336 206.563 150.345 1.00 163.45 ? 1542 ARG A CG    1 
ATOM   736   C  CD    . ARG A 1 1542 ? 177.296 206.242 151.828 1.00 162.70 ? 1542 ARG A CD    1 
ATOM   737   N  NE    . ARG A 1 1542 ? 175.944 205.967 152.296 1.00 163.41 ? 1542 ARG A NE    1 
ATOM   738   C  CZ    . ARG A 1 1542 ? 175.326 204.805 152.139 1.00 164.33 ? 1542 ARG A CZ    1 
ATOM   739   N  NH1   . ARG A 1 1542 ? 175.916 203.785 151.538 1.00 164.15 ? 1542 ARG A NH1   1 
ATOM   740   N  NH2   . ARG A 1 1542 ? 174.088 204.661 152.603 1.00 163.70 ? 1542 ARG A NH2   1 
ATOM   741   N  N     . ARG A 1 1543 ? 175.365 206.273 147.171 1.00 168.19 ? 1543 ARG A N     1 
ATOM   742   C  CA    . ARG A 1 1543 ? 175.432 205.143 146.251 1.00 168.40 ? 1543 ARG A CA    1 
ATOM   743   C  C     . ARG A 1 1543 ? 175.933 205.575 144.881 1.00 169.73 ? 1543 ARG A C     1 
ATOM   744   O  O     . ARG A 1 1543 ? 176.742 204.881 144.257 1.00 168.97 ? 1543 ARG A O     1 
ATOM   745   C  CB    . ARG A 1 1543 ? 174.084 204.422 146.136 1.00 167.74 ? 1543 ARG A CB    1 
ATOM   746   C  CG    . ARG A 1 1543 ? 174.290 202.989 145.641 1.00 167.42 ? 1543 ARG A CG    1 
ATOM   747   C  CD    . ARG A 1 1543 ? 173.250 201.951 146.060 1.00 167.55 ? 1543 ARG A CD    1 
ATOM   748   N  NE    . ARG A 1 1543 ? 172.554 202.235 147.307 1.00 167.43 ? 1543 ARG A NE    1 
ATOM   749   C  CZ    . ARG A 1 1543 ? 171.310 201.850 147.559 1.00 168.63 ? 1543 ARG A CZ    1 
ATOM   750   N  NH1   . ARG A 1 1543 ? 170.634 201.096 146.709 1.00 169.08 ? 1543 ARG A NH1   1 
ATOM   751   N  NH2   . ARG A 1 1543 ? 170.738 202.209 148.704 1.00 168.70 ? 1543 ARG A NH2   1 
ATOM   752   N  N     . TRP A 1 1544 ? 175.474 206.731 144.400 1.00 176.75 ? 1544 TRP A N     1 
ATOM   753   C  CA    . TRP A 1 1544 ? 175.966 207.228 143.121 1.00 176.11 ? 1544 TRP A CA    1 
ATOM   754   C  C     . TRP A 1 1544 ? 177.435 207.616 143.216 1.00 173.92 ? 1544 TRP A C     1 
ATOM   755   O  O     . TRP A 1 1544 ? 178.200 207.414 142.267 1.00 173.55 ? 1544 TRP A O     1 
ATOM   756   C  CB    . TRP A 1 1544 ? 175.136 208.420 142.642 1.00 176.13 ? 1544 TRP A CB    1 
ATOM   757   C  CG    . TRP A 1 1544 ? 175.601 208.912 141.306 1.00 175.49 ? 1544 TRP A CG    1 
ATOM   758   C  CD1   . TRP A 1 1544 ? 175.227 208.427 140.088 1.00 174.66 ? 1544 TRP A CD1   1 
ATOM   759   C  CD2   . TRP A 1 1544 ? 176.554 209.952 141.047 1.00 175.95 ? 1544 TRP A CD2   1 
ATOM   760   N  NE1   . TRP A 1 1544 ? 175.873 209.107 139.088 1.00 174.61 ? 1544 TRP A NE1   1 
ATOM   761   C  CE2   . TRP A 1 1544 ? 176.694 210.049 139.648 1.00 174.63 ? 1544 TRP A CE2   1 
ATOM   762   C  CE3   . TRP A 1 1544 ? 177.295 210.816 141.860 1.00 176.75 ? 1544 TRP A CE3   1 
ATOM   763   C  CZ2   . TRP A 1 1544 ? 177.544 210.971 139.044 1.00 174.51 ? 1544 TRP A CZ2   1 
ATOM   764   C  CZ3   . TRP A 1 1544 ? 178.140 211.734 141.256 1.00 175.87 ? 1544 TRP A CZ3   1 
ATOM   765   C  CH2   . TRP A 1 1544 ? 178.255 211.804 139.862 1.00 174.58 ? 1544 TRP A CH2   1 
ATOM   766   N  N     . VAL A 1 1545 ? 177.848 208.184 144.354 1.00 166.39 ? 1545 VAL A N     1 
ATOM   767   C  CA    . VAL A 1 1545 ? 179.226 208.651 144.490 1.00 166.86 ? 1545 VAL A CA    1 
ATOM   768   C  C     . VAL A 1 1545 ? 180.194 207.478 144.420 1.00 165.78 ? 1545 VAL A C     1 
ATOM   769   O  O     . VAL A 1 1545 ? 181.161 207.493 143.650 1.00 165.30 ? 1545 VAL A O     1 
ATOM   770   C  CB    . VAL A 1 1545 ? 179.405 209.452 145.791 1.00 167.08 ? 1545 VAL A CB    1 
ATOM   771   C  CG1   . VAL A 1 1545 ? 180.872 209.491 146.195 1.00 165.58 ? 1545 VAL A CG1   1 
ATOM   772   C  CG2   . VAL A 1 1545 ? 178.879 210.861 145.608 1.00 167.22 ? 1545 VAL A CG2   1 
ATOM   773   N  N     . TYR A 1 1546 ? 179.943 206.428 145.209 1.00 161.67 ? 1546 TYR A N     1 
ATOM   774   C  CA    . TYR A 1 1546 ? 180.897 205.321 145.168 1.00 160.23 ? 1546 TYR A CA    1 
ATOM   775   C  C     . TYR A 1 1546 ? 180.641 204.391 143.988 1.00 161.18 ? 1546 TYR A C     1 
ATOM   776   O  O     . TYR A 1 1546 ? 181.510 203.582 143.644 1.00 160.76 ? 1546 TYR A O     1 
ATOM   777   C  CB    . TYR A 1 1546 ? 180.917 204.533 146.480 1.00 160.23 ? 1546 TYR A CB    1 
ATOM   778   C  CG    . TYR A 1 1546 ? 179.818 203.514 146.675 1.00 160.07 ? 1546 TYR A CG    1 
ATOM   779   C  CD1   . TYR A 1 1546 ? 180.084 202.160 146.606 1.00 158.97 ? 1546 TYR A CD1   1 
ATOM   780   C  CD2   . TYR A 1 1546 ? 178.542 203.899 147.022 1.00 160.92 ? 1546 TYR A CD2   1 
ATOM   781   C  CE1   . TYR A 1 1546 ? 179.083 201.229 146.807 1.00 159.56 ? 1546 TYR A CE1   1 
ATOM   782   C  CE2   . TYR A 1 1546 ? 177.547 202.969 147.237 1.00 160.95 ? 1546 TYR A CE2   1 
ATOM   783   C  CZ    . TYR A 1 1546 ? 177.819 201.639 147.123 1.00 161.55 ? 1546 TYR A CZ    1 
ATOM   784   O  OH    . TYR A 1 1546 ? 176.821 200.716 147.332 1.00 162.64 ? 1546 TYR A OH    1 
ATOM   785   N  N     . LEU A 1 1547 ? 179.469 204.482 143.356 1.00 172.50 ? 1547 LEU A N     1 
ATOM   786   C  CA    . LEU A 1 1547 ? 179.252 203.730 142.125 1.00 172.99 ? 1547 LEU A CA    1 
ATOM   787   C  C     . LEU A 1 1547 ? 179.914 204.417 140.937 1.00 173.54 ? 1547 LEU A C     1 
ATOM   788   O  O     . LEU A 1 1547 ? 180.352 203.752 139.991 1.00 171.99 ? 1547 LEU A O     1 
ATOM   789   C  CB    . LEU A 1 1547 ? 177.756 203.541 141.882 1.00 171.97 ? 1547 LEU A CB    1 
ATOM   790   C  CG    . LEU A 1 1547 ? 177.202 202.206 142.383 1.00 171.69 ? 1547 LEU A CG    1 
ATOM   791   C  CD1   . LEU A 1 1547 ? 175.790 201.977 141.873 1.00 172.04 ? 1547 LEU A CD1   1 
ATOM   792   C  CD2   . LEU A 1 1547 ? 178.118 201.061 141.976 1.00 171.23 ? 1547 LEU A CD2   1 
ATOM   793   N  N     . GLU A 1 1548 ? 179.990 205.750 140.965 1.00 179.27 ? 1548 GLU A N     1 
ATOM   794   C  CA    . GLU A 1 1548 ? 180.646 206.480 139.884 1.00 178.85 ? 1548 GLU A CA    1 
ATOM   795   C  C     . GLU A 1 1548 ? 182.133 206.152 139.825 1.00 176.98 ? 1548 GLU A C     1 
ATOM   796   O  O     . GLU A 1 1548 ? 182.702 205.985 138.741 1.00 176.88 ? 1548 GLU A O     1 
ATOM   797   C  CB    . GLU A 1 1548 ? 180.430 207.983 140.058 1.00 179.12 ? 1548 GLU A CB    1 
ATOM   798   C  CG    . GLU A 1 1548 ? 180.477 208.771 138.760 1.00 179.18 ? 1548 GLU A CG    1 
ATOM   799   C  CD    . GLU A 1 1548 ? 181.867 209.286 138.443 1.00 180.10 ? 1548 GLU A CD    1 
ATOM   800   O  OE1   . GLU A 1 1548 ? 182.705 209.343 139.367 1.00 179.81 ? 1548 GLU A OE1   1 
ATOM   801   O  OE2   . GLU A 1 1548 ? 182.122 209.632 137.271 1.00 180.03 ? 1548 GLU A OE2   1 
ATOM   802   N  N     . GLY A 1 1549 ? 182.779 206.049 140.988 1.00 165.91 ? 1549 GLY A N     1 
ATOM   803   C  CA    . GLY A 1 1549 ? 184.193 205.721 141.026 1.00 165.28 ? 1549 GLY A CA    1 
ATOM   804   C  C     . GLY A 1 1549 ? 184.513 204.330 140.522 1.00 166.91 ? 1549 GLY A C     1 
ATOM   805   O  O     . GLY A 1 1549 ? 185.675 204.042 140.216 1.00 167.93 ? 1549 GLY A O     1 
ATOM   806   N  N     . ILE A 1 1550 ? 183.510 203.461 140.427 1.00 170.39 ? 1550 ILE A N     1 
ATOM   807   C  CA    . ILE A 1 1550 ? 183.723 202.121 139.895 1.00 171.03 ? 1550 ILE A CA    1 
ATOM   808   C  C     . ILE A 1 1550 ? 183.530 202.081 138.381 1.00 171.92 ? 1550 ILE A C     1 
ATOM   809   O  O     . ILE A 1 1550 ? 184.317 201.444 137.674 1.00 171.86 ? 1550 ILE A O     1 
ATOM   810   C  CB    . ILE A 1 1550 ? 182.790 201.122 140.602 1.00 171.00 ? 1550 ILE A CB    1 
ATOM   811   C  CG1   . ILE A 1 1550 ? 183.441 200.599 141.882 1.00 170.70 ? 1550 ILE A CG1   1 
ATOM   812   C  CG2   . ILE A 1 1550 ? 182.432 199.963 139.684 1.00 172.22 ? 1550 ILE A CG2   1 
ATOM   813   C  CD1   . ILE A 1 1550 ? 182.613 199.562 142.608 1.00 171.57 ? 1550 ILE A CD1   1 
ATOM   814   N  N     . PHE A 1 1551 ? 182.512 202.766 137.865 1.00 180.13 ? 1551 PHE A N     1 
ATOM   815   C  CA    . PHE A 1 1551 ? 182.199 202.760 136.444 1.00 180.75 ? 1551 PHE A CA    1 
ATOM   816   C  C     . PHE A 1 1551 ? 182.951 203.828 135.660 1.00 181.72 ? 1551 PHE A C     1 
ATOM   817   O  O     . PHE A 1 1551 ? 182.747 203.942 134.448 1.00 181.20 ? 1551 PHE A O     1 
ATOM   818   C  CB    . PHE A 1 1551 ? 180.692 202.935 136.238 1.00 179.83 ? 1551 PHE A CB    1 
ATOM   819   C  CG    . PHE A 1 1551 ? 179.893 201.697 136.533 1.00 179.85 ? 1551 PHE A CG    1 
ATOM   820   C  CD1   . PHE A 1 1551 ? 179.905 200.626 135.656 1.00 179.84 ? 1551 PHE A CD1   1 
ATOM   821   C  CD2   . PHE A 1 1551 ? 179.136 201.603 137.688 1.00 179.86 ? 1551 PHE A CD2   1 
ATOM   822   C  CE1   . PHE A 1 1551 ? 179.172 199.486 135.923 1.00 179.85 ? 1551 PHE A CE1   1 
ATOM   823   C  CE2   . PHE A 1 1551 ? 178.402 200.466 137.961 1.00 179.68 ? 1551 PHE A CE2   1 
ATOM   824   C  CZ    . PHE A 1 1551 ? 178.420 199.406 137.077 1.00 179.57 ? 1551 PHE A CZ    1 
ATOM   825   N  N     . THR A 1 1552 ? 183.801 204.615 136.315 1.00 179.91 ? 1552 THR A N     1 
ATOM   826   C  CA    . THR A 1 1552 ? 184.618 205.611 135.631 1.00 176.80 ? 1552 THR A CA    1 
ATOM   827   C  C     . THR A 1 1552 ? 186.106 205.358 135.804 1.00 175.93 ? 1552 THR A C     1 
ATOM   828   O  O     . THR A 1 1552 ? 186.853 205.382 134.818 1.00 175.78 ? 1552 THR A O     1 
ATOM   829   C  CB    . THR A 1 1552 ? 184.268 207.022 136.132 1.00 176.97 ? 1552 THR A CB    1 
ATOM   830   O  OG1   . THR A 1 1552 ? 182.850 207.218 136.058 1.00 177.40 ? 1552 THR A OG1   1 
ATOM   831   C  CG2   . THR A 1 1552 ? 184.964 208.074 135.285 1.00 177.10 ? 1552 THR A CG2   1 
ATOM   832   N  N     . GLY A 1 1553 ? 186.562 205.115 137.034 1.00 175.87 ? 1553 GLY A N     1 
ATOM   833   C  CA    . GLY A 1 1553 ? 187.977 204.878 137.261 1.00 176.02 ? 1553 GLY A CA    1 
ATOM   834   C  C     . GLY A 1 1553 ? 188.483 203.591 136.644 1.00 176.29 ? 1553 GLY A C     1 
ATOM   835   O  O     . GLY A 1 1553 ? 189.622 203.533 136.170 1.00 176.20 ? 1553 GLY A O     1 
ATOM   836   N  N     . SER A 1 1554 ? 187.659 202.548 136.638 1.00 182.77 ? 1554 SER A N     1 
ATOM   837   C  CA    . SER A 1 1554 ? 188.051 201.239 136.134 1.00 183.86 ? 1554 SER A CA    1 
ATOM   838   C  C     . SER A 1 1554 ? 187.627 201.097 134.678 1.00 184.59 ? 1554 SER A C     1 
ATOM   839   O  O     . SER A 1 1554 ? 186.476 201.381 134.331 1.00 185.10 ? 1554 SER A O     1 
ATOM   840   C  CB    . SER A 1 1554 ? 187.429 200.124 136.975 1.00 184.03 ? 1554 SER A CB    1 
ATOM   841   O  OG    . SER A 1 1554 ? 186.015 200.151 136.891 1.00 183.97 ? 1554 SER A OG    1 
ATOM   842   N  N     . ALA A 1 1555 ? 188.560 200.657 133.833 1.00 184.08 ? 1555 ALA A N     1 
ATOM   843   C  CA    . ALA A 1 1555 ? 188.288 200.461 132.416 1.00 183.04 ? 1555 ALA A CA    1 
ATOM   844   C  C     . ALA A 1 1555 ? 187.918 199.028 132.064 1.00 184.36 ? 1555 ALA A C     1 
ATOM   845   O  O     . ALA A 1 1555 ? 187.268 198.810 131.036 1.00 184.64 ? 1555 ALA A O     1 
ATOM   846   C  CB    . ALA A 1 1555 ? 189.501 200.885 131.579 1.00 182.31 ? 1555 ALA A CB    1 
ATOM   847   N  N     . ASP A 1 1556 ? 188.312 198.051 132.884 1.00 191.04 ? 1556 ASP A N     1 
ATOM   848   C  CA    . ASP A 1 1556 ? 187.999 196.658 132.591 1.00 191.90 ? 1556 ASP A CA    1 
ATOM   849   C  C     . ASP A 1 1556 ? 186.518 196.345 132.764 1.00 191.42 ? 1556 ASP A C     1 
ATOM   850   O  O     . ASP A 1 1556 ? 186.023 195.392 132.150 1.00 189.69 ? 1556 ASP A O     1 
ATOM   851   C  CB    . ASP A 1 1556 ? 188.829 195.734 133.483 1.00 192.09 ? 1556 ASP A CB    1 
ATOM   852   C  CG    . ASP A 1 1556 ? 190.287 195.679 133.070 1.00 191.11 ? 1556 ASP A CG    1 
ATOM   853   O  OD1   . ASP A 1 1556 ? 190.787 196.681 132.518 1.00 190.32 ? 1556 ASP A OD1   1 
ATOM   854   O  OD2   . ASP A 1 1556 ? 190.933 194.635 133.299 1.00 190.68 ? 1556 ASP A OD2   1 
ATOM   855   N  N     . ILE A 1 1557 ? 185.804 197.122 133.583 1.00 188.95 ? 1557 ILE A N     1 
ATOM   856   C  CA    . ILE A 1 1557 ? 184.390 196.851 133.817 1.00 188.60 ? 1557 ILE A CA    1 
ATOM   857   C  C     . ILE A 1 1557 ? 183.566 197.129 132.566 1.00 188.98 ? 1557 ILE A C     1 
ATOM   858   O  O     . ILE A 1 1557 ? 182.490 196.546 132.384 1.00 189.19 ? 1557 ILE A O     1 
ATOM   859   C  CB    . ILE A 1 1557 ? 183.885 197.658 135.029 1.00 187.53 ? 1557 ILE A CB    1 
ATOM   860   C  CG1   . ILE A 1 1557 ? 182.591 197.050 135.572 1.00 188.12 ? 1557 ILE A CG1   1 
ATOM   861   C  CG2   . ILE A 1 1557 ? 183.681 199.122 134.666 1.00 186.82 ? 1557 ILE A CG2   1 
ATOM   862   C  CD1   . ILE A 1 1557 ? 182.110 197.684 136.853 1.00 187.98 ? 1557 ILE A CD1   1 
ATOM   863   N  N     . LYS A 1 1558 ? 184.041 198.020 131.691 1.00 186.99 ? 1558 LYS A N     1 
ATOM   864   C  CA    . LYS A 1 1558 ? 183.326 198.282 130.446 1.00 185.40 ? 1558 LYS A CA    1 
ATOM   865   C  C     . LYS A 1 1558 ? 183.276 197.039 129.568 1.00 185.79 ? 1558 LYS A C     1 
ATOM   866   O  O     . LYS A 1 1558 ? 182.219 196.695 129.026 1.00 184.61 ? 1558 LYS A O     1 
ATOM   867   C  CB    . LYS A 1 1558 ? 183.984 199.437 129.693 1.00 185.66 ? 1558 LYS A CB    1 
ATOM   868   C  CG    . LYS A 1 1558 ? 184.472 200.568 130.579 1.00 185.62 ? 1558 LYS A CG    1 
ATOM   869   C  CD    . LYS A 1 1558 ? 183.406 201.636 130.742 1.00 185.19 ? 1558 LYS A CD    1 
ATOM   870   C  CE    . LYS A 1 1558 ? 183.839 202.692 131.741 1.00 184.55 ? 1558 LYS A CE    1 
ATOM   871   N  NZ    . LYS A 1 1558 ? 183.916 202.146 133.124 1.00 185.25 ? 1558 LYS A NZ    1 
ATOM   872   N  N     . HIS A 1 1559 ? 184.410 196.352 129.418 1.00 194.65 ? 1559 HIS A N     1 
ATOM   873   C  CA    . HIS A 1 1559 ? 184.444 195.135 128.616 1.00 194.37 ? 1559 HIS A CA    1 
ATOM   874   C  C     . HIS A 1 1559 ? 183.811 193.961 129.351 1.00 194.51 ? 1559 HIS A C     1 
ATOM   875   O  O     . HIS A 1 1559 ? 183.117 193.143 128.736 1.00 194.77 ? 1559 HIS A O     1 
ATOM   876   C  CB    . HIS A 1 1559 ? 185.886 194.806 128.227 1.00 193.45 ? 1559 HIS A CB    1 
ATOM   877   C  CG    . HIS A 1 1559 ? 186.702 196.007 127.862 1.00 194.40 ? 1559 HIS A CG    1 
ATOM   878   N  ND1   . HIS A 1 1559 ? 187.342 196.786 128.802 1.00 194.54 ? 1559 HIS A ND1   1 
ATOM   879   C  CD2   . HIS A 1 1559 ? 186.980 196.564 126.660 1.00 194.43 ? 1559 HIS A CD2   1 
ATOM   880   C  CE1   . HIS A 1 1559 ? 187.980 197.770 128.195 1.00 194.49 ? 1559 HIS A CE1   1 
ATOM   881   N  NE2   . HIS A 1 1559 ? 187.777 197.658 126.895 1.00 194.57 ? 1559 HIS A NE2   1 
ATOM   882   N  N     . LEU A 1 1560 ? 184.042 193.859 130.661 1.00 190.19 ? 1560 LEU A N     1 
ATOM   883   C  CA    . LEU A 1 1560 ? 183.510 192.729 131.416 1.00 190.23 ? 1560 LEU A CA    1 
ATOM   884   C  C     . LEU A 1 1560 ? 181.994 192.806 131.553 1.00 190.35 ? 1560 LEU A C     1 
ATOM   885   O  O     . LEU A 1 1560 ? 181.291 191.826 131.283 1.00 189.87 ? 1560 LEU A O     1 
ATOM   886   C  CB    . LEU A 1 1560 ? 184.165 192.672 132.795 1.00 189.53 ? 1560 LEU A CB    1 
ATOM   887   C  CG    . LEU A 1 1560 ? 184.244 191.302 133.469 1.00 188.92 ? 1560 LEU A CG    1 
ATOM   888   C  CD1   . LEU A 1 1560 ? 185.086 190.338 132.647 1.00 188.47 ? 1560 LEU A CD1   1 
ATOM   889   C  CD2   . LEU A 1 1560 ? 184.796 191.442 134.876 1.00 188.23 ? 1560 LEU A CD2   1 
ATOM   890   N  N     . LEU A 1 1561 ? 181.473 193.960 131.965 1.00 191.46 ? 1561 LEU A N     1 
ATOM   891   C  CA    . LEU A 1 1561 ? 180.058 194.112 132.309 1.00 190.43 ? 1561 LEU A CA    1 
ATOM   892   C  C     . LEU A 1 1561 ? 179.494 195.340 131.610 1.00 190.84 ? 1561 LEU A C     1 
ATOM   893   O  O     . LEU A 1 1561 ? 179.349 196.410 132.213 1.00 191.07 ? 1561 LEU A O     1 
ATOM   894   C  CB    . LEU A 1 1561 ? 179.875 194.209 133.826 1.00 189.55 ? 1561 LEU A CB    1 
ATOM   895   C  CG    . LEU A 1 1561 ? 180.866 193.440 134.705 1.00 190.21 ? 1561 LEU A CG    1 
ATOM   896   C  CD1   . LEU A 1 1561 ? 180.790 193.901 136.151 1.00 190.34 ? 1561 LEU A CD1   1 
ATOM   897   C  CD2   . LEU A 1 1561 ? 180.611 191.943 134.612 1.00 190.37 ? 1561 LEU A CD2   1 
ATOM   898   N  N     . PRO A 1 1562 ? 179.157 195.220 130.323 1.00 186.50 ? 1562 PRO A N     1 
ATOM   899   C  CA    . PRO A 1 1562 ? 178.714 196.398 129.562 1.00 185.67 ? 1562 PRO A CA    1 
ATOM   900   C  C     . PRO A 1 1562 ? 177.263 196.793 129.802 1.00 185.66 ? 1562 PRO A C     1 
ATOM   901   O  O     . PRO A 1 1562 ? 176.935 197.984 129.773 1.00 185.56 ? 1562 PRO A O     1 
ATOM   902   C  CB    . PRO A 1 1562 ? 178.928 195.971 128.100 1.00 184.05 ? 1562 PRO A CB    1 
ATOM   903   C  CG    . PRO A 1 1562 ? 179.672 194.651 128.156 1.00 183.96 ? 1562 PRO A CG    1 
ATOM   904   C  CD    . PRO A 1 1562 ? 179.302 194.039 129.461 1.00 185.23 ? 1562 PRO A CD    1 
ATOM   905   N  N     . VAL A 1 1563 ? 176.383 195.813 130.022 1.00 189.21 ? 1563 VAL A N     1 
ATOM   906   C  CA    . VAL A 1 1563 ? 174.950 196.100 130.075 1.00 189.82 ? 1563 VAL A CA    1 
ATOM   907   C  C     . VAL A 1 1563 ? 174.617 196.993 131.268 1.00 189.81 ? 1563 VAL A C     1 
ATOM   908   O  O     . VAL A 1 1563 ? 173.976 198.043 131.120 1.00 189.42 ? 1563 VAL A O     1 
ATOM   909   C  CB    . VAL A 1 1563 ? 174.139 194.789 130.087 1.00 189.20 ? 1563 VAL A CB    1 
ATOM   910   C  CG1   . VAL A 1 1563 ? 174.654 193.828 131.155 1.00 188.54 ? 1563 VAL A CG1   1 
ATOM   911   C  CG2   . VAL A 1 1563 ? 172.661 195.084 130.296 1.00 187.85 ? 1563 VAL A CG2   1 
ATOM   912   N  N     . GLU A 1 1564 ? 175.068 196.617 132.463 1.00 190.41 ? 1564 GLU A N     1 
ATOM   913   C  CA    . GLU A 1 1564 ? 174.806 197.485 133.601 1.00 190.18 ? 1564 GLU A CA    1 
ATOM   914   C  C     . GLU A 1 1564 ? 175.728 198.694 133.631 1.00 190.45 ? 1564 GLU A C     1 
ATOM   915   O  O     . GLU A 1 1564 ? 175.411 199.666 134.317 1.00 190.64 ? 1564 GLU A O     1 
ATOM   916   C  CB    . GLU A 1 1564 ? 174.892 196.708 134.918 1.00 189.69 ? 1564 GLU A CB    1 
ATOM   917   C  CG    . GLU A 1 1564 ? 176.262 196.639 135.547 1.00 190.15 ? 1564 GLU A CG    1 
ATOM   918   C  CD    . GLU A 1 1564 ? 176.982 195.360 135.197 1.00 190.55 ? 1564 GLU A CD    1 
ATOM   919   O  OE1   . GLU A 1 1564 ? 176.752 194.831 134.089 1.00 190.69 ? 1564 GLU A OE1   1 
ATOM   920   O  OE2   . GLU A 1 1564 ? 177.759 194.871 136.042 1.00 190.17 ? 1564 GLU A OE2   1 
ATOM   921   N  N     . THR A 1 1565 ? 176.828 198.683 132.875 1.00 188.37 ? 1565 THR A N     1 
ATOM   922   C  CA    . THR A 1 1565 ? 177.576 199.919 132.666 1.00 187.82 ? 1565 THR A CA    1 
ATOM   923   C  C     . THR A 1 1565 ? 176.727 200.948 131.928 1.00 188.32 ? 1565 THR A C     1 
ATOM   924   O  O     . THR A 1 1565 ? 176.675 202.119 132.320 1.00 188.21 ? 1565 THR A O     1 
ATOM   925   C  CB    . THR A 1 1565 ? 178.865 199.636 131.895 1.00 186.87 ? 1565 THR A CB    1 
ATOM   926   O  OG1   . THR A 1 1565 ? 179.612 198.614 132.566 1.00 187.97 ? 1565 THR A OG1   1 
ATOM   927   C  CG2   . THR A 1 1565 ? 179.714 200.894 131.794 1.00 186.28 ? 1565 THR A CG2   1 
ATOM   928   N  N     . GLN A 1 1566 ? 176.036 200.523 130.868 1.00 189.04 ? 1566 GLN A N     1 
ATOM   929   C  CA    . GLN A 1 1566 ? 175.126 201.424 130.166 1.00 188.99 ? 1566 GLN A CA    1 
ATOM   930   C  C     . GLN A 1 1566 ? 173.943 201.811 131.047 1.00 189.00 ? 1566 GLN A C     1 
ATOM   931   O  O     . GLN A 1 1566 ? 173.482 202.962 131.014 1.00 188.58 ? 1566 GLN A O     1 
ATOM   932   C  CB    . GLN A 1 1566 ? 174.641 200.776 128.870 1.00 187.78 ? 1566 GLN A CB    1 
ATOM   933   C  CG    . GLN A 1 1566 ? 175.733 200.576 127.834 1.00 188.61 ? 1566 GLN A CG    1 
ATOM   934   C  CD    . GLN A 1 1566 ? 176.366 201.882 127.400 1.00 189.16 ? 1566 GLN A CD    1 
ATOM   935   O  OE1   . GLN A 1 1566 ? 177.514 202.172 127.737 1.00 189.47 ? 1566 GLN A OE1   1 
ATOM   936   N  NE2   . GLN A 1 1566 ? 175.617 202.681 126.648 1.00 188.73 ? 1566 GLN A NE2   1 
ATOM   937   N  N     . ARG A 1 1567 ? 173.431 200.859 131.830 1.00 183.12 ? 1567 ARG A N     1 
ATOM   938   C  CA    . ARG A 1 1567 ? 172.351 201.175 132.761 1.00 181.82 ? 1567 ARG A CA    1 
ATOM   939   C  C     . ARG A 1 1567 ? 172.780 202.254 133.749 1.00 182.20 ? 1567 ARG A C     1 
ATOM   940   O  O     . ARG A 1 1567 ? 172.045 203.219 133.995 1.00 183.06 ? 1567 ARG A O     1 
ATOM   941   C  CB    . ARG A 1 1567 ? 171.906 199.912 133.499 1.00 182.32 ? 1567 ARG A CB    1 
ATOM   942   C  CG    . ARG A 1 1567 ? 171.025 198.983 132.678 1.00 182.13 ? 1567 ARG A CG    1 
ATOM   943   C  CD    . ARG A 1 1567 ? 171.212 197.532 133.100 1.00 183.10 ? 1567 ARG A CD    1 
ATOM   944   N  NE    . ARG A 1 1567 ? 170.093 196.687 132.698 1.00 183.66 ? 1567 ARG A NE    1 
ATOM   945   C  CZ    . ARG A 1 1567 ? 168.901 196.691 133.278 1.00 182.83 ? 1567 ARG A CZ    1 
ATOM   946   N  NH1   . ARG A 1 1567 ? 168.634 197.480 134.305 1.00 182.56 ? 1567 ARG A NH1   1 
ATOM   947   N  NH2   . ARG A 1 1567 ? 167.953 195.878 132.819 1.00 182.20 ? 1567 ARG A NH2   1 
ATOM   948   N  N     . PHE A 1 1568 ? 173.982 202.115 134.315 1.00 181.81 ? 1568 PHE A N     1 
ATOM   949   C  CA    . PHE A 1 1568 ? 174.489 203.122 135.236 1.00 182.81 ? 1568 PHE A CA    1 
ATOM   950   C  C     . PHE A 1 1568 ? 174.768 204.437 134.530 1.00 182.43 ? 1568 PHE A C     1 
ATOM   951   O  O     . PHE A 1 1568 ? 174.636 205.495 135.143 1.00 181.13 ? 1568 PHE A O     1 
ATOM   952   C  CB    . PHE A 1 1568 ? 175.755 202.632 135.936 1.00 182.43 ? 1568 PHE A CB    1 
ATOM   953   C  CG    . PHE A 1 1568 ? 176.345 203.641 136.879 1.00 182.03 ? 1568 PHE A CG    1 
ATOM   954   C  CD1   . PHE A 1 1568 ? 175.745 203.898 138.100 1.00 181.90 ? 1568 PHE A CD1   1 
ATOM   955   C  CD2   . PHE A 1 1568 ? 177.488 204.345 136.540 1.00 181.64 ? 1568 PHE A CD2   1 
ATOM   956   C  CE1   . PHE A 1 1568 ? 176.277 204.830 138.967 1.00 180.81 ? 1568 PHE A CE1   1 
ATOM   957   C  CE2   . PHE A 1 1568 ? 178.027 205.277 137.405 1.00 181.61 ? 1568 PHE A CE2   1 
ATOM   958   C  CZ    . PHE A 1 1568 ? 177.420 205.520 138.620 1.00 181.40 ? 1568 PHE A CZ    1 
ATOM   959   N  N     . GLN A 1 1569 ? 175.163 204.398 133.257 1.00 185.53 ? 1569 GLN A N     1 
ATOM   960   C  CA    . GLN A 1 1569 ? 175.319 205.641 132.510 1.00 185.43 ? 1569 GLN A CA    1 
ATOM   961   C  C     . GLN A 1 1569 ? 173.992 206.381 132.405 1.00 185.53 ? 1569 GLN A C     1 
ATOM   962   O  O     . GLN A 1 1569 ? 173.928 207.596 132.628 1.00 185.50 ? 1569 GLN A O     1 
ATOM   963   C  CB    . GLN A 1 1569 ? 175.887 205.352 131.121 1.00 185.51 ? 1569 GLN A CB    1 
ATOM   964   C  CG    . GLN A 1 1569 ? 176.204 206.597 130.311 1.00 186.31 ? 1569 GLN A CG    1 
ATOM   965   C  CD    . GLN A 1 1569 ? 177.261 207.464 130.967 1.00 186.44 ? 1569 GLN A CD    1 
ATOM   966   O  OE1   . GLN A 1 1569 ? 176.955 208.509 131.542 1.00 186.86 ? 1569 GLN A OE1   1 
ATOM   967   N  NE2   . GLN A 1 1569 ? 178.514 207.032 130.886 1.00 185.23 ? 1569 GLN A NE2   1 
ATOM   968   N  N     . SER A 1 1570 ? 172.916 205.658 132.087 1.00 187.99 ? 1570 SER A N     1 
ATOM   969   C  CA    . SER A 1 1570 ? 171.597 206.285 132.002 1.00 188.16 ? 1570 SER A CA    1 
ATOM   970   C  C     . SER A 1 1570 ? 171.152 206.826 133.359 1.00 188.14 ? 1570 SER A C     1 
ATOM   971   O  O     . SER A 1 1570 ? 170.634 207.948 133.461 1.00 187.18 ? 1570 SER A O     1 
ATOM   972   C  CB    . SER A 1 1570 ? 170.577 205.282 131.461 1.00 187.45 ? 1570 SER A CB    1 
ATOM   973   O  OG    . SER A 1 1570 ? 171.109 204.549 130.373 1.00 187.47 ? 1570 SER A OG    1 
ATOM   974   N  N     . ILE A 1 1571 ? 171.347 206.036 134.417 1.00 187.89 ? 1571 ILE A N     1 
ATOM   975   C  CA    . ILE A 1 1571 ? 170.929 206.471 135.747 1.00 187.13 ? 1571 ILE A CA    1 
ATOM   976   C  C     . ILE A 1 1571 ? 171.765 207.654 136.222 1.00 187.28 ? 1571 ILE A C     1 
ATOM   977   O  O     . ILE A 1 1571 ? 171.246 208.564 136.877 1.00 187.00 ? 1571 ILE A O     1 
ATOM   978   C  CB    . ILE A 1 1571 ? 170.982 205.289 136.733 1.00 186.12 ? 1571 ILE A CB    1 
ATOM   979   C  CG1   . ILE A 1 1571 ? 169.975 204.220 136.309 1.00 186.04 ? 1571 ILE A CG1   1 
ATOM   980   C  CG2   . ILE A 1 1571 ? 170.701 205.751 138.152 1.00 186.09 ? 1571 ILE A CG2   1 
ATOM   981   C  CD1   . ILE A 1 1571 ? 170.402 202.814 136.620 1.00 186.21 ? 1571 ILE A CD1   1 
ATOM   982   N  N     . SER A 1 1572 ? 173.058 207.673 135.896 1.00 187.38 ? 1572 SER A N     1 
ATOM   983   C  CA    . SER A 1 1572 ? 173.898 208.819 136.215 1.00 187.86 ? 1572 SER A CA    1 
ATOM   984   C  C     . SER A 1 1572 ? 173.455 210.054 135.447 1.00 187.83 ? 1572 SER A C     1 
ATOM   985   O  O     . SER A 1 1572 ? 173.487 211.164 135.983 1.00 187.14 ? 1572 SER A O     1 
ATOM   986   C  CB    . SER A 1 1572 ? 175.361 208.493 135.913 1.00 187.49 ? 1572 SER A CB    1 
ATOM   987   O  OG    . SER A 1 1572 ? 176.220 209.521 136.373 1.00 189.00 ? 1572 SER A OG    1 
ATOM   988   N  N     . THR A 1 1573 ? 173.046 209.884 134.188 1.00 186.94 ? 1573 THR A N     1 
ATOM   989   C  CA    . THR A 1 1573 ? 172.511 211.013 133.435 1.00 186.29 ? 1573 THR A CA    1 
ATOM   990   C  C     . THR A 1 1573 ? 171.269 211.577 134.111 1.00 186.10 ? 1573 THR A C     1 
ATOM   991   O  O     . THR A 1 1573 ? 171.133 212.798 134.262 1.00 186.23 ? 1573 THR A O     1 
ATOM   992   C  CB    . THR A 1 1573 ? 172.192 210.585 132.001 1.00 185.74 ? 1573 THR A CB    1 
ATOM   993   O  OG1   . THR A 1 1573 ? 173.391 210.136 131.356 1.00 185.89 ? 1573 THR A OG1   1 
ATOM   994   C  CG2   . THR A 1 1573 ? 171.603 211.747 131.216 1.00 185.82 ? 1573 THR A CG2   1 
ATOM   995   N  N     . GLU A 1 1574 ? 170.361 210.698 134.544 1.00 181.46 ? 1574 GLU A N     1 
ATOM   996   C  CA    . GLU A 1 1574 ? 169.169 211.157 135.256 1.00 181.00 ? 1574 GLU A CA    1 
ATOM   997   C  C     . GLU A 1 1574 ? 169.537 211.860 136.559 1.00 182.27 ? 1574 GLU A C     1 
ATOM   998   O  O     . GLU A 1 1574 ? 168.959 212.903 136.902 1.00 181.97 ? 1574 GLU A O     1 
ATOM   999   C  CB    . GLU A 1 1574 ? 168.237 209.978 135.532 1.00 180.27 ? 1574 GLU A CB    1 
ATOM   1000  C  CG    . GLU A 1 1574 ? 167.529 209.440 134.303 1.00 180.32 ? 1574 GLU A CG    1 
ATOM   1001  C  CD    . GLU A 1 1574 ? 166.162 210.062 134.107 1.00 181.20 ? 1574 GLU A CD    1 
ATOM   1002  O  OE1   . GLU A 1 1574 ? 165.475 209.699 133.129 1.00 181.46 ? 1574 GLU A OE1   1 
ATOM   1003  O  OE2   . GLU A 1 1574 ? 165.774 210.916 134.932 1.00 181.23 ? 1574 GLU A OE2   1 
ATOM   1004  N  N     . PHE A 1 1575 ? 170.492 211.297 137.302 1.00 183.11 ? 1575 PHE A N     1 
ATOM   1005  C  CA    . PHE A 1 1575 ? 170.895 211.885 138.574 1.00 182.52 ? 1575 PHE A CA    1 
ATOM   1006  C  C     . PHE A 1 1575 ? 171.521 213.257 138.376 1.00 184.24 ? 1575 PHE A C     1 
ATOM   1007  O  O     . PHE A 1 1575 ? 171.227 214.188 139.129 1.00 184.08 ? 1575 PHE A O     1 
ATOM   1008  C  CB    . PHE A 1 1575 ? 171.859 210.949 139.304 1.00 181.22 ? 1575 PHE A CB    1 
ATOM   1009  C  CG    . PHE A 1 1575 ? 172.341 211.482 140.623 1.00 181.66 ? 1575 PHE A CG    1 
ATOM   1010  C  CD1   . PHE A 1 1575 ? 171.474 211.599 141.697 1.00 181.85 ? 1575 PHE A CD1   1 
ATOM   1011  C  CD2   . PHE A 1 1575 ? 173.662 211.861 140.793 1.00 181.77 ? 1575 PHE A CD2   1 
ATOM   1012  C  CE1   . PHE A 1 1575 ? 171.913 212.088 142.912 1.00 182.02 ? 1575 PHE A CE1   1 
ATOM   1013  C  CE2   . PHE A 1 1575 ? 174.108 212.350 142.006 1.00 181.51 ? 1575 PHE A CE2   1 
ATOM   1014  C  CZ    . PHE A 1 1575 ? 173.232 212.463 143.067 1.00 181.94 ? 1575 PHE A CZ    1 
ATOM   1015  N  N     . LEU A 1 1576 ? 172.377 213.411 137.362 1.00 182.85 ? 1576 LEU A N     1 
ATOM   1016  C  CA    . LEU A 1 1576 ? 172.976 214.716 137.100 1.00 181.29 ? 1576 LEU A CA    1 
ATOM   1017  C  C     . LEU A 1 1576 ? 171.945 215.710 136.583 1.00 181.75 ? 1576 LEU A C     1 
ATOM   1018  O  O     . LEU A 1 1576 ? 172.049 216.907 136.858 1.00 181.18 ? 1576 LEU A O     1 
ATOM   1019  C  CB    . LEU A 1 1576 ? 174.147 214.597 136.123 1.00 180.88 ? 1576 LEU A CB    1 
ATOM   1020  C  CG    . LEU A 1 1576 ? 175.281 213.620 136.439 1.00 180.08 ? 1576 LEU A CG    1 
ATOM   1021  C  CD1   . LEU A 1 1576 ? 176.534 214.008 135.672 1.00 179.85 ? 1576 LEU A CD1   1 
ATOM   1022  C  CD2   . LEU A 1 1576 ? 175.564 213.608 137.931 1.00 180.86 ? 1576 LEU A CD2   1 
ATOM   1023  N  N     . ALA A 1 1577 ? 170.941 215.242 135.839 1.00 184.89 ? 1577 ALA A N     1 
ATOM   1024  C  CA    . ALA A 1 1577 ? 169.861 216.140 135.440 1.00 184.66 ? 1577 ALA A CA    1 
ATOM   1025  C  C     . ALA A 1 1577 ? 169.119 216.676 136.659 1.00 185.00 ? 1577 ALA A C     1 
ATOM   1026  O  O     . ALA A 1 1577 ? 168.948 217.895 136.812 1.00 185.77 ? 1577 ALA A O     1 
ATOM   1027  C  CB    . ALA A 1 1577 ? 168.900 215.419 134.495 1.00 182.99 ? 1577 ALA A CB    1 
ATOM   1028  N  N     . LEU A 1 1578 ? 168.692 215.777 137.552 1.00 185.47 ? 1578 LEU A N     1 
ATOM   1029  C  CA    . LEU A 1 1578 ? 168.019 216.205 138.776 1.00 184.71 ? 1578 LEU A CA    1 
ATOM   1030  C  C     . LEU A 1 1578 ? 168.929 217.090 139.617 1.00 185.44 ? 1578 LEU A C     1 
ATOM   1031  O  O     . LEU A 1 1578 ? 168.474 218.043 140.259 1.00 187.41 ? 1578 LEU A O     1 
ATOM   1032  C  CB    . LEU A 1 1578 ? 167.575 214.983 139.582 1.00 184.93 ? 1578 LEU A CB    1 
ATOM   1033  C  CG    . LEU A 1 1578 ? 166.721 215.157 140.844 1.00 186.05 ? 1578 LEU A CG    1 
ATOM   1034  C  CD1   . LEU A 1 1578 ? 165.804 216.370 140.758 1.00 186.27 ? 1578 LEU A CD1   1 
ATOM   1035  C  CD2   . LEU A 1 1578 ? 165.919 213.895 141.129 1.00 186.73 ? 1578 LEU A CD2   1 
ATOM   1036  N  N     . MET A 1 1579 ? 170.227 216.799 139.605 1.00 186.04 ? 1579 MET A N     1 
ATOM   1037  C  CA    . MET A 1 1579 ? 171.158 217.481 140.489 1.00 186.42 ? 1579 MET A CA    1 
ATOM   1038  C  C     . MET A 1 1579 ? 171.455 218.886 139.979 1.00 187.36 ? 1579 MET A C     1 
ATOM   1039  O  O     . MET A 1 1579 ? 171.575 219.829 140.768 1.00 187.48 ? 1579 MET A O     1 
ATOM   1040  C  CB    . MET A 1 1579 ? 172.422 216.634 140.592 1.00 186.09 ? 1579 MET A CB    1 
ATOM   1041  C  CG    . MET A 1 1579 ? 172.545 215.906 141.913 1.00 187.24 ? 1579 MET A CG    1 
ATOM   1042  S  SD    . MET A 1 1579 ? 172.822 216.916 143.361 1.00 188.74 ? 1579 MET A SD    1 
ATOM   1043  C  CE    . MET A 1 1579 ? 174.568 216.589 143.528 1.00 186.55 ? 1579 MET A CE    1 
ATOM   1044  N  N     . LYS A 1 1580 ? 171.562 219.044 138.658 1.00 184.78 ? 1580 LYS A N     1 
ATOM   1045  C  CA    . LYS A 1 1580 ? 171.637 220.371 138.059 1.00 184.17 ? 1580 LYS A CA    1 
ATOM   1046  C  C     . LYS A 1 1580 ? 170.363 221.159 138.326 1.00 184.43 ? 1580 LYS A C     1 
ATOM   1047  O  O     . LYS A 1 1580 ? 170.413 222.365 138.601 1.00 184.22 ? 1580 LYS A O     1 
ATOM   1048  C  CB    . LYS A 1 1580 ? 171.887 220.255 136.554 1.00 184.02 ? 1580 LYS A CB    1 
ATOM   1049  C  CG    . LYS A 1 1580 ? 171.378 221.440 135.742 1.00 184.36 ? 1580 LYS A CG    1 
ATOM   1050  C  CD    . LYS A 1 1580 ? 171.364 221.132 134.254 1.00 184.51 ? 1580 LYS A CD    1 
ATOM   1051  C  CE    . LYS A 1 1580 ? 170.445 219.963 133.941 1.00 184.70 ? 1580 LYS A CE    1 
ATOM   1052  N  NZ    . LYS A 1 1580 ? 169.079 220.163 134.501 1.00 184.47 ? 1580 LYS A NZ    1 
ATOM   1053  N  N     . LYS A 1 1581 ? 169.206 220.492 138.247 1.00 187.39 ? 1581 LYS A N     1 
ATOM   1054  C  CA    . LYS A 1 1581 ? 167.953 221.160 138.585 1.00 186.48 ? 1581 LYS A CA    1 
ATOM   1055  C  C     . LYS A 1 1581 ? 167.970 221.663 140.024 1.00 186.43 ? 1581 LYS A C     1 
ATOM   1056  O  O     . LYS A 1 1581 ? 167.496 222.769 140.311 1.00 185.62 ? 1581 LYS A O     1 
ATOM   1057  C  CB    . LYS A 1 1581 ? 166.779 220.208 138.357 1.00 186.26 ? 1581 LYS A CB    1 
ATOM   1058  C  CG    . LYS A 1 1581 ? 165.452 220.692 138.919 1.00 185.54 ? 1581 LYS A CG    1 
ATOM   1059  C  CD    . LYS A 1 1581 ? 164.314 220.339 137.979 1.00 185.87 ? 1581 LYS A CD    1 
ATOM   1060  C  CE    . LYS A 1 1581 ? 163.734 218.973 138.302 1.00 186.01 ? 1581 LYS A CE    1 
ATOM   1061  N  NZ    . LYS A 1 1581 ? 162.304 218.876 137.906 1.00 185.89 ? 1581 LYS A NZ    1 
ATOM   1062  N  N     . VAL A 1 1582 ? 168.509 220.859 140.941 1.00 192.73 ? 1582 VAL A N     1 
ATOM   1063  C  CA    . VAL A 1 1582 ? 168.658 221.293 142.328 1.00 192.19 ? 1582 VAL A CA    1 
ATOM   1064  C  C     . VAL A 1 1582 ? 169.619 222.473 142.422 1.00 192.65 ? 1582 VAL A C     1 
ATOM   1065  O  O     . VAL A 1 1582 ? 169.374 223.435 143.159 1.00 193.53 ? 1582 VAL A O     1 
ATOM   1066  C  CB    . VAL A 1 1582 ? 169.121 220.116 143.206 1.00 191.92 ? 1582 VAL A CB    1 
ATOM   1067  C  CG1   . VAL A 1 1582 ? 169.554 220.608 144.578 1.00 191.46 ? 1582 VAL A CG1   1 
ATOM   1068  C  CG2   . VAL A 1 1582 ? 168.012 219.086 143.334 1.00 192.40 ? 1582 VAL A CG2   1 
ATOM   1069  N  N     . SER A 1 1583 ? 170.729 222.412 141.683 1.00 193.88 ? 1583 SER A N     1 
ATOM   1070  C  CA    . SER A 1 1583 ? 171.718 223.485 141.717 1.00 194.03 ? 1583 SER A CA    1 
ATOM   1071  C  C     . SER A 1 1583 ? 171.139 224.804 141.224 1.00 194.57 ? 1583 SER A C     1 
ATOM   1072  O  O     . SER A 1 1583 ? 171.534 225.871 141.707 1.00 193.87 ? 1583 SER A O     1 
ATOM   1073  C  CB    . SER A 1 1583 ? 172.939 223.100 140.881 1.00 192.79 ? 1583 SER A CB    1 
ATOM   1074  O  OG    . SER A 1 1583 ? 173.866 224.168 140.806 1.00 192.73 ? 1583 SER A OG    1 
ATOM   1075  N  N     . LYS A 1 1584 ? 170.215 224.754 140.262 1.00 198.20 ? 1584 LYS A N     1 
ATOM   1076  C  CA    . LYS A 1 1584 ? 169.581 225.978 139.782 1.00 197.38 ? 1584 LYS A CA    1 
ATOM   1077  C  C     . LYS A 1 1584 ? 168.790 226.660 140.893 1.00 196.73 ? 1584 LYS A C     1 
ATOM   1078  O  O     . LYS A 1 1584 ? 168.851 227.884 141.054 1.00 196.13 ? 1584 LYS A O     1 
ATOM   1079  C  CB    . LYS A 1 1584 ? 168.677 225.670 138.588 1.00 196.43 ? 1584 LYS A CB    1 
ATOM   1080  C  CG    . LYS A 1 1584 ? 169.416 225.190 137.350 1.00 196.16 ? 1584 LYS A CG    1 
ATOM   1081  C  CD    . LYS A 1 1584 ? 170.186 226.325 136.698 1.00 195.82 ? 1584 LYS A CD    1 
ATOM   1082  C  CE    . LYS A 1 1584 ? 170.939 225.849 135.467 1.00 195.89 ? 1584 LYS A CE    1 
ATOM   1083  N  NZ    . LYS A 1 1584 ? 170.060 225.082 134.543 1.00 196.23 ? 1584 LYS A NZ    1 
ATOM   1084  N  N     . SER A 1 1585 ? 168.042 225.881 141.674 1.00 204.59 ? 1585 SER A N     1 
ATOM   1085  C  CA    . SER A 1 1585 ? 167.213 226.404 142.759 1.00 205.26 ? 1585 SER A CA    1 
ATOM   1086  C  C     . SER A 1 1585 ? 167.534 225.635 144.033 1.00 205.84 ? 1585 SER A C     1 
ATOM   1087  O  O     . SER A 1 1585 ? 166.892 224.622 144.340 1.00 206.74 ? 1585 SER A O     1 
ATOM   1088  C  CB    . SER A 1 1585 ? 165.728 226.308 142.414 1.00 205.13 ? 1585 SER A CB    1 
ATOM   1089  O  OG    . SER A 1 1585 ? 165.373 224.986 142.047 1.00 205.49 ? 1585 SER A OG    1 
ATOM   1090  N  N     . PRO A 1 1586 ? 168.525 226.088 144.802 1.00 204.12 ? 1586 PRO A N     1 
ATOM   1091  C  CA    . PRO A 1 1586 ? 168.928 225.369 146.016 1.00 203.76 ? 1586 PRO A CA    1 
ATOM   1092  C  C     . PRO A 1 1586 ? 167.977 225.521 147.194 1.00 203.78 ? 1586 PRO A C     1 
ATOM   1093  O  O     . PRO A 1 1586 ? 168.313 225.066 148.291 1.00 203.67 ? 1586 PRO A O     1 
ATOM   1094  C  CB    . PRO A 1 1586 ? 170.292 225.998 146.337 1.00 202.77 ? 1586 PRO A CB    1 
ATOM   1095  C  CG    . PRO A 1 1586 ? 170.184 227.384 145.817 1.00 203.18 ? 1586 PRO A CG    1 
ATOM   1096  C  CD    . PRO A 1 1586 ? 169.333 227.300 144.578 1.00 203.52 ? 1586 PRO A CD    1 
ATOM   1097  N  N     . LEU A 1 1587 ? 166.818 226.147 147.009 1.00 208.53 ? 1587 LEU A N     1 
ATOM   1098  C  CA    . LEU A 1 1587 ? 165.855 226.269 148.094 1.00 209.04 ? 1587 LEU A CA    1 
ATOM   1099  C  C     . LEU A 1 1587 ? 165.294 224.901 148.462 1.00 209.47 ? 1587 LEU A C     1 
ATOM   1100  O  O     . LEU A 1 1587 ? 165.101 224.039 147.600 1.00 208.93 ? 1587 LEU A O     1 
ATOM   1101  C  CB    . LEU A 1 1587 ? 164.723 227.217 147.698 1.00 209.09 ? 1587 LEU A CB    1 
ATOM   1102  C  CG    . LEU A 1 1587 ? 164.129 228.072 148.820 1.00 209.09 ? 1587 LEU A CG    1 
ATOM   1103  C  CD1   . LEU A 1 1587 ? 165.222 228.846 149.542 1.00 208.65 ? 1587 LEU A CD1   1 
ATOM   1104  C  CD2   . LEU A 1 1587 ? 163.069 229.016 148.274 1.00 208.26 ? 1587 LEU A CD2   1 
ATOM   1105  N  N     . VAL A 1 1588 ? 165.041 224.703 149.758 1.00 211.76 ? 1588 VAL A N     1 
ATOM   1106  C  CA    . VAL A 1 1588 ? 164.583 223.402 150.237 1.00 211.86 ? 1588 VAL A CA    1 
ATOM   1107  C  C     . VAL A 1 1588 ? 163.220 223.056 149.650 1.00 211.80 ? 1588 VAL A C     1 
ATOM   1108  O  O     . VAL A 1 1588 ? 163.012 221.947 149.144 1.00 211.10 ? 1588 VAL A O     1 
ATOM   1109  C  CB    . VAL A 1 1588 ? 164.560 223.379 151.776 1.00 210.48 ? 1588 VAL A CB    1 
ATOM   1110  C  CG1   . VAL A 1 1588 ? 164.001 222.058 152.279 1.00 210.59 ? 1588 VAL A CG1   1 
ATOM   1111  C  CG2   . VAL A 1 1588 ? 165.957 223.614 152.328 1.00 210.07 ? 1588 VAL A CG2   1 
ATOM   1112  N  N     . MET A 1 1589 ? 162.272 223.995 149.696 1.00 211.77 ? 1589 MET A N     1 
ATOM   1113  C  CA    . MET A 1 1589 ? 160.954 223.723 149.132 1.00 211.37 ? 1589 MET A CA    1 
ATOM   1114  C  C     . MET A 1 1589 ? 161.004 223.666 147.611 1.00 212.06 ? 1589 MET A C     1 
ATOM   1115  O  O     . MET A 1 1589 ? 160.246 222.913 146.989 1.00 212.74 ? 1589 MET A O     1 
ATOM   1116  C  CB    . MET A 1 1589 ? 159.946 224.771 149.599 1.00 210.24 ? 1589 MET A CB    1 
ATOM   1117  C  CG    . MET A 1 1589 ? 159.791 224.848 151.105 1.00 210.13 ? 1589 MET A CG    1 
ATOM   1118  S  SD    . MET A 1 1589 ? 161.299 225.410 151.909 1.00 211.27 ? 1589 MET A SD    1 
ATOM   1119  C  CE    . MET A 1 1589 ? 161.042 227.178 151.840 1.00 211.32 ? 1589 MET A CE    1 
ATOM   1120  N  N     . ASP A 1 1590 ? 161.887 224.457 146.994 1.00 208.72 ? 1590 ASP A N     1 
ATOM   1121  C  CA    . ASP A 1 1590 ? 162.040 224.393 145.544 1.00 207.93 ? 1590 ASP A CA    1 
ATOM   1122  C  C     . ASP A 1 1590 ? 162.524 223.017 145.108 1.00 207.70 ? 1590 ASP A C     1 
ATOM   1123  O  O     . ASP A 1 1590 ? 162.202 222.554 144.008 1.00 206.70 ? 1590 ASP A O     1 
ATOM   1124  C  CB    . ASP A 1 1590 ? 163.002 225.481 145.067 1.00 207.37 ? 1590 ASP A CB    1 
ATOM   1125  C  CG    . ASP A 1 1590 ? 162.444 226.284 143.910 1.00 207.90 ? 1590 ASP A CG    1 
ATOM   1126  O  OD1   . ASP A 1 1590 ? 161.623 225.736 143.144 1.00 208.65 ? 1590 ASP A OD1   1 
ATOM   1127  O  OD2   . ASP A 1 1590 ? 162.824 227.465 143.766 1.00 207.77 ? 1590 ASP A OD2   1 
ATOM   1128  N  N     . VAL A 1 1591 ? 163.319 222.357 145.950 1.00 203.15 ? 1591 VAL A N     1 
ATOM   1129  C  CA    . VAL A 1 1591 ? 163.627 220.948 145.730 1.00 202.62 ? 1591 VAL A CA    1 
ATOM   1130  C  C     . VAL A 1 1591 ? 162.401 220.090 146.016 1.00 203.57 ? 1591 VAL A C     1 
ATOM   1131  O  O     . VAL A 1 1591 ? 162.102 219.137 145.286 1.00 203.56 ? 1591 VAL A O     1 
ATOM   1132  C  CB    . VAL A 1 1591 ? 164.832 220.528 146.592 1.00 201.64 ? 1591 VAL A CB    1 
ATOM   1133  C  CG1   . VAL A 1 1591 ? 165.012 219.022 146.565 1.00 202.68 ? 1591 VAL A CG1   1 
ATOM   1134  C  CG2   . VAL A 1 1591 ? 166.094 221.230 146.118 1.00 202.00 ? 1591 VAL A CG2   1 
ATOM   1135  N  N     . LEU A 1 1592 ? 161.666 220.423 147.081 1.00 205.40 ? 1592 LEU A N     1 
ATOM   1136  C  CA    . LEU A 1 1592 ? 160.538 219.601 147.505 1.00 205.56 ? 1592 LEU A CA    1 
ATOM   1137  C  C     . LEU A 1 1592 ? 159.378 219.649 146.517 1.00 205.76 ? 1592 LEU A C     1 
ATOM   1138  O  O     . LEU A 1 1592 ? 158.811 218.602 146.185 1.00 205.70 ? 1592 LEU A O     1 
ATOM   1139  C  CB    . LEU A 1 1592 ? 160.066 220.039 148.891 1.00 205.03 ? 1592 LEU A CB    1 
ATOM   1140  C  CG    . LEU A 1 1592 ? 159.175 219.056 149.652 1.00 204.67 ? 1592 LEU A CG    1 
ATOM   1141  C  CD1   . LEU A 1 1592 ? 160.009 217.952 150.282 1.00 204.88 ? 1592 LEU A CD1   1 
ATOM   1142  C  CD2   . LEU A 1 1592 ? 158.357 219.782 150.707 1.00 204.58 ? 1592 LEU A CD2   1 
ATOM   1143  N  N     . ASN A 1 1593 ? 159.012 220.835 146.033 1.00 203.03 ? 1593 ASN A N     1 
ATOM   1144  C  CA    . ASN A 1 1593 ? 157.840 220.980 145.178 1.00 201.53 ? 1593 ASN A CA    1 
ATOM   1145  C  C     . ASN A 1 1593 ? 158.067 220.468 143.761 1.00 201.52 ? 1593 ASN A C     1 
ATOM   1146  O  O     . ASN A 1 1593 ? 157.173 220.605 142.919 1.00 201.11 ? 1593 ASN A O     1 
ATOM   1147  C  CB    . ASN A 1 1593 ? 157.384 222.445 145.136 1.00 201.12 ? 1593 ASN A CB    1 
ATOM   1148  C  CG    . ASN A 1 1593 ? 158.447 223.380 144.591 1.00 201.72 ? 1593 ASN A CG    1 
ATOM   1149  O  OD1   . ASN A 1 1593 ? 159.514 222.948 144.163 1.00 202.67 ? 1593 ASN A OD1   1 
ATOM   1150  N  ND2   . ASN A 1 1593 ? 158.155 224.675 144.607 1.00 201.88 ? 1593 ASN A ND2   1 
ATOM   1151  N  N     . ILE A 1 1594 ? 159.239 219.896 143.476 1.00 199.44 ? 1594 ILE A N     1 
ATOM   1152  C  CA    . ILE A 1 1594 ? 159.479 219.289 142.174 1.00 199.49 ? 1594 ILE A CA    1 
ATOM   1153  C  C     . ILE A 1 1594 ? 158.517 218.128 141.980 1.00 200.32 ? 1594 ILE A C     1 
ATOM   1154  O  O     . ILE A 1 1594 ? 158.304 217.317 142.890 1.00 200.66 ? 1594 ILE A O     1 
ATOM   1155  C  CB    . ILE A 1 1594 ? 160.944 218.838 142.062 1.00 198.80 ? 1594 ILE A CB    1 
ATOM   1156  C  CG1   . ILE A 1 1594 ? 161.868 220.053 141.961 1.00 198.36 ? 1594 ILE A CG1   1 
ATOM   1157  C  CG2   . ILE A 1 1594 ? 161.138 217.914 140.868 1.00 198.26 ? 1594 ILE A CG2   1 
ATOM   1158  C  CD1   . ILE A 1 1594 ? 163.339 219.704 141.960 1.00 198.88 ? 1594 ILE A CD1   1 
ATOM   1159  N  N     . GLN A 1 1595 ? 157.913 218.053 140.796 1.00 199.82 ? 1595 GLN A N     1 
ATOM   1160  C  CA    . GLN A 1 1595 ? 156.951 216.996 140.517 1.00 198.80 ? 1595 GLN A CA    1 
ATOM   1161  C  C     . GLN A 1 1595 ? 157.637 215.634 140.526 1.00 198.58 ? 1595 GLN A C     1 
ATOM   1162  O  O     . GLN A 1 1595 ? 158.710 215.458 139.938 1.00 198.71 ? 1595 GLN A O     1 
ATOM   1163  C  CB    . GLN A 1 1595 ? 156.257 217.253 139.176 1.00 198.36 ? 1595 GLN A CB    1 
ATOM   1164  C  CG    . GLN A 1 1595 ? 157.134 217.080 137.941 1.00 199.06 ? 1595 GLN A CG    1 
ATOM   1165  C  CD    . GLN A 1 1595 ? 157.971 218.308 137.637 1.00 198.94 ? 1595 GLN A CD    1 
ATOM   1166  O  OE1   . GLN A 1 1595 ? 158.794 218.731 138.449 1.00 197.98 ? 1595 GLN A OE1   1 
ATOM   1167  N  NE2   . GLN A 1 1595 ? 157.765 218.886 136.459 1.00 199.11 ? 1595 GLN A NE2   1 
ATOM   1168  N  N     . GLY A 1 1596 ? 157.028 214.678 141.224 1.00 193.30 ? 1596 GLY A N     1 
ATOM   1169  C  CA    . GLY A 1 1596 ? 157.549 213.322 141.270 1.00 193.10 ? 1596 GLY A CA    1 
ATOM   1170  C  C     . GLY A 1 1596 ? 158.957 213.200 141.809 1.00 193.48 ? 1596 GLY A C     1 
ATOM   1171  O  O     . GLY A 1 1596 ? 159.669 212.258 141.446 1.00 193.24 ? 1596 GLY A O     1 
ATOM   1172  N  N     . VAL A 1 1597 ? 159.383 214.132 142.665 1.00 193.89 ? 1597 VAL A N     1 
ATOM   1173  C  CA    . VAL A 1 1597 ? 160.748 214.084 143.183 1.00 193.34 ? 1597 VAL A CA    1 
ATOM   1174  C  C     . VAL A 1 1597 ? 160.941 212.868 144.082 1.00 193.26 ? 1597 VAL A C     1 
ATOM   1175  O  O     . VAL A 1 1597 ? 161.962 212.173 143.999 1.00 192.99 ? 1597 VAL A O     1 
ATOM   1176  C  CB    . VAL A 1 1597 ? 161.098 215.399 143.908 1.00 192.08 ? 1597 VAL A CB    1 
ATOM   1177  C  CG1   . VAL A 1 1597 ? 160.077 215.720 144.994 1.00 191.95 ? 1597 VAL A CG1   1 
ATOM   1178  C  CG2   . VAL A 1 1597 ? 162.503 215.332 144.487 1.00 191.09 ? 1597 VAL A CG2   1 
ATOM   1179  N  N     . GLN A 1 1598 ? 159.964 212.583 144.948 1.00 190.03 ? 1598 GLN A N     1 
ATOM   1180  C  CA    . GLN A 1 1598 ? 160.073 211.434 145.840 1.00 189.25 ? 1598 GLN A CA    1 
ATOM   1181  C  C     . GLN A 1 1598 ? 160.117 210.132 145.050 1.00 188.83 ? 1598 GLN A C     1 
ATOM   1182  O  O     . GLN A 1 1598 ? 160.959 209.262 145.306 1.00 188.35 ? 1598 GLN A O     1 
ATOM   1183  C  CB    . GLN A 1 1598 ? 158.903 211.429 146.825 1.00 187.49 ? 1598 GLN A CB    1 
ATOM   1184  C  CG    . GLN A 1 1598 ? 159.012 210.385 147.922 1.00 187.41 ? 1598 GLN A CG    1 
ATOM   1185  C  CD    . GLN A 1 1598 ? 159.951 210.808 149.034 1.00 187.95 ? 1598 GLN A CD    1 
ATOM   1186  O  OE1   . GLN A 1 1598 ? 159.703 211.794 149.728 1.00 187.95 ? 1598 GLN A OE1   1 
ATOM   1187  N  NE2   . GLN A 1 1598 ? 161.036 210.063 149.209 1.00 188.54 ? 1598 GLN A NE2   1 
ATOM   1188  N  N     . ARG A 1 1599 ? 159.219 209.988 144.072 1.00 186.14 ? 1599 ARG A N     1 
ATOM   1189  C  CA    . ARG A 1 1599 ? 159.205 208.782 143.252 1.00 185.93 ? 1599 ARG A CA    1 
ATOM   1190  C  C     . ARG A 1 1599 ? 160.489 208.651 142.444 1.00 186.00 ? 1599 ARG A C     1 
ATOM   1191  O  O     . ARG A 1 1599 ? 161.011 207.543 142.271 1.00 185.55 ? 1599 ARG A O     1 
ATOM   1192  C  CB    . ARG A 1 1599 ? 157.987 208.788 142.328 1.00 185.99 ? 1599 ARG A CB    1 
ATOM   1193  C  CG    . ARG A 1 1599 ? 157.693 207.441 141.687 1.00 185.87 ? 1599 ARG A CG    1 
ATOM   1194  C  CD    . ARG A 1 1599 ? 157.140 207.606 140.281 1.00 185.81 ? 1599 ARG A CD    1 
ATOM   1195  N  NE    . ARG A 1 1599 ? 158.201 207.662 139.282 1.00 186.49 ? 1599 ARG A NE    1 
ATOM   1196  C  CZ    . ARG A 1 1599 ? 158.625 208.775 138.700 1.00 186.19 ? 1599 ARG A CZ    1 
ATOM   1197  N  NH1   . ARG A 1 1599 ? 158.096 209.952 138.990 1.00 186.31 ? 1599 ARG A NH1   1 
ATOM   1198  N  NH2   . ARG A 1 1599 ? 159.605 208.706 137.803 1.00 184.84 ? 1599 ARG A NH2   1 
ATOM   1199  N  N     . SER A 1 1600 ? 161.007 209.771 141.932 1.00 184.85 ? 1600 SER A N     1 
ATOM   1200  C  CA    . SER A 1 1600 ? 162.262 209.731 141.190 1.00 185.12 ? 1600 SER A CA    1 
ATOM   1201  C  C     . SER A 1 1600 ? 163.409 209.269 142.079 1.00 185.82 ? 1600 SER A C     1 
ATOM   1202  O  O     . SER A 1 1600 ? 164.235 208.448 141.664 1.00 186.12 ? 1600 SER A O     1 
ATOM   1203  C  CB    . SER A 1 1600 ? 162.569 211.103 140.590 1.00 185.04 ? 1600 SER A CB    1 
ATOM   1204  O  OG    . SER A 1 1600 ? 162.684 212.086 141.602 1.00 184.83 ? 1600 SER A OG    1 
ATOM   1205  N  N     . LEU A 1 1601 ? 163.470 209.778 143.312 1.00 183.25 ? 1601 LEU A N     1 
ATOM   1206  C  CA    . LEU A 1 1601 ? 164.504 209.329 144.238 1.00 183.06 ? 1601 LEU A CA    1 
ATOM   1207  C  C     . LEU A 1 1601 ? 164.359 207.844 144.545 1.00 182.59 ? 1601 LEU A C     1 
ATOM   1208  O  O     . LEU A 1 1601 ? 165.356 207.115 144.612 1.00 182.15 ? 1601 LEU A O     1 
ATOM   1209  C  CB    . LEU A 1 1601 ? 164.455 210.154 145.524 1.00 182.79 ? 1601 LEU A CB    1 
ATOM   1210  C  CG    . LEU A 1 1601 ? 165.422 211.338 145.624 1.00 182.02 ? 1601 LEU A CG    1 
ATOM   1211  C  CD1   . LEU A 1 1601 ? 166.862 210.853 145.586 1.00 181.86 ? 1601 LEU A CD1   1 
ATOM   1212  C  CD2   . LEU A 1 1601 ? 165.169 212.355 144.523 1.00 182.14 ? 1601 LEU A CD2   1 
ATOM   1213  N  N     . GLU A 1 1602 ? 163.122 207.376 144.731 1.00 181.42 ? 1602 GLU A N     1 
ATOM   1214  C  CA    . GLU A 1 1602 ? 162.909 205.961 145.024 1.00 181.53 ? 1602 GLU A CA    1 
ATOM   1215  C  C     . GLU A 1 1602 ? 163.354 205.073 143.866 1.00 180.57 ? 1602 GLU A C     1 
ATOM   1216  O  O     . GLU A 1 1602 ? 164.015 204.050 144.081 1.00 182.76 ? 1602 GLU A O     1 
ATOM   1217  C  CB    . GLU A 1 1602 ? 161.442 205.704 145.371 1.00 182.73 ? 1602 GLU A CB    1 
ATOM   1218  C  CG    . GLU A 1 1602 ? 160.955 206.461 146.596 1.00 182.35 ? 1602 GLU A CG    1 
ATOM   1219  C  CD    . GLU A 1 1602 ? 159.984 205.656 147.436 1.00 181.29 ? 1602 GLU A CD    1 
ATOM   1220  O  OE1   . GLU A 1 1602 ? 159.094 205.000 146.855 1.00 182.74 ? 1602 GLU A OE1   1 
ATOM   1221  O  OE2   . GLU A 1 1602 ? 160.109 205.681 148.678 1.00 179.50 ? 1602 GLU A OE2   1 
ATOM   1222  N  N     . ARG A 1 1603 ? 163.006 205.443 142.629 1.00 173.73 ? 1603 ARG A N     1 
ATOM   1223  C  CA    . ARG A 1 1603 ? 163.409 204.609 141.498 1.00 174.26 ? 1603 ARG A CA    1 
ATOM   1224  C  C     . ARG A 1 1603 ? 164.916 204.674 141.278 1.00 175.95 ? 1603 ARG A C     1 
ATOM   1225  O  O     . ARG A 1 1603 ? 165.533 203.674 140.892 1.00 175.07 ? 1603 ARG A O     1 
ATOM   1226  C  CB    . ARG A 1 1603 ? 162.664 205.004 140.220 1.00 174.96 ? 1603 ARG A CB    1 
ATOM   1227  C  CG    . ARG A 1 1603 ? 162.656 206.480 139.903 1.00 176.07 ? 1603 ARG A CG    1 
ATOM   1228  C  CD    . ARG A 1 1603 ? 162.397 206.736 138.428 1.00 175.73 ? 1603 ARG A CD    1 
ATOM   1229  N  NE    . ARG A 1 1603 ? 163.590 206.518 137.619 1.00 174.58 ? 1603 ARG A NE    1 
ATOM   1230  C  CZ    . ARG A 1 1603 ? 163.648 205.708 136.571 1.00 174.26 ? 1603 ARG A CZ    1 
ATOM   1231  N  NH1   . ARG A 1 1603 ? 162.593 205.015 136.175 1.00 174.85 ? 1603 ARG A NH1   1 
ATOM   1232  N  NH2   . ARG A 1 1603 ? 164.793 205.590 135.904 1.00 174.33 ? 1603 ARG A NH2   1 
ATOM   1233  N  N     . LEU A 1 1604 ? 165.528 205.838 141.521 1.00 180.00 ? 1604 LEU A N     1 
ATOM   1234  C  CA    . LEU A 1 1604 ? 166.982 205.927 141.442 1.00 179.83 ? 1604 LEU A CA    1 
ATOM   1235  C  C     . LEU A 1 1604 ? 167.641 205.007 142.460 1.00 179.10 ? 1604 LEU A C     1 
ATOM   1236  O  O     . LEU A 1 1604 ? 168.605 204.303 142.139 1.00 178.21 ? 1604 LEU A O     1 
ATOM   1237  C  CB    . LEU A 1 1604 ? 167.436 207.372 141.654 1.00 179.37 ? 1604 LEU A CB    1 
ATOM   1238  C  CG    . LEU A 1 1604 ? 167.189 208.357 140.510 1.00 177.74 ? 1604 LEU A CG    1 
ATOM   1239  C  CD1   . LEU A 1 1604 ? 167.511 209.777 140.949 1.00 177.97 ? 1604 LEU A CD1   1 
ATOM   1240  C  CD2   . LEU A 1 1604 ? 168.004 207.974 139.286 1.00 178.10 ? 1604 LEU A CD2   1 
ATOM   1241  N  N     . ALA A 1 1605 ? 167.126 204.992 143.693 1.00 172.09 ? 1605 ALA A N     1 
ATOM   1242  C  CA    . ALA A 1 1605 ? 167.669 204.100 144.712 1.00 170.66 ? 1605 ALA A CA    1 
ATOM   1243  C  C     . ALA A 1 1605 ? 167.496 202.640 144.314 1.00 171.28 ? 1605 ALA A C     1 
ATOM   1244  O  O     . ALA A 1 1605 ? 168.414 201.830 144.484 1.00 171.08 ? 1605 ALA A O     1 
ATOM   1245  C  CB    . ALA A 1 1605 ? 166.997 204.366 146.058 1.00 170.86 ? 1605 ALA A CB    1 
ATOM   1246  N  N     . ASP A 1 1606 ? 166.323 202.289 143.784 1.00 176.40 ? 1606 ASP A N     1 
ATOM   1247  C  CA    . ASP A 1 1606 ? 166.067 200.909 143.381 1.00 175.77 ? 1606 ASP A CA    1 
ATOM   1248  C  C     . ASP A 1 1606 ? 167.038 200.484 142.283 1.00 176.94 ? 1606 ASP A C     1 
ATOM   1249  O  O     . ASP A 1 1606 ? 167.639 199.404 142.350 1.00 177.84 ? 1606 ASP A O     1 
ATOM   1250  C  CB    . ASP A 1 1606 ? 164.604 200.783 142.930 1.00 176.24 ? 1606 ASP A CB    1 
ATOM   1251  C  CG    . ASP A 1 1606 ? 164.355 199.629 141.958 1.00 176.30 ? 1606 ASP A CG    1 
ATOM   1252  O  OD1   . ASP A 1 1606 ? 165.078 198.611 141.982 1.00 176.32 ? 1606 ASP A OD1   1 
ATOM   1253  O  OD2   . ASP A 1 1606 ? 163.412 199.750 141.148 1.00 176.66 ? 1606 ASP A OD2   1 
ATOM   1254  N  N     . LEU A 1 1607 ? 167.217 201.333 141.269 1.00 176.04 ? 1607 LEU A N     1 
ATOM   1255  C  CA    . LEU A 1 1607 ? 168.110 200.991 140.167 1.00 175.39 ? 1607 LEU A CA    1 
ATOM   1256  C  C     . LEU A 1 1607 ? 169.562 200.910 140.627 1.00 175.06 ? 1607 LEU A C     1 
ATOM   1257  O  O     . LEU A 1 1607 ? 170.303 200.014 140.203 1.00 174.41 ? 1607 LEU A O     1 
ATOM   1258  C  CB    . LEU A 1 1607 ? 167.953 202.007 139.036 1.00 175.39 ? 1607 LEU A CB    1 
ATOM   1259  C  CG    . LEU A 1 1607 ? 166.603 201.996 138.315 1.00 175.65 ? 1607 LEU A CG    1 
ATOM   1260  C  CD1   . LEU A 1 1607 ? 166.662 202.818 137.038 1.00 176.12 ? 1607 LEU A CD1   1 
ATOM   1261  C  CD2   . LEU A 1 1607 ? 166.166 200.570 138.014 1.00 174.96 ? 1607 LEU A CD2   1 
ATOM   1262  N  N     . LEU A 1 1608 ? 169.988 201.833 141.495 1.00 171.32 ? 1608 LEU A N     1 
ATOM   1263  C  CA    . LEU A 1 1608 ? 171.354 201.788 142.005 1.00 170.70 ? 1608 LEU A CA    1 
ATOM   1264  C  C     . LEU A 1 1608 ? 171.588 200.535 142.838 1.00 170.02 ? 1608 LEU A C     1 
ATOM   1265  O  O     . LEU A 1 1608 ? 172.668 199.934 142.780 1.00 169.49 ? 1608 LEU A O     1 
ATOM   1266  C  CB    . LEU A 1 1608 ? 171.650 203.045 142.822 1.00 170.65 ? 1608 LEU A CB    1 
ATOM   1267  C  CG    . LEU A 1 1608 ? 171.864 204.332 142.021 1.00 169.59 ? 1608 LEU A CG    1 
ATOM   1268  C  CD1   . LEU A 1 1608 ? 172.170 205.501 142.944 1.00 168.87 ? 1608 LEU A CD1   1 
ATOM   1269  C  CD2   . LEU A 1 1608 ? 172.970 204.153 140.993 1.00 169.90 ? 1608 LEU A CD2   1 
ATOM   1270  N  N     . GLY A 1 1609 ? 170.590 200.127 143.624 1.00 169.31 ? 1609 GLY A N     1 
ATOM   1271  C  CA    . GLY A 1 1609 ? 170.708 198.881 144.363 1.00 168.98 ? 1609 GLY A CA    1 
ATOM   1272  C  C     . GLY A 1 1609 ? 170.782 197.672 143.453 1.00 168.72 ? 1609 GLY A C     1 
ATOM   1273  O  O     . GLY A 1 1609 ? 171.537 196.732 143.713 1.00 168.45 ? 1609 GLY A O     1 
ATOM   1274  N  N     . LYS A 1 1610 ? 169.994 197.675 142.375 1.00 165.22 ? 1610 LYS A N     1 
ATOM   1275  C  CA    . LYS A 1 1610 ? 170.065 196.578 141.413 1.00 164.88 ? 1610 LYS A CA    1 
ATOM   1276  C  C     . LYS A 1 1610 ? 171.440 196.504 140.762 1.00 166.86 ? 1610 LYS A C     1 
ATOM   1277  O  O     . LYS A 1 1610 ? 171.978 195.410 140.556 1.00 166.36 ? 1610 LYS A O     1 
ATOM   1278  C  CB    . LYS A 1 1610 ? 168.975 196.726 140.351 1.00 165.03 ? 1610 LYS A CB    1 
ATOM   1279  C  CG    . LYS A 1 1610 ? 167.714 195.926 140.641 1.00 166.97 ? 1610 LYS A CG    1 
ATOM   1280  C  CD    . LYS A 1 1610 ? 166.704 196.053 139.512 1.00 166.89 ? 1610 LYS A CD    1 
ATOM   1281  C  CE    . LYS A 1 1610 ? 165.282 196.119 140.041 1.00 165.47 ? 1610 LYS A CE    1 
ATOM   1282  N  NZ    . LYS A 1 1610 ? 164.276 196.048 138.946 1.00 165.41 ? 1610 LYS A NZ    1 
ATOM   1283  N  N     . ILE A 1 1611 ? 172.021 197.655 140.420 1.00 169.93 ? 1611 ILE A N     1 
ATOM   1284  C  CA    . ILE A 1 1611 ? 173.370 197.660 139.857 1.00 167.99 ? 1611 ILE A CA    1 
ATOM   1285  C  C     . ILE A 1 1611 ? 174.385 197.186 140.889 1.00 168.41 ? 1611 ILE A C     1 
ATOM   1286  O  O     . ILE A 1 1611 ? 175.296 196.410 140.575 1.00 167.31 ? 1611 ILE A O     1 
ATOM   1287  C  CB    . ILE A 1 1611 ? 173.724 199.056 139.316 1.00 166.20 ? 1611 ILE A CB    1 
ATOM   1288  C  CG1   . ILE A 1 1611 ? 172.781 199.436 138.179 1.00 166.97 ? 1611 ILE A CG1   1 
ATOM   1289  C  CG2   . ILE A 1 1611 ? 175.168 199.096 138.844 1.00 166.84 ? 1611 ILE A CG2   1 
ATOM   1290  C  CD1   . ILE A 1 1611 ? 173.101 200.764 137.569 1.00 167.08 ? 1611 ILE A CD1   1 
ATOM   1291  N  N     . GLN A 1 1612 ? 174.248 197.648 142.135 1.00 168.60 ? 1612 GLN A N     1 
ATOM   1292  C  CA    . GLN A 1 1612 ? 175.204 197.276 143.174 1.00 167.23 ? 1612 GLN A CA    1 
ATOM   1293  C  C     . GLN A 1 1612 ? 175.206 195.772 143.416 1.00 166.75 ? 1612 GLN A C     1 
ATOM   1294  O  O     . GLN A 1 1612 ? 176.270 195.162 143.576 1.00 164.56 ? 1612 GLN A O     1 
ATOM   1295  C  CB    . GLN A 1 1612 ? 174.891 198.028 144.469 1.00 165.31 ? 1612 GLN A CB    1 
ATOM   1296  C  CG    . GLN A 1 1612 ? 175.373 197.324 145.727 1.00 164.54 ? 1612 GLN A CG    1 
ATOM   1297  C  CD    . GLN A 1 1612 ? 175.060 198.098 146.991 1.00 165.67 ? 1612 GLN A CD    1 
ATOM   1298  O  OE1   . GLN A 1 1612 ? 174.712 199.277 146.941 1.00 165.98 ? 1612 GLN A OE1   1 
ATOM   1299  N  NE2   . GLN A 1 1612 ? 175.184 197.437 148.136 1.00 166.49 ? 1612 GLN A NE2   1 
ATOM   1300  N  N     . LYS A 1 1613 ? 174.024 195.153 143.434 1.00 167.12 ? 1613 LYS A N     1 
ATOM   1301  C  CA    . LYS A 1 1613 ? 173.932 193.725 143.715 1.00 166.32 ? 1613 LYS A CA    1 
ATOM   1302  C  C     . LYS A 1 1613 ? 174.482 192.865 142.583 1.00 167.05 ? 1613 LYS A C     1 
ATOM   1303  O  O     . LYS A 1 1613 ? 174.653 191.656 142.772 1.00 167.06 ? 1613 LYS A O     1 
ATOM   1304  C  CB    . LYS A 1 1613 ? 172.479 193.341 144.003 1.00 164.80 ? 1613 LYS A CB    1 
ATOM   1305  C  CG    . LYS A 1 1613 ? 171.649 193.065 142.760 1.00 166.75 ? 1613 LYS A CG    1 
ATOM   1306  C  CD    . LYS A 1 1613 ? 170.279 192.512 143.118 1.00 167.00 ? 1613 LYS A CD    1 
ATOM   1307  C  CE    . LYS A 1 1613 ? 169.769 191.568 142.041 1.00 166.03 ? 1613 LYS A CE    1 
ATOM   1308  N  NZ    . LYS A 1 1613 ? 168.285 191.445 142.063 1.00 164.19 ? 1613 LYS A NZ    1 
ATOM   1309  N  N     . ALA A 1 1614 ? 174.761 193.452 141.418 1.00 160.33 ? 1614 ALA A N     1 
ATOM   1310  C  CA    . ALA A 1 1614 ? 175.249 192.711 140.261 1.00 159.58 ? 1614 ALA A CA    1 
ATOM   1311  C  C     . ALA A 1 1614 ? 176.725 192.974 139.976 1.00 159.76 ? 1614 ALA A C     1 
ATOM   1312  O  O     . ALA A 1 1614 ? 177.158 192.886 138.822 1.00 159.16 ? 1614 ALA A O     1 
ATOM   1313  C  CB    . ALA A 1 1614 ? 174.404 193.039 139.031 1.00 159.33 ? 1614 ALA A CB    1 
ATOM   1314  N  N     . LEU A 1 1615 ? 177.511 193.293 141.006 1.00 162.86 ? 1615 LEU A N     1 
ATOM   1315  C  CA    . LEU A 1 1615 ? 178.933 193.581 140.850 1.00 162.75 ? 1615 LEU A CA    1 
ATOM   1316  C  C     . LEU A 1 1615 ? 179.792 192.574 141.608 1.00 163.01 ? 1615 LEU A C     1 
ATOM   1317  O  O     . LEU A 1 1615 ? 180.949 192.856 141.929 1.00 164.38 ? 1615 LEU A O     1 
ATOM   1318  C  CB    . LEU A 1 1615 ? 179.255 195.004 141.311 1.00 162.71 ? 1615 LEU A CB    1 
ATOM   1319  C  CG    . LEU A 1 1615 ? 178.621 196.177 140.560 1.00 162.03 ? 1615 LEU A CG    1 
ATOM   1320  C  CD1   . LEU A 1 1615 ? 179.456 197.434 140.745 1.00 160.97 ? 1615 LEU A CD1   1 
ATOM   1321  C  CD2   . LEU A 1 1615 ? 178.464 195.861 139.082 1.00 162.89 ? 1615 LEU A CD2   1 
ATOM   1322  N  N     . GLY A 1 1616 ? 179.238 191.397 141.905 1.00 153.30 ? 1616 GLY A N     1 
ATOM   1323  C  CA    . GLY A 1 1616 ? 179.958 190.436 142.728 1.00 153.26 ? 1616 GLY A CA    1 
ATOM   1324  C  C     . GLY A 1 1616 ? 181.209 189.888 142.066 1.00 152.36 ? 1616 GLY A C     1 
ATOM   1325  O  O     . GLY A 1 1616 ? 182.251 189.748 142.713 1.00 153.31 ? 1616 GLY A O     1 
ATOM   1326  N  N     . GLU A 1 1617 ? 181.123 189.557 140.775 1.00 147.32 ? 1617 GLU A N     1 
ATOM   1327  C  CA    . GLU A 1 1617 ? 182.271 188.987 140.074 1.00 148.40 ? 1617 GLU A CA    1 
ATOM   1328  C  C     . GLU A 1 1617 ? 183.429 189.976 140.012 1.00 148.86 ? 1617 GLU A C     1 
ATOM   1329  O  O     . GLU A 1 1617 ? 184.595 189.597 140.195 1.00 148.39 ? 1617 GLU A O     1 
ATOM   1330  C  CB    . GLU A 1 1617 ? 181.872 188.545 138.662 1.00 148.81 ? 1617 GLU A CB    1 
ATOM   1331  C  CG    . GLU A 1 1617 ? 180.820 187.432 138.566 1.00 147.36 ? 1617 GLU A CG    1 
ATOM   1332  C  CD    . GLU A 1 1617 ? 179.499 187.775 139.228 1.00 147.91 ? 1617 GLU A CD    1 
ATOM   1333  O  OE1   . GLU A 1 1617 ? 179.089 187.044 140.154 1.00 147.95 ? 1617 GLU A OE1   1 
ATOM   1334  O  OE2   . GLU A 1 1617 ? 178.873 188.776 138.823 1.00 148.64 ? 1617 GLU A OE2   1 
ATOM   1335  N  N     . TYR A 1 1618 ? 183.124 191.249 139.748 1.00 149.63 ? 1618 TYR A N     1 
ATOM   1336  C  CA    . TYR A 1 1618 ? 184.162 192.271 139.728 1.00 150.23 ? 1618 TYR A CA    1 
ATOM   1337  C  C     . TYR A 1 1618 ? 184.821 192.394 141.094 1.00 149.91 ? 1618 TYR A C     1 
ATOM   1338  O  O     . TYR A 1 1618 ? 186.038 192.584 141.193 1.00 147.33 ? 1618 TYR A O     1 
ATOM   1339  C  CB    . TYR A 1 1618 ? 183.568 193.608 139.285 1.00 148.94 ? 1618 TYR A CB    1 
ATOM   1340  C  CG    . TYR A 1 1618 ? 184.543 194.761 139.311 1.00 149.31 ? 1618 TYR A CG    1 
ATOM   1341  C  CD1   . TYR A 1 1618 ? 185.610 194.810 138.425 1.00 148.96 ? 1618 TYR A CD1   1 
ATOM   1342  C  CD2   . TYR A 1 1618 ? 184.388 195.810 140.208 1.00 149.24 ? 1618 TYR A CD2   1 
ATOM   1343  C  CE1   . TYR A 1 1618 ? 186.503 195.862 138.439 1.00 149.82 ? 1618 TYR A CE1   1 
ATOM   1344  C  CE2   . TYR A 1 1618 ? 185.277 196.869 140.229 1.00 149.45 ? 1618 TYR A CE2   1 
ATOM   1345  C  CZ    . TYR A 1 1618 ? 186.332 196.889 139.341 1.00 150.24 ? 1618 TYR A CZ    1 
ATOM   1346  O  OH    . TYR A 1 1618 ? 187.221 197.938 139.355 1.00 150.11 ? 1618 TYR A OH    1 
ATOM   1347  N  N     . LEU A 1 1619 ? 184.030 192.269 142.162 1.00 138.67 ? 1619 LEU A N     1 
ATOM   1348  C  CA    . LEU A 1 1619 ? 184.596 192.292 143.504 1.00 136.18 ? 1619 LEU A CA    1 
ATOM   1349  C  C     . LEU A 1 1619 ? 185.480 191.083 143.760 1.00 137.73 ? 1619 LEU A C     1 
ATOM   1350  O  O     . LEU A 1 1619 ? 186.493 191.187 144.456 1.00 140.17 ? 1619 LEU A O     1 
ATOM   1351  C  CB    . LEU A 1 1619 ? 183.490 192.354 144.549 1.00 137.06 ? 1619 LEU A CB    1 
ATOM   1352  C  CG    . LEU A 1 1619 ? 182.861 193.719 144.771 1.00 136.51 ? 1619 LEU A CG    1 
ATOM   1353  C  CD1   . LEU A 1 1619 ? 182.208 193.708 146.133 1.00 138.77 ? 1619 LEU A CD1   1 
ATOM   1354  C  CD2   . LEU A 1 1619 ? 183.913 194.810 144.661 1.00 134.32 ? 1619 LEU A CD2   1 
ATOM   1355  N  N     . GLU A 1 1620 ? 185.101 189.919 143.233 1.00 137.47 ? 1620 GLU A N     1 
ATOM   1356  C  CA    . GLU A 1 1620 ? 185.939 188.740 143.417 1.00 138.36 ? 1620 GLU A CA    1 
ATOM   1357  C  C     . GLU A 1 1620 ? 187.281 188.920 142.715 1.00 137.77 ? 1620 GLU A C     1 
ATOM   1358  O  O     . GLU A 1 1620 ? 188.335 188.580 143.269 1.00 138.54 ? 1620 GLU A O     1 
ATOM   1359  C  CB    . GLU A 1 1620 ? 185.214 187.498 142.903 1.00 136.73 ? 1620 GLU A CB    1 
ATOM   1360  C  CG    . GLU A 1 1620 ? 184.335 186.831 143.951 1.00 136.97 ? 1620 GLU A CG    1 
ATOM   1361  C  CD    . GLU A 1 1620 ? 185.119 186.294 145.128 1.00 137.83 ? 1620 GLU A CD    1 
ATOM   1362  O  OE1   . GLU A 1 1620 ? 186.105 185.562 144.904 1.00 137.50 ? 1620 GLU A OE1   1 
ATOM   1363  O  OE2   . GLU A 1 1620 ? 184.747 186.603 146.280 1.00 136.80 ? 1620 GLU A OE2   1 
ATOM   1364  N  N     . ARG A 1 1621 ? 187.261 189.478 141.502 1.00 134.39 ? 1621 ARG A N     1 
ATOM   1365  C  CA    . ARG A 1 1621 ? 188.516 189.767 140.809 1.00 134.68 ? 1621 ARG A CA    1 
ATOM   1366  C  C     . ARG A 1 1621 ? 189.339 190.817 141.551 1.00 133.67 ? 1621 ARG A C     1 
ATOM   1367  O  O     . ARG A 1 1621 ? 190.569 190.705 141.633 1.00 132.91 ? 1621 ARG A O     1 
ATOM   1368  C  CB    . ARG A 1 1621 ? 188.241 190.206 139.371 1.00 136.31 ? 1621 ARG A CB    1 
ATOM   1369  C  CG    . ARG A 1 1621 ? 187.464 189.180 138.571 1.00 135.96 ? 1621 ARG A CG    1 
ATOM   1370  C  CD    . ARG A 1 1621 ? 186.432 189.821 137.659 1.00 136.50 ? 1621 ARG A CD    1 
ATOM   1371  N  NE    . ARG A 1 1621 ? 185.831 188.867 136.730 1.00 138.50 ? 1621 ARG A NE    1 
ATOM   1372  C  CZ    . ARG A 1 1621 ? 185.134 187.793 137.082 1.00 136.91 ? 1621 ARG A CZ    1 
ATOM   1373  N  NH1   . ARG A 1 1621 ? 184.909 187.494 138.351 1.00 138.19 ? 1621 ARG A NH1   1 
ATOM   1374  N  NH2   . ARG A 1 1621 ? 184.642 187.002 136.133 1.00 134.86 ? 1621 ARG A NH2   1 
ATOM   1375  N  N     . GLU A 1 1622 ? 188.684 191.844 142.097 1.00 129.94 ? 1622 GLU A N     1 
ATOM   1376  C  CA    . GLU A 1 1622 ? 189.406 192.852 142.870 1.00 131.60 ? 1622 GLU A CA    1 
ATOM   1377  C  C     . GLU A 1 1622 ? 190.041 192.246 144.117 1.00 131.75 ? 1622 GLU A C     1 
ATOM   1378  O  O     . GLU A 1 1622 ? 191.181 192.577 144.463 1.00 132.31 ? 1622 GLU A O     1 
ATOM   1379  C  CB    . GLU A 1 1622 ? 188.468 193.998 143.246 1.00 132.75 ? 1622 GLU A CB    1 
ATOM   1380  C  CG    . GLU A 1 1622 ? 188.109 194.917 142.089 1.00 132.47 ? 1622 GLU A CG    1 
ATOM   1381  C  CD    . GLU A 1 1622 ? 189.133 196.014 141.875 1.00 134.83 ? 1622 GLU A CD    1 
ATOM   1382  O  OE1   . GLU A 1 1622 ? 190.024 196.174 142.735 1.00 135.37 ? 1622 GLU A OE1   1 
ATOM   1383  O  OE2   . GLU A 1 1622 ? 189.044 196.719 140.848 1.00 135.05 ? 1622 GLU A OE2   1 
ATOM   1384  N  N     . ARG A 1 1623 ? 189.315 191.362 144.805 1.00 115.36 ? 1623 ARG A N     1 
ATOM   1385  C  CA    . ARG A 1 1623 ? 189.876 190.664 145.957 1.00 111.10 ? 1623 ARG A CA    1 
ATOM   1386  C  C     . ARG A 1 1623 ? 191.068 189.814 145.547 1.00 111.70 ? 1623 ARG A C     1 
ATOM   1387  O  O     . ARG A 1 1623 ? 192.063 189.730 146.276 1.00 113.17 ? 1623 ARG A O     1 
ATOM   1388  C  CB    . ARG A 1 1623 ? 188.807 189.794 146.617 1.00 112.10 ? 1623 ARG A CB    1 
ATOM   1389  C  CG    . ARG A 1 1623 ? 187.691 190.560 147.300 1.00 108.54 ? 1623 ARG A CG    1 
ATOM   1390  C  CD    . ARG A 1 1623 ? 186.470 189.672 147.469 1.00 108.66 ? 1623 ARG A CD    1 
ATOM   1391  N  NE    . ARG A 1 1623 ? 185.235 190.436 147.606 1.00 111.26 ? 1623 ARG A NE    1 
ATOM   1392  C  CZ    . ARG A 1 1623 ? 184.821 191.003 148.730 1.00 111.95 ? 1623 ARG A CZ    1 
ATOM   1393  N  NH1   . ARG A 1 1623 ? 185.518 190.907 149.850 1.00 111.98 ? 1623 ARG A NH1   1 
ATOM   1394  N  NH2   . ARG A 1 1623 ? 183.677 191.680 148.731 1.00 110.15 ? 1623 ARG A NH2   1 
ATOM   1395  N  N     . SER A 1 1624 ? 190.978 189.159 144.388 1.00 116.24 ? 1624 SER A N     1 
ATOM   1396  C  CA    . SER A 1 1624 ? 192.124 188.414 143.879 1.00 117.49 ? 1624 SER A CA    1 
ATOM   1397  C  C     . SER A 1 1624 ? 193.305 189.334 143.596 1.00 117.58 ? 1624 SER A C     1 
ATOM   1398  O  O     . SER A 1 1624 ? 194.461 188.926 143.758 1.00 112.41 ? 1624 SER A O     1 
ATOM   1399  C  CB    . SER A 1 1624 ? 191.733 187.644 142.618 1.00 117.81 ? 1624 SER A CB    1 
ATOM   1400  O  OG    . SER A 1 1624 ? 190.722 186.690 142.895 1.00 115.21 ? 1624 SER A OG    1 
ATOM   1401  N  N     . SER A 1 1625 ? 193.038 190.571 143.171 1.00 120.26 ? 1625 SER A N     1 
ATOM   1402  C  CA    . SER A 1 1625 ? 194.122 191.510 142.890 1.00 118.98 ? 1625 SER A CA    1 
ATOM   1403  C  C     . SER A 1 1625 ? 194.867 191.896 144.163 1.00 116.34 ? 1625 SER A C     1 
ATOM   1404  O  O     . SER A 1 1625 ? 196.101 191.826 144.217 1.00 113.31 ? 1625 SER A O     1 
ATOM   1405  C  CB    . SER A 1 1625 ? 193.570 192.752 142.191 1.00 118.97 ? 1625 SER A CB    1 
ATOM   1406  O  OG    . SER A 1 1625 ? 192.755 193.510 143.067 1.00 121.10 ? 1625 SER A OG    1 
ATOM   1407  N  N     . PHE A 1 1626 ? 194.140 192.312 145.193 1.00 117.16 ? 1626 PHE A N     1 
ATOM   1408  C  CA    . PHE A 1 1626 ? 194.733 192.640 146.491 1.00 116.99 ? 1626 PHE A CA    1 
ATOM   1409  C  C     . PHE A 1 1626 ? 194.213 191.665 147.534 1.00 119.56 ? 1626 PHE A C     1 
ATOM   1410  O  O     . PHE A 1 1626 ? 193.020 191.722 147.890 1.00 117.39 ? 1626 PHE A O     1 
ATOM   1411  C  CB    . PHE A 1 1626 ? 194.418 194.079 146.897 1.00 115.70 ? 1626 PHE A CB    1 
ATOM   1412  C  CG    . PHE A 1 1626 ? 195.179 194.546 148.106 1.00 115.52 ? 1626 PHE A CG    1 
ATOM   1413  C  CD1   . PHE A 1 1626 ? 196.560 194.469 148.143 1.00 114.39 ? 1626 PHE A CD1   1 
ATOM   1414  C  CD2   . PHE A 1 1626 ? 194.514 195.067 149.202 1.00 115.80 ? 1626 PHE A CD2   1 
ATOM   1415  C  CE1   . PHE A 1 1626 ? 197.264 194.897 149.252 1.00 112.62 ? 1626 PHE A CE1   1 
ATOM   1416  C  CE2   . PHE A 1 1626 ? 195.213 195.498 150.314 1.00 115.68 ? 1626 PHE A CE2   1 
ATOM   1417  C  CZ    . PHE A 1 1626 ? 196.590 195.412 150.338 1.00 112.96 ? 1626 PHE A CZ    1 
ATOM   1418  N  N     . PRO A 1 1627 ? 195.057 190.774 148.059 1.00 107.68 ? 1627 PRO A N     1 
ATOM   1419  C  CA    . PRO A 1 1627 ? 194.546 189.680 148.903 1.00 104.54 ? 1627 PRO A CA    1 
ATOM   1420  C  C     . PRO A 1 1627 ? 193.792 190.141 150.137 1.00 102.93 ? 1627 PRO A C     1 
ATOM   1421  O  O     . PRO A 1 1627 ? 192.831 189.476 150.543 1.00 103.84 ? 1627 PRO A O     1 
ATOM   1422  C  CB    . PRO A 1 1627 ? 195.820 188.910 149.279 1.00 100.53 ? 1627 PRO A CB    1 
ATOM   1423  C  CG    . PRO A 1 1627 ? 196.935 189.885 149.087 1.00 96.65  ? 1627 PRO A CG    1 
ATOM   1424  C  CD    . PRO A 1 1627 ? 196.524 190.746 147.938 1.00 100.14 ? 1627 PRO A CD    1 
ATOM   1425  N  N     . ARG A 1 1628 ? 194.189 191.259 150.748 1.00 94.15  ? 1628 ARG A N     1 
ATOM   1426  C  CA    . ARG A 1 1628 ? 193.563 191.678 151.997 1.00 97.15  ? 1628 ARG A CA    1 
ATOM   1427  C  C     . ARG A 1 1628 ? 192.118 192.120 151.811 1.00 99.00  ? 1628 ARG A C     1 
ATOM   1428  O  O     . ARG A 1 1628 ? 191.404 192.292 152.805 1.00 99.74  ? 1628 ARG A O     1 
ATOM   1429  C  CB    . ARG A 1 1628 ? 194.377 192.798 152.643 1.00 98.70  ? 1628 ARG A CB    1 
ATOM   1430  C  CG    . ARG A 1 1628 ? 195.463 192.303 153.581 1.00 98.93  ? 1628 ARG A CG    1 
ATOM   1431  C  CD    . ARG A 1 1628 ? 196.685 193.201 153.544 1.00 98.22  ? 1628 ARG A CD    1 
ATOM   1432  N  NE    . ARG A 1 1628 ? 197.827 192.590 154.213 1.00 95.52  ? 1628 ARG A NE    1 
ATOM   1433  C  CZ    . ARG A 1 1628 ? 198.133 192.775 155.489 1.00 95.60  ? 1628 ARG A CZ    1 
ATOM   1434  N  NH1   . ARG A 1 1628 ? 197.391 193.537 156.275 1.00 97.27  ? 1628 ARG A NH1   1 
ATOM   1435  N  NH2   . ARG A 1 1628 ? 199.210 192.177 155.991 1.00 95.82  ? 1628 ARG A NH2   1 
ATOM   1436  N  N     . PHE A 1 1629 ? 191.667 192.310 150.570 1.00 108.19 ? 1629 PHE A N     1 
ATOM   1437  C  CA    . PHE A 1 1629 ? 190.275 192.676 150.337 1.00 112.60 ? 1629 PHE A CA    1 
ATOM   1438  C  C     . PHE A 1 1629 ? 189.317 191.531 150.635 1.00 112.41 ? 1629 PHE A C     1 
ATOM   1439  O  O     . PHE A 1 1629 ? 188.102 191.754 150.692 1.00 113.64 ? 1629 PHE A O     1 
ATOM   1440  C  CB    . PHE A 1 1629 ? 190.087 193.150 148.896 1.00 112.20 ? 1629 PHE A CB    1 
ATOM   1441  C  CG    . PHE A 1 1629 ? 190.527 194.566 148.663 1.00 113.35 ? 1629 PHE A CG    1 
ATOM   1442  C  CD1   . PHE A 1 1629 ? 190.458 195.501 149.681 1.00 112.90 ? 1629 PHE A CD1   1 
ATOM   1443  C  CD2   . PHE A 1 1629 ? 191.002 194.964 147.425 1.00 110.75 ? 1629 PHE A CD2   1 
ATOM   1444  C  CE1   . PHE A 1 1629 ? 190.859 196.805 149.471 1.00 112.95 ? 1629 PHE A CE1   1 
ATOM   1445  C  CE2   . PHE A 1 1629 ? 191.404 196.266 147.209 1.00 109.63 ? 1629 PHE A CE2   1 
ATOM   1446  C  CZ    . PHE A 1 1629 ? 191.333 197.187 148.233 1.00 113.69 ? 1629 PHE A CZ    1 
ATOM   1447  N  N     . TYR A 1 1630 ? 189.830 190.312 150.822 1.00 96.53  ? 1630 TYR A N     1 
ATOM   1448  C  CA    . TYR A 1 1630 ? 188.969 189.169 151.101 1.00 95.59  ? 1630 TYR A CA    1 
ATOM   1449  C  C     . TYR A 1 1630 ? 188.214 189.317 152.415 1.00 98.59  ? 1630 TYR A C     1 
ATOM   1450  O  O     . TYR A 1 1630 ? 187.134 188.735 152.565 1.00 101.76 ? 1630 TYR A O     1 
ATOM   1451  C  CB    . TYR A 1 1630 ? 189.795 187.883 151.125 1.00 94.52  ? 1630 TYR A CB    1 
ATOM   1452  C  CG    . TYR A 1 1630 ? 189.899 187.195 149.786 1.00 92.77  ? 1630 TYR A CG    1 
ATOM   1453  C  CD1   . TYR A 1 1630 ? 188.847 186.436 149.291 1.00 93.43  ? 1630 TYR A CD1   1 
ATOM   1454  C  CD2   . TYR A 1 1630 ? 191.047 187.304 149.015 1.00 93.17  ? 1630 TYR A CD2   1 
ATOM   1455  C  CE1   . TYR A 1 1630 ? 188.937 185.804 148.067 1.00 95.46  ? 1630 TYR A CE1   1 
ATOM   1456  C  CE2   . TYR A 1 1630 ? 191.145 186.677 147.790 1.00 97.37  ? 1630 TYR A CE2   1 
ATOM   1457  C  CZ    . TYR A 1 1630 ? 190.088 185.928 147.321 1.00 99.20  ? 1630 TYR A CZ    1 
ATOM   1458  O  OH    . TYR A 1 1630 ? 190.183 185.301 146.101 1.00 99.03  ? 1630 TYR A OH    1 
ATOM   1459  N  N     . PHE A 1 1631 ? 188.751 190.079 153.364 1.00 90.68  ? 1631 PHE A N     1 
ATOM   1460  C  CA    . PHE A 1 1631 ? 188.115 190.285 154.658 1.00 89.77  ? 1631 PHE A CA    1 
ATOM   1461  C  C     . PHE A 1 1631 ? 187.232 191.524 154.676 1.00 94.27  ? 1631 PHE A C     1 
ATOM   1462  O  O     . PHE A 1 1631 ? 186.948 192.058 155.752 1.00 96.25  ? 1631 PHE A O     1 
ATOM   1463  C  CB    . PHE A 1 1631 ? 189.176 190.379 155.756 1.00 87.40  ? 1631 PHE A CB    1 
ATOM   1464  C  CG    . PHE A 1 1631 ? 190.296 189.390 155.599 1.00 90.60  ? 1631 PHE A CG    1 
ATOM   1465  C  CD1   . PHE A 1 1631 ? 190.032 188.059 155.320 1.00 89.04  ? 1631 PHE A CD1   1 
ATOM   1466  C  CD2   . PHE A 1 1631 ? 191.614 189.795 155.720 1.00 92.26  ? 1631 PHE A CD2   1 
ATOM   1467  C  CE1   . PHE A 1 1631 ? 191.060 187.151 155.170 1.00 89.42  ? 1631 PHE A CE1   1 
ATOM   1468  C  CE2   . PHE A 1 1631 ? 192.647 188.891 155.572 1.00 94.09  ? 1631 PHE A CE2   1 
ATOM   1469  C  CZ    . PHE A 1 1631 ? 192.370 187.568 155.296 1.00 95.22  ? 1631 PHE A CZ    1 
ATOM   1470  N  N     . VAL A 1 1632 ? 186.794 191.989 153.509 1.00 102.77 ? 1632 VAL A N     1 
ATOM   1471  C  CA    . VAL A 1 1632 ? 185.987 193.194 153.375 1.00 100.44 ? 1632 VAL A CA    1 
ATOM   1472  C  C     . VAL A 1 1632 ? 184.692 192.820 152.669 1.00 99.96  ? 1632 VAL A C     1 
ATOM   1473  O  O     . VAL A 1 1632 ? 184.716 192.125 151.647 1.00 101.24 ? 1632 VAL A O     1 
ATOM   1474  C  CB    . VAL A 1 1632 ? 186.740 194.292 152.603 1.00 99.68  ? 1632 VAL A CB    1 
ATOM   1475  C  CG1   . VAL A 1 1632 ? 185.848 195.494 152.376 1.00 103.77 ? 1632 VAL A CG1   1 
ATOM   1476  C  CG2   . VAL A 1 1632 ? 187.998 194.698 153.354 1.00 100.16 ? 1632 VAL A CG2   1 
ATOM   1477  N  N     . GLY A 1 1633 ? 183.568 193.276 153.213 1.00 114.07 ? 1633 GLY A N     1 
ATOM   1478  C  CA    . GLY A 1 1633 ? 182.279 192.964 152.634 1.00 115.29 ? 1633 GLY A CA    1 
ATOM   1479  C  C     . GLY A 1 1633 ? 182.060 193.653 151.300 1.00 119.50 ? 1633 GLY A C     1 
ATOM   1480  O  O     . GLY A 1 1633 ? 182.825 194.515 150.867 1.00 122.14 ? 1633 GLY A O     1 
ATOM   1481  N  N     . ASP A 1 1634 ? 180.977 193.246 150.632 1.00 130.16 ? 1634 ASP A N     1 
ATOM   1482  C  CA    . ASP A 1 1634 ? 180.659 193.799 149.318 1.00 127.90 ? 1634 ASP A CA    1 
ATOM   1483  C  C     . ASP A 1 1634 ? 180.423 195.301 149.386 1.00 128.00 ? 1634 ASP A C     1 
ATOM   1484  O  O     . ASP A 1 1634 ? 180.984 196.063 148.588 1.00 132.00 ? 1634 ASP A O     1 
ATOM   1485  C  CB    . ASP A 1 1634 ? 179.435 193.092 148.738 1.00 129.87 ? 1634 ASP A CB    1 
ATOM   1486  C  CG    . ASP A 1 1634 ? 178.706 193.935 147.707 1.00 131.38 ? 1634 ASP A CG    1 
ATOM   1487  O  OD1   . ASP A 1 1634 ? 179.143 193.968 146.539 1.00 133.03 ? 1634 ASP A OD1   1 
ATOM   1488  O  OD2   . ASP A 1 1634 ? 177.692 194.567 148.067 1.00 129.73 ? 1634 ASP A OD2   1 
ATOM   1489  N  N     . GLU A 1 1635 ? 179.594 195.745 150.334 1.00 128.14 ? 1635 GLU A N     1 
ATOM   1490  C  CA    . GLU A 1 1635 ? 179.313 197.170 150.478 1.00 127.11 ? 1635 GLU A CA    1 
ATOM   1491  C  C     . GLU A 1 1635 ? 180.592 197.952 150.742 1.00 130.88 ? 1635 GLU A C     1 
ATOM   1492  O  O     . GLU A 1 1635 ? 180.874 198.955 150.075 1.00 131.46 ? 1635 GLU A O     1 
ATOM   1493  C  CB    . GLU A 1 1635 ? 178.307 197.384 151.611 1.00 129.08 ? 1635 GLU A CB    1 
ATOM   1494  C  CG    . GLU A 1 1635 ? 176.943 197.889 151.170 1.00 133.20 ? 1635 GLU A CG    1 
ATOM   1495  C  CD    . GLU A 1 1635 ? 175.950 197.953 152.318 1.00 134.38 ? 1635 GLU A CD    1 
ATOM   1496  O  OE1   . GLU A 1 1635 ? 174.730 197.906 152.056 1.00 134.87 ? 1635 GLU A OE1   1 
ATOM   1497  O  OE2   . GLU A 1 1635 ? 176.390 198.043 153.484 1.00 132.61 ? 1635 GLU A OE2   1 
ATOM   1498  N  N     . ASP A 1 1636 ? 181.399 197.483 151.695 1.00 132.54 ? 1636 ASP A N     1 
ATOM   1499  C  CA    . ASP A 1 1636 ? 182.626 198.186 152.042 1.00 130.27 ? 1636 ASP A CA    1 
ATOM   1500  C  C     . ASP A 1 1636 ? 183.663 198.111 150.928 1.00 127.35 ? 1636 ASP A C     1 
ATOM   1501  O  O     . ASP A 1 1636 ? 184.425 199.064 150.733 1.00 130.34 ? 1636 ASP A O     1 
ATOM   1502  C  CB    . ASP A 1 1636 ? 183.193 197.630 153.347 1.00 130.97 ? 1636 ASP A CB    1 
ATOM   1503  C  CG    . ASP A 1 1636 ? 182.141 197.502 154.427 1.00 132.54 ? 1636 ASP A CG    1 
ATOM   1504  O  OD1   . ASP A 1 1636 ? 181.456 198.508 154.712 1.00 133.06 ? 1636 ASP A OD1   1 
ATOM   1505  O  OD2   . ASP A 1 1636 ? 182.001 196.396 154.988 1.00 129.92 ? 1636 ASP A OD2   1 
ATOM   1506  N  N     . LEU A 1 1637 ? 183.709 197.006 150.178 1.00 118.43 ? 1637 LEU A N     1 
ATOM   1507  C  CA    . LEU A 1 1637 ? 184.694 196.919 149.104 1.00 117.24 ? 1637 LEU A CA    1 
ATOM   1508  C  C     . LEU A 1 1637 ? 184.321 197.835 147.944 1.00 119.90 ? 1637 LEU A C     1 
ATOM   1509  O  O     . LEU A 1 1637 ? 185.195 198.485 147.356 1.00 123.01 ? 1637 LEU A O     1 
ATOM   1510  C  CB    . LEU A 1 1637 ? 184.850 195.479 148.621 1.00 118.60 ? 1637 LEU A CB    1 
ATOM   1511  C  CG    . LEU A 1 1637 ? 186.002 195.281 147.633 1.00 117.40 ? 1637 LEU A CG    1 
ATOM   1512  C  CD1   . LEU A 1 1637 ? 187.280 195.864 148.205 1.00 116.50 ? 1637 LEU A CD1   1 
ATOM   1513  C  CD2   . LEU A 1 1637 ? 186.198 193.820 147.317 1.00 119.31 ? 1637 LEU A CD2   1 
ATOM   1514  N  N     . LEU A 1 1638 ? 183.030 197.905 147.600 1.00 133.74 ? 1638 LEU A N     1 
ATOM   1515  C  CA    . LEU A 1 1638 ? 182.588 198.925 146.653 1.00 132.76 ? 1638 LEU A CA    1 
ATOM   1516  C  C     . LEU A 1 1638 ? 182.902 200.325 147.165 1.00 133.10 ? 1638 LEU A C     1 
ATOM   1517  O  O     . LEU A 1 1638 ? 183.322 201.194 146.393 1.00 133.93 ? 1638 LEU A O     1 
ATOM   1518  C  CB    . LEU A 1 1638 ? 181.090 198.812 146.374 1.00 133.71 ? 1638 LEU A CB    1 
ATOM   1519  C  CG    . LEU A 1 1638 ? 180.398 198.062 145.230 1.00 135.50 ? 1638 LEU A CG    1 
ATOM   1520  C  CD1   . LEU A 1 1638 ? 181.039 196.748 144.890 1.00 133.92 ? 1638 LEU A CD1   1 
ATOM   1521  C  CD2   . LEU A 1 1638 ? 178.907 197.896 145.511 1.00 136.45 ? 1638 LEU A CD2   1 
ATOM   1522  N  N     . GLU A 1 1639 ? 182.683 200.566 148.461 1.00 136.10 ? 1639 GLU A N     1 
ATOM   1523  C  CA    . GLU A 1 1639 ? 182.994 201.869 149.044 1.00 135.17 ? 1639 GLU A CA    1 
ATOM   1524  C  C     . GLU A 1 1639 ? 184.463 202.222 148.857 1.00 133.52 ? 1639 GLU A C     1 
ATOM   1525  O  O     . GLU A 1 1639 ? 184.798 203.360 148.510 1.00 133.98 ? 1639 GLU A O     1 
ATOM   1526  C  CB    . GLU A 1 1639 ? 182.629 201.870 150.531 1.00 135.69 ? 1639 GLU A CB    1 
ATOM   1527  C  CG    . GLU A 1 1639 ? 182.528 203.233 151.255 1.00 136.26 ? 1639 GLU A CG    1 
ATOM   1528  C  CD    . GLU A 1 1639 ? 181.546 204.235 150.654 1.00 137.98 ? 1639 GLU A CD    1 
ATOM   1529  O  OE1   . GLU A 1 1639 ? 181.352 204.275 149.428 1.00 136.69 ? 1639 GLU A OE1   1 
ATOM   1530  O  OE2   . GLU A 1 1639 ? 180.953 205.005 151.437 1.00 137.40 ? 1639 GLU A OE2   1 
ATOM   1531  N  N     . ILE A 1 1640 ? 185.352 201.261 149.099 1.00 128.26 ? 1640 ILE A N     1 
ATOM   1532  C  CA    . ILE A 1 1640 ? 186.783 201.511 148.955 1.00 127.23 ? 1640 ILE A CA    1 
ATOM   1533  C  C     . ILE A 1 1640 ? 187.138 201.764 147.494 1.00 128.61 ? 1640 ILE A C     1 
ATOM   1534  O  O     . ILE A 1 1640 ? 187.844 202.727 147.170 1.00 131.36 ? 1640 ILE A O     1 
ATOM   1535  C  CB    . ILE A 1 1640 ? 187.591 200.338 149.537 1.00 125.82 ? 1640 ILE A CB    1 
ATOM   1536  C  CG1   . ILE A 1 1640 ? 187.591 200.397 151.064 1.00 125.15 ? 1640 ILE A CG1   1 
ATOM   1537  C  CG2   . ILE A 1 1640 ? 189.013 200.347 148.997 1.00 123.97 ? 1640 ILE A CG2   1 
ATOM   1538  C  CD1   . ILE A 1 1640 ? 188.135 199.150 151.717 1.00 127.47 ? 1640 ILE A CD1   1 
ATOM   1539  N  N     . ILE A 1 1641 ? 186.655 200.907 146.591 1.00 130.84 ? 1641 ILE A N     1 
ATOM   1540  C  CA    . ILE A 1 1641 ? 187.048 201.010 145.187 1.00 129.33 ? 1641 ILE A CA    1 
ATOM   1541  C  C     . ILE A 1 1641 ? 186.538 202.309 144.574 1.00 130.71 ? 1641 ILE A C     1 
ATOM   1542  O  O     . ILE A 1 1641 ? 187.270 203.007 143.861 1.00 130.69 ? 1641 ILE A O     1 
ATOM   1543  C  CB    . ILE A 1 1641 ? 186.555 199.780 144.403 1.00 129.93 ? 1641 ILE A CB    1 
ATOM   1544  C  CG1   . ILE A 1 1641 ? 187.246 198.515 144.911 1.00 129.78 ? 1641 ILE A CG1   1 
ATOM   1545  C  CG2   . ILE A 1 1641 ? 186.821 199.951 142.919 1.00 129.21 ? 1641 ILE A CG2   1 
ATOM   1546  C  CD1   . ILE A 1 1641 ? 188.739 198.517 144.705 1.00 128.46 ? 1641 ILE A CD1   1 
ATOM   1547  N  N     . GLY A 1 1642 ? 185.278 202.657 144.841 1.00 142.28 ? 1642 GLY A N     1 
ATOM   1548  C  CA    . GLY A 1 1642 ? 184.713 203.863 144.257 1.00 143.27 ? 1642 GLY A CA    1 
ATOM   1549  C  C     . GLY A 1 1642 ? 185.341 205.137 144.790 1.00 141.72 ? 1642 GLY A C     1 
ATOM   1550  O  O     . GLY A 1 1642 ? 185.559 206.092 144.040 1.00 141.96 ? 1642 GLY A O     1 
ATOM   1551  N  N     . ASN A 1 1643 ? 185.635 205.173 146.090 1.00 137.91 ? 1643 ASN A N     1 
ATOM   1552  C  CA    . ASN A 1 1643 ? 186.169 206.360 146.745 1.00 137.50 ? 1643 ASN A CA    1 
ATOM   1553  C  C     . ASN A 1 1643 ? 187.690 206.335 146.845 1.00 140.12 ? 1643 ASN A C     1 
ATOM   1554  O  O     . ASN A 1 1643 ? 188.256 206.859 147.810 1.00 142.02 ? 1643 ASN A O     1 
ATOM   1555  C  CB    . ASN A 1 1643 ? 185.549 206.524 148.132 1.00 138.91 ? 1643 ASN A CB    1 
ATOM   1556  C  CG    . ASN A 1 1643 ? 184.122 207.025 148.075 1.00 138.52 ? 1643 ASN A CG    1 
ATOM   1557  O  OD1   . ASN A 1 1643 ? 183.184 206.300 148.403 1.00 139.89 ? 1643 ASN A OD1   1 
ATOM   1558  N  ND2   . ASN A 1 1643 ? 183.949 208.274 147.659 1.00 137.57 ? 1643 ASN A ND2   1 
ATOM   1559  N  N     . SER A 1 1644 ? 188.364 205.722 145.870 1.00 140.50 ? 1644 SER A N     1 
ATOM   1560  C  CA    . SER A 1 1644 ? 189.823 205.719 145.874 1.00 139.80 ? 1644 SER A CA    1 
ATOM   1561  C  C     . SER A 1 1644 ? 190.377 207.132 145.738 1.00 139.77 ? 1644 SER A C     1 
ATOM   1562  O  O     . SER A 1 1644 ? 191.381 207.477 146.372 1.00 139.98 ? 1644 SER A O     1 
ATOM   1563  C  CB    . SER A 1 1644 ? 190.348 204.824 144.752 1.00 138.63 ? 1644 SER A CB    1 
ATOM   1564  O  OG    . SER A 1 1644 ? 190.005 205.346 143.481 1.00 139.52 ? 1644 SER A OG    1 
ATOM   1565  N  N     . LYS A 1 1645 ? 189.738 207.962 144.909 1.00 142.19 ? 1645 LYS A N     1 
ATOM   1566  C  CA    . LYS A 1 1645 ? 190.199 209.336 144.734 1.00 143.20 ? 1645 LYS A CA    1 
ATOM   1567  C  C     . LYS A 1 1645 ? 190.073 210.134 146.025 1.00 141.59 ? 1645 LYS A C     1 
ATOM   1568  O  O     . LYS A 1 1645 ? 190.978 210.896 146.384 1.00 143.46 ? 1645 LYS A O     1 
ATOM   1569  C  CB    . LYS A 1 1645 ? 189.417 210.011 143.607 1.00 143.99 ? 1645 LYS A CB    1 
ATOM   1570  C  CG    . LYS A 1 1645 ? 189.844 209.584 142.212 1.00 143.08 ? 1645 LYS A CG    1 
ATOM   1571  C  CD    . LYS A 1 1645 ? 191.357 209.607 142.064 1.00 143.60 ? 1645 LYS A CD    1 
ATOM   1572  C  CE    . LYS A 1 1645 ? 191.871 211.023 141.858 1.00 143.82 ? 1645 LYS A CE    1 
ATOM   1573  N  NZ    . LYS A 1 1645 ? 193.359 211.083 141.882 1.00 140.70 ? 1645 LYS A NZ    1 
ATOM   1574  N  N     . ASN A 1 1646 ? 188.959 209.976 146.737 1.00 133.84 ? 1646 ASN A N     1 
ATOM   1575  C  CA    . ASN A 1 1646 ? 188.732 210.668 148.006 1.00 135.51 ? 1646 ASN A CA    1 
ATOM   1576  C  C     . ASN A 1 1646 ? 189.181 209.732 149.123 1.00 136.83 ? 1646 ASN A C     1 
ATOM   1577  O  O     . ASN A 1 1646 ? 188.394 208.956 149.666 1.00 138.57 ? 1646 ASN A O     1 
ATOM   1578  C  CB    . ASN A 1 1646 ? 187.270 211.074 148.154 1.00 137.90 ? 1646 ASN A CB    1 
ATOM   1579  C  CG    . ASN A 1 1646 ? 187.105 212.403 148.865 1.00 137.89 ? 1646 ASN A CG    1 
ATOM   1580  O  OD1   . ASN A 1 1646 ? 187.647 213.421 148.436 1.00 136.53 ? 1646 ASN A OD1   1 
ATOM   1581  N  ND2   . ASN A 1 1646 ? 186.353 212.399 149.960 1.00 137.02 ? 1646 ASN A ND2   1 
ATOM   1582  N  N     . VAL A 1 1647 ? 190.468 209.817 149.470 1.00 134.42 ? 1647 VAL A N     1 
ATOM   1583  C  CA    . VAL A 1 1647 ? 191.046 208.916 150.458 1.00 137.22 ? 1647 VAL A CA    1 
ATOM   1584  C  C     . VAL A 1 1647 ? 190.464 209.142 151.849 1.00 137.47 ? 1647 VAL A C     1 
ATOM   1585  O  O     . VAL A 1 1647 ? 190.499 208.233 152.686 1.00 139.53 ? 1647 VAL A O     1 
ATOM   1586  C  CB    . VAL A 1 1647 ? 192.579 209.068 150.469 1.00 134.16 ? 1647 VAL A CB    1 
ATOM   1587  C  CG1   . VAL A 1 1647 ? 193.230 207.932 151.245 1.00 134.91 ? 1647 VAL A CG1   1 
ATOM   1588  C  CG2   . VAL A 1 1647 ? 193.114 209.123 149.047 1.00 131.50 ? 1647 VAL A CG2   1 
ATOM   1589  N  N     . ALA A 1 1648 ? 189.914 210.330 152.115 1.00 128.31 ? 1648 ALA A N     1 
ATOM   1590  C  CA    . ALA A 1 1648 ? 189.372 210.625 153.438 1.00 128.07 ? 1648 ALA A CA    1 
ATOM   1591  C  C     . ALA A 1 1648 ? 188.216 209.708 153.816 1.00 128.36 ? 1648 ALA A C     1 
ATOM   1592  O  O     . ALA A 1 1648 ? 187.929 209.553 155.007 1.00 128.87 ? 1648 ALA A O     1 
ATOM   1593  C  CB    . ALA A 1 1648 ? 188.922 212.085 153.508 1.00 127.72 ? 1648 ALA A CB    1 
ATOM   1594  N  N     . LYS A 1 1649 ? 187.546 209.100 152.837 1.00 128.62 ? 1649 LYS A N     1 
ATOM   1595  C  CA    . LYS A 1 1649 ? 186.457 208.177 153.126 1.00 130.88 ? 1649 LYS A CA    1 
ATOM   1596  C  C     . LYS A 1 1649 ? 186.926 206.741 153.319 1.00 130.13 ? 1649 LYS A C     1 
ATOM   1597  O  O     . LYS A 1 1649 ? 186.105 205.879 153.651 1.00 128.81 ? 1649 LYS A O     1 
ATOM   1598  C  CB    . LYS A 1 1649 ? 185.411 208.228 152.010 1.00 130.82 ? 1649 LYS A CB    1 
ATOM   1599  C  CG    . LYS A 1 1649 ? 184.786 209.598 151.810 1.00 130.27 ? 1649 LYS A CG    1 
ATOM   1600  C  CD    . LYS A 1 1649 ? 183.640 209.823 152.783 1.00 130.24 ? 1649 LYS A CD    1 
ATOM   1601  C  CE    . LYS A 1 1649 ? 182.557 208.769 152.612 1.00 130.77 ? 1649 LYS A CE    1 
ATOM   1602  N  NZ    . LYS A 1 1649 ? 181.197 209.323 152.855 1.00 130.97 ? 1649 LYS A NZ    1 
ATOM   1603  N  N     . LEU A 1 1650 ? 188.212 206.461 153.116 1.00 122.64 ? 1650 LEU A N     1 
ATOM   1604  C  CA    . LEU A 1 1650 ? 188.754 205.128 153.334 1.00 121.39 ? 1650 LEU A CA    1 
ATOM   1605  C  C     . LEU A 1 1650 ? 189.312 204.935 154.736 1.00 120.99 ? 1650 LEU A C     1 
ATOM   1606  O  O     . LEU A 1 1650 ? 189.730 203.821 155.069 1.00 120.62 ? 1650 LEU A O     1 
ATOM   1607  C  CB    . LEU A 1 1650 ? 189.854 204.826 152.311 1.00 120.06 ? 1650 LEU A CB    1 
ATOM   1608  C  CG    . LEU A 1 1650 ? 189.577 205.207 150.857 1.00 119.77 ? 1650 LEU A CG    1 
ATOM   1609  C  CD1   . LEU A 1 1650 ? 190.774 204.873 149.981 1.00 118.61 ? 1650 LEU A CD1   1 
ATOM   1610  C  CD2   . LEU A 1 1650 ? 188.325 204.514 150.349 1.00 120.93 ? 1650 LEU A CD2   1 
ATOM   1611  N  N     . GLN A 1 1651 ? 189.323 205.984 155.562 1.00 124.63 ? 1651 GLN A N     1 
ATOM   1612  C  CA    . GLN A 1 1651 ? 189.947 205.891 156.878 1.00 126.61 ? 1651 GLN A CA    1 
ATOM   1613  C  C     . GLN A 1 1651 ? 189.228 204.902 157.785 1.00 125.98 ? 1651 GLN A C     1 
ATOM   1614  O  O     . GLN A 1 1651 ? 189.871 204.237 158.603 1.00 126.79 ? 1651 GLN A O     1 
ATOM   1615  C  CB    . GLN A 1 1651 ? 189.993 207.271 157.533 1.00 123.55 ? 1651 GLN A CB    1 
ATOM   1616  C  CG    . GLN A 1 1651 ? 190.597 208.354 156.656 1.00 122.62 ? 1651 GLN A CG    1 
ATOM   1617  C  CD    . GLN A 1 1651 ? 192.111 208.381 156.717 1.00 123.82 ? 1651 GLN A CD    1 
ATOM   1618  O  OE1   . GLN A 1 1651 ? 192.738 207.486 157.282 1.00 124.88 ? 1651 GLN A OE1   1 
ATOM   1619  N  NE2   . GLN A 1 1651 ? 192.707 209.413 156.134 1.00 125.67 ? 1651 GLN A NE2   1 
ATOM   1620  N  N     . LYS A 1 1652 ? 187.909 204.784 157.658 1.00 119.03 ? 1652 LYS A N     1 
ATOM   1621  C  CA    . LYS A 1 1652 ? 187.144 203.897 158.524 1.00 121.38 ? 1652 LYS A CA    1 
ATOM   1622  C  C     . LYS A 1 1652 ? 187.104 202.460 158.021 1.00 122.77 ? 1652 LYS A C     1 
ATOM   1623  O  O     . LYS A 1 1652 ? 186.442 201.624 158.645 1.00 124.96 ? 1652 LYS A O     1 
ATOM   1624  C  CB    . LYS A 1 1652 ? 185.720 204.433 158.695 1.00 121.13 ? 1652 LYS A CB    1 
ATOM   1625  C  CG    . LYS A 1 1652 ? 184.908 204.475 157.415 1.00 121.78 ? 1652 LYS A CG    1 
ATOM   1626  C  CD    . LYS A 1 1652 ? 183.481 204.928 157.679 1.00 122.25 ? 1652 LYS A CD    1 
ATOM   1627  C  CE    . LYS A 1 1652 ? 182.662 204.942 156.399 1.00 121.26 ? 1652 LYS A CE    1 
ATOM   1628  N  NZ    . LYS A 1 1652 ? 181.259 205.379 156.640 1.00 121.99 ? 1652 LYS A NZ    1 
ATOM   1629  N  N     . HIS A 1 1653 ? 187.788 202.150 156.920 1.00 114.55 ? 1653 HIS A N     1 
ATOM   1630  C  CA    . HIS A 1 1653 ? 187.825 200.795 156.387 1.00 115.07 ? 1653 HIS A CA    1 
ATOM   1631  C  C     . HIS A 1 1653 ? 189.164 200.098 156.591 1.00 115.49 ? 1653 HIS A C     1 
ATOM   1632  O  O     . HIS A 1 1653 ? 189.282 198.916 156.253 1.00 118.53 ? 1653 HIS A O     1 
ATOM   1633  C  CB    . HIS A 1 1653 ? 187.488 200.802 154.890 1.00 115.48 ? 1653 HIS A CB    1 
ATOM   1634  C  CG    . HIS A 1 1653 ? 186.058 201.125 154.592 1.00 118.70 ? 1653 HIS A CG    1 
ATOM   1635  N  ND1   . HIS A 1 1653 ? 185.349 200.504 153.587 1.00 118.07 ? 1653 HIS A ND1   1 
ATOM   1636  C  CD2   . HIS A 1 1653 ? 185.204 202.004 155.167 1.00 119.09 ? 1653 HIS A CD2   1 
ATOM   1637  C  CE1   . HIS A 1 1653 ? 184.120 200.987 153.556 1.00 120.11 ? 1653 HIS A CE1   1 
ATOM   1638  N  NE2   . HIS A 1 1653 ? 184.005 201.898 154.504 1.00 117.18 ? 1653 HIS A NE2   1 
ATOM   1639  N  N     . PHE A 1 1654 ? 190.171 200.790 157.127 1.00 100.24 ? 1654 PHE A N     1 
ATOM   1640  C  CA    . PHE A 1 1654 ? 191.481 200.173 157.300 1.00 101.26 ? 1654 PHE A CA    1 
ATOM   1641  C  C     . PHE A 1 1654 ? 191.522 199.193 158.464 1.00 100.83 ? 1654 PHE A C     1 
ATOM   1642  O  O     . PHE A 1 1654 ? 192.332 198.261 158.440 1.00 100.09 ? 1654 PHE A O     1 
ATOM   1643  C  CB    . PHE A 1 1654 ? 192.552 201.246 157.496 1.00 106.05 ? 1654 PHE A CB    1 
ATOM   1644  C  CG    . PHE A 1 1654 ? 193.077 201.816 156.213 1.00 102.82 ? 1654 PHE A CG    1 
ATOM   1645  C  CD1   . PHE A 1 1654 ? 194.056 201.151 155.496 1.00 99.22  ? 1654 PHE A CD1   1 
ATOM   1646  C  CD2   . PHE A 1 1654 ? 192.598 203.018 155.726 1.00 103.37 ? 1654 PHE A CD2   1 
ATOM   1647  C  CE1   . PHE A 1 1654 ? 194.543 201.673 154.316 1.00 98.39  ? 1654 PHE A CE1   1 
ATOM   1648  C  CE2   . PHE A 1 1654 ? 193.080 203.544 154.545 1.00 104.35 ? 1654 PHE A CE2   1 
ATOM   1649  C  CZ    . PHE A 1 1654 ? 194.054 202.871 153.839 1.00 102.07 ? 1654 PHE A CZ    1 
ATOM   1650  N  N     . LYS A 1 1655 ? 190.676 199.380 159.479 1.00 104.71 ? 1655 LYS A N     1 
ATOM   1651  C  CA    . LYS A 1 1655 ? 190.725 198.516 160.652 1.00 105.65 ? 1655 LYS A CA    1 
ATOM   1652  C  C     . LYS A 1 1655 ? 190.336 197.078 160.335 1.00 108.82 ? 1655 LYS A C     1 
ATOM   1653  O  O     . LYS A 1 1655 ? 190.793 196.161 161.026 1.00 111.81 ? 1655 LYS A O     1 
ATOM   1654  C  CB    . LYS A 1 1655 ? 189.827 199.073 161.758 1.00 104.47 ? 1655 LYS A CB    1 
ATOM   1655  C  CG    . LYS A 1 1655 ? 188.343 199.045 161.442 1.00 105.08 ? 1655 LYS A CG    1 
ATOM   1656  C  CD    . LYS A 1 1655 ? 187.515 199.168 162.709 1.00 107.47 ? 1655 LYS A CD    1 
ATOM   1657  C  CE    . LYS A 1 1655 ? 187.733 200.512 163.383 1.00 108.76 ? 1655 LYS A CE    1 
ATOM   1658  N  NZ    . LYS A 1 1655 ? 187.301 201.644 162.519 1.00 109.43 ? 1655 LYS A NZ    1 
ATOM   1659  N  N     . LYS A 1 1656 ? 189.513 196.857 159.310 1.00 103.55 ? 1656 LYS A N     1 
ATOM   1660  C  CA    . LYS A 1 1656 ? 189.152 195.505 158.908 1.00 103.39 ? 1656 LYS A CA    1 
ATOM   1661  C  C     . LYS A 1 1656 ? 190.145 194.895 157.931 1.00 96.98  ? 1656 LYS A C     1 
ATOM   1662  O  O     . LYS A 1 1656 ? 189.980 193.734 157.543 1.00 96.31  ? 1656 LYS A O     1 
ATOM   1663  C  CB    . LYS A 1 1656 ? 187.755 195.489 158.278 1.00 100.76 ? 1656 LYS A CB    1 
ATOM   1664  C  CG    . LYS A 1 1656 ? 187.686 196.136 156.905 1.00 96.79  ? 1656 LYS A CG    1 
ATOM   1665  C  CD    . LYS A 1 1656 ? 186.257 196.200 156.391 1.00 99.75  ? 1656 LYS A CD    1 
ATOM   1666  C  CE    . LYS A 1 1656 ? 185.309 196.738 157.449 1.00 98.54  ? 1656 LYS A CE    1 
ATOM   1667  N  NZ    . LYS A 1 1656 ? 185.619 198.151 157.798 1.00 99.40  ? 1656 LYS A NZ    1 
ATOM   1668  N  N     . MET A 1 1657 ? 191.169 195.647 157.530 1.00 97.07  ? 1657 MET A N     1 
ATOM   1669  C  CA    . MET A 1 1657 ? 192.146 195.171 156.563 1.00 101.07 ? 1657 MET A CA    1 
ATOM   1670  C  C     . MET A 1 1657 ? 193.530 194.959 157.161 1.00 97.96  ? 1657 MET A C     1 
ATOM   1671  O  O     . MET A 1 1657 ? 194.347 194.257 156.555 1.00 94.30  ? 1657 MET A O     1 
ATOM   1672  C  CB    . MET A 1 1657 ? 192.248 196.157 155.393 1.00 104.47 ? 1657 MET A CB    1 
ATOM   1673  C  CG    . MET A 1 1657 ? 192.675 195.529 154.080 1.00 101.11 ? 1657 MET A CG    1 
ATOM   1674  S  SD    . MET A 1 1657 ? 192.678 196.696 152.705 1.00 104.25 ? 1657 MET A SD    1 
ATOM   1675  C  CE    . MET A 1 1657 ? 191.390 197.831 153.214 1.00 96.16  ? 1657 MET A CE    1 
ATOM   1676  N  N     . PHE A 1 1658 ? 193.811 195.540 158.325 1.00 97.77  ? 1658 PHE A N     1 
ATOM   1677  C  CA    . PHE A 1 1658 ? 195.104 195.413 158.978 1.00 98.33  ? 1658 PHE A CA    1 
ATOM   1678  C  C     . PHE A 1 1658 ? 194.901 195.120 160.458 1.00 102.57 ? 1658 PHE A C     1 
ATOM   1679  O  O     . PHE A 1 1658 ? 193.823 195.340 161.016 1.00 102.10 ? 1658 PHE A O     1 
ATOM   1680  C  CB    . PHE A 1 1658 ? 195.957 196.678 158.812 1.00 99.10  ? 1658 PHE A CB    1 
ATOM   1681  C  CG    . PHE A 1 1658 ? 196.339 196.975 157.389 1.00 100.61 ? 1658 PHE A CG    1 
ATOM   1682  C  CD1   . PHE A 1 1658 ? 195.444 197.591 156.529 1.00 101.79 ? 1658 PHE A CD1   1 
ATOM   1683  C  CD2   . PHE A 1 1658 ? 197.597 196.649 156.915 1.00 99.90  ? 1658 PHE A CD2   1 
ATOM   1684  C  CE1   . PHE A 1 1658 ? 195.796 197.867 155.222 1.00 101.26 ? 1658 PHE A CE1   1 
ATOM   1685  C  CE2   . PHE A 1 1658 ? 197.954 196.923 155.610 1.00 99.95  ? 1658 PHE A CE2   1 
ATOM   1686  C  CZ    . PHE A 1 1658 ? 197.053 197.534 154.763 1.00 97.94  ? 1658 PHE A CZ    1 
ATOM   1687  N  N     . ALA A 1 1659 ? 195.960 194.610 161.090 1.00 95.45  ? 1659 ALA A N     1 
ATOM   1688  C  CA    . ALA A 1 1659 ? 195.875 194.234 162.497 1.00 95.21  ? 1659 ALA A CA    1 
ATOM   1689  C  C     . ALA A 1 1659 ? 195.716 195.457 163.392 1.00 98.71  ? 1659 ALA A C     1 
ATOM   1690  O  O     . ALA A 1 1659 ? 194.845 195.487 164.269 1.00 103.35 ? 1659 ALA A O     1 
ATOM   1691  C  CB    . ALA A 1 1659 ? 197.109 193.428 162.899 1.00 93.59  ? 1659 ALA A CB    1 
ATOM   1692  N  N     . GLY A 1 1660 ? 196.546 196.476 163.187 1.00 104.30 ? 1660 GLY A N     1 
ATOM   1693  C  CA    . GLY A 1 1660 ? 196.530 197.632 164.062 1.00 104.36 ? 1660 GLY A CA    1 
ATOM   1694  C  C     . GLY A 1 1660 ? 196.487 198.967 163.350 1.00 103.93 ? 1660 GLY A C     1 
ATOM   1695  O  O     . GLY A 1 1660 ? 196.602 200.016 163.989 1.00 108.98 ? 1660 GLY A O     1 
ATOM   1696  N  N     . VAL A 1 1661 ? 196.325 198.948 162.029 1.00 98.01  ? 1661 VAL A N     1 
ATOM   1697  C  CA    . VAL A 1 1661 ? 196.239 200.171 161.238 1.00 93.57  ? 1661 VAL A CA    1 
ATOM   1698  C  C     . VAL A 1 1661 ? 194.768 200.566 161.163 1.00 94.41  ? 1661 VAL A C     1 
ATOM   1699  O  O     . VAL A 1 1661 ? 193.978 199.947 160.449 1.00 100.18 ? 1661 VAL A O     1 
ATOM   1700  C  CB    . VAL A 1 1661 ? 196.850 199.995 159.848 1.00 90.83  ? 1661 VAL A CB    1 
ATOM   1701  C  CG1   . VAL A 1 1661 ? 196.701 201.272 159.044 1.00 91.61  ? 1661 VAL A CG1   1 
ATOM   1702  C  CG2   . VAL A 1 1661 ? 198.313 199.618 159.966 1.00 95.58  ? 1661 VAL A CG2   1 
ATOM   1703  N  N     . SER A 1 1662 ? 194.400 201.608 161.908 1.00 103.49 ? 1662 SER A N     1 
ATOM   1704  C  CA    . SER A 1 1662 ? 193.040 202.125 161.877 1.00 108.11 ? 1662 SER A CA    1 
ATOM   1705  C  C     . SER A 1 1662 ? 192.880 203.313 160.941 1.00 105.80 ? 1662 SER A C     1 
ATOM   1706  O  O     . SER A 1 1662 ? 191.753 203.615 160.534 1.00 104.92 ? 1662 SER A O     1 
ATOM   1707  C  CB    . SER A 1 1662 ? 192.595 202.531 163.286 1.00 107.77 ? 1662 SER A CB    1 
ATOM   1708  O  OG    . SER A 1 1662 ? 193.142 203.786 163.648 1.00 107.43 ? 1662 SER A OG    1 
ATOM   1709  N  N     . SER A 1 1663 ? 193.972 203.989 160.594 1.00 106.84 ? 1663 SER A N     1 
ATOM   1710  C  CA    . SER A 1 1663 ? 193.923 205.120 159.679 1.00 106.26 ? 1663 SER A CA    1 
ATOM   1711  C  C     . SER A 1 1663 ? 195.319 205.357 159.125 1.00 108.61 ? 1663 SER A C     1 
ATOM   1712  O  O     . SER A 1 1663 ? 196.311 204.853 159.657 1.00 112.74 ? 1663 SER A O     1 
ATOM   1713  C  CB    . SER A 1 1663 ? 193.393 206.382 160.369 1.00 106.50 ? 1663 SER A CB    1 
ATOM   1714  O  OG    . SER A 1 1663 ? 194.363 206.933 161.241 1.00 105.87 ? 1663 SER A OG    1 
ATOM   1715  N  N     . ILE A 1 1664 ? 195.382 206.134 158.048 1.00 106.36 ? 1664 ILE A N     1 
ATOM   1716  C  CA    . ILE A 1 1664 ? 196.644 206.474 157.406 1.00 105.28 ? 1664 ILE A CA    1 
ATOM   1717  C  C     . ILE A 1 1664 ? 196.849 207.979 157.491 1.00 106.64 ? 1664 ILE A C     1 
ATOM   1718  O  O     . ILE A 1 1664 ? 195.891 208.755 157.565 1.00 105.43 ? 1664 ILE A O     1 
ATOM   1719  C  CB    . ILE A 1 1664 ? 196.694 205.998 155.939 1.00 101.40 ? 1664 ILE A CB    1 
ATOM   1720  C  CG1   . ILE A 1 1664 ? 195.497 206.539 155.159 1.00 103.25 ? 1664 ILE A CG1   1 
ATOM   1721  C  CG2   . ILE A 1 1664 ? 196.734 204.481 155.874 1.00 105.86 ? 1664 ILE A CG2   1 
ATOM   1722  C  CD1   . ILE A 1 1664 ? 195.681 206.502 153.659 1.00 101.93 ? 1664 ILE A CD1   1 
ATOM   1723  N  N     . ILE A 1 1665 ? 198.115 208.388 157.480 1.00 111.84 ? 1665 ILE A N     1 
ATOM   1724  C  CA    . ILE A 1 1665 ? 198.495 209.793 157.572 1.00 108.94 ? 1665 ILE A CA    1 
ATOM   1725  C  C     . ILE A 1 1665 ? 198.828 210.298 156.177 1.00 113.18 ? 1665 ILE A C     1 
ATOM   1726  O  O     . ILE A 1 1665 ? 199.660 209.710 155.475 1.00 111.44 ? 1665 ILE A O     1 
ATOM   1727  C  CB    . ILE A 1 1665 ? 199.685 209.988 158.526 1.00 108.93 ? 1665 ILE A CB    1 
ATOM   1728  C  CG1   . ILE A 1 1665 ? 199.324 209.510 159.933 1.00 115.00 ? 1665 ILE A CG1   1 
ATOM   1729  C  CG2   . ILE A 1 1665 ? 200.113 211.445 158.553 1.00 109.67 ? 1665 ILE A CG2   1 
ATOM   1730  C  CD1   . ILE A 1 1665 ? 200.514 209.376 160.855 1.00 113.04 ? 1665 ILE A CD1   1 
ATOM   1731  N  N     . LEU A 1 1666 ? 198.182 211.388 155.777 1.00 123.94 ? 1666 LEU A N     1 
ATOM   1732  C  CA    . LEU A 1 1666 ? 198.350 211.976 154.458 1.00 122.11 ? 1666 LEU A CA    1 
ATOM   1733  C  C     . LEU A 1 1666 ? 198.834 213.414 154.590 1.00 121.95 ? 1666 LEU A C     1 
ATOM   1734  O  O     . LEU A 1 1666 ? 198.623 214.077 155.609 1.00 120.38 ? 1666 LEU A O     1 
ATOM   1735  C  CB    . LEU A 1 1666 ? 197.037 211.933 153.665 1.00 120.88 ? 1666 LEU A CB    1 
ATOM   1736  C  CG    . LEU A 1 1666 ? 196.608 210.585 153.087 1.00 120.77 ? 1666 LEU A CG    1 
ATOM   1737  C  CD1   . LEU A 1 1666 ? 195.402 210.762 152.183 1.00 119.86 ? 1666 LEU A CD1   1 
ATOM   1738  C  CD2   . LEU A 1 1666 ? 197.753 209.935 152.332 1.00 118.72 ? 1666 LEU A CD2   1 
ATOM   1739  N  N     . ASN A 1 1667 ? 199.488 213.895 153.537 1.00 125.25 ? 1667 ASN A N     1 
ATOM   1740  C  CA    . ASN A 1 1667 ? 199.940 215.278 153.486 1.00 123.49 ? 1667 ASN A CA    1 
ATOM   1741  C  C     . ASN A 1 1667 ? 198.748 216.185 153.180 1.00 125.92 ? 1667 ASN A C     1 
ATOM   1742  O  O     . ASN A 1 1667 ? 197.598 215.742 153.117 1.00 126.20 ? 1667 ASN A O     1 
ATOM   1743  C  CB    . ASN A 1 1667 ? 201.062 215.432 152.463 1.00 122.08 ? 1667 ASN A CB    1 
ATOM   1744  C  CG    . ASN A 1 1667 ? 200.710 214.833 151.117 1.00 122.45 ? 1667 ASN A CG    1 
ATOM   1745  O  OD1   . ASN A 1 1667 ? 199.682 214.174 150.968 1.00 123.75 ? 1667 ASN A OD1   1 
ATOM   1746  N  ND2   . ASN A 1 1667 ? 201.563 215.064 150.127 1.00 122.48 ? 1667 ASN A ND2   1 
ATOM   1747  N  N     . GLU A 1 1668 ? 199.013 217.479 152.987 1.00 131.74 ? 1668 GLU A N     1 
ATOM   1748  C  CA    . GLU A 1 1668 ? 197.929 218.420 152.725 1.00 131.29 ? 1668 GLU A CA    1 
ATOM   1749  C  C     . GLU A 1 1668 ? 197.260 218.155 151.382 1.00 130.60 ? 1668 GLU A C     1 
ATOM   1750  O  O     . GLU A 1 1668 ? 196.051 218.369 151.241 1.00 132.36 ? 1668 GLU A O     1 
ATOM   1751  C  CB    . GLU A 1 1668 ? 198.453 219.855 152.785 1.00 130.73 ? 1668 GLU A CB    1 
ATOM   1752  C  CG    . GLU A 1 1668 ? 198.400 220.472 154.173 1.00 130.73 ? 1668 GLU A CG    1 
ATOM   1753  C  CD    . GLU A 1 1668 ? 197.032 221.034 154.507 1.00 130.70 ? 1668 GLU A CD    1 
ATOM   1754  O  OE1   . GLU A 1 1668 ? 196.248 221.293 153.570 1.00 130.20 ? 1668 GLU A OE1   1 
ATOM   1755  O  OE2   . GLU A 1 1668 ? 196.740 221.215 155.708 1.00 130.76 ? 1668 GLU A OE2   1 
ATOM   1756  N  N     . ASP A 1 1669 ? 198.022 217.692 150.392 1.00 129.64 ? 1669 ASP A N     1 
ATOM   1757  C  CA    . ASP A 1 1669 ? 197.467 217.404 149.076 1.00 131.84 ? 1669 ASP A CA    1 
ATOM   1758  C  C     . ASP A 1 1669 ? 196.681 216.096 149.061 1.00 132.67 ? 1669 ASP A C     1 
ATOM   1759  O  O     . ASP A 1 1669 ? 195.928 215.847 148.113 1.00 132.19 ? 1669 ASP A O     1 
ATOM   1760  C  CB    . ASP A 1 1669 ? 198.605 217.364 148.046 1.00 133.22 ? 1669 ASP A CB    1 
ATOM   1761  C  CG    . ASP A 1 1669 ? 198.121 217.144 146.619 1.00 135.67 ? 1669 ASP A CG    1 
ATOM   1762  O  OD1   . ASP A 1 1669 ? 196.944 217.437 146.321 1.00 135.24 ? 1669 ASP A OD1   1 
ATOM   1763  O  OD2   . ASP A 1 1669 ? 198.928 216.676 145.789 1.00 136.00 ? 1669 ASP A OD2   1 
ATOM   1764  N  N     . ASN A 1 1670 ? 196.815 215.275 150.106 1.00 127.54 ? 1670 ASN A N     1 
ATOM   1765  C  CA    . ASN A 1 1670 ? 196.213 213.939 150.151 1.00 127.43 ? 1670 ASN A CA    1 
ATOM   1766  C  C     . ASN A 1 1670 ? 196.670 213.096 148.964 1.00 125.62 ? 1670 ASN A C     1 
ATOM   1767  O  O     . ASN A 1 1670 ? 195.886 212.364 148.356 1.00 125.62 ? 1670 ASN A O     1 
ATOM   1768  C  CB    . ASN A 1 1670 ? 194.685 214.010 150.213 1.00 127.26 ? 1670 ASN A CB    1 
ATOM   1769  C  CG    . ASN A 1 1670 ? 194.177 214.548 151.536 1.00 125.87 ? 1670 ASN A CG    1 
ATOM   1770  O  OD1   . ASN A 1 1670 ? 194.954 215.008 152.371 1.00 124.33 ? 1670 ASN A OD1   1 
ATOM   1771  N  ND2   . ASN A 1 1670 ? 192.866 214.492 151.732 1.00 125.28 ? 1670 ASN A ND2   1 
ATOM   1772  N  N     . SER A 1 1671 ? 197.957 213.200 148.632 1.00 125.48 ? 1671 SER A N     1 
ATOM   1773  C  CA    . SER A 1 1671 ? 198.535 212.466 147.519 1.00 126.23 ? 1671 SER A CA    1 
ATOM   1774  C  C     . SER A 1 1671 ? 199.728 211.607 147.908 1.00 128.46 ? 1671 SER A C     1 
ATOM   1775  O  O     . SER A 1 1671 ? 200.142 210.760 147.108 1.00 126.82 ? 1671 SER A O     1 
ATOM   1776  C  CB    . SER A 1 1671 ? 198.963 213.434 146.406 1.00 124.44 ? 1671 SER A CB    1 
ATOM   1777  O  OG    . SER A 1 1671 ? 199.790 214.463 146.920 1.00 125.67 ? 1671 SER A OG    1 
ATOM   1778  N  N     . VAL A 1 1672 ? 200.291 211.796 149.098 1.00 124.09 ? 1672 VAL A N     1 
ATOM   1779  C  CA    . VAL A 1 1672 ? 201.462 211.057 149.550 1.00 121.01 ? 1672 VAL A CA    1 
ATOM   1780  C  C     . VAL A 1 1672 ? 201.157 210.460 150.916 1.00 122.43 ? 1672 VAL A C     1 
ATOM   1781  O  O     . VAL A 1 1672 ? 200.732 211.177 151.830 1.00 121.92 ? 1672 VAL A O     1 
ATOM   1782  C  CB    . VAL A 1 1672 ? 202.710 211.956 149.616 1.00 117.92 ? 1672 VAL A CB    1 
ATOM   1783  C  CG1   . VAL A 1 1672 ? 203.867 211.208 150.234 1.00 119.94 ? 1672 VAL A CG1   1 
ATOM   1784  C  CG2   . VAL A 1 1672 ? 203.078 212.453 148.227 1.00 118.89 ? 1672 VAL A CG2   1 
ATOM   1785  N  N     . VAL A 1 1673 ? 201.374 209.156 151.056 1.00 115.24 ? 1673 VAL A N     1 
ATOM   1786  C  CA    . VAL A 1 1673 ? 201.117 208.449 152.305 1.00 113.32 ? 1673 VAL A CA    1 
ATOM   1787  C  C     . VAL A 1 1673 ? 202.363 208.561 153.175 1.00 112.86 ? 1673 VAL A C     1 
ATOM   1788  O  O     . VAL A 1 1673 ? 203.358 207.870 152.944 1.00 109.64 ? 1673 VAL A O     1 
ATOM   1789  C  CB    . VAL A 1 1673 ? 200.743 206.984 152.057 1.00 111.00 ? 1673 VAL A CB    1 
ATOM   1790  C  CG1   . VAL A 1 1673 ? 200.475 206.277 153.375 1.00 111.00 ? 1673 VAL A CG1   1 
ATOM   1791  C  CG2   . VAL A 1 1673 ? 199.533 206.894 151.141 1.00 109.97 ? 1673 VAL A CG2   1 
ATOM   1792  N  N     . LEU A 1 1674 ? 202.310 209.439 154.178 1.00 114.30 ? 1674 LEU A N     1 
ATOM   1793  C  CA    . LEU A 1 1674 ? 203.447 209.633 155.069 1.00 113.66 ? 1674 LEU A CA    1 
ATOM   1794  C  C     . LEU A 1 1674 ? 203.598 208.515 156.092 1.00 114.27 ? 1674 LEU A C     1 
ATOM   1795  O  O     . LEU A 1 1674 ? 204.730 208.178 156.453 1.00 114.56 ? 1674 LEU A O     1 
ATOM   1796  C  CB    . LEU A 1 1674 ? 203.326 210.975 155.793 1.00 112.65 ? 1674 LEU A CB    1 
ATOM   1797  C  CG    . LEU A 1 1674 ? 203.277 212.219 154.905 1.00 113.11 ? 1674 LEU A CG    1 
ATOM   1798  C  CD1   . LEU A 1 1674 ? 203.212 213.479 155.751 1.00 113.34 ? 1674 LEU A CD1   1 
ATOM   1799  C  CD2   . LEU A 1 1674 ? 204.478 212.256 153.975 1.00 112.98 ? 1674 LEU A CD2   1 
ATOM   1800  N  N     . GLY A 1 1675 ? 202.498 207.936 156.563 1.00 111.53 ? 1675 GLY A N     1 
ATOM   1801  C  CA    . GLY A 1 1675 ? 202.590 206.898 157.572 1.00 109.03 ? 1675 GLY A CA    1 
ATOM   1802  C  C     . GLY A 1 1675 ? 201.223 206.330 157.901 1.00 108.57 ? 1675 GLY A C     1 
ATOM   1803  O  O     . GLY A 1 1675 ? 200.263 206.513 157.151 1.00 112.31 ? 1675 GLY A O     1 
ATOM   1804  N  N     . ILE A 1 1676 ? 201.157 205.637 159.039 1.00 97.24  ? 1676 ILE A N     1 
ATOM   1805  C  CA    . ILE A 1 1676 ? 199.947 204.960 159.482 1.00 97.46  ? 1676 ILE A CA    1 
ATOM   1806  C  C     . ILE A 1 1676 ? 199.694 205.299 160.944 1.00 97.19  ? 1676 ILE A C     1 
ATOM   1807  O  O     . ILE A 1 1676 ? 200.565 205.812 161.650 1.00 100.48 ? 1676 ILE A O     1 
ATOM   1808  C  CB    . ILE A 1 1676 ? 200.036 203.432 159.295 1.00 101.15 ? 1676 ILE A CB    1 
ATOM   1809  C  CG1   . ILE A 1 1676 ? 201.441 202.937 159.638 1.00 98.50  ? 1676 ILE A CG1   1 
ATOM   1810  C  CG2   . ILE A 1 1676 ? 199.679 203.050 157.870 1.00 101.11 ? 1676 ILE A CG2   1 
ATOM   1811  C  CD1   . ILE A 1 1676 ? 201.645 201.461 159.384 1.00 97.54  ? 1676 ILE A CD1   1 
ATOM   1812  N  N     . SER A 1 1677 ? 198.477 205.000 161.395 1.00 96.38  ? 1677 SER A N     1 
ATOM   1813  C  CA    . SER A 1 1677 ? 198.065 205.290 162.760 1.00 96.08  ? 1677 SER A CA    1 
ATOM   1814  C  C     . SER A 1 1677 ? 197.196 204.157 163.284 1.00 97.40  ? 1677 SER A C     1 
ATOM   1815  O  O     . SER A 1 1677 ? 196.587 203.406 162.518 1.00 100.13 ? 1677 SER A O     1 
ATOM   1816  C  CB    . SER A 1 1677 ? 197.306 206.621 162.848 1.00 101.98 ? 1677 SER A CB    1 
ATOM   1817  O  OG    . SER A 1 1677 ? 196.793 206.829 164.152 1.00 105.29 ? 1677 SER A OG    1 
ATOM   1818  N  N     . SER A 1 1678 ? 197.147 204.044 164.607 1.00 103.79 ? 1678 SER A N     1 
ATOM   1819  C  CA    . SER A 1 1678 ? 196.336 203.050 165.295 1.00 106.50 ? 1678 SER A CA    1 
ATOM   1820  C  C     . SER A 1 1678 ? 195.141 203.722 165.961 1.00 108.88 ? 1678 SER A C     1 
ATOM   1821  O  O     . SER A 1 1678 ? 195.018 204.949 165.984 1.00 110.57 ? 1678 SER A O     1 
ATOM   1822  C  CB    . SER A 1 1678 ? 197.172 202.291 166.331 1.00 107.88 ? 1678 SER A CB    1 
ATOM   1823  O  OG    . SER A 1 1678 ? 197.651 203.166 167.337 1.00 109.76 ? 1678 SER A OG    1 
ATOM   1824  N  N     . ARG A 1 1679 ? 194.248 202.892 166.507 1.00 119.95 ? 1679 ARG A N     1 
ATOM   1825  C  CA    . ARG A 1 1679 ? 193.054 203.413 167.164 1.00 121.52 ? 1679 ARG A CA    1 
ATOM   1826  C  C     . ARG A 1 1679 ? 193.384 204.235 168.403 1.00 122.40 ? 1679 ARG A C     1 
ATOM   1827  O  O     . ARG A 1 1679 ? 192.634 205.159 168.736 1.00 123.20 ? 1679 ARG A O     1 
ATOM   1828  C  CB    . ARG A 1 1679 ? 192.110 202.267 167.535 1.00 120.69 ? 1679 ARG A CB    1 
ATOM   1829  C  CG    . ARG A 1 1679 ? 192.765 201.140 168.317 1.00 120.86 ? 1679 ARG A CG    1 
ATOM   1830  C  CD    . ARG A 1 1679 ? 192.250 199.786 167.857 1.00 123.22 ? 1679 ARG A CD    1 
ATOM   1831  N  NE    . ARG A 1 1679 ? 192.677 199.472 166.499 1.00 126.77 ? 1679 ARG A NE    1 
ATOM   1832  C  CZ    . ARG A 1 1679 ? 192.099 198.568 165.721 1.00 125.95 ? 1679 ARG A CZ    1 
ATOM   1833  N  NH1   . ARG A 1 1679 ? 191.062 197.860 166.138 1.00 124.06 ? 1679 ARG A NH1   1 
ATOM   1834  N  NH2   . ARG A 1 1679 ? 192.573 198.368 164.495 1.00 122.32 ? 1679 ARG A NH2   1 
ATOM   1835  N  N     . GLU A 1 1680 ? 194.481 203.925 169.086 1.00 118.69 ? 1680 GLU A N     1 
ATOM   1836  C  CA    . GLU A 1 1680 ? 194.943 204.704 170.226 1.00 120.60 ? 1680 GLU A CA    1 
ATOM   1837  C  C     . GLU A 1 1680 ? 195.508 206.057 169.812 1.00 122.03 ? 1680 GLU A C     1 
ATOM   1838  O  O     . GLU A 1 1680 ? 195.307 207.045 170.526 1.00 123.76 ? 1680 GLU A O     1 
ATOM   1839  C  CB    . GLU A 1 1680 ? 195.998 203.898 171.002 1.00 119.04 ? 1680 GLU A CB    1 
ATOM   1840  C  CG    . GLU A 1 1680 ? 197.062 204.695 171.769 1.00 122.10 ? 1680 GLU A CG    1 
ATOM   1841  C  CD    . GLU A 1 1680 ? 196.498 205.692 172.772 1.00 124.34 ? 1680 GLU A CD    1 
ATOM   1842  O  OE1   . GLU A 1 1680 ? 195.326 205.549 173.179 1.00 125.41 ? 1680 GLU A OE1   1 
ATOM   1843  O  OE2   . GLU A 1 1680 ? 197.231 206.633 173.144 1.00 121.42 ? 1680 GLU A OE2   1 
ATOM   1844  N  N     . GLY A 1 1681 ? 196.167 206.133 168.659 1.00 112.89 ? 1681 GLY A N     1 
ATOM   1845  C  CA    . GLY A 1 1681 ? 196.825 207.343 168.222 1.00 114.33 ? 1681 GLY A CA    1 
ATOM   1846  C  C     . GLY A 1 1681 ? 198.305 207.196 167.948 1.00 114.86 ? 1681 GLY A C     1 
ATOM   1847  O  O     . GLY A 1 1681 ? 198.923 208.144 167.449 1.00 113.33 ? 1681 GLY A O     1 
ATOM   1848  N  N     . GLU A 1 1682 ? 198.888 206.042 168.259 1.00 108.74 ? 1682 GLU A N     1 
ATOM   1849  C  CA    . GLU A 1 1682 ? 200.290 205.796 167.956 1.00 108.00 ? 1682 GLU A CA    1 
ATOM   1850  C  C     . GLU A 1 1682 ? 200.513 205.810 166.449 1.00 107.25 ? 1682 GLU A C     1 
ATOM   1851  O  O     . GLU A 1 1682 ? 199.752 205.210 165.686 1.00 109.14 ? 1682 GLU A O     1 
ATOM   1852  C  CB    . GLU A 1 1682 ? 200.722 204.456 168.548 1.00 109.39 ? 1682 GLU A CB    1 
ATOM   1853  C  CG    . GLU A 1 1682 ? 202.217 204.217 168.558 1.00 106.38 ? 1682 GLU A CG    1 
ATOM   1854  C  CD    . GLU A 1 1682 ? 202.569 202.814 169.008 1.00 109.94 ? 1682 GLU A CD    1 
ATOM   1855  O  OE1   . GLU A 1 1682 ? 202.319 201.862 168.241 1.00 110.11 ? 1682 GLU A OE1   1 
ATOM   1856  O  OE2   . GLU A 1 1682 ? 203.089 202.663 170.133 1.00 109.23 ? 1682 GLU A OE2   1 
ATOM   1857  N  N     . GLU A 1 1683 ? 201.566 206.501 166.020 1.00 111.74 ? 1683 GLU A N     1 
ATOM   1858  C  CA    . GLU A 1 1683 ? 201.836 206.720 164.607 1.00 111.55 ? 1683 GLU A CA    1 
ATOM   1859  C  C     . GLU A 1 1683 ? 203.172 206.104 164.220 1.00 111.25 ? 1683 GLU A C     1 
ATOM   1860  O  O     . GLU A 1 1683 ? 204.125 206.115 165.005 1.00 113.64 ? 1683 GLU A O     1 
ATOM   1861  C  CB    . GLU A 1 1683 ? 201.846 208.215 164.272 1.00 110.86 ? 1683 GLU A CB    1 
ATOM   1862  C  CG    . GLU A 1 1683 ? 200.566 208.949 164.635 1.00 114.82 ? 1683 GLU A CG    1 
ATOM   1863  C  CD    . GLU A 1 1683 ? 200.763 210.450 164.717 1.00 117.64 ? 1683 GLU A CD    1 
ATOM   1864  O  OE1   . GLU A 1 1683 ? 200.746 211.113 163.658 1.00 117.43 ? 1683 GLU A OE1   1 
ATOM   1865  O  OE2   . GLU A 1 1683 ? 200.937 210.968 165.840 1.00 117.17 ? 1683 GLU A OE2   1 
ATOM   1866  N  N     . VAL A 1 1684 ? 203.232 205.568 163.004 1.00 98.94  ? 1684 VAL A N     1 
ATOM   1867  C  CA    . VAL A 1 1684 ? 204.463 205.057 162.414 1.00 98.10  ? 1684 VAL A CA    1 
ATOM   1868  C  C     . VAL A 1 1684 ? 204.728 205.864 161.152 1.00 100.66 ? 1684 VAL A C     1 
ATOM   1869  O  O     . VAL A 1 1684 ? 203.889 205.894 160.243 1.00 102.78 ? 1684 VAL A O     1 
ATOM   1870  C  CB    . VAL A 1 1684 ? 204.370 203.556 162.097 1.00 96.19  ? 1684 VAL A CB    1 
ATOM   1871  C  CG1   . VAL A 1 1684 ? 205.459 203.151 161.119 1.00 95.57  ? 1684 VAL A CG1   1 
ATOM   1872  C  CG2   . VAL A 1 1684 ? 204.460 202.738 163.373 1.00 98.74  ? 1684 VAL A CG2   1 
ATOM   1873  N  N     . MET A 1 1685 ? 205.887 206.514 161.092 1.00 103.19 ? 1685 MET A N     1 
ATOM   1874  C  CA    . MET A 1 1685 ? 206.241 207.381 159.977 1.00 99.66  ? 1685 MET A CA    1 
ATOM   1875  C  C     . MET A 1 1685 ? 207.106 206.606 158.991 1.00 102.23 ? 1685 MET A C     1 
ATOM   1876  O  O     . MET A 1 1685 ? 208.164 206.087 159.361 1.00 102.82 ? 1685 MET A O     1 
ATOM   1877  C  CB    . MET A 1 1685 ? 206.971 208.631 160.467 1.00 100.97 ? 1685 MET A CB    1 
ATOM   1878  C  CG    . MET A 1 1685 ? 206.052 209.677 161.075 1.00 105.48 ? 1685 MET A CG    1 
ATOM   1879  S  SD    . MET A 1 1685 ? 204.523 209.878 160.142 1.00 117.02 ? 1685 MET A SD    1 
ATOM   1880  C  CE    . MET A 1 1685 ? 204.113 211.578 160.522 1.00 106.17 ? 1685 MET A CE    1 
ATOM   1881  N  N     . PHE A 1 1686 ? 206.652 206.530 157.743 1.00 105.07 ? 1686 PHE A N     1 
ATOM   1882  C  CA    . PHE A 1 1686 ? 207.371 205.778 156.724 1.00 103.95 ? 1686 PHE A CA    1 
ATOM   1883  C  C     . PHE A 1 1686 ? 208.700 206.450 156.403 1.00 105.17 ? 1686 PHE A C     1 
ATOM   1884  O  O     . PHE A 1 1686 ? 208.784 207.676 156.292 1.00 104.78 ? 1686 PHE A O     1 
ATOM   1885  C  CB    . PHE A 1 1686 ? 206.530 205.664 155.450 1.00 102.67 ? 1686 PHE A CB    1 
ATOM   1886  C  CG    . PHE A 1 1686 ? 205.335 204.755 155.576 1.00 99.33  ? 1686 PHE A CG    1 
ATOM   1887  C  CD1   . PHE A 1 1686 ? 205.000 204.176 156.787 1.00 103.39 ? 1686 PHE A CD1   1 
ATOM   1888  C  CD2   . PHE A 1 1686 ? 204.542 204.489 154.473 1.00 99.30  ? 1686 PHE A CD2   1 
ATOM   1889  C  CE1   . PHE A 1 1686 ? 203.901 203.348 156.895 1.00 107.72 ? 1686 PHE A CE1   1 
ATOM   1890  C  CE2   . PHE A 1 1686 ? 203.443 203.662 154.575 1.00 102.92 ? 1686 PHE A CE2   1 
ATOM   1891  C  CZ    . PHE A 1 1686 ? 203.122 203.091 155.787 1.00 106.89 ? 1686 PHE A CZ    1 
ATOM   1892  N  N     . LYS A 1 1687 ? 209.748 205.636 156.257 1.00 109.13 ? 1687 LYS A N     1 
ATOM   1893  C  CA    . LYS A 1 1687 ? 211.031 206.172 155.813 1.00 108.68 ? 1687 LYS A CA    1 
ATOM   1894  C  C     . LYS A 1 1687 ? 210.955 206.651 154.369 1.00 111.49 ? 1687 LYS A C     1 
ATOM   1895  O  O     . LYS A 1 1687 ? 211.501 207.708 154.030 1.00 112.57 ? 1687 LYS A O     1 
ATOM   1896  C  CB    . LYS A 1 1687 ? 212.128 205.121 155.977 1.00 106.59 ? 1687 LYS A CB    1 
ATOM   1897  C  CG    . LYS A 1 1687 ? 211.936 204.204 157.170 1.00 108.30 ? 1687 LYS A CG    1 
ATOM   1898  C  CD    . LYS A 1 1687 ? 212.223 204.935 158.471 1.00 107.22 ? 1687 LYS A CD    1 
ATOM   1899  C  CE    . LYS A 1 1687 ? 213.663 204.737 158.911 1.00 107.86 ? 1687 LYS A CE    1 
ATOM   1900  N  NZ    . LYS A 1 1687 ? 213.896 205.249 160.289 1.00 108.67 ? 1687 LYS A NZ    1 
ATOM   1901  N  N     . THR A 1 1688 ? 210.284 205.893 153.508 1.00 109.79 ? 1688 THR A N     1 
ATOM   1902  C  CA    . THR A 1 1688 ? 210.060 206.288 152.117 1.00 108.50 ? 1688 THR A CA    1 
ATOM   1903  C  C     . THR A 1 1688 ? 208.560 206.465 151.921 1.00 111.32 ? 1688 THR A C     1 
ATOM   1904  O  O     . THR A 1 1688 ? 207.814 205.471 151.872 1.00 113.32 ? 1688 THR A O     1 
ATOM   1905  C  CB    . THR A 1 1688 ? 210.626 205.251 151.146 1.00 109.91 ? 1688 THR A CB    1 
ATOM   1906  O  OG1   . THR A 1 1688 ? 212.035 205.461 151.000 1.00 111.73 ? 1688 THR A OG1   1 
ATOM   1907  C  CG2   . THR A 1 1688 ? 209.983 205.383 149.769 1.00 110.87 ? 1688 THR A CG2   1 
ATOM   1908  N  N     . PRO A 1 1689 ? 208.066 207.698 151.854 1.00 106.32 ? 1689 PRO A N     1 
ATOM   1909  C  CA    . PRO A 1 1689 ? 206.621 207.903 151.699 1.00 105.48 ? 1689 PRO A CA    1 
ATOM   1910  C  C     . PRO A 1 1689 ? 206.110 207.345 150.378 1.00 103.95 ? 1689 PRO A C     1 
ATOM   1911  O  O     . PRO A 1 1689 ? 206.817 207.340 149.368 1.00 103.60 ? 1689 PRO A O     1 
ATOM   1912  C  CB    . PRO A 1 1689 ? 206.471 209.427 151.766 1.00 101.84 ? 1689 PRO A CB    1 
ATOM   1913  C  CG    . PRO A 1 1689 ? 207.710 209.910 152.445 1.00 102.40 ? 1689 PRO A CG    1 
ATOM   1914  C  CD    . PRO A 1 1689 ? 208.791 208.965 152.031 1.00 102.92 ? 1689 PRO A CD    1 
ATOM   1915  N  N     . VAL A 1 1690 ? 204.870 206.868 150.399 1.00 106.70 ? 1690 VAL A N     1 
ATOM   1916  C  CA    . VAL A 1 1690 ? 204.226 206.308 149.216 1.00 106.72 ? 1690 VAL A CA    1 
ATOM   1917  C  C     . VAL A 1 1690 ? 203.317 207.368 148.609 1.00 110.64 ? 1690 VAL A C     1 
ATOM   1918  O  O     . VAL A 1 1690 ? 202.485 207.961 149.307 1.00 111.73 ? 1690 VAL A O     1 
ATOM   1919  C  CB    . VAL A 1 1690 ? 203.437 205.037 149.571 1.00 108.03 ? 1690 VAL A CB    1 
ATOM   1920  C  CG1   . VAL A 1 1690 ? 202.304 204.810 148.580 1.00 106.96 ? 1690 VAL A CG1   1 
ATOM   1921  C  CG2   . VAL A 1 1690 ? 204.363 203.833 149.610 1.00 111.16 ? 1690 VAL A CG2   1 
ATOM   1922  N  N     . SER A 1 1691 ? 203.475 207.610 147.311 1.00 118.51 ? 1691 SER A N     1 
ATOM   1923  C  CA    . SER A 1 1691 ? 202.717 208.632 146.602 1.00 115.98 ? 1691 SER A CA    1 
ATOM   1924  C  C     . SER A 1 1691 ? 201.612 207.979 145.783 1.00 116.38 ? 1691 SER A C     1 
ATOM   1925  O  O     . SER A 1 1691 ? 201.873 207.063 144.997 1.00 115.63 ? 1691 SER A O     1 
ATOM   1926  C  CB    . SER A 1 1691 ? 203.633 209.452 145.692 1.00 117.20 ? 1691 SER A CB    1 
ATOM   1927  O  OG    . SER A 1 1691 ? 204.544 208.613 145.003 1.00 118.32 ? 1691 SER A OG    1 
ATOM   1928  N  N     . ILE A 1 1692 ? 200.379 208.455 145.968 1.00 117.75 ? 1692 ILE A N     1 
ATOM   1929  C  CA    . ILE A 1 1692 ? 199.254 207.871 145.247 1.00 119.40 ? 1692 ILE A CA    1 
ATOM   1930  C  C     . ILE A 1 1692 ? 199.157 208.424 143.830 1.00 120.69 ? 1692 ILE A C     1 
ATOM   1931  O  O     . ILE A 1 1692 ? 198.492 207.830 142.974 1.00 120.32 ? 1692 ILE A O     1 
ATOM   1932  C  CB    . ILE A 1 1692 ? 197.945 208.092 146.024 1.00 117.39 ? 1692 ILE A CB    1 
ATOM   1933  C  CG1   . ILE A 1 1692 ? 197.413 209.506 145.793 1.00 117.06 ? 1692 ILE A CG1   1 
ATOM   1934  C  CG2   . ILE A 1 1692 ? 198.158 207.842 147.508 1.00 116.27 ? 1692 ILE A CG2   1 
ATOM   1935  C  CD1   . ILE A 1 1692 ? 195.903 209.601 145.800 1.00 117.63 ? 1692 ILE A CD1   1 
ATOM   1936  N  N     . THR A 1 1693 ? 199.798 209.564 143.556 1.00 134.51 ? 1693 THR A N     1 
ATOM   1937  C  CA    . THR A 1 1693 ? 199.781 210.112 142.203 1.00 133.91 ? 1693 THR A CA    1 
ATOM   1938  C  C     . THR A 1 1693 ? 200.515 209.199 141.229 1.00 133.60 ? 1693 THR A C     1 
ATOM   1939  O  O     . THR A 1 1693 ? 200.059 208.986 140.100 1.00 134.97 ? 1693 THR A O     1 
ATOM   1940  C  CB    . THR A 1 1693 ? 200.398 211.510 142.189 1.00 132.91 ? 1693 THR A CB    1 
ATOM   1941  O  OG1   . THR A 1 1693 ? 201.681 211.474 142.826 1.00 133.59 ? 1693 THR A OG1   1 
ATOM   1942  C  CG2   . THR A 1 1693 ? 199.500 212.494 142.920 1.00 131.07 ? 1693 THR A CG2   1 
ATOM   1943  N  N     . GLU A 1 1694 ? 201.658 208.653 141.649 1.00 132.66 ? 1694 GLU A N     1 
ATOM   1944  C  CA    . GLU A 1 1694 ? 202.408 207.749 140.785 1.00 133.74 ? 1694 GLU A CA    1 
ATOM   1945  C  C     . GLU A 1 1694 ? 201.677 206.426 140.591 1.00 135.92 ? 1694 GLU A C     1 
ATOM   1946  O  O     . GLU A 1 1694 ? 201.790 205.806 139.528 1.00 137.01 ? 1694 GLU A O     1 
ATOM   1947  C  CB    . GLU A 1 1694 ? 203.808 207.523 141.365 1.00 132.38 ? 1694 GLU A CB    1 
ATOM   1948  C  CG    . GLU A 1 1694 ? 204.569 206.331 140.797 1.00 135.18 ? 1694 GLU A CG    1 
ATOM   1949  C  CD    . GLU A 1 1694 ? 204.797 206.420 139.298 1.00 137.14 ? 1694 GLU A CD    1 
ATOM   1950  O  OE1   . GLU A 1 1694 ? 205.056 205.368 138.677 1.00 135.93 ? 1694 GLU A OE1   1 
ATOM   1951  O  OE2   . GLU A 1 1694 ? 204.741 207.538 138.743 1.00 139.01 ? 1694 GLU A OE2   1 
ATOM   1952  N  N     . HIS A 1 1695 ? 200.905 205.994 141.587 1.00 130.60 ? 1695 HIS A N     1 
ATOM   1953  C  CA    . HIS A 1 1695 ? 200.174 204.728 141.543 1.00 127.69 ? 1695 HIS A CA    1 
ATOM   1954  C  C     . HIS A 1 1695 ? 198.702 205.016 141.802 1.00 128.55 ? 1695 HIS A C     1 
ATOM   1955  O  O     . HIS A 1 1695 ? 198.203 204.813 142.917 1.00 132.03 ? 1695 HIS A O     1 
ATOM   1956  C  CB    . HIS A 1 1695 ? 200.728 203.733 142.561 1.00 129.22 ? 1695 HIS A CB    1 
ATOM   1957  C  CG    . HIS A 1 1695 ? 202.224 203.688 142.611 1.00 130.42 ? 1695 HIS A CG    1 
ATOM   1958  N  ND1   . HIS A 1 1695 ? 202.968 202.820 141.841 1.00 128.70 ? 1695 HIS A ND1   1 
ATOM   1959  C  CD2   . HIS A 1 1695 ? 203.113 204.404 143.337 1.00 131.27 ? 1695 HIS A CD2   1 
ATOM   1960  C  CE1   . HIS A 1 1695 ? 204.252 203.003 142.092 1.00 128.00 ? 1695 HIS A CE1   1 
ATOM   1961  N  NE2   . HIS A 1 1695 ? 204.367 203.957 142.998 1.00 129.99 ? 1695 HIS A NE2   1 
ATOM   1962  N  N     . PRO A 1 1696 ? 197.976 205.502 140.791 1.00 127.27 ? 1696 PRO A N     1 
ATOM   1963  C  CA    . PRO A 1 1696 ? 196.560 205.847 141.003 1.00 128.53 ? 1696 PRO A CA    1 
ATOM   1964  C  C     . PRO A 1 1696 ? 195.697 204.670 141.420 1.00 129.69 ? 1696 PRO A C     1 
ATOM   1965  O  O     . PRO A 1 1696 ? 194.695 204.870 142.120 1.00 129.57 ? 1696 PRO A O     1 
ATOM   1966  C  CB    . PRO A 1 1696 ? 196.127 206.409 139.641 1.00 127.82 ? 1696 PRO A CB    1 
ATOM   1967  C  CG    . PRO A 1 1696 ? 197.402 206.770 138.940 1.00 127.72 ? 1696 PRO A CG    1 
ATOM   1968  C  CD    . PRO A 1 1696 ? 198.413 205.777 139.413 1.00 127.55 ? 1696 PRO A CD    1 
ATOM   1969  N  N     . LYS A 1 1697 ? 196.041 203.452 141.005 1.00 124.70 ? 1697 LYS A N     1 
ATOM   1970  C  CA    . LYS A 1 1697 ? 195.244 202.289 141.368 1.00 123.24 ? 1697 LYS A CA    1 
ATOM   1971  C  C     . LYS A 1 1697 ? 195.269 202.070 142.876 1.00 126.09 ? 1697 LYS A C     1 
ATOM   1972  O  O     . LYS A 1 1697 ? 196.323 202.136 143.513 1.00 125.50 ? 1697 LYS A O     1 
ATOM   1973  C  CB    . LYS A 1 1697 ? 195.757 201.044 140.645 1.00 122.60 ? 1697 LYS A CB    1 
ATOM   1974  C  CG    . LYS A 1 1697 ? 195.161 200.847 139.262 1.00 123.15 ? 1697 LYS A CG    1 
ATOM   1975  C  CD    . LYS A 1 1697 ? 195.235 199.392 138.832 1.00 124.72 ? 1697 LYS A CD    1 
ATOM   1976  C  CE    . LYS A 1 1697 ? 194.103 198.580 139.442 1.00 123.80 ? 1697 LYS A CE    1 
ATOM   1977  N  NZ    . LYS A 1 1697 ? 192.773 199.192 139.174 1.00 123.61 ? 1697 LYS A NZ    1 
ATOM   1978  N  N     . ILE A 1 1698 ? 194.090 201.801 143.442 1.00 122.04 ? 1698 ILE A N     1 
ATOM   1979  C  CA    . ILE A 1 1698 ? 193.960 201.670 144.892 1.00 118.44 ? 1698 ILE A CA    1 
ATOM   1980  C  C     . ILE A 1 1698 ? 194.782 200.492 145.403 1.00 117.99 ? 1698 ILE A C     1 
ATOM   1981  O  O     . ILE A 1 1698 ? 195.513 200.604 146.396 1.00 123.05 ? 1698 ILE A O     1 
ATOM   1982  C  CB    . ILE A 1 1698 ? 192.475 201.544 145.283 1.00 117.67 ? 1698 ILE A CB    1 
ATOM   1983  C  CG1   . ILE A 1 1698 ? 192.324 201.181 146.762 1.00 117.51 ? 1698 ILE A CG1   1 
ATOM   1984  C  CG2   . ILE A 1 1698 ? 191.759 200.542 144.386 1.00 118.89 ? 1698 ILE A CG2   1 
ATOM   1985  C  CD1   . ILE A 1 1698 ? 192.707 202.290 147.706 1.00 118.99 ? 1698 ILE A CD1   1 
ATOM   1986  N  N     . ASN A 1 1699 ? 194.691 199.348 144.720 1.00 117.50 ? 1699 ASN A N     1 
ATOM   1987  C  CA    . ASN A 1 1699 ? 195.374 198.148 145.190 1.00 121.15 ? 1699 ASN A CA    1 
ATOM   1988  C  C     . ASN A 1 1699 ? 196.888 198.307 145.135 1.00 120.89 ? 1699 ASN A C     1 
ATOM   1989  O  O     . ASN A 1 1699 ? 197.599 197.832 146.027 1.00 123.51 ? 1699 ASN A O     1 
ATOM   1990  C  CB    . ASN A 1 1699 ? 194.926 196.935 144.374 1.00 120.56 ? 1699 ASN A CB    1 
ATOM   1991  C  CG    . ASN A 1 1699 ? 195.102 197.137 142.882 1.00 121.18 ? 1699 ASN A CG    1 
ATOM   1992  O  OD1   . ASN A 1 1699 ? 195.647 198.147 142.438 1.00 123.85 ? 1699 ASN A OD1   1 
ATOM   1993  N  ND2   . ASN A 1 1699 ? 194.637 196.172 142.098 1.00 120.20 ? 1699 ASN A ND2   1 
ATOM   1994  N  N     . GLU A 1 1700 ? 197.397 198.979 144.100 1.00 120.34 ? 1700 GLU A N     1 
ATOM   1995  C  CA    . GLU A 1 1700 ? 198.841 199.124 143.950 1.00 121.72 ? 1700 GLU A CA    1 
ATOM   1996  C  C     . GLU A 1 1700 ? 199.438 199.925 145.101 1.00 123.43 ? 1700 GLU A C     1 
ATOM   1997  O  O     . GLU A 1 1700 ? 200.400 199.488 145.746 1.00 123.83 ? 1700 GLU A O     1 
ATOM   1998  C  CB    . GLU A 1 1700 ? 199.163 199.782 142.609 1.00 122.85 ? 1700 GLU A CB    1 
ATOM   1999  C  CG    . GLU A 1 1700 ? 200.637 200.083 142.402 1.00 125.55 ? 1700 GLU A CG    1 
ATOM   2000  C  CD    . GLU A 1 1700 ? 201.383 198.930 141.762 1.00 125.38 ? 1700 GLU A CD    1 
ATOM   2001  O  OE1   . GLU A 1 1700 ? 200.798 197.833 141.644 1.00 125.75 ? 1700 GLU A OE1   1 
ATOM   2002  O  OE2   . GLU A 1 1700 ? 202.554 199.122 141.374 1.00 122.77 ? 1700 GLU A OE2   1 
ATOM   2003  N  N     . TRP A 1 1701 ? 198.874 201.101 145.386 1.00 113.85 ? 1701 TRP A N     1 
ATOM   2004  C  CA    . TRP A 1 1701 ? 199.418 201.900 146.475 1.00 112.67 ? 1701 TRP A CA    1 
ATOM   2005  C  C     . TRP A 1 1701 ? 199.073 201.324 147.840 1.00 113.16 ? 1701 TRP A C     1 
ATOM   2006  O  O     . TRP A 1 1701 ? 199.819 201.556 148.792 1.00 113.05 ? 1701 TRP A O     1 
ATOM   2007  C  CB    . TRP A 1 1701 ? 198.963 203.361 146.366 1.00 107.71 ? 1701 TRP A CB    1 
ATOM   2008  C  CG    . TRP A 1 1701 ? 197.558 203.662 146.796 1.00 106.82 ? 1701 TRP A CG    1 
ATOM   2009  C  CD1   . TRP A 1 1701 ? 196.460 203.753 145.994 1.00 106.34 ? 1701 TRP A CD1   1 
ATOM   2010  C  CD2   . TRP A 1 1701 ? 197.111 203.974 148.122 1.00 106.65 ? 1701 TRP A CD2   1 
ATOM   2011  N  NE1   . TRP A 1 1701 ? 195.353 204.072 146.740 1.00 105.76 ? 1701 TRP A NE1   1 
ATOM   2012  C  CE2   . TRP A 1 1701 ? 195.726 204.214 148.050 1.00 106.05 ? 1701 TRP A CE2   1 
ATOM   2013  C  CE3   . TRP A 1 1701 ? 197.746 204.058 149.364 1.00 109.02 ? 1701 TRP A CE3   1 
ATOM   2014  C  CZ2   . TRP A 1 1701 ? 194.965 204.534 149.171 1.00 107.87 ? 1701 TRP A CZ2   1 
ATOM   2015  C  CZ3   . TRP A 1 1701 ? 196.988 204.375 150.476 1.00 109.75 ? 1701 TRP A CZ3   1 
ATOM   2016  C  CH2   . TRP A 1 1701 ? 195.612 204.608 150.372 1.00 109.09 ? 1701 TRP A CH2   1 
ATOM   2017  N  N     . LEU A 1 1702 ? 197.993 200.546 147.957 1.00 110.83 ? 1702 LEU A N     1 
ATOM   2018  C  CA    . LEU A 1 1702 ? 197.758 199.822 149.203 1.00 107.47 ? 1702 LEU A CA    1 
ATOM   2019  C  C     . LEU A 1 1702 ? 198.850 198.786 149.454 1.00 110.89 ? 1702 LEU A C     1 
ATOM   2020  O  O     . LEU A 1 1702 ? 199.362 198.667 150.575 1.00 117.53 ? 1702 LEU A O     1 
ATOM   2021  C  CB    . LEU A 1 1702 ? 196.382 199.160 149.175 1.00 107.33 ? 1702 LEU A CB    1 
ATOM   2022  C  CG    . LEU A 1 1702 ? 195.226 200.000 149.719 1.00 109.98 ? 1702 LEU A CG    1 
ATOM   2023  C  CD1   . LEU A 1 1702 ? 193.925 199.217 149.674 1.00 108.74 ? 1702 LEU A CD1   1 
ATOM   2024  C  CD2   . LEU A 1 1702 ? 195.525 200.472 151.131 1.00 112.95 ? 1702 LEU A CD2   1 
ATOM   2025  N  N     . THR A 1 1703 ? 199.225 198.031 148.417 1.00 109.01 ? 1703 THR A N     1 
ATOM   2026  C  CA    . THR A 1 1703 ? 200.315 197.070 148.551 1.00 111.05 ? 1703 THR A CA    1 
ATOM   2027  C  C     . THR A 1 1703 ? 201.629 197.774 148.860 1.00 111.01 ? 1703 THR A C     1 
ATOM   2028  O  O     . THR A 1 1703 ? 202.441 197.279 149.654 1.00 117.22 ? 1703 THR A O     1 
ATOM   2029  C  CB    . THR A 1 1703 ? 200.446 196.238 147.276 1.00 110.45 ? 1703 THR A CB    1 
ATOM   2030  O  OG1   . THR A 1 1703 ? 199.160 195.736 146.893 1.00 114.06 ? 1703 THR A OG1   1 
ATOM   2031  C  CG2   . THR A 1 1703 ? 201.393 195.069 147.498 1.00 108.09 ? 1703 THR A CG2   1 
ATOM   2032  N  N     . LEU A 1 1704 ? 201.865 198.922 148.223 1.00 106.22 ? 1704 LEU A N     1 
ATOM   2033  C  CA    . LEU A 1 1704 ? 203.066 199.695 148.519 1.00 108.45 ? 1704 LEU A CA    1 
ATOM   2034  C  C     . LEU A 1 1704 ? 203.073 200.173 149.965 1.00 110.08 ? 1704 LEU A C     1 
ATOM   2035  O  O     . LEU A 1 1704 ? 204.117 200.156 150.625 1.00 109.81 ? 1704 LEU A O     1 
ATOM   2036  C  CB    . LEU A 1 1704 ? 203.182 200.877 147.562 1.00 110.90 ? 1704 LEU A CB    1 
ATOM   2037  C  CG    . LEU A 1 1704 ? 203.835 200.548 146.222 1.00 110.73 ? 1704 LEU A CG    1 
ATOM   2038  C  CD1   . LEU A 1 1704 ? 203.421 201.563 145.179 1.00 111.25 ? 1704 LEU A CD1   1 
ATOM   2039  C  CD2   . LEU A 1 1704 ? 205.347 200.504 146.366 1.00 109.09 ? 1704 LEU A CD2   1 
ATOM   2040  N  N     . VAL A 1 1705 ? 201.917 200.605 150.473 1.00 106.40 ? 1705 VAL A N     1 
ATOM   2041  C  CA    . VAL A 1 1705 ? 201.819 201.013 151.871 1.00 106.03 ? 1705 VAL A CA    1 
ATOM   2042  C  C     . VAL A 1 1705 ? 202.127 199.839 152.788 1.00 108.24 ? 1705 VAL A C     1 
ATOM   2043  O  O     . VAL A 1 1705 ? 202.812 199.993 153.802 1.00 110.35 ? 1705 VAL A O     1 
ATOM   2044  C  CB    . VAL A 1 1705 ? 200.430 201.614 152.159 1.00 104.13 ? 1705 VAL A CB    1 
ATOM   2045  C  CG1   . VAL A 1 1705 ? 200.146 201.624 153.652 1.00 102.40 ? 1705 VAL A CG1   1 
ATOM   2046  C  CG2   . VAL A 1 1705 ? 200.341 203.024 151.601 1.00 107.51 ? 1705 VAL A CG2   1 
ATOM   2047  N  N     . GLU A 1 1706 ? 201.626 198.650 152.449 1.00 106.91 ? 1706 GLU A N     1 
ATOM   2048  C  CA    . GLU A 1 1706 ? 201.909 197.474 153.271 1.00 102.97 ? 1706 GLU A CA    1 
ATOM   2049  C  C     . GLU A 1 1706 ? 203.400 197.144 153.285 1.00 101.36 ? 1706 GLU A C     1 
ATOM   2050  O  O     . GLU A 1 1706 ? 203.990 196.914 154.351 1.00 107.70 ? 1706 GLU A O     1 
ATOM   2051  C  CB    . GLU A 1 1706 ? 201.092 196.284 152.770 1.00 102.86 ? 1706 GLU A CB    1 
ATOM   2052  C  CG    . GLU A 1 1706 ? 201.632 194.930 153.188 1.00 107.69 ? 1706 GLU A CG    1 
ATOM   2053  C  CD    . GLU A 1 1706 ? 200.724 193.789 152.769 1.00 111.94 ? 1706 GLU A CD    1 
ATOM   2054  O  OE1   . GLU A 1 1706 ? 200.212 193.818 151.630 1.00 110.35 ? 1706 GLU A OE1   1 
ATOM   2055  O  OE2   . GLU A 1 1706 ? 200.524 192.860 153.579 1.00 111.26 ? 1706 GLU A OE2   1 
ATOM   2056  N  N     . LYS A 1 1707 ? 204.030 197.113 152.110 1.00 100.57 ? 1707 LYS A N     1 
ATOM   2057  C  CA    . LYS A 1 1707 ? 205.454 196.796 152.063 1.00 104.50 ? 1707 LYS A CA    1 
ATOM   2058  C  C     . LYS A 1 1707 ? 206.275 197.854 152.792 1.00 105.36 ? 1707 LYS A C     1 
ATOM   2059  O  O     . LYS A 1 1707 ? 207.233 197.528 153.507 1.00 110.02 ? 1707 LYS A O     1 
ATOM   2060  C  CB    . LYS A 1 1707 ? 205.917 196.645 150.614 1.00 106.73 ? 1707 LYS A CB    1 
ATOM   2061  C  CG    . LYS A 1 1707 ? 207.425 196.743 150.428 1.00 106.17 ? 1707 LYS A CG    1 
ATOM   2062  C  CD    . LYS A 1 1707 ? 208.126 195.554 151.070 1.00 105.67 ? 1707 LYS A CD    1 
ATOM   2063  C  CE    . LYS A 1 1707 ? 207.518 194.239 150.611 1.00 105.20 ? 1707 LYS A CE    1 
ATOM   2064  N  NZ    . LYS A 1 1707 ? 208.272 193.061 151.119 1.00 104.39 ? 1707 LYS A NZ    1 
ATOM   2065  N  N     . GLU A 1 1708 ? 205.910 199.128 152.631 1.00 100.62 ? 1708 GLU A N     1 
ATOM   2066  C  CA    . GLU A 1 1708 ? 206.614 200.192 153.332 1.00 101.70 ? 1708 GLU A CA    1 
ATOM   2067  C  C     . GLU A 1 1708 ? 206.408 200.098 154.835 1.00 101.22 ? 1708 GLU A C     1 
ATOM   2068  O  O     . GLU A 1 1708 ? 207.334 200.378 155.599 1.00 102.67 ? 1708 GLU A O     1 
ATOM   2069  C  CB    . GLU A 1 1708 ? 206.155 201.556 152.822 1.00 106.44 ? 1708 GLU A CB    1 
ATOM   2070  C  CG    . GLU A 1 1708 ? 207.219 202.635 152.894 1.00 110.53 ? 1708 GLU A CG    1 
ATOM   2071  C  CD    . GLU A 1 1708 ? 208.530 202.207 152.258 1.00 110.09 ? 1708 GLU A CD    1 
ATOM   2072  O  OE1   . GLU A 1 1708 ? 208.539 201.923 151.041 1.00 108.94 ? 1708 GLU A OE1   1 
ATOM   2073  O  OE2   . GLU A 1 1708 ? 209.554 202.164 152.972 1.00 105.60 ? 1708 GLU A OE2   1 
ATOM   2074  N  N     . MET A 1 1709 ? 205.207 199.719 155.274 1.00 93.42  ? 1709 MET A N     1 
ATOM   2075  C  CA    . MET A 1 1709 ? 204.942 199.536 156.696 1.00 91.58  ? 1709 MET A CA    1 
ATOM   2076  C  C     . MET A 1 1709 ? 205.850 198.459 157.272 1.00 94.23  ? 1709 MET A C     1 
ATOM   2077  O  O     . MET A 1 1709 ? 206.479 198.653 158.321 1.00 95.43  ? 1709 MET A O     1 
ATOM   2078  C  CB    . MET A 1 1709 ? 203.452 199.211 156.888 1.00 91.85  ? 1709 MET A CB    1 
ATOM   2079  C  CG    . MET A 1 1709 ? 203.090 197.744 157.115 1.00 93.37  ? 1709 MET A CG    1 
ATOM   2080  S  SD    . MET A 1 1709 ? 201.321 197.459 157.272 1.00 104.35 ? 1709 MET A SD    1 
ATOM   2081  C  CE    . MET A 1 1709 ? 201.128 197.571 159.029 1.00 97.20  ? 1709 MET A CE    1 
ATOM   2082  N  N     . ARG A 1 1710 ? 205.989 197.343 156.551 1.00 97.52  ? 1710 ARG A N     1 
ATOM   2083  C  CA    . ARG A 1 1710 ? 206.881 196.280 157.004 1.00 90.47  ? 1710 ARG A CA    1 
ATOM   2084  C  C     . ARG A 1 1710 ? 208.327 196.759 157.070 1.00 93.39  ? 1710 ARG A C     1 
ATOM   2085  O  O     . ARG A 1 1710 ? 209.014 196.558 158.082 1.00 97.03  ? 1710 ARG A O     1 
ATOM   2086  C  CB    . ARG A 1 1710 ? 206.754 195.072 156.078 1.00 88.63  ? 1710 ARG A CB    1 
ATOM   2087  C  CG    . ARG A 1 1710 ? 205.663 194.107 156.486 1.00 88.43  ? 1710 ARG A CG    1 
ATOM   2088  C  CD    . ARG A 1 1710 ? 205.926 192.707 155.959 1.00 94.08  ? 1710 ARG A CD    1 
ATOM   2089  N  NE    . ARG A 1 1710 ? 205.249 192.449 154.693 1.00 98.56  ? 1710 ARG A NE    1 
ATOM   2090  C  CZ    . ARG A 1 1710 ? 203.933 192.372 154.546 1.00 99.77  ? 1710 ARG A CZ    1 
ATOM   2091  N  NH1   . ARG A 1 1710 ? 203.111 192.528 155.572 1.00 96.73  ? 1710 ARG A NH1   1 
ATOM   2092  N  NH2   . ARG A 1 1710 ? 203.428 192.128 153.340 1.00 97.08  ? 1710 ARG A NH2   1 
ATOM   2093  N  N     . VAL A 1 1711 ? 208.801 197.413 156.007 1.00 95.19  ? 1711 VAL A N     1 
ATOM   2094  C  CA    . VAL A 1 1711 ? 210.205 197.813 155.951 1.00 92.34  ? 1711 VAL A CA    1 
ATOM   2095  C  C     . VAL A 1 1711 ? 210.519 198.855 157.020 1.00 93.28  ? 1711 VAL A C     1 
ATOM   2096  O  O     . VAL A 1 1711 ? 211.560 198.783 157.690 1.00 92.66  ? 1711 VAL A O     1 
ATOM   2097  C  CB    . VAL A 1 1711 ? 210.558 198.316 154.541 1.00 93.87  ? 1711 VAL A CB    1 
ATOM   2098  C  CG1   . VAL A 1 1711 ? 211.942 198.937 154.531 1.00 96.10  ? 1711 VAL A CG1   1 
ATOM   2099  C  CG2   . VAL A 1 1711 ? 210.474 197.174 153.541 1.00 92.11  ? 1711 VAL A CG2   1 
ATOM   2100  N  N     . THR A 1 1712 ? 209.638 199.843 157.199 1.00 90.21  ? 1712 THR A N     1 
ATOM   2101  C  CA    . THR A 1 1712 ? 209.900 200.869 158.199 1.00 88.08  ? 1712 THR A CA    1 
ATOM   2102  C  C     . THR A 1 1712 ? 209.825 200.303 159.609 1.00 92.28  ? 1712 THR A C     1 
ATOM   2103  O  O     . THR A 1 1712 ? 210.597 200.726 160.477 1.00 98.90  ? 1712 THR A O     1 
ATOM   2104  C  CB    . THR A 1 1712 ? 208.943 202.057 158.037 1.00 93.66  ? 1712 THR A CB    1 
ATOM   2105  O  OG1   . THR A 1 1712 ? 209.376 203.133 158.878 1.00 96.66  ? 1712 THR A OG1   1 
ATOM   2106  C  CG2   . THR A 1 1712 ? 207.520 201.690 158.415 1.00 92.96  ? 1712 THR A CG2   1 
ATOM   2107  N  N     . LEU A 1 1713 ? 208.937 199.334 159.861 1.00 81.35  ? 1713 LEU A N     1 
ATOM   2108  C  CA    . LEU A 1 1713 ? 208.944 198.696 161.171 1.00 79.31  ? 1713 LEU A CA    1 
ATOM   2109  C  C     . LEU A 1 1713 ? 210.247 197.944 161.403 1.00 82.30  ? 1713 LEU A C     1 
ATOM   2110  O  O     . LEU A 1 1713 ? 210.805 197.986 162.505 1.00 83.33  ? 1713 LEU A O     1 
ATOM   2111  C  CB    . LEU A 1 1713 ? 207.741 197.769 161.321 1.00 75.82  ? 1713 LEU A CB    1 
ATOM   2112  C  CG    . LEU A 1 1713 ? 206.445 198.518 161.627 1.00 75.04  ? 1713 LEU A CG    1 
ATOM   2113  C  CD1   . LEU A 1 1713 ? 205.249 197.590 161.553 1.00 81.53  ? 1713 LEU A CD1   1 
ATOM   2114  C  CD2   . LEU A 1 1713 ? 206.531 199.189 162.987 1.00 71.92  ? 1713 LEU A CD2   1 
ATOM   2115  N  N     . ALA A 1 1714 ? 210.761 197.269 160.371 1.00 88.42  ? 1714 ALA A N     1 
ATOM   2116  C  CA    . ALA A 1 1714 ? 212.036 196.571 160.518 1.00 90.21  ? 1714 ALA A CA    1 
ATOM   2117  C  C     . ALA A 1 1714 ? 213.172 197.539 160.833 1.00 92.53  ? 1714 ALA A C     1 
ATOM   2118  O  O     . ALA A 1 1714 ? 213.984 197.290 161.735 1.00 96.87  ? 1714 ALA A O     1 
ATOM   2119  C  CB    . ALA A 1 1714 ? 212.347 195.775 159.252 1.00 90.24  ? 1714 ALA A CB    1 
ATOM   2120  N  N     . LYS A 1 1715 ? 213.243 198.654 160.102 1.00 95.17  ? 1715 LYS A N     1 
ATOM   2121  C  CA    . LYS A 1 1715 ? 214.327 199.609 160.326 1.00 93.99  ? 1715 LYS A CA    1 
ATOM   2122  C  C     . LYS A 1 1715 ? 214.217 200.270 161.696 1.00 93.35  ? 1715 LYS A C     1 
ATOM   2123  O  O     . LYS A 1 1715 ? 215.229 200.464 162.385 1.00 95.72  ? 1715 LYS A O     1 
ATOM   2124  C  CB    . LYS A 1 1715 ? 214.341 200.657 159.215 1.00 95.04  ? 1715 LYS A CB    1 
ATOM   2125  C  CG    . LYS A 1 1715 ? 214.719 200.094 157.855 1.00 94.74  ? 1715 LYS A CG    1 
ATOM   2126  C  CD    . LYS A 1 1715 ? 214.642 201.155 156.774 1.00 96.41  ? 1715 LYS A CD    1 
ATOM   2127  C  CE    . LYS A 1 1715 ? 215.081 200.600 155.430 1.00 93.91  ? 1715 LYS A CE    1 
ATOM   2128  N  NZ    . LYS A 1 1715 ? 214.920 201.603 154.343 1.00 97.00  ? 1715 LYS A NZ    1 
ATOM   2129  N  N     . LEU A 1 1716 ? 212.999 200.624 162.110 1.00 81.73  ? 1716 LEU A N     1 
ATOM   2130  C  CA    . LEU A 1 1716 ? 212.820 201.210 163.432 1.00 78.19  ? 1716 LEU A CA    1 
ATOM   2131  C  C     . LEU A 1 1716 ? 213.161 200.208 164.527 1.00 84.76  ? 1716 LEU A C     1 
ATOM   2132  O  O     . LEU A 1 1716 ? 213.708 200.585 165.567 1.00 91.95  ? 1716 LEU A O     1 
ATOM   2133  C  CB    . LEU A 1 1716 ? 211.393 201.728 163.590 1.00 83.09  ? 1716 LEU A CB    1 
ATOM   2134  C  CG    . LEU A 1 1716 ? 211.059 203.017 162.838 1.00 86.40  ? 1716 LEU A CG    1 
ATOM   2135  C  CD1   . LEU A 1 1716 ? 209.558 203.255 162.828 1.00 85.94  ? 1716 LEU A CD1   1 
ATOM   2136  C  CD2   . LEU A 1 1716 ? 211.789 204.200 163.451 1.00 88.51  ? 1716 LEU A CD2   1 
ATOM   2137  N  N     . LEU A 1 1717 ? 212.854 198.924 164.312 1.00 82.97  ? 1717 LEU A N     1 
ATOM   2138  C  CA    . LEU A 1 1717 ? 213.262 197.903 165.270 1.00 81.85  ? 1717 LEU A CA    1 
ATOM   2139  C  C     . LEU A 1 1717 ? 214.778 197.813 165.360 1.00 82.45  ? 1717 LEU A C     1 
ATOM   2140  O  O     . LEU A 1 1717 ? 215.332 197.660 166.454 1.00 88.34  ? 1717 LEU A O     1 
ATOM   2141  C  CB    . LEU A 1 1717 ? 212.675 196.545 164.887 1.00 80.98  ? 1717 LEU A CB    1 
ATOM   2142  C  CG    . LEU A 1 1717 ? 213.333 195.345 165.574 1.00 79.83  ? 1717 LEU A CG    1 
ATOM   2143  C  CD1   . LEU A 1 1717 ? 212.951 195.293 167.043 1.00 83.38  ? 1717 LEU A CD1   1 
ATOM   2144  C  CD2   . LEU A 1 1717 ? 212.974 194.043 164.880 1.00 80.50  ? 1717 LEU A CD2   1 
ATOM   2145  N  N     . ALA A 1 1718 ? 215.465 197.893 164.219 1.00 79.28  ? 1718 ALA A N     1 
ATOM   2146  C  CA    . ALA A 1 1718 ? 216.925 197.859 164.241 1.00 76.61  ? 1718 ALA A CA    1 
ATOM   2147  C  C     . ALA A 1 1718 ? 217.487 199.032 165.036 1.00 77.15  ? 1718 ALA A C     1 
ATOM   2148  O  O     . ALA A 1 1718 ? 218.384 198.862 165.875 1.00 83.16  ? 1718 ALA A O     1 
ATOM   2149  C  CB    . ALA A 1 1718 ? 217.472 197.860 162.814 1.00 78.63  ? 1718 ALA A CB    1 
ATOM   2150  N  N     . GLU A 1 1719 ? 216.958 200.234 164.794 1.00 84.10  ? 1719 GLU A N     1 
ATOM   2151  C  CA    . GLU A 1 1719 ? 217.422 201.404 165.538 1.00 84.58  ? 1719 GLU A CA    1 
ATOM   2152  C  C     . GLU A 1 1719 ? 217.131 201.265 167.028 1.00 87.70  ? 1719 GLU A C     1 
ATOM   2153  O  O     . GLU A 1 1719 ? 217.974 201.602 167.869 1.00 85.74  ? 1719 GLU A O     1 
ATOM   2154  C  CB    . GLU A 1 1719 ? 216.779 202.676 164.988 1.00 82.60  ? 1719 GLU A CB    1 
ATOM   2155  C  CG    . GLU A 1 1719 ? 217.015 202.912 163.510 1.00 87.82  ? 1719 GLU A CG    1 
ATOM   2156  C  CD    . GLU A 1 1719 ? 216.291 204.141 163.002 1.00 91.35  ? 1719 GLU A CD    1 
ATOM   2157  O  OE1   . GLU A 1 1719 ? 215.559 204.769 163.796 1.00 89.54  ? 1719 GLU A OE1   1 
ATOM   2158  O  OE2   . GLU A 1 1719 ? 216.454 204.480 161.812 1.00 92.09  ? 1719 GLU A OE2   1 
ATOM   2159  N  N     . SER A 1 1720 ? 215.939 200.773 167.374 1.00 87.34  ? 1720 SER A N     1 
ATOM   2160  C  CA    . SER A 1 1720 ? 215.577 200.615 168.777 1.00 83.44  ? 1720 SER A CA    1 
ATOM   2161  C  C     . SER A 1 1720 ? 216.464 199.589 169.466 1.00 80.69  ? 1720 SER A C     1 
ATOM   2162  O  O     . SER A 1 1720 ? 216.840 199.772 170.627 1.00 86.31  ? 1720 SER A O     1 
ATOM   2163  C  CB    . SER A 1 1720 ? 214.106 200.221 168.899 1.00 84.72  ? 1720 SER A CB    1 
ATOM   2164  O  OG    . SER A 1 1720 ? 213.747 200.020 170.255 1.00 87.40  ? 1720 SER A OG    1 
ATOM   2165  N  N     . VAL A 1 1721 ? 216.799 198.499 168.775 1.00 70.68  ? 1721 VAL A N     1 
ATOM   2166  C  CA    . VAL A 1 1721 ? 217.689 197.494 169.350 1.00 72.21  ? 1721 VAL A CA    1 
ATOM   2167  C  C     . VAL A 1 1721 ? 219.074 198.085 169.578 1.00 80.78  ? 1721 VAL A C     1 
ATOM   2168  O  O     . VAL A 1 1721 ? 219.693 197.882 170.632 1.00 82.38  ? 1721 VAL A O     1 
ATOM   2169  C  CB    . VAL A 1 1721 ? 217.744 196.248 168.449 1.00 73.08  ? 1721 VAL A CB    1 
ATOM   2170  C  CG1   . VAL A 1 1721 ? 219.012 195.452 168.711 1.00 74.73  ? 1721 VAL A CG1   1 
ATOM   2171  C  CG2   . VAL A 1 1721 ? 216.516 195.385 168.670 1.00 80.33  ? 1721 VAL A CG2   1 
ATOM   2172  N  N     . THR A 1 1722 ? 219.580 198.831 168.591 1.00 91.69  ? 1722 THR A N     1 
ATOM   2173  C  CA    . THR A 1 1722 ? 220.889 199.457 168.748 1.00 85.88  ? 1722 THR A CA    1 
ATOM   2174  C  C     . THR A 1 1722 ? 220.895 200.427 169.923 1.00 84.75  ? 1722 THR A C     1 
ATOM   2175  O  O     . THR A 1 1722 ? 221.881 200.508 170.666 1.00 87.82  ? 1722 THR A O     1 
ATOM   2176  C  CB    . THR A 1 1722 ? 221.289 200.173 167.458 1.00 87.02  ? 1722 THR A CB    1 
ATOM   2177  O  OG1   . THR A 1 1722 ? 221.271 199.242 166.368 1.00 91.41  ? 1722 THR A OG1   1 
ATOM   2178  C  CG2   . THR A 1 1722 ? 222.686 200.759 167.584 1.00 86.53  ? 1722 THR A CG2   1 
ATOM   2179  N  N     . GLU A 1 1723 ? 219.799 201.164 170.114 1.00 89.41  ? 1723 GLU A N     1 
ATOM   2180  C  CA    . GLU A 1 1723 ? 219.721 202.088 171.242 1.00 92.94  ? 1723 GLU A CA    1 
ATOM   2181  C  C     . GLU A 1 1723 ? 219.608 201.347 172.570 1.00 96.10  ? 1723 GLU A C     1 
ATOM   2182  O  O     . GLU A 1 1723 ? 220.237 201.739 173.560 1.00 93.53  ? 1723 GLU A O     1 
ATOM   2183  C  CB    . GLU A 1 1723 ? 218.540 203.040 171.060 1.00 92.26  ? 1723 GLU A CB    1 
ATOM   2184  C  CG    . GLU A 1 1723 ? 218.759 204.414 171.664 1.00 92.73  ? 1723 GLU A CG    1 
ATOM   2185  C  CD    . GLU A 1 1723 ? 217.760 205.435 171.163 1.00 93.45  ? 1723 GLU A CD    1 
ATOM   2186  O  OE1   . GLU A 1 1723 ? 217.361 205.349 169.983 1.00 92.74  ? 1723 GLU A OE1   1 
ATOM   2187  O  OE2   . GLU A 1 1723 ? 217.371 206.322 171.951 1.00 93.51  ? 1723 GLU A OE2   1 
ATOM   2188  N  N     . VAL A 1 1724 ? 218.812 200.274 172.614 1.00 98.26  ? 1724 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 1724 ? 218.564 199.556 173.863 1.00 92.32  ? 1724 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 1724 ? 219.729 198.676 174.276 1.00 94.51  ? 1724 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 1724 ? 219.777 198.235 175.432 1.00 95.31  ? 1724 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 1724 ? 217.285 198.702 173.756 1.00 88.61  ? 1724 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 1724 ? 217.577 197.376 173.073 1.00 91.07  ? 1724 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 1724 ? 216.668 198.480 175.129 1.00 92.55  ? 1724 VAL A CG2   1 
ATOM   2195  N  N     . GLU A 1 1725 ? 220.669 198.400 173.369 1.00 106.24 ? 1725 GLU A N     1 
ATOM   2196  C  CA    . GLU A 1 1725 ? 221.882 197.701 173.782 1.00 106.02 ? 1725 GLU A CA    1 
ATOM   2197  C  C     . GLU A 1 1725 ? 222.647 198.467 174.854 1.00 109.01 ? 1725 GLU A C     1 
ATOM   2198  O  O     . GLU A 1 1725 ? 223.377 197.851 175.638 1.00 111.41 ? 1725 GLU A O     1 
ATOM   2199  C  CB    . GLU A 1 1725 ? 222.793 197.445 172.579 1.00 105.25 ? 1725 GLU A CB    1 
ATOM   2200  C  CG    . GLU A 1 1725 ? 222.257 196.420 171.598 1.00 106.17 ? 1725 GLU A CG    1 
ATOM   2201  C  CD    . GLU A 1 1725 ? 222.559 194.996 172.017 1.00 109.79 ? 1725 GLU A CD    1 
ATOM   2202  O  OE1   . GLU A 1 1725 ? 223.686 194.740 172.491 1.00 114.34 ? 1725 GLU A OE1   1 
ATOM   2203  O  OE2   . GLU A 1 1725 ? 221.668 194.133 171.875 1.00 105.37 ? 1725 GLU A OE2   1 
ATOM   2204  N  N     . ILE A 1 1726 ? 222.497 199.792 174.906 1.00 107.95 ? 1726 ILE A N     1 
ATOM   2205  C  CA    . ILE A 1 1726 ? 223.148 200.579 175.950 1.00 107.18 ? 1726 ILE A CA    1 
ATOM   2206  C  C     . ILE A 1 1726 ? 222.493 200.319 177.301 1.00 105.51 ? 1726 ILE A C     1 
ATOM   2207  O  O     . ILE A 1 1726 ? 223.174 200.206 178.327 1.00 104.20 ? 1726 ILE A O     1 
ATOM   2208  C  CB    . ILE A 1 1726 ? 223.123 202.074 175.588 1.00 106.19 ? 1726 ILE A CB    1 
ATOM   2209  C  CG1   . ILE A 1 1726 ? 223.643 202.289 174.166 1.00 106.84 ? 1726 ILE A CG1   1 
ATOM   2210  C  CG2   . ILE A 1 1726 ? 223.943 202.877 176.585 1.00 103.79 ? 1726 ILE A CG2   1 
ATOM   2211  C  CD1   . ILE A 1 1726 ? 225.023 201.715 173.925 1.00 102.07 ? 1726 ILE A CD1   1 
ATOM   2212  N  N     . PHE A 1 1727 ? 221.160 200.237 177.325 1.00 106.48 ? 1727 PHE A N     1 
ATOM   2213  C  CA    . PHE A 1 1727 ? 220.460 199.947 178.574 1.00 109.52 ? 1727 PHE A CA    1 
ATOM   2214  C  C     . PHE A 1 1727 ? 220.801 198.554 179.084 1.00 111.47 ? 1727 PHE A C     1 
ATOM   2215  O  O     . PHE A 1 1727 ? 220.950 198.346 180.294 1.00 109.66 ? 1727 PHE A O     1 
ATOM   2216  C  CB    . PHE A 1 1727 ? 218.953 200.103 178.381 1.00 109.23 ? 1727 PHE A CB    1 
ATOM   2217  C  CG    . PHE A 1 1727 ? 218.555 201.435 177.818 1.00 108.52 ? 1727 PHE A CG    1 
ATOM   2218  C  CD1   . PHE A 1 1727 ? 219.045 202.605 178.370 1.00 105.57 ? 1727 PHE A CD1   1 
ATOM   2219  C  CD2   . PHE A 1 1727 ? 217.698 201.517 176.736 1.00 106.33 ? 1727 PHE A CD2   1 
ATOM   2220  C  CE1   . PHE A 1 1727 ? 218.685 203.832 177.856 1.00 106.68 ? 1727 PHE A CE1   1 
ATOM   2221  C  CE2   . PHE A 1 1727 ? 217.336 202.741 176.217 1.00 106.70 ? 1727 PHE A CE2   1 
ATOM   2222  C  CZ    . PHE A 1 1727 ? 217.829 203.900 176.777 1.00 109.66 ? 1727 PHE A CZ    1 
ATOM   2223  N  N     . GLY A 1 1728 ? 220.925 197.586 178.179 1.00 117.24 ? 1728 GLY A N     1 
ATOM   2224  C  CA    . GLY A 1 1728 ? 221.478 196.303 178.557 1.00 112.85 ? 1728 GLY A CA    1 
ATOM   2225  C  C     . GLY A 1 1728 ? 222.947 196.426 178.911 1.00 116.09 ? 1728 GLY A C     1 
ATOM   2226  O  O     . GLY A 1 1728 ? 223.583 197.450 178.664 1.00 114.20 ? 1728 GLY A O     1 
ATOM   2227  N  N     . LYS A 1 1729 ? 223.480 195.365 179.524 1.00 122.24 ? 1729 LYS A N     1 
ATOM   2228  C  CA    . LYS A 1 1729 ? 224.872 195.301 179.993 1.00 122.65 ? 1729 LYS A CA    1 
ATOM   2229  C  C     . LYS A 1 1729 ? 225.284 196.564 180.753 1.00 121.59 ? 1729 LYS A C     1 
ATOM   2230  O  O     . LYS A 1 1729 ? 226.457 196.946 180.764 1.00 121.31 ? 1729 LYS A O     1 
ATOM   2231  C  CB    . LYS A 1 1729 ? 225.847 195.004 178.840 1.00 121.67 ? 1729 LYS A CB    1 
ATOM   2232  C  CG    . LYS A 1 1729 ? 226.101 196.134 177.843 1.00 123.34 ? 1729 LYS A CG    1 
ATOM   2233  C  CD    . LYS A 1 1729 ? 226.902 195.660 176.643 1.00 121.72 ? 1729 LYS A CD    1 
ATOM   2234  C  CE    . LYS A 1 1729 ? 227.364 196.835 175.795 1.00 120.44 ? 1729 LYS A CE    1 
ATOM   2235  N  NZ    . LYS A 1 1729 ? 228.374 197.671 176.501 1.00 117.32 ? 1729 LYS A NZ    1 
ATOM   2236  N  N     . ALA A 1 1730 ? 224.326 197.207 181.418 1.00 119.18 ? 1730 ALA A N     1 
ATOM   2237  C  CA    . ALA A 1 1730 ? 224.560 198.429 182.174 1.00 118.55 ? 1730 ALA A CA    1 
ATOM   2238  C  C     . ALA A 1 1730 ? 224.096 198.229 183.608 1.00 119.20 ? 1730 ALA A C     1 
ATOM   2239  O  O     . ALA A 1 1730 ? 222.987 197.736 183.843 1.00 116.40 ? 1730 ALA A O     1 
ATOM   2240  C  CB    . ALA A 1 1730 ? 223.834 199.618 181.540 1.00 116.01 ? 1730 ALA A CB    1 
ATOM   2241  N  N     . THR A 1 1731 ? 224.947 198.610 184.564 1.00 123.42 ? 1731 THR A N     1 
ATOM   2242  C  CA    . THR A 1 1731 ? 224.625 198.395 185.971 1.00 122.55 ? 1731 THR A CA    1 
ATOM   2243  C  C     . THR A 1 1731 ? 223.465 199.274 186.423 1.00 123.80 ? 1731 THR A C     1 
ATOM   2244  O  O     . THR A 1 1731 ? 222.535 198.793 187.080 1.00 124.33 ? 1731 THR A O     1 
ATOM   2245  C  CB    . THR A 1 1731 ? 225.858 198.656 186.836 1.00 123.26 ? 1731 THR A CB    1 
ATOM   2246  O  OG1   . THR A 1 1731 ? 226.249 200.029 186.712 1.00 123.02 ? 1731 THR A OG1   1 
ATOM   2247  C  CG2   . THR A 1 1731 ? 227.011 197.764 186.402 1.00 122.69 ? 1731 THR A CG2   1 
ATOM   2248  N  N     . SER A 1 1732 ? 223.499 200.560 186.084 1.00 119.69 ? 1732 SER A N     1 
ATOM   2249  C  CA    . SER A 1 1732 ? 222.481 201.512 186.503 1.00 120.00 ? 1732 SER A CA    1 
ATOM   2250  C  C     . SER A 1 1732 ? 221.862 202.176 185.283 1.00 120.58 ? 1732 SER A C     1 
ATOM   2251  O  O     . SER A 1 1732 ? 222.564 202.522 184.328 1.00 117.73 ? 1732 SER A O     1 
ATOM   2252  C  CB    . SER A 1 1732 ? 223.068 202.577 187.435 1.00 120.65 ? 1732 SER A CB    1 
ATOM   2253  O  OG    . SER A 1 1732 ? 223.996 203.398 186.749 1.00 120.04 ? 1732 SER A OG    1 
ATOM   2254  N  N     . ILE A 1 1733 ? 220.544 202.353 185.321 1.00 110.94 ? 1733 ILE A N     1 
ATOM   2255  C  CA    . ILE A 1 1733 ? 219.788 202.946 184.224 1.00 110.74 ? 1733 ILE A CA    1 
ATOM   2256  C  C     . ILE A 1 1733 ? 219.163 204.244 184.712 1.00 109.12 ? 1733 ILE A C     1 
ATOM   2257  O  O     . ILE A 1 1733 ? 218.469 204.258 185.734 1.00 109.83 ? 1733 ILE A O     1 
ATOM   2258  C  CB    . ILE A 1 1733 ? 218.706 201.988 183.696 1.00 106.75 ? 1733 ILE A CB    1 
ATOM   2259  C  CG1   . ILE A 1 1733 ? 219.262 200.569 183.582 1.00 109.09 ? 1733 ILE A CG1   1 
ATOM   2260  C  CG2   . ILE A 1 1733 ? 218.177 202.468 182.356 1.00 106.25 ? 1733 ILE A CG2   1 
ATOM   2261  C  CD1   . ILE A 1 1733 ? 218.198 199.505 183.572 1.00 107.36 ? 1733 ILE A CD1   1 
ATOM   2262  N  N     . ASP A 1 1734 ? 219.410 205.324 183.985 1.00 106.69 ? 1734 ASP A N     1 
ATOM   2263  C  CA    . ASP A 1 1734 ? 218.773 206.598 184.290 1.00 106.43 ? 1734 ASP A CA    1 
ATOM   2264  C  C     . ASP A 1 1734 ? 217.309 206.537 183.878 1.00 106.51 ? 1734 ASP A C     1 
ATOM   2265  O  O     . ASP A 1 1734 ? 217.017 206.230 182.715 1.00 107.17 ? 1734 ASP A O     1 
ATOM   2266  C  CB    . ASP A 1 1734 ? 219.486 207.735 183.566 1.00 108.44 ? 1734 ASP A CB    1 
ATOM   2267  C  CG    . ASP A 1 1734 ? 219.104 209.100 184.102 1.00 111.87 ? 1734 ASP A CG    1 
ATOM   2268  O  OD1   . ASP A 1 1734 ? 218.709 209.189 185.283 1.00 112.32 ? 1734 ASP A OD1   1 
ATOM   2269  O  OD2   . ASP A 1 1734 ? 219.197 210.086 183.341 1.00 112.51 ? 1734 ASP A OD2   1 
ATOM   2270  N  N     . PRO A 1 1735 ? 216.362 206.800 184.784 1.00 104.65 ? 1735 PRO A N     1 
ATOM   2271  C  CA    . PRO A 1 1735 ? 214.943 206.714 184.396 1.00 103.73 ? 1735 PRO A CA    1 
ATOM   2272  C  C     . PRO A 1 1735 ? 214.565 207.640 183.253 1.00 104.46 ? 1735 PRO A C     1 
ATOM   2273  O  O     . PRO A 1 1735 ? 213.726 207.274 182.421 1.00 106.07 ? 1735 PRO A O     1 
ATOM   2274  C  CB    . PRO A 1 1735 ? 214.207 207.079 185.693 1.00 102.03 ? 1735 PRO A CB    1 
ATOM   2275  C  CG    . PRO A 1 1735 ? 215.171 206.750 186.781 1.00 101.12 ? 1735 PRO A CG    1 
ATOM   2276  C  CD    . PRO A 1 1735 ? 216.530 207.050 186.225 1.00 104.27 ? 1735 PRO A CD    1 
ATOM   2277  N  N     . ASN A 1 1736 ? 215.165 208.831 183.186 1.00 106.91 ? 1736 ASN A N     1 
ATOM   2278  C  CA    . ASN A 1 1736 ? 214.810 209.777 182.132 1.00 108.34 ? 1736 ASN A CA    1 
ATOM   2279  C  C     . ASN A 1 1736 ? 215.165 209.237 180.752 1.00 108.11 ? 1736 ASN A C     1 
ATOM   2280  O  O     . ASN A 1 1736 ? 214.357 209.323 179.820 1.00 108.39 ? 1736 ASN A O     1 
ATOM   2281  C  CB    . ASN A 1 1736 ? 215.503 211.117 182.376 1.00 107.51 ? 1736 ASN A CB    1 
ATOM   2282  C  CG    . ASN A 1 1736 ? 214.552 212.292 182.272 1.00 109.01 ? 1736 ASN A CG    1 
ATOM   2283  O  OD1   . ASN A 1 1736 ? 213.337 212.115 182.184 1.00 109.21 ? 1736 ASN A OD1   1 
ATOM   2284  N  ND2   . ASN A 1 1736 ? 215.101 213.500 182.281 1.00 106.79 ? 1736 ASN A ND2   1 
ATOM   2285  N  N     . THR A 1 1737 ? 216.366 208.672 180.603 1.00 99.43  ? 1737 THR A N     1 
ATOM   2286  C  CA    . THR A 1 1737 ? 216.775 208.138 179.308 1.00 100.28 ? 1737 THR A CA    1 
ATOM   2287  C  C     . THR A 1 1737 ? 215.903 206.959 178.895 1.00 98.92  ? 1737 THR A C     1 
ATOM   2288  O  O     . THR A 1 1737 ? 215.512 206.842 177.727 1.00 98.45  ? 1737 THR A O     1 
ATOM   2289  C  CB    . THR A 1 1737 ? 218.246 207.724 179.351 1.00 99.79  ? 1737 THR A CB    1 
ATOM   2290  O  OG1   . THR A 1 1737 ? 219.024 208.782 179.924 1.00 97.71  ? 1737 THR A OG1   1 
ATOM   2291  C  CG2   . THR A 1 1737 ? 218.757 207.430 177.950 1.00 98.79  ? 1737 THR A CG2   1 
ATOM   2292  N  N     . TYR A 1 1738 ? 215.592 206.069 179.841 1.00 93.45  ? 1738 TYR A N     1 
ATOM   2293  C  CA    . TYR A 1 1738 ? 214.748 204.924 179.523 1.00 91.27  ? 1738 TYR A CA    1 
ATOM   2294  C  C     . TYR A 1 1738 ? 213.347 205.369 179.123 1.00 92.36  ? 1738 TYR A C     1 
ATOM   2295  O  O     . TYR A 1 1738 ? 212.760 204.823 178.183 1.00 99.23  ? 1738 TYR A O     1 
ATOM   2296  C  CB    . TYR A 1 1738 ? 214.693 203.964 180.711 1.00 92.93  ? 1738 TYR A CB    1 
ATOM   2297  C  CG    . TYR A 1 1738 ? 214.519 202.518 180.308 1.00 94.62  ? 1738 TYR A CG    1 
ATOM   2298  C  CD1   . TYR A 1 1738 ? 215.551 201.823 179.692 1.00 95.77  ? 1738 TYR A CD1   1 
ATOM   2299  C  CD2   . TYR A 1 1738 ? 213.325 201.849 180.536 1.00 93.85  ? 1738 TYR A CD2   1 
ATOM   2300  C  CE1   . TYR A 1 1738 ? 215.399 200.503 179.319 1.00 97.45  ? 1738 TYR A CE1   1 
ATOM   2301  C  CE2   . TYR A 1 1738 ? 213.165 200.529 180.164 1.00 92.41  ? 1738 TYR A CE2   1 
ATOM   2302  C  CZ    . TYR A 1 1738 ? 214.205 199.861 179.557 1.00 97.57  ? 1738 TYR A CZ    1 
ATOM   2303  O  OH    . TYR A 1 1738 ? 214.048 198.546 179.187 1.00 100.83 ? 1738 TYR A OH    1 
ATOM   2304  N  N     . ILE A 1 1739 ? 212.796 206.363 179.823 1.00 84.91  ? 1739 ILE A N     1 
ATOM   2305  C  CA    . ILE A 1 1739 ? 211.476 206.875 179.472 1.00 84.04  ? 1739 ILE A CA    1 
ATOM   2306  C  C     . ILE A 1 1739 ? 211.504 207.529 178.096 1.00 91.67  ? 1739 ILE A C     1 
ATOM   2307  O  O     . ILE A 1 1739 ? 210.563 207.386 177.306 1.00 94.10  ? 1739 ILE A O     1 
ATOM   2308  C  CB    . ILE A 1 1739 ? 210.973 207.844 180.557 1.00 86.03  ? 1739 ILE A CB    1 
ATOM   2309  C  CG1   . ILE A 1 1739 ? 210.605 207.071 181.824 1.00 88.91  ? 1739 ILE A CG1   1 
ATOM   2310  C  CG2   . ILE A 1 1739 ? 209.778 208.641 180.061 1.00 88.52  ? 1739 ILE A CG2   1 
ATOM   2311  C  CD1   . ILE A 1 1739 ? 209.568 205.998 181.598 1.00 89.10  ? 1739 ILE A CD1   1 
ATOM   2312  N  N     . THR A 1 1740 ? 212.582 208.253 177.784 1.00 97.73  ? 1740 THR A N     1 
ATOM   2313  C  CA    . THR A 1 1740 ? 212.710 208.851 176.459 1.00 94.99  ? 1740 THR A CA    1 
ATOM   2314  C  C     . THR A 1 1740 ? 212.750 207.780 175.376 1.00 95.67  ? 1740 THR A C     1 
ATOM   2315  O  O     . THR A 1 1740 ? 212.092 207.911 174.336 1.00 97.79  ? 1740 THR A O     1 
ATOM   2316  C  CB    . THR A 1 1740 ? 213.963 209.724 176.395 1.00 92.81  ? 1740 THR A CB    1 
ATOM   2317  O  OG1   . THR A 1 1740 ? 213.871 210.769 177.370 1.00 96.92  ? 1740 THR A OG1   1 
ATOM   2318  C  CG2   . THR A 1 1740 ? 214.114 210.340 175.014 1.00 93.08  ? 1740 THR A CG2   1 
ATOM   2319  N  N     . TRP A 1 1741 ? 213.512 206.708 175.605 1.00 88.10  ? 1741 TRP A N     1 
ATOM   2320  C  CA    . TRP A 1 1741 ? 213.564 205.620 174.634 1.00 82.10  ? 1741 TRP A CA    1 
ATOM   2321  C  C     . TRP A 1 1741 ? 212.203 204.954 174.477 1.00 83.80  ? 1741 TRP A C     1 
ATOM   2322  O  O     . TRP A 1 1741 ? 211.805 204.591 173.364 1.00 88.83  ? 1741 TRP A O     1 
ATOM   2323  C  CB    . TRP A 1 1741 ? 214.615 204.591 175.046 1.00 82.54  ? 1741 TRP A CB    1 
ATOM   2324  C  CG    . TRP A 1 1741 ? 214.490 203.293 174.309 1.00 87.70  ? 1741 TRP A CG    1 
ATOM   2325  C  CD1   . TRP A 1 1741 ? 214.881 203.039 173.028 1.00 90.17  ? 1741 TRP A CD1   1 
ATOM   2326  C  CD2   . TRP A 1 1741 ? 213.930 202.073 174.807 1.00 89.17  ? 1741 TRP A CD2   1 
ATOM   2327  N  NE1   . TRP A 1 1741 ? 214.602 201.735 172.698 1.00 88.34  ? 1741 TRP A NE1   1 
ATOM   2328  C  CE2   . TRP A 1 1741 ? 214.018 201.121 173.773 1.00 87.79  ? 1741 TRP A CE2   1 
ATOM   2329  C  CE3   . TRP A 1 1741 ? 213.365 201.692 176.028 1.00 83.11  ? 1741 TRP A CE3   1 
ATOM   2330  C  CZ2   . TRP A 1 1741 ? 213.561 199.815 173.922 1.00 83.07  ? 1741 TRP A CZ2   1 
ATOM   2331  C  CZ3   . TRP A 1 1741 ? 212.913 200.395 176.173 1.00 84.67  ? 1741 TRP A CZ3   1 
ATOM   2332  C  CH2   . TRP A 1 1741 ? 213.014 199.472 175.126 1.00 85.41  ? 1741 TRP A CH2   1 
ATOM   2333  N  N     . ILE A 1 1742 ? 211.480 204.776 175.584 1.00 86.89  ? 1742 ILE A N     1 
ATOM   2334  C  CA    . ILE A 1 1742 ? 210.151 204.172 175.525 1.00 87.95  ? 1742 ILE A CA    1 
ATOM   2335  C  C     . ILE A 1 1742 ? 209.211 205.042 174.701 1.00 91.06  ? 1742 ILE A C     1 
ATOM   2336  O  O     . ILE A 1 1742 ? 208.454 204.548 173.857 1.00 95.82  ? 1742 ILE A O     1 
ATOM   2337  C  CB    . ILE A 1 1742 ? 209.603 203.942 176.945 1.00 85.22  ? 1742 ILE A CB    1 
ATOM   2338  C  CG1   . ILE A 1 1742 ? 210.332 202.783 177.620 1.00 85.23  ? 1742 ILE A CG1   1 
ATOM   2339  C  CG2   . ILE A 1 1742 ? 208.109 203.673 176.907 1.00 84.43  ? 1742 ILE A CG2   1 
ATOM   2340  C  CD1   . ILE A 1 1742 ? 210.114 202.726 179.113 1.00 89.53  ? 1742 ILE A CD1   1 
ATOM   2341  N  N     . ASP A 1 1743 ? 209.250 206.356 174.932 1.00 89.38  ? 1743 ASP A N     1 
ATOM   2342  C  CA    . ASP A 1 1743 ? 208.363 207.262 174.212 1.00 89.27  ? 1743 ASP A CA    1 
ATOM   2343  C  C     . ASP A 1 1743 ? 208.748 207.385 172.744 1.00 90.63  ? 1743 ASP A C     1 
ATOM   2344  O  O     . ASP A 1 1743 ? 207.889 207.667 171.902 1.00 87.11  ? 1743 ASP A O     1 
ATOM   2345  C  CB    . ASP A 1 1743 ? 208.370 208.638 174.876 1.00 86.62  ? 1743 ASP A CB    1 
ATOM   2346  C  CG    . ASP A 1 1743 ? 207.375 208.741 176.013 1.00 91.50  ? 1743 ASP A CG    1 
ATOM   2347  O  OD1   . ASP A 1 1743 ? 206.366 208.006 175.991 1.00 94.99  ? 1743 ASP A OD1   1 
ATOM   2348  O  OD2   . ASP A 1 1743 ? 207.601 209.559 176.928 1.00 89.57  ? 1743 ASP A OD2   1 
ATOM   2349  N  N     . LYS A 1 1744 ? 210.027 207.185 172.419 1.00 87.36  ? 1744 LYS A N     1 
ATOM   2350  C  CA    . LYS A 1 1744 ? 210.476 207.352 171.041 1.00 83.99  ? 1744 LYS A CA    1 
ATOM   2351  C  C     . LYS A 1 1744 ? 209.864 206.306 170.115 1.00 85.95  ? 1744 LYS A C     1 
ATOM   2352  O  O     . LYS A 1 1744 ? 209.455 206.628 168.994 1.00 90.06  ? 1744 LYS A O     1 
ATOM   2353  C  CB    . LYS A 1 1744 ? 212.001 207.293 170.977 1.00 85.44  ? 1744 LYS A CB    1 
ATOM   2354  C  CG    . LYS A 1 1744 ? 212.571 207.450 169.578 1.00 84.68  ? 1744 LYS A CG    1 
ATOM   2355  C  CD    . LYS A 1 1744 ? 214.074 207.663 169.616 1.00 87.16  ? 1744 LYS A CD    1 
ATOM   2356  C  CE    . LYS A 1 1744 ? 214.679 207.565 168.227 1.00 87.52  ? 1744 LYS A CE    1 
ATOM   2357  N  NZ    . LYS A 1 1744 ? 214.047 208.525 167.281 1.00 86.39  ? 1744 LYS A NZ    1 
ATOM   2358  N  N     . TYR A 1 1745 ? 209.787 205.057 170.561 1.00 83.72  ? 1745 TYR A N     1 
ATOM   2359  C  CA    . TYR A 1 1745 ? 209.393 203.947 169.707 1.00 80.23  ? 1745 TYR A CA    1 
ATOM   2360  C  C     . TYR A 1 1745 ? 208.016 203.420 170.092 1.00 76.66  ? 1745 TYR A C     1 
ATOM   2361  O  O     . TYR A 1 1745 ? 207.435 203.795 171.113 1.00 82.91  ? 1745 TYR A O     1 
ATOM   2362  C  CB    . TYR A 1 1745 ? 210.430 202.821 169.772 1.00 78.49  ? 1745 TYR A CB    1 
ATOM   2363  C  CG    . TYR A 1 1745 ? 211.773 203.205 169.200 1.00 78.95  ? 1745 TYR A CG    1 
ATOM   2364  C  CD1   . TYR A 1 1745 ? 212.013 203.133 167.835 1.00 79.73  ? 1745 TYR A CD1   1 
ATOM   2365  C  CD2   . TYR A 1 1745 ? 212.800 203.645 170.023 1.00 80.54  ? 1745 TYR A CD2   1 
ATOM   2366  C  CE1   . TYR A 1 1745 ? 213.238 203.486 167.306 1.00 83.82  ? 1745 TYR A CE1   1 
ATOM   2367  C  CE2   . TYR A 1 1745 ? 214.028 204.000 169.503 1.00 82.24  ? 1745 TYR A CE2   1 
ATOM   2368  C  CZ    . TYR A 1 1745 ? 214.242 203.919 168.144 1.00 85.19  ? 1745 TYR A CZ    1 
ATOM   2369  O  OH    . TYR A 1 1745 ? 215.464 204.271 167.622 1.00 85.67  ? 1745 TYR A OH    1 
ATOM   2370  N  N     . GLN A 1 1746 ? 207.501 202.535 169.243 1.00 79.98  ? 1746 GLN A N     1 
ATOM   2371  C  CA    . GLN A 1 1746 ? 206.181 201.958 169.439 1.00 88.30  ? 1746 GLN A CA    1 
ATOM   2372  C  C     . GLN A 1 1746 ? 206.212 200.900 170.540 1.00 91.96  ? 1746 GLN A C     1 
ATOM   2373  O  O     . GLN A 1 1746 ? 207.272 200.433 170.963 1.00 99.56  ? 1746 GLN A O     1 
ATOM   2374  C  CB    . GLN A 1 1746 ? 205.669 201.348 168.134 1.00 88.67  ? 1746 GLN A CB    1 
ATOM   2375  C  CG    . GLN A 1 1746 ? 205.345 202.367 167.050 1.00 89.66  ? 1746 GLN A CG    1 
ATOM   2376  C  CD    . GLN A 1 1746 ? 206.583 202.953 166.403 1.00 91.64  ? 1746 GLN A CD    1 
ATOM   2377  O  OE1   . GLN A 1 1746 ? 207.683 202.425 166.555 1.00 87.64  ? 1746 GLN A OE1   1 
ATOM   2378  N  NE2   . GLN A 1 1746 ? 206.412 204.055 165.684 1.00 93.51  ? 1746 GLN A NE2   1 
ATOM   2379  N  N     . ALA A 1 1747 ? 205.018 200.524 171.006 1.00 76.23  ? 1747 ALA A N     1 
ATOM   2380  C  CA    . ALA A 1 1747 ? 204.918 199.554 172.093 1.00 78.80  ? 1747 ALA A CA    1 
ATOM   2381  C  C     . ALA A 1 1747 ? 205.480 198.200 171.678 1.00 80.92  ? 1747 ALA A C     1 
ATOM   2382  O  O     . ALA A 1 1747 ? 206.302 197.606 172.390 1.00 85.39  ? 1747 ALA A O     1 
ATOM   2383  C  CB    . ALA A 1 1747 ? 203.463 199.420 172.540 1.00 77.35  ? 1747 ALA A CB    1 
ATOM   2384  N  N     . GLN A 1 1748 ? 205.053 197.696 170.517 1.00 69.97  ? 1748 GLN A N     1 
ATOM   2385  C  CA    . GLN A 1 1748 ? 205.571 196.416 170.053 1.00 68.76  ? 1748 GLN A CA    1 
ATOM   2386  C  C     . GLN A 1 1748 ? 207.073 196.484 169.826 1.00 71.71  ? 1748 GLN A C     1 
ATOM   2387  O  O     . GLN A 1 1748 ? 207.787 195.519 170.116 1.00 81.79  ? 1748 GLN A O     1 
ATOM   2388  C  CB    . GLN A 1 1748 ? 204.841 195.974 168.780 1.00 63.57  ? 1748 GLN A CB    1 
ATOM   2389  C  CG    . GLN A 1 1748 ? 205.343 196.601 167.490 1.00 65.03  ? 1748 GLN A CG    1 
ATOM   2390  C  CD    . GLN A 1 1748 ? 204.591 196.110 166.271 1.00 69.75  ? 1748 GLN A CD    1 
ATOM   2391  O  OE1   . GLN A 1 1748 ? 203.424 196.445 166.072 1.00 72.66  ? 1748 GLN A OE1   1 
ATOM   2392  N  NE2   . GLN A 1 1748 ? 205.256 195.309 165.448 1.00 69.65  ? 1748 GLN A NE2   1 
ATOM   2393  N  N     . LEU A 1 1749 ? 207.579 197.631 169.367 1.00 66.78  ? 1749 LEU A N     1 
ATOM   2394  C  CA    . LEU A 1 1749 ? 209.005 197.742 169.090 1.00 68.67  ? 1749 LEU A CA    1 
ATOM   2395  C  C     . LEU A 1 1749 ? 209.824 197.784 170.373 1.00 68.93  ? 1749 LEU A C     1 
ATOM   2396  O  O     . LEU A 1 1749 ? 210.896 197.177 170.443 1.00 69.05  ? 1749 LEU A O     1 
ATOM   2397  C  CB    . LEU A 1 1749 ? 209.280 198.970 168.228 1.00 71.66  ? 1749 LEU A CB    1 
ATOM   2398  C  CG    . LEU A 1 1749 ? 208.929 198.763 166.755 1.00 73.57  ? 1749 LEU A CG    1 
ATOM   2399  C  CD1   . LEU A 1 1749 ? 209.507 199.877 165.913 1.00 76.05  ? 1749 LEU A CD1   1 
ATOM   2400  C  CD2   . LEU A 1 1749 ? 209.418 197.409 166.268 1.00 70.05  ? 1749 LEU A CD2   1 
ATOM   2401  N  N     . VAL A 1 1750 ? 209.342 198.480 171.406 1.00 66.79  ? 1750 VAL A N     1 
ATOM   2402  C  CA    . VAL A 1 1750 ? 210.094 198.509 172.657 1.00 68.40  ? 1750 VAL A CA    1 
ATOM   2403  C  C     . VAL A 1 1750 ? 210.051 197.145 173.339 1.00 74.01  ? 1750 VAL A C     1 
ATOM   2404  O  O     . VAL A 1 1750 ? 211.057 196.689 173.901 1.00 80.48  ? 1750 VAL A O     1 
ATOM   2405  C  CB    . VAL A 1 1750 ? 209.597 199.638 173.582 1.00 69.11  ? 1750 VAL A CB    1 
ATOM   2406  C  CG1   . VAL A 1 1750 ? 209.754 200.987 172.901 1.00 73.98  ? 1750 VAL A CG1   1 
ATOM   2407  C  CG2   . VAL A 1 1750 ? 208.160 199.423 174.012 1.00 65.92  ? 1750 VAL A CG2   1 
ATOM   2408  N  N     . VAL A 1 1751 ? 208.904 196.458 173.286 1.00 63.48  ? 1751 VAL A N     1 
ATOM   2409  C  CA    . VAL A 1 1751 ? 208.840 195.114 173.857 1.00 60.77  ? 1751 VAL A CA    1 
ATOM   2410  C  C     . VAL A 1 1751 ? 209.783 194.174 173.113 1.00 64.08  ? 1751 VAL A C     1 
ATOM   2411  O  O     . VAL A 1 1751 ? 210.513 193.383 173.728 1.00 74.80  ? 1751 VAL A O     1 
ATOM   2412  C  CB    . VAL A 1 1751 ? 207.392 194.590 173.850 1.00 58.00  ? 1751 VAL A CB    1 
ATOM   2413  C  CG1   . VAL A 1 1751 ? 207.345 193.169 174.378 1.00 60.48  ? 1751 VAL A CG1   1 
ATOM   2414  C  CG2   . VAL A 1 1751 ? 206.505 195.486 174.691 1.00 63.80  ? 1751 VAL A CG2   1 
ATOM   2415  N  N     . LEU A 1 1752 ? 209.794 194.255 171.780 1.00 56.64  ? 1752 LEU A N     1 
ATOM   2416  C  CA    . LEU A 1 1752 ? 210.678 193.407 170.990 1.00 54.56  ? 1752 LEU A CA    1 
ATOM   2417  C  C     . LEU A 1 1752 ? 212.142 193.722 171.265 1.00 69.21  ? 1752 LEU A C     1 
ATOM   2418  O  O     . LEU A 1 1752 ? 212.976 192.814 171.329 1.00 78.36  ? 1752 LEU A O     1 
ATOM   2419  C  CB    . LEU A 1 1752 ? 210.360 193.575 169.507 1.00 57.89  ? 1752 LEU A CB    1 
ATOM   2420  C  CG    . LEU A 1 1752 ? 210.585 192.364 168.608 1.00 60.70  ? 1752 LEU A CG    1 
ATOM   2421  C  CD1   . LEU A 1 1752 ? 209.955 191.127 169.220 1.00 61.88  ? 1752 LEU A CD1   1 
ATOM   2422  C  CD2   . LEU A 1 1752 ? 210.001 192.640 167.237 1.00 68.09  ? 1752 LEU A CD2   1 
ATOM   2423  N  N     . SER A 1 1753 ? 212.476 195.005 171.420 1.00 68.81  ? 1753 SER A N     1 
ATOM   2424  C  CA    . SER A 1 1753 ? 213.853 195.383 171.717 1.00 62.86  ? 1753 SER A CA    1 
ATOM   2425  C  C     . SER A 1 1753 ? 214.288 194.847 173.073 1.00 59.99  ? 1753 SER A C     1 
ATOM   2426  O  O     . SER A 1 1753 ? 215.409 194.345 173.219 1.00 65.19  ? 1753 SER A O     1 
ATOM   2427  C  CB    . SER A 1 1753 ? 213.999 196.903 171.669 1.00 73.20  ? 1753 SER A CB    1 
ATOM   2428  O  OG    . SER A 1 1753 ? 213.287 197.446 170.572 1.00 80.00  ? 1753 SER A OG    1 
ATOM   2429  N  N     . ALA A 1 1754 ? 213.414 194.943 174.078 1.00 59.25  ? 1754 ALA A N     1 
ATOM   2430  C  CA    . ALA A 1 1754 ? 213.739 194.383 175.385 1.00 67.09  ? 1754 ALA A CA    1 
ATOM   2431  C  C     . ALA A 1 1754 ? 213.944 192.877 175.301 1.00 69.11  ? 1754 ALA A C     1 
ATOM   2432  O  O     . ALA A 1 1754 ? 214.893 192.337 175.884 1.00 76.34  ? 1754 ALA A O     1 
ATOM   2433  C  CB    . ALA A 1 1754 ? 212.641 194.722 176.391 1.00 66.59  ? 1754 ALA A CB    1 
ATOM   2434  N  N     . GLN A 1 1755 ? 213.069 192.182 174.567 1.00 59.48  ? 1755 GLN A N     1 
ATOM   2435  C  CA    . GLN A 1 1755 ? 213.209 190.735 174.429 1.00 54.57  ? 1755 GLN A CA    1 
ATOM   2436  C  C     . GLN A 1 1755 ? 214.511 190.367 173.729 1.00 56.30  ? 1755 GLN A C     1 
ATOM   2437  O  O     . GLN A 1 1755 ? 215.211 189.440 174.153 1.00 61.85  ? 1755 GLN A O     1 
ATOM   2438  C  CB    . GLN A 1 1755 ? 212.014 190.160 173.671 1.00 53.14  ? 1755 GLN A CB    1 
ATOM   2439  C  CG    . GLN A 1 1755 ? 210.726 190.158 174.467 1.00 52.73  ? 1755 GLN A CG    1 
ATOM   2440  C  CD    . GLN A 1 1755 ? 209.557 189.586 173.693 1.00 56.89  ? 1755 GLN A CD    1 
ATOM   2441  O  OE1   . GLN A 1 1755 ? 209.269 190.013 172.576 1.00 60.94  ? 1755 GLN A OE1   1 
ATOM   2442  N  NE2   . GLN A 1 1755 ? 208.876 188.614 174.286 1.00 63.42  ? 1755 GLN A NE2   1 
ATOM   2443  N  N     . ILE A 1 1756 ? 214.855 191.087 172.659 1.00 58.76  ? 1756 ILE A N     1 
ATOM   2444  C  CA    . ILE A 1 1756 ? 216.081 190.793 171.921 1.00 59.15  ? 1756 ILE A CA    1 
ATOM   2445  C  C     . ILE A 1 1756 ? 217.303 191.041 172.794 1.00 61.67  ? 1756 ILE A C     1 
ATOM   2446  O  O     . ILE A 1 1756 ? 218.240 190.233 172.821 1.00 67.74  ? 1756 ILE A O     1 
ATOM   2447  C  CB    . ILE A 1 1756 ? 216.138 191.622 170.624 1.00 56.47  ? 1756 ILE A CB    1 
ATOM   2448  C  CG1   . ILE A 1 1756 ? 215.076 191.144 169.636 1.00 69.27  ? 1756 ILE A CG1   1 
ATOM   2449  C  CG2   . ILE A 1 1756 ? 217.517 191.537 169.996 1.00 56.25  ? 1756 ILE A CG2   1 
ATOM   2450  C  CD1   . ILE A 1 1756 ? 214.747 192.156 168.567 1.00 64.38  ? 1756 ILE A CD1   1 
ATOM   2451  N  N     . ALA A 1 1757 ? 217.317 192.164 173.518 1.00 59.44  ? 1757 ALA A N     1 
ATOM   2452  C  CA    . ALA A 1 1757 ? 218.449 192.465 174.385 1.00 66.21  ? 1757 ALA A CA    1 
ATOM   2453  C  C     . ALA A 1 1757 ? 218.610 191.407 175.468 1.00 64.78  ? 1757 ALA A C     1 
ATOM   2454  O  O     . ALA A 1 1757 ? 219.726 190.940 175.726 1.00 71.04  ? 1757 ALA A O     1 
ATOM   2455  C  CB    . ALA A 1 1757 ? 218.281 193.850 175.007 1.00 67.87  ? 1757 ALA A CB    1 
ATOM   2456  N  N     . TRP A 1 1758 ? 217.506 191.005 176.104 1.00 60.08  ? 1758 TRP A N     1 
ATOM   2457  C  CA    . TRP A 1 1758 ? 217.597 189.990 177.148 1.00 61.97  ? 1758 TRP A CA    1 
ATOM   2458  C  C     . TRP A 1 1758 ? 218.067 188.656 176.584 1.00 66.69  ? 1758 TRP A C     1 
ATOM   2459  O  O     . TRP A 1 1758 ? 218.897 187.974 177.196 1.00 74.97  ? 1758 TRP A O     1 
ATOM   2460  C  CB    . TRP A 1 1758 ? 216.252 189.819 177.846 1.00 63.74  ? 1758 TRP A CB    1 
ATOM   2461  C  CG    . TRP A 1 1758 ? 216.203 188.598 178.707 1.00 62.35  ? 1758 TRP A CG    1 
ATOM   2462  C  CD1   . TRP A 1 1758 ? 216.712 188.462 179.964 1.00 65.37  ? 1758 TRP A CD1   1 
ATOM   2463  C  CD2   . TRP A 1 1758 ? 215.631 187.331 178.366 1.00 60.65  ? 1758 TRP A CD2   1 
ATOM   2464  N  NE1   . TRP A 1 1758 ? 216.483 187.192 180.433 1.00 61.65  ? 1758 TRP A NE1   1 
ATOM   2465  C  CE2   . TRP A 1 1758 ? 215.821 186.478 179.469 1.00 58.08  ? 1758 TRP A CE2   1 
ATOM   2466  C  CE3   . TRP A 1 1758 ? 214.972 186.838 177.237 1.00 65.03  ? 1758 TRP A CE3   1 
ATOM   2467  C  CZ2   . TRP A 1 1758 ? 215.377 185.160 179.476 1.00 59.36  ? 1758 TRP A CZ2   1 
ATOM   2468  C  CZ3   . TRP A 1 1758 ? 214.531 185.529 177.247 1.00 62.96  ? 1758 TRP A CZ3   1 
ATOM   2469  C  CH2   . TRP A 1 1758 ? 214.736 184.705 178.358 1.00 63.56  ? 1758 TRP A CH2   1 
ATOM   2470  N  N     . SER A 1 1759 ? 217.539 188.260 175.422 1.00 67.74  ? 1759 SER A N     1 
ATOM   2471  C  CA    . SER A 1 1759 ? 217.937 186.989 174.829 1.00 66.84  ? 1759 SER A CA    1 
ATOM   2472  C  C     . SER A 1 1759 ? 219.416 186.988 174.469 1.00 70.88  ? 1759 SER A C     1 
ATOM   2473  O  O     . SER A 1 1759 ? 220.123 186.007 174.728 1.00 75.98  ? 1759 SER A O     1 
ATOM   2474  C  CB    . SER A 1 1759 ? 217.084 186.694 173.596 1.00 65.58  ? 1759 SER A CB    1 
ATOM   2475  O  OG    . SER A 1 1759 ? 217.827 185.977 172.628 1.00 72.18  ? 1759 SER A OG    1 
ATOM   2476  N  N     . GLU A 1 1760 ? 219.906 188.081 173.880 1.00 76.21  ? 1760 GLU A N     1 
ATOM   2477  C  CA    . GLU A 1 1760 ? 221.320 188.150 173.528 1.00 75.06  ? 1760 GLU A CA    1 
ATOM   2478  C  C     . GLU A 1 1760 ? 222.202 188.155 174.771 1.00 80.53  ? 1760 GLU A C     1 
ATOM   2479  O  O     . GLU A 1 1760 ? 223.254 187.506 174.792 1.00 84.97  ? 1760 GLU A O     1 
ATOM   2480  C  CB    . GLU A 1 1760 ? 221.590 189.382 172.667 1.00 75.87  ? 1760 GLU A CB    1 
ATOM   2481  C  CG    . GLU A 1 1760 ? 221.125 189.233 171.228 1.00 80.21  ? 1760 GLU A CG    1 
ATOM   2482  C  CD    . GLU A 1 1760 ? 221.482 190.429 170.371 1.00 86.71  ? 1760 GLU A CD    1 
ATOM   2483  O  OE1   . GLU A 1 1760 ? 221.942 191.446 170.929 1.00 89.32  ? 1760 GLU A OE1   1 
ATOM   2484  O  OE2   . GLU A 1 1760 ? 221.303 190.352 169.137 1.00 84.68  ? 1760 GLU A OE2   1 
ATOM   2485  N  N     . ASN A 1 1761 ? 221.789 188.873 175.820 1.00 73.82  ? 1761 ASN A N     1 
ATOM   2486  C  CA    . ASN A 1 1761 ? 222.567 188.881 177.055 1.00 66.92  ? 1761 ASN A CA    1 
ATOM   2487  C  C     . ASN A 1 1761 ? 222.630 187.492 177.676 1.00 73.13  ? 1761 ASN A C     1 
ATOM   2488  O  O     . ASN A 1 1761 ? 223.695 187.054 178.128 1.00 83.98  ? 1761 ASN A O     1 
ATOM   2489  C  CB    . ASN A 1 1761 ? 221.971 189.881 178.044 1.00 72.97  ? 1761 ASN A CB    1 
ATOM   2490  C  CG    . ASN A 1 1761 ? 222.291 191.316 177.685 1.00 78.18  ? 1761 ASN A CG    1 
ATOM   2491  O  OD1   . ASN A 1 1761 ? 222.843 191.594 176.621 1.00 80.94  ? 1761 ASN A OD1   1 
ATOM   2492  N  ND2   . ASN A 1 1761 ? 221.942 192.240 178.573 1.00 79.74  ? 1761 ASN A ND2   1 
ATOM   2493  N  N     . VAL A 1 1762 ? 221.501 186.781 177.700 1.00 65.24  ? 1762 VAL A N     1 
ATOM   2494  C  CA    . VAL A 1 1762 ? 221.483 185.445 178.286 1.00 64.97  ? 1762 VAL A CA    1 
ATOM   2495  C  C     . VAL A 1 1762 ? 222.321 184.485 177.451 1.00 74.44  ? 1762 VAL A C     1 
ATOM   2496  O  O     . VAL A 1 1762 ? 223.037 183.636 177.994 1.00 76.91  ? 1762 VAL A O     1 
ATOM   2497  C  CB    . VAL A 1 1762 ? 220.035 184.951 178.449 1.00 64.80  ? 1762 VAL A CB    1 
ATOM   2498  C  CG1   . VAL A 1 1762 ? 219.998 183.440 178.588 1.00 67.17  ? 1762 VAL A CG1   1 
ATOM   2499  C  CG2   . VAL A 1 1762 ? 219.388 185.609 179.652 1.00 75.63  ? 1762 VAL A CG2   1 
ATOM   2500  N  N     . GLU A 1 1763 ? 222.250 184.601 176.122 1.00 81.78  ? 1763 GLU A N     1 
ATOM   2501  C  CA    . GLU A 1 1763 ? 223.068 183.750 175.265 1.00 75.26  ? 1763 GLU A CA    1 
ATOM   2502  C  C     . GLU A 1 1763 ? 224.553 184.007 175.489 1.00 80.25  ? 1763 GLU A C     1 
ATOM   2503  O  O     . GLU A 1 1763 ? 225.350 183.064 175.563 1.00 87.90  ? 1763 GLU A O     1 
ATOM   2504  C  CB    . GLU A 1 1763 ? 222.701 183.975 173.799 1.00 78.52  ? 1763 GLU A CB    1 
ATOM   2505  C  CG    . GLU A 1 1763 ? 223.092 182.834 172.878 1.00 81.90  ? 1763 GLU A CG    1 
ATOM   2506  C  CD    . GLU A 1 1763 ? 221.987 181.811 172.717 1.00 90.64  ? 1763 GLU A CD    1 
ATOM   2507  O  OE1   . GLU A 1 1763 ? 220.942 181.951 173.387 1.00 91.47  ? 1763 GLU A OE1   1 
ATOM   2508  O  OE2   . GLU A 1 1763 ? 222.162 180.866 171.919 1.00 88.60  ? 1763 GLU A OE2   1 
ATOM   2509  N  N     . THR A 1 1764 ? 224.943 185.280 175.602 1.00 80.57  ? 1764 THR A N     1 
ATOM   2510  C  CA    . THR A 1 1764 ? 226.342 185.604 175.864 1.00 81.84  ? 1764 THR A CA    1 
ATOM   2511  C  C     . THR A 1 1764 ? 226.789 185.060 177.215 1.00 82.45  ? 1764 THR A C     1 
ATOM   2512  O  O     . THR A 1 1764 ? 227.889 184.506 177.338 1.00 86.00  ? 1764 THR A O     1 
ATOM   2513  C  CB    . THR A 1 1764 ? 226.551 187.117 175.800 1.00 81.26  ? 1764 THR A CB    1 
ATOM   2514  O  OG1   . THR A 1 1764 ? 226.145 187.603 174.515 1.00 84.44  ? 1764 THR A OG1   1 
ATOM   2515  C  CG2   . THR A 1 1764 ? 228.013 187.463 176.026 1.00 78.56  ? 1764 THR A CG2   1 
ATOM   2516  N  N     . ALA A 1 1765 ? 225.947 185.202 178.241 1.00 87.06  ? 1765 ALA A N     1 
ATOM   2517  C  CA    . ALA A 1 1765 ? 226.295 184.679 179.558 1.00 85.42  ? 1765 ALA A CA    1 
ATOM   2518  C  C     . ALA A 1 1765 ? 226.442 183.163 179.528 1.00 93.35  ? 1765 ALA A C     1 
ATOM   2519  O  O     . ALA A 1 1765 ? 227.380 182.612 180.116 1.00 98.99  ? 1765 ALA A O     1 
ATOM   2520  C  CB    . ALA A 1 1765 ? 225.244 185.098 180.584 1.00 85.97  ? 1765 ALA A CB    1 
ATOM   2521  N  N     . LEU A 1 1766 ? 225.527 182.472 178.844 1.00 90.91  ? 1766 LEU A N     1 
ATOM   2522  C  CA    . LEU A 1 1766 ? 225.609 181.019 178.743 1.00 88.62  ? 1766 LEU A CA    1 
ATOM   2523  C  C     . LEU A 1 1766 ? 226.867 180.587 178.003 1.00 92.60  ? 1766 LEU A C     1 
ATOM   2524  O  O     . LEU A 1 1766 ? 227.520 179.612 178.394 1.00 97.65  ? 1766 LEU A O     1 
ATOM   2525  C  CB    . LEU A 1 1766 ? 224.365 180.470 178.046 1.00 86.29  ? 1766 LEU A CB    1 
ATOM   2526  C  CG    . LEU A 1 1766 ? 223.067 180.429 178.853 1.00 85.47  ? 1766 LEU A CG    1 
ATOM   2527  C  CD1   . LEU A 1 1766 ? 222.018 179.629 178.111 1.00 91.06  ? 1766 LEU A CD1   1 
ATOM   2528  C  CD2   . LEU A 1 1766 ? 223.301 179.840 180.229 1.00 84.62  ? 1766 LEU A CD2   1 
ATOM   2529  N  N     . SER A 1 1767 ? 227.221 181.296 176.929 1.00 95.60  ? 1767 SER A N     1 
ATOM   2530  C  CA    . SER A 1 1767 ? 228.450 180.979 176.211 1.00 94.59  ? 1767 SER A CA    1 
ATOM   2531  C  C     . SER A 1 1767 ? 229.675 181.239 177.079 1.00 94.42  ? 1767 SER A C     1 
ATOM   2532  O  O     . SER A 1 1767 ? 230.695 180.552 176.948 1.00 93.64  ? 1767 SER A O     1 
ATOM   2533  C  CB    . SER A 1 1767 ? 228.526 181.786 174.916 1.00 94.16  ? 1767 SER A CB    1 
ATOM   2534  O  OG    . SER A 1 1767 ? 227.446 181.467 174.055 1.00 96.99  ? 1767 SER A OG    1 
ATOM   2535  N  N     . SER A 1 1768 ? 229.596 182.233 177.967 1.00 103.84 ? 1768 SER A N     1 
ATOM   2536  C  CA    . SER A 1 1768 ? 230.721 182.524 178.851 1.00 104.70 ? 1768 SER A CA    1 
ATOM   2537  C  C     . SER A 1 1768 ? 231.015 181.356 179.784 1.00 106.99 ? 1768 SER A C     1 
ATOM   2538  O  O     . SER A 1 1768 ? 232.179 180.977 179.962 1.00 111.74 ? 1768 SER A O     1 
ATOM   2539  C  CB    . SER A 1 1768 ? 230.444 183.796 179.652 1.00 105.95 ? 1768 SER A CB    1 
ATOM   2540  O  OG    . SER A 1 1768 ? 230.530 184.945 178.828 1.00 106.91 ? 1768 SER A OG    1 
ATOM   2541  N  N     . MET A 1 1769 ? 229.981 180.769 180.389 1.00 105.87 ? 1769 MET A N     1 
ATOM   2542  C  CA    . MET A 1 1769 ? 230.188 179.636 181.281 1.00 107.46 ? 1769 MET A CA    1 
ATOM   2543  C  C     . MET A 1 1769 ? 230.073 178.292 180.576 1.00 110.85 ? 1769 MET A C     1 
ATOM   2544  O  O     . MET A 1 1769 ? 229.725 177.301 181.227 1.00 112.83 ? 1769 MET A O     1 
ATOM   2545  C  CB    . MET A 1 1769 ? 229.201 179.676 182.452 1.00 106.95 ? 1769 MET A CB    1 
ATOM   2546  C  CG    . MET A 1 1769 ? 228.637 181.046 182.760 1.00 107.40 ? 1769 MET A CG    1 
ATOM   2547  S  SD    . MET A 1 1769 ? 227.108 180.964 183.712 1.00 110.40 ? 1769 MET A SD    1 
ATOM   2548  C  CE    . MET A 1 1769 ? 225.884 180.977 182.412 1.00 107.15 ? 1769 MET A CE    1 
ATOM   2549  N  N     . GLY A 1 1770 ? 230.350 178.233 179.276 1.00 123.84 ? 1770 GLY A N     1 
ATOM   2550  C  CA    . GLY A 1 1770 ? 230.298 176.983 178.546 1.00 124.79 ? 1770 GLY A CA    1 
ATOM   2551  C  C     . GLY A 1 1770 ? 231.294 175.962 179.055 1.00 126.01 ? 1770 GLY A C     1 
ATOM   2552  O  O     . GLY A 1 1770 ? 231.097 174.754 178.889 1.00 124.62 ? 1770 GLY A O     1 
ATOM   2553  N  N     . GLY A 1 1771 ? 232.372 176.439 179.682 1.00 128.34 ? 1771 GLY A N     1 
ATOM   2554  C  CA    . GLY A 1 1771 ? 233.370 175.542 180.235 1.00 128.86 ? 1771 GLY A CA    1 
ATOM   2555  C  C     . GLY A 1 1771 ? 232.953 174.876 181.530 1.00 130.13 ? 1771 GLY A C     1 
ATOM   2556  O  O     . GLY A 1 1771 ? 233.654 173.976 182.004 1.00 129.71 ? 1771 GLY A O     1 
ATOM   2557  N  N     . GLY A 1 1772 ? 231.835 175.299 182.114 1.00 129.91 ? 1772 GLY A N     1 
ATOM   2558  C  CA    . GLY A 1 1772 ? 231.343 174.692 183.335 1.00 128.32 ? 1772 GLY A CA    1 
ATOM   2559  C  C     . GLY A 1 1772 ? 231.949 175.276 184.594 1.00 128.63 ? 1772 GLY A C     1 
ATOM   2560  O  O     . GLY A 1 1772 ? 231.226 175.715 185.493 1.00 126.98 ? 1772 GLY A O     1 
ATOM   2561  N  N     . GLY A 1 1773 ? 233.278 175.286 184.671 1.00 139.36 ? 1773 GLY A N     1 
ATOM   2562  C  CA    . GLY A 1 1773 ? 233.982 175.784 185.833 1.00 138.78 ? 1773 GLY A CA    1 
ATOM   2563  C  C     . GLY A 1 1773 ? 234.196 177.278 185.883 1.00 140.68 ? 1773 GLY A C     1 
ATOM   2564  O  O     . GLY A 1 1773 ? 234.842 177.769 186.813 1.00 139.94 ? 1773 GLY A O     1 
ATOM   2565  N  N     . ASP A 1 1774 ? 233.673 178.022 184.912 1.00 137.73 ? 1774 ASP A N     1 
ATOM   2566  C  CA    . ASP A 1 1774 ? 233.870 179.462 184.871 1.00 136.36 ? 1774 ASP A CA    1 
ATOM   2567  C  C     . ASP A 1 1774 ? 232.965 180.154 185.891 1.00 135.92 ? 1774 ASP A C     1 
ATOM   2568  O  O     . ASP A 1 1774 ? 232.301 179.519 186.716 1.00 134.81 ? 1774 ASP A O     1 
ATOM   2569  C  CB    . ASP A 1 1774 ? 233.610 179.991 183.462 1.00 134.76 ? 1774 ASP A CB    1 
ATOM   2570  C  CG    . ASP A 1 1774 ? 234.595 179.449 182.446 1.00 136.04 ? 1774 ASP A CG    1 
ATOM   2571  O  OD1   . ASP A 1 1774 ? 235.745 179.154 182.831 1.00 138.03 ? 1774 ASP A OD1   1 
ATOM   2572  O  OD2   . ASP A 1 1774 ? 234.219 179.320 181.261 1.00 134.29 ? 1774 ASP A OD2   1 
ATOM   2573  N  N     . ALA A 1 1775 ? 232.943 181.483 185.827 1.00 136.86 ? 1775 ALA A N     1 
ATOM   2574  C  CA    . ALA A 1 1775 ? 232.124 182.278 186.729 1.00 135.16 ? 1775 ALA A CA    1 
ATOM   2575  C  C     . ALA A 1 1775 ? 230.657 182.199 186.311 1.00 136.41 ? 1775 ALA A C     1 
ATOM   2576  O  O     . ALA A 1 1775 ? 230.268 181.419 185.438 1.00 136.50 ? 1775 ALA A O     1 
ATOM   2577  C  CB    . ALA A 1 1775 ? 232.614 183.724 186.753 1.00 131.09 ? 1775 ALA A CB    1 
ATOM   2578  N  N     . ALA A 1 1776 ? 229.823 183.019 186.953 1.00 117.82 ? 1776 ALA A N     1 
ATOM   2579  C  CA    . ALA A 1 1776 ? 228.381 183.036 186.707 1.00 111.88 ? 1776 ALA A CA    1 
ATOM   2580  C  C     . ALA A 1 1776 ? 227.933 184.452 186.370 1.00 110.18 ? 1776 ALA A C     1 
ATOM   2581  O  O     . ALA A 1 1776 ? 227.398 185.166 187.233 1.00 106.24 ? 1776 ALA A O     1 
ATOM   2582  C  CB    . ALA A 1 1776 ? 227.616 182.494 187.912 1.00 105.81 ? 1776 ALA A CB    1 
ATOM   2583  N  N     . PRO A 1 1777 ? 228.130 184.903 185.128 1.00 106.29 ? 1777 PRO A N     1 
ATOM   2584  C  CA    . PRO A 1 1777 ? 227.588 186.202 184.712 1.00 105.48 ? 1777 PRO A CA    1 
ATOM   2585  C  C     . PRO A 1 1777 ? 226.079 186.216 184.532 1.00 105.08 ? 1777 PRO A C     1 
ATOM   2586  O  O     . PRO A 1 1777 ? 225.519 187.284 184.263 1.00 106.08 ? 1777 PRO A O     1 
ATOM   2587  C  CB    . PRO A 1 1777 ? 228.300 186.459 183.375 1.00 102.29 ? 1777 PRO A CB    1 
ATOM   2588  C  CG    . PRO A 1 1777 ? 228.649 185.110 182.870 1.00 100.81 ? 1777 PRO A CG    1 
ATOM   2589  C  CD    . PRO A 1 1777 ? 228.971 184.296 184.084 1.00 104.78 ? 1777 PRO A CD    1 
ATOM   2590  N  N     . LEU A 1 1778 ? 225.408 185.067 184.656 1.00 95.64  ? 1778 LEU A N     1 
ATOM   2591  C  CA    . LEU A 1 1778 ? 223.949 185.058 184.619 1.00 94.77  ? 1778 LEU A CA    1 
ATOM   2592  C  C     . LEU A 1 1778 ? 223.365 185.883 185.756 1.00 99.14  ? 1778 LEU A C     1 
ATOM   2593  O  O     . LEU A 1 1778 ? 222.286 186.472 185.610 1.00 105.19 ? 1778 LEU A O     1 
ATOM   2594  C  CB    . LEU A 1 1778 ? 223.432 183.621 184.681 1.00 91.21  ? 1778 LEU A CB    1 
ATOM   2595  C  CG    . LEU A 1 1778 ? 222.887 183.040 183.376 1.00 95.42  ? 1778 LEU A CG    1 
ATOM   2596  C  CD1   . LEU A 1 1778 ? 222.335 181.643 183.604 1.00 99.39  ? 1778 LEU A CD1   1 
ATOM   2597  C  CD2   . LEU A 1 1778 ? 221.821 183.949 182.791 1.00 98.08  ? 1778 LEU A CD2   1 
ATOM   2598  N  N     . HIS A 1 1779 ? 224.062 185.936 186.894 1.00 96.05  ? 1779 HIS A N     1 
ATOM   2599  C  CA    . HIS A 1 1779 ? 223.643 186.814 187.978 1.00 95.15  ? 1779 HIS A CA    1 
ATOM   2600  C  C     . HIS A 1 1779 ? 223.668 188.273 187.549 1.00 95.16  ? 1779 HIS A C     1 
ATOM   2601  O  O     . HIS A 1 1779 ? 222.825 189.060 187.988 1.00 97.97  ? 1779 HIS A O     1 
ATOM   2602  C  CB    . HIS A 1 1779 ? 224.535 186.600 189.200 1.00 96.56  ? 1779 HIS A CB    1 
ATOM   2603  C  CG    . HIS A 1 1779 ? 224.242 185.336 189.947 1.00 99.68  ? 1779 HIS A CG    1 
ATOM   2604  N  ND1   . HIS A 1 1779 ? 225.123 184.277 189.990 1.00 99.71  ? 1779 HIS A ND1   1 
ATOM   2605  C  CD2   . HIS A 1 1779 ? 223.168 184.962 190.681 1.00 98.11  ? 1779 HIS A CD2   1 
ATOM   2606  C  CE1   . HIS A 1 1779 ? 224.603 183.304 190.717 1.00 97.54  ? 1779 HIS A CE1   1 
ATOM   2607  N  NE2   . HIS A 1 1779 ? 223.418 183.695 191.148 1.00 97.78  ? 1779 HIS A NE2   1 
ATOM   2608  N  N     . SER A 1 1780 ? 224.618 188.653 186.691 1.00 86.27  ? 1780 SER A N     1 
ATOM   2609  C  CA    . SER A 1 1780 ? 224.628 190.011 186.158 1.00 84.87  ? 1780 SER A CA    1 
ATOM   2610  C  C     . SER A 1 1780 ? 223.389 190.280 185.314 1.00 86.38  ? 1780 SER A C     1 
ATOM   2611  O  O     . SER A 1 1780 ? 222.798 191.363 185.392 1.00 90.49  ? 1780 SER A O     1 
ATOM   2612  C  CB    . SER A 1 1780 ? 225.897 190.249 185.339 1.00 86.61  ? 1780 SER A CB    1 
ATOM   2613  O  OG    . SER A 1 1780 ? 227.052 190.161 186.154 1.00 93.99  ? 1780 SER A OG    1 
ATOM   2614  N  N     . VAL A 1 1781 ? 222.981 189.304 184.498 1.00 79.14  ? 1781 VAL A N     1 
ATOM   2615  C  CA    . VAL A 1 1781 ? 221.771 189.463 183.695 1.00 81.61  ? 1781 VAL A CA    1 
ATOM   2616  C  C     . VAL A 1 1781 ? 220.549 189.597 184.593 1.00 84.74  ? 1781 VAL A C     1 
ATOM   2617  O  O     . VAL A 1 1781 ? 219.673 190.440 184.357 1.00 87.76  ? 1781 VAL A O     1 
ATOM   2618  C  CB    . VAL A 1 1781 ? 221.624 188.287 182.712 1.00 76.08  ? 1781 VAL A CB    1 
ATOM   2619  C  CG1   . VAL A 1 1781 ? 220.356 188.440 181.891 1.00 80.24  ? 1781 VAL A CG1   1 
ATOM   2620  C  CG2   . VAL A 1 1781 ? 222.841 188.198 181.809 1.00 78.85  ? 1781 VAL A CG2   1 
ATOM   2621  N  N     . LEU A 1 1782 ? 220.468 188.767 185.636 1.00 80.77  ? 1782 LEU A N     1 
ATOM   2622  C  CA    . LEU A 1 1782 ? 219.344 188.860 186.562 1.00 75.19  ? 1782 LEU A CA    1 
ATOM   2623  C  C     . LEU A 1 1782 ? 219.324 190.207 187.273 1.00 83.16  ? 1782 LEU A C     1 
ATOM   2624  O  O     . LEU A 1 1782 ? 218.257 190.802 187.460 1.00 86.49  ? 1782 LEU A O     1 
ATOM   2625  C  CB    . LEU A 1 1782 ? 219.399 187.719 187.576 1.00 78.86  ? 1782 LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1 1782 ? 218.268 187.701 188.605 1.00 81.48  ? 1782 LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1 1782 ? 216.921 187.585 187.913 1.00 79.90  ? 1782 LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1 1782 ? 218.461 186.569 189.600 1.00 83.89  ? 1782 LEU A CD2   1 
ATOM   2629  N  N     . SER A 1 1783 ? 220.495 190.704 187.678 1.00 88.84  ? 1783 SER A N     1 
ATOM   2630  C  CA    . SER A 1 1783 ? 220.565 192.005 188.336 1.00 83.87  ? 1783 SER A CA    1 
ATOM   2631  C  C     . SER A 1 1783 ? 220.146 193.126 187.396 1.00 86.09  ? 1783 SER A C     1 
ATOM   2632  O  O     . SER A 1 1783 ? 219.451 194.059 187.809 1.00 89.61  ? 1783 SER A O     1 
ATOM   2633  C  CB    . SER A 1 1783 ? 221.977 192.249 188.866 1.00 85.10  ? 1783 SER A CB    1 
ATOM   2634  O  OG    . SER A 1 1783 ? 222.234 191.460 190.013 1.00 91.78  ? 1783 SER A OG    1 
ATOM   2635  N  N     . ASN A 1 1784 ? 220.568 193.059 186.131 1.00 90.36  ? 1784 ASN A N     1 
ATOM   2636  C  CA    . ASN A 1 1784 ? 220.151 194.066 185.161 1.00 90.66  ? 1784 ASN A CA    1 
ATOM   2637  C  C     . ASN A 1 1784 ? 218.642 194.037 184.957 1.00 88.36  ? 1784 ASN A C     1 
ATOM   2638  O  O     . ASN A 1 1784 ? 217.991 195.089 184.903 1.00 88.28  ? 1784 ASN A O     1 
ATOM   2639  C  CB    . ASN A 1 1784 ? 220.880 193.847 183.835 1.00 87.53  ? 1784 ASN A CB    1 
ATOM   2640  C  CG    . ASN A 1 1784 ? 220.742 195.022 182.889 1.00 92.87  ? 1784 ASN A CG    1 
ATOM   2641  O  OD1   . ASN A 1 1784 ? 219.636 195.404 182.508 1.00 97.19  ? 1784 ASN A OD1   1 
ATOM   2642  N  ND2   . ASN A 1 1784 ? 221.871 195.605 182.506 1.00 94.59  ? 1784 ASN A ND2   1 
ATOM   2643  N  N     . VAL A 1 1785 ? 218.067 192.836 184.850 1.00 81.94  ? 1785 VAL A N     1 
ATOM   2644  C  CA    . VAL A 1 1785 ? 216.622 192.716 184.685 1.00 80.52  ? 1785 VAL A CA    1 
ATOM   2645  C  C     . VAL A 1 1785 ? 215.902 193.282 185.901 1.00 82.73  ? 1785 VAL A C     1 
ATOM   2646  O  O     . VAL A 1 1785 ? 214.897 193.988 185.771 1.00 85.90  ? 1785 VAL A O     1 
ATOM   2647  C  CB    . VAL A 1 1785 ? 216.232 191.250 184.422 1.00 79.73  ? 1785 VAL A CB    1 
ATOM   2648  C  CG1   . VAL A 1 1785 ? 214.734 191.058 184.586 1.00 76.85  ? 1785 VAL A CG1   1 
ATOM   2649  C  CG2   . VAL A 1 1785 ? 216.674 190.827 183.033 1.00 79.77  ? 1785 VAL A CG2   1 
ATOM   2650  N  N     . GLU A 1 1786 ? 216.408 192.990 187.101 1.00 81.42  ? 1786 GLU A N     1 
ATOM   2651  C  CA    . GLU A 1 1786 ? 215.776 193.493 188.317 1.00 78.84  ? 1786 GLU A CA    1 
ATOM   2652  C  C     . GLU A 1 1786 ? 215.879 195.010 188.416 1.00 85.93  ? 1786 GLU A C     1 
ATOM   2653  O  O     . GLU A 1 1786 ? 214.933 195.672 188.857 1.00 92.20  ? 1786 GLU A O     1 
ATOM   2654  C  CB    . GLU A 1 1786 ? 216.399 192.829 189.544 1.00 83.37  ? 1786 GLU A CB    1 
ATOM   2655  C  CG    . GLU A 1 1786 ? 215.732 191.525 189.943 1.00 89.86  ? 1786 GLU A CG    1 
ATOM   2656  C  CD    . GLU A 1 1786 ? 216.506 190.778 191.011 1.00 93.91  ? 1786 GLU A CD    1 
ATOM   2657  O  OE1   . GLU A 1 1786 ? 217.691 191.108 191.229 1.00 90.73  ? 1786 GLU A OE1   1 
ATOM   2658  O  OE2   . GLU A 1 1786 ? 215.930 189.860 191.630 1.00 94.01  ? 1786 GLU A OE2   1 
ATOM   2659  N  N     . VAL A 1 1787 ? 217.018 195.580 188.020 1.00 83.01  ? 1787 VAL A N     1 
ATOM   2660  C  CA    . VAL A 1 1787 ? 217.176 197.033 188.051 1.00 83.68  ? 1787 VAL A CA    1 
ATOM   2661  C  C     . VAL A 1 1787 ? 216.205 197.691 187.078 1.00 82.93  ? 1787 VAL A C     1 
ATOM   2662  O  O     . VAL A 1 1787 ? 215.539 198.683 187.407 1.00 85.05  ? 1787 VAL A O     1 
ATOM   2663  C  CB    . VAL A 1 1787 ? 218.634 197.421 187.743 1.00 83.81  ? 1787 VAL A CB    1 
ATOM   2664  C  CG1   . VAL A 1 1787 ? 218.727 198.889 187.361 1.00 84.69  ? 1787 VAL A CG1   1 
ATOM   2665  C  CG2   . VAL A 1 1787 ? 219.524 197.121 188.937 1.00 86.05  ? 1787 VAL A CG2   1 
ATOM   2666  N  N     . THR A 1 1788 ? 216.104 197.142 185.865 1.00 72.48  ? 1788 THR A N     1 
ATOM   2667  C  CA    . THR A 1 1788 ? 215.165 197.688 184.892 1.00 69.16  ? 1788 THR A CA    1 
ATOM   2668  C  C     . THR A 1 1788 ? 213.727 197.549 185.380 1.00 71.71  ? 1788 THR A C     1 
ATOM   2669  O  O     . THR A 1 1788 ? 212.908 198.455 185.185 1.00 77.46  ? 1788 THR A O     1 
ATOM   2670  C  CB    . THR A 1 1788 ? 215.341 196.996 183.542 1.00 69.10  ? 1788 THR A CB    1 
ATOM   2671  O  OG1   . THR A 1 1788 ? 216.725 196.685 183.339 1.00 76.65  ? 1788 THR A OG1   1 
ATOM   2672  C  CG2   . THR A 1 1788 ? 214.869 197.903 182.420 1.00 75.12  ? 1788 THR A CG2   1 
ATOM   2673  N  N     . LEU A 1 1789 ? 213.406 196.424 186.021 1.00 68.30  ? 1789 LEU A N     1 
ATOM   2674  C  CA    . LEU A 1 1789 ? 212.064 196.224 186.556 1.00 66.00  ? 1789 LEU A CA    1 
ATOM   2675  C  C     . LEU A 1 1789 ? 211.757 197.216 187.669 1.00 69.54  ? 1789 LEU A C     1 
ATOM   2676  O  O     . LEU A 1 1789 ? 210.633 197.715 187.765 1.00 76.65  ? 1789 LEU A O     1 
ATOM   2677  C  CB    . LEU A 1 1789 ? 211.911 194.789 187.059 1.00 67.40  ? 1789 LEU A CB    1 
ATOM   2678  C  CG    . LEU A 1 1789 ? 210.482 194.283 187.248 1.00 64.17  ? 1789 LEU A CG    1 
ATOM   2679  C  CD1   . LEU A 1 1789 ? 209.649 194.564 186.012 1.00 63.31  ? 1789 LEU A CD1   1 
ATOM   2680  C  CD2   . LEU A 1 1789 ? 210.482 192.800 187.573 1.00 67.74  ? 1789 LEU A CD2   1 
ATOM   2681  N  N     . ASN A 1 1790 ? 212.736 197.502 188.530 1.00 69.52  ? 1790 ASN A N     1 
ATOM   2682  C  CA    . ASN A 1 1790 ? 212.531 198.498 189.577 1.00 75.31  ? 1790 ASN A CA    1 
ATOM   2683  C  C     . ASN A 1 1790 ? 212.312 199.882 188.980 1.00 79.36  ? 1790 ASN A C     1 
ATOM   2684  O  O     . ASN A 1 1790 ? 211.443 200.637 189.438 1.00 79.22  ? 1790 ASN A O     1 
ATOM   2685  C  CB    . ASN A 1 1790 ? 213.723 198.510 190.533 1.00 75.28  ? 1790 ASN A CB    1 
ATOM   2686  C  CG    . ASN A 1 1790 ? 213.815 197.247 191.365 1.00 78.20  ? 1790 ASN A CG    1 
ATOM   2687  O  OD1   . ASN A 1 1790 ? 212.822 196.547 191.563 1.00 77.22  ? 1790 ASN A OD1   1 
ATOM   2688  N  ND2   . ASN A 1 1790 ? 215.011 196.948 191.856 1.00 78.18  ? 1790 ASN A ND2   1 
ATOM   2689  N  N     . VAL A 1 1791 ? 213.091 200.230 187.953 1.00 73.62  ? 1791 VAL A N     1 
ATOM   2690  C  CA    . VAL A 1 1791 ? 212.912 201.517 187.285 1.00 68.71  ? 1791 VAL A CA    1 
ATOM   2691  C  C     . VAL A 1 1791 ? 211.519 201.609 186.676 1.00 70.35  ? 1791 VAL A C     1 
ATOM   2692  O  O     . VAL A 1 1791 ? 210.848 202.644 186.772 1.00 71.91  ? 1791 VAL A O     1 
ATOM   2693  C  CB    . VAL A 1 1791 ? 214.009 201.725 186.225 1.00 66.03  ? 1791 VAL A CB    1 
ATOM   2694  C  CG1   . VAL A 1 1791 ? 213.665 202.899 185.321 1.00 66.25  ? 1791 VAL A CG1   1 
ATOM   2695  C  CG2   . VAL A 1 1791 ? 215.357 201.939 186.894 1.00 71.86  ? 1791 VAL A CG2   1 
ATOM   2696  N  N     . LEU A 1 1792 ? 211.063 200.527 186.042 1.00 66.48  ? 1792 LEU A N     1 
ATOM   2697  C  CA    . LEU A 1 1792 ? 209.723 200.510 185.463 1.00 58.31  ? 1792 LEU A CA    1 
ATOM   2698  C  C     . LEU A 1 1792 ? 208.649 200.626 186.537 1.00 67.28  ? 1792 LEU A C     1 
ATOM   2699  O  O     . LEU A 1 1792 ? 207.669 201.361 186.368 1.00 71.13  ? 1792 LEU A O     1 
ATOM   2700  C  CB    . LEU A 1 1792 ? 209.528 199.233 184.650 1.00 62.51  ? 1792 LEU A CB    1 
ATOM   2701  C  CG    . LEU A 1 1792 ? 209.714 199.325 183.137 1.00 66.38  ? 1792 LEU A CG    1 
ATOM   2702  C  CD1   . LEU A 1 1792 ? 210.938 200.146 182.797 1.00 65.59  ? 1792 LEU A CD1   1 
ATOM   2703  C  CD2   . LEU A 1 1792 ? 209.836 197.932 182.559 1.00 69.91  ? 1792 LEU A CD2   1 
ATOM   2704  N  N     . ALA A 1 1793 ? 208.814 199.906 187.649 1.00 73.97  ? 1793 ALA A N     1 
ATOM   2705  C  CA    . ALA A 1 1793 ? 207.816 199.929 188.712 1.00 66.66  ? 1793 ALA A CA    1 
ATOM   2706  C  C     . ALA A 1 1793 ? 207.702 201.312 189.335 1.00 70.39  ? 1793 ALA A C     1 
ATOM   2707  O  O     . ALA A 1 1793 ? 206.596 201.773 189.635 1.00 75.63  ? 1793 ALA A O     1 
ATOM   2708  C  CB    . ALA A 1 1793 ? 208.159 198.888 189.776 1.00 65.75  ? 1793 ALA A CB    1 
ATOM   2709  N  N     . ASP A 1 1794 ? 208.834 201.988 189.542 1.00 83.85  ? 1794 ASP A N     1 
ATOM   2710  C  CA    . ASP A 1 1794 ? 208.783 203.356 190.048 1.00 86.06  ? 1794 ASP A CA    1 
ATOM   2711  C  C     . ASP A 1 1794 ? 208.089 204.283 189.057 1.00 84.38  ? 1794 ASP A C     1 
ATOM   2712  O  O     . ASP A 1 1794 ? 207.441 205.258 189.456 1.00 87.19  ? 1794 ASP A O     1 
ATOM   2713  C  CB    . ASP A 1 1794 ? 210.194 203.856 190.355 1.00 89.37  ? 1794 ASP A CB    1 
ATOM   2714  C  CG    . ASP A 1 1794 ? 210.816 203.150 191.543 1.00 93.45  ? 1794 ASP A CG    1 
ATOM   2715  O  OD1   . ASP A 1 1794 ? 210.159 202.253 192.112 1.00 93.07  ? 1794 ASP A OD1   1 
ATOM   2716  O  OD2   . ASP A 1 1794 ? 211.960 203.492 191.907 1.00 93.27  ? 1794 ASP A OD2   1 
ATOM   2717  N  N     . SER A 1 1795 ? 208.214 203.995 187.759 1.00 80.96  ? 1795 SER A N     1 
ATOM   2718  C  CA    . SER A 1 1795 ? 207.617 204.858 186.745 1.00 81.25  ? 1795 SER A CA    1 
ATOM   2719  C  C     . SER A 1 1795 ? 206.094 204.804 186.782 1.00 81.29  ? 1795 SER A C     1 
ATOM   2720  O  O     . SER A 1 1795 ? 205.428 205.837 186.654 1.00 81.38  ? 1795 SER A O     1 
ATOM   2721  C  CB    . SER A 1 1795 ? 208.131 204.468 185.360 1.00 85.72  ? 1795 SER A CB    1 
ATOM   2722  O  OG    . SER A 1 1795 ? 208.165 205.592 184.498 1.00 86.61  ? 1795 SER A OG    1 
ATOM   2723  N  N     . VAL A 1 1796 ? 205.520 203.609 186.948 1.00 77.26  ? 1796 VAL A N     1 
ATOM   2724  C  CA    . VAL A 1 1796 ? 204.064 203.476 186.937 1.00 77.80  ? 1796 VAL A CA    1 
ATOM   2725  C  C     . VAL A 1 1796 ? 203.421 203.947 188.231 1.00 83.23  ? 1796 VAL A C     1 
ATOM   2726  O  O     . VAL A 1 1796 ? 202.217 204.235 188.244 1.00 83.87  ? 1796 VAL A O     1 
ATOM   2727  C  CB    . VAL A 1 1796 ? 203.659 202.019 186.645 1.00 71.11  ? 1796 VAL A CB    1 
ATOM   2728  C  CG1   . VAL A 1 1796 ? 202.213 201.943 186.186 1.00 77.60  ? 1796 VAL A CG1   1 
ATOM   2729  C  CG2   . VAL A 1 1796 ? 204.565 201.435 185.586 1.00 73.84  ? 1796 VAL A CG2   1 
ATOM   2730  N  N     . LEU A 1 1797 ? 204.188 204.060 189.314 1.00 92.78  ? 1797 LEU A N     1 
ATOM   2731  C  CA    . LEU A 1 1797 ? 203.659 204.567 190.574 1.00 88.37  ? 1797 LEU A CA    1 
ATOM   2732  C  C     . LEU A 1 1797 ? 203.290 206.043 190.510 1.00 90.71  ? 1797 LEU A C     1 
ATOM   2733  O  O     . LEU A 1 1797 ? 202.620 206.535 191.424 1.00 92.24  ? 1797 LEU A O     1 
ATOM   2734  C  CB    . LEU A 1 1797 ? 204.670 204.336 191.700 1.00 87.31  ? 1797 LEU A CB    1 
ATOM   2735  C  CG    . LEU A 1 1797 ? 204.419 203.140 192.622 1.00 88.13  ? 1797 LEU A CG    1 
ATOM   2736  C  CD1   . LEU A 1 1797 ? 204.230 201.860 191.826 1.00 88.13  ? 1797 LEU A CD1   1 
ATOM   2737  C  CD2   . LEU A 1 1797 ? 205.556 202.988 193.622 1.00 90.33  ? 1797 LEU A CD2   1 
ATOM   2738  N  N     . MET A 1 1798 ? 203.703 206.755 189.465 1.00 107.71 ? 1798 MET A N     1 
ATOM   2739  C  CA    . MET A 1 1798 ? 203.358 208.155 189.273 1.00 107.09 ? 1798 MET A CA    1 
ATOM   2740  C  C     . MET A 1 1798 ? 202.500 208.290 188.022 1.00 107.54 ? 1798 MET A C     1 
ATOM   2741  O  O     . MET A 1 1798 ? 202.235 207.316 187.314 1.00 110.52 ? 1798 MET A O     1 
ATOM   2742  C  CB    . MET A 1 1798 ? 204.612 209.034 189.165 1.00 104.88 ? 1798 MET A CB    1 
ATOM   2743  C  CG    . MET A 1 1798 ? 205.514 208.690 187.994 1.00 104.77 ? 1798 MET A CG    1 
ATOM   2744  S  SD    . MET A 1 1798 ? 207.045 209.641 187.991 1.00 116.13 ? 1798 MET A SD    1 
ATOM   2745  C  CE    . MET A 1 1798 ? 207.405 209.705 189.744 1.00 109.63 ? 1798 MET A CE    1 
ATOM   2746  N  N     . GLU A 1 1799 ? 202.059 209.518 187.756 1.00 114.93 ? 1799 GLU A N     1 
ATOM   2747  C  CA    . GLU A 1 1799 ? 201.193 209.768 186.612 1.00 113.35 ? 1799 GLU A CA    1 
ATOM   2748  C  C     . GLU A 1 1799 ? 201.978 209.634 185.311 1.00 116.46 ? 1799 GLU A C     1 
ATOM   2749  O  O     . GLU A 1 1799 ? 203.154 210.006 185.238 1.00 117.29 ? 1799 GLU A O     1 
ATOM   2750  C  CB    . GLU A 1 1799 ? 200.554 211.155 186.723 1.00 113.80 ? 1799 GLU A CB    1 
ATOM   2751  C  CG    . GLU A 1 1799 ? 201.340 212.317 186.107 1.00 116.50 ? 1799 GLU A CG    1 
ATOM   2752  C  CD    . GLU A 1 1799 ? 202.698 212.563 186.754 1.00 120.31 ? 1799 GLU A CD    1 
ATOM   2753  O  OE1   . GLU A 1 1799 ? 203.438 213.434 186.249 1.00 120.54 ? 1799 GLU A OE1   1 
ATOM   2754  O  OE2   . GLU A 1 1799 ? 203.027 211.910 187.766 1.00 120.99 ? 1799 GLU A OE2   1 
ATOM   2755  N  N     . GLN A 1 1800 ? 201.339 209.067 184.298 1.00 102.40 ? 1800 GLN A N     1 
ATOM   2756  C  CA    . GLN A 1 1800 ? 201.913 208.892 182.975 1.00 100.52 ? 1800 GLN A CA    1 
ATOM   2757  C  C     . GLN A 1 1800 ? 200.845 209.134 181.922 1.00 100.69 ? 1800 GLN A C     1 
ATOM   2758  O  O     . GLN A 1 1800 ? 199.650 208.963 182.186 1.00 100.29 ? 1800 GLN A O     1 
ATOM   2759  C  CB    . GLN A 1 1800 ? 202.497 207.481 182.792 1.00 97.84  ? 1800 GLN A CB    1 
ATOM   2760  C  CG    . GLN A 1 1800 ? 203.421 207.012 183.904 1.00 96.07  ? 1800 GLN A CG    1 
ATOM   2761  C  CD    . GLN A 1 1800 ? 204.824 207.569 183.774 1.00 100.29 ? 1800 GLN A CD    1 
ATOM   2762  O  OE1   . GLN A 1 1800 ? 205.112 208.354 182.872 1.00 101.36 ? 1800 GLN A OE1   1 
ATOM   2763  N  NE2   . GLN A 1 1800 ? 205.707 207.163 184.678 1.00 101.76 ? 1800 GLN A NE2   1 
ATOM   2764  N  N     . PRO A 1 1801 ? 201.242 209.545 180.719 1.00 94.57  ? 1801 PRO A N     1 
ATOM   2765  C  CA    . PRO A 1 1801 ? 200.292 209.564 179.613 1.00 91.46  ? 1801 PRO A CA    1 
ATOM   2766  C  C     . PRO A 1 1801 ? 199.808 208.160 179.312 1.00 98.29  ? 1801 PRO A C     1 
ATOM   2767  O  O     . PRO A 1 1801 ? 200.539 207.175 179.523 1.00 102.74 ? 1801 PRO A O     1 
ATOM   2768  C  CB    . PRO A 1 1801 ? 201.114 210.140 178.451 1.00 92.89  ? 1801 PRO A CB    1 
ATOM   2769  C  CG    . PRO A 1 1801 ? 202.220 210.895 179.104 1.00 91.37  ? 1801 PRO A CG    1 
ATOM   2770  C  CD    . PRO A 1 1801 ? 202.540 210.132 180.349 1.00 92.50  ? 1801 PRO A CD    1 
ATOM   2771  N  N     . PRO A 1 1802 ? 198.568 208.017 178.832 1.00 99.28  ? 1802 PRO A N     1 
ATOM   2772  C  CA    . PRO A 1 1802 ? 198.007 206.664 178.654 1.00 99.26  ? 1802 PRO A CA    1 
ATOM   2773  C  C     . PRO A 1 1802 ? 198.831 205.767 177.745 1.00 96.47  ? 1802 PRO A C     1 
ATOM   2774  O  O     . PRO A 1 1802 ? 198.988 204.576 178.041 1.00 95.99  ? 1802 PRO A O     1 
ATOM   2775  C  CB    . PRO A 1 1802 ? 196.615 206.942 178.068 1.00 99.94  ? 1802 PRO A CB    1 
ATOM   2776  C  CG    . PRO A 1 1802 ? 196.301 208.346 178.474 1.00 99.59  ? 1802 PRO A CG    1 
ATOM   2777  C  CD    . PRO A 1 1802 ? 197.610 209.069 178.458 1.00 94.81  ? 1802 PRO A CD    1 
ATOM   2778  N  N     . LEU A 1 1803 ? 199.375 206.305 176.652 1.00 92.29  ? 1803 LEU A N     1 
ATOM   2779  C  CA    . LEU A 1 1803 ? 200.181 205.487 175.751 1.00 88.90  ? 1803 LEU A CA    1 
ATOM   2780  C  C     . LEU A 1 1803 ? 201.456 205.013 176.437 1.00 89.88  ? 1803 LEU A C     1 
ATOM   2781  O  O     . LEU A 1 1803 ? 201.815 203.830 176.363 1.00 92.91  ? 1803 LEU A O     1 
ATOM   2782  C  CB    . LEU A 1 1803 ? 200.508 206.272 174.482 1.00 92.13  ? 1803 LEU A CB    1 
ATOM   2783  C  CG    . LEU A 1 1803 ? 201.311 205.517 173.424 1.00 94.60  ? 1803 LEU A CG    1 
ATOM   2784  C  CD1   . LEU A 1 1803 ? 200.545 204.294 172.958 1.00 90.89  ? 1803 LEU A CD1   1 
ATOM   2785  C  CD2   . LEU A 1 1803 ? 201.639 206.426 172.250 1.00 95.47  ? 1803 LEU A CD2   1 
ATOM   2786  N  N     . ARG A 1 1804 ? 202.152 205.926 177.117 1.00 81.98  ? 1804 ARG A N     1 
ATOM   2787  C  CA    . ARG A 1 1804 ? 203.347 205.534 177.853 1.00 79.89  ? 1804 ARG A CA    1 
ATOM   2788  C  C     . ARG A 1 1804 ? 203.004 204.593 178.997 1.00 80.79  ? 1804 ARG A C     1 
ATOM   2789  O  O     . ARG A 1 1804 ? 203.798 203.708 179.327 1.00 90.58  ? 1804 ARG A O     1 
ATOM   2790  C  CB    . ARG A 1 1804 ? 204.078 206.770 178.375 1.00 79.67  ? 1804 ARG A CB    1 
ATOM   2791  C  CG    . ARG A 1 1804 ? 205.461 206.475 178.925 1.00 82.50  ? 1804 ARG A CG    1 
ATOM   2792  C  CD    . ARG A 1 1804 ? 205.930 207.567 179.867 1.00 83.97  ? 1804 ARG A CD    1 
ATOM   2793  N  NE    . ARG A 1 1804 ? 206.257 208.800 179.161 1.00 85.97  ? 1804 ARG A NE    1 
ATOM   2794  C  CZ    . ARG A 1 1804 ? 206.473 209.966 179.754 1.00 86.78  ? 1804 ARG A CZ    1 
ATOM   2795  N  NH1   . ARG A 1 1804 ? 206.404 210.096 181.068 1.00 89.41  ? 1804 ARG A NH1   1 
ATOM   2796  N  NH2   . ARG A 1 1804 ? 206.766 211.027 179.009 1.00 85.30  ? 1804 ARG A NH2   1 
ATOM   2797  N  N     . ARG A 1 1805 ? 201.828 204.758 179.605 1.00 71.93  ? 1805 ARG A N     1 
ATOM   2798  C  CA    . ARG A 1 1805 ? 201.412 203.841 180.661 1.00 75.68  ? 1805 ARG A CA    1 
ATOM   2799  C  C     . ARG A 1 1805 ? 201.207 202.430 180.121 1.00 81.82  ? 1805 ARG A C     1 
ATOM   2800  O  O     . ARG A 1 1805 ? 201.627 201.451 180.749 1.00 83.58  ? 1805 ARG A O     1 
ATOM   2801  C  CB    . ARG A 1 1805 ? 200.139 204.357 181.330 1.00 78.16  ? 1805 ARG A CB    1 
ATOM   2802  C  CG    . ARG A 1 1805 ? 199.826 203.695 182.660 1.00 77.43  ? 1805 ARG A CG    1 
ATOM   2803  C  CD    . ARG A 1 1805 ? 198.373 203.905 183.043 1.00 84.46  ? 1805 ARG A CD    1 
ATOM   2804  N  NE    . ARG A 1 1805 ? 197.470 203.106 182.224 1.00 89.66  ? 1805 ARG A NE    1 
ATOM   2805  C  CZ    . ARG A 1 1805 ? 196.471 203.604 181.510 1.00 86.11  ? 1805 ARG A CZ    1 
ATOM   2806  N  NH1   . ARG A 1 1805 ? 196.216 204.902 181.488 1.00 80.37  ? 1805 ARG A NH1   1 
ATOM   2807  N  NH2   . ARG A 1 1805 ? 195.707 202.779 180.798 1.00 82.92  ? 1805 ARG A NH2   1 
ATOM   2808  N  N     . ARG A 1 1806 ? 200.568 202.303 178.955 1.00 84.63  ? 1806 ARG A N     1 
ATOM   2809  C  CA    . ARG A 1 1806 ? 200.402 200.982 178.351 1.00 75.48  ? 1806 ARG A CA    1 
ATOM   2810  C  C     . ARG A 1 1806 ? 201.747 200.384 177.956 1.00 78.69  ? 1806 ARG A C     1 
ATOM   2811  O  O     . ARG A 1 1806 ? 201.972 199.177 178.125 1.00 88.55  ? 1806 ARG A O     1 
ATOM   2812  C  CB    . ARG A 1 1806 ? 199.473 201.065 177.141 1.00 76.35  ? 1806 ARG A CB    1 
ATOM   2813  C  CG    . ARG A 1 1806 ? 198.100 201.631 177.456 1.00 79.83  ? 1806 ARG A CG    1 
ATOM   2814  C  CD    . ARG A 1 1806 ? 197.070 200.532 177.643 1.00 77.92  ? 1806 ARG A CD    1 
ATOM   2815  N  NE    . ARG A 1 1806 ? 196.864 199.762 176.423 1.00 83.39  ? 1806 ARG A NE    1 
ATOM   2816  C  CZ    . ARG A 1 1806 ? 196.086 200.144 175.419 1.00 84.07  ? 1806 ARG A CZ    1 
ATOM   2817  N  NH1   . ARG A 1 1806 ? 195.430 201.292 175.453 1.00 83.73  ? 1806 ARG A NH1   1 
ATOM   2818  N  NH2   . ARG A 1 1806 ? 195.962 199.354 174.357 1.00 80.69  ? 1806 ARG A NH2   1 
ATOM   2819  N  N     . LYS A 1 1807 ? 202.652 201.210 177.426 1.00 68.75  ? 1807 LYS A N     1 
ATOM   2820  C  CA    . LYS A 1 1807 ? 203.987 200.721 177.096 1.00 67.84  ? 1807 LYS A CA    1 
ATOM   2821  C  C     . LYS A 1 1807 ? 204.709 200.217 178.340 1.00 74.11  ? 1807 LYS A C     1 
ATOM   2822  O  O     . LYS A 1 1807 ? 205.360 199.166 178.308 1.00 83.69  ? 1807 LYS A O     1 
ATOM   2823  C  CB    . LYS A 1 1807 ? 204.799 201.823 176.418 1.00 71.99  ? 1807 LYS A CB    1 
ATOM   2824  C  CG    . LYS A 1 1807 ? 204.347 202.157 175.010 1.00 73.23  ? 1807 LYS A CG    1 
ATOM   2825  C  CD    . LYS A 1 1807 ? 205.251 203.205 174.386 1.00 73.88  ? 1807 LYS A CD    1 
ATOM   2826  C  CE    . LYS A 1 1807 ? 204.661 203.746 173.097 1.00 74.12  ? 1807 LYS A CE    1 
ATOM   2827  N  NZ    . LYS A 1 1807 ? 205.477 204.860 172.545 1.00 78.38  ? 1807 LYS A NZ    1 
ATOM   2828  N  N     . LEU A 1 1808 ? 204.599 200.954 179.447 1.00 68.05  ? 1808 LEU A N     1 
ATOM   2829  C  CA    . LEU A 1 1808 ? 205.236 200.532 180.689 1.00 63.15  ? 1808 LEU A CA    1 
ATOM   2830  C  C     . LEU A 1 1808 ? 204.612 199.251 181.224 1.00 66.46  ? 1808 LEU A C     1 
ATOM   2831  O  O     . LEU A 1 1808 ? 205.315 198.397 181.770 1.00 68.77  ? 1808 LEU A O     1 
ATOM   2832  C  CB    . LEU A 1 1808 ? 205.151 201.647 181.731 1.00 58.59  ? 1808 LEU A CB    1 
ATOM   2833  C  CG    . LEU A 1 1808 ? 206.071 202.846 181.504 1.00 58.43  ? 1808 LEU A CG    1 
ATOM   2834  C  CD1   . LEU A 1 1808 ? 205.667 204.006 182.395 1.00 67.91  ? 1808 LEU A CD1   1 
ATOM   2835  C  CD2   . LEU A 1 1808 ? 207.518 202.461 181.749 1.00 63.58  ? 1808 LEU A CD2   1 
ATOM   2836  N  N     . GLU A 1 1809 ? 203.293 199.099 181.088 1.00 62.32  ? 1809 GLU A N     1 
ATOM   2837  C  CA    . GLU A 1 1809 ? 202.652 197.859 181.516 1.00 61.76  ? 1809 GLU A CA    1 
ATOM   2838  C  C     . GLU A 1 1809 ? 203.157 196.670 180.706 1.00 66.94  ? 1809 GLU A C     1 
ATOM   2839  O  O     . GLU A 1 1809 ? 203.475 195.611 181.267 1.00 80.47  ? 1809 GLU A O     1 
ATOM   2840  C  CB    . GLU A 1 1809 ? 201.134 197.981 181.394 1.00 67.18  ? 1809 GLU A CB    1 
ATOM   2841  C  CG    . GLU A 1 1809 ? 200.501 198.937 182.390 1.00 75.70  ? 1809 GLU A CG    1 
ATOM   2842  C  CD    . GLU A 1 1809 ? 199.022 199.149 182.132 1.00 79.22  ? 1809 GLU A CD    1 
ATOM   2843  O  OE1   . GLU A 1 1809 ? 198.480 198.505 181.210 1.00 78.82  ? 1809 GLU A OE1   1 
ATOM   2844  O  OE2   . GLU A 1 1809 ? 198.402 199.961 182.849 1.00 76.39  ? 1809 GLU A OE2   1 
ATOM   2845  N  N     . HIS A 1 1810 ? 203.242 196.830 179.382 1.00 54.63  ? 1810 HIS A N     1 
ATOM   2846  C  CA    . HIS A 1 1810 ? 203.756 195.752 178.542 1.00 52.11  ? 1810 HIS A CA    1 
ATOM   2847  C  C     . HIS A 1 1810 ? 205.196 195.415 178.906 1.00 58.64  ? 1810 HIS A C     1 
ATOM   2848  O  O     . HIS A 1 1810 ? 205.562 194.236 179.014 1.00 67.10  ? 1810 HIS A O     1 
ATOM   2849  C  CB    . HIS A 1 1810 ? 203.663 196.138 177.066 1.00 46.29  ? 1810 HIS A CB    1 
ATOM   2850  C  CG    . HIS A 1 1810 ? 202.267 196.389 176.589 1.00 62.74  ? 1810 HIS A CG    1 
ATOM   2851  N  ND1   . HIS A 1 1810 ? 201.167 196.286 177.412 1.00 72.81  ? 1810 HIS A ND1   1 
ATOM   2852  C  CD2   . HIS A 1 1810 ? 201.792 196.733 175.369 1.00 66.76  ? 1810 HIS A CD2   1 
ATOM   2853  C  CE1   . HIS A 1 1810 ? 200.075 196.560 176.721 1.00 73.07  ? 1810 HIS A CE1   1 
ATOM   2854  N  NE2   . HIS A 1 1810 ? 200.427 196.834 175.478 1.00 73.84  ? 1810 HIS A NE2   1 
ATOM   2855  N  N     . LEU A 1 1811 ? 206.024 196.441 179.110 1.00 59.17  ? 1811 LEU A N     1 
ATOM   2856  C  CA    . LEU A 1 1811 ? 207.418 196.207 179.464 1.00 57.02  ? 1811 LEU A CA    1 
ATOM   2857  C  C     . LEU A 1 1811 ? 207.540 195.527 180.821 1.00 63.15  ? 1811 LEU A C     1 
ATOM   2858  O  O     . LEU A 1 1811 ? 208.395 194.657 181.007 1.00 69.49  ? 1811 LEU A O     1 
ATOM   2859  C  CB    . LEU A 1 1811 ? 208.189 197.524 179.450 1.00 57.30  ? 1811 LEU A CB    1 
ATOM   2860  C  CG    . LEU A 1 1811 ? 208.885 197.860 178.134 1.00 54.74  ? 1811 LEU A CG    1 
ATOM   2861  C  CD1   . LEU A 1 1811 ? 209.557 199.214 178.223 1.00 66.17  ? 1811 LEU A CD1   1 
ATOM   2862  C  CD2   . LEU A 1 1811 ? 209.891 196.782 177.782 1.00 62.34  ? 1811 LEU A CD2   1 
ATOM   2863  N  N     . ILE A 1 1812 ? 206.698 195.911 181.782 1.00 64.83  ? 1812 ILE A N     1 
ATOM   2864  C  CA    . ILE A 1 1812 ? 206.741 195.290 183.102 1.00 58.22  ? 1812 ILE A CA    1 
ATOM   2865  C  C     . ILE A 1 1812 ? 206.369 193.819 183.012 1.00 64.46  ? 1812 ILE A C     1 
ATOM   2866  O  O     . ILE A 1 1812 ? 207.022 192.965 183.621 1.00 79.90  ? 1812 ILE A O     1 
ATOM   2867  C  CB    . ILE A 1 1812 ? 205.827 196.044 184.085 1.00 54.92  ? 1812 ILE A CB    1 
ATOM   2868  C  CG1   . ILE A 1 1812 ? 206.535 197.284 184.622 1.00 57.28  ? 1812 ILE A CG1   1 
ATOM   2869  C  CG2   . ILE A 1 1812 ? 205.406 195.140 185.232 1.00 62.45  ? 1812 ILE A CG2   1 
ATOM   2870  C  CD1   . ILE A 1 1812 ? 205.707 198.071 185.599 1.00 65.30  ? 1812 ILE A CD1   1 
ATOM   2871  N  N     . THR A 1 1813 ? 205.319 193.495 182.255 1.00 57.23  ? 1813 THR A N     1 
ATOM   2872  C  CA    . THR A 1 1813 ? 204.949 192.090 182.088 1.00 57.17  ? 1813 THR A CA    1 
ATOM   2873  C  C     . THR A 1 1813 ? 206.082 191.301 181.439 1.00 64.03  ? 1813 THR A C     1 
ATOM   2874  O  O     . THR A 1 1813 ? 206.457 190.213 181.907 1.00 71.23  ? 1813 THR A O     1 
ATOM   2875  C  CB    . THR A 1 1813 ? 203.673 191.979 181.255 1.00 55.62  ? 1813 THR A CB    1 
ATOM   2876  O  OG1   . THR A 1 1813 ? 202.620 192.718 181.885 1.00 60.83  ? 1813 THR A OG1   1 
ATOM   2877  C  CG2   . THR A 1 1813 ? 203.255 190.526 181.115 1.00 60.41  ? 1813 THR A CG2   1 
ATOM   2878  N  N     . GLU A 1 1814 ? 206.655 191.853 180.367 1.00 64.78  ? 1814 GLU A N     1 
ATOM   2879  C  CA    . GLU A 1 1814 ? 207.703 191.145 179.642 1.00 62.95  ? 1814 GLU A CA    1 
ATOM   2880  C  C     . GLU A 1 1814 ? 208.929 190.941 180.526 1.00 62.35  ? 1814 GLU A C     1 
ATOM   2881  O  O     . GLU A 1 1814 ? 209.529 189.859 180.536 1.00 72.90  ? 1814 GLU A O     1 
ATOM   2882  C  CB    . GLU A 1 1814 ? 208.062 191.926 178.377 1.00 62.68  ? 1814 GLU A CB    1 
ATOM   2883  C  CG    . GLU A 1 1814 ? 209.140 191.333 177.470 1.00 68.84  ? 1814 GLU A CG    1 
ATOM   2884  C  CD    . GLU A 1 1814 ? 209.280 189.818 177.557 1.00 77.23  ? 1814 GLU A CD    1 
ATOM   2885  O  OE1   . GLU A 1 1814 ? 208.254 189.102 177.551 1.00 75.66  ? 1814 GLU A OE1   1 
ATOM   2886  O  OE2   . GLU A 1 1814 ? 210.427 189.336 177.603 1.00 79.69  ? 1814 GLU A OE2   1 
ATOM   2887  N  N     . LEU A 1 1815 ? 209.297 191.962 181.302 1.00 55.98  ? 1815 LEU A N     1 
ATOM   2888  C  CA    . LEU A 1 1815 ? 210.460 191.872 182.174 1.00 57.64  ? 1815 LEU A CA    1 
ATOM   2889  C  C     . LEU A 1 1815 ? 210.219 190.966 183.372 1.00 60.87  ? 1815 LEU A C     1 
ATOM   2890  O  O     . LEU A 1 1815 ? 211.162 190.338 183.856 1.00 74.80  ? 1815 LEU A O     1 
ATOM   2891  C  CB    . LEU A 1 1815 ? 210.869 193.267 182.642 1.00 55.16  ? 1815 LEU A CB    1 
ATOM   2892  C  CG    . LEU A 1 1815 ? 212.007 193.920 181.861 1.00 63.37  ? 1815 LEU A CG    1 
ATOM   2893  C  CD1   . LEU A 1 1815 ? 211.599 194.193 180.427 1.00 65.69  ? 1815 LEU A CD1   1 
ATOM   2894  C  CD2   . LEU A 1 1815 ? 212.415 195.204 182.543 1.00 68.01  ? 1815 LEU A CD2   1 
ATOM   2895  N  N     . VAL A 1 1816 ? 208.984 190.884 183.868 1.00 54.24  ? 1816 VAL A N     1 
ATOM   2896  C  CA    . VAL A 1 1816 ? 208.675 189.901 184.902 1.00 55.21  ? 1816 VAL A CA    1 
ATOM   2897  C  C     . VAL A 1 1816 ? 208.866 188.494 184.357 1.00 61.99  ? 1816 VAL A C     1 
ATOM   2898  O  O     . VAL A 1 1816 ? 209.437 187.621 185.027 1.00 75.14  ? 1816 VAL A O     1 
ATOM   2899  C  CB    . VAL A 1 1816 ? 207.248 190.116 185.441 1.00 57.38  ? 1816 VAL A CB    1 
ATOM   2900  C  CG1   . VAL A 1 1816 ? 206.772 188.883 186.188 1.00 62.74  ? 1816 VAL A CG1   1 
ATOM   2901  C  CG2   . VAL A 1 1816 ? 207.207 191.328 186.352 1.00 62.10  ? 1816 VAL A CG2   1 
ATOM   2902  N  N     . HIS A 1 1817 ? 208.405 188.254 183.127 1.00 56.73  ? 1817 HIS A N     1 
ATOM   2903  C  CA    . HIS A 1 1817 ? 208.649 186.953 182.508 1.00 55.51  ? 1817 HIS A CA    1 
ATOM   2904  C  C     . HIS A 1 1817 ? 210.143 186.684 182.355 1.00 59.71  ? 1817 HIS A C     1 
ATOM   2905  O  O     . HIS A 1 1817 ? 210.610 185.566 182.610 1.00 64.89  ? 1817 HIS A O     1 
ATOM   2906  C  CB    . HIS A 1 1817 ? 207.953 186.867 181.153 1.00 55.82  ? 1817 HIS A CB    1 
ATOM   2907  C  CG    . HIS A 1 1817 ? 208.267 185.614 180.399 1.00 58.73  ? 1817 HIS A CG    1 
ATOM   2908  N  ND1   . HIS A 1 1817 ? 207.936 184.362 180.869 1.00 62.93  ? 1817 HIS A ND1   1 
ATOM   2909  C  CD2   . HIS A 1 1817 ? 208.888 185.419 179.212 1.00 66.36  ? 1817 HIS A CD2   1 
ATOM   2910  C  CE1   . HIS A 1 1817 ? 208.335 183.449 180.003 1.00 62.35  ? 1817 HIS A CE1   1 
ATOM   2911  N  NE2   . HIS A 1 1817 ? 208.917 184.064 178.989 1.00 71.70  ? 1817 HIS A NE2   1 
ATOM   2912  N  N     . GLN A 1 1818 ? 210.906 187.696 181.935 1.00 60.00  ? 1818 GLN A N     1 
ATOM   2913  C  CA    . GLN A 1 1818 ? 212.351 187.526 181.794 1.00 60.52  ? 1818 GLN A CA    1 
ATOM   2914  C  C     . GLN A 1 1818 ? 213.010 187.211 183.130 1.00 64.32  ? 1818 GLN A C     1 
ATOM   2915  O  O     . GLN A 1 1818 ? 213.905 186.362 183.202 1.00 72.61  ? 1818 GLN A O     1 
ATOM   2916  C  CB    . GLN A 1 1818 ? 212.981 188.778 181.186 1.00 62.81  ? 1818 GLN A CB    1 
ATOM   2917  C  CG    . GLN A 1 1818 ? 212.469 189.122 179.813 1.00 66.63  ? 1818 GLN A CG    1 
ATOM   2918  C  CD    . GLN A 1 1818 ? 213.164 190.324 179.213 1.00 65.99  ? 1818 GLN A CD    1 
ATOM   2919  O  OE1   . GLN A 1 1818 ? 213.921 191.019 179.888 1.00 67.87  ? 1818 GLN A OE1   1 
ATOM   2920  N  NE2   . GLN A 1 1818 ? 212.910 190.576 177.935 1.00 60.44  ? 1818 GLN A NE2   1 
ATOM   2921  N  N     . ARG A 1 1819 ? 212.598 187.902 184.194 1.00 63.73  ? 1819 ARG A N     1 
ATOM   2922  C  CA    . ARG A 1 1819 ? 213.162 187.642 185.513 1.00 56.15  ? 1819 ARG A CA    1 
ATOM   2923  C  C     . ARG A 1 1819 ? 212.852 186.225 185.966 1.00 63.77  ? 1819 ARG A C     1 
ATOM   2924  O  O     . ARG A 1 1819 ? 213.721 185.537 186.514 1.00 80.84  ? 1819 ARG A O     1 
ATOM   2925  C  CB    . ARG A 1 1819 ? 212.625 188.655 186.523 1.00 56.27  ? 1819 ARG A CB    1 
ATOM   2926  C  CG    . ARG A 1 1819 ? 213.159 188.462 187.930 1.00 67.30  ? 1819 ARG A CG    1 
ATOM   2927  C  CD    . ARG A 1 1819 ? 212.362 189.265 188.942 1.00 67.56  ? 1819 ARG A CD    1 
ATOM   2928  N  NE    . ARG A 1 1819 ? 210.987 188.794 189.055 1.00 68.84  ? 1819 ARG A NE    1 
ATOM   2929  C  CZ    . ARG A 1 1819 ? 210.031 189.433 189.713 1.00 72.78  ? 1819 ARG A CZ    1 
ATOM   2930  N  NH1   . ARG A 1 1819 ? 210.265 190.579 190.331 1.00 69.63  ? 1819 ARG A NH1   1 
ATOM   2931  N  NH2   . ARG A 1 1819 ? 208.809 188.909 189.753 1.00 74.06  ? 1819 ARG A NH2   1 
ATOM   2932  N  N     . ASP A 1 1820 ? 211.617 185.769 185.742 1.00 58.42  ? 1820 ASP A N     1 
ATOM   2933  C  CA    . ASP A 1 1820 ? 211.257 184.404 186.114 1.00 64.40  ? 1820 ASP A CA    1 
ATOM   2934  C  C     . ASP A 1 1820 ? 212.110 183.400 185.345 1.00 68.98  ? 1820 ASP A C     1 
ATOM   2935  O  O     . ASP A 1 1820 ? 212.645 182.449 185.931 1.00 76.51  ? 1820 ASP A O     1 
ATOM   2936  C  CB    . ASP A 1 1820 ? 209.758 184.190 185.858 1.00 73.30  ? 1820 ASP A CB    1 
ATOM   2937  C  CG    . ASP A 1 1820 ? 209.281 182.755 186.116 1.00 79.87  ? 1820 ASP A CG    1 
ATOM   2938  O  OD1   . ASP A 1 1820 ? 210.091 181.823 186.294 1.00 79.94  ? 1820 ASP A OD1   1 
ATOM   2939  O  OD2   . ASP A 1 1820 ? 208.048 182.560 186.139 1.00 80.34  ? 1820 ASP A OD2   1 
ATOM   2940  N  N     . VAL A 1 1821 ? 212.272 183.610 184.037 1.00 58.13  ? 1821 VAL A N     1 
ATOM   2941  C  CA    . VAL A 1 1821 ? 213.040 182.670 183.224 1.00 53.29  ? 1821 VAL A CA    1 
ATOM   2942  C  C     . VAL A 1 1821 ? 214.502 182.654 183.653 1.00 58.27  ? 1821 VAL A C     1 
ATOM   2943  O  O     . VAL A 1 1821 ? 215.128 181.591 183.740 1.00 61.25  ? 1821 VAL A O     1 
ATOM   2944  C  CB    . VAL A 1 1821 ? 212.889 183.006 181.729 1.00 50.59  ? 1821 VAL A CB    1 
ATOM   2945  C  CG1   . VAL A 1 1821 ? 213.957 182.299 180.915 1.00 55.30  ? 1821 VAL A CG1   1 
ATOM   2946  C  CG2   . VAL A 1 1821 ? 211.507 182.620 181.239 1.00 57.17  ? 1821 VAL A CG2   1 
ATOM   2947  N  N     . THR A 1 1822 ? 215.074 183.830 183.923 1.00 68.56  ? 1822 THR A N     1 
ATOM   2948  C  CA    . THR A 1 1822 ? 216.469 183.896 184.345 1.00 60.85  ? 1822 THR A CA    1 
ATOM   2949  C  C     . THR A 1 1822 ? 216.668 183.245 185.709 1.00 68.02  ? 1822 THR A C     1 
ATOM   2950  O  O     . THR A 1 1822 ? 217.677 182.565 185.936 1.00 77.63  ? 1822 THR A O     1 
ATOM   2951  C  CB    . THR A 1 1822 ? 216.945 185.348 184.369 1.00 66.75  ? 1822 THR A CB    1 
ATOM   2952  O  OG1   . THR A 1 1822 ? 216.663 185.963 183.106 1.00 67.10  ? 1822 THR A OG1   1 
ATOM   2953  C  CG2   . THR A 1 1822 ? 218.440 185.413 184.628 1.00 68.00  ? 1822 THR A CG2   1 
ATOM   2954  N  N     . ARG A 1 1823 ? 215.722 183.441 186.631 1.00 69.09  ? 1823 ARG A N     1 
ATOM   2955  C  CA    . ARG A 1 1823 ? 215.800 182.764 187.921 1.00 67.13  ? 1823 ARG A CA    1 
ATOM   2956  C  C     . ARG A 1 1823 ? 215.737 181.253 187.748 1.00 80.04  ? 1823 ARG A C     1 
ATOM   2957  O  O     . ARG A 1 1823 ? 216.464 180.512 188.419 1.00 85.13  ? 1823 ARG A O     1 
ATOM   2958  C  CB    . ARG A 1 1823 ? 214.675 183.241 188.837 1.00 67.92  ? 1823 ARG A CB    1 
ATOM   2959  C  CG    . ARG A 1 1823 ? 214.947 184.560 189.533 1.00 70.06  ? 1823 ARG A CG    1 
ATOM   2960  C  CD    . ARG A 1 1823 ? 213.733 185.008 190.327 1.00 73.90  ? 1823 ARG A CD    1 
ATOM   2961  N  NE    . ARG A 1 1823 ? 213.976 186.248 191.052 1.00 76.60  ? 1823 ARG A NE    1 
ATOM   2962  C  CZ    . ARG A 1 1823 ? 213.031 186.964 191.646 1.00 79.12  ? 1823 ARG A CZ    1 
ATOM   2963  N  NH1   . ARG A 1 1823 ? 211.763 186.589 191.620 1.00 74.29  ? 1823 ARG A NH1   1 
ATOM   2964  N  NH2   . ARG A 1 1823 ? 213.367 188.083 192.280 1.00 78.13  ? 1823 ARG A NH2   1 
ATOM   2965  N  N     . SER A 1 1824 ? 214.866 180.777 186.854 1.00 80.01  ? 1824 SER A N     1 
ATOM   2966  C  CA    . SER A 1 1824 ? 214.791 179.344 186.589 1.00 76.09  ? 1824 SER A CA    1 
ATOM   2967  C  C     . SER A 1 1824 ? 216.098 178.822 186.006 1.00 73.17  ? 1824 SER A C     1 
ATOM   2968  O  O     . SER A 1 1824 ? 216.556 177.731 186.365 1.00 75.81  ? 1824 SER A O     1 
ATOM   2969  C  CB    . SER A 1 1824 ? 213.626 179.045 185.647 1.00 78.67  ? 1824 SER A CB    1 
ATOM   2970  O  OG    . SER A 1 1824 ? 213.676 177.706 185.187 1.00 83.73  ? 1824 SER A OG    1 
ATOM   2971  N  N     . LEU A 1 1825 ? 216.707 179.583 185.095 1.00 68.03  ? 1825 LEU A N     1 
ATOM   2972  C  CA    . LEU A 1 1825 ? 217.982 179.173 184.516 1.00 63.59  ? 1825 LEU A CA    1 
ATOM   2973  C  C     . LEU A 1 1825 ? 219.074 179.104 185.576 1.00 69.14  ? 1825 LEU A C     1 
ATOM   2974  O  O     . LEU A 1 1825 ? 219.878 178.165 185.591 1.00 76.92  ? 1825 LEU A O     1 
ATOM   2975  C  CB    . LEU A 1 1825 ? 218.387 180.134 183.399 1.00 62.93  ? 1825 LEU A CB    1 
ATOM   2976  C  CG    . LEU A 1 1825 ? 217.621 180.035 182.080 1.00 68.13  ? 1825 LEU A CG    1 
ATOM   2977  C  CD1   . LEU A 1 1825 ? 218.305 180.866 181.010 1.00 67.88  ? 1825 LEU A CD1   1 
ATOM   2978  C  CD2   . LEU A 1 1825 ? 217.496 178.589 181.638 1.00 71.04  ? 1825 LEU A CD2   1 
ATOM   2979  N  N     . ILE A 1 1826 ? 219.123 180.097 186.466 1.00 77.51  ? 1826 ILE A N     1 
ATOM   2980  C  CA    . ILE A 1 1826 ? 220.136 180.106 187.517 1.00 77.01  ? 1826 ILE A CA    1 
ATOM   2981  C  C     . ILE A 1 1826 ? 219.925 178.942 188.478 1.00 82.29  ? 1826 ILE A C     1 
ATOM   2982  O  O     . ILE A 1 1826 ? 220.882 178.266 188.875 1.00 88.68  ? 1826 ILE A O     1 
ATOM   2983  C  CB    . ILE A 1 1826 ? 220.130 181.458 188.250 1.00 75.34  ? 1826 ILE A CB    1 
ATOM   2984  C  CG1   . ILE A 1 1826 ? 220.648 182.563 187.330 1.00 76.87  ? 1826 ILE A CG1   1 
ATOM   2985  C  CG2   . ILE A 1 1826 ? 220.966 181.387 189.516 1.00 79.59  ? 1826 ILE A CG2   1 
ATOM   2986  C  CD1   . ILE A 1 1826 ? 220.499 183.951 187.903 1.00 80.14  ? 1826 ILE A CD1   1 
ATOM   2987  N  N     . LYS A 1 1827 ? 218.672 178.686 188.864 1.00 86.13  ? 1827 LYS A N     1 
ATOM   2988  C  CA    . LYS A 1 1827 ? 218.390 177.633 189.834 1.00 88.81  ? 1827 LYS A CA    1 
ATOM   2989  C  C     . LYS A 1 1827 ? 218.783 176.257 189.309 1.00 89.37  ? 1827 LYS A C     1 
ATOM   2990  O  O     . LYS A 1 1827 ? 219.337 175.444 190.057 1.00 88.01  ? 1827 LYS A O     1 
ATOM   2991  C  CB    . LYS A 1 1827 ? 216.909 177.660 190.215 1.00 88.57  ? 1827 LYS A CB    1 
ATOM   2992  C  CG    . LYS A 1 1827 ? 216.361 176.336 190.717 1.00 88.88  ? 1827 LYS A CG    1 
ATOM   2993  C  CD    . LYS A 1 1827 ? 215.051 176.535 191.462 1.00 92.54  ? 1827 LYS A CD    1 
ATOM   2994  C  CE    . LYS A 1 1827 ? 214.884 175.507 192.568 1.00 92.78  ? 1827 LYS A CE    1 
ATOM   2995  N  NZ    . LYS A 1 1827 ? 213.572 175.642 193.259 1.00 91.12  ? 1827 LYS A NZ    1 
ATOM   2996  N  N     . SER A 1 1828 ? 218.521 175.983 188.034 1.00 93.09  ? 1828 SER A N     1 
ATOM   2997  C  CA    . SER A 1 1828 ? 218.828 174.689 187.438 1.00 90.50  ? 1828 SER A CA    1 
ATOM   2998  C  C     . SER A 1 1828 ? 220.303 174.523 187.097 1.00 92.63  ? 1828 SER A C     1 
ATOM   2999  O  O     . SER A 1 1828 ? 220.678 173.486 186.541 1.00 94.67  ? 1828 SER A O     1 
ATOM   3000  C  CB    . SER A 1 1828 ? 217.984 174.474 186.179 1.00 89.51  ? 1828 SER A CB    1 
ATOM   3001  O  OG    . SER A 1 1828 ? 216.608 174.370 186.500 1.00 92.67  ? 1828 SER A OG    1 
ATOM   3002  N  N     . LYS A 1 1829 ? 221.139 175.515 187.412 1.00 91.05  ? 1829 LYS A N     1 
ATOM   3003  C  CA    . LYS A 1 1829 ? 222.583 175.450 187.176 1.00 91.64  ? 1829 LYS A CA    1 
ATOM   3004  C  C     . LYS A 1 1829 ? 222.893 175.194 185.701 1.00 92.46  ? 1829 LYS A C     1 
ATOM   3005  O  O     . LYS A 1 1829 ? 223.712 174.342 185.351 1.00 93.31  ? 1829 LYS A O     1 
ATOM   3006  C  CB    . LYS A 1 1829 ? 223.237 174.391 188.067 1.00 93.82  ? 1829 LYS A CB    1 
ATOM   3007  C  CG    . LYS A 1 1829 ? 223.157 174.695 189.554 1.00 93.69  ? 1829 LYS A CG    1 
ATOM   3008  C  CD    . LYS A 1 1829 ? 224.459 175.284 190.069 1.00 93.24  ? 1829 LYS A CD    1 
ATOM   3009  C  CE    . LYS A 1 1829 ? 224.254 175.997 191.394 1.00 93.14  ? 1829 LYS A CE    1 
ATOM   3010  N  NZ    . LYS A 1 1829 ? 223.862 177.420 191.202 1.00 95.24  ? 1829 LYS A NZ    1 
ATOM   3011  N  N     . ILE A 1 1830 ? 222.224 175.942 184.832 1.00 89.96  ? 1830 ILE A N     1 
ATOM   3012  C  CA    . ILE A 1 1830 ? 222.427 175.810 183.394 1.00 89.63  ? 1830 ILE A CA    1 
ATOM   3013  C  C     . ILE A 1 1830 ? 223.702 176.545 183.004 1.00 97.13  ? 1830 ILE A C     1 
ATOM   3014  O  O     . ILE A 1 1830 ? 223.899 177.709 183.372 1.00 99.81  ? 1830 ILE A O     1 
ATOM   3015  C  CB    . ILE A 1 1830 ? 221.214 176.349 182.621 1.00 86.50  ? 1830 ILE A CB    1 
ATOM   3016  C  CG1   . ILE A 1 1830 ? 219.940 175.659 183.103 1.00 90.30  ? 1830 ILE A CG1   1 
ATOM   3017  C  CG2   . ILE A 1 1830 ? 221.398 176.142 181.128 1.00 85.56  ? 1830 ILE A CG2   1 
ATOM   3018  C  CD1   . ILE A 1 1830 ? 219.981 174.158 182.969 1.00 91.27  ? 1830 ILE A CD1   1 
ATOM   3019  N  N     . ASP A 1 1831 ? 224.573 175.865 182.259 1.00 100.42 ? 1831 ASP A N     1 
ATOM   3020  C  CA    . ASP A 1 1831 ? 225.853 176.429 181.860 1.00 96.06  ? 1831 ASP A CA    1 
ATOM   3021  C  C     . ASP A 1 1831 ? 226.162 176.281 180.379 1.00 94.32  ? 1831 ASP A C     1 
ATOM   3022  O  O     . ASP A 1 1831 ? 227.207 176.772 179.936 1.00 97.57  ? 1831 ASP A O     1 
ATOM   3023  C  CB    . ASP A 1 1831 ? 226.992 175.790 182.670 1.00 97.08  ? 1831 ASP A CB    1 
ATOM   3024  C  CG    . ASP A 1 1831 ? 226.909 174.278 182.698 1.00 102.32 ? 1831 ASP A CG    1 
ATOM   3025  O  OD1   . ASP A 1 1831 ? 225.913 173.727 182.185 1.00 104.11 ? 1831 ASP A OD1   1 
ATOM   3026  O  OD2   . ASP A 1 1831 ? 227.839 173.638 183.233 1.00 105.09 ? 1831 ASP A OD2   1 
ATOM   3027  N  N     . ASN A 1 1832 ? 225.301 175.632 179.602 1.00 83.68  ? 1832 ASN A N     1 
ATOM   3028  C  CA    . ASN A 1 1832 ? 225.537 175.408 178.183 1.00 85.86  ? 1832 ASN A CA    1 
ATOM   3029  C  C     . ASN A 1 1832 ? 224.408 176.027 177.372 1.00 87.14  ? 1832 ASN A C     1 
ATOM   3030  O  O     . ASN A 1 1832 ? 223.234 175.901 177.738 1.00 88.43  ? 1832 ASN A O     1 
ATOM   3031  C  CB    . ASN A 1 1832 ? 225.652 173.913 177.876 1.00 89.56  ? 1832 ASN A CB    1 
ATOM   3032  C  CG    . ASN A 1 1832 ? 226.290 173.644 176.529 1.00 90.98  ? 1832 ASN A CG    1 
ATOM   3033  O  OD1   . ASN A 1 1832 ? 227.136 174.408 176.066 1.00 91.17  ? 1832 ASN A OD1   1 
ATOM   3034  N  ND2   . ASN A 1 1832 ? 225.888 172.551 175.892 1.00 87.85  ? 1832 ASN A ND2   1 
ATOM   3035  N  N     . ALA A 1 1833 ? 224.766 176.692 176.272 1.00 81.40  ? 1833 ALA A N     1 
ATOM   3036  C  CA    . ALA A 1 1833 ? 223.775 177.330 175.416 1.00 77.86  ? 1833 ALA A CA    1 
ATOM   3037  C  C     . ALA A 1 1833 ? 222.923 176.331 174.647 1.00 81.35  ? 1833 ALA A C     1 
ATOM   3038  O  O     . ALA A 1 1833 ? 221.871 176.715 174.126 1.00 83.57  ? 1833 ALA A O     1 
ATOM   3039  C  CB    . ALA A 1 1833 ? 224.463 178.281 174.436 1.00 77.41  ? 1833 ALA A CB    1 
ATOM   3040  N  N     . LYS A 1 1834 ? 223.346 175.072 174.560 1.00 81.75  ? 1834 LYS A N     1 
ATOM   3041  C  CA    . LYS A 1 1834 ? 222.579 174.036 173.882 1.00 79.81  ? 1834 LYS A CA    1 
ATOM   3042  C  C     . LYS A 1 1834 ? 221.711 173.223 174.833 1.00 77.85  ? 1834 LYS A C     1 
ATOM   3043  O  O     . LYS A 1 1834 ? 221.057 172.273 174.392 1.00 78.67  ? 1834 LYS A O     1 
ATOM   3044  C  CB    . LYS A 1 1834 ? 223.519 173.099 173.117 1.00 82.35  ? 1834 LYS A CB    1 
ATOM   3045  C  CG    . LYS A 1 1834 ? 224.595 173.813 172.318 1.00 81.40  ? 1834 LYS A CG    1 
ATOM   3046  C  CD    . LYS A 1 1834 ? 223.989 174.681 171.228 1.00 81.65  ? 1834 LYS A CD    1 
ATOM   3047  C  CE    . LYS A 1 1834 ? 223.409 173.835 170.108 1.00 82.85  ? 1834 LYS A CE    1 
ATOM   3048  N  NZ    . LYS A 1 1834 ? 222.904 174.673 168.985 1.00 83.42  ? 1834 LYS A NZ    1 
ATOM   3049  N  N     . SER A 1 1835 ? 221.696 173.564 176.119 1.00 72.03  ? 1835 SER A N     1 
ATOM   3050  C  CA    . SER A 1 1835 ? 220.846 172.862 177.069 1.00 73.13  ? 1835 SER A CA    1 
ATOM   3051  C  C     . SER A 1 1835 ? 219.379 173.135 176.767 1.00 72.00  ? 1835 SER A C     1 
ATOM   3052  O  O     . SER A 1 1835 ? 218.990 174.268 176.470 1.00 79.69  ? 1835 SER A O     1 
ATOM   3053  C  CB    . SER A 1 1835 ? 221.177 173.291 178.497 1.00 80.66  ? 1835 SER A CB    1 
ATOM   3054  O  OG    . SER A 1 1835 ? 220.230 172.775 179.415 1.00 85.39  ? 1835 SER A OG    1 
ATOM   3055  N  N     . PHE A 1 1836 ? 218.559 172.084 176.842 1.00 67.49  ? 1836 PHE A N     1 
ATOM   3056  C  CA    . PHE A 1 1836 ? 217.147 172.226 176.509 1.00 63.08  ? 1836 PHE A CA    1 
ATOM   3057  C  C     . PHE A 1 1836 ? 216.403 173.129 177.483 1.00 68.13  ? 1836 PHE A C     1 
ATOM   3058  O  O     . PHE A 1 1836 ? 215.351 173.667 177.124 1.00 69.55  ? 1836 PHE A O     1 
ATOM   3059  C  CB    . PHE A 1 1836 ? 216.468 170.860 176.453 1.00 63.43  ? 1836 PHE A CB    1 
ATOM   3060  C  CG    . PHE A 1 1836 ? 215.138 170.881 175.760 1.00 63.47  ? 1836 PHE A CG    1 
ATOM   3061  C  CD1   . PHE A 1 1836 ? 215.064 170.941 174.381 1.00 65.10  ? 1836 PHE A CD1   1 
ATOM   3062  C  CD2   . PHE A 1 1836 ? 213.962 170.854 176.488 1.00 63.69  ? 1836 PHE A CD2   1 
ATOM   3063  C  CE1   . PHE A 1 1836 ? 213.843 170.966 173.739 1.00 68.96  ? 1836 PHE A CE1   1 
ATOM   3064  C  CE2   . PHE A 1 1836 ? 212.739 170.880 175.851 1.00 66.20  ? 1836 PHE A CE2   1 
ATOM   3065  C  CZ    . PHE A 1 1836 ? 212.679 170.935 174.475 1.00 73.49  ? 1836 PHE A CZ    1 
ATOM   3066  N  N     . GLU A 1 1837 ? 216.917 173.307 178.703 1.00 79.87  ? 1837 GLU A N     1 
ATOM   3067  C  CA    . GLU A 1 1837 ? 216.289 174.247 179.627 1.00 79.64  ? 1837 GLU A CA    1 
ATOM   3068  C  C     . GLU A 1 1837 ? 216.368 175.674 179.104 1.00 81.91  ? 1837 GLU A C     1 
ATOM   3069  O  O     . GLU A 1 1837 ? 215.598 176.538 179.539 1.00 81.04  ? 1837 GLU A O     1 
ATOM   3070  C  CB    . GLU A 1 1837 ? 216.938 174.143 181.006 1.00 76.46  ? 1837 GLU A CB    1 
ATOM   3071  C  CG    . GLU A 1 1837 ? 216.585 172.871 181.759 1.00 82.13  ? 1837 GLU A CG    1 
ATOM   3072  C  CD    . GLU A 1 1837 ? 217.705 171.851 181.743 1.00 86.01  ? 1837 GLU A CD    1 
ATOM   3073  O  OE1   . GLU A 1 1837 ? 218.347 171.687 180.685 1.00 86.20  ? 1837 GLU A OE1   1 
ATOM   3074  O  OE2   . GLU A 1 1837 ? 217.945 171.213 182.790 1.00 85.94  ? 1837 GLU A OE2   1 
ATOM   3075  N  N     . TRP A 1 1838 ? 217.289 175.941 178.179 1.00 70.18  ? 1838 TRP A N     1 
ATOM   3076  C  CA    . TRP A 1 1838 ? 217.361 177.224 177.494 1.00 66.87  ? 1838 TRP A CA    1 
ATOM   3077  C  C     . TRP A 1 1838 ? 216.805 177.179 176.080 1.00 66.47  ? 1838 TRP A C     1 
ATOM   3078  O  O     . TRP A 1 1838 ? 216.239 178.175 175.620 1.00 76.22  ? 1838 TRP A O     1 
ATOM   3079  C  CB    . TRP A 1 1838 ? 218.808 177.724 177.447 1.00 62.91  ? 1838 TRP A CB    1 
ATOM   3080  C  CG    . TRP A 1 1838 ? 218.999 178.930 176.579 1.00 57.00  ? 1838 TRP A CG    1 
ATOM   3081  C  CD1   . TRP A 1 1838 ? 219.843 179.045 175.516 1.00 60.95  ? 1838 TRP A CD1   1 
ATOM   3082  C  CD2   . TRP A 1 1838 ? 218.326 180.191 176.694 1.00 67.18  ? 1838 TRP A CD2   1 
ATOM   3083  N  NE1   . TRP A 1 1838 ? 219.744 180.297 174.964 1.00 61.83  ? 1838 TRP A NE1   1 
ATOM   3084  C  CE2   . TRP A 1 1838 ? 218.818 181.020 175.669 1.00 62.41  ? 1838 TRP A CE2   1 
ATOM   3085  C  CE3   . TRP A 1 1838 ? 217.357 180.699 177.564 1.00 73.91  ? 1838 TRP A CE3   1 
ATOM   3086  C  CZ2   . TRP A 1 1838 ? 218.375 182.327 175.489 1.00 69.09  ? 1838 TRP A CZ2   1 
ATOM   3087  C  CZ3   . TRP A 1 1838 ? 216.919 181.998 177.384 1.00 68.25  ? 1838 TRP A CZ3   1 
ATOM   3088  C  CH2   . TRP A 1 1838 ? 217.426 182.796 176.354 1.00 71.51  ? 1838 TRP A CH2   1 
ATOM   3089  N  N     . LEU A 1 1839 ? 216.946 176.051 175.380 1.00 54.60  ? 1839 LEU A N     1 
ATOM   3090  C  CA    . LEU A 1 1839 ? 216.403 175.959 174.029 1.00 51.28  ? 1839 LEU A CA    1 
ATOM   3091  C  C     . LEU A 1 1839 ? 214.881 175.975 174.031 1.00 61.20  ? 1839 LEU A C     1 
ATOM   3092  O  O     . LEU A 1 1839 ? 214.268 176.410 173.051 1.00 67.13  ? 1839 LEU A O     1 
ATOM   3093  C  CB    . LEU A 1 1839 ? 216.920 174.701 173.333 1.00 57.04  ? 1839 LEU A CB    1 
ATOM   3094  C  CG    . LEU A 1 1839 ? 218.399 174.701 172.946 1.00 62.02  ? 1839 LEU A CG    1 
ATOM   3095  C  CD1   . LEU A 1 1839 ? 218.763 173.411 172.233 1.00 64.02  ? 1839 LEU A CD1   1 
ATOM   3096  C  CD2   . LEU A 1 1839 ? 218.729 175.904 172.082 1.00 55.34  ? 1839 LEU A CD2   1 
ATOM   3097  N  N     . SER A 1 1840 ? 214.254 175.512 175.114 1.00 62.36  ? 1840 SER A N     1 
ATOM   3098  C  CA    . SER A 1 1840 ? 212.799 175.520 175.193 1.00 57.86  ? 1840 SER A CA    1 
ATOM   3099  C  C     . SER A 1 1840 ? 212.226 176.920 175.358 1.00 61.65  ? 1840 SER A C     1 
ATOM   3100  O  O     . SER A 1 1840 ? 211.059 177.135 175.015 1.00 69.76  ? 1840 SER A O     1 
ATOM   3101  C  CB    . SER A 1 1840 ? 212.330 174.632 176.347 1.00 57.01  ? 1840 SER A CB    1 
ATOM   3102  O  OG    . SER A 1 1840 ? 213.009 174.954 177.547 1.00 60.04  ? 1840 SER A OG    1 
ATOM   3103  N  N     . GLN A 1 1841 ? 213.007 177.867 175.868 1.00 58.50  ? 1841 GLN A N     1 
ATOM   3104  C  CA    . GLN A 1 1841 ? 212.549 179.240 175.987 1.00 52.84  ? 1841 GLN A CA    1 
ATOM   3105  C  C     . GLN A 1 1841 ? 212.513 179.906 174.615 1.00 61.85  ? 1841 GLN A C     1 
ATOM   3106  O  O     . GLN A 1 1841 ? 213.247 179.539 173.694 1.00 67.48  ? 1841 GLN A O     1 
ATOM   3107  C  CB    . GLN A 1 1841 ? 213.449 180.028 176.937 1.00 55.80  ? 1841 GLN A CB    1 
ATOM   3108  C  CG    . GLN A 1 1841 ? 213.694 179.349 178.270 1.00 60.86  ? 1841 GLN A CG    1 
ATOM   3109  C  CD    . GLN A 1 1841 ? 212.415 179.118 179.049 1.00 68.99  ? 1841 GLN A CD    1 
ATOM   3110  O  OE1   . GLN A 1 1841 ? 211.514 179.955 179.045 1.00 71.93  ? 1841 GLN A OE1   1 
ATOM   3111  N  NE2   . GLN A 1 1841 ? 212.331 177.979 179.724 1.00 67.74  ? 1841 GLN A NE2   1 
ATOM   3112  N  N     . MET A 1 1842 ? 211.639 180.900 174.483 1.00 66.66  ? 1842 MET A N     1 
ATOM   3113  C  CA    . MET A 1 1842 ? 211.489 181.640 173.235 1.00 61.17  ? 1842 MET A CA    1 
ATOM   3114  C  C     . MET A 1 1842 ? 212.618 182.659 173.147 1.00 59.05  ? 1842 MET A C     1 
ATOM   3115  O  O     . MET A 1 1842 ? 212.615 183.665 173.863 1.00 67.41  ? 1842 MET A O     1 
ATOM   3116  C  CB    . MET A 1 1842 ? 210.123 182.315 173.170 1.00 58.91  ? 1842 MET A CB    1 
ATOM   3117  C  CG    . MET A 1 1842 ? 209.958 183.273 172.006 1.00 66.66  ? 1842 MET A CG    1 
ATOM   3118  S  SD    . MET A 1 1842 ? 208.230 183.481 171.545 1.00 77.66  ? 1842 MET A SD    1 
ATOM   3119  C  CE    . MET A 1 1842 ? 208.065 182.223 170.283 1.00 57.96  ? 1842 MET A CE    1 
ATOM   3120  N  N     . ARG A 1 1843 ? 213.582 182.399 172.269 1.00 56.97  ? 1843 ARG A N     1 
ATOM   3121  C  CA    . ARG A 1 1843 ? 214.774 183.222 172.136 1.00 58.64  ? 1843 ARG A CA    1 
ATOM   3122  C  C     . ARG A 1 1843 ? 214.697 184.042 170.857 1.00 62.35  ? 1843 ARG A C     1 
ATOM   3123  O  O     . ARG A 1 1843 ? 214.307 183.530 169.803 1.00 71.49  ? 1843 ARG A O     1 
ATOM   3124  C  CB    . ARG A 1 1843 ? 216.038 182.359 172.126 1.00 57.38  ? 1843 ARG A CB    1 
ATOM   3125  C  CG    . ARG A 1 1843 ? 215.948 181.138 173.019 1.00 53.16  ? 1843 ARG A CG    1 
ATOM   3126  C  CD    . ARG A 1 1843 ? 217.128 180.208 172.812 1.00 56.98  ? 1843 ARG A CD    1 
ATOM   3127  N  NE    . ARG A 1 1843 ? 217.187 179.686 171.453 1.00 69.72  ? 1843 ARG A NE    1 
ATOM   3128  C  CZ    . ARG A 1 1843 ? 216.410 178.719 170.986 1.00 71.13  ? 1843 ARG A CZ    1 
ATOM   3129  N  NH1   . ARG A 1 1843 ? 215.481 178.155 171.739 1.00 69.16  ? 1843 ARG A NH1   1 
ATOM   3130  N  NH2   . ARG A 1 1843 ? 216.567 178.310 169.731 1.00 64.69  ? 1843 ARG A NH2   1 
ATOM   3131  N  N     . PHE A 1 1844 ? 215.068 185.314 170.957 1.00 55.75  ? 1844 PHE A N     1 
ATOM   3132  C  CA    . PHE A 1 1844 ? 215.076 186.228 169.823 1.00 58.44  ? 1844 PHE A CA    1 
ATOM   3133  C  C     . PHE A 1 1844 ? 216.518 186.488 169.416 1.00 60.68  ? 1844 PHE A C     1 
ATOM   3134  O  O     . PHE A 1 1844 ? 217.347 186.853 170.256 1.00 70.14  ? 1844 PHE A O     1 
ATOM   3135  C  CB    . PHE A 1 1844 ? 214.373 187.541 170.166 1.00 53.61  ? 1844 PHE A CB    1 
ATOM   3136  C  CG    . PHE A 1 1844 ? 212.958 187.370 170.629 1.00 59.81  ? 1844 PHE A CG    1 
ATOM   3137  C  CD1   . PHE A 1 1844 ? 212.678 187.024 171.939 1.00 65.36  ? 1844 PHE A CD1   1 
ATOM   3138  C  CD2   . PHE A 1 1844 ? 211.906 187.555 169.752 1.00 63.15  ? 1844 PHE A CD2   1 
ATOM   3139  C  CE1   . PHE A 1 1844 ? 211.377 186.866 172.364 1.00 66.88  ? 1844 PHE A CE1   1 
ATOM   3140  C  CE2   . PHE A 1 1844 ? 210.604 187.399 170.171 1.00 65.15  ? 1844 PHE A CE2   1 
ATOM   3141  C  CZ    . PHE A 1 1844 ? 210.339 187.053 171.480 1.00 66.98  ? 1844 PHE A CZ    1 
ATOM   3142  N  N     . TYR A 1 1845 ? 216.813 186.303 168.133 1.00 64.51  ? 1845 TYR A N     1 
ATOM   3143  C  CA    . TYR A 1 1845 ? 218.137 186.551 167.584 1.00 63.55  ? 1845 TYR A CA    1 
ATOM   3144  C  C     . TYR A 1 1845 ? 218.040 187.635 166.524 1.00 73.55  ? 1845 TYR A C     1 
ATOM   3145  O  O     . TYR A 1 1845 ? 217.231 187.533 165.597 1.00 83.48  ? 1845 TYR A O     1 
ATOM   3146  C  CB    . TYR A 1 1845 ? 218.737 185.274 166.992 1.00 66.98  ? 1845 TYR A CB    1 
ATOM   3147  C  CG    . TYR A 1 1845 ? 218.949 184.177 168.008 1.00 74.90  ? 1845 TYR A CG    1 
ATOM   3148  C  CD1   . TYR A 1 1845 ? 219.716 184.397 169.144 1.00 76.34  ? 1845 TYR A CD1   1 
ATOM   3149  C  CD2   . TYR A 1 1845 ? 218.381 182.923 167.835 1.00 71.40  ? 1845 TYR A CD2   1 
ATOM   3150  C  CE1   . TYR A 1 1845 ? 219.913 183.400 170.077 1.00 71.73  ? 1845 TYR A CE1   1 
ATOM   3151  C  CE2   . TYR A 1 1845 ? 218.573 181.920 168.763 1.00 71.94  ? 1845 TYR A CE2   1 
ATOM   3152  C  CZ    . TYR A 1 1845 ? 219.340 182.164 169.882 1.00 73.49  ? 1845 TYR A CZ    1 
ATOM   3153  O  OH    . TYR A 1 1845 ? 219.535 181.168 170.810 1.00 74.92  ? 1845 TYR A OH    1 
ATOM   3154  N  N     . PHE A 1 1846 ? 218.863 188.669 166.664 1.00 79.95  ? 1846 PHE A N     1 
ATOM   3155  C  CA    . PHE A 1 1846 ? 218.889 189.792 165.739 1.00 80.13  ? 1846 PHE A CA    1 
ATOM   3156  C  C     . PHE A 1 1846 ? 220.211 189.796 164.988 1.00 85.85  ? 1846 PHE A C     1 
ATOM   3157  O  O     . PHE A 1 1846 ? 221.277 189.659 165.597 1.00 87.48  ? 1846 PHE A O     1 
ATOM   3158  C  CB    . PHE A 1 1846 ? 218.695 191.116 166.478 1.00 85.16  ? 1846 PHE A CB    1 
ATOM   3159  C  CG    . PHE A 1 1846 ? 218.253 192.243 165.593 1.00 83.63  ? 1846 PHE A CG    1 
ATOM   3160  C  CD1   . PHE A 1 1846 ? 217.003 192.225 165.001 1.00 84.39  ? 1846 PHE A CD1   1 
ATOM   3161  C  CD2   . PHE A 1 1846 ? 219.087 193.320 165.353 1.00 82.68  ? 1846 PHE A CD2   1 
ATOM   3162  C  CE1   . PHE A 1 1846 ? 216.593 193.260 164.185 1.00 83.28  ? 1846 PHE A CE1   1 
ATOM   3163  C  CE2   . PHE A 1 1846 ? 218.682 194.357 164.540 1.00 85.50  ? 1846 PHE A CE2   1 
ATOM   3164  C  CZ    . PHE A 1 1846 ? 217.434 194.326 163.955 1.00 85.39  ? 1846 PHE A CZ    1 
ATOM   3165  N  N     . ASP A 1 1847 ? 220.138 189.955 163.666 1.00 111.51 ? 1847 ASP A N     1 
ATOM   3166  C  CA    . ASP A 1 1847 ? 221.312 189.986 162.797 1.00 114.32 ? 1847 ASP A CA    1 
ATOM   3167  C  C     . ASP A 1 1847 ? 221.291 191.291 162.013 1.00 118.35 ? 1847 ASP A C     1 
ATOM   3168  O  O     . ASP A 1 1847 ? 220.738 191.351 160.903 1.00 117.96 ? 1847 ASP A O     1 
ATOM   3169  C  CB    . ASP A 1 1847 ? 221.336 188.780 161.861 1.00 114.13 ? 1847 ASP A CB    1 
ATOM   3170  C  CG    . ASP A 1 1847 ? 222.692 188.570 161.216 1.00 117.67 ? 1847 ASP A CG    1 
ATOM   3171  O  OD1   . ASP A 1 1847 ? 223.649 189.277 161.595 1.00 118.85 ? 1847 ASP A OD1   1 
ATOM   3172  O  OD2   . ASP A 1 1847 ? 222.801 187.697 160.329 1.00 118.29 ? 1847 ASP A OD2   1 
ATOM   3173  N  N     . PRO A 1 1848 ? 221.870 192.365 162.555 1.00 122.18 ? 1848 PRO A N     1 
ATOM   3174  C  CA    . PRO A 1 1848 ? 221.906 193.633 161.809 1.00 121.12 ? 1848 PRO A CA    1 
ATOM   3175  C  C     . PRO A 1 1848 ? 222.704 193.553 160.521 1.00 123.08 ? 1848 PRO A C     1 
ATOM   3176  O  O     . PRO A 1 1848 ? 222.495 194.382 159.627 1.00 122.61 ? 1848 PRO A O     1 
ATOM   3177  C  CB    . PRO A 1 1848 ? 222.543 194.617 162.802 1.00 119.83 ? 1848 PRO A CB    1 
ATOM   3178  C  CG    . PRO A 1 1848 ? 222.522 193.927 164.135 1.00 119.26 ? 1848 PRO A CG    1 
ATOM   3179  C  CD    . PRO A 1 1848 ? 222.542 192.462 163.860 1.00 120.08 ? 1848 PRO A CD    1 
ATOM   3180  N  N     . LYS A 1 1849 ? 223.610 192.583 160.395 1.00 122.30 ? 1849 LYS A N     1 
ATOM   3181  C  CA    . LYS A 1 1849 ? 224.405 192.422 159.185 1.00 121.95 ? 1849 LYS A CA    1 
ATOM   3182  C  C     . LYS A 1 1849 ? 223.599 191.877 158.013 1.00 122.81 ? 1849 LYS A C     1 
ATOM   3183  O  O     . LYS A 1 1849 ? 224.109 191.866 156.887 1.00 125.67 ? 1849 LYS A O     1 
ATOM   3184  C  CB    . LYS A 1 1849 ? 225.600 191.499 159.450 1.00 122.31 ? 1849 LYS A CB    1 
ATOM   3185  C  CG    . LYS A 1 1849 ? 226.851 192.180 160.013 1.00 124.49 ? 1849 LYS A CG    1 
ATOM   3186  C  CD    . LYS A 1 1849 ? 226.573 193.020 161.251 1.00 124.32 ? 1849 LYS A CD    1 
ATOM   3187  C  CE    . LYS A 1 1849 ? 227.771 193.884 161.612 1.00 125.48 ? 1849 LYS A CE    1 
ATOM   3188  N  NZ    . LYS A 1 1849 ? 227.762 194.277 163.048 1.00 125.39 ? 1849 LYS A NZ    1 
ATOM   3189  N  N     . GLN A 1 1850 ? 222.370 191.424 158.244 1.00 124.98 ? 1850 GLN A N     1 
ATOM   3190  C  CA    . GLN A 1 1850 ? 221.549 190.896 157.163 1.00 126.79 ? 1850 GLN A CA    1 
ATOM   3191  C  C     . GLN A 1 1850 ? 221.105 192.024 156.240 1.00 127.43 ? 1850 GLN A C     1 
ATOM   3192  O  O     . GLN A 1 1850 ? 220.618 193.062 156.698 1.00 125.00 ? 1850 GLN A O     1 
ATOM   3193  C  CB    . GLN A 1 1850 ? 220.334 190.165 157.731 1.00 125.98 ? 1850 GLN A CB    1 
ATOM   3194  C  CG    . GLN A 1 1850 ? 219.417 189.567 156.677 1.00 126.29 ? 1850 GLN A CG    1 
ATOM   3195  C  CD    . GLN A 1 1850 ? 219.794 188.145 156.315 1.00 126.86 ? 1850 GLN A CD    1 
ATOM   3196  O  OE1   . GLN A 1 1850 ? 220.157 187.348 157.180 1.00 125.83 ? 1850 GLN A OE1   1 
ATOM   3197  N  NE2   . GLN A 1 1850 ? 219.703 187.817 155.032 1.00 126.10 ? 1850 GLN A NE2   1 
ATOM   3198  N  N     . THR A 1 1851 ? 221.279 191.817 154.932 1.00 136.79 ? 1851 THR A N     1 
ATOM   3199  C  CA    . THR A 1 1851 ? 220.897 192.841 153.964 1.00 137.18 ? 1851 THR A CA    1 
ATOM   3200  C  C     . THR A 1 1851 ? 219.388 193.051 153.942 1.00 137.07 ? 1851 THR A C     1 
ATOM   3201  O  O     . THR A 1 1851 ? 218.916 194.194 153.922 1.00 136.37 ? 1851 THR A O     1 
ATOM   3202  C  CB    . THR A 1 1851 ? 221.405 192.466 152.572 1.00 136.33 ? 1851 THR A CB    1 
ATOM   3203  O  OG1   . THR A 1 1851 ? 220.912 191.169 152.214 1.00 137.25 ? 1851 THR A OG1   1 
ATOM   3204  C  CG2   . THR A 1 1851 ? 222.926 192.450 152.547 1.00 133.11 ? 1851 THR A CG2   1 
ATOM   3205  N  N     . ASP A 1 1852 ? 218.617 191.967 153.947 1.00 126.52 ? 1852 ASP A N     1 
ATOM   3206  C  CA    . ASP A 1 1852 ? 217.161 192.061 153.932 1.00 126.11 ? 1852 ASP A CA    1 
ATOM   3207  C  C     . ASP A 1 1852 ? 216.683 192.401 155.337 1.00 126.75 ? 1852 ASP A C     1 
ATOM   3208  O  O     . ASP A 1 1852 ? 216.903 191.632 156.279 1.00 128.59 ? 1852 ASP A O     1 
ATOM   3209  C  CB    . ASP A 1 1852 ? 216.547 190.758 153.431 1.00 125.72 ? 1852 ASP A CB    1 
ATOM   3210  C  CG    . ASP A 1 1852 ? 215.118 190.932 152.958 1.00 128.17 ? 1852 ASP A CG    1 
ATOM   3211  O  OD1   . ASP A 1 1852 ? 214.631 192.082 152.947 1.00 127.50 ? 1852 ASP A OD1   1 
ATOM   3212  O  OD2   . ASP A 1 1852 ? 214.486 189.923 152.583 1.00 129.11 ? 1852 ASP A OD2   1 
ATOM   3213  N  N     . VAL A 1 1853 ? 216.029 193.556 155.481 1.00 116.81 ? 1853 VAL A N     1 
ATOM   3214  C  CA    . VAL A 1 1853 ? 215.641 194.036 156.804 1.00 116.12 ? 1853 VAL A CA    1 
ATOM   3215  C  C     . VAL A 1 1853 ? 214.605 193.122 157.444 1.00 116.20 ? 1853 VAL A C     1 
ATOM   3216  O  O     . VAL A 1 1853 ? 214.616 192.920 158.665 1.00 115.06 ? 1853 VAL A O     1 
ATOM   3217  C  CB    . VAL A 1 1853 ? 215.136 195.490 156.715 1.00 116.07 ? 1853 VAL A CB    1 
ATOM   3218  C  CG1   . VAL A 1 1853 ? 216.296 196.434 156.444 1.00 113.71 ? 1853 VAL A CG1   1 
ATOM   3219  C  CG2   . VAL A 1 1853 ? 214.080 195.622 155.630 1.00 115.08 ? 1853 VAL A CG2   1 
ATOM   3220  N  N     . LEU A 1 1854 ? 213.698 192.555 156.646 1.00 104.65 ? 1854 LEU A N     1 
ATOM   3221  C  CA    . LEU A 1 1854 ? 212.645 191.705 157.188 1.00 104.38 ? 1854 LEU A CA    1 
ATOM   3222  C  C     . LEU A 1 1854 ? 213.173 190.400 157.771 1.00 109.74 ? 1854 LEU A C     1 
ATOM   3223  O  O     . LEU A 1 1854 ? 212.489 189.795 158.603 1.00 110.60 ? 1854 LEU A O     1 
ATOM   3224  C  CB    . LEU A 1 1854 ? 211.602 191.401 156.110 1.00 99.18  ? 1854 LEU A CB    1 
ATOM   3225  C  CG    . LEU A 1 1854 ? 210.913 192.590 155.436 1.00 103.29 ? 1854 LEU A CG    1 
ATOM   3226  C  CD1   . LEU A 1 1854 ? 211.674 193.044 154.199 1.00 106.60 ? 1854 LEU A CD1   1 
ATOM   3227  C  CD2   . LEU A 1 1854 ? 209.478 192.240 155.084 1.00 106.97 ? 1854 LEU A CD2   1 
ATOM   3228  N  N     . GLN A 1 1855 ? 214.359 189.953 157.360 1.00 107.57 ? 1855 GLN A N     1 
ATOM   3229  C  CA    . GLN A 1 1855 ? 214.959 188.731 157.880 1.00 102.31 ? 1855 GLN A CA    1 
ATOM   3230  C  C     . GLN A 1 1855 ? 216.055 189.006 158.901 1.00 99.97  ? 1855 GLN A C     1 
ATOM   3231  O  O     . GLN A 1 1855 ? 216.813 188.092 159.244 1.00 103.61 ? 1855 GLN A O     1 
ATOM   3232  C  CB    . GLN A 1 1855 ? 215.513 187.877 156.736 1.00 103.13 ? 1855 GLN A CB    1 
ATOM   3233  C  CG    . GLN A 1 1855 ? 214.473 187.035 156.003 1.00 102.89 ? 1855 GLN A CG    1 
ATOM   3234  C  CD    . GLN A 1 1855 ? 213.413 187.864 155.300 1.00 108.08 ? 1855 GLN A CD    1 
ATOM   3235  O  OE1   . GLN A 1 1855 ? 213.595 189.057 155.063 1.00 112.64 ? 1855 GLN A OE1   1 
ATOM   3236  N  NE2   . GLN A 1 1855 ? 212.297 187.230 154.963 1.00 105.68 ? 1855 GLN A NE2   1 
ATOM   3237  N  N     . GLN A 1 1856 ? 216.162 190.242 159.393 1.00 99.99  ? 1856 GLN A N     1 
ATOM   3238  C  CA    . GLN A 1 1856 ? 217.179 190.549 160.392 1.00 101.94 ? 1856 GLN A CA    1 
ATOM   3239  C  C     . GLN A 1 1856 ? 216.870 189.896 161.732 1.00 105.56 ? 1856 GLN A C     1 
ATOM   3240  O  O     . GLN A 1 1856 ? 217.792 189.546 162.476 1.00 109.54 ? 1856 GLN A O     1 
ATOM   3241  C  CB    . GLN A 1 1856 ? 217.314 192.062 160.560 1.00 104.89 ? 1856 GLN A CB    1 
ATOM   3242  C  CG    . GLN A 1 1856 ? 217.944 192.766 159.371 1.00 108.28 ? 1856 GLN A CG    1 
ATOM   3243  C  CD    . GLN A 1 1856 ? 218.399 194.174 159.703 1.00 108.80 ? 1856 GLN A CD    1 
ATOM   3244  O  OE1   . GLN A 1 1856 ? 217.645 194.966 160.266 1.00 110.54 ? 1856 GLN A OE1   1 
ATOM   3245  N  NE2   . GLN A 1 1856 ? 219.641 194.491 159.357 1.00 106.21 ? 1856 GLN A NE2   1 
ATOM   3246  N  N     . LEU A 1 1857 ? 215.593 189.722 162.056 1.00 78.95  ? 1857 LEU A N     1 
ATOM   3247  C  CA    . LEU A 1 1857 ? 215.171 189.168 163.335 1.00 77.05  ? 1857 LEU A CA    1 
ATOM   3248  C  C     . LEU A 1 1857 ? 214.626 187.761 163.135 1.00 77.96  ? 1857 LEU A C     1 
ATOM   3249  O  O     . LEU A 1 1857 ? 213.824 187.524 162.226 1.00 80.04  ? 1857 LEU A O     1 
ATOM   3250  C  CB    . LEU A 1 1857 ? 214.112 190.053 163.993 1.00 73.97  ? 1857 LEU A CB    1 
ATOM   3251  C  CG    . LEU A 1 1857 ? 213.452 189.462 165.239 1.00 69.11  ? 1857 LEU A CG    1 
ATOM   3252  C  CD1   . LEU A 1 1857 ? 214.472 189.278 166.347 1.00 71.74  ? 1857 LEU A CD1   1 
ATOM   3253  C  CD2   . LEU A 1 1857 ? 212.310 190.341 165.702 1.00 76.60  ? 1857 LEU A CD2   1 
ATOM   3254  N  N     . SER A 1 1858 ? 215.066 186.836 163.984 1.00 68.13  ? 1858 SER A N     1 
ATOM   3255  C  CA    . SER A 1 1858 ? 214.591 185.461 163.973 1.00 59.43  ? 1858 SER A CA    1 
ATOM   3256  C  C     . SER A 1 1858 ? 214.140 185.076 165.372 1.00 61.94  ? 1858 SER A C     1 
ATOM   3257  O  O     . SER A 1 1858 ? 214.851 185.320 166.351 1.00 71.28  ? 1858 SER A O     1 
ATOM   3258  C  CB    . SER A 1 1858 ? 215.680 184.500 163.488 1.00 65.31  ? 1858 SER A CB    1 
ATOM   3259  O  OG    . SER A 1 1858 ? 215.197 183.170 163.438 1.00 75.12  ? 1858 SER A OG    1 
ATOM   3260  N  N     . ILE A 1 1859 ? 212.959 184.472 165.462 1.00 54.92  ? 1859 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 1859 ? 212.377 184.042 166.729 1.00 49.52  ? 1859 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 1859 ? 212.377 182.523 166.751 1.00 59.13  ? 1859 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 1859 ? 211.834 181.884 165.842 1.00 67.10  ? 1859 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 1859 ? 210.957 184.593 166.923 1.00 45.30  ? 1859 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 1859 ? 210.927 186.093 166.628 1.00 51.07  ? 1859 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 1859 ? 210.464 184.304 168.329 1.00 53.95  ? 1859 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 1859 ? 209.546 186.694 166.674 1.00 56.47  ? 1859 ILE A CD1   1 
ATOM   3268  N  N     . GLN A 1 1860 ? 212.980 181.945 167.786 1.00 70.85  ? 1860 GLN A N     1 
ATOM   3269  C  CA    . GLN A 1 1860 ? 213.166 180.505 167.877 1.00 68.16  ? 1860 GLN A CA    1 
ATOM   3270  C  C     . GLN A 1 1860 ? 212.620 179.977 169.195 1.00 69.78  ? 1860 GLN A C     1 
ATOM   3271  O  O     . GLN A 1 1860 ? 212.763 180.616 170.241 1.00 78.95  ? 1860 GLN A O     1 
ATOM   3272  C  CB    . GLN A 1 1860 ? 214.644 180.132 167.748 1.00 62.48  ? 1860 GLN A CB    1 
ATOM   3273  C  CG    . GLN A 1 1860 ? 215.380 180.873 166.649 1.00 69.82  ? 1860 GLN A CG    1 
ATOM   3274  C  CD    . GLN A 1 1860 ? 216.688 180.208 166.279 1.00 83.35  ? 1860 GLN A CD    1 
ATOM   3275  O  OE1   . GLN A 1 1860 ? 217.004 179.123 166.765 1.00 83.34  ? 1860 GLN A OE1   1 
ATOM   3276  N  NE2   . GLN A 1 1860 ? 217.457 180.857 165.413 1.00 80.33  ? 1860 GLN A NE2   1 
ATOM   3277  N  N     . MET A 1 1861 ? 211.994 178.805 169.132 1.00 58.82  ? 1861 MET A N     1 
ATOM   3278  C  CA    . MET A 1 1861 ? 211.556 178.077 170.317 1.00 54.84  ? 1861 MET A CA    1 
ATOM   3279  C  C     . MET A 1 1861 ? 211.756 176.595 170.051 1.00 72.60  ? 1861 MET A C     1 
ATOM   3280  O  O     . MET A 1 1861 ? 211.159 176.049 169.117 1.00 78.46  ? 1861 MET A O     1 
ATOM   3281  C  CB    . MET A 1 1861 ? 210.093 178.374 170.654 1.00 53.77  ? 1861 MET A CB    1 
ATOM   3282  C  CG    . MET A 1 1861 ? 209.785 178.299 172.138 1.00 64.01  ? 1861 MET A CG    1 
ATOM   3283  S  SD    . MET A 1 1861 ? 208.034 178.479 172.515 1.00 85.20  ? 1861 MET A SD    1 
ATOM   3284  C  CE    . MET A 1 1861 ? 208.069 178.381 174.302 1.00 66.67  ? 1861 MET A CE    1 
ATOM   3285  N  N     . ALA A 1 1862 ? 212.594 175.952 170.866 1.00 67.94  ? 1862 ALA A N     1 
ATOM   3286  C  CA    . ALA A 1 1862 ? 212.981 174.548 170.694 1.00 60.41  ? 1862 ALA A CA    1 
ATOM   3287  C  C     . ALA A 1 1862 ? 213.638 174.418 169.325 1.00 65.88  ? 1862 ALA A C     1 
ATOM   3288  O  O     . ALA A 1 1862 ? 214.649 175.099 169.082 1.00 71.03  ? 1862 ALA A O     1 
ATOM   3289  C  CB    . ALA A 1 1862 ? 211.769 173.649 170.945 1.00 62.54  ? 1862 ALA A CB    1 
ATOM   3290  N  N     . ASN A 1 1863 ? 213.131 173.588 168.418 1.00 64.92  ? 1863 ASN A N     1 
ATOM   3291  C  CA    . ASN A 1 1863 ? 213.720 173.432 167.096 1.00 67.77  ? 1863 ASN A CA    1 
ATOM   3292  C  C     . ASN A 1 1863 ? 213.060 174.307 166.038 1.00 71.30  ? 1863 ASN A C     1 
ATOM   3293  O  O     . ASN A 1 1863 ? 213.518 174.316 164.891 1.00 73.59  ? 1863 ASN A O     1 
ATOM   3294  C  CB    . ASN A 1 1863 ? 213.650 171.967 166.658 1.00 70.11  ? 1863 ASN A CB    1 
ATOM   3295  C  CG    . ASN A 1 1863 ? 212.228 171.491 166.446 1.00 74.53  ? 1863 ASN A CG    1 
ATOM   3296  O  OD1   . ASN A 1 1863 ? 211.432 171.441 167.383 1.00 74.41  ? 1863 ASN A OD1   1 
ATOM   3297  N  ND2   . ASN A 1 1863 ? 211.900 171.140 165.208 1.00 77.55  ? 1863 ASN A ND2   1 
ATOM   3298  N  N     . ALA A 1 1864 ? 212.005 175.037 166.388 1.00 68.40  ? 1864 ALA A N     1 
ATOM   3299  C  CA    . ALA A 1 1864 ? 211.253 175.825 165.422 1.00 67.36  ? 1864 ALA A CA    1 
ATOM   3300  C  C     . ALA A 1 1864 ? 211.870 177.209 165.272 1.00 72.26  ? 1864 ALA A C     1 
ATOM   3301  O  O     . ALA A 1 1864 ? 212.269 177.828 166.263 1.00 80.99  ? 1864 ALA A O     1 
ATOM   3302  C  CB    . ALA A 1 1864 ? 209.790 175.943 165.849 1.00 60.05  ? 1864 ALA A CB    1 
ATOM   3303  N  N     . LYS A 1 1865 ? 211.945 177.688 164.033 1.00 69.62  ? 1865 LYS A N     1 
ATOM   3304  C  CA    . LYS A 1 1865 ? 212.459 179.013 163.721 1.00 67.67  ? 1865 LYS A CA    1 
ATOM   3305  C  C     . LYS A 1 1865 ? 211.429 179.783 162.908 1.00 70.14  ? 1865 LYS A C     1 
ATOM   3306  O  O     . LYS A 1 1865 ? 210.878 179.260 161.934 1.00 74.45  ? 1865 LYS A O     1 
ATOM   3307  C  CB    . LYS A 1 1865 ? 213.778 178.930 162.947 1.00 63.85  ? 1865 LYS A CB    1 
ATOM   3308  C  CG    . LYS A 1 1865 ? 214.892 178.220 163.697 1.00 70.86  ? 1865 LYS A CG    1 
ATOM   3309  C  CD    . LYS A 1 1865 ? 216.078 177.941 162.789 1.00 76.81  ? 1865 LYS A CD    1 
ATOM   3310  C  CE    . LYS A 1 1865 ? 217.167 177.176 163.523 1.00 72.39  ? 1865 LYS A CE    1 
ATOM   3311  N  NZ    . LYS A 1 1865 ? 216.688 175.849 163.999 1.00 71.68  ? 1865 LYS A NZ    1 
ATOM   3312  N  N     . PHE A 1 1866 ? 211.176 181.027 163.308 1.00 62.20  ? 1866 PHE A N     1 
ATOM   3313  C  CA    . PHE A 1 1866 ? 210.209 181.877 162.631 1.00 55.21  ? 1866 PHE A CA    1 
ATOM   3314  C  C     . PHE A 1 1866 ? 210.827 183.239 162.357 1.00 58.01  ? 1866 PHE A C     1 
ATOM   3315  O  O     . PHE A 1 1866 ? 211.789 183.647 163.012 1.00 69.33  ? 1866 PHE A O     1 
ATOM   3316  C  CB    . PHE A 1 1866 ? 208.926 182.058 163.451 1.00 52.97  ? 1866 PHE A CB    1 
ATOM   3317  C  CG    . PHE A 1 1866 ? 208.358 180.777 163.983 1.00 57.16  ? 1866 PHE A CG    1 
ATOM   3318  C  CD1   . PHE A 1 1866 ? 207.563 179.974 163.184 1.00 56.23  ? 1866 PHE A CD1   1 
ATOM   3319  C  CD2   . PHE A 1 1866 ? 208.613 180.380 165.282 1.00 57.74  ? 1866 PHE A CD2   1 
ATOM   3320  C  CE1   . PHE A 1 1866 ? 207.036 178.797 163.671 1.00 59.01  ? 1866 PHE A CE1   1 
ATOM   3321  C  CE2   . PHE A 1 1866 ? 208.090 179.204 165.773 1.00 57.09  ? 1866 PHE A CE2   1 
ATOM   3322  C  CZ    . PHE A 1 1866 ? 207.299 178.412 164.967 1.00 63.09  ? 1866 PHE A CZ    1 
ATOM   3323  N  N     . ASN A 1 1867 ? 210.260 183.935 161.378 1.00 70.24  ? 1867 ASN A N     1 
ATOM   3324  C  CA    . ASN A 1 1867 ? 210.655 185.295 161.045 1.00 72.63  ? 1867 ASN A CA    1 
ATOM   3325  C  C     . ASN A 1 1867 ? 209.547 186.258 161.445 1.00 75.59  ? 1867 ASN A C     1 
ATOM   3326  O  O     . ASN A 1 1867 ? 208.365 185.989 161.213 1.00 76.16  ? 1867 ASN A O     1 
ATOM   3327  C  CB    . ASN A 1 1867 ? 210.949 185.430 159.551 1.00 71.06  ? 1867 ASN A CB    1 
ATOM   3328  C  CG    . ASN A 1 1867 ? 212.298 184.861 159.170 1.00 78.24  ? 1867 ASN A CG    1 
ATOM   3329  O  OD1   . ASN A 1 1867 ? 213.227 184.845 159.976 1.00 79.77  ? 1867 ASN A OD1   1 
ATOM   3330  N  ND2   . ASN A 1 1867 ? 212.413 184.389 157.934 1.00 80.14  ? 1867 ASN A ND2   1 
ATOM   3331  N  N     . TYR A 1 1868 ? 209.934 187.376 162.053 1.00 64.43  ? 1868 TYR A N     1 
ATOM   3332  C  CA    . TYR A 1 1868 ? 208.958 188.381 162.446 1.00 59.11  ? 1868 TYR A CA    1 
ATOM   3333  C  C     . TYR A 1 1868 ? 208.265 188.947 161.215 1.00 65.98  ? 1868 TYR A C     1 
ATOM   3334  O  O     . TYR A 1 1868 ? 208.918 189.424 160.282 1.00 70.01  ? 1868 TYR A O     1 
ATOM   3335  C  CB    . TYR A 1 1868 ? 209.637 189.497 163.238 1.00 54.73  ? 1868 TYR A CB    1 
ATOM   3336  C  CG    . TYR A 1 1868 ? 208.700 190.270 164.137 1.00 54.78  ? 1868 TYR A CG    1 
ATOM   3337  C  CD1   . TYR A 1 1868 ? 208.181 189.698 165.287 1.00 61.76  ? 1868 TYR A CD1   1 
ATOM   3338  C  CD2   . TYR A 1 1868 ? 208.332 191.572 163.832 1.00 64.02  ? 1868 TYR A CD2   1 
ATOM   3339  C  CE1   . TYR A 1 1868 ? 207.325 190.401 166.110 1.00 63.54  ? 1868 TYR A CE1   1 
ATOM   3340  C  CE2   . TYR A 1 1868 ? 207.475 192.283 164.648 1.00 61.63  ? 1868 TYR A CE2   1 
ATOM   3341  C  CZ    . TYR A 1 1868 ? 206.975 191.692 165.785 1.00 61.83  ? 1868 TYR A CZ    1 
ATOM   3342  O  OH    . TYR A 1 1868 ? 206.121 192.395 166.603 1.00 71.41  ? 1868 TYR A OH    1 
ATOM   3343  N  N     . GLY A 1 1869 ? 206.932 188.892 161.213 1.00 70.46  ? 1869 GLY A N     1 
ATOM   3344  C  CA    . GLY A 1 1869 ? 206.174 189.372 160.072 1.00 69.84  ? 1869 GLY A CA    1 
ATOM   3345  C  C     . GLY A 1 1869 ? 206.134 190.879 159.946 1.00 70.47  ? 1869 GLY A C     1 
ATOM   3346  O  O     . GLY A 1 1869 ? 205.777 191.390 158.880 1.00 76.06  ? 1869 GLY A O     1 
ATOM   3347  N  N     . PHE A 1 1870 ? 206.480 191.599 161.014 1.00 70.66  ? 1870 PHE A N     1 
ATOM   3348  C  CA    . PHE A 1 1870 ? 206.537 193.061 161.011 1.00 67.15  ? 1870 PHE A CA    1 
ATOM   3349  C  C     . PHE A 1 1870 ? 205.190 193.690 160.664 1.00 71.28  ? 1870 PHE A C     1 
ATOM   3350  O  O     . PHE A 1 1870 ? 205.132 194.761 160.059 1.00 83.35  ? 1870 PHE A O     1 
ATOM   3351  C  CB    . PHE A 1 1870 ? 207.629 193.572 160.068 1.00 67.86  ? 1870 PHE A CB    1 
ATOM   3352  C  CG    . PHE A 1 1870 ? 209.014 193.407 160.612 1.00 66.87  ? 1870 PHE A CG    1 
ATOM   3353  C  CD1   . PHE A 1 1870 ? 209.385 194.043 161.780 1.00 66.94  ? 1870 PHE A CD1   1 
ATOM   3354  C  CD2   . PHE A 1 1870 ? 209.941 192.613 159.962 1.00 71.99  ? 1870 PHE A CD2   1 
ATOM   3355  C  CE1   . PHE A 1 1870 ? 210.652 193.892 162.293 1.00 66.32  ? 1870 PHE A CE1   1 
ATOM   3356  C  CE2   . PHE A 1 1870 ? 211.214 192.460 160.469 1.00 74.22  ? 1870 PHE A CE2   1 
ATOM   3357  C  CZ    . PHE A 1 1870 ? 211.571 193.101 161.636 1.00 71.72  ? 1870 PHE A CZ    1 
ATOM   3358  N  N     . GLU A 1 1871 ? 204.099 193.027 161.034 1.00 80.18  ? 1871 GLU A N     1 
ATOM   3359  C  CA    . GLU A 1 1871 ? 202.777 193.621 160.891 1.00 76.80  ? 1871 GLU A CA    1 
ATOM   3360  C  C     . GLU A 1 1871 ? 202.482 194.516 162.088 1.00 84.37  ? 1871 GLU A C     1 
ATOM   3361  O  O     . GLU A 1 1871 ? 202.572 194.077 163.238 1.00 94.64  ? 1871 GLU A O     1 
ATOM   3362  C  CB    . GLU A 1 1871 ? 201.721 192.525 160.766 1.00 75.29  ? 1871 GLU A CB    1 
ATOM   3363  C  CG    . GLU A 1 1871 ? 200.298 192.988 161.008 1.00 87.90  ? 1871 GLU A CG    1 
ATOM   3364  C  CD    . GLU A 1 1871 ? 199.649 193.550 159.763 1.00 93.79  ? 1871 GLU A CD    1 
ATOM   3365  O  OE1   . GLU A 1 1871 ? 200.095 193.197 158.652 1.00 94.28  ? 1871 GLU A OE1   1 
ATOM   3366  O  OE2   . GLU A 1 1871 ? 198.692 194.341 159.894 1.00 92.48  ? 1871 GLU A OE2   1 
ATOM   3367  N  N     . TYR A 1 1872 ? 202.127 195.772 161.823 1.00 82.43  ? 1872 TYR A N     1 
ATOM   3368  C  CA    . TYR A 1 1872 ? 201.879 196.729 162.897 1.00 86.63  ? 1872 TYR A CA    1 
ATOM   3369  C  C     . TYR A 1 1872 ? 200.611 196.334 163.639 1.00 88.25  ? 1872 TYR A C     1 
ATOM   3370  O  O     . TYR A 1 1872 ? 199.505 196.439 163.100 1.00 89.41  ? 1872 TYR A O     1 
ATOM   3371  C  CB    . TYR A 1 1872 ? 201.768 198.142 162.337 1.00 84.37  ? 1872 TYR A CB    1 
ATOM   3372  C  CG    . TYR A 1 1872 ? 201.550 199.214 163.372 1.00 85.87  ? 1872 TYR A CG    1 
ATOM   3373  C  CD1   . TYR A 1 1872 ? 202.386 199.325 164.470 1.00 87.41  ? 1872 TYR A CD1   1 
ATOM   3374  C  CD2   . TYR A 1 1872 ? 200.502 200.115 163.251 1.00 82.50  ? 1872 TYR A CD2   1 
ATOM   3375  C  CE1   . TYR A 1 1872 ? 202.191 200.302 165.414 1.00 86.00  ? 1872 TYR A CE1   1 
ATOM   3376  C  CE2   . TYR A 1 1872 ? 200.296 201.093 164.190 1.00 86.85  ? 1872 TYR A CE2   1 
ATOM   3377  C  CZ    . TYR A 1 1872 ? 201.145 201.183 165.272 1.00 90.28  ? 1872 TYR A CZ    1 
ATOM   3378  O  OH    . TYR A 1 1872 ? 200.955 202.156 166.223 1.00 94.86  ? 1872 TYR A OH    1 
ATOM   3379  N  N     . LEU A 1 1873 ? 200.774 195.882 164.877 1.00 78.74  ? 1873 LEU A N     1 
ATOM   3380  C  CA    . LEU A 1 1873 ? 199.672 195.427 165.706 1.00 80.29  ? 1873 LEU A CA    1 
ATOM   3381  C  C     . LEU A 1 1873 ? 199.083 196.539 166.560 1.00 84.32  ? 1873 LEU A C     1 
ATOM   3382  O  O     . LEU A 1 1873 ? 198.090 196.307 167.254 1.00 88.24  ? 1873 LEU A O     1 
ATOM   3383  C  CB    . LEU A 1 1873 ? 200.142 194.280 166.602 1.00 80.23  ? 1873 LEU A CB    1 
ATOM   3384  C  CG    . LEU A 1 1873 ? 200.969 193.202 165.901 1.00 78.56  ? 1873 LEU A CG    1 
ATOM   3385  C  CD1   . LEU A 1 1873 ? 201.895 192.525 166.890 1.00 81.18  ? 1873 LEU A CD1   1 
ATOM   3386  C  CD2   . LEU A 1 1873 ? 200.063 192.184 165.226 1.00 78.30  ? 1873 LEU A CD2   1 
ATOM   3387  N  N     . GLY A 1 1874 ? 199.656 197.736 166.515 1.00 79.49  ? 1874 GLY A N     1 
ATOM   3388  C  CA    . GLY A 1 1874 ? 199.175 198.800 167.379 1.00 76.71  ? 1874 GLY A CA    1 
ATOM   3389  C  C     . GLY A 1 1874 ? 199.597 198.533 168.808 1.00 77.41  ? 1874 GLY A C     1 
ATOM   3390  O  O     . GLY A 1 1874 ? 200.673 197.982 169.066 1.00 80.39  ? 1874 GLY A O     1 
ATOM   3391  N  N     . VAL A 1 1875 ? 198.748 198.920 169.754 1.00 74.17  ? 1875 VAL A N     1 
ATOM   3392  C  CA    . VAL A 1 1875 ? 198.990 198.689 171.173 1.00 75.18  ? 1875 VAL A CA    1 
ATOM   3393  C  C     . VAL A 1 1875 ? 197.994 197.627 171.619 1.00 75.94  ? 1875 VAL A C     1 
ATOM   3394  O  O     . VAL A 1 1875 ? 196.832 197.934 171.911 1.00 76.86  ? 1875 VAL A O     1 
ATOM   3395  C  CB    . VAL A 1 1875 ? 198.855 199.967 172.005 1.00 72.23  ? 1875 VAL A CB    1 
ATOM   3396  C  CG1   . VAL A 1 1875 ? 199.183 199.682 173.461 1.00 73.20  ? 1875 VAL A CG1   1 
ATOM   3397  C  CG2   . VAL A 1 1875 ? 199.759 201.053 171.455 1.00 74.56  ? 1875 VAL A CG2   1 
ATOM   3398  N  N     . GLN A 1 1876 ? 198.442 196.377 171.673 1.00 74.05  ? 1876 GLN A N     1 
ATOM   3399  C  CA    . GLN A 1 1876 ? 197.587 195.266 172.063 1.00 77.15  ? 1876 GLN A CA    1 
ATOM   3400  C  C     . GLN A 1 1876 ? 197.819 194.908 173.523 1.00 79.44  ? 1876 GLN A C     1 
ATOM   3401  O  O     . GLN A 1 1876 ? 198.921 195.081 174.052 1.00 75.24  ? 1876 GLN A O     1 
ATOM   3402  C  CB    . GLN A 1 1876 ? 197.847 194.045 171.179 1.00 79.19  ? 1876 GLN A CB    1 
ATOM   3403  C  CG    . GLN A 1 1876 ? 197.687 194.283 169.678 1.00 78.61  ? 1876 GLN A CG    1 
ATOM   3404  C  CD    . GLN A 1 1876 ? 196.244 194.485 169.234 1.00 81.40  ? 1876 GLN A CD    1 
ATOM   3405  O  OE1   . GLN A 1 1876 ? 195.457 195.163 169.894 1.00 80.78  ? 1876 GLN A OE1   1 
ATOM   3406  N  NE2   . GLN A 1 1876 ? 195.895 193.890 168.100 1.00 77.48  ? 1876 GLN A NE2   1 
ATOM   3407  N  N     . ASP A 1 1877 ? 196.771 194.409 174.171 1.00 84.99  ? 1877 ASP A N     1 
ATOM   3408  C  CA    . ASP A 1 1877 ? 196.853 194.018 175.573 1.00 81.16  ? 1877 ASP A CA    1 
ATOM   3409  C  C     . ASP A 1 1877 ? 197.667 192.736 175.696 1.00 82.97  ? 1877 ASP A C     1 
ATOM   3410  O  O     . ASP A 1 1877 ? 197.192 191.653 175.341 1.00 82.47  ? 1877 ASP A O     1 
ATOM   3411  C  CB    . ASP A 1 1877 ? 195.453 193.836 176.149 1.00 85.00  ? 1877 ASP A CB    1 
ATOM   3412  C  CG    . ASP A 1 1877 ? 194.586 195.066 175.966 1.00 89.68  ? 1877 ASP A CG    1 
ATOM   3413  O  OD1   . ASP A 1 1877 ? 195.147 196.169 175.798 1.00 87.86  ? 1877 ASP A OD1   1 
ATOM   3414  O  OD2   . ASP A 1 1877 ? 193.344 194.930 175.988 1.00 90.27  ? 1877 ASP A OD2   1 
ATOM   3415  N  N     . LYS A 1 1878 ? 198.894 192.856 176.194 1.00 80.30  ? 1878 LYS A N     1 
ATOM   3416  C  CA    . LYS A 1 1878 ? 199.733 191.687 176.409 1.00 81.86  ? 1878 LYS A CA    1 
ATOM   3417  C  C     . LYS A 1 1878 ? 199.182 190.832 177.544 1.00 78.09  ? 1878 LYS A C     1 
ATOM   3418  O  O     . LYS A 1 1878 ? 198.544 191.329 178.475 1.00 76.10  ? 1878 LYS A O     1 
ATOM   3419  C  CB    . LYS A 1 1878 ? 201.167 192.108 176.727 1.00 75.61  ? 1878 LYS A CB    1 
ATOM   3420  C  CG    . LYS A 1 1878 ? 201.939 192.652 175.539 1.00 72.04  ? 1878 LYS A CG    1 
ATOM   3421  C  CD    . LYS A 1 1878 ? 203.138 191.775 175.222 1.00 73.84  ? 1878 LYS A CD    1 
ATOM   3422  C  CE    . LYS A 1 1878 ? 203.993 191.545 176.457 1.00 77.23  ? 1878 LYS A CE    1 
ATOM   3423  N  NZ    . LYS A 1 1878 ? 205.098 190.584 176.196 1.00 78.83  ? 1878 LYS A NZ    1 
ATOM   3424  N  N     . LEU A 1 1879 ? 199.435 189.531 177.458 1.00 64.69  ? 1879 LEU A N     1 
ATOM   3425  C  CA    . LEU A 1 1879 ? 199.023 188.585 178.485 1.00 60.18  ? 1879 LEU A CA    1 
ATOM   3426  C  C     . LEU A 1 1879 ? 200.232 188.155 179.302 1.00 62.70  ? 1879 LEU A C     1 
ATOM   3427  O  O     . LEU A 1 1879 ? 201.347 188.075 178.775 1.00 65.48  ? 1879 LEU A O     1 
ATOM   3428  C  CB    . LEU A 1 1879 ? 198.344 187.359 177.874 1.00 56.60  ? 1879 LEU A CB    1 
ATOM   3429  C  CG    . LEU A 1 1879 ? 197.578 187.515 176.565 1.00 62.38  ? 1879 LEU A CG    1 
ATOM   3430  C  CD1   . LEU A 1 1879 ? 197.213 186.145 176.035 1.00 64.49  ? 1879 LEU A CD1   1 
ATOM   3431  C  CD2   . LEU A 1 1879 ? 196.333 188.359 176.771 1.00 67.92  ? 1879 LEU A CD2   1 
ATOM   3432  N  N     . VAL A 1 1880 ? 200.006 187.887 180.588 1.00 55.84  ? 1880 VAL A N     1 
ATOM   3433  C  CA    . VAL A 1 1880 ? 201.075 187.406 181.451 1.00 55.07  ? 1880 VAL A CA    1 
ATOM   3434  C  C     . VAL A 1 1880 ? 201.549 186.049 180.962 1.00 63.47  ? 1880 VAL A C     1 
ATOM   3435  O  O     . VAL A 1 1880 ? 200.741 185.160 180.672 1.00 72.99  ? 1880 VAL A O     1 
ATOM   3436  C  CB    . VAL A 1 1880 ? 200.595 187.342 182.910 1.00 55.54  ? 1880 VAL A CB    1 
ATOM   3437  C  CG1   . VAL A 1 1880 ? 201.766 187.072 183.828 1.00 58.83  ? 1880 VAL A CG1   1 
ATOM   3438  C  CG2   . VAL A 1 1880 ? 199.898 188.637 183.292 1.00 55.49  ? 1880 VAL A CG2   1 
ATOM   3439  N  N     . GLN A 1 1881 ? 202.868 185.884 180.874 1.00 63.45  ? 1881 GLN A N     1 
ATOM   3440  C  CA    . GLN A 1 1881 ? 203.467 184.651 180.365 1.00 64.65  ? 1881 GLN A CA    1 
ATOM   3441  C  C     . GLN A 1 1881 ? 203.497 183.615 181.486 1.00 65.31  ? 1881 GLN A C     1 
ATOM   3442  O  O     . GLN A 1 1881 ? 204.532 183.322 182.089 1.00 68.36  ? 1881 GLN A O     1 
ATOM   3443  C  CB    . GLN A 1 1881 ? 204.859 184.921 179.811 1.00 71.53  ? 1881 GLN A CB    1 
ATOM   3444  C  CG    . GLN A 1 1881 ? 204.862 185.658 178.486 1.00 65.74  ? 1881 GLN A CG    1 
ATOM   3445  C  CD    . GLN A 1 1881 ? 204.511 184.758 177.321 1.00 70.76  ? 1881 GLN A CD    1 
ATOM   3446  O  OE1   . GLN A 1 1881 ? 204.456 183.537 177.460 1.00 71.67  ? 1881 GLN A OE1   1 
ATOM   3447  N  NE2   . GLN A 1 1881 ? 204.270 185.358 176.162 1.00 76.79  ? 1881 GLN A NE2   1 
ATOM   3448  N  N     . THR A 1 1882 ? 202.328 183.054 181.765 1.00 64.17  ? 1882 THR A N     1 
ATOM   3449  C  CA    . THR A 1 1882 ? 202.195 181.995 182.750 1.00 69.82  ? 1882 THR A CA    1 
ATOM   3450  C  C     . THR A 1 1882 ? 202.778 180.700 182.200 1.00 72.18  ? 1882 THR A C     1 
ATOM   3451  O  O     . THR A 1 1882 ? 202.966 180.554 180.991 1.00 79.51  ? 1882 THR A O     1 
ATOM   3452  C  CB    . THR A 1 1882 ? 200.725 181.824 183.124 1.00 68.28  ? 1882 THR A CB    1 
ATOM   3453  O  OG1   . THR A 1 1882 ? 199.981 181.409 181.973 1.00 74.77  ? 1882 THR A OG1   1 
ATOM   3454  C  CG2   . THR A 1 1882 ? 200.160 183.132 183.636 1.00 65.35  ? 1882 THR A CG2   1 
ATOM   3455  N  N     . PRO A 1 1883 ? 203.100 179.739 183.073 1.00 61.23  ? 1883 PRO A N     1 
ATOM   3456  C  CA    . PRO A 1 1883 ? 203.612 178.450 182.576 1.00 66.35  ? 1883 PRO A CA    1 
ATOM   3457  C  C     . PRO A 1 1883 ? 202.677 177.758 181.598 1.00 66.72  ? 1883 PRO A C     1 
ATOM   3458  O  O     . PRO A 1 1883 ? 203.148 177.089 180.669 1.00 70.69  ? 1883 PRO A O     1 
ATOM   3459  C  CB    . PRO A 1 1883 ? 203.794 177.638 183.864 1.00 61.64  ? 1883 PRO A CB    1 
ATOM   3460  C  CG    . PRO A 1 1883 ? 204.062 178.661 184.904 1.00 61.82  ? 1883 PRO A CG    1 
ATOM   3461  C  CD    . PRO A 1 1883 ? 203.211 179.844 184.538 1.00 60.43  ? 1883 PRO A CD    1 
ATOM   3462  N  N     . LEU A 1 1884 ? 201.362 177.895 181.780 1.00 63.33  ? 1884 LEU A N     1 
ATOM   3463  C  CA    . LEU A 1 1884 ? 200.427 177.343 180.805 1.00 60.78  ? 1884 LEU A CA    1 
ATOM   3464  C  C     . LEU A 1 1884 ? 200.587 178.020 179.450 1.00 62.55  ? 1884 LEU A C     1 
ATOM   3465  O  O     . LEU A 1 1884 ? 200.533 177.359 178.407 1.00 70.32  ? 1884 LEU A O     1 
ATOM   3466  C  CB    . LEU A 1 1884 ? 198.993 177.483 181.310 1.00 63.64  ? 1884 LEU A CB    1 
ATOM   3467  C  CG    . LEU A 1 1884 ? 197.910 177.061 180.316 1.00 64.90  ? 1884 LEU A CG    1 
ATOM   3468  C  CD1   . LEU A 1 1884 ? 197.972 175.564 180.069 1.00 67.29  ? 1884 LEU A CD1   1 
ATOM   3469  C  CD2   . LEU A 1 1884 ? 196.535 177.467 180.814 1.00 67.00  ? 1884 LEU A CD2   1 
ATOM   3470  N  N     . THR A 1 1885 ? 200.786 179.340 179.443 1.00 67.88  ? 1885 THR A N     1 
ATOM   3471  C  CA    . THR A 1 1885 ? 201.026 180.042 178.186 1.00 65.52  ? 1885 THR A CA    1 
ATOM   3472  C  C     . THR A 1 1885 ? 202.343 179.606 177.555 1.00 68.58  ? 1885 THR A C     1 
ATOM   3473  O  O     . THR A 1 1885 ? 202.453 179.521 176.328 1.00 77.01  ? 1885 THR A O     1 
ATOM   3474  C  CB    . THR A 1 1885 ? 201.010 181.554 178.414 1.00 65.60  ? 1885 THR A CB    1 
ATOM   3475  O  OG1   . THR A 1 1885 ? 199.761 181.935 179.002 1.00 75.83  ? 1885 THR A OG1   1 
ATOM   3476  C  CG2   . THR A 1 1885 ? 201.183 182.296 177.099 1.00 64.38  ? 1885 THR A CG2   1 
ATOM   3477  N  N     . ASP A 1 1886 ? 203.356 179.325 178.378 1.00 65.52  ? 1886 ASP A N     1 
ATOM   3478  C  CA    . ASP A 1 1886 ? 204.618 178.813 177.851 1.00 63.07  ? 1886 ASP A CA    1 
ATOM   3479  C  C     . ASP A 1 1886 ? 204.425 177.447 177.205 1.00 68.60  ? 1886 ASP A C     1 
ATOM   3480  O  O     . ASP A 1 1886 ? 204.974 177.167 176.132 1.00 73.97  ? 1886 ASP A O     1 
ATOM   3481  C  CB    . ASP A 1 1886 ? 205.657 178.741 178.969 1.00 67.70  ? 1886 ASP A CB    1 
ATOM   3482  C  CG    . ASP A 1 1886 ? 206.543 179.966 179.019 1.00 80.02  ? 1886 ASP A CG    1 
ATOM   3483  O  OD1   . ASP A 1 1886 ? 206.549 180.737 178.036 1.00 80.22  ? 1886 ASP A OD1   1 
ATOM   3484  O  OD2   . ASP A 1 1886 ? 207.230 180.162 180.043 1.00 76.98  ? 1886 ASP A OD2   1 
ATOM   3485  N  N     . ARG A 1 1887 ? 203.646 176.578 177.853 1.00 66.20  ? 1887 ARG A N     1 
ATOM   3486  C  CA    . ARG A 1 1887 ? 203.330 175.280 177.265 1.00 58.17  ? 1887 ARG A CA    1 
ATOM   3487  C  C     . ARG A 1 1887 ? 202.571 175.445 175.957 1.00 62.14  ? 1887 ARG A C     1 
ATOM   3488  O  O     . ARG A 1 1887 ? 202.814 174.712 174.990 1.00 70.31  ? 1887 ARG A O     1 
ATOM   3489  C  CB    . ARG A 1 1887 ? 202.520 174.444 178.255 1.00 62.66  ? 1887 ARG A CB    1 
ATOM   3490  C  CG    . ARG A 1 1887 ? 202.614 172.946 178.039 1.00 62.80  ? 1887 ARG A CG    1 
ATOM   3491  C  CD    . ARG A 1 1887 ? 202.533 172.200 179.361 1.00 70.90  ? 1887 ARG A CD    1 
ATOM   3492  N  NE    . ARG A 1 1887 ? 201.162 171.846 179.709 1.00 74.23  ? 1887 ARG A NE    1 
ATOM   3493  C  CZ    . ARG A 1 1887 ? 200.525 170.776 179.255 1.00 76.87  ? 1887 ARG A CZ    1 
ATOM   3494  N  NH1   . ARG A 1 1887 ? 201.106 169.928 178.422 1.00 74.52  ? 1887 ARG A NH1   1 
ATOM   3495  N  NH2   . ARG A 1 1887 ? 199.274 170.550 179.646 1.00 73.45  ? 1887 ARG A NH2   1 
ATOM   3496  N  N     . CYS A 1 1888 ? 201.639 176.399 175.913 1.00 55.28  ? 1888 CYS A N     1 
ATOM   3497  C  CA    . CYS A 1 1888 ? 200.910 176.673 174.680 1.00 48.54  ? 1888 CYS A CA    1 
ATOM   3498  C  C     . CYS A 1 1888 ? 201.847 177.125 173.573 1.00 54.50  ? 1888 CYS A C     1 
ATOM   3499  O  O     . CYS A 1 1888 ? 201.733 176.670 172.431 1.00 67.44  ? 1888 CYS A O     1 
ATOM   3500  C  CB    . CYS A 1 1888 ? 199.840 177.733 174.920 1.00 52.35  ? 1888 CYS A CB    1 
ATOM   3501  S  SG    . CYS A 1 1888 ? 198.866 178.127 173.450 1.00 74.73  ? 1888 CYS A SG    1 
ATOM   3502  N  N     . TYR A 1 1889 ? 202.774 178.030 173.890 1.00 57.39  ? 1889 TYR A N     1 
ATOM   3503  C  CA    . TYR A 1 1889 ? 203.724 178.497 172.888 1.00 48.87  ? 1889 TYR A CA    1 
ATOM   3504  C  C     . TYR A 1 1889 ? 204.572 177.344 172.374 1.00 54.96  ? 1889 TYR A C     1 
ATOM   3505  O  O     . TYR A 1 1889 ? 204.770 177.196 171.165 1.00 61.53  ? 1889 TYR A O     1 
ATOM   3506  C  CB    . TYR A 1 1889 ? 204.611 179.597 173.472 1.00 45.09  ? 1889 TYR A CB    1 
ATOM   3507  C  CG    . TYR A 1 1889 ? 203.992 180.975 173.452 1.00 49.23  ? 1889 TYR A CG    1 
ATOM   3508  C  CD1   . TYR A 1 1889 ? 202.616 181.141 173.419 1.00 56.39  ? 1889 TYR A CD1   1 
ATOM   3509  C  CD2   . TYR A 1 1889 ? 204.788 182.111 173.471 1.00 52.20  ? 1889 TYR A CD2   1 
ATOM   3510  C  CE1   . TYR A 1 1889 ? 202.049 182.399 173.404 1.00 54.45  ? 1889 TYR A CE1   1 
ATOM   3511  C  CE2   . TYR A 1 1889 ? 204.230 183.373 173.456 1.00 58.56  ? 1889 TYR A CE2   1 
ATOM   3512  C  CZ    . TYR A 1 1889 ? 202.861 183.510 173.422 1.00 59.94  ? 1889 TYR A CZ    1 
ATOM   3513  O  OH    . TYR A 1 1889 ? 202.301 184.766 173.407 1.00 59.26  ? 1889 TYR A OH    1 
ATOM   3514  N  N     . LEU A 1 1890 ? 205.060 176.499 173.285 1.00 62.17  ? 1890 LEU A N     1 
ATOM   3515  C  CA    . LEU A 1 1890 ? 205.885 175.365 172.880 1.00 51.36  ? 1890 LEU A CA    1 
ATOM   3516  C  C     . LEU A 1 1890 ? 205.114 174.422 171.963 1.00 57.14  ? 1890 LEU A C     1 
ATOM   3517  O  O     . LEU A 1 1890 ? 205.593 174.059 170.882 1.00 69.21  ? 1890 LEU A O     1 
ATOM   3518  C  CB    . LEU A 1 1890 ? 206.392 174.621 174.114 1.00 52.05  ? 1890 LEU A CB    1 
ATOM   3519  C  CG    . LEU A 1 1890 ? 207.279 173.403 173.858 1.00 52.07  ? 1890 LEU A CG    1 
ATOM   3520  C  CD1   . LEU A 1 1890 ? 208.563 173.813 173.162 1.00 55.95  ? 1890 LEU A CD1   1 
ATOM   3521  C  CD2   . LEU A 1 1890 ? 207.580 172.684 175.160 1.00 58.84  ? 1890 LEU A CD2   1 
ATOM   3522  N  N     . THR A 1 1891 ? 203.908 174.024 172.376 1.00 53.30  ? 1891 THR A N     1 
ATOM   3523  C  CA    . THR A 1 1891 ? 203.132 173.076 171.582 1.00 47.63  ? 1891 THR A CA    1 
ATOM   3524  C  C     . THR A 1 1891 ? 202.743 173.666 170.233 1.00 50.35  ? 1891 THR A C     1 
ATOM   3525  O  O     . THR A 1 1891 ? 202.839 172.991 169.201 1.00 56.16  ? 1891 THR A O     1 
ATOM   3526  C  CB    . THR A 1 1891 ? 201.886 172.642 172.352 1.00 53.19  ? 1891 THR A CB    1 
ATOM   3527  O  OG1   . THR A 1 1891 ? 202.252 172.270 173.686 1.00 67.26  ? 1891 THR A OG1   1 
ATOM   3528  C  CG2   . THR A 1 1891 ? 201.229 171.456 171.667 1.00 61.04  ? 1891 THR A CG2   1 
ATOM   3529  N  N     . MET A 1 1892 ? 202.307 174.928 170.216 1.00 50.13  ? 1892 MET A N     1 
ATOM   3530  C  CA    . MET A 1 1892 ? 201.887 175.548 168.967 1.00 47.81  ? 1892 MET A CA    1 
ATOM   3531  C  C     . MET A 1 1892 ? 203.062 175.734 168.016 1.00 52.90  ? 1892 MET A C     1 
ATOM   3532  O  O     . MET A 1 1892 ? 202.919 175.538 166.806 1.00 63.32  ? 1892 MET A O     1 
ATOM   3533  C  CB    . MET A 1 1892 ? 201.203 176.883 169.250 1.00 52.58  ? 1892 MET A CB    1 
ATOM   3534  C  CG    . MET A 1 1892 ? 199.800 176.770 169.827 1.00 53.76  ? 1892 MET A CG    1 
ATOM   3535  S  SD    . MET A 1 1892 ? 198.899 175.319 169.254 1.00 83.88  ? 1892 MET A SD    1 
ATOM   3536  C  CE    . MET A 1 1892 ? 198.967 174.273 170.704 1.00 58.66  ? 1892 MET A CE    1 
ATOM   3537  N  N     . THR A 1 1893 ? 204.233 176.110 168.537 1.00 43.41  ? 1893 THR A N     1 
ATOM   3538  C  CA    . THR A 1 1893 ? 205.404 176.241 167.678 1.00 43.21  ? 1893 THR A CA    1 
ATOM   3539  C  C     . THR A 1 1893 ? 205.860 174.890 167.145 1.00 60.18  ? 1893 THR A C     1 
ATOM   3540  O  O     . THR A 1 1893 ? 206.286 174.797 165.988 1.00 64.90  ? 1893 THR A O     1 
ATOM   3541  C  CB    . THR A 1 1893 ? 206.541 176.925 168.435 1.00 47.48  ? 1893 THR A CB    1 
ATOM   3542  O  OG1   . THR A 1 1893 ? 206.686 176.322 169.726 1.00 63.31  ? 1893 THR A OG1   1 
ATOM   3543  C  CG2   . THR A 1 1893 ? 206.247 178.405 168.606 1.00 55.64  ? 1893 THR A CG2   1 
ATOM   3544  N  N     . GLN A 1 1894 ? 205.781 173.837 167.964 1.00 66.61  ? 1894 GLN A N     1 
ATOM   3545  C  CA    . GLN A 1 1894 ? 206.107 172.503 167.471 1.00 56.80  ? 1894 GLN A CA    1 
ATOM   3546  C  C     . GLN A 1 1894 ? 205.144 172.076 166.372 1.00 61.01  ? 1894 GLN A C     1 
ATOM   3547  O  O     . GLN A 1 1894 ? 205.552 171.454 165.385 1.00 70.04  ? 1894 GLN A O     1 
ATOM   3548  C  CB    . GLN A 1 1894 ? 206.091 171.496 168.620 1.00 54.79  ? 1894 GLN A CB    1 
ATOM   3549  C  CG    . GLN A 1 1894 ? 207.232 171.662 169.602 1.00 59.75  ? 1894 GLN A CG    1 
ATOM   3550  C  CD    . GLN A 1 1894 ? 208.579 171.367 168.982 1.00 63.98  ? 1894 GLN A CD    1 
ATOM   3551  O  OE1   . GLN A 1 1894 ? 208.876 170.228 168.627 1.00 68.33  ? 1894 GLN A OE1   1 
ATOM   3552  N  NE2   . GLN A 1 1894 ? 209.405 172.397 168.848 1.00 62.40  ? 1894 GLN A NE2   1 
ATOM   3553  N  N     . ALA A 1 1895 ? 203.858 172.394 166.532 1.00 57.38  ? 1895 ALA A N     1 
ATOM   3554  C  CA    . ALA A 1 1895 ? 202.887 172.096 165.484 1.00 57.15  ? 1895 ALA A CA    1 
ATOM   3555  C  C     . ALA A 1 1895 ? 203.180 172.886 164.215 1.00 58.12  ? 1895 ALA A C     1 
ATOM   3556  O  O     . ALA A 1 1895 ? 203.085 172.352 163.105 1.00 65.82  ? 1895 ALA A O     1 
ATOM   3557  C  CB    . ALA A 1 1895 ? 201.474 172.391 165.981 1.00 54.30  ? 1895 ALA A CB    1 
ATOM   3558  N  N     . LEU A 1 1896 ? 203.528 174.165 164.363 1.00 50.12  ? 1896 LEU A N     1 
ATOM   3559  C  CA    . LEU A 1 1896 ? 203.797 175.009 163.204 1.00 49.23  ? 1896 LEU A CA    1 
ATOM   3560  C  C     . LEU A 1 1896 ? 205.025 174.531 162.442 1.00 57.23  ? 1896 LEU A C     1 
ATOM   3561  O  O     . LEU A 1 1896 ? 205.039 174.541 161.206 1.00 71.05  ? 1896 LEU A O     1 
ATOM   3562  C  CB    . LEU A 1 1896 ? 203.974 176.459 163.647 1.00 54.20  ? 1896 LEU A CB    1 
ATOM   3563  C  CG    . LEU A 1 1896 ? 202.700 177.206 164.040 1.00 53.11  ? 1896 LEU A CG    1 
ATOM   3564  C  CD1   . LEU A 1 1896 ? 202.951 178.698 164.032 1.00 58.27  ? 1896 LEU A CD1   1 
ATOM   3565  C  CD2   . LEU A 1 1896 ? 201.552 176.847 163.113 1.00 50.08  ? 1896 LEU A CD2   1 
ATOM   3566  N  N     . GLU A 1 1897 ? 206.072 174.122 163.162 1.00 61.45  ? 1897 GLU A N     1 
ATOM   3567  C  CA    . GLU A 1 1897 ? 207.266 173.615 162.496 1.00 65.19  ? 1897 GLU A CA    1 
ATOM   3568  C  C     . GLU A 1 1897 ? 206.966 172.356 161.696 1.00 74.07  ? 1897 GLU A C     1 
ATOM   3569  O  O     . GLU A 1 1897 ? 207.486 172.186 160.588 1.00 76.81  ? 1897 GLU A O     1 
ATOM   3570  C  CB    . GLU A 1 1897 ? 208.370 173.347 163.520 1.00 70.25  ? 1897 GLU A CB    1 
ATOM   3571  C  CG    . GLU A 1 1897 ? 209.730 173.008 162.916 1.00 77.39  ? 1897 GLU A CG    1 
ATOM   3572  C  CD    . GLU A 1 1897 ? 210.276 174.084 161.987 1.00 86.57  ? 1897 GLU A CD    1 
ATOM   3573  O  OE1   . GLU A 1 1897 ? 211.227 173.783 161.235 1.00 91.06  ? 1897 GLU A OE1   1 
ATOM   3574  O  OE2   . GLU A 1 1897 ? 209.789 175.234 162.025 1.00 83.24  ? 1897 GLU A OE2   1 
ATOM   3575  N  N     . ALA A 1 1898 ? 206.133 171.469 162.234 1.00 63.50  ? 1898 ALA A N     1 
ATOM   3576  C  CA    . ALA A 1 1898 ? 205.682 170.287 161.512 1.00 60.00  ? 1898 ALA A CA    1 
ATOM   3577  C  C     . ALA A 1 1898 ? 204.607 170.603 160.480 1.00 64.38  ? 1898 ALA A C     1 
ATOM   3578  O  O     . ALA A 1 1898 ? 204.041 169.674 159.894 1.00 68.83  ? 1898 ALA A O     1 
ATOM   3579  C  CB    . ALA A 1 1898 ? 205.162 169.236 162.496 1.00 59.72  ? 1898 ALA A CB    1 
ATOM   3580  N  N     . ARG A 1 1899 ? 204.322 171.887 160.252 1.00 71.92  ? 1899 ARG A N     1 
ATOM   3581  C  CA    . ARG A 1 1899 ? 203.319 172.327 159.282 1.00 65.17  ? 1899 ARG A CA    1 
ATOM   3582  C  C     . ARG A 1 1899 ? 201.953 171.712 159.570 1.00 64.63  ? 1899 ARG A C     1 
ATOM   3583  O  O     . ARG A 1 1899 ? 201.248 171.261 158.666 1.00 78.31  ? 1899 ARG A O     1 
ATOM   3584  C  CB    . ARG A 1 1899 ? 203.769 172.033 157.850 1.00 69.93  ? 1899 ARG A CB    1 
ATOM   3585  C  CG    . ARG A 1 1899 ? 204.928 172.909 157.401 1.00 70.25  ? 1899 ARG A CG    1 
ATOM   3586  C  CD    . ARG A 1 1899 ? 204.752 174.328 157.925 1.00 73.45  ? 1899 ARG A CD    1 
ATOM   3587  N  NE    . ARG A 1 1899 ? 205.452 175.322 157.123 1.00 77.94  ? 1899 ARG A NE    1 
ATOM   3588  C  CZ    . ARG A 1 1899 ? 206.756 175.550 157.183 1.00 79.78  ? 1899 ARG A CZ    1 
ATOM   3589  N  NH1   . ARG A 1 1899 ? 207.540 174.869 158.002 1.00 78.19  ? 1899 ARG A NH1   1 
ATOM   3590  N  NH2   . ARG A 1 1899 ? 207.288 176.487 156.403 1.00 81.67  ? 1899 ARG A NH2   1 
ATOM   3591  N  N     . LEU A 1 1900 ? 201.581 171.693 160.844 1.00 60.13  ? 1900 LEU A N     1 
ATOM   3592  C  CA    . LEU A 1 1900 ? 200.258 171.288 161.290 1.00 53.34  ? 1900 LEU A CA    1 
ATOM   3593  C  C     . LEU A 1 1900 ? 199.503 172.501 161.815 1.00 58.71  ? 1900 LEU A C     1 
ATOM   3594  O  O     . LEU A 1 1900 ? 199.979 173.638 161.758 1.00 66.24  ? 1900 LEU A O     1 
ATOM   3595  C  CB    . LEU A 1 1900 ? 200.352 170.210 162.376 1.00 47.21  ? 1900 LEU A CB    1 
ATOM   3596  C  CG    . LEU A 1 1900 ? 200.864 168.833 161.957 1.00 60.06  ? 1900 LEU A CG    1 
ATOM   3597  C  CD1   . LEU A 1 1900 ? 200.905 167.900 163.153 1.00 60.72  ? 1900 LEU A CD1   1 
ATOM   3598  C  CD2   . LEU A 1 1900 ? 199.995 168.252 160.857 1.00 60.78  ? 1900 LEU A CD2   1 
ATOM   3599  N  N     . GLY A 1 1901 ? 198.303 172.248 162.325 1.00 54.63  ? 1901 GLY A N     1 
ATOM   3600  C  CA    . GLY A 1 1901 ? 197.531 173.289 162.965 1.00 55.42  ? 1901 GLY A CA    1 
ATOM   3601  C  C     . GLY A 1 1901 ? 197.648 173.250 164.476 1.00 59.86  ? 1901 GLY A C     1 
ATOM   3602  O  O     . GLY A 1 1901 ? 198.365 172.435 165.052 1.00 71.67  ? 1901 GLY A O     1 
ATOM   3603  N  N     . GLY A 1 1902 ? 196.922 174.153 165.121 1.00 46.97  ? 1902 GLY A N     1 
ATOM   3604  C  CA    . GLY A 1 1902 ? 196.869 174.226 166.574 1.00 47.27  ? 1902 GLY A CA    1 
ATOM   3605  C  C     . GLY A 1 1902 ? 195.442 174.040 167.054 1.00 48.92  ? 1902 GLY A C     1 
ATOM   3606  O  O     . GLY A 1 1902 ? 194.519 174.677 166.541 1.00 62.15  ? 1902 GLY A O     1 
ATOM   3607  N  N     . SER A 1 1903 ? 195.266 173.165 168.041 1.00 34.09  ? 1903 SER A N     1 
ATOM   3608  C  CA    . SER A 1 1903 ? 193.943 172.840 168.573 1.00 32.80  ? 1903 SER A CA    1 
ATOM   3609  C  C     . SER A 1 1903 ? 193.946 172.920 170.091 1.00 46.51  ? 1903 SER A C     1 
ATOM   3610  O  O     . SER A 1 1903 ? 193.849 171.900 170.784 1.00 57.25  ? 1903 SER A O     1 
ATOM   3611  C  CB    . SER A 1 1903 ? 193.492 171.455 168.104 1.00 48.57  ? 1903 SER A CB    1 
ATOM   3612  O  OG    . SER A 1 1903 ? 192.263 171.090 168.705 1.00 54.35  ? 1903 SER A OG    1 
ATOM   3613  N  N     . PRO A 1 1904 ? 194.038 174.128 170.653 1.00 43.73  ? 1904 PRO A N     1 
ATOM   3614  C  CA    . PRO A 1 1904 ? 193.949 174.266 172.114 1.00 44.11  ? 1904 PRO A CA    1 
ATOM   3615  C  C     . PRO A 1 1904 ? 192.505 174.109 172.568 1.00 45.97  ? 1904 PRO A C     1 
ATOM   3616  O  O     . PRO A 1 1904 ? 191.641 174.914 172.214 1.00 61.07  ? 1904 PRO A O     1 
ATOM   3617  C  CB    . PRO A 1 1904 ? 194.472 175.684 172.369 1.00 44.28  ? 1904 PRO A CB    1 
ATOM   3618  C  CG    . PRO A 1 1904 ? 194.204 176.417 171.109 1.00 37.27  ? 1904 PRO A CG    1 
ATOM   3619  C  CD    . PRO A 1 1904 ? 194.273 175.422 169.987 1.00 38.27  ? 1904 PRO A CD    1 
ATOM   3620  N  N     . PHE A 1 1905 ? 192.242 173.068 173.351 1.00 44.26  ? 1905 PHE A N     1 
ATOM   3621  C  CA    . PHE A 1 1905 ? 190.899 172.771 173.820 1.00 48.57  ? 1905 PHE A CA    1 
ATOM   3622  C  C     . PHE A 1 1905 ? 190.832 172.891 175.336 1.00 60.30  ? 1905 PHE A C     1 
ATOM   3623  O  O     . PHE A 1 1905 ? 191.853 172.931 176.027 1.00 74.77  ? 1905 PHE A O     1 
ATOM   3624  C  CB    . PHE A 1 1905 ? 190.446 171.370 173.380 1.00 48.07  ? 1905 PHE A CB    1 
ATOM   3625  C  CG    . PHE A 1 1905 ? 191.234 170.248 173.997 1.00 53.57  ? 1905 PHE A CG    1 
ATOM   3626  C  CD1   . PHE A 1 1905 ? 192.380 169.771 173.386 1.00 58.66  ? 1905 PHE A CD1   1 
ATOM   3627  C  CD2   . PHE A 1 1905 ? 190.817 169.657 175.179 1.00 59.50  ? 1905 PHE A CD2   1 
ATOM   3628  C  CE1   . PHE A 1 1905 ? 193.103 168.738 173.948 1.00 58.29  ? 1905 PHE A CE1   1 
ATOM   3629  C  CE2   . PHE A 1 1905 ? 191.537 168.624 175.745 1.00 57.99  ? 1905 PHE A CE2   1 
ATOM   3630  C  CZ    . PHE A 1 1905 ? 192.680 168.164 175.128 1.00 58.52  ? 1905 PHE A CZ    1 
ATOM   3631  N  N     . GLY A 1 1906 ? 189.605 172.949 175.846 1.00 49.24  ? 1906 GLY A N     1 
ATOM   3632  C  CA    . GLY A 1 1906 ? 189.368 173.065 177.263 1.00 46.67  ? 1906 GLY A CA    1 
ATOM   3633  C  C     . GLY A 1 1906 ? 188.079 173.804 177.552 1.00 56.24  ? 1906 GLY A C     1 
ATOM   3634  O  O     . GLY A 1 1906 ? 187.327 174.163 176.641 1.00 66.39  ? 1906 GLY A O     1 
ATOM   3635  N  N     . PRO A 1 1907 ? 187.795 174.045 178.828 1.00 60.05  ? 1907 PRO A N     1 
ATOM   3636  C  CA    . PRO A 1 1907 ? 186.600 174.815 179.186 1.00 53.99  ? 1907 PRO A CA    1 
ATOM   3637  C  C     . PRO A 1 1907 ? 186.731 176.266 178.748 1.00 64.67  ? 1907 PRO A C     1 
ATOM   3638  O  O     . PRO A 1 1907 ? 187.780 176.722 178.289 1.00 74.88  ? 1907 PRO A O     1 
ATOM   3639  C  CB    . PRO A 1 1907 ? 186.533 174.688 180.709 1.00 55.73  ? 1907 PRO A CB    1 
ATOM   3640  C  CG    . PRO A 1 1907 ? 187.933 174.415 181.124 1.00 60.45  ? 1907 PRO A CG    1 
ATOM   3641  C  CD    . PRO A 1 1907 ? 188.554 173.616 180.014 1.00 65.74  ? 1907 PRO A CD    1 
ATOM   3642  N  N     . ALA A 1 1908 ? 185.629 176.994 178.887 1.00 69.15  ? 1908 ALA A N     1 
ATOM   3643  C  CA    . ALA A 1 1908 ? 185.595 178.384 178.464 1.00 68.80  ? 1908 ALA A CA    1 
ATOM   3644  C  C     . ALA A 1 1908 ? 186.414 179.263 179.405 1.00 72.61  ? 1908 ALA A C     1 
ATOM   3645  O  O     . ALA A 1 1908 ? 186.510 179.017 180.611 1.00 81.01  ? 1908 ALA A O     1 
ATOM   3646  C  CB    . ALA A 1 1908 ? 184.154 178.888 178.400 1.00 64.55  ? 1908 ALA A CB    1 
ATOM   3647  N  N     . GLY A 1 1909 ? 187.006 180.307 178.833 1.00 60.52  ? 1909 GLY A N     1 
ATOM   3648  C  CA    . GLY A 1 1909 ? 187.733 181.292 179.619 1.00 63.23  ? 1909 GLY A CA    1 
ATOM   3649  C  C     . GLY A 1 1909 ? 188.995 180.785 180.283 1.00 65.84  ? 1909 GLY A C     1 
ATOM   3650  O  O     . GLY A 1 1909 ? 189.235 181.083 181.459 1.00 77.67  ? 1909 GLY A O     1 
ATOM   3651  N  N     . THR A 1 1910 ? 189.811 180.022 179.556 1.00 59.56  ? 1910 THR A N     1 
ATOM   3652  C  CA    . THR A 1 1910 ? 191.099 179.558 180.058 1.00 58.51  ? 1910 THR A CA    1 
ATOM   3653  C  C     . THR A 1 1910 ? 192.255 180.091 179.217 1.00 57.51  ? 1910 THR A C     1 
ATOM   3654  O  O     . THR A 1 1910 ? 193.343 179.514 179.208 1.00 67.06  ? 1910 THR A O     1 
ATOM   3655  C  CB    . THR A 1 1910 ? 191.149 178.032 180.119 1.00 60.49  ? 1910 THR A CB    1 
ATOM   3656  O  OG1   . THR A 1 1910 ? 191.413 177.505 178.813 1.00 63.78  ? 1910 THR A OG1   1 
ATOM   3657  C  CG2   . THR A 1 1910 ? 189.838 177.473 180.638 1.00 62.10  ? 1910 THR A CG2   1 
ATOM   3658  N  N     . GLY A 1 1911 ? 192.033 181.196 178.509 1.00 53.71  ? 1911 GLY A N     1 
ATOM   3659  C  CA    . GLY A 1 1911 ? 193.082 181.811 177.720 1.00 52.45  ? 1911 GLY A CA    1 
ATOM   3660  C  C     . GLY A 1 1911 ? 193.546 180.983 176.542 1.00 64.16  ? 1911 GLY A C     1 
ATOM   3661  O  O     . GLY A 1 1911 ? 194.741 180.711 176.408 1.00 74.40  ? 1911 GLY A O     1 
ATOM   3662  N  N     . LYS A 1 1912 ? 192.613 180.556 175.692 1.00 53.64  ? 1912 LYS A N     1 
ATOM   3663  C  CA    . LYS A 1 1912 ? 192.958 179.794 174.495 1.00 47.20  ? 1912 LYS A CA    1 
ATOM   3664  C  C     . LYS A 1 1912 ? 193.064 180.695 173.265 1.00 48.72  ? 1912 LYS A C     1 
ATOM   3665  O  O     . LYS A 1 1912 ? 194.125 180.782 172.636 1.00 61.48  ? 1912 LYS A O     1 
ATOM   3666  C  CB    . LYS A 1 1912 ? 191.924 178.685 174.275 1.00 44.46  ? 1912 LYS A CB    1 
ATOM   3667  C  CG    . LYS A 1 1912 ? 191.384 178.100 175.571 1.00 55.04  ? 1912 LYS A CG    1 
ATOM   3668  C  CD    . LYS A 1 1912 ? 190.682 176.774 175.346 1.00 49.17  ? 1912 LYS A CD    1 
ATOM   3669  C  CE    . LYS A 1 1912 ? 189.590 176.901 174.304 1.00 52.68  ? 1912 LYS A CE    1 
ATOM   3670  N  NZ    . LYS A 1 1912 ? 188.575 177.912 174.701 1.00 53.74  ? 1912 LYS A NZ    1 
ATOM   3671  N  N     . THR A 1 1913 ? 191.970 181.378 172.921 1.00 51.60  ? 1913 THR A N     1 
ATOM   3672  C  CA    . THR A 1 1913 ? 191.995 182.294 171.786 1.00 49.18  ? 1913 THR A CA    1 
ATOM   3673  C  C     . THR A 1 1913 ? 192.968 183.439 172.029 1.00 53.17  ? 1913 THR A C     1 
ATOM   3674  O  O     . THR A 1 1913 ? 193.698 183.851 171.119 1.00 62.64  ? 1913 THR A O     1 
ATOM   3675  C  CB    . THR A 1 1913 ? 190.592 182.836 171.514 1.00 50.65  ? 1913 THR A CB    1 
ATOM   3676  O  OG1   . THR A 1 1913 ? 189.672 181.744 171.389 1.00 53.33  ? 1913 THR A OG1   1 
ATOM   3677  C  CG2   . THR A 1 1913 ? 190.577 183.650 170.233 1.00 54.83  ? 1913 THR A CG2   1 
ATOM   3678  N  N     . GLU A 1 1914 ? 192.993 183.966 173.254 1.00 64.14  ? 1914 GLU A N     1 
ATOM   3679  C  CA    . GLU A 1 1914 ? 193.950 185.016 173.579 1.00 54.41  ? 1914 GLU A CA    1 
ATOM   3680  C  C     . GLU A 1 1914 ? 195.380 184.501 173.512 1.00 57.98  ? 1914 GLU A C     1 
ATOM   3681  O  O     . GLU A 1 1914 ? 196.284 185.232 173.102 1.00 66.84  ? 1914 GLU A O     1 
ATOM   3682  C  CB    . GLU A 1 1914 ? 193.652 185.599 174.958 1.00 59.07  ? 1914 GLU A CB    1 
ATOM   3683  C  CG    . GLU A 1 1914 ? 192.359 186.387 175.019 1.00 72.01  ? 1914 GLU A CG    1 
ATOM   3684  C  CD    . GLU A 1 1914 ? 192.345 187.559 174.058 1.00 78.71  ? 1914 GLU A CD    1 
ATOM   3685  O  OE1   . GLU A 1 1914 ? 193.266 188.399 174.131 1.00 78.53  ? 1914 GLU A OE1   1 
ATOM   3686  O  OE2   . GLU A 1 1914 ? 191.411 187.642 173.234 1.00 76.87  ? 1914 GLU A OE2   1 
ATOM   3687  N  N     . SER A 1 1915 ? 195.610 183.248 173.911 1.00 40.22  ? 1915 SER A N     1 
ATOM   3688  C  CA    . SER A 1 1915 ? 196.951 182.684 173.793 1.00 41.62  ? 1915 SER A CA    1 
ATOM   3689  C  C     . SER A 1 1915 ? 197.377 182.578 172.335 1.00 55.14  ? 1915 SER A C     1 
ATOM   3690  O  O     . SER A 1 1915 ? 198.520 182.899 171.989 1.00 61.28  ? 1915 SER A O     1 
ATOM   3691  C  CB    . SER A 1 1915 ? 197.014 181.314 174.464 1.00 41.14  ? 1915 SER A CB    1 
ATOM   3692  O  OG    . SER A 1 1915 ? 196.940 181.435 175.873 1.00 44.40  ? 1915 SER A OG    1 
ATOM   3693  N  N     . VAL A 1 1916 ? 196.468 182.132 171.463 1.00 49.62  ? 1916 VAL A N     1 
ATOM   3694  C  CA    . VAL A 1 1916 ? 196.787 182.056 170.040 1.00 33.22  ? 1916 VAL A CA    1 
ATOM   3695  C  C     . VAL A 1 1916 ? 197.077 183.440 169.477 1.00 42.01  ? 1916 VAL A C     1 
ATOM   3696  O  O     . VAL A 1 1916 ? 198.050 183.629 168.734 1.00 53.55  ? 1916 VAL A O     1 
ATOM   3697  C  CB    . VAL A 1 1916 ? 195.644 181.365 169.272 1.00 32.03  ? 1916 VAL A CB    1 
ATOM   3698  C  CG1   . VAL A 1 1916 ? 195.846 181.512 167.775 1.00 35.59  ? 1916 VAL A CG1   1 
ATOM   3699  C  CG2   . VAL A 1 1916 ? 195.555 179.900 169.661 1.00 47.09  ? 1916 VAL A CG2   1 
ATOM   3700  N  N     . LYS A 1 1917 ? 196.252 184.431 169.826 1.00 54.45  ? 1917 LYS A N     1 
ATOM   3701  C  CA    . LYS A 1 1917 ? 196.476 185.787 169.336 1.00 42.49  ? 1917 LYS A CA    1 
ATOM   3702  C  C     . LYS A 1 1917 ? 197.787 186.359 169.859 1.00 48.35  ? 1917 LYS A C     1 
ATOM   3703  O  O     . LYS A 1 1917 ? 198.497 187.058 169.130 1.00 64.86  ? 1917 LYS A O     1 
ATOM   3704  C  CB    . LYS A 1 1917 ? 195.308 186.692 169.726 1.00 44.19  ? 1917 LYS A CB    1 
ATOM   3705  C  CG    . LYS A 1 1917 ? 194.045 186.463 168.921 1.00 51.43  ? 1917 LYS A CG    1 
ATOM   3706  C  CD    . LYS A 1 1917 ? 193.167 187.701 168.927 1.00 58.90  ? 1917 LYS A CD    1 
ATOM   3707  C  CE    . LYS A 1 1917 ? 192.836 188.137 170.342 1.00 61.67  ? 1917 LYS A CE    1 
ATOM   3708  N  NZ    . LYS A 1 1917 ? 192.139 189.450 170.366 1.00 60.25  ? 1917 LYS A NZ    1 
ATOM   3709  N  N     . ALA A 1 1918 ? 198.119 186.086 171.122 1.00 29.27  ? 1918 ALA A N     1 
ATOM   3710  C  CA    . ALA A 1 1918 ? 199.363 186.589 171.691 1.00 37.74  ? 1918 ALA A CA    1 
ATOM   3711  C  C     . ALA A 1 1918 ? 200.571 185.943 171.033 1.00 43.85  ? 1918 ALA A C     1 
ATOM   3712  O  O     . ALA A 1 1918 ? 201.586 186.608 170.807 1.00 59.72  ? 1918 ALA A O     1 
ATOM   3713  C  CB    . ALA A 1 1918 ? 199.386 186.354 173.199 1.00 51.26  ? 1918 ALA A CB    1 
ATOM   3714  N  N     . LEU A 1 1919 ? 200.492 184.645 170.734 1.00 48.88  ? 1919 LEU A N     1 
ATOM   3715  C  CA    . LEU A 1 1919 ? 201.577 184.005 169.999 1.00 46.23  ? 1919 LEU A CA    1 
ATOM   3716  C  C     . LEU A 1 1919 ? 201.718 184.600 168.605 1.00 46.50  ? 1919 LEU A C     1 
ATOM   3717  O  O     . LEU A 1 1919 ? 202.836 184.844 168.138 1.00 53.62  ? 1919 LEU A O     1 
ATOM   3718  C  CB    . LEU A 1 1919 ? 201.346 182.498 169.913 1.00 41.60  ? 1919 LEU A CB    1 
ATOM   3719  C  CG    . LEU A 1 1919 ? 202.278 181.746 168.961 1.00 36.70  ? 1919 LEU A CG    1 
ATOM   3720  C  CD1   . LEU A 1 1919 ? 203.736 181.935 169.350 1.00 42.01  ? 1919 LEU A CD1   1 
ATOM   3721  C  CD2   . LEU A 1 1919 ? 201.922 180.281 168.924 1.00 42.84  ? 1919 LEU A CD2   1 
ATOM   3722  N  N     . GLY A 1 1920 ? 200.595 184.843 167.926 1.00 55.92  ? 1920 GLY A N     1 
ATOM   3723  C  CA    . GLY A 1 1920 ? 200.662 185.458 166.611 1.00 49.45  ? 1920 GLY A CA    1 
ATOM   3724  C  C     . GLY A 1 1920 ? 201.270 186.846 166.646 1.00 54.31  ? 1920 GLY A C     1 
ATOM   3725  O  O     . GLY A 1 1920 ? 202.090 187.198 165.796 1.00 66.28  ? 1920 GLY A O     1 
ATOM   3726  N  N     . HIS A 1 1921 ? 200.877 187.653 167.633 1.00 52.47  ? 1921 HIS A N     1 
ATOM   3727  C  CA    . HIS A 1 1921 ? 201.459 188.981 167.790 1.00 53.85  ? 1921 HIS A CA    1 
ATOM   3728  C  C     . HIS A 1 1921 ? 202.928 188.906 168.182 1.00 60.64  ? 1921 HIS A C     1 
ATOM   3729  O  O     . HIS A 1 1921 ? 203.705 189.806 167.848 1.00 73.35  ? 1921 HIS A O     1 
ATOM   3730  C  CB    . HIS A 1 1921 ? 200.675 189.780 168.830 1.00 54.02  ? 1921 HIS A CB    1 
ATOM   3731  C  CG    . HIS A 1 1921 ? 199.235 189.986 168.476 1.00 62.65  ? 1921 HIS A CG    1 
ATOM   3732  N  ND1   . HIS A 1 1921 ? 198.758 189.847 167.191 1.00 69.94  ? 1921 HIS A ND1   1 
ATOM   3733  C  CD2   . HIS A 1 1921 ? 198.168 190.321 169.239 1.00 60.99  ? 1921 HIS A CD2   1 
ATOM   3734  C  CE1   . HIS A 1 1921 ? 197.460 190.089 167.177 1.00 67.31  ? 1921 HIS A CE1   1 
ATOM   3735  N  NE2   . HIS A 1 1921 ? 197.077 190.378 168.407 1.00 66.85  ? 1921 HIS A NE2   1 
ATOM   3736  N  N     . GLN A 1 1922 ? 203.321 187.849 168.894 1.00 56.52  ? 1922 GLN A N     1 
ATOM   3737  C  CA    . GLN A 1 1922 ? 204.717 187.690 169.281 1.00 54.35  ? 1922 GLN A CA    1 
ATOM   3738  C  C     . GLN A 1 1922 ? 205.606 187.485 168.064 1.00 51.97  ? 1922 GLN A C     1 
ATOM   3739  O  O     . GLN A 1 1922 ? 206.744 187.966 168.037 1.00 60.08  ? 1922 GLN A O     1 
ATOM   3740  C  CB    . GLN A 1 1922 ? 204.861 186.517 170.250 1.00 55.38  ? 1922 GLN A CB    1 
ATOM   3741  C  CG    . GLN A 1 1922 ? 206.249 186.357 170.841 1.00 47.02  ? 1922 GLN A CG    1 
ATOM   3742  C  CD    . GLN A 1 1922 ? 206.834 187.668 171.324 1.00 63.17  ? 1922 GLN A CD    1 
ATOM   3743  O  OE1   . GLN A 1 1922 ? 206.608 188.077 172.463 1.00 70.76  ? 1922 GLN A OE1   1 
ATOM   3744  N  NE2   . GLN A 1 1922 ? 207.599 188.332 170.465 1.00 63.69  ? 1922 GLN A NE2   1 
ATOM   3745  N  N     . LEU A 1 1923 ? 205.108 186.775 167.057 1.00 54.22  ? 1923 LEU A N     1 
ATOM   3746  C  CA    . LEU A 1 1923 ? 205.816 186.579 165.801 1.00 50.64  ? 1923 LEU A CA    1 
ATOM   3747  C  C     . LEU A 1 1923 ? 205.495 187.657 164.775 1.00 60.03  ? 1923 LEU A C     1 
ATOM   3748  O  O     . LEU A 1 1923 ? 205.954 187.563 163.633 1.00 65.13  ? 1923 LEU A O     1 
ATOM   3749  C  CB    . LEU A 1 1923 ? 205.486 185.202 165.218 1.00 43.69  ? 1923 LEU A CB    1 
ATOM   3750  C  CG    . LEU A 1 1923 ? 205.678 184.002 166.147 1.00 47.08  ? 1923 LEU A CG    1 
ATOM   3751  C  CD1   . LEU A 1 1923 ? 205.293 182.715 165.439 1.00 55.91  ? 1923 LEU A CD1   1 
ATOM   3752  C  CD2   . LEU A 1 1923 ? 207.108 183.932 166.649 1.00 53.06  ? 1923 LEU A CD2   1 
ATOM   3753  N  N     . GLY A 1 1924 ? 204.719 188.668 165.151 1.00 64.76  ? 1924 GLY A N     1 
ATOM   3754  C  CA    . GLY A 1 1924 ? 204.364 189.737 164.236 1.00 62.16  ? 1924 GLY A CA    1 
ATOM   3755  C  C     . GLY A 1 1924 ? 203.476 189.305 163.090 1.00 58.53  ? 1924 GLY A C     1 
ATOM   3756  O  O     . GLY A 1 1924 ? 203.647 189.787 161.964 1.00 67.84  ? 1924 GLY A O     1 
ATOM   3757  N  N     . ARG A 1 1925 ? 202.524 188.416 163.350 1.00 59.00  ? 1925 ARG A N     1 
ATOM   3758  C  CA    . ARG A 1 1925 ? 201.623 187.910 162.329 1.00 55.58  ? 1925 ARG A CA    1 
ATOM   3759  C  C     . ARG A 1 1925 ? 200.253 188.561 162.458 1.00 61.54  ? 1925 ARG A C     1 
ATOM   3760  O  O     . ARG A 1 1925 ? 199.916 189.166 163.479 1.00 75.13  ? 1925 ARG A O     1 
ATOM   3761  C  CB    . ARG A 1 1925 ? 201.480 186.388 162.425 1.00 58.56  ? 1925 ARG A CB    1 
ATOM   3762  C  CG    . ARG A 1 1925 ? 202.780 185.625 162.273 1.00 65.78  ? 1925 ARG A CG    1 
ATOM   3763  C  CD    . ARG A 1 1925 ? 203.201 185.535 160.819 1.00 63.30  ? 1925 ARG A CD    1 
ATOM   3764  N  NE    . ARG A 1 1925 ? 204.111 184.421 160.587 1.00 66.33  ? 1925 ARG A NE    1 
ATOM   3765  C  CZ    . ARG A 1 1925 ? 205.406 184.437 160.871 1.00 70.23  ? 1925 ARG A CZ    1 
ATOM   3766  N  NH1   . ARG A 1 1925 ? 205.984 185.501 161.403 1.00 69.22  ? 1925 ARG A NH1   1 
ATOM   3767  N  NH2   . ARG A 1 1925 ? 206.140 183.358 160.616 1.00 68.10  ? 1925 ARG A NH2   1 
ATOM   3768  N  N     . PHE A 1 1926 ? 199.463 188.427 161.398 1.00 63.00  ? 1926 PHE A N     1 
ATOM   3769  C  CA    . PHE A 1 1926 ? 198.088 188.911 161.376 1.00 63.03  ? 1926 PHE A CA    1 
ATOM   3770  C  C     . PHE A 1 1926 ? 197.178 187.764 161.800 1.00 66.07  ? 1926 PHE A C     1 
ATOM   3771  O  O     . PHE A 1 1926 ? 197.014 186.787 161.063 1.00 72.99  ? 1926 PHE A O     1 
ATOM   3772  C  CB    . PHE A 1 1926 ? 197.727 189.428 159.985 1.00 64.27  ? 1926 PHE A CB    1 
ATOM   3773  C  CG    . PHE A 1 1926 ? 196.418 190.166 159.924 1.00 68.20  ? 1926 PHE A CG    1 
ATOM   3774  C  CD1   . PHE A 1 1926 ? 195.805 190.626 161.078 1.00 69.33  ? 1926 PHE A CD1   1 
ATOM   3775  C  CD2   . PHE A 1 1926 ? 195.805 190.405 158.706 1.00 67.65  ? 1926 PHE A CD2   1 
ATOM   3776  C  CE1   . PHE A 1 1926 ? 194.602 191.302 161.016 1.00 68.91  ? 1926 PHE A CE1   1 
ATOM   3777  C  CE2   . PHE A 1 1926 ? 194.604 191.083 158.639 1.00 68.33  ? 1926 PHE A CE2   1 
ATOM   3778  C  CZ    . PHE A 1 1926 ? 194.002 191.532 159.796 1.00 70.48  ? 1926 PHE A CZ    1 
ATOM   3779  N  N     . VAL A 1 1927 ? 196.595 187.875 162.989 1.00 43.12  ? 1927 VAL A N     1 
ATOM   3780  C  CA    . VAL A 1 1927 ? 195.732 186.837 163.539 1.00 42.22  ? 1927 VAL A CA    1 
ATOM   3781  C  C     . VAL A 1 1927 ? 194.284 187.255 163.329 1.00 54.55  ? 1927 VAL A C     1 
ATOM   3782  O  O     . VAL A 1 1927 ? 193.877 188.346 163.744 1.00 63.96  ? 1927 VAL A O     1 
ATOM   3783  C  CB    . VAL A 1 1927 ? 196.025 186.594 165.026 1.00 45.36  ? 1927 VAL A CB    1 
ATOM   3784  C  CG1   . VAL A 1 1927 ? 195.174 185.451 165.547 1.00 60.65  ? 1927 VAL A CG1   1 
ATOM   3785  C  CG2   . VAL A 1 1927 ? 197.495 186.299 165.226 1.00 46.22  ? 1927 VAL A CG2   1 
ATOM   3786  N  N     . LEU A 1 1928 ? 193.508 186.388 162.688 1.00 50.34  ? 1928 LEU A N     1 
ATOM   3787  C  CA    . LEU A 1 1928 ? 192.098 186.636 162.427 1.00 46.63  ? 1928 LEU A CA    1 
ATOM   3788  C  C     . LEU A 1 1928 ? 191.256 185.667 163.245 1.00 58.92  ? 1928 LEU A C     1 
ATOM   3789  O  O     . LEU A 1 1928 ? 191.491 184.455 163.215 1.00 68.89  ? 1928 LEU A O     1 
ATOM   3790  C  CB    . LEU A 1 1928 ? 191.781 186.485 160.939 1.00 42.00  ? 1928 LEU A CB    1 
ATOM   3791  C  CG    . LEU A 1 1928 ? 192.080 187.689 160.045 1.00 43.52  ? 1928 LEU A CG    1 
ATOM   3792  C  CD1   . LEU A 1 1928 ? 193.566 187.800 159.765 1.00 50.50  ? 1928 LEU A CD1   1 
ATOM   3793  C  CD2   . LEU A 1 1928 ? 191.297 187.596 158.750 1.00 50.70  ? 1928 LEU A CD2   1 
ATOM   3794  N  N     . VAL A 1 1929 ? 190.278 186.201 163.968 1.00 56.33  ? 1929 VAL A N     1 
ATOM   3795  C  CA    . VAL A 1 1929 ? 189.398 185.405 164.814 1.00 59.15  ? 1929 VAL A CA    1 
ATOM   3796  C  C     . VAL A 1 1929 ? 188.063 185.238 164.105 1.00 63.68  ? 1929 VAL A C     1 
ATOM   3797  O  O     . VAL A 1 1929 ? 187.354 186.222 163.859 1.00 74.05  ? 1929 VAL A O     1 
ATOM   3798  C  CB    . VAL A 1 1929 ? 189.209 186.059 166.192 1.00 60.45  ? 1929 VAL A CB    1 
ATOM   3799  C  CG1   . VAL A 1 1929 ? 188.226 185.258 167.028 1.00 54.95  ? 1929 VAL A CG1   1 
ATOM   3800  C  CG2   . VAL A 1 1929 ? 190.544 186.185 166.902 1.00 61.54  ? 1929 VAL A CG2   1 
ATOM   3801  N  N     . PHE A 1 1930 ? 187.719 183.996 163.776 1.00 53.50  ? 1930 PHE A N     1 
ATOM   3802  C  CA    . PHE A 1 1930 ? 186.463 183.674 163.115 1.00 56.81  ? 1930 PHE A CA    1 
ATOM   3803  C  C     . PHE A 1 1930 ? 185.574 182.902 164.076 1.00 60.07  ? 1930 PHE A C     1 
ATOM   3804  O  O     . PHE A 1 1930 ? 185.900 181.774 164.456 1.00 68.73  ? 1930 PHE A O     1 
ATOM   3805  C  CB    . PHE A 1 1930 ? 186.697 182.854 161.845 1.00 59.00  ? 1930 PHE A CB    1 
ATOM   3806  C  CG    . PHE A 1 1930 ? 187.474 183.580 160.789 1.00 58.40  ? 1930 PHE A CG    1 
ATOM   3807  C  CD1   . PHE A 1 1930 ? 186.844 184.464 159.932 1.00 63.44  ? 1930 PHE A CD1   1 
ATOM   3808  C  CD2   . PHE A 1 1930 ? 188.833 183.370 160.645 1.00 56.91  ? 1930 PHE A CD2   1 
ATOM   3809  C  CE1   . PHE A 1 1930 ? 187.555 185.130 158.958 1.00 63.29  ? 1930 PHE A CE1   1 
ATOM   3810  C  CE2   . PHE A 1 1930 ? 189.549 184.032 159.671 1.00 57.54  ? 1930 PHE A CE2   1 
ATOM   3811  C  CZ    . PHE A 1 1930 ? 188.909 184.913 158.827 1.00 62.85  ? 1930 PHE A CZ    1 
ATOM   3812  N  N     . ASN A 1 1931 ? 184.451 183.504 164.457 1.00 63.24  ? 1931 ASN A N     1 
ATOM   3813  C  CA    . ASN A 1 1931 ? 183.495 182.860 165.355 1.00 62.27  ? 1931 ASN A CA    1 
ATOM   3814  C  C     . ASN A 1 1931 ? 182.685 181.867 164.533 1.00 68.15  ? 1931 ASN A C     1 
ATOM   3815  O  O     . ASN A 1 1931 ? 181.632 182.205 163.988 1.00 75.41  ? 1931 ASN A O     1 
ATOM   3816  C  CB    . ASN A 1 1931 ? 182.604 183.891 166.035 1.00 70.00  ? 1931 ASN A CB    1 
ATOM   3817  C  CG    . ASN A 1 1931 ? 181.913 183.338 167.262 1.00 73.08  ? 1931 ASN A CG    1 
ATOM   3818  O  OD1   . ASN A 1 1931 ? 182.264 183.679 168.390 1.00 79.75  ? 1931 ASN A OD1   1 
ATOM   3819  N  ND2   . ASN A 1 1931 ? 180.928 182.474 167.050 1.00 67.93  ? 1931 ASN A ND2   1 
ATOM   3820  N  N     . CYS A 1 1932 ? 183.181 180.638 164.446 1.00 70.17  ? 1932 CYS A N     1 
ATOM   3821  C  CA    . CYS A 1 1932 ? 182.548 179.625 163.618 1.00 67.90  ? 1932 CYS A CA    1 
ATOM   3822  C  C     . CYS A 1 1932 ? 181.187 179.226 164.177 1.00 71.38  ? 1932 CYS A C     1 
ATOM   3823  O  O     . CYS A 1 1932 ? 180.932 179.303 165.382 1.00 80.82  ? 1932 CYS A O     1 
ATOM   3824  C  CB    . CYS A 1 1932 ? 183.447 178.396 163.506 1.00 66.29  ? 1932 CYS A CB    1 
ATOM   3825  S  SG    . CYS A 1 1932 ? 184.912 178.644 162.483 1.00 87.89  ? 1932 CYS A SG    1 
ATOM   3826  N  N     . ASP A 1 1933 ? 180.307 178.800 163.276 1.00 72.01  ? 1933 ASP A N     1 
ATOM   3827  C  CA    . ASP A 1 1933 ? 178.976 178.321 163.625 1.00 77.48  ? 1933 ASP A CA    1 
ATOM   3828  C  C     . ASP A 1 1933 ? 178.565 177.261 162.606 1.00 82.26  ? 1933 ASP A C     1 
ATOM   3829  O  O     . ASP A 1 1933 ? 179.397 176.741 161.857 1.00 90.72  ? 1933 ASP A O     1 
ATOM   3830  C  CB    . ASP A 1 1933 ? 177.993 179.496 163.742 1.00 83.64  ? 1933 ASP A CB    1 
ATOM   3831  C  CG    . ASP A 1 1933 ? 177.573 180.068 162.394 1.00 87.83  ? 1933 ASP A CG    1 
ATOM   3832  O  OD1   . ASP A 1 1933 ? 178.009 179.562 161.342 1.00 81.50  ? 1933 ASP A OD1   1 
ATOM   3833  O  OD2   . ASP A 1 1933 ? 176.777 181.029 162.387 1.00 85.30  ? 1933 ASP A OD2   1 
ATOM   3834  N  N     . GLU A 1 1934 ? 177.270 176.943 162.570 1.00 74.85  ? 1934 GLU A N     1 
ATOM   3835  C  CA    . GLU A 1 1934 ? 176.812 175.855 161.714 1.00 78.22  ? 1934 GLU A CA    1 
ATOM   3836  C  C     . GLU A 1 1934 ? 176.641 176.268 160.257 1.00 77.07  ? 1934 GLU A C     1 
ATOM   3837  O  O     . GLU A 1 1934 ? 176.534 175.390 159.395 1.00 78.37  ? 1934 GLU A O     1 
ATOM   3838  C  CB    . GLU A 1 1934 ? 175.501 175.278 162.247 1.00 75.15  ? 1934 GLU A CB    1 
ATOM   3839  C  CG    . GLU A 1 1934 ? 174.265 176.055 161.845 1.00 80.79  ? 1934 GLU A CG    1 
ATOM   3840  C  CD    . GLU A 1 1934 ? 173.787 176.989 162.935 1.00 84.41  ? 1934 GLU A CD    1 
ATOM   3841  O  OE1   . GLU A 1 1934 ? 174.306 176.899 164.068 1.00 82.44  ? 1934 GLU A OE1   1 
ATOM   3842  O  OE2   . GLU A 1 1934 ? 172.889 177.811 162.661 1.00 85.34  ? 1934 GLU A OE2   1 
ATOM   3843  N  N     . THR A 1 1935 ? 176.611 177.565 159.950 1.00 72.36  ? 1935 THR A N     1 
ATOM   3844  C  CA    . THR A 1 1935 ? 176.467 177.991 158.562 1.00 75.98  ? 1935 THR A CA    1 
ATOM   3845  C  C     . THR A 1 1935 ? 177.804 178.252 157.879 1.00 76.97  ? 1935 THR A C     1 
ATOM   3846  O  O     . THR A 1 1935 ? 177.816 178.663 156.715 1.00 79.20  ? 1935 THR A O     1 
ATOM   3847  C  CB    . THR A 1 1935 ? 175.580 179.239 158.453 1.00 75.24  ? 1935 THR A CB    1 
ATOM   3848  O  OG1   . THR A 1 1935 ? 175.331 179.522 157.071 1.00 70.15  ? 1935 THR A OG1   1 
ATOM   3849  C  CG2   . THR A 1 1935 ? 176.254 180.445 159.065 1.00 76.70  ? 1935 THR A CG2   1 
ATOM   3850  N  N     . PHE A 1 1936 ? 178.923 178.028 158.569 1.00 74.23  ? 1936 PHE A N     1 
ATOM   3851  C  CA    . PHE A 1 1936 ? 180.243 178.055 157.937 1.00 76.76  ? 1936 PHE A CA    1 
ATOM   3852  C  C     . PHE A 1 1936 ? 180.402 176.760 157.146 1.00 79.45  ? 1936 PHE A C     1 
ATOM   3853  O  O     . PHE A 1 1936 ? 181.004 175.781 157.595 1.00 82.89  ? 1936 PHE A O     1 
ATOM   3854  C  CB    . PHE A 1 1936 ? 181.346 178.211 158.976 1.00 76.56  ? 1936 PHE A CB    1 
ATOM   3855  C  CG    . PHE A 1 1936 ? 181.637 179.634 159.353 1.00 77.85  ? 1936 PHE A CG    1 
ATOM   3856  C  CD1   . PHE A 1 1936 ? 180.681 180.410 159.982 1.00 79.49  ? 1936 PHE A CD1   1 
ATOM   3857  C  CD2   . PHE A 1 1936 ? 182.876 180.191 159.089 1.00 73.58  ? 1936 PHE A CD2   1 
ATOM   3858  C  CE1   . PHE A 1 1936 ? 180.952 181.716 160.335 1.00 75.04  ? 1936 PHE A CE1   1 
ATOM   3859  C  CE2   . PHE A 1 1936 ? 183.153 181.497 159.439 1.00 68.67  ? 1936 PHE A CE2   1 
ATOM   3860  C  CZ    . PHE A 1 1936 ? 182.190 182.260 160.063 1.00 73.91  ? 1936 PHE A CZ    1 
ATOM   3861  N  N     . ASP A 1 1937 ? 179.844 176.760 155.941 1.00 77.88  ? 1937 ASP A N     1 
ATOM   3862  C  CA    . ASP A 1 1937 ? 179.811 175.560 155.118 1.00 75.40  ? 1937 ASP A CA    1 
ATOM   3863  C  C     . ASP A 1 1937 ? 181.156 175.367 154.419 1.00 78.06  ? 1937 ASP A C     1 
ATOM   3864  O  O     . ASP A 1 1937 ? 182.155 176.020 154.735 1.00 83.77  ? 1937 ASP A O     1 
ATOM   3865  C  CB    . ASP A 1 1937 ? 178.656 175.631 154.124 1.00 77.67  ? 1937 ASP A CB    1 
ATOM   3866  C  CG    . ASP A 1 1937 ? 178.604 176.949 153.383 1.00 87.80  ? 1937 ASP A CG    1 
ATOM   3867  O  OD1   . ASP A 1 1937 ? 179.492 177.796 153.611 1.00 91.15  ? 1937 ASP A OD1   1 
ATOM   3868  O  OD2   . ASP A 1 1937 ? 177.675 177.140 152.570 1.00 89.58  ? 1937 ASP A OD2   1 
ATOM   3869  N  N     . PHE A 1 1938 ? 181.188 174.441 153.460 1.00 67.90  ? 1938 PHE A N     1 
ATOM   3870  C  CA    . PHE A 1 1938 ? 182.422 174.139 152.743 1.00 65.82  ? 1938 PHE A CA    1 
ATOM   3871  C  C     . PHE A 1 1938 ? 182.906 175.337 151.933 1.00 73.23  ? 1938 PHE A C     1 
ATOM   3872  O  O     . PHE A 1 1938 ? 184.103 175.643 151.919 1.00 77.34  ? 1938 PHE A O     1 
ATOM   3873  C  CB    . PHE A 1 1938 ? 182.199 172.925 151.841 1.00 65.38  ? 1938 PHE A CB    1 
ATOM   3874  C  CG    . PHE A 1 1938 ? 183.390 172.547 151.009 1.00 66.52  ? 1938 PHE A CG    1 
ATOM   3875  C  CD1   . PHE A 1 1938 ? 184.449 171.855 151.567 1.00 69.89  ? 1938 PHE A CD1   1 
ATOM   3876  C  CD2   . PHE A 1 1938 ? 183.442 172.868 149.664 1.00 70.92  ? 1938 PHE A CD2   1 
ATOM   3877  C  CE1   . PHE A 1 1938 ? 185.539 171.495 150.802 1.00 69.07  ? 1938 PHE A CE1   1 
ATOM   3878  C  CE2   . PHE A 1 1938 ? 184.532 172.514 148.895 1.00 72.47  ? 1938 PHE A CE2   1 
ATOM   3879  C  CZ    . PHE A 1 1938 ? 185.583 171.828 149.466 1.00 70.34  ? 1938 PHE A CZ    1 
ATOM   3880  N  N     . GLN A 1 1939 ? 181.988 176.034 151.260 1.00 76.34  ? 1939 GLN A N     1 
ATOM   3881  C  CA    . GLN A 1 1939 ? 182.387 177.106 150.351 1.00 71.94  ? 1939 GLN A CA    1 
ATOM   3882  C  C     . GLN A 1 1939 ? 182.900 178.327 151.106 1.00 74.45  ? 1939 GLN A C     1 
ATOM   3883  O  O     . GLN A 1 1939 ? 183.908 178.928 150.713 1.00 84.51  ? 1939 GLN A O     1 
ATOM   3884  C  CB    . GLN A 1 1939 ? 181.214 177.488 149.452 1.00 75.55  ? 1939 GLN A CB    1 
ATOM   3885  C  CG    . GLN A 1 1939 ? 180.651 176.327 148.658 1.00 81.14  ? 1939 GLN A CG    1 
ATOM   3886  C  CD    . GLN A 1 1939 ? 181.165 176.304 147.236 1.00 85.70  ? 1939 GLN A CD    1 
ATOM   3887  O  OE1   . GLN A 1 1939 ? 181.737 177.282 146.757 1.00 84.88  ? 1939 GLN A OE1   1 
ATOM   3888  N  NE2   . GLN A 1 1939 ? 180.971 175.182 146.553 1.00 82.30  ? 1939 GLN A NE2   1 
ATOM   3889  N  N     . ALA A 1 1940 ? 182.209 178.723 152.176 1.00 63.52  ? 1940 ALA A N     1 
ATOM   3890  C  CA    . ALA A 1 1940 ? 182.646 179.884 152.943 1.00 62.32  ? 1940 ALA A CA    1 
ATOM   3891  C  C     . ALA A 1 1940 ? 184.011 179.643 153.573 1.00 71.56  ? 1940 ALA A C     1 
ATOM   3892  O  O     . ALA A 1 1940 ? 184.879 180.526 153.555 1.00 78.29  ? 1940 ALA A O     1 
ATOM   3893  C  CB    . ALA A 1 1940 ? 181.610 180.228 154.010 1.00 66.09  ? 1940 ALA A CB    1 
ATOM   3894  N  N     . MET A 1 1941 ? 184.225 178.449 154.125 1.00 67.17  ? 1941 MET A N     1 
ATOM   3895  C  CA    . MET A 1 1941 ? 185.529 178.134 154.694 1.00 60.92  ? 1941 MET A CA    1 
ATOM   3896  C  C     . MET A 1 1941 ? 186.595 178.038 153.614 1.00 59.86  ? 1941 MET A C     1 
ATOM   3897  O  O     . MET A 1 1941 ? 187.749 178.408 153.846 1.00 64.18  ? 1941 MET A O     1 
ATOM   3898  C  CB    . MET A 1 1941 ? 185.460 176.844 155.504 1.00 57.38  ? 1941 MET A CB    1 
ATOM   3899  C  CG    . MET A 1 1941 ? 184.855 177.037 156.878 1.00 61.92  ? 1941 MET A CG    1 
ATOM   3900  S  SD    . MET A 1 1941 ? 186.086 177.588 158.070 1.00 75.19  ? 1941 MET A SD    1 
ATOM   3901  C  CE    . MET A 1 1941 ? 186.403 176.061 158.939 1.00 74.83  ? 1941 MET A CE    1 
ATOM   3902  N  N     . GLY A 1 1942 ? 186.237 177.545 152.428 1.00 69.78  ? 1942 GLY A N     1 
ATOM   3903  C  CA    . GLY A 1 1942 ? 187.192 177.549 151.332 1.00 71.01  ? 1942 GLY A CA    1 
ATOM   3904  C  C     . GLY A 1 1942 ? 187.622 178.952 150.953 1.00 69.60  ? 1942 GLY A C     1 
ATOM   3905  O  O     . GLY A 1 1942 ? 188.806 179.209 150.720 1.00 78.15  ? 1942 GLY A O     1 
ATOM   3906  N  N     . ARG A 1 1943 ? 186.669 179.883 150.904 1.00 73.66  ? 1943 ARG A N     1 
ATOM   3907  C  CA    . ARG A 1 1943 ? 187.004 181.269 150.596 1.00 71.26  ? 1943 ARG A CA    1 
ATOM   3908  C  C     . ARG A 1 1943 ? 187.854 181.895 151.698 1.00 75.03  ? 1943 ARG A C     1 
ATOM   3909  O  O     . ARG A 1 1943 ? 188.799 182.643 151.414 1.00 80.08  ? 1943 ARG A O     1 
ATOM   3910  C  CB    . ARG A 1 1943 ? 185.727 182.075 150.372 1.00 75.75  ? 1943 ARG A CB    1 
ATOM   3911  C  CG    . ARG A 1 1943 ? 185.954 183.446 149.773 1.00 81.15  ? 1943 ARG A CG    1 
ATOM   3912  C  CD    . ARG A 1 1943 ? 184.634 184.116 149.444 1.00 80.14  ? 1943 ARG A CD    1 
ATOM   3913  N  NE    . ARG A 1 1943 ? 184.795 185.542 149.194 1.00 84.00  ? 1943 ARG A NE    1 
ATOM   3914  C  CZ    . ARG A 1 1943 ? 184.838 186.469 150.141 1.00 82.39  ? 1943 ARG A CZ    1 
ATOM   3915  N  NH1   . ARG A 1 1943 ? 184.742 186.152 151.422 1.00 82.58  ? 1943 ARG A NH1   1 
ATOM   3916  N  NH2   . ARG A 1 1943 ? 184.982 187.744 149.795 1.00 84.45  ? 1943 ARG A NH2   1 
ATOM   3917  N  N     . ILE A 1 1944 ? 187.537 181.598 152.961 1.00 68.32  ? 1944 ILE A N     1 
ATOM   3918  C  CA    . ILE A 1 1944 ? 188.340 182.113 154.069 1.00 65.25  ? 1944 ILE A CA    1 
ATOM   3919  C  C     . ILE A 1 1944 ? 189.762 181.568 153.995 1.00 63.29  ? 1944 ILE A C     1 
ATOM   3920  O  O     . ILE A 1 1944 ? 190.737 182.296 154.223 1.00 70.13  ? 1944 ILE A O     1 
ATOM   3921  C  CB    . ILE A 1 1944 ? 187.672 181.779 155.415 1.00 53.20  ? 1944 ILE A CB    1 
ATOM   3922  C  CG1   . ILE A 1 1944 ? 186.395 182.602 155.593 1.00 60.14  ? 1944 ILE A CG1   1 
ATOM   3923  C  CG2   . ILE A 1 1944 ? 188.629 182.028 156.568 1.00 49.34  ? 1944 ILE A CG2   1 
ATOM   3924  C  CD1   . ILE A 1 1944 ? 185.555 182.178 156.774 1.00 62.38  ? 1944 ILE A CD1   1 
ATOM   3925  N  N     . PHE A 1 1945 ? 189.901 180.279 153.680 1.00 61.79  ? 1945 PHE A N     1 
ATOM   3926  C  CA    . PHE A 1 1945 ? 191.223 179.682 153.534 1.00 56.64  ? 1945 PHE A CA    1 
ATOM   3927  C  C     . PHE A 1 1945 ? 191.985 180.306 152.373 1.00 53.11  ? 1945 PHE A C     1 
ATOM   3928  O  O     . PHE A 1 1945 ? 193.199 180.506 152.460 1.00 56.68  ? 1945 PHE A O     1 
ATOM   3929  C  CB    . PHE A 1 1945 ? 191.097 178.172 153.346 1.00 52.14  ? 1945 PHE A CB    1 
ATOM   3930  C  CG    . PHE A 1 1945 ? 190.850 177.422 154.622 1.00 51.82  ? 1945 PHE A CG    1 
ATOM   3931  C  CD1   . PHE A 1 1945 ? 191.294 177.923 155.831 1.00 54.71  ? 1945 PHE A CD1   1 
ATOM   3932  C  CD2   . PHE A 1 1945 ? 190.163 176.222 154.612 1.00 62.33  ? 1945 PHE A CD2   1 
ATOM   3933  C  CE1   . PHE A 1 1945 ? 191.065 177.236 157.005 1.00 61.01  ? 1945 PHE A CE1   1 
ATOM   3934  C  CE2   . PHE A 1 1945 ? 189.931 175.532 155.783 1.00 56.70  ? 1945 PHE A CE2   1 
ATOM   3935  C  CZ    . PHE A 1 1945 ? 190.381 176.039 156.980 1.00 55.23  ? 1945 PHE A CZ    1 
ATOM   3936  N  N     . VAL A 1 1946 ? 191.293 180.609 151.273 1.00 69.77  ? 1946 VAL A N     1 
ATOM   3937  C  CA    . VAL A 1 1946 ? 191.939 181.287 150.151 1.00 68.47  ? 1946 VAL A CA    1 
ATOM   3938  C  C     . VAL A 1 1946 ? 192.459 182.650 150.589 1.00 68.47  ? 1946 VAL A C     1 
ATOM   3939  O  O     . VAL A 1 1946 ? 193.589 183.043 150.265 1.00 77.86  ? 1946 VAL A O     1 
ATOM   3940  C  CB    . VAL A 1 1946 ? 190.965 181.415 148.966 1.00 69.20  ? 1946 VAL A CB    1 
ATOM   3941  C  CG1   . VAL A 1 1946 ? 191.476 182.435 147.964 1.00 67.43  ? 1946 VAL A CG1   1 
ATOM   3942  C  CG2   . VAL A 1 1946 ? 190.767 180.073 148.297 1.00 73.01  ? 1946 VAL A CG2   1 
ATOM   3943  N  N     . GLY A 1 1947 ? 191.635 183.393 151.329 1.00 61.68  ? 1947 GLY A N     1 
ATOM   3944  C  CA    . GLY A 1 1947 ? 192.067 184.693 151.817 1.00 64.66  ? 1947 GLY A CA    1 
ATOM   3945  C  C     . GLY A 1 1947 ? 193.279 184.596 152.723 1.00 65.11  ? 1947 GLY A C     1 
ATOM   3946  O  O     . GLY A 1 1947 ? 194.224 185.379 152.605 1.00 66.68  ? 1947 GLY A O     1 
ATOM   3947  N  N     . LEU A 1 1948 ? 193.269 183.624 153.638 1.00 67.01  ? 1948 LEU A N     1 
ATOM   3948  C  CA    . LEU A 1 1948 ? 194.407 183.440 154.534 1.00 62.89  ? 1948 LEU A CA    1 
ATOM   3949  C  C     . LEU A 1 1948 ? 195.660 183.026 153.770 1.00 63.04  ? 1948 LEU A C     1 
ATOM   3950  O  O     . LEU A 1 1948 ? 196.762 183.494 154.076 1.00 64.04  ? 1948 LEU A O     1 
ATOM   3951  C  CB    . LEU A 1 1948 ? 194.072 182.410 155.612 1.00 59.27  ? 1948 LEU A CB    1 
ATOM   3952  C  CG    . LEU A 1 1948 ? 192.950 182.786 156.579 1.00 58.69  ? 1948 LEU A CG    1 
ATOM   3953  C  CD1   . LEU A 1 1948 ? 192.697 181.657 157.563 1.00 60.69  ? 1948 LEU A CD1   1 
ATOM   3954  C  CD2   . LEU A 1 1948 ? 193.283 184.074 157.309 1.00 53.28  ? 1948 LEU A CD2   1 
ATOM   3955  N  N     . CYS A 1 1949 ? 195.512 182.143 152.778 1.00 71.50  ? 1949 CYS A N     1 
ATOM   3956  C  CA    . CYS A 1 1949 ? 196.658 181.706 151.989 1.00 66.91  ? 1949 CYS A CA    1 
ATOM   3957  C  C     . CYS A 1 1949 ? 197.276 182.866 151.224 1.00 76.97  ? 1949 CYS A C     1 
ATOM   3958  O  O     . CYS A 1 1949 ? 198.503 183.014 151.190 1.00 83.47  ? 1949 CYS A O     1 
ATOM   3959  C  CB    . CYS A 1 1949 ? 196.239 180.602 151.016 1.00 66.10  ? 1949 CYS A CB    1 
ATOM   3960  S  SG    . CYS A 1 1949 ? 195.854 179.006 151.764 1.00 84.01  ? 1949 CYS A SG    1 
ATOM   3961  N  N     . GLN A 1 1950 ? 196.443 183.700 150.599 1.00 82.25  ? 1950 GLN A N     1 
ATOM   3962  C  CA    . GLN A 1 1950 ? 196.980 184.801 149.807 1.00 78.45  ? 1950 GLN A CA    1 
ATOM   3963  C  C     . GLN A 1 1950 ? 197.564 185.894 150.695 1.00 81.29  ? 1950 GLN A C     1 
ATOM   3964  O  O     . GLN A 1 1950 ? 198.654 186.408 150.417 1.00 84.50  ? 1950 GLN A O     1 
ATOM   3965  C  CB    . GLN A 1 1950 ? 195.899 185.368 148.890 1.00 81.15  ? 1950 GLN A CB    1 
ATOM   3966  C  CG    . GLN A 1 1950 ? 195.743 184.610 147.586 1.00 81.63  ? 1950 GLN A CG    1 
ATOM   3967  C  CD    . GLN A 1 1950 ? 194.772 185.280 146.638 1.00 93.56  ? 1950 GLN A CD    1 
ATOM   3968  O  OE1   . GLN A 1 1950 ? 194.119 186.261 146.991 1.00 94.09  ? 1950 GLN A OE1   1 
ATOM   3969  N  NE2   . GLN A 1 1950 ? 194.672 184.753 145.423 1.00 93.74  ? 1950 GLN A NE2   1 
ATOM   3970  N  N     . VAL A 1 1951 ? 196.856 186.265 151.764 1.00 68.83  ? 1951 VAL A N     1 
ATOM   3971  C  CA    . VAL A 1 1951 ? 197.355 187.306 152.657 1.00 69.96  ? 1951 VAL A CA    1 
ATOM   3972  C  C     . VAL A 1 1951 ? 198.587 186.822 153.411 1.00 73.41  ? 1951 VAL A C     1 
ATOM   3973  O  O     . VAL A 1 1951 ? 199.595 187.533 153.503 1.00 76.22  ? 1951 VAL A O     1 
ATOM   3974  C  CB    . VAL A 1 1951 ? 196.245 187.755 153.624 1.00 72.17  ? 1951 VAL A CB    1 
ATOM   3975  C  CG1   . VAL A 1 1951 ? 196.824 188.602 154.745 1.00 73.50  ? 1951 VAL A CG1   1 
ATOM   3976  C  CG2   . VAL A 1 1951 ? 195.171 188.519 152.878 1.00 72.88  ? 1951 VAL A CG2   1 
ATOM   3977  N  N     . GLY A 1 1952 ? 198.533 185.608 153.951 1.00 67.77  ? 1952 GLY A N     1 
ATOM   3978  C  CA    . GLY A 1 1952 ? 199.590 185.118 154.810 1.00 63.61  ? 1952 GLY A CA    1 
ATOM   3979  C  C     . GLY A 1 1952 ? 199.319 185.463 156.258 1.00 64.50  ? 1952 GLY A C     1 
ATOM   3980  O  O     . GLY A 1 1952 ? 200.172 186.036 156.943 1.00 67.48  ? 1952 GLY A O     1 
ATOM   3981  N  N     . ALA A 1 1953 ? 198.127 185.118 156.733 1.00 59.61  ? 1953 ALA A N     1 
ATOM   3982  C  CA    . ALA A 1 1953 ? 197.661 185.506 158.052 1.00 56.20  ? 1953 ALA A CA    1 
ATOM   3983  C  C     . ALA A 1 1953 ? 197.170 184.286 158.818 1.00 53.07  ? 1953 ALA A C     1 
ATOM   3984  O  O     . ALA A 1 1953 ? 196.789 183.268 158.234 1.00 63.95  ? 1953 ALA A O     1 
ATOM   3985  C  CB    . ALA A 1 1953 ? 196.541 186.549 157.953 1.00 61.43  ? 1953 ALA A CB    1 
ATOM   3986  N  N     . TRP A 1 1954 ? 197.182 184.402 160.142 1.00 44.12  ? 1954 TRP A N     1 
ATOM   3987  C  CA    . TRP A 1 1954 ? 196.753 183.325 161.021 1.00 46.92  ? 1954 TRP A CA    1 
ATOM   3988  C  C     . TRP A 1 1954 ? 195.241 183.367 161.188 1.00 51.95  ? 1954 TRP A C     1 
ATOM   3989  O  O     . TRP A 1 1954 ? 194.665 184.435 161.409 1.00 70.54  ? 1954 TRP A O     1 
ATOM   3990  C  CB    . TRP A 1 1954 ? 197.428 183.441 162.387 1.00 57.70  ? 1954 TRP A CB    1 
ATOM   3991  C  CG    . TRP A 1 1954 ? 198.879 183.093 162.384 1.00 54.99  ? 1954 TRP A CG    1 
ATOM   3992  C  CD1   . TRP A 1 1954 ? 199.729 183.130 161.321 1.00 51.29  ? 1954 TRP A CD1   1 
ATOM   3993  C  CD2   . TRP A 1 1954 ? 199.655 182.663 163.505 1.00 51.05  ? 1954 TRP A CD2   1 
ATOM   3994  N  NE1   . TRP A 1 1954 ? 200.989 182.747 161.708 1.00 51.59  ? 1954 TRP A NE1   1 
ATOM   3995  C  CE2   . TRP A 1 1954 ? 200.969 182.455 163.046 1.00 54.56  ? 1954 TRP A CE2   1 
ATOM   3996  C  CE3   . TRP A 1 1954 ? 199.366 182.433 164.852 1.00 47.45  ? 1954 TRP A CE3   1 
ATOM   3997  C  CZ2   . TRP A 1 1954 ? 201.992 182.029 163.886 1.00 61.06  ? 1954 TRP A CZ2   1 
ATOM   3998  C  CZ3   . TRP A 1 1954 ? 200.382 182.009 165.684 1.00 52.40  ? 1954 TRP A CZ3   1 
ATOM   3999  C  CH2   . TRP A 1 1954 ? 201.679 181.811 165.199 1.00 62.71  ? 1954 TRP A CH2   1 
ATOM   4000  N  N     . GLY A 1 1955 ? 194.605 182.205 161.087 1.00 30.51  ? 1955 GLY A N     1 
ATOM   4001  C  CA    . GLY A 1 1955 ? 193.175 182.120 161.297 1.00 33.24  ? 1955 GLY A CA    1 
ATOM   4002  C  C     . GLY A 1 1955 ? 192.817 181.333 162.539 1.00 45.70  ? 1955 GLY A C     1 
ATOM   4003  O  O     . GLY A 1 1955 ? 192.976 180.111 162.571 1.00 61.47  ? 1955 GLY A O     1 
ATOM   4004  N  N     . CYS A 1 1956 ? 192.332 182.019 163.569 1.00 51.19  ? 1956 CYS A N     1 
ATOM   4005  C  CA    . CYS A 1 1956 ? 191.947 181.381 164.826 1.00 50.26  ? 1956 CYS A CA    1 
ATOM   4006  C  C     . CYS A 1 1956 ? 190.444 181.136 164.789 1.00 53.38  ? 1956 CYS A C     1 
ATOM   4007  O  O     . CYS A 1 1956 ? 189.651 182.021 165.120 1.00 68.38  ? 1956 CYS A O     1 
ATOM   4008  C  CB    . CYS A 1 1956 ? 192.347 182.244 166.017 1.00 51.35  ? 1956 CYS A CB    1 
ATOM   4009  S  SG    . CYS A 1 1956 ? 192.060 181.467 167.622 1.00 79.12  ? 1956 CYS A SG    1 
ATOM   4010  N  N     . PHE A 1 1957 ? 190.053 179.929 164.389 1.00 45.26  ? 1957 PHE A N     1 
ATOM   4011  C  CA    . PHE A 1 1957 ? 188.645 179.551 164.274 1.00 44.76  ? 1957 PHE A CA    1 
ATOM   4012  C  C     . PHE A 1 1957 ? 188.172 179.037 165.629 1.00 47.74  ? 1957 PHE A C     1 
ATOM   4013  O  O     . PHE A 1 1957 ? 188.139 177.832 165.877 1.00 54.77  ? 1957 PHE A O     1 
ATOM   4014  C  CB    . PHE A 1 1957 ? 188.448 178.500 163.187 1.00 49.46  ? 1957 PHE A CB    1 
ATOM   4015  C  CG    . PHE A 1 1957 ? 188.880 178.944 161.820 1.00 53.53  ? 1957 PHE A CG    1 
ATOM   4016  C  CD1   . PHE A 1 1957 ? 190.197 178.812 161.417 1.00 50.20  ? 1957 PHE A CD1   1 
ATOM   4017  C  CD2   . PHE A 1 1957 ? 187.967 179.487 160.934 1.00 53.65  ? 1957 PHE A CD2   1 
ATOM   4018  C  CE1   . PHE A 1 1957 ? 190.594 179.216 160.159 1.00 49.20  ? 1957 PHE A CE1   1 
ATOM   4019  C  CE2   . PHE A 1 1957 ? 188.359 179.892 159.676 1.00 48.45  ? 1957 PHE A CE2   1 
ATOM   4020  C  CZ    . PHE A 1 1957 ? 189.674 179.756 159.288 1.00 48.09  ? 1957 PHE A CZ    1 
ATOM   4021  N  N     . ASP A 1 1958 ? 187.800 179.957 166.513 1.00 58.90  ? 1958 ASP A N     1 
ATOM   4022  C  CA    . ASP A 1 1958 ? 187.247 179.546 167.793 1.00 60.97  ? 1958 ASP A CA    1 
ATOM   4023  C  C     . ASP A 1 1958 ? 185.838 178.988 167.609 1.00 59.10  ? 1958 ASP A C     1 
ATOM   4024  O  O     . ASP A 1 1958 ? 185.144 179.292 166.635 1.00 65.03  ? 1958 ASP A O     1 
ATOM   4025  C  CB    . ASP A 1 1958 ? 187.260 180.708 168.795 1.00 62.85  ? 1958 ASP A CB    1 
ATOM   4026  C  CG    . ASP A 1 1958 ? 186.400 181.881 168.362 1.00 76.64  ? 1958 ASP A CG    1 
ATOM   4027  O  OD1   . ASP A 1 1958 ? 186.314 182.859 169.135 1.00 79.09  ? 1958 ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A 1 1958 ? 185.837 181.852 167.252 1.00 79.44  ? 1958 ASP A OD2   1 
ATOM   4029  N  N     . GLU A 1 1959 ? 185.426 178.146 168.559 1.00 66.16  ? 1959 GLU A N     1 
ATOM   4030  C  CA    . GLU A 1 1959 ? 184.176 177.392 168.447 1.00 67.16  ? 1959 GLU A CA    1 
ATOM   4031  C  C     . GLU A 1 1959 ? 184.135 176.591 167.149 1.00 71.47  ? 1959 GLU A C     1 
ATOM   4032  O  O     . GLU A 1 1959 ? 183.128 176.579 166.436 1.00 74.36  ? 1959 GLU A O     1 
ATOM   4033  C  CB    . GLU A 1 1959 ? 182.954 178.310 168.564 1.00 71.13  ? 1959 GLU A CB    1 
ATOM   4034  C  CG    . GLU A 1 1959 ? 183.062 179.419 169.615 1.00 78.02  ? 1959 GLU A CG    1 
ATOM   4035  C  CD    . GLU A 1 1959 ? 183.259 178.914 171.042 1.00 83.76  ? 1959 GLU A CD    1 
ATOM   4036  O  OE1   . GLU A 1 1959 ? 183.417 179.761 171.945 1.00 75.45  ? 1959 GLU A OE1   1 
ATOM   4037  O  OE2   . GLU A 1 1959 ? 183.217 177.687 171.278 1.00 84.56  ? 1959 GLU A OE2   1 
ATOM   4038  N  N     . PHE A 1 1960 ? 185.247 175.924 166.835 1.00 58.71  ? 1960 PHE A N     1 
ATOM   4039  C  CA    . PHE A 1 1960 ? 185.343 175.155 165.599 1.00 47.55  ? 1960 PHE A CA    1 
ATOM   4040  C  C     . PHE A 1 1960 ? 184.359 173.996 165.572 1.00 56.36  ? 1960 PHE A C     1 
ATOM   4041  O  O     . PHE A 1 1960 ? 183.900 173.597 164.496 1.00 69.93  ? 1960 PHE A O     1 
ATOM   4042  C  CB    . PHE A 1 1960 ? 186.766 174.632 165.431 1.00 59.35  ? 1960 PHE A CB    1 
ATOM   4043  C  CG    . PHE A 1 1960 ? 187.047 174.064 164.075 1.00 57.08  ? 1960 PHE A CG    1 
ATOM   4044  C  CD1   . PHE A 1 1960 ? 186.906 174.839 162.944 1.00 52.89  ? 1960 PHE A CD1   1 
ATOM   4045  C  CD2   . PHE A 1 1960 ? 187.448 172.748 163.932 1.00 65.24  ? 1960 PHE A CD2   1 
ATOM   4046  C  CE1   . PHE A 1 1960 ? 187.169 174.316 161.700 1.00 51.99  ? 1960 PHE A CE1   1 
ATOM   4047  C  CE2   . PHE A 1 1960 ? 187.710 172.221 162.685 1.00 66.93  ? 1960 PHE A CE2   1 
ATOM   4048  C  CZ    . PHE A 1 1960 ? 187.568 173.007 161.569 1.00 59.18  ? 1960 PHE A CZ    1 
ATOM   4049  N  N     . ASN A 1 1961 ? 184.018 173.444 166.737 1.00 69.30  ? 1961 ASN A N     1 
ATOM   4050  C  CA    . ASN A 1 1961 ? 183.141 172.284 166.783 1.00 64.97  ? 1961 ASN A CA    1 
ATOM   4051  C  C     . ASN A 1 1961 ? 181.675 172.645 166.593 1.00 74.40  ? 1961 ASN A C     1 
ATOM   4052  O  O     . ASN A 1 1961 ? 180.830 171.743 166.594 1.00 78.73  ? 1961 ASN A O     1 
ATOM   4053  C  CB    . ASN A 1 1961 ? 183.326 171.536 168.104 1.00 62.14  ? 1961 ASN A CB    1 
ATOM   4054  C  CG    . ASN A 1 1961 ? 183.429 172.468 169.291 1.00 71.49  ? 1961 ASN A CG    1 
ATOM   4055  O  OD1   . ASN A 1 1961 ? 183.509 173.685 169.135 1.00 75.06  ? 1961 ASN A OD1   1 
ATOM   4056  N  ND2   . ASN A 1 1961 ? 183.430 171.899 170.490 1.00 75.56  ? 1961 ASN A ND2   1 
ATOM   4057  N  N     . ARG A 1 1962 ? 181.351 173.928 166.439 1.00 66.22  ? 1962 ARG A N     1 
ATOM   4058  C  CA    . ARG A 1 1962 ? 179.983 174.342 166.160 1.00 63.35  ? 1962 ARG A CA    1 
ATOM   4059  C  C     . ARG A 1 1962 ? 179.554 174.038 164.730 1.00 67.20  ? 1962 ARG A C     1 
ATOM   4060  O  O     . ARG A 1 1962 ? 178.360 174.129 164.428 1.00 72.00  ? 1962 ARG A O     1 
ATOM   4061  C  CB    . ARG A 1 1962 ? 179.816 175.837 166.443 1.00 62.26  ? 1962 ARG A CB    1 
ATOM   4062  C  CG    . ARG A 1 1962 ? 179.565 176.163 167.904 1.00 61.65  ? 1962 ARG A CG    1 
ATOM   4063  C  CD    . ARG A 1 1962 ? 179.444 177.663 168.127 1.00 65.55  ? 1962 ARG A CD    1 
ATOM   4064  N  NE    . ARG A 1 1962 ? 178.409 178.272 167.300 1.00 70.72  ? 1962 ARG A NE    1 
ATOM   4065  C  CZ    . ARG A 1 1962 ? 177.106 178.086 167.463 1.00 72.87  ? 1962 ARG A CZ    1 
ATOM   4066  N  NH1   . ARG A 1 1962 ? 176.632 177.317 168.430 1.00 74.30  ? 1962 ARG A NH1   1 
ATOM   4067  N  NH2   . ARG A 1 1962 ? 176.256 178.690 166.638 1.00 65.78  ? 1962 ARG A NH2   1 
ATOM   4068  N  N     . LEU A 1 1963 ? 180.487 173.685 163.852 1.00 61.99  ? 1963 LEU A N     1 
ATOM   4069  C  CA    . LEU A 1 1963 ? 180.156 173.261 162.501 1.00 59.38  ? 1963 LEU A CA    1 
ATOM   4070  C  C     . LEU A 1 1963 ? 179.495 171.889 162.527 1.00 68.93  ? 1963 LEU A C     1 
ATOM   4071  O  O     . LEU A 1 1963 ? 179.622 171.128 163.488 1.00 78.09  ? 1963 LEU A O     1 
ATOM   4072  C  CB    . LEU A 1 1963 ? 181.406 173.206 161.619 1.00 59.42  ? 1963 LEU A CB    1 
ATOM   4073  C  CG    . LEU A 1 1963 ? 181.834 174.453 160.845 1.00 57.37  ? 1963 LEU A CG    1 
ATOM   4074  C  CD1   . LEU A 1 1963 ? 182.338 175.518 161.788 1.00 65.74  ? 1963 LEU A CD1   1 
ATOM   4075  C  CD2   . LEU A 1 1963 ? 182.895 174.103 159.816 1.00 60.73  ? 1963 LEU A CD2   1 
ATOM   4076  N  N     . GLU A 1 1964 ? 178.779 171.580 161.451 1.00 78.07  ? 1964 GLU A N     1 
ATOM   4077  C  CA    . GLU A 1 1964 ? 178.230 170.243 161.296 1.00 82.35  ? 1964 GLU A CA    1 
ATOM   4078  C  C     . GLU A 1 1964 ? 179.353 169.242 161.053 1.00 89.20  ? 1964 GLU A C     1 
ATOM   4079  O  O     . GLU A 1 1964 ? 180.428 169.589 160.559 1.00 98.22  ? 1964 GLU A O     1 
ATOM   4080  C  CB    . GLU A 1 1964 ? 177.229 170.203 160.143 1.00 84.50  ? 1964 GLU A CB    1 
ATOM   4081  C  CG    . GLU A 1 1964 ? 175.985 171.041 160.373 1.00 86.21  ? 1964 GLU A CG    1 
ATOM   4082  C  CD    . GLU A 1 1964 ? 175.212 171.296 159.096 1.00 92.39  ? 1964 GLU A CD    1 
ATOM   4083  O  OE1   . GLU A 1 1964 ? 175.750 171.010 158.006 1.00 92.29  ? 1964 GLU A OE1   1 
ATOM   4084  O  OE2   . GLU A 1 1964 ? 174.065 171.783 159.181 1.00 90.17  ? 1964 GLU A OE2   1 
ATOM   4085  N  N     . GLU A 1 1965 ? 179.096 167.983 161.417 1.00 74.18  ? 1965 GLU A N     1 
ATOM   4086  C  CA    . GLU A 1 1965 ? 180.110 166.947 161.249 1.00 77.61  ? 1965 GLU A CA    1 
ATOM   4087  C  C     . GLU A 1 1965 ? 180.483 166.774 159.782 1.00 79.67  ? 1965 GLU A C     1 
ATOM   4088  O  O     . GLU A 1 1965 ? 181.666 166.640 159.443 1.00 86.96  ? 1965 GLU A O     1 
ATOM   4089  C  CB    . GLU A 1 1965 ? 179.612 165.629 161.838 1.00 79.03  ? 1965 GLU A CB    1 
ATOM   4090  C  CG    . GLU A 1 1965 ? 180.636 164.909 162.694 1.00 85.64  ? 1965 GLU A CG    1 
ATOM   4091  C  CD    . GLU A 1 1965 ? 179.995 163.998 163.719 1.00 87.34  ? 1965 GLU A CD    1 
ATOM   4092  O  OE1   . GLU A 1 1965 ? 178.795 164.184 164.013 1.00 85.39  ? 1965 GLU A OE1   1 
ATOM   4093  O  OE2   . GLU A 1 1965 ? 180.690 163.096 164.231 1.00 88.48  ? 1965 GLU A OE2   1 
ATOM   4094  N  N     . ARG A 1 1966 ? 179.485 166.783 158.896 1.00 70.69  ? 1966 ARG A N     1 
ATOM   4095  C  CA    . ARG A 1 1966 ? 179.762 166.684 157.468 1.00 74.08  ? 1966 ARG A CA    1 
ATOM   4096  C  C     . ARG A 1 1966 ? 180.596 167.865 156.989 1.00 77.79  ? 1966 ARG A C     1 
ATOM   4097  O  O     . ARG A 1 1966 ? 181.510 167.700 156.172 1.00 83.20  ? 1966 ARG A O     1 
ATOM   4098  C  CB    . ARG A 1 1966 ? 178.452 166.594 156.687 1.00 67.39  ? 1966 ARG A CB    1 
ATOM   4099  C  CG    . ARG A 1 1966 ? 177.404 167.605 157.117 1.00 70.19  ? 1966 ARG A CG    1 
ATOM   4100  C  CD    . ARG A 1 1966 ? 176.068 167.339 156.447 1.00 73.34  ? 1966 ARG A CD    1 
ATOM   4101  N  NE    . ARG A 1 1966 ? 175.229 168.531 156.416 1.00 79.81  ? 1966 ARG A NE    1 
ATOM   4102  C  CZ    . ARG A 1 1966 ? 175.064 169.303 155.351 1.00 82.18  ? 1966 ARG A CZ    1 
ATOM   4103  N  NH1   . ARG A 1 1966 ? 175.672 169.041 154.206 1.00 83.13  ? 1966 ARG A NH1   1 
ATOM   4104  N  NH2   . ARG A 1 1966 ? 174.270 170.367 155.438 1.00 76.88  ? 1966 ARG A NH2   1 
ATOM   4105  N  N     . MET A 1 1967 ? 180.301 169.065 157.492 1.00 67.71  ? 1967 MET A N     1 
ATOM   4106  C  CA    . MET A 1 1967 ? 181.065 170.237 157.082 1.00 57.84  ? 1967 MET A CA    1 
ATOM   4107  C  C     . MET A 1 1967 ? 182.498 170.168 157.592 1.00 63.48  ? 1967 MET A C     1 
ATOM   4108  O  O     . MET A 1 1967 ? 183.430 170.569 156.887 1.00 79.75  ? 1967 MET A O     1 
ATOM   4109  C  CB    . MET A 1 1967 ? 180.374 171.509 157.565 1.00 63.07  ? 1967 MET A CB    1 
ATOM   4110  C  CG    . MET A 1 1967 ? 179.350 172.044 156.581 1.00 71.71  ? 1967 MET A CG    1 
ATOM   4111  S  SD    . MET A 1 1967 ? 179.903 171.886 154.873 1.00 91.28  ? 1967 MET A SD    1 
ATOM   4112  C  CE    . MET A 1 1967 ? 178.336 171.891 154.007 1.00 69.06  ? 1967 MET A CE    1 
ATOM   4113  N  N     . LEU A 1 1968 ? 182.698 169.663 158.812 1.00 54.37  ? 1968 LEU A N     1 
ATOM   4114  C  CA    . LEU A 1 1968 ? 184.055 169.472 159.316 1.00 56.10  ? 1968 LEU A CA    1 
ATOM   4115  C  C     . LEU A 1 1968 ? 184.821 168.473 158.460 1.00 65.22  ? 1968 LEU A C     1 
ATOM   4116  O  O     . LEU A 1 1968 ? 185.993 168.695 158.121 1.00 75.45  ? 1968 LEU A O     1 
ATOM   4117  C  CB    . LEU A 1 1968 ? 184.014 169.006 160.771 1.00 52.91  ? 1968 LEU A CB    1 
ATOM   4118  C  CG    . LEU A 1 1968 ? 183.443 169.981 161.798 1.00 52.60  ? 1968 LEU A CG    1 
ATOM   4119  C  CD1   . LEU A 1 1968 ? 183.122 169.260 163.094 1.00 58.35  ? 1968 LEU A CD1   1 
ATOM   4120  C  CD2   . LEU A 1 1968 ? 184.414 171.117 162.044 1.00 62.13  ? 1968 LEU A CD2   1 
ATOM   4121  N  N     . SER A 1 1969 ? 184.169 167.368 158.091 1.00 57.86  ? 1969 SER A N     1 
ATOM   4122  C  CA    . SER A 1 1969 ? 184.813 166.387 157.226 1.00 53.03  ? 1969 SER A CA    1 
ATOM   4123  C  C     . SER A 1 1969 ? 185.188 167.003 155.885 1.00 56.54  ? 1969 SER A C     1 
ATOM   4124  O  O     . SER A 1 1969 ? 186.285 166.763 155.369 1.00 61.75  ? 1969 SER A O     1 
ATOM   4125  C  CB    . SER A 1 1969 ? 183.895 165.182 157.028 1.00 53.85  ? 1969 SER A CB    1 
ATOM   4126  O  OG    . SER A 1 1969 ? 184.411 164.310 156.039 1.00 66.71  ? 1969 SER A OG    1 
ATOM   4127  N  N     . ALA A 1 1970 ? 184.292 167.808 155.311 1.00 52.37  ? 1970 ALA A N     1 
ATOM   4128  C  CA    . ALA A 1 1970 ? 184.585 168.456 154.036 1.00 50.47  ? 1970 ALA A CA    1 
ATOM   4129  C  C     . ALA A 1 1970 ? 185.747 169.436 154.159 1.00 53.53  ? 1970 ALA A C     1 
ATOM   4130  O  O     . ALA A 1 1970 ? 186.620 169.484 153.284 1.00 62.82  ? 1970 ALA A O     1 
ATOM   4131  C  CB    . ALA A 1 1970 ? 183.338 169.163 153.512 1.00 50.02  ? 1970 ALA A CB    1 
ATOM   4132  N  N     . VAL A 1 1971 ? 185.775 170.228 155.235 1.00 54.27  ? 1971 VAL A N     1 
ATOM   4133  C  CA    . VAL A 1 1971 ? 186.849 171.194 155.444 1.00 44.82  ? 1971 VAL A CA    1 
ATOM   4134  C  C     . VAL A 1 1971 ? 188.189 170.504 155.673 1.00 51.34  ? 1971 VAL A C     1 
ATOM   4135  O  O     . VAL A 1 1971 ? 189.244 171.088 155.376 1.00 65.39  ? 1971 VAL A O     1 
ATOM   4136  C  CB    . VAL A 1 1971 ? 186.481 172.128 156.615 1.00 40.26  ? 1971 VAL A CB    1 
ATOM   4137  C  CG1   . VAL A 1 1971 ? 187.656 173.002 157.022 1.00 57.18  ? 1971 VAL A CG1   1 
ATOM   4138  C  CG2   . VAL A 1 1971 ? 185.298 173.000 156.237 1.00 49.02  ? 1971 VAL A CG2   1 
ATOM   4139  N  N     . SER A 1 1972 ? 188.172 169.273 156.196 1.00 52.28  ? 1972 SER A N     1 
ATOM   4140  C  CA    . SER A 1 1972 ? 189.415 168.531 156.383 1.00 52.50  ? 1972 SER A CA    1 
ATOM   4141  C  C     . SER A 1 1972 ? 190.206 168.408 155.086 1.00 53.95  ? 1972 SER A C     1 
ATOM   4142  O  O     . SER A 1 1972 ? 191.442 168.425 155.113 1.00 63.82  ? 1972 SER A O     1 
ATOM   4143  C  CB    . SER A 1 1972 ? 189.121 167.145 156.954 1.00 55.43  ? 1972 SER A CB    1 
ATOM   4144  O  OG    . SER A 1 1972 ? 188.552 166.300 155.970 1.00 61.50  ? 1972 SER A OG    1 
ATOM   4145  N  N     . GLN A 1 1973 ? 189.520 168.292 153.945 1.00 58.75  ? 1973 GLN A N     1 
ATOM   4146  C  CA    . GLN A 1 1973 ? 190.213 168.228 152.660 1.00 59.70  ? 1973 GLN A CA    1 
ATOM   4147  C  C     . GLN A 1 1973 ? 191.040 169.484 152.414 1.00 67.47  ? 1973 GLN A C     1 
ATOM   4148  O  O     . GLN A 1 1973 ? 192.232 169.406 152.086 1.00 79.72  ? 1973 GLN A O     1 
ATOM   4149  C  CB    . GLN A 1 1973 ? 189.204 168.035 151.529 1.00 60.52  ? 1973 GLN A CB    1 
ATOM   4150  C  CG    . GLN A 1 1973 ? 189.170 166.641 150.943 1.00 69.15  ? 1973 GLN A CG    1 
ATOM   4151  C  CD    . GLN A 1 1973 ? 188.204 166.537 149.781 1.00 77.01  ? 1973 GLN A CD    1 
ATOM   4152  O  OE1   . GLN A 1 1973 ? 188.565 166.076 148.698 1.00 79.66  ? 1973 GLN A OE1   1 
ATOM   4153  N  NE2   . GLN A 1 1973 ? 186.968 166.971 149.998 1.00 70.85  ? 1973 GLN A NE2   1 
ATOM   4154  N  N     . GLN A 1 1974 ? 190.415 170.655 152.551 1.00 60.20  ? 1974 GLN A N     1 
ATOM   4155  C  CA    . GLN A 1 1974 ? 191.127 171.906 152.319 1.00 54.74  ? 1974 GLN A CA    1 
ATOM   4156  C  C     . GLN A 1 1974 ? 192.261 172.081 153.317 1.00 60.06  ? 1974 GLN A C     1 
ATOM   4157  O  O     . GLN A 1 1974 ? 193.345 172.558 152.959 1.00 69.27  ? 1974 GLN A O     1 
ATOM   4158  C  CB    . GLN A 1 1974 ? 190.158 173.083 152.397 1.00 43.18  ? 1974 GLN A CB    1 
ATOM   4159  C  CG    . GLN A 1 1974 ? 189.057 173.045 151.358 1.00 54.91  ? 1974 GLN A CG    1 
ATOM   4160  C  CD    . GLN A 1 1974 ? 187.781 173.691 151.847 1.00 59.59  ? 1974 GLN A CD    1 
ATOM   4161  O  OE1   . GLN A 1 1974 ? 187.448 173.617 153.029 1.00 56.26  ? 1974 GLN A OE1   1 
ATOM   4162  N  NE2   . GLN A 1 1974 ? 187.053 174.326 150.938 1.00 66.33  ? 1974 GLN A NE2   1 
ATOM   4163  N  N     . VAL A 1 1975 ? 192.028 171.701 154.575 1.00 55.56  ? 1975 VAL A N     1 
ATOM   4164  C  CA    . VAL A 1 1975 ? 193.081 171.807 155.580 1.00 39.97  ? 1975 VAL A CA    1 
ATOM   4165  C  C     . VAL A 1 1975 ? 194.274 170.943 155.189 1.00 58.66  ? 1975 VAL A C     1 
ATOM   4166  O  O     . VAL A 1 1975 ? 195.429 171.379 155.273 1.00 71.46  ? 1975 VAL A O     1 
ATOM   4167  C  CB    . VAL A 1 1975 ? 192.540 171.431 156.971 1.00 49.29  ? 1975 VAL A CB    1 
ATOM   4168  C  CG1   . VAL A 1 1975 ? 193.656 171.466 157.996 1.00 61.09  ? 1975 VAL A CG1   1 
ATOM   4169  C  CG2   . VAL A 1 1975 ? 191.423 172.374 157.376 1.00 58.42  ? 1975 VAL A CG2   1 
ATOM   4170  N  N     . GLN A 1 1976 ? 194.014 169.711 154.745 1.00 69.91  ? 1976 GLN A N     1 
ATOM   4171  C  CA    . GLN A 1 1976 ? 195.097 168.815 154.353 1.00 67.64  ? 1976 GLN A CA    1 
ATOM   4172  C  C     . GLN A 1 1976 ? 195.860 169.351 153.148 1.00 71.75  ? 1976 GLN A C     1 
ATOM   4173  O  O     . GLN A 1 1976 ? 197.095 169.294 153.115 1.00 82.34  ? 1976 GLN A O     1 
ATOM   4174  C  CB    . GLN A 1 1976 ? 194.543 167.423 154.060 1.00 55.14  ? 1976 GLN A CB    1 
ATOM   4175  C  CG    . GLN A 1 1976 ? 195.595 166.418 153.639 1.00 62.06  ? 1976 GLN A CG    1 
ATOM   4176  C  CD    . GLN A 1 1976 ? 195.069 164.999 153.632 1.00 77.41  ? 1976 GLN A CD    1 
ATOM   4177  O  OE1   . GLN A 1 1976 ? 193.859 164.774 153.638 1.00 79.45  ? 1976 GLN A OE1   1 
ATOM   4178  N  NE2   . GLN A 1 1976 ? 195.977 164.032 153.619 1.00 82.52  ? 1976 GLN A NE2   1 
ATOM   4179  N  N     . CYS A 1 1977 ? 195.146 169.867 152.144 1.00 65.05  ? 1977 CYS A N     1 
ATOM   4180  C  CA    . CYS A 1 1977 ? 195.831 170.416 150.975 1.00 65.51  ? 1977 CYS A CA    1 
ATOM   4181  C  C     . CYS A 1 1977 ? 196.690 171.621 151.345 1.00 72.65  ? 1977 CYS A C     1 
ATOM   4182  O  O     . CYS A 1 1977 ? 197.827 171.750 150.871 1.00 78.15  ? 1977 CYS A O     1 
ATOM   4183  C  CB    . CYS A 1 1977 ? 194.823 170.786 149.886 1.00 66.68  ? 1977 CYS A CB    1 
ATOM   4184  S  SG    . CYS A 1 1977 ? 193.682 169.465 149.423 1.00 91.06  ? 1977 CYS A SG    1 
ATOM   4185  N  N     . ILE A 1 1978 ? 196.167 172.511 152.192 1.00 65.86  ? 1978 ILE A N     1 
ATOM   4186  C  CA    . ILE A 1 1978 ? 196.939 173.678 152.609 1.00 59.75  ? 1978 ILE A CA    1 
ATOM   4187  C  C     . ILE A 1 1978 ? 198.175 173.248 153.389 1.00 65.75  ? 1978 ILE A C     1 
ATOM   4188  O  O     . ILE A 1 1978 ? 199.269 173.799 153.204 1.00 76.89  ? 1978 ILE A O     1 
ATOM   4189  C  CB    . ILE A 1 1978 ? 196.054 174.639 153.424 1.00 57.45  ? 1978 ILE A CB    1 
ATOM   4190  C  CG1   . ILE A 1 1978 ? 195.190 175.484 152.490 1.00 63.05  ? 1978 ILE A CG1   1 
ATOM   4191  C  CG2   . ILE A 1 1978 ? 196.903 175.538 154.299 1.00 62.93  ? 1978 ILE A CG2   1 
ATOM   4192  C  CD1   . ILE A 1 1978 ? 193.827 175.800 153.050 1.00 65.95  ? 1978 ILE A CD1   1 
ATOM   4193  N  N     . GLN A 1 1979 ? 198.023 172.258 154.272 1.00 62.45  ? 1979 GLN A N     1 
ATOM   4194  C  CA    . GLN A 1 1979 ? 199.166 171.776 155.039 1.00 58.03  ? 1979 GLN A CA    1 
ATOM   4195  C  C     . GLN A 1 1979 ? 200.217 171.148 154.133 1.00 68.79  ? 1979 GLN A C     1 
ATOM   4196  O  O     . GLN A 1 1979 ? 201.418 171.334 154.351 1.00 77.73  ? 1979 GLN A O     1 
ATOM   4197  C  CB    . GLN A 1 1979 ? 198.705 170.780 156.100 1.00 51.58  ? 1979 GLN A CB    1 
ATOM   4198  C  CG    . GLN A 1 1979 ? 197.998 171.424 157.277 1.00 56.54  ? 1979 GLN A CG    1 
ATOM   4199  C  CD    . GLN A 1 1979 ? 197.528 170.410 158.295 1.00 64.20  ? 1979 GLN A CD    1 
ATOM   4200  O  OE1   . GLN A 1 1979 ? 197.840 169.225 158.194 1.00 67.56  ? 1979 GLN A OE1   1 
ATOM   4201  N  NE2   . GLN A 1 1979 ? 196.773 170.871 159.284 1.00 65.50  ? 1979 GLN A NE2   1 
ATOM   4202  N  N     . GLU A 1 1980 ? 199.788 170.402 153.112 1.00 74.23  ? 1980 GLU A N     1 
ATOM   4203  C  CA    . GLU A 1 1980 ? 200.747 169.829 152.173 1.00 74.50  ? 1980 GLU A CA    1 
ATOM   4204  C  C     . GLU A 1 1980 ? 201.488 170.917 151.406 1.00 80.19  ? 1980 GLU A C     1 
ATOM   4205  O  O     . GLU A 1 1980 ? 202.705 170.824 151.202 1.00 91.19  ? 1980 GLU A O     1 
ATOM   4206  C  CB    . GLU A 1 1980 ? 200.042 168.878 151.207 1.00 75.33  ? 1980 GLU A CB    1 
ATOM   4207  C  CG    . GLU A 1 1980 ? 199.672 167.540 151.819 1.00 81.46  ? 1980 GLU A CG    1 
ATOM   4208  C  CD    . GLU A 1 1980 ? 198.831 166.688 150.891 1.00 87.45  ? 1980 GLU A CD    1 
ATOM   4209  O  OE1   . GLU A 1 1980 ? 198.610 167.106 149.735 1.00 87.71  ? 1980 GLU A OE1   1 
ATOM   4210  O  OE2   . GLU A 1 1980 ? 198.392 165.599 151.316 1.00 83.26  ? 1980 GLU A OE2   1 
ATOM   4211  N  N     . ALA A 1 1981 ? 200.771 171.955 150.967 1.00 73.15  ? 1981 ALA A N     1 
ATOM   4212  C  CA    . ALA A 1 1981 ? 201.431 173.057 150.274 1.00 77.28  ? 1981 ALA A CA    1 
ATOM   4213  C  C     . ALA A 1 1981 ? 202.449 173.744 151.177 1.00 79.37  ? 1981 ALA A C     1 
ATOM   4214  O  O     . ALA A 1 1981 ? 203.565 174.061 150.744 1.00 80.59  ? 1981 ALA A O     1 
ATOM   4215  C  CB    . ALA A 1 1981 ? 200.394 174.059 149.770 1.00 83.73  ? 1981 ALA A CB    1 
ATOM   4216  N  N     . LEU A 1 1982 ? 202.082 173.976 152.440 1.00 84.42  ? 1982 LEU A N     1 
ATOM   4217  C  CA    . LEU A 1 1982 ? 203.017 174.574 153.387 1.00 77.52  ? 1982 LEU A CA    1 
ATOM   4218  C  C     . LEU A 1 1982 ? 204.240 173.688 153.586 1.00 81.94  ? 1982 LEU A C     1 
ATOM   4219  O  O     . LEU A 1 1982 ? 205.373 174.181 153.642 1.00 92.22  ? 1982 LEU A O     1 
ATOM   4220  C  CB    . LEU A 1 1982 ? 202.319 174.828 154.722 1.00 70.63  ? 1982 LEU A CB    1 
ATOM   4221  C  CG    . LEU A 1 1982 ? 201.436 176.072 154.806 1.00 76.44  ? 1982 LEU A CG    1 
ATOM   4222  C  CD1   . LEU A 1 1982 ? 200.647 176.076 156.104 1.00 84.69  ? 1982 LEU A CD1   1 
ATOM   4223  C  CD2   . LEU A 1 1982 ? 202.281 177.327 154.687 1.00 81.43  ? 1982 LEU A CD2   1 
ATOM   4224  N  N     . ARG A 1 1983 ? 204.027 172.375 153.694 1.00 83.80  ? 1983 ARG A N     1 
ATOM   4225  C  CA    . ARG A 1 1983 ? 205.138 171.453 153.892 1.00 88.27  ? 1983 ARG A CA    1 
ATOM   4226  C  C     . ARG A 1 1983 ? 206.094 171.476 152.706 1.00 89.55  ? 1983 ARG A C     1 
ATOM   4227  O  O     . ARG A 1 1983 ? 207.317 171.486 152.887 1.00 92.84  ? 1983 ARG A O     1 
ATOM   4228  C  CB    . ARG A 1 1983 ? 204.603 170.041 154.124 1.00 85.75  ? 1983 ARG A CB    1 
ATOM   4229  C  CG    . ARG A 1 1983 ? 205.556 169.127 154.866 1.00 89.01  ? 1983 ARG A CG    1 
ATOM   4230  C  CD    . ARG A 1 1983 ? 204.955 167.745 155.033 1.00 91.39  ? 1983 ARG A CD    1 
ATOM   4231  N  NE    . ARG A 1 1983 ? 203.499 167.792 155.087 1.00 90.03  ? 1983 ARG A NE    1 
ATOM   4232  C  CZ    . ARG A 1 1983 ? 202.793 167.907 156.203 1.00 88.40  ? 1983 ARG A CZ    1 
ATOM   4233  N  NH1   . ARG A 1 1983 ? 203.380 167.992 157.386 1.00 87.56  ? 1983 ARG A NH1   1 
ATOM   4234  N  NH2   . ARG A 1 1983 ? 201.466 167.938 156.132 1.00 89.36  ? 1983 ARG A NH2   1 
ATOM   4235  N  N     . GLU A 1 1984 ? 205.556 171.486 151.485 1.00 103.63 ? 1984 GLU A N     1 
ATOM   4236  C  CA    . GLU A 1 1984 ? 206.418 171.567 150.310 1.00 106.07 ? 1984 GLU A CA    1 
ATOM   4237  C  C     . GLU A 1 1984 ? 207.120 172.913 150.192 1.00 108.53 ? 1984 GLU A C     1 
ATOM   4238  O  O     . GLU A 1 1984 ? 208.238 172.967 149.669 1.00 108.10 ? 1984 GLU A O     1 
ATOM   4239  C  CB    . GLU A 1 1984 ? 205.627 171.277 149.032 1.00 106.11 ? 1984 GLU A CB    1 
ATOM   4240  C  CG    . GLU A 1 1984 ? 204.791 170.004 149.070 1.00 108.82 ? 1984 GLU A CG    1 
ATOM   4241  C  CD    . GLU A 1 1984 ? 205.591 168.760 149.435 1.00 110.04 ? 1984 GLU A CD    1 
ATOM   4242  O  OE1   . GLU A 1 1984 ? 206.826 168.748 149.241 1.00 111.47 ? 1984 GLU A OE1   1 
ATOM   4243  O  OE2   . GLU A 1 1984 ? 204.978 167.787 149.921 1.00 110.11 ? 1984 GLU A OE2   1 
ATOM   4244  N  N     . HIS A 1 1985 ? 206.497 173.999 150.658 1.00 121.39 ? 1985 HIS A N     1 
ATOM   4245  C  CA    . HIS A 1 1985 ? 207.190 175.282 150.639 1.00 119.57 ? 1985 HIS A CA    1 
ATOM   4246  C  C     . HIS A 1 1985 ? 208.277 175.323 151.707 1.00 118.19 ? 1985 HIS A C     1 
ATOM   4247  O  O     . HIS A 1 1985 ? 209.249 176.075 151.572 1.00 119.76 ? 1985 HIS A O     1 
ATOM   4248  C  CB    . HIS A 1 1985 ? 206.181 176.426 150.818 1.00 118.66 ? 1985 HIS A CB    1 
ATOM   4249  C  CG    . HIS A 1 1985 ? 206.793 177.796 150.907 1.00 121.02 ? 1985 HIS A CG    1 
ATOM   4250  N  ND1   . HIS A 1 1985 ? 207.927 178.078 151.639 1.00 123.42 ? 1985 HIS A ND1   1 
ATOM   4251  C  CD2   . HIS A 1 1985 ? 206.423 178.965 150.331 1.00 121.84 ? 1985 HIS A CD2   1 
ATOM   4252  C  CE1   . HIS A 1 1985 ? 208.225 179.358 151.517 1.00 122.24 ? 1985 HIS A CE1   1 
ATOM   4253  N  NE2   . HIS A 1 1985 ? 207.329 179.919 150.726 1.00 122.71 ? 1985 HIS A NE2   1 
ATOM   4254  N  N     . SER A 1 1986 ? 208.131 174.528 152.768 1.00 114.04 ? 1986 SER A N     1 
ATOM   4255  C  CA    . SER A 1 1986 ? 209.123 174.493 153.837 1.00 113.51 ? 1986 SER A CA    1 
ATOM   4256  C  C     . SER A 1 1986 ? 210.448 173.885 153.401 1.00 118.05 ? 1986 SER A C     1 
ATOM   4257  O  O     . SER A 1 1986 ? 211.484 174.206 153.993 1.00 119.87 ? 1986 SER A O     1 
ATOM   4258  C  CB    . SER A 1 1986 ? 208.581 173.703 155.029 1.00 114.03 ? 1986 SER A CB    1 
ATOM   4259  O  OG    . SER A 1 1986 ? 208.773 172.312 154.843 1.00 117.51 ? 1986 SER A OG    1 
ATOM   4260  N  N     . ASN A 1 1987 ? 210.438 173.019 152.397 1.00 142.82 ? 1987 ASN A N     1 
ATOM   4261  C  CA    . ASN A 1 1987 ? 211.652 172.318 152.000 1.00 144.94 ? 1987 ASN A CA    1 
ATOM   4262  C  C     . ASN A 1 1987 ? 212.658 173.303 151.413 1.00 147.19 ? 1987 ASN A C     1 
ATOM   4263  O  O     . ASN A 1 1987 ? 212.291 174.127 150.566 1.00 144.74 ? 1987 ASN A O     1 
ATOM   4264  C  CB    . ASN A 1 1987 ? 211.314 171.225 150.989 1.00 145.06 ? 1987 ASN A CB    1 
ATOM   4265  C  CG    . ASN A 1 1987 ? 212.298 170.074 151.023 1.00 145.97 ? 1987 ASN A CG    1 
ATOM   4266  O  OD1   . ASN A 1 1987 ? 213.494 170.256 150.800 1.00 144.93 ? 1987 ASN A OD1   1 
ATOM   4267  N  ND2   . ASN A 1 1987 ? 211.797 168.878 151.306 1.00 145.06 ? 1987 ASN A ND2   1 
ATOM   4268  N  N     . PRO A 1 1988 ? 213.924 173.259 151.837 1.00 165.00 ? 1988 PRO A N     1 
ATOM   4269  C  CA    . PRO A 1 1988 ? 214.902 174.247 151.347 1.00 163.50 ? 1988 PRO A CA    1 
ATOM   4270  C  C     . PRO A 1 1988 ? 215.190 174.162 149.856 1.00 164.16 ? 1988 PRO A C     1 
ATOM   4271  O  O     . PRO A 1 1988 ? 215.705 175.136 149.293 1.00 163.34 ? 1988 PRO A O     1 
ATOM   4272  C  CB    . PRO A 1 1988 ? 216.157 173.940 152.176 1.00 162.56 ? 1988 PRO A CB    1 
ATOM   4273  C  CG    . PRO A 1 1988 ? 215.973 172.531 152.649 1.00 161.97 ? 1988 PRO A CG    1 
ATOM   4274  C  CD    . PRO A 1 1988 ? 214.500 172.373 152.862 1.00 162.57 ? 1988 PRO A CD    1 
ATOM   4275  N  N     . ASN A 1 1989 ? 214.890 173.039 149.196 1.00 164.98 ? 1989 ASN A N     1 
ATOM   4276  C  CA    . ASN A 1 1989 ? 215.163 172.949 147.764 1.00 162.75 ? 1989 ASN A CA    1 
ATOM   4277  C  C     . ASN A 1 1989 ? 214.293 173.909 146.965 1.00 162.23 ? 1989 ASN A C     1 
ATOM   4278  O  O     . ASN A 1 1989 ? 214.648 174.279 145.840 1.00 161.09 ? 1989 ASN A O     1 
ATOM   4279  C  CB    . ASN A 1 1989 ? 214.970 171.515 147.266 1.00 161.14 ? 1989 ASN A CB    1 
ATOM   4280  C  CG    . ASN A 1 1989 ? 213.715 170.869 147.809 1.00 161.44 ? 1989 ASN A CG    1 
ATOM   4281  O  OD1   . ASN A 1 1989 ? 212.610 171.383 147.634 1.00 161.02 ? 1989 ASN A OD1   1 
ATOM   4282  N  ND2   . ASN A 1 1989 ? 213.877 169.722 148.455 1.00 161.13 ? 1989 ASN A ND2   1 
ATOM   4283  N  N     . TYR A 1 1990 ? 213.156 174.319 147.521 1.00 172.01 ? 1990 TYR A N     1 
ATOM   4284  C  CA    . TYR A 1 1990 ? 212.332 175.330 146.875 1.00 173.40 ? 1990 TYR A CA    1 
ATOM   4285  C  C     . TYR A 1 1990 ? 213.046 176.675 146.877 1.00 173.93 ? 1990 TYR A C     1 
ATOM   4286  O  O     . TYR A 1 1990 ? 213.698 177.052 147.855 1.00 172.81 ? 1990 TYR A O     1 
ATOM   4287  C  CB    . TYR A 1 1990 ? 210.982 175.449 147.583 1.00 171.73 ? 1990 TYR A CB    1 
ATOM   4288  C  CG    . TYR A 1 1990 ? 210.246 176.738 147.288 1.00 172.62 ? 1990 TYR A CG    1 
ATOM   4289  C  CD1   . TYR A 1 1990 ? 209.586 176.923 146.080 1.00 171.79 ? 1990 TYR A CD1   1 
ATOM   4290  C  CD2   . TYR A 1 1990 ? 210.214 177.771 148.217 1.00 172.36 ? 1990 TYR A CD2   1 
ATOM   4291  C  CE1   . TYR A 1 1990 ? 208.913 178.099 145.807 1.00 172.02 ? 1990 TYR A CE1   1 
ATOM   4292  C  CE2   . TYR A 1 1990 ? 209.545 178.950 147.951 1.00 172.37 ? 1990 TYR A CE2   1 
ATOM   4293  C  CZ    . TYR A 1 1990 ? 208.897 179.109 146.745 1.00 172.85 ? 1990 TYR A CZ    1 
ATOM   4294  O  OH    . TYR A 1 1990 ? 208.229 180.282 146.477 1.00 172.21 ? 1990 TYR A OH    1 
ATOM   4295  N  N     . ASP A 1 1991 ? 212.920 177.410 145.769 1.00 185.45 ? 1991 ASP A N     1 
ATOM   4296  C  CA    . ASP A 1 1991 ? 213.635 178.709 145.644 1.00 184.41 ? 1991 ASP A CA    1 
ATOM   4297  C  C     . ASP A 1 1991 ? 212.630 179.831 145.369 1.00 185.16 ? 1991 ASP A C     1 
ATOM   4298  O  O     . ASP A 1 1991 ? 211.472 179.520 145.032 1.00 185.68 ? 1991 ASP A O     1 
ATOM   4299  C  CB    . ASP A 1 1991 ? 214.702 178.634 144.552 1.00 184.62 ? 1991 ASP A CB    1 
ATOM   4300  C  CG    . ASP A 1 1991 ? 214.222 177.905 143.309 1.00 184.77 ? 1991 ASP A CG    1 
ATOM   4301  O  OD1   . ASP A 1 1991 ? 213.876 176.713 143.427 1.00 183.41 ? 1991 ASP A OD1   1 
ATOM   4302  O  OD2   . ASP A 1 1991 ? 214.192 178.535 142.236 1.00 184.72 ? 1991 ASP A OD2   1 
ATOM   4303  N  N     . LYS A 1 1992 ? 213.065 181.086 145.508 1.00 185.58 ? 1992 LYS A N     1 
ATOM   4304  C  CA    . LYS A 1 1992 ? 212.173 182.243 145.230 1.00 186.12 ? 1992 LYS A CA    1 
ATOM   4305  C  C     . LYS A 1 1992 ? 211.791 182.232 143.747 1.00 186.26 ? 1992 LYS A C     1 
ATOM   4306  O  O     . LYS A 1 1992 ? 210.602 182.452 143.444 1.00 185.84 ? 1992 LYS A O     1 
ATOM   4307  C  CB    . LYS A 1 1992 ? 212.876 183.553 145.594 1.00 185.60 ? 1992 LYS A CB    1 
ATOM   4308  C  CG    . LYS A 1 1992 ? 213.386 183.644 147.025 1.00 185.01 ? 1992 LYS A CG    1 
ATOM   4309  C  CD    . LYS A 1 1992 ? 214.143 184.925 147.301 1.00 184.89 ? 1992 LYS A CD    1 
ATOM   4310  C  CE    . LYS A 1 1992 ? 215.314 185.128 146.363 1.00 185.31 ? 1992 LYS A CE    1 
ATOM   4311  N  NZ    . LYS A 1 1992 ? 216.017 186.404 146.630 1.00 185.67 ? 1992 LYS A NZ    1 
ATOM   4312  N  N     . THR A 1 1993 ? 212.762 181.977 142.865 1.00 190.47 ? 1993 THR A N     1 
ATOM   4313  C  CA    . THR A 1 1993 ? 212.494 181.996 141.402 1.00 190.34 ? 1993 THR A CA    1 
ATOM   4314  C  C     . THR A 1 1993 ? 211.422 180.951 141.075 1.00 189.97 ? 1993 THR A C     1 
ATOM   4315  O  O     . THR A 1 1993 ? 210.511 181.274 140.289 1.00 189.94 ? 1993 THR A O     1 
ATOM   4316  C  CB    . THR A 1 1993 ? 213.780 181.766 140.598 1.00 189.89 ? 1993 THR A CB    1 
ATOM   4317  O  OG1   . THR A 1 1993 ? 214.111 180.379 140.659 1.00 189.73 ? 1993 THR A OG1   1 
ATOM   4318  C  CG2   . THR A 1 1993 ? 214.941 182.596 141.100 1.00 189.90 ? 1993 THR A CG2   1 
ATOM   4319  N  N     . SER A 1 1994 ? 211.525 179.756 141.663 1.00 182.10 ? 1994 SER A N     1 
ATOM   4320  C  CA    . SER A 1 1994 ? 210.488 178.714 141.447 1.00 181.08 ? 1994 SER A CA    1 
ATOM   4321  C  C     . SER A 1 1994 ? 209.134 179.252 141.921 1.00 181.44 ? 1994 SER A C     1 
ATOM   4322  O  O     . SER A 1 1994 ? 209.086 179.829 143.026 1.00 181.30 ? 1994 SER A O     1 
ATOM   4323  C  CB    . SER A 1 1994 ? 210.851 177.427 142.141 1.00 178.72 ? 1994 SER A CB    1 
ATOM   4324  O  OG    . SER A 1 1994 ? 211.069 177.642 143.527 1.00 178.02 ? 1994 SER A OG    1 
ATOM   4325  N  N     . ALA A 1 1995 ? 208.082 179.071 141.116 1.00 168.53 ? 1995 ALA A N     1 
ATOM   4326  C  CA    . ALA A 1 1995 ? 206.752 179.623 141.467 1.00 167.62 ? 1995 ALA A CA    1 
ATOM   4327  C  C     . ALA A 1 1995 ? 206.345 179.146 142.865 1.00 166.78 ? 1995 ALA A C     1 
ATOM   4328  O  O     . ALA A 1 1995 ? 206.547 177.955 143.171 1.00 166.72 ? 1995 ALA A O     1 
ATOM   4329  C  CB    . ALA A 1 1995 ? 205.736 179.216 140.430 1.00 166.16 ? 1995 ALA A CB    1 
ATOM   4330  N  N     . PRO A 1 1996 ? 205.777 180.024 143.719 1.00 150.01 ? 1996 PRO A N     1 
ATOM   4331  C  CA    . PRO A 1 1996 ? 205.361 179.636 145.066 1.00 150.54 ? 1996 PRO A CA    1 
ATOM   4332  C  C     . PRO A 1 1996 ? 204.420 178.427 145.011 1.00 148.07 ? 1996 PRO A C     1 
ATOM   4333  O  O     . PRO A 1 1996 ? 203.625 178.349 144.093 1.00 146.99 ? 1996 PRO A O     1 
ATOM   4334  C  CB    . PRO A 1 1996 ? 204.592 180.864 145.572 1.00 149.18 ? 1996 PRO A CB    1 
ATOM   4335  C  CG    . PRO A 1 1996 ? 205.191 182.015 144.797 1.00 149.17 ? 1996 PRO A CG    1 
ATOM   4336  C  CD    . PRO A 1 1996 ? 205.516 181.436 143.436 1.00 148.55 ? 1996 PRO A CD    1 
ATOM   4337  N  N     . ILE A 1 1997 ? 204.535 177.522 145.987 1.00 122.07 ? 1997 ILE A N     1 
ATOM   4338  C  CA    . ILE A 1 1997 ? 203.665 176.311 146.015 1.00 119.94 ? 1997 ILE A CA    1 
ATOM   4339  C  C     . ILE A 1 1997 ? 202.212 176.768 145.854 1.00 120.32 ? 1997 ILE A C     1 
ATOM   4340  O  O     . ILE A 1 1997 ? 201.790 177.662 146.611 1.00 122.10 ? 1997 ILE A O     1 
ATOM   4341  C  CB    . ILE A 1 1997 ? 203.873 175.518 147.319 1.00 120.56 ? 1997 ILE A CB    1 
ATOM   4342  C  CG1   . ILE A 1 1997 ? 205.359 175.288 147.610 1.00 120.65 ? 1997 ILE A CG1   1 
ATOM   4343  C  CG2   . ILE A 1 1997 ? 203.095 174.213 147.286 1.00 119.81 ? 1997 ILE A CG2   1 
ATOM   4344  C  CD1   . ILE A 1 1997 ? 206.080 174.504 146.540 1.00 119.58 ? 1997 ILE A CD1   1 
ATOM   4345  N  N     . THR A 1 1998 ? 201.486 176.180 144.900 1.00 106.27 ? 1998 THR A N     1 
ATOM   4346  C  CA    . THR A 1 1998 ? 200.084 176.600 144.640 1.00 109.73 ? 1998 THR A CA    1 
ATOM   4347  C  C     . THR A 1 1998 ? 199.124 175.511 145.122 1.00 110.06 ? 1998 THR A C     1 
ATOM   4348  O  O     . THR A 1 1998 ? 199.072 174.447 144.476 1.00 105.41 ? 1998 THR A O     1 
ATOM   4349  C  CB    . THR A 1 1998 ? 199.864 176.911 143.155 1.00 108.18 ? 1998 THR A CB    1 
ATOM   4350  O  OG1   . THR A 1 1998 ? 200.160 175.730 142.409 1.00 105.47 ? 1998 THR A OG1   1 
ATOM   4351  C  CG2   . THR A 1 1998 ? 200.718 178.058 142.662 1.00 110.80 ? 1998 THR A CG2   1 
ATOM   4352  N  N     . CYS A 1 1999 ? 198.398 175.771 146.213 1.00 108.44 ? 1999 CYS A N     1 
ATOM   4353  C  CA    . CYS A 1 1999 ? 197.388 174.799 146.705 1.00 102.39 ? 1999 CYS A CA    1 
ATOM   4354  C  C     . CYS A 1 1999 ? 196.104 174.969 145.889 1.00 103.97 ? 1999 CYS A C     1 
ATOM   4355  O  O     . CYS A 1 1999 ? 195.830 176.104 145.455 1.00 104.54 ? 1999 CYS A O     1 
ATOM   4356  C  CB    . CYS A 1 1999 ? 197.084 175.034 148.178 1.00 98.79  ? 1999 CYS A CB    1 
ATOM   4357  S  SG    . CYS A 1 1999 ? 196.031 173.750 148.901 1.00 112.26 ? 1999 CYS A SG    1 
ATOM   4358  N  N     . GLU A 1 2000 ? 195.354 173.883 145.687 1.00 98.60  ? 2000 GLU A N     1 
ATOM   4359  C  CA    . GLU A 1 2000 ? 194.070 173.971 144.943 1.00 96.98  ? 2000 GLU A CA    1 
ATOM   4360  C  C     . GLU A 1 2000 ? 192.923 174.168 145.938 1.00 98.75  ? 2000 GLU A C     1 
ATOM   4361  O  O     . GLU A 1 2000 ? 192.543 173.185 146.602 1.00 96.92  ? 2000 GLU A O     1 
ATOM   4362  C  CB    . GLU A 1 2000 ? 193.840 172.716 144.100 1.00 98.77  ? 2000 GLU A CB    1 
ATOM   4363  C  CG    . GLU A 1 2000 ? 192.545 172.764 143.310 1.00 101.32 ? 2000 GLU A CG    1 
ATOM   4364  C  CD    . GLU A 1 2000 ? 192.292 171.556 142.425 1.00 104.82 ? 2000 GLU A CD    1 
ATOM   4365  O  OE1   . GLU A 1 2000 ? 193.144 170.646 142.412 1.00 106.28 ? 2000 GLU A OE1   1 
ATOM   4366  O  OE2   . GLU A 1 2000 ? 191.243 171.530 141.752 1.00 103.82 ? 2000 GLU A OE2   1 
ATOM   4367  N  N     . LEU A 1 2001 ? 192.397 175.393 146.031 1.00 93.08  ? 2001 LEU A N     1 
ATOM   4368  C  CA    . LEU A 1 2001 ? 191.254 175.671 146.941 1.00 89.14  ? 2001 LEU A CA    1 
ATOM   4369  C  C     . LEU A 1 2001 ? 190.038 176.088 146.113 1.00 93.86  ? 2001 LEU A C     1 
ATOM   4370  O  O     . LEU A 1 2001 ? 190.163 177.048 145.328 1.00 95.73  ? 2001 LEU A O     1 
ATOM   4371  C  CB    . LEU A 1 2001 ? 191.643 176.774 147.930 1.00 87.60  ? 2001 LEU A CB    1 
ATOM   4372  C  CG    . LEU A 1 2001 ? 192.255 176.297 149.246 1.00 86.19  ? 2001 LEU A CG    1 
ATOM   4373  C  CD1   . LEU A 1 2001 ? 191.659 174.965 149.670 1.00 87.39  ? 2001 LEU A CD1   1 
ATOM   4374  C  CD2   . LEU A 1 2001 ? 193.767 176.200 149.143 1.00 88.75  ? 2001 LEU A CD2   1 
ATOM   4375  N  N     . LEU A 1 2002 ? 188.914 175.387 146.280 1.00 93.66  ? 2002 LEU A N     1 
ATOM   4376  C  CA    . LEU A 1 2002 ? 187.682 175.741 145.575 1.00 92.38  ? 2002 LEU A CA    1 
ATOM   4377  C  C     . LEU A 1 2002 ? 187.873 175.689 144.061 1.00 97.05  ? 2002 LEU A C     1 
ATOM   4378  O  O     . LEU A 1 2002 ? 187.454 176.589 143.330 1.00 99.77  ? 2002 LEU A O     1 
ATOM   4379  C  CB    . LEU A 1 2002 ? 187.177 177.116 146.014 1.00 92.62  ? 2002 LEU A CB    1 
ATOM   4380  C  CG    . LEU A 1 2002 ? 186.189 177.144 147.182 1.00 92.08  ? 2002 LEU A CG    1 
ATOM   4381  C  CD1   . LEU A 1 2002 ? 185.341 178.405 147.132 1.00 94.15  ? 2002 LEU A CD1   1 
ATOM   4382  C  CD2   . LEU A 1 2002 ? 185.311 175.903 147.182 1.00 92.16  ? 2002 LEU A CD2   1 
ATOM   4383  N  N     . ASN A 1 2003 ? 188.523 174.622 143.591 1.00 104.09 ? 2003 ASN A N     1 
ATOM   4384  C  CA    . ASN A 1 2003 ? 188.791 174.411 142.167 1.00 103.40 ? 2003 ASN A CA    1 
ATOM   4385  C  C     . ASN A 1 2003 ? 189.602 175.555 141.564 1.00 103.76 ? 2003 ASN A C     1 
ATOM   4386  O  O     . ASN A 1 2003 ? 189.424 175.909 140.397 1.00 107.54 ? 2003 ASN A O     1 
ATOM   4387  C  CB    . ASN A 1 2003 ? 187.492 174.207 141.380 1.00 102.55 ? 2003 ASN A CB    1 
ATOM   4388  C  CG    . ASN A 1 2003 ? 186.862 172.855 141.639 1.00 106.06 ? 2003 ASN A CG    1 
ATOM   4389  O  OD1   . ASN A 1 2003 ? 187.546 171.832 141.656 1.00 108.42 ? 2003 ASN A OD1   1 
ATOM   4390  N  ND2   . ASN A 1 2003 ? 185.550 172.843 141.844 1.00 106.00 ? 2003 ASN A ND2   1 
ATOM   4391  N  N     . LYS A 1 2004 ? 190.498 176.140 142.354 1.00 95.09  ? 2004 LYS A N     1 
ATOM   4392  C  CA    . LYS A 1 2004 ? 191.328 177.248 141.910 1.00 95.30  ? 2004 LYS A CA    1 
ATOM   4393  C  C     . LYS A 1 2004 ? 192.737 177.079 142.458 1.00 99.90  ? 2004 LYS A C     1 
ATOM   4394  O  O     . LYS A 1 2004 ? 192.945 176.443 143.494 1.00 101.36 ? 2004 LYS A O     1 
ATOM   4395  C  CB    . LYS A 1 2004 ? 190.741 178.597 142.358 1.00 98.05  ? 2004 LYS A CB    1 
ATOM   4396  C  CG    . LYS A 1 2004 ? 191.344 179.814 141.674 1.00 99.39  ? 2004 LYS A CG    1 
ATOM   4397  C  CD    . LYS A 1 2004 ? 190.636 181.090 142.096 1.00 99.54  ? 2004 LYS A CD    1 
ATOM   4398  C  CE    . LYS A 1 2004 ? 191.312 181.726 143.299 1.00 98.35  ? 2004 LYS A CE    1 
ATOM   4399  N  NZ    . LYS A 1 2004 ? 192.711 182.138 143.000 1.00 99.22  ? 2004 LYS A NZ    1 
ATOM   4400  N  N     . GLN A 1 2005 ? 193.706 177.653 141.749 1.00 100.43 ? 2005 GLN A N     1 
ATOM   4401  C  CA    . GLN A 1 2005 ? 195.101 177.638 142.174 1.00 101.73 ? 2005 GLN A CA    1 
ATOM   4402  C  C     . GLN A 1 2005 ? 195.382 178.921 142.945 1.00 101.72 ? 2005 GLN A C     1 
ATOM   4403  O  O     . GLN A 1 2005 ? 195.369 180.015 142.370 1.00 101.90 ? 2005 GLN A O     1 
ATOM   4404  C  CB    . GLN A 1 2005 ? 196.031 177.498 140.972 1.00 100.40 ? 2005 GLN A CB    1 
ATOM   4405  C  CG    . GLN A 1 2005 ? 195.771 176.279 140.086 1.00 103.08 ? 2005 GLN A CG    1 
ATOM   4406  C  CD    . GLN A 1 2005 ? 196.028 174.948 140.781 1.00 102.18 ? 2005 GLN A CD    1 
ATOM   4407  O  OE1   . GLN A 1 2005 ? 195.436 174.639 141.815 1.00 99.74  ? 2005 GLN A OE1   1 
ATOM   4408  N  NE2   . GLN A 1 2005 ? 196.924 174.154 140.207 1.00 100.97 ? 2005 GLN A NE2   1 
ATOM   4409  N  N     . VAL A 1 2006 ? 195.636 178.790 144.244 1.00 93.74  ? 2006 VAL A N     1 
ATOM   4410  C  CA    . VAL A 1 2006 ? 195.856 179.926 145.131 1.00 94.12  ? 2006 VAL A CA    1 
ATOM   4411  C  C     . VAL A 1 2006 ? 197.264 179.834 145.702 1.00 91.56  ? 2006 VAL A C     1 
ATOM   4412  O  O     . VAL A 1 2006 ? 197.674 178.778 146.198 1.00 90.91  ? 2006 VAL A O     1 
ATOM   4413  C  CB    . VAL A 1 2006 ? 194.802 179.976 146.250 1.00 92.99  ? 2006 VAL A CB    1 
ATOM   4414  C  CG1   . VAL A 1 2006 ? 194.620 178.605 146.878 1.00 91.24  ? 2006 VAL A CG1   1 
ATOM   4415  C  CG2   . VAL A 1 2006 ? 195.190 181.001 147.303 1.00 94.35  ? 2006 VAL A CG2   1 
ATOM   4416  N  N     . LYS A 1 2007 ? 198.006 180.935 145.614 1.00 91.09  ? 2007 LYS A N     1 
ATOM   4417  C  CA    . LYS A 1 2007 ? 199.339 180.992 146.196 1.00 89.93  ? 2007 LYS A CA    1 
ATOM   4418  C  C     . LYS A 1 2007 ? 199.261 180.861 147.712 1.00 95.15  ? 2007 LYS A C     1 
ATOM   4419  O  O     . LYS A 1 2007 ? 198.388 181.447 148.358 1.00 101.08 ? 2007 LYS A O     1 
ATOM   4420  C  CB    . LYS A 1 2007 ? 200.026 182.302 145.812 1.00 92.03  ? 2007 LYS A CB    1 
ATOM   4421  C  CG    . LYS A 1 2007 ? 201.401 182.492 146.427 1.00 92.56  ? 2007 LYS A CG    1 
ATOM   4422  C  CD    . LYS A 1 2007 ? 201.722 183.965 146.619 1.00 93.56  ? 2007 LYS A CD    1 
ATOM   4423  C  CE    . LYS A 1 2007 ? 200.848 184.586 147.696 1.00 95.57  ? 2007 LYS A CE    1 
ATOM   4424  N  NZ    . LYS A 1 2007 ? 201.503 185.761 148.333 1.00 95.33  ? 2007 LYS A NZ    1 
ATOM   4425  N  N     . VAL A 1 2008 ? 200.182 180.087 148.280 1.00 83.60  ? 2008 VAL A N     1 
ATOM   4426  C  CA    . VAL A 1 2008 ? 200.226 179.829 149.714 1.00 84.32  ? 2008 VAL A CA    1 
ATOM   4427  C  C     . VAL A 1 2008 ? 201.396 180.597 150.308 1.00 83.88  ? 2008 VAL A C     1 
ATOM   4428  O  O     . VAL A 1 2008 ? 202.549 180.391 149.911 1.00 87.55  ? 2008 VAL A O     1 
ATOM   4429  C  CB    . VAL A 1 2008 ? 200.348 178.326 150.014 1.00 83.82  ? 2008 VAL A CB    1 
ATOM   4430  C  CG1   . VAL A 1 2008 ? 200.521 178.098 151.504 1.00 81.56  ? 2008 VAL A CG1   1 
ATOM   4431  C  CG2   . VAL A 1 2008 ? 199.129 177.586 149.498 1.00 83.03  ? 2008 VAL A CG2   1 
ATOM   4432  N  N     . SER A 1 2009 ? 201.100 181.481 151.256 1.00 79.06  ? 2009 SER A N     1 
ATOM   4433  C  CA    . SER A 1 2009 ? 202.175 182.222 151.902 1.00 79.22  ? 2009 SER A CA    1 
ATOM   4434  C  C     . SER A 1 2009 ? 202.694 181.451 153.113 1.00 87.74  ? 2009 SER A C     1 
ATOM   4435  O  O     . SER A 1 2009 ? 201.908 180.838 153.840 1.00 93.53  ? 2009 SER A O     1 
ATOM   4436  C  CB    . SER A 1 2009 ? 201.693 183.600 152.339 1.00 78.44  ? 2009 SER A CB    1 
ATOM   4437  O  OG    . SER A 1 2009 ? 202.740 184.337 152.945 1.00 83.74  ? 2009 SER A OG    1 
ATOM   4438  N  N     . PRO A 1 2010 ? 204.013 181.459 153.328 1.00 84.21  ? 2010 PRO A N     1 
ATOM   4439  C  CA    . PRO A 1 2010 ? 204.578 180.715 154.467 1.00 82.60  ? 2010 PRO A CA    1 
ATOM   4440  C  C     . PRO A 1 2010 ? 204.012 181.128 155.815 1.00 87.85  ? 2010 PRO A C     1 
ATOM   4441  O  O     . PRO A 1 2010 ? 203.882 180.272 156.699 1.00 88.95  ? 2010 PRO A O     1 
ATOM   4442  C  CB    . PRO A 1 2010 ? 206.080 181.031 154.397 1.00 85.94  ? 2010 PRO A CB    1 
ATOM   4443  C  CG    . PRO A 1 2010 ? 206.302 181.811 153.138 1.00 84.72  ? 2010 PRO A CG    1 
ATOM   4444  C  CD    . PRO A 1 2010 ? 205.037 181.860 152.352 1.00 81.26  ? 2010 PRO A CD    1 
ATOM   4445  N  N     . ASP A 1 2011 ? 203.671 182.402 156.001 1.00 79.04  ? 2011 ASP A N     1 
ATOM   4446  C  CA    . ASP A 1 2011 ? 203.311 182.933 157.310 1.00 78.39  ? 2011 ASP A CA    1 
ATOM   4447  C  C     . ASP A 1 2011 ? 201.976 182.420 157.835 1.00 84.84  ? 2011 ASP A C     1 
ATOM   4448  O  O     . ASP A 1 2011 ? 201.680 182.626 159.016 1.00 91.95  ? 2011 ASP A O     1 
ATOM   4449  C  CB    . ASP A 1 2011 ? 203.277 184.462 157.260 1.00 79.90  ? 2011 ASP A CB    1 
ATOM   4450  C  CG    . ASP A 1 2011 ? 204.648 185.069 157.038 1.00 86.97  ? 2011 ASP A CG    1 
ATOM   4451  O  OD1   . ASP A 1 2011 ? 205.548 184.346 156.561 1.00 86.13  ? 2011 ASP A OD1   1 
ATOM   4452  O  OD2   . ASP A 1 2011 ? 204.825 186.267 157.342 1.00 87.83  ? 2011 ASP A OD2   1 
ATOM   4453  N  N     . MET A 1 2012 ? 201.170 181.762 157.009 1.00 68.18  ? 2012 MET A N     1 
ATOM   4454  C  CA    . MET A 1 2012 ? 199.815 181.417 157.408 1.00 63.32  ? 2012 MET A CA    1 
ATOM   4455  C  C     . MET A 1 2012 ? 199.793 180.184 158.304 1.00 64.48  ? 2012 MET A C     1 
ATOM   4456  O  O     . MET A 1 2012 ? 200.737 179.388 158.332 1.00 65.92  ? 2012 MET A O     1 
ATOM   4457  C  CB    . MET A 1 2012 ? 198.941 181.171 156.182 1.00 60.15  ? 2012 MET A CB    1 
ATOM   4458  C  CG    . MET A 1 2012 ? 199.031 179.763 155.642 1.00 58.82  ? 2012 MET A CG    1 
ATOM   4459  S  SD    . MET A 1 2012 ? 197.558 179.337 154.708 1.00 84.69  ? 2012 MET A SD    1 
ATOM   4460  C  CE    . MET A 1 2012 ? 196.526 178.675 156.010 1.00 69.05  ? 2012 MET A CE    1 
ATOM   4461  N  N     . ALA A 1 2013 ? 198.698 180.040 159.048 1.00 57.63  ? 2013 ALA A N     1 
ATOM   4462  C  CA    . ALA A 1 2013 ? 198.470 178.882 159.898 1.00 50.20  ? 2013 ALA A CA    1 
ATOM   4463  C  C     . ALA A 1 2013 ? 196.982 178.780 160.194 1.00 46.84  ? 2013 ALA A C     1 
ATOM   4464  O  O     . ALA A 1 2013 ? 196.238 179.756 160.074 1.00 62.76  ? 2013 ALA A O     1 
ATOM   4465  C  CB    . ALA A 1 2013 ? 199.273 178.966 161.199 1.00 52.46  ? 2013 ALA A CB    1 
ATOM   4466  N  N     . ILE A 1 2014 ? 196.552 177.584 160.589 1.00 46.61  ? 2014 ILE A N     1 
ATOM   4467  C  CA    . ILE A 1 2014 ? 195.150 177.305 160.887 1.00 45.79  ? 2014 ILE A CA    1 
ATOM   4468  C  C     . ILE A 1 2014 ? 195.077 176.840 162.335 1.00 51.84  ? 2014 ILE A C     1 
ATOM   4469  O  O     . ILE A 1 2014 ? 195.453 175.706 162.649 1.00 63.06  ? 2014 ILE A O     1 
ATOM   4470  C  CB    . ILE A 1 2014 ? 194.548 176.257 159.945 1.00 47.06  ? 2014 ILE A CB    1 
ATOM   4471  C  CG1   . ILE A 1 2014 ? 194.685 176.702 158.490 1.00 55.61  ? 2014 ILE A CG1   1 
ATOM   4472  C  CG2   . ILE A 1 2014 ? 193.089 176.009 160.289 1.00 44.08  ? 2014 ILE A CG2   1 
ATOM   4473  C  CD1   . ILE A 1 2014 ? 195.215 175.622 157.578 1.00 58.34  ? 2014 ILE A CD1   1 
ATOM   4474  N  N     . PHE A 1 2015 ? 194.590 177.705 163.218 1.00 35.98  ? 2015 PHE A N     1 
ATOM   4475  C  CA    . PHE A 1 2015 ? 194.346 177.351 164.609 1.00 31.78  ? 2015 PHE A CA    1 
ATOM   4476  C  C     . PHE A 1 2015 ? 192.849 177.223 164.847 1.00 40.88  ? 2015 PHE A C     1 
ATOM   4477  O  O     . PHE A 1 2015 ? 192.075 178.098 164.447 1.00 57.20  ? 2015 PHE A O     1 
ATOM   4478  C  CB    . PHE A 1 2015 ? 194.939 178.387 165.565 1.00 43.81  ? 2015 PHE A CB    1 
ATOM   4479  C  CG    . PHE A 1 2015 ? 196.437 178.401 165.595 1.00 35.90  ? 2015 PHE A CG    1 
ATOM   4480  C  CD1   . PHE A 1 2015 ? 197.162 178.999 164.582 1.00 42.98  ? 2015 PHE A CD1   1 
ATOM   4481  C  CD2   . PHE A 1 2015 ? 197.122 177.812 166.643 1.00 40.18  ? 2015 PHE A CD2   1 
ATOM   4482  C  CE1   . PHE A 1 2015 ? 198.540 179.011 164.616 1.00 56.88  ? 2015 PHE A CE1   1 
ATOM   4483  C  CE2   . PHE A 1 2015 ? 198.499 177.819 166.680 1.00 49.36  ? 2015 PHE A CE2   1 
ATOM   4484  C  CZ    . PHE A 1 2015 ? 199.209 178.419 165.665 1.00 56.22  ? 2015 PHE A CZ    1 
ATOM   4485  N  N     . ILE A 1 2016 ? 192.448 176.132 165.489 1.00 32.14  ? 2016 ILE A N     1 
ATOM   4486  C  CA    . ILE A 1 2016 ? 191.058 175.888 165.853 1.00 26.48  ? 2016 ILE A CA    1 
ATOM   4487  C  C     . ILE A 1 2016 ? 191.001 175.699 167.361 1.00 47.91  ? 2016 ILE A C     1 
ATOM   4488  O  O     . ILE A 1 2016 ? 191.784 174.929 167.928 1.00 70.43  ? 2016 ILE A O     1 
ATOM   4489  C  CB    . ILE A 1 2016 ? 190.484 174.673 165.109 1.00 37.85  ? 2016 ILE A CB    1 
ATOM   4490  C  CG1   . ILE A 1 2016 ? 191.344 173.432 165.355 1.00 45.09  ? 2016 ILE A CG1   1 
ATOM   4491  C  CG2   . ILE A 1 2016 ? 190.400 174.957 163.621 1.00 51.15  ? 2016 ILE A CG2   1 
ATOM   4492  C  CD1   . ILE A 1 2016 ? 190.765 172.163 164.786 1.00 48.18  ? 2016 ILE A CD1   1 
ATOM   4493  N  N     . THR A 1 2017 ? 190.101 176.419 168.019 1.00 51.32  ? 2017 THR A N     1 
ATOM   4494  C  CA    . THR A 1 2017 ? 189.896 176.268 169.451 1.00 43.18  ? 2017 THR A CA    1 
ATOM   4495  C  C     . THR A 1 2017 ? 188.459 175.840 169.712 1.00 49.19  ? 2017 THR A C     1 
ATOM   4496  O  O     . THR A 1 2017 ? 187.518 176.372 169.117 1.00 62.25  ? 2017 THR A O     1 
ATOM   4497  C  CB    . THR A 1 2017 ? 190.200 177.566 170.204 1.00 55.33  ? 2017 THR A CB    1 
ATOM   4498  O  OG1   . THR A 1 2017 ? 189.054 178.422 170.171 1.00 66.02  ? 2017 THR A OG1   1 
ATOM   4499  C  CG2   . THR A 1 2017 ? 191.379 178.289 169.568 1.00 51.59  ? 2017 THR A CG2   1 
ATOM   4500  N  N     . MET A 1 2018 ? 188.295 174.872 170.609 1.00 52.73  ? 2018 MET A N     1 
ATOM   4501  C  CA    . MET A 1 2018 ? 186.982 174.292 170.839 1.00 67.15  ? 2018 MET A CA    1 
ATOM   4502  C  C     . MET A 1 2018 ? 186.839 173.919 172.306 1.00 64.84  ? 2018 MET A C     1 
ATOM   4503  O  O     . MET A 1 2018 ? 187.832 173.644 172.983 1.00 65.86  ? 2018 MET A O     1 
ATOM   4504  C  CB    . MET A 1 2018 ? 186.763 173.059 169.955 1.00 66.24  ? 2018 MET A CB    1 
ATOM   4505  C  CG    . MET A 1 2018 ? 187.568 171.842 170.378 1.00 66.35  ? 2018 MET A CG    1 
ATOM   4506  S  SD    . MET A 1 2018 ? 187.869 170.699 169.021 1.00 66.20  ? 2018 MET A SD    1 
ATOM   4507  C  CE    . MET A 1 2018 ? 188.671 171.787 167.849 1.00 55.39  ? 2018 MET A CE    1 
ATOM   4508  N  N     . ASN A 1 2019 ? 185.600 173.922 172.787 1.00 65.20  ? 2019 ASN A N     1 
ATOM   4509  C  CA    . ASN A 1 2019 ? 185.286 173.474 174.135 1.00 59.96  ? 2019 ASN A CA    1 
ATOM   4510  C  C     . ASN A 1 2019 ? 184.628 172.102 174.066 1.00 63.25  ? 2019 ASN A C     1 
ATOM   4511  O  O     . ASN A 1 2019 ? 183.501 171.979 173.569 1.00 76.46  ? 2019 ASN A O     1 
ATOM   4512  C  CB    . ASN A 1 2019 ? 184.375 174.477 174.843 1.00 65.09  ? 2019 ASN A CB    1 
ATOM   4513  C  CG    . ASN A 1 2019 ? 184.687 175.911 174.468 1.00 70.44  ? 2019 ASN A CG    1 
ATOM   4514  O  OD1   . ASN A 1 2019 ? 185.832 176.253 174.179 1.00 75.46  ? 2019 ASN A OD1   1 
ATOM   4515  N  ND2   . ASN A 1 2019 ? 183.666 176.759 174.470 1.00 65.95  ? 2019 ASN A ND2   1 
ATOM   4516  N  N     . PRO A 1 2020 ? 185.289 171.052 174.551 1.00 70.84  ? 2020 PRO A N     1 
ATOM   4517  C  CA    . PRO A 1 2020 ? 184.721 169.705 174.427 1.00 76.56  ? 2020 PRO A CA    1 
ATOM   4518  C  C     . PRO A 1 2020 ? 183.674 169.446 175.500 1.00 79.84  ? 2020 PRO A C     1 
ATOM   4519  O  O     . PRO A 1 2020 ? 183.871 169.769 176.673 1.00 78.26  ? 2020 PRO A O     1 
ATOM   4520  C  CB    . PRO A 1 2020 ? 185.942 168.788 174.591 1.00 77.10  ? 2020 PRO A CB    1 
ATOM   4521  C  CG    . PRO A 1 2020 ? 187.123 169.717 174.910 1.00 79.92  ? 2020 PRO A CG    1 
ATOM   4522  C  CD    . PRO A 1 2020 ? 186.538 171.028 175.320 1.00 77.32  ? 2020 PRO A CD    1 
ATOM   4523  N  N     . GLY A 1 2021 ? 182.553 168.857 175.085 1.00 88.50  ? 2021 GLY A N     1 
ATOM   4524  C  CA    . GLY A 1 2021 ? 181.483 168.489 175.981 1.00 87.72  ? 2021 GLY A CA    1 
ATOM   4525  C  C     . GLY A 1 2021 ? 180.406 169.540 176.153 1.00 85.17  ? 2021 GLY A C     1 
ATOM   4526  O  O     . GLY A 1 2021 ? 179.366 169.246 176.753 1.00 89.10  ? 2021 GLY A O     1 
ATOM   4527  N  N     . TYR A 1 2022 ? 180.624 170.750 175.648 1.00 81.11  ? 2022 TYR A N     1 
ATOM   4528  C  CA    . TYR A 1 2022 ? 179.626 171.799 175.776 1.00 81.37  ? 2022 TYR A CA    1 
ATOM   4529  C  C     . TYR A 1 2022 ? 178.433 171.523 174.864 1.00 87.52  ? 2022 TYR A C     1 
ATOM   4530  O  O     . TYR A 1 2022 ? 178.509 170.745 173.909 1.00 89.57  ? 2022 TYR A O     1 
ATOM   4531  C  CB    . TYR A 1 2022 ? 180.234 173.165 175.454 1.00 84.14  ? 2022 TYR A CB    1 
ATOM   4532  C  CG    . TYR A 1 2022 ? 180.960 173.801 176.617 1.00 81.81  ? 2022 TYR A CG    1 
ATOM   4533  C  CD1   . TYR A 1 2022 ? 181.610 173.023 177.565 1.00 86.97  ? 2022 TYR A CD1   1 
ATOM   4534  C  CD2   . TYR A 1 2022 ? 180.993 175.179 176.769 1.00 82.11  ? 2022 TYR A CD2   1 
ATOM   4535  C  CE1   . TYR A 1 2022 ? 182.273 173.599 178.629 1.00 88.05  ? 2022 TYR A CE1   1 
ATOM   4536  C  CE2   . TYR A 1 2022 ? 181.654 175.764 177.830 1.00 86.50  ? 2022 TYR A CE2   1 
ATOM   4537  C  CZ    . TYR A 1 2022 ? 182.292 174.969 178.757 1.00 89.48  ? 2022 TYR A CZ    1 
ATOM   4538  O  OH    . TYR A 1 2022 ? 182.952 175.545 179.817 1.00 92.50  ? 2022 TYR A OH    1 
ATOM   4539  N  N     . ALA A 1 2023 ? 177.315 172.168 175.182 1.00 91.44  ? 2023 ALA A N     1 
ATOM   4540  C  CA    . ALA A 1 2023 ? 176.098 171.987 174.408 1.00 87.65  ? 2023 ALA A CA    1 
ATOM   4541  C  C     . ALA A 1 2023 ? 176.223 172.646 173.038 1.00 88.90  ? 2023 ALA A C     1 
ATOM   4542  O  O     . ALA A 1 2023 ? 176.923 173.646 172.857 1.00 89.30  ? 2023 ALA A O     1 
ATOM   4543  C  CB    . ALA A 1 2023 ? 174.895 172.559 175.158 1.00 85.17  ? 2023 ALA A CB    1 
ATOM   4544  N  N     . GLY A 1 2024 ? 175.524 172.069 172.065 1.00 87.90  ? 2024 GLY A N     1 
ATOM   4545  C  CA    . GLY A 1 2024 ? 175.536 172.601 170.713 1.00 89.70  ? 2024 GLY A CA    1 
ATOM   4546  C  C     . GLY A 1 2024 ? 176.873 172.499 170.015 1.00 92.75  ? 2024 GLY A C     1 
ATOM   4547  O  O     . GLY A 1 2024 ? 177.227 173.390 169.236 1.00 96.86  ? 2024 GLY A O     1 
ATOM   4548  N  N     . ARG A 1 2025 ? 177.627 171.432 170.270 1.00 82.44  ? 2025 ARG A N     1 
ATOM   4549  C  CA    . ARG A 1 2025 ? 178.914 171.205 169.629 1.00 79.96  ? 2025 ARG A CA    1 
ATOM   4550  C  C     . ARG A 1 2025 ? 178.927 169.820 169.004 1.00 83.97  ? 2025 ARG A C     1 
ATOM   4551  O  O     . ARG A 1 2025 ? 178.357 168.875 169.555 1.00 84.51  ? 2025 ARG A O     1 
ATOM   4552  C  CB    . ARG A 1 2025 ? 180.073 171.331 170.625 1.00 81.15  ? 2025 ARG A CB    1 
ATOM   4553  C  CG    . ARG A 1 2025 ? 179.937 172.472 171.618 1.00 75.43  ? 2025 ARG A CG    1 
ATOM   4554  C  CD    . ARG A 1 2025 ? 180.009 173.823 170.933 1.00 78.32  ? 2025 ARG A CD    1 
ATOM   4555  N  NE    . ARG A 1 2025 ? 179.674 174.905 171.850 1.00 82.39  ? 2025 ARG A NE    1 
ATOM   4556  C  CZ    . ARG A 1 2025 ? 180.529 175.833 172.253 1.00 85.90  ? 2025 ARG A CZ    1 
ATOM   4557  N  NH1   . ARG A 1 2025 ? 181.783 175.848 171.831 1.00 84.07  ? 2025 ARG A NH1   1 
ATOM   4558  N  NH2   . ARG A 1 2025 ? 180.118 176.768 173.104 1.00 83.14  ? 2025 ARG A NH2   1 
ATOM   4559  N  N     . SER A 1 2026 ? 179.582 169.705 167.854 1.00 81.08  ? 2026 SER A N     1 
ATOM   4560  C  CA    . SER A 1 2026 ? 179.689 168.448 167.137 1.00 78.13  ? 2026 SER A CA    1 
ATOM   4561  C  C     . SER A 1 2026 ? 180.974 167.727 167.541 1.00 75.09  ? 2026 SER A C     1 
ATOM   4562  O  O     . SER A 1 2026 ? 181.664 168.115 168.488 1.00 76.16  ? 2026 SER A O     1 
ATOM   4563  C  CB    . SER A 1 2026 ? 179.631 168.702 165.631 1.00 74.25  ? 2026 SER A CB    1 
ATOM   4564  O  OG    . SER A 1 2026 ? 178.470 169.437 165.284 1.00 77.65  ? 2026 SER A OG    1 
ATOM   4565  N  N     . ASN A 1 2027 ? 181.298 166.658 166.820 1.00 80.73  ? 2027 ASN A N     1 
ATOM   4566  C  CA    . ASN A 1 2027 ? 182.541 165.929 167.005 1.00 81.90  ? 2027 ASN A CA    1 
ATOM   4567  C  C     . ASN A 1 2027 ? 183.399 166.069 165.756 1.00 84.35  ? 2027 ASN A C     1 
ATOM   4568  O  O     . ASN A 1 2027 ? 182.891 166.217 164.641 1.00 93.19  ? 2027 ASN A O     1 
ATOM   4569  C  CB    . ASN A 1 2027 ? 182.286 164.446 167.303 1.00 82.74  ? 2027 ASN A CB    1 
ATOM   4570  C  CG    . ASN A 1 2027 ? 181.296 164.238 168.430 1.00 90.31  ? 2027 ASN A CG    1 
ATOM   4571  O  OD1   . ASN A 1 2027 ? 181.514 164.690 169.554 1.00 93.45  ? 2027 ASN A OD1   1 
ATOM   4572  N  ND2   . ASN A 1 2027 ? 180.201 163.548 168.136 1.00 91.12  ? 2027 ASN A ND2   1 
ATOM   4573  N  N     . LEU A 1 2028 ? 184.711 166.019 165.952 1.00 65.89  ? 2028 LEU A N     1 
ATOM   4574  C  CA    . LEU A 1 2028 ? 185.649 166.155 164.852 1.00 66.95  ? 2028 LEU A CA    1 
ATOM   4575  C  C     . LEU A 1 2028 ? 186.053 164.784 164.339 1.00 73.77  ? 2028 LEU A C     1 
ATOM   4576  O  O     . LEU A 1 2028 ? 186.521 163.948 165.124 1.00 79.26  ? 2028 LEU A O     1 
ATOM   4577  C  CB    . LEU A 1 2028 ? 186.892 166.937 165.289 1.00 63.82  ? 2028 LEU A CB    1 
ATOM   4578  C  CG    . LEU A 1 2028 ? 186.809 168.462 165.203 1.00 58.70  ? 2028 LEU A CG    1 
ATOM   4579  C  CD1   . LEU A 1 2028 ? 185.944 169.027 166.317 1.00 74.99  ? 2028 LEU A CD1   1 
ATOM   4580  C  CD2   . LEU A 1 2028 ? 188.197 169.079 165.236 1.00 67.92  ? 2028 LEU A CD2   1 
ATOM   4581  N  N     . PRO A 1 2029 ? 185.878 164.510 163.047 1.00 65.10  ? 2029 PRO A N     1 
ATOM   4582  C  CA    . PRO A 1 2029 ? 186.286 163.208 162.509 1.00 67.04  ? 2029 PRO A CA    1 
ATOM   4583  C  C     . PRO A 1 2029 ? 187.789 163.008 162.626 1.00 70.83  ? 2029 PRO A C     1 
ATOM   4584  O  O     . PRO A 1 2029 ? 188.567 163.964 162.632 1.00 79.43  ? 2029 PRO A O     1 
ATOM   4585  C  CB    . PRO A 1 2029 ? 185.837 163.269 161.045 1.00 70.93  ? 2029 PRO A CB    1 
ATOM   4586  C  CG    . PRO A 1 2029 ? 185.670 164.721 160.748 1.00 69.68  ? 2029 PRO A CG    1 
ATOM   4587  C  CD    . PRO A 1 2029 ? 185.248 165.363 162.028 1.00 61.20  ? 2029 PRO A CD    1 
ATOM   4588  N  N     . ASP A 1 2030 ? 188.191 161.738 162.726 1.00 75.72  ? 2030 ASP A N     1 
ATOM   4589  C  CA    . ASP A 1 2030 ? 189.590 161.416 162.990 1.00 79.16  ? 2030 ASP A CA    1 
ATOM   4590  C  C     . ASP A 1 2030 ? 190.513 161.903 161.881 1.00 81.50  ? 2030 ASP A C     1 
ATOM   4591  O  O     . ASP A 1 2030 ? 191.682 162.207 162.141 1.00 88.18  ? 2030 ASP A O     1 
ATOM   4592  C  CB    . ASP A 1 2030 ? 189.750 159.910 163.191 1.00 84.27  ? 2030 ASP A CB    1 
ATOM   4593  C  CG    . ASP A 1 2030 ? 189.084 159.419 164.461 1.00 87.26  ? 2030 ASP A CG    1 
ATOM   4594  O  OD1   . ASP A 1 2030 ? 188.676 160.265 165.284 1.00 84.39  ? 2030 ASP A OD1   1 
ATOM   4595  O  OD2   . ASP A 1 2030 ? 188.967 158.188 164.636 1.00 89.96  ? 2030 ASP A OD2   1 
ATOM   4596  N  N     . ASN A 1 2031 ? 190.020 161.982 160.642 1.00 67.44  ? 2031 ASN A N     1 
ATOM   4597  C  CA    . ASN A 1 2031 ? 190.849 162.510 159.565 1.00 66.08  ? 2031 ASN A CA    1 
ATOM   4598  C  C     . ASN A 1 2031 ? 191.101 164.003 159.715 1.00 72.81  ? 2031 ASN A C     1 
ATOM   4599  O  O     . ASN A 1 2031 ? 192.023 164.529 159.082 1.00 76.80  ? 2031 ASN A O     1 
ATOM   4600  C  CB    . ASN A 1 2031 ? 190.210 162.225 158.205 1.00 70.11  ? 2031 ASN A CB    1 
ATOM   4601  C  CG    . ASN A 1 2031 ? 188.953 163.032 157.969 1.00 71.37  ? 2031 ASN A CG    1 
ATOM   4602  O  OD1   . ASN A 1 2031 ? 188.017 162.987 158.764 1.00 68.76  ? 2031 ASN A OD1   1 
ATOM   4603  N  ND2   . ASN A 1 2031 ? 188.924 163.776 156.871 1.00 67.47  ? 2031 ASN A ND2   1 
ATOM   4604  N  N     . LEU A 1 2032 ? 190.306 164.693 160.531 1.00 59.73  ? 2032 LEU A N     1 
ATOM   4605  C  CA    . LEU A 1 2032 ? 190.516 166.111 160.793 1.00 54.99  ? 2032 LEU A CA    1 
ATOM   4606  C  C     . LEU A 1 2032 ? 191.320 166.346 162.065 1.00 50.62  ? 2032 LEU A C     1 
ATOM   4607  O  O     . LEU A 1 2032 ? 192.108 167.295 162.132 1.00 64.37  ? 2032 LEU A O     1 
ATOM   4608  C  CB    . LEU A 1 2032 ? 189.168 166.832 160.884 1.00 52.17  ? 2032 LEU A CB    1 
ATOM   4609  C  CG    . LEU A 1 2032 ? 189.195 168.328 161.200 1.00 57.30  ? 2032 LEU A CG    1 
ATOM   4610  C  CD1   . LEU A 1 2032 ? 189.890 169.093 160.091 1.00 58.75  ? 2032 LEU A CD1   1 
ATOM   4611  C  CD2   . LEU A 1 2032 ? 187.787 168.852 161.411 1.00 60.15  ? 2032 LEU A CD2   1 
ATOM   4612  N  N     . LYS A 1 2033 ? 191.146 165.491 163.075 1.00 42.76  ? 2033 LYS A N     1 
ATOM   4613  C  CA    . LYS A 1 2033 ? 191.887 165.661 164.320 1.00 52.44  ? 2033 LYS A CA    1 
ATOM   4614  C  C     . LYS A 1 2033 ? 193.368 165.357 164.143 1.00 60.56  ? 2033 LYS A C     1 
ATOM   4615  O  O     . LYS A 1 2033 ? 194.205 165.944 164.836 1.00 65.16  ? 2033 LYS A O     1 
ATOM   4616  C  CB    . LYS A 1 2033 ? 191.291 164.776 165.414 1.00 57.91  ? 2033 LYS A CB    1 
ATOM   4617  C  CG    . LYS A 1 2033 ? 190.096 165.391 166.119 1.00 57.98  ? 2033 LYS A CG    1 
ATOM   4618  C  CD    . LYS A 1 2033 ? 189.743 164.626 167.383 1.00 55.42  ? 2033 LYS A CD    1 
ATOM   4619  C  CE    . LYS A 1 2033 ? 189.147 163.269 167.060 1.00 59.87  ? 2033 LYS A CE    1 
ATOM   4620  N  NZ    . LYS A 1 2033 ? 188.610 162.599 168.276 1.00 63.43  ? 2033 LYS A NZ    1 
ATOM   4621  N  N     . LYS A 1 2034 ? 193.712 164.449 163.229 1.00 59.65  ? 2034 LYS A N     1 
ATOM   4622  C  CA    . LYS A 1 2034 ? 195.111 164.119 162.989 1.00 50.43  ? 2034 LYS A CA    1 
ATOM   4623  C  C     . LYS A 1 2034 ? 195.880 165.252 162.324 1.00 54.89  ? 2034 LYS A C     1 
ATOM   4624  O  O     . LYS A 1 2034 ? 197.113 165.192 162.270 1.00 64.70  ? 2034 LYS A O     1 
ATOM   4625  C  CB    . LYS A 1 2034 ? 195.210 162.849 162.140 1.00 53.92  ? 2034 LYS A CB    1 
ATOM   4626  C  CG    . LYS A 1 2034 ? 195.318 163.096 160.644 1.00 63.21  ? 2034 LYS A CG    1 
ATOM   4627  C  CD    . LYS A 1 2034 ? 195.277 161.790 159.868 1.00 65.53  ? 2034 LYS A CD    1 
ATOM   4628  C  CE    . LYS A 1 2034 ? 195.480 162.022 158.379 1.00 65.84  ? 2034 LYS A CE    1 
ATOM   4629  N  NZ    . LYS A 1 2034 ? 194.468 162.958 157.817 1.00 72.21  ? 2034 LYS A NZ    1 
ATOM   4630  N  N     . LEU A 1 2035 ? 195.193 166.276 161.824 1.00 46.74  ? 2035 LEU A N     1 
ATOM   4631  C  CA    . LEU A 1 2035 ? 195.837 167.416 161.189 1.00 43.30  ? 2035 LEU A CA    1 
ATOM   4632  C  C     . LEU A 1 2035 ? 196.191 168.523 162.172 1.00 59.62  ? 2035 LEU A C     1 
ATOM   4633  O  O     . LEU A 1 2035 ? 196.815 169.510 161.770 1.00 73.60  ? 2035 LEU A O     1 
ATOM   4634  C  CB    . LEU A 1 2035 ? 194.935 167.984 160.089 1.00 38.79  ? 2035 LEU A CB    1 
ATOM   4635  C  CG    . LEU A 1 2035 ? 194.462 167.005 159.015 1.00 54.31  ? 2035 LEU A CG    1 
ATOM   4636  C  CD1   . LEU A 1 2035 ? 193.414 167.654 158.129 1.00 54.48  ? 2035 LEU A CD1   1 
ATOM   4637  C  CD2   . LEU A 1 2035 ? 195.636 166.511 158.189 1.00 61.07  ? 2035 LEU A CD2   1 
ATOM   4638  N  N     . PHE A 1 2036 ? 195.814 168.388 163.441 1.00 49.42  ? 2036 PHE A N     1 
ATOM   4639  C  CA    . PHE A 1 2036 ? 196.029 169.426 164.439 1.00 38.15  ? 2036 PHE A CA    1 
ATOM   4640  C  C     . PHE A 1 2036 ? 196.701 168.835 165.668 1.00 36.31  ? 2036 PHE A C     1 
ATOM   4641  O  O     . PHE A 1 2036 ? 196.390 167.714 166.079 1.00 46.75  ? 2036 PHE A O     1 
ATOM   4642  C  CB    . PHE A 1 2036 ? 194.707 170.090 164.844 1.00 47.50  ? 2036 PHE A CB    1 
ATOM   4643  C  CG    . PHE A 1 2036 ? 194.017 170.807 163.720 1.00 45.27  ? 2036 PHE A CG    1 
ATOM   4644  C  CD1   . PHE A 1 2036 ? 193.085 170.155 162.935 1.00 46.42  ? 2036 PHE A CD1   1 
ATOM   4645  C  CD2   . PHE A 1 2036 ? 194.293 172.135 163.456 1.00 45.01  ? 2036 PHE A CD2   1 
ATOM   4646  C  CE1   . PHE A 1 2036 ? 192.448 170.812 161.904 1.00 40.38  ? 2036 PHE A CE1   1 
ATOM   4647  C  CE2   . PHE A 1 2036 ? 193.659 172.797 162.425 1.00 47.80  ? 2036 PHE A CE2   1 
ATOM   4648  C  CZ    . PHE A 1 2036 ? 192.735 172.134 161.649 1.00 41.93  ? 2036 PHE A CZ    1 
ATOM   4649  N  N     . ARG A 1 2037 ? 197.622 169.596 166.252 1.00 47.88  ? 2037 ARG A N     1 
ATOM   4650  C  CA    . ARG A 1 2037 ? 198.276 169.213 167.496 1.00 48.29  ? 2037 ARG A CA    1 
ATOM   4651  C  C     . ARG A 1 2037 ? 197.504 169.815 168.663 1.00 57.22  ? 2037 ARG A C     1 
ATOM   4652  O  O     . ARG A 1 2037 ? 197.625 171.013 168.941 1.00 62.94  ? 2037 ARG A O     1 
ATOM   4653  C  CB    . ARG A 1 2037 ? 199.729 169.683 167.511 1.00 50.19  ? 2037 ARG A CB    1 
ATOM   4654  C  CG    . ARG A 1 2037 ? 200.611 168.955 168.507 1.00 57.16  ? 2037 ARG A CG    1 
ATOM   4655  C  CD    . ARG A 1 2037 ? 201.084 167.623 167.956 1.00 53.38  ? 2037 ARG A CD    1 
ATOM   4656  N  NE    . ARG A 1 2037 ? 202.223 167.779 167.059 1.00 63.48  ? 2037 ARG A NE    1 
ATOM   4657  C  CZ    . ARG A 1 2037 ? 203.476 167.941 167.461 1.00 67.97  ? 2037 ARG A CZ    1 
ATOM   4658  N  NH1   . ARG A 1 2037 ? 203.792 167.976 168.745 1.00 63.85  ? 2037 ARG A NH1   1 
ATOM   4659  N  NH2   . ARG A 1 2037 ? 204.438 168.069 166.551 1.00 64.18  ? 2037 ARG A NH2   1 
ATOM   4660  N  N     . SER A 1 2038 ? 196.723 168.987 169.347 1.00 55.52  ? 2038 SER A N     1 
ATOM   4661  C  CA    . SER A 1 2038 ? 195.831 169.447 170.399 1.00 54.02  ? 2038 SER A CA    1 
ATOM   4662  C  C     . SER A 1 2038 ? 196.597 169.707 171.689 1.00 56.42  ? 2038 SER A C     1 
ATOM   4663  O  O     . SER A 1 2038 ? 197.654 169.123 171.937 1.00 61.69  ? 2038 SER A O     1 
ATOM   4664  C  CB    . SER A 1 2038 ? 194.720 168.428 170.654 1.00 55.70  ? 2038 SER A CB    1 
ATOM   4665  O  OG    . SER A 1 2038 ? 195.233 167.260 171.267 1.00 63.88  ? 2038 SER A OG    1 
ATOM   4666  N  N     . LEU A 1 2039 ? 196.047 170.600 172.509 1.00 52.13  ? 2039 LEU A N     1 
ATOM   4667  C  CA    . LEU A 1 2039 ? 196.613 170.933 173.808 1.00 54.43  ? 2039 LEU A CA    1 
ATOM   4668  C  C     . LEU A 1 2039 ? 195.478 171.178 174.788 1.00 59.44  ? 2039 LEU A C     1 
ATOM   4669  O  O     . LEU A 1 2039 ? 194.495 171.840 174.445 1.00 64.81  ? 2039 LEU A O     1 
ATOM   4670  C  CB    . LEU A 1 2039 ? 197.513 172.169 173.722 1.00 49.94  ? 2039 LEU A CB    1 
ATOM   4671  C  CG    . LEU A 1 2039 ? 197.818 172.848 175.056 1.00 61.23  ? 2039 LEU A CG    1 
ATOM   4672  C  CD1   . LEU A 1 2039 ? 198.787 172.009 175.875 1.00 59.98  ? 2039 LEU A CD1   1 
ATOM   4673  C  CD2   . LEU A 1 2039 ? 198.356 174.242 174.834 1.00 62.61  ? 2039 LEU A CD2   1 
ATOM   4674  N  N     . ALA A 1 2040 ? 195.616 170.654 176.004 1.00 61.80  ? 2040 ALA A N     1 
ATOM   4675  C  CA    . ALA A 1 2040 ? 194.572 170.775 177.016 1.00 59.93  ? 2040 ALA A CA    1 
ATOM   4676  C  C     . ALA A 1 2040 ? 194.817 172.025 177.853 1.00 67.34  ? 2040 ALA A C     1 
ATOM   4677  O  O     . ALA A 1 2040 ? 195.845 172.139 178.528 1.00 75.12  ? 2040 ALA A O     1 
ATOM   4678  C  CB    . ALA A 1 2040 ? 194.536 169.530 177.895 1.00 64.27  ? 2040 ALA A CB    1 
ATOM   4679  N  N     . MET A 1 2041 ? 193.875 172.961 177.810 1.00 63.53  ? 2041 MET A N     1 
ATOM   4680  C  CA    . MET A 1 2041 ? 193.905 174.178 178.618 1.00 61.10  ? 2041 MET A CA    1 
ATOM   4681  C  C     . MET A 1 2041 ? 192.728 174.129 179.588 1.00 64.27  ? 2041 MET A C     1 
ATOM   4682  O  O     . MET A 1 2041 ? 191.613 174.531 179.254 1.00 71.72  ? 2041 MET A O     1 
ATOM   4683  C  CB    . MET A 1 2041 ? 193.847 175.421 177.746 1.00 58.95  ? 2041 MET A CB    1 
ATOM   4684  C  CG    . MET A 1 2041 ? 195.182 175.866 177.202 1.00 60.22  ? 2041 MET A CG    1 
ATOM   4685  S  SD    . MET A 1 2041 ? 194.975 177.203 176.020 1.00 71.63  ? 2041 MET A SD    1 
ATOM   4686  C  CE    . MET A 1 2041 ? 196.587 177.958 176.111 1.00 64.57  ? 2041 MET A CE    1 
ATOM   4687  N  N     . THR A 1 2042 ? 192.984 173.638 180.794 1.00 71.55  ? 2042 THR A N     1 
ATOM   4688  C  CA    . THR A 1 2042 ? 191.942 173.491 181.803 1.00 75.53  ? 2042 THR A CA    1 
ATOM   4689  C  C     . THR A 1 2042 ? 192.139 174.380 183.018 1.00 76.92  ? 2042 THR A C     1 
ATOM   4690  O  O     . THR A 1 2042 ? 191.161 174.916 183.545 1.00 76.86  ? 2042 THR A O     1 
ATOM   4691  C  CB    . THR A 1 2042 ? 191.854 172.028 182.259 1.00 77.29  ? 2042 THR A CB    1 
ATOM   4692  O  OG1   . THR A 1 2042 ? 193.167 171.542 182.565 1.00 78.68  ? 2042 THR A OG1   1 
ATOM   4693  C  CG2   . THR A 1 2042 ? 191.241 171.167 181.167 1.00 72.15  ? 2042 THR A CG2   1 
ATOM   4694  N  N     . LYS A 1 2043 ? 193.377 174.552 183.486 1.00 85.89  ? 2043 LYS A N     1 
ATOM   4695  C  CA    . LYS A 1 2043 ? 193.665 175.274 184.725 1.00 82.56  ? 2043 LYS A CA    1 
ATOM   4696  C  C     . LYS A 1 2043 ? 194.667 176.389 184.458 1.00 82.14  ? 2043 LYS A C     1 
ATOM   4697  O  O     . LYS A 1 2043 ? 195.884 176.185 184.585 1.00 84.57  ? 2043 LYS A O     1 
ATOM   4698  C  CB    . LYS A 1 2043 ? 194.190 174.321 185.796 1.00 82.07  ? 2043 LYS A CB    1 
ATOM   4699  C  CG    . LYS A 1 2043 ? 193.174 173.293 186.258 1.00 79.67  ? 2043 LYS A CG    1 
ATOM   4700  C  CD    . LYS A 1 2043 ? 193.643 172.583 187.515 1.00 84.48  ? 2043 LYS A CD    1 
ATOM   4701  C  CE    . LYS A 1 2043 ? 192.635 171.538 187.961 1.00 86.31  ? 2043 LYS A CE    1 
ATOM   4702  N  NZ    . LYS A 1 2043 ? 191.255 171.881 187.521 1.00 83.37  ? 2043 LYS A NZ    1 
ATOM   4703  N  N     . PRO A 1 2044 ? 194.206 177.580 184.082 1.00 74.55  ? 2044 PRO A N     1 
ATOM   4704  C  CA    . PRO A 1 2044 ? 195.122 178.718 183.976 1.00 74.30  ? 2044 PRO A CA    1 
ATOM   4705  C  C     . PRO A 1 2044 ? 195.664 179.114 185.339 1.00 80.58  ? 2044 PRO A C     1 
ATOM   4706  O  O     . PRO A 1 2044 ? 195.000 178.962 186.367 1.00 90.11  ? 2044 PRO A O     1 
ATOM   4707  C  CB    . PRO A 1 2044 ? 194.247 179.827 183.381 1.00 69.55  ? 2044 PRO A CB    1 
ATOM   4708  C  CG    . PRO A 1 2044 ? 192.854 179.438 183.731 1.00 73.09  ? 2044 PRO A CG    1 
ATOM   4709  C  CD    . PRO A 1 2044 ? 192.827 177.940 183.715 1.00 75.92  ? 2044 PRO A CD    1 
ATOM   4710  N  N     . ASP A 1 2045 ? 196.894 179.629 185.338 1.00 81.37  ? 2045 ASP A N     1 
ATOM   4711  C  CA    . ASP A 1 2045 ? 197.565 180.037 186.573 1.00 84.39  ? 2045 ASP A CA    1 
ATOM   4712  C  C     . ASP A 1 2045 ? 197.046 181.415 186.972 1.00 82.60  ? 2045 ASP A C     1 
ATOM   4713  O  O     . ASP A 1 2045 ? 197.654 182.451 186.699 1.00 85.06  ? 2045 ASP A O     1 
ATOM   4714  C  CB    . ASP A 1 2045 ? 199.076 180.028 186.391 1.00 83.06  ? 2045 ASP A CB    1 
ATOM   4715  C  CG    . ASP A 1 2045 ? 199.610 178.656 186.032 1.00 87.26  ? 2045 ASP A CG    1 
ATOM   4716  O  OD1   . ASP A 1 2045 ? 199.574 177.757 186.898 1.00 87.65  ? 2045 ASP A OD1   1 
ATOM   4717  O  OD2   . ASP A 1 2045 ? 200.064 178.476 184.883 1.00 83.51  ? 2045 ASP A OD2   1 
ATOM   4718  N  N     . ARG A 1 2046 ? 195.894 181.412 187.648 1.00 76.61  ? 2046 ARG A N     1 
ATOM   4719  C  CA    . ARG A 1 2046 ? 195.220 182.663 187.981 1.00 72.35  ? 2046 ARG A CA    1 
ATOM   4720  C  C     . ARG A 1 2046 ? 196.044 183.523 188.932 1.00 76.76  ? 2046 ARG A C     1 
ATOM   4721  O  O     . ARG A 1 2046 ? 196.026 184.755 188.824 1.00 84.06  ? 2046 ARG A O     1 
ATOM   4722  C  CB    . ARG A 1 2046 ? 193.848 182.369 188.589 1.00 69.68  ? 2046 ARG A CB    1 
ATOM   4723  C  CG    . ARG A 1 2046 ? 192.775 182.051 187.563 1.00 71.24  ? 2046 ARG A CG    1 
ATOM   4724  C  CD    . ARG A 1 2046 ? 191.994 180.806 187.943 1.00 74.45  ? 2046 ARG A CD    1 
ATOM   4725  N  NE    . ARG A 1 2046 ? 191.429 180.900 189.283 1.00 78.00  ? 2046 ARG A NE    1 
ATOM   4726  C  CZ    . ARG A 1 2046 ? 190.156 181.165 189.540 1.00 81.51  ? 2046 ARG A CZ    1 
ATOM   4727  N  NH1   . ARG A 1 2046 ? 189.282 181.368 188.568 1.00 81.17  ? 2046 ARG A NH1   1 
ATOM   4728  N  NH2   . ARG A 1 2046 ? 189.749 181.228 190.805 1.00 85.47  ? 2046 ARG A NH2   1 
ATOM   4729  N  N     . GLN A 1 2047 ? 196.760 182.900 189.870 1.00 75.54  ? 2047 GLN A N     1 
ATOM   4730  C  CA    . GLN A 1 2047 ? 197.510 183.666 190.861 1.00 72.65  ? 2047 GLN A CA    1 
ATOM   4731  C  C     . GLN A 1 2047 ? 198.608 184.489 190.199 1.00 75.01  ? 2047 GLN A C     1 
ATOM   4732  O  O     . GLN A 1 2047 ? 198.811 185.660 190.539 1.00 83.17  ? 2047 GLN A O     1 
ATOM   4733  C  CB    . GLN A 1 2047 ? 198.084 182.720 191.921 1.00 76.41  ? 2047 GLN A CB    1 
ATOM   4734  C  CG    . GLN A 1 2047 ? 198.933 183.373 193.017 1.00 73.57  ? 2047 GLN A CG    1 
ATOM   4735  C  CD    . GLN A 1 2047 ? 200.337 183.731 192.566 1.00 80.07  ? 2047 GLN A CD    1 
ATOM   4736  O  OE1   . GLN A 1 2047 ? 200.920 183.058 191.717 1.00 83.89  ? 2047 GLN A OE1   1 
ATOM   4737  N  NE2   . GLN A 1 2047 ? 200.885 184.800 193.133 1.00 79.85  ? 2047 GLN A NE2   1 
ATOM   4738  N  N     . LEU A 1 2048 ? 199.332 183.890 189.252 1.00 67.24  ? 2048 LEU A N     1 
ATOM   4739  C  CA    . LEU A 1 2048 ? 200.398 184.614 188.565 1.00 66.61  ? 2048 LEU A CA    1 
ATOM   4740  C  C     . LEU A 1 2048 ? 199.835 185.767 187.742 1.00 70.88  ? 2048 LEU A C     1 
ATOM   4741  O  O     . LEU A 1 2048 ? 200.404 186.866 187.724 1.00 71.79  ? 2048 LEU A O     1 
ATOM   4742  C  CB    . LEU A 1 2048 ? 201.196 183.658 187.680 1.00 64.47  ? 2048 LEU A CB    1 
ATOM   4743  C  CG    . LEU A 1 2048 ? 202.371 184.266 186.915 1.00 67.59  ? 2048 LEU A CG    1 
ATOM   4744  C  CD1   . LEU A 1 2048 ? 203.252 185.078 187.847 1.00 66.82  ? 2048 LEU A CD1   1 
ATOM   4745  C  CD2   . LEU A 1 2048 ? 203.179 183.182 186.225 1.00 74.63  ? 2048 LEU A CD2   1 
ATOM   4746  N  N     . ILE A 1 2049 ? 198.715 185.532 187.054 1.00 63.41  ? 2049 ILE A N     1 
ATOM   4747  C  CA    . ILE A 1 2049 ? 198.075 186.594 186.280 1.00 49.38  ? 2049 ILE A CA    1 
ATOM   4748  C  C     . ILE A 1 2049 ? 197.696 187.750 187.191 1.00 58.48  ? 2049 ILE A C     1 
ATOM   4749  O  O     . ILE A 1 2049 ? 197.977 188.916 186.895 1.00 71.23  ? 2049 ILE A O     1 
ATOM   4750  C  CB    . ILE A 1 2049 ? 196.845 186.052 185.531 1.00 53.81  ? 2049 ILE A CB    1 
ATOM   4751  C  CG1   . ILE A 1 2049 ? 197.206 184.798 184.739 1.00 60.74  ? 2049 ILE A CG1   1 
ATOM   4752  C  CG2   . ILE A 1 2049 ? 196.261 187.126 184.628 1.00 63.01  ? 2049 ILE A CG2   1 
ATOM   4753  C  CD1   . ILE A 1 2049 ? 196.245 184.479 183.620 1.00 63.46  ? 2049 ILE A CD1   1 
ATOM   4754  N  N     . ALA A 1 2050 ? 197.051 187.439 188.317 1.00 59.41  ? 2050 ALA A N     1 
ATOM   4755  C  CA    . ALA A 1 2050 ? 196.621 188.483 189.239 1.00 58.60  ? 2050 ALA A CA    1 
ATOM   4756  C  C     . ALA A 1 2050 ? 197.815 189.257 189.783 1.00 60.20  ? 2050 ALA A C     1 
ATOM   4757  O  O     . ALA A 1 2050 ? 197.803 190.492 189.832 1.00 76.04  ? 2050 ALA A O     1 
ATOM   4758  C  CB    . ALA A 1 2050 ? 195.806 187.870 190.378 1.00 65.80  ? 2050 ALA A CB    1 
ATOM   4759  N  N     . GLN A 1 2051 ? 198.869 188.541 190.180 1.00 60.72  ? 2051 GLN A N     1 
ATOM   4760  C  CA    . GLN A 1 2051 ? 200.032 189.197 190.766 1.00 64.27  ? 2051 GLN A CA    1 
ATOM   4761  C  C     . GLN A 1 2051 ? 200.709 190.120 189.763 1.00 62.27  ? 2051 GLN A C     1 
ATOM   4762  O  O     . GLN A 1 2051 ? 201.017 191.275 190.076 1.00 72.19  ? 2051 GLN A O     1 
ATOM   4763  C  CB    . GLN A 1 2051 ? 201.018 188.151 191.285 1.00 66.85  ? 2051 GLN A CB    1 
ATOM   4764  C  CG    . GLN A 1 2051 ? 202.427 188.679 191.481 1.00 66.03  ? 2051 GLN A CG    1 
ATOM   4765  C  CD    . GLN A 1 2051 ? 203.437 187.573 191.696 1.00 73.89  ? 2051 GLN A CD    1 
ATOM   4766  O  OE1   . GLN A 1 2051 ? 203.139 186.560 192.329 1.00 73.80  ? 2051 GLN A OE1   1 
ATOM   4767  N  NE2   . GLN A 1 2051 ? 204.640 187.760 191.169 1.00 75.44  ? 2051 GLN A NE2   1 
ATOM   4768  N  N     . VAL A 1 2052 ? 200.932 189.635 188.540 1.00 52.45  ? 2052 VAL A N     1 
ATOM   4769  C  CA    . VAL A 1 2052 ? 201.627 190.452 187.551 1.00 53.88  ? 2052 VAL A CA    1 
ATOM   4770  C  C     . VAL A 1 2052 ? 200.761 191.626 187.113 1.00 54.94  ? 2052 VAL A C     1 
ATOM   4771  O  O     . VAL A 1 2052 ? 201.263 192.739 186.909 1.00 58.20  ? 2052 VAL A O     1 
ATOM   4772  C  CB    . VAL A 1 2052 ? 202.070 189.588 186.359 1.00 56.82  ? 2052 VAL A CB    1 
ATOM   4773  C  CG1   . VAL A 1 2052 ? 202.643 190.456 185.254 1.00 51.98  ? 2052 VAL A CG1   1 
ATOM   4774  C  CG2   . VAL A 1 2052 ? 203.100 188.573 186.813 1.00 61.82  ? 2052 VAL A CG2   1 
ATOM   4775  N  N     . MET A 1 2053 ? 199.450 191.411 186.966 1.00 55.25  ? 2053 MET A N     1 
ATOM   4776  C  CA    . MET A 1 2053 ? 198.570 192.512 186.593 1.00 51.13  ? 2053 MET A CA    1 
ATOM   4777  C  C     . MET A 1 2053 ? 198.551 193.593 187.663 1.00 60.85  ? 2053 MET A C     1 
ATOM   4778  O  O     . MET A 1 2053 ? 198.650 194.784 187.351 1.00 75.77  ? 2053 MET A O     1 
ATOM   4779  C  CB    . MET A 1 2053 ? 197.157 191.998 186.330 1.00 50.70  ? 2053 MET A CB    1 
ATOM   4780  C  CG    . MET A 1 2053 ? 196.955 191.437 184.940 1.00 58.25  ? 2053 MET A CG    1 
ATOM   4781  S  SD    . MET A 1 2053 ? 195.219 191.458 184.474 1.00 73.68  ? 2053 MET A SD    1 
ATOM   4782  C  CE    . MET A 1 2053 ? 195.153 193.015 183.591 1.00 70.66  ? 2053 MET A CE    1 
ATOM   4783  N  N     . LEU A 1 2054 ? 198.437 193.202 188.934 1.00 53.58  ? 2054 LEU A N     1 
ATOM   4784  C  CA    . LEU A 1 2054 ? 198.443 194.197 189.997 1.00 53.81  ? 2054 LEU A CA    1 
ATOM   4785  C  C     . LEU A 1 2054 ? 199.800 194.878 190.118 1.00 55.84  ? 2054 LEU A C     1 
ATOM   4786  O  O     . LEU A 1 2054 ? 199.870 196.057 190.481 1.00 64.04  ? 2054 LEU A O     1 
ATOM   4787  C  CB    . LEU A 1 2054 ? 198.038 193.550 191.320 1.00 56.35  ? 2054 LEU A CB    1 
ATOM   4788  C  CG    . LEU A 1 2054 ? 196.587 193.071 191.360 1.00 49.43  ? 2054 LEU A CG    1 
ATOM   4789  C  CD1   . LEU A 1 2054 ? 196.276 192.394 192.679 1.00 55.51  ? 2054 LEU A CD1   1 
ATOM   4790  C  CD2   . LEU A 1 2054 ? 195.638 194.230 191.113 1.00 53.92  ? 2054 LEU A CD2   1 
ATOM   4791  N  N     . TYR A 1 2055 ? 200.884 194.160 189.815 1.00 56.40  ? 2055 TYR A N     1 
ATOM   4792  C  CA    . TYR A 1 2055 ? 202.207 194.775 189.843 1.00 61.04  ? 2055 TYR A CA    1 
ATOM   4793  C  C     . TYR A 1 2055 ? 202.363 195.806 188.733 1.00 56.69  ? 2055 TYR A C     1 
ATOM   4794  O  O     . TYR A 1 2055 ? 202.957 196.870 188.946 1.00 62.42  ? 2055 TYR A O     1 
ATOM   4795  C  CB    . TYR A 1 2055 ? 203.282 193.696 189.731 1.00 63.98  ? 2055 TYR A CB    1 
ATOM   4796  C  CG    . TYR A 1 2055 ? 204.690 194.210 189.908 1.00 64.50  ? 2055 TYR A CG    1 
ATOM   4797  C  CD1   . TYR A 1 2055 ? 205.033 194.987 191.005 1.00 64.53  ? 2055 TYR A CD1   1 
ATOM   4798  C  CD2   . TYR A 1 2055 ? 205.678 193.915 188.980 1.00 61.85  ? 2055 TYR A CD2   1 
ATOM   4799  C  CE1   . TYR A 1 2055 ? 206.320 195.457 191.172 1.00 69.58  ? 2055 TYR A CE1   1 
ATOM   4800  C  CE2   . TYR A 1 2055 ? 206.968 194.381 189.138 1.00 65.70  ? 2055 TYR A CE2   1 
ATOM   4801  C  CZ    . TYR A 1 2055 ? 207.283 195.152 190.236 1.00 70.15  ? 2055 TYR A CZ    1 
ATOM   4802  O  OH    . TYR A 1 2055 ? 208.566 195.619 190.399 1.00 66.93  ? 2055 TYR A OH    1 
ATOM   4803  N  N     . SER A 1 2056 ? 201.838 195.512 187.542 1.00 54.29  ? 2056 SER A N     1 
ATOM   4804  C  CA    . SER A 1 2056 ? 201.996 196.414 186.409 1.00 54.53  ? 2056 SER A CA    1 
ATOM   4805  C  C     . SER A 1 2056 ? 201.116 197.653 186.508 1.00 53.54  ? 2056 SER A C     1 
ATOM   4806  O  O     . SER A 1 2056 ? 201.486 198.701 185.968 1.00 56.92  ? 2056 SER A O     1 
ATOM   4807  C  CB    . SER A 1 2056 ? 201.696 195.678 185.102 1.00 54.37  ? 2056 SER A CB    1 
ATOM   4808  O  OG    . SER A 1 2056 ? 200.341 195.271 185.045 1.00 64.25  ? 2056 SER A OG    1 
ATOM   4809  N  N     . GLN A 1 2057 ? 199.969 197.565 187.179 1.00 64.98  ? 2057 GLN A N     1 
ATOM   4810  C  CA    . GLN A 1 2057 ? 199.084 198.711 187.325 1.00 64.64  ? 2057 GLN A CA    1 
ATOM   4811  C  C     . GLN A 1 2057 ? 199.546 199.691 188.395 1.00 66.23  ? 2057 GLN A C     1 
ATOM   4812  O  O     . GLN A 1 2057 ? 198.988 200.789 188.487 1.00 67.55  ? 2057 GLN A O     1 
ATOM   4813  C  CB    . GLN A 1 2057 ? 197.658 198.248 187.644 1.00 62.80  ? 2057 GLN A CB    1 
ATOM   4814  C  CG    . GLN A 1 2057 ? 197.052 197.331 186.597 1.00 58.21  ? 2057 GLN A CG    1 
ATOM   4815  C  CD    . GLN A 1 2057 ? 196.177 198.068 185.607 1.00 67.81  ? 2057 GLN A CD    1 
ATOM   4816  O  OE1   . GLN A 1 2057 ? 196.403 199.242 185.316 1.00 73.92  ? 2057 GLN A OE1   1 
ATOM   4817  N  NE2   . GLN A 1 2057 ? 195.170 197.381 185.081 1.00 70.49  ? 2057 GLN A NE2   1 
ATOM   4818  N  N     . GLY A 1 2058 ? 200.545 199.330 189.196 1.00 61.62  ? 2058 GLY A N     1 
ATOM   4819  C  CA    . GLY A 1 2058 ? 201.095 200.225 190.190 1.00 63.55  ? 2058 GLY A CA    1 
ATOM   4820  C  C     . GLY A 1 2058 ? 200.794 199.886 191.635 1.00 66.57  ? 2058 GLY A C     1 
ATOM   4821  O  O     . GLY A 1 2058 ? 201.018 200.734 192.506 1.00 76.00  ? 2058 GLY A O     1 
ATOM   4822  N  N     . PHE A 1 2059 ? 200.298 198.687 191.923 1.00 62.18  ? 2059 PHE A N     1 
ATOM   4823  C  CA    . PHE A 1 2059 ? 200.000 198.304 193.296 1.00 66.49  ? 2059 PHE A CA    1 
ATOM   4824  C  C     . PHE A 1 2059 ? 201.276 197.857 194.000 1.00 68.85  ? 2059 PHE A C     1 
ATOM   4825  O  O     . PHE A 1 2059 ? 201.962 196.940 193.539 1.00 76.73  ? 2059 PHE A O     1 
ATOM   4826  C  CB    . PHE A 1 2059 ? 198.958 197.187 193.327 1.00 65.85  ? 2059 PHE A CB    1 
ATOM   4827  C  CG    . PHE A 1 2059 ? 197.575 197.632 192.939 1.00 61.39  ? 2059 PHE A CG    1 
ATOM   4828  C  CD1   . PHE A 1 2059 ? 197.233 197.794 191.608 1.00 64.29  ? 2059 PHE A CD1   1 
ATOM   4829  C  CD2   . PHE A 1 2059 ? 196.618 197.884 193.905 1.00 61.67  ? 2059 PHE A CD2   1 
ATOM   4830  C  CE1   . PHE A 1 2059 ? 195.964 198.199 191.250 1.00 65.65  ? 2059 PHE A CE1   1 
ATOM   4831  C  CE2   . PHE A 1 2059 ? 195.347 198.290 193.552 1.00 67.90  ? 2059 PHE A CE2   1 
ATOM   4832  C  CZ    . PHE A 1 2059 ? 195.021 198.447 192.222 1.00 66.09  ? 2059 PHE A CZ    1 
ATOM   4833  N  N     . ARG A 1 2060 ? 201.591 198.508 195.122 1.00 94.10  ? 2060 ARG A N     1 
ATOM   4834  C  CA    . ARG A 1 2060 ? 202.809 198.175 195.854 1.00 95.25  ? 2060 ARG A CA    1 
ATOM   4835  C  C     . ARG A 1 2060 ? 202.719 196.806 196.516 1.00 98.32  ? 2060 ARG A C     1 
ATOM   4836  O  O     . ARG A 1 2060 ? 203.737 196.121 196.660 1.00 104.33 ? 2060 ARG A O     1 
ATOM   4837  C  CB    . ARG A 1 2060 ? 203.101 199.249 196.902 1.00 96.88  ? 2060 ARG A CB    1 
ATOM   4838  C  CG    . ARG A 1 2060 ? 202.725 200.656 196.469 1.00 98.52  ? 2060 ARG A CG    1 
ATOM   4839  C  CD    . ARG A 1 2060 ? 202.584 201.584 197.665 1.00 104.84 ? 2060 ARG A CD    1 
ATOM   4840  N  NE    . ARG A 1 2060 ? 201.418 201.258 198.479 1.00 106.33 ? 2060 ARG A NE    1 
ATOM   4841  C  CZ    . ARG A 1 2060 ? 201.475 200.747 199.702 1.00 103.49 ? 2060 ARG A CZ    1 
ATOM   4842  N  NH1   . ARG A 1 2060 ? 202.632 200.488 200.289 1.00 100.66 ? 2060 ARG A NH1   1 
ATOM   4843  N  NH2   . ARG A 1 2060 ? 200.343 200.492 200.352 1.00 98.16  ? 2060 ARG A NH2   1 
ATOM   4844  N  N     . THR A 1 2061 ? 201.521 196.394 196.923 1.00 84.24  ? 2061 THR A N     1 
ATOM   4845  C  CA    . THR A 1 2061 ? 201.297 195.128 197.620 1.00 83.33  ? 2061 THR A CA    1 
ATOM   4846  C  C     . THR A 1 2061 ? 200.683 194.079 196.703 1.00 86.31  ? 2061 THR A C     1 
ATOM   4847  O  O     . THR A 1 2061 ? 199.774 193.347 197.104 1.00 92.64  ? 2061 THR A O     1 
ATOM   4848  C  CB    . THR A 1 2061 ? 200.418 195.346 198.847 1.00 85.71  ? 2061 THR A CB    1 
ATOM   4849  O  OG1   . THR A 1 2061 ? 199.195 195.980 198.453 1.00 88.69  ? 2061 THR A OG1   1 
ATOM   4850  C  CG2   . THR A 1 2061 ? 201.133 196.225 199.860 1.00 87.95  ? 2061 THR A CG2   1 
ATOM   4851  N  N     . ALA A 1 2062 ? 201.162 194.000 195.458 1.00 75.21  ? 2062 ALA A N     1 
ATOM   4852  C  CA    . ALA A 1 2062 ? 200.521 193.156 194.454 1.00 74.34  ? 2062 ALA A CA    1 
ATOM   4853  C  C     . ALA A 1 2062 ? 200.513 191.687 194.864 1.00 81.03  ? 2062 ALA A C     1 
ATOM   4854  O  O     . ALA A 1 2062 ? 199.516 190.988 194.656 1.00 83.64  ? 2062 ALA A O     1 
ATOM   4855  C  CB    . ALA A 1 2062 ? 201.220 193.328 193.108 1.00 73.83  ? 2062 ALA A CB    1 
ATOM   4856  N  N     . GLU A 1 2063 ? 201.617 191.196 195.430 1.00 89.22  ? 2063 GLU A N     1 
ATOM   4857  C  CA    . GLU A 1 2063 ? 201.692 189.782 195.793 1.00 90.07  ? 2063 GLU A CA    1 
ATOM   4858  C  C     . GLU A 1 2063 ? 200.656 189.428 196.854 1.00 95.76  ? 2063 GLU A C     1 
ATOM   4859  O  O     . GLU A 1 2063 ? 199.929 188.434 196.725 1.00 99.83  ? 2063 GLU A O     1 
ATOM   4860  C  CB    . GLU A 1 2063 ? 203.100 189.441 196.281 1.00 91.53  ? 2063 GLU A CB    1 
ATOM   4861  C  CG    . GLU A 1 2063 ? 204.037 188.957 195.189 1.00 93.31  ? 2063 GLU A CG    1 
ATOM   4862  C  CD    . GLU A 1 2063 ? 204.966 190.048 194.695 1.00 97.75  ? 2063 GLU A CD    1 
ATOM   4863  O  OE1   . GLU A 1 2063 ? 205.325 190.934 195.499 1.00 96.91  ? 2063 GLU A OE1   1 
ATOM   4864  O  OE2   . GLU A 1 2063 ? 205.339 190.020 193.503 1.00 99.30  ? 2063 GLU A OE2   1 
ATOM   4865  N  N     . VAL A 1 2064 ? 200.572 190.239 197.911 1.00 85.91  ? 2064 VAL A N     1 
ATOM   4866  C  CA    . VAL A 1 2064 ? 199.603 189.986 198.974 1.00 81.47  ? 2064 VAL A CA    1 
ATOM   4867  C  C     . VAL A 1 2064 ? 198.184 190.091 198.435 1.00 86.72  ? 2064 VAL A C     1 
ATOM   4868  O  O     . VAL A 1 2064 ? 197.316 189.272 198.760 1.00 91.11  ? 2064 VAL A O     1 
ATOM   4869  C  CB    . VAL A 1 2064 ? 199.838 190.954 200.149 1.00 80.52  ? 2064 VAL A CB    1 
ATOM   4870  C  CG1   . VAL A 1 2064 ? 198.745 190.801 201.193 1.00 83.92  ? 2064 VAL A CG1   1 
ATOM   4871  C  CG2   . VAL A 1 2064 ? 201.207 190.717 200.764 1.00 82.95  ? 2064 VAL A CG2   1 
ATOM   4872  N  N     . LEU A 1 2065 ? 197.927 191.099 197.598 1.00 79.20  ? 2065 LEU A N     1 
ATOM   4873  C  CA    . LEU A 1 2065 ? 196.590 191.276 197.043 1.00 73.71  ? 2065 LEU A CA    1 
ATOM   4874  C  C     . LEU A 1 2065 ? 196.181 190.082 196.189 1.00 76.93  ? 2065 LEU A C     1 
ATOM   4875  O  O     . LEU A 1 2065 ? 195.042 189.614 196.273 1.00 86.73  ? 2065 LEU A O     1 
ATOM   4876  C  CB    . LEU A 1 2065 ? 196.531 192.567 196.230 1.00 70.13  ? 2065 LEU A CB    1 
ATOM   4877  C  CG    . LEU A 1 2065 ? 196.519 193.867 197.032 1.00 72.28  ? 2065 LEU A CG    1 
ATOM   4878  C  CD1   . LEU A 1 2065 ? 196.601 195.065 196.105 1.00 77.42  ? 2065 LEU A CD1   1 
ATOM   4879  C  CD2   . LEU A 1 2065 ? 195.277 193.943 197.899 1.00 76.34  ? 2065 LEU A CD2   1 
ATOM   4880  N  N     . ALA A 1 2066 ? 197.096 189.574 195.361 1.00 71.76  ? 2066 ALA A N     1 
ATOM   4881  C  CA    . ALA A 1 2066 ? 196.781 188.410 194.538 1.00 79.92  ? 2066 ALA A CA    1 
ATOM   4882  C  C     . ALA A 1 2066 ? 196.545 187.175 195.398 1.00 86.33  ? 2066 ALA A C     1 
ATOM   4883  O  O     . ALA A 1 2066 ? 195.585 186.421 195.177 1.00 94.46  ? 2066 ALA A O     1 
ATOM   4884  C  CB    . ALA A 1 2066 ? 197.905 188.159 193.535 1.00 75.91  ? 2066 ALA A CB    1 
ATOM   4885  N  N     . ASN A 1 2067 ? 197.416 186.950 196.388 1.00 86.56  ? 2067 ASN A N     1 
ATOM   4886  C  CA    . ASN A 1 2067 ? 197.261 185.803 197.272 1.00 85.75  ? 2067 ASN A CA    1 
ATOM   4887  C  C     . ASN A 1 2067 ? 196.004 185.901 198.122 1.00 89.45  ? 2067 ASN A C     1 
ATOM   4888  O  O     . ASN A 1 2067 ? 195.557 184.888 198.669 1.00 95.50  ? 2067 ASN A O     1 
ATOM   4889  C  CB    . ASN A 1 2067 ? 198.488 185.660 198.173 1.00 85.58  ? 2067 ASN A CB    1 
ATOM   4890  C  CG    . ASN A 1 2067 ? 199.736 185.289 197.400 1.00 91.83  ? 2067 ASN A CG    1 
ATOM   4891  O  OD1   . ASN A 1 2067 ? 199.816 184.214 196.806 1.00 92.55  ? 2067 ASN A OD1   1 
ATOM   4892  N  ND2   . ASN A 1 2067 ? 200.721 186.179 197.403 1.00 94.23  ? 2067 ASN A ND2   1 
ATOM   4893  N  N     . LYS A 1 2068 ? 195.444 187.099 198.270 1.00 81.68  ? 2068 LYS A N     1 
ATOM   4894  C  CA    . LYS A 1 2068 ? 194.182 187.254 198.980 1.00 78.58  ? 2068 LYS A CA    1 
ATOM   4895  C  C     . LYS A 1 2068 ? 192.975 187.224 198.053 1.00 80.95  ? 2068 LYS A C     1 
ATOM   4896  O  O     . LYS A 1 2068 ? 191.861 186.952 198.513 1.00 92.25  ? 2068 LYS A O     1 
ATOM   4897  C  CB    . LYS A 1 2068 ? 194.185 188.564 199.771 1.00 79.63  ? 2068 LYS A CB    1 
ATOM   4898  C  CG    . LYS A 1 2068 ? 194.982 188.508 201.063 1.00 78.33  ? 2068 LYS A CG    1 
ATOM   4899  C  CD    . LYS A 1 2068 ? 195.037 189.869 201.736 1.00 79.60  ? 2068 LYS A CD    1 
ATOM   4900  C  CE    . LYS A 1 2068 ? 195.383 189.743 203.209 1.00 82.34  ? 2068 LYS A CE    1 
ATOM   4901  N  NZ    . LYS A 1 2068 ? 194.409 188.883 203.936 1.00 83.53  ? 2068 LYS A NZ    1 
ATOM   4902  N  N     . ILE A 1 2069 ? 193.162 187.495 196.762 1.00 72.60  ? 2069 ILE A N     1 
ATOM   4903  C  CA    . ILE A 1 2069 ? 192.030 187.635 195.853 1.00 74.64  ? 2069 ILE A CA    1 
ATOM   4904  C  C     . ILE A 1 2069 ? 191.733 186.331 195.120 1.00 77.71  ? 2069 ILE A C     1 
ATOM   4905  O  O     . ILE A 1 2069 ? 190.573 186.045 194.806 1.00 86.48  ? 2069 ILE A O     1 
ATOM   4906  C  CB    . ILE A 1 2069 ? 192.257 188.790 194.857 1.00 72.39  ? 2069 ILE A CB    1 
ATOM   4907  C  CG1   . ILE A 1 2069 ? 190.932 189.219 194.228 1.00 75.74  ? 2069 ILE A CG1   1 
ATOM   4908  C  CG2   . ILE A 1 2069 ? 193.245 188.405 193.770 1.00 72.77  ? 2069 ILE A CG2   1 
ATOM   4909  C  CD1   . ILE A 1 2069 ? 189.860 189.540 195.240 1.00 73.73  ? 2069 ILE A CD1   1 
ATOM   4910  N  N     . VAL A 1 2070 ? 192.756 185.527 194.840 1.00 67.13  ? 2070 VAL A N     1 
ATOM   4911  C  CA    . VAL A 1 2070 ? 192.520 184.295 194.084 1.00 67.91  ? 2070 VAL A CA    1 
ATOM   4912  C  C     . VAL A 1 2070 ? 191.865 183.242 194.979 1.00 80.06  ? 2070 VAL A C     1 
ATOM   4913  O  O     . VAL A 1 2070 ? 190.835 182.660 194.586 1.00 80.67  ? 2070 VAL A O     1 
ATOM   4914  C  CB    . VAL A 1 2070 ? 193.814 183.774 193.436 1.00 66.03  ? 2070 VAL A CB    1 
ATOM   4915  C  CG1   . VAL A 1 2070 ? 193.547 182.476 192.696 1.00 68.24  ? 2070 VAL A CG1   1 
ATOM   4916  C  CG2   . VAL A 1 2070 ? 194.384 184.820 192.496 1.00 70.49  ? 2070 VAL A CG2   1 
ATOM   4917  N  N     . PRO A 1 2071 ? 192.396 182.956 196.176 1.00 85.63  ? 2071 PRO A N     1 
ATOM   4918  C  CA    . PRO A 1 2071 ? 191.647 182.081 197.090 1.00 82.60  ? 2071 PRO A CA    1 
ATOM   4919  C  C     . PRO A 1 2071 ? 190.281 182.632 197.435 1.00 81.04  ? 2071 PRO A C     1 
ATOM   4920  O  O     . PRO A 1 2071 ? 189.367 181.853 197.717 1.00 87.05  ? 2071 PRO A O     1 
ATOM   4921  C  CB    . PRO A 1 2071 ? 192.555 182.000 198.323 1.00 82.85  ? 2071 PRO A CB    1 
ATOM   4922  C  CG    . PRO A 1 2071 ? 193.906 182.244 197.795 1.00 85.24  ? 2071 PRO A CG    1 
ATOM   4923  C  CD    . PRO A 1 2071 ? 193.716 183.290 196.741 1.00 81.38  ? 2071 PRO A CD    1 
ATOM   4924  N  N     . PHE A 1 2072 ? 190.110 183.955 197.411 1.00 71.62  ? 2072 PHE A N     1 
ATOM   4925  C  CA    . PHE A 1 2072 ? 188.778 184.522 197.586 1.00 69.49  ? 2072 PHE A CA    1 
ATOM   4926  C  C     . PHE A 1 2072 ? 187.846 184.099 196.459 1.00 68.67  ? 2072 PHE A C     1 
ATOM   4927  O  O     . PHE A 1 2072 ? 186.672 183.799 196.696 1.00 78.82  ? 2072 PHE A O     1 
ATOM   4928  C  CB    . PHE A 1 2072 ? 188.849 186.044 197.670 1.00 72.71  ? 2072 PHE A CB    1 
ATOM   4929  C  CG    . PHE A 1 2072 ? 187.525 186.715 197.468 1.00 74.02  ? 2072 PHE A CG    1 
ATOM   4930  C  CD1   . PHE A 1 2072 ? 186.556 186.672 198.454 1.00 75.65  ? 2072 PHE A CD1   1 
ATOM   4931  C  CD2   . PHE A 1 2072 ? 187.245 187.382 196.289 1.00 77.50  ? 2072 PHE A CD2   1 
ATOM   4932  C  CE1   . PHE A 1 2072 ? 185.335 187.283 198.267 1.00 76.45  ? 2072 PHE A CE1   1 
ATOM   4933  C  CE2   . PHE A 1 2072 ? 186.027 187.996 196.097 1.00 75.77  ? 2072 PHE A CE2   1 
ATOM   4934  C  CZ    . PHE A 1 2072 ? 185.071 187.949 197.087 1.00 78.32  ? 2072 PHE A CZ    1 
ATOM   4935  N  N     . PHE A 1 2073 ? 188.345 184.079 195.222 1.00 62.62  ? 2073 PHE A N     1 
ATOM   4936  C  CA    . PHE A 1 2073 ? 187.510 183.641 194.108 1.00 68.55  ? 2073 PHE A CA    1 
ATOM   4937  C  C     . PHE A 1 2073 ? 187.173 182.161 194.218 1.00 74.42  ? 2073 PHE A C     1 
ATOM   4938  O  O     . PHE A 1 2073 ? 186.042 181.752 193.927 1.00 82.56  ? 2073 PHE A O     1 
ATOM   4939  C  CB    . PHE A 1 2073 ? 188.196 183.946 192.778 1.00 64.58  ? 2073 PHE A CB    1 
ATOM   4940  C  CG    . PHE A 1 2073 ? 187.729 185.221 192.142 1.00 63.63  ? 2073 PHE A CG    1 
ATOM   4941  C  CD1   . PHE A 1 2073 ? 188.224 186.442 192.563 1.00 69.36  ? 2073 PHE A CD1   1 
ATOM   4942  C  CD2   . PHE A 1 2073 ? 186.783 185.199 191.134 1.00 63.65  ? 2073 PHE A CD2   1 
ATOM   4943  C  CE1   . PHE A 1 2073 ? 187.791 187.615 191.984 1.00 71.46  ? 2073 PHE A CE1   1 
ATOM   4944  C  CE2   . PHE A 1 2073 ? 186.346 186.369 190.551 1.00 63.65  ? 2073 PHE A CE2   1 
ATOM   4945  C  CZ    . PHE A 1 2073 ? 186.850 187.579 190.977 1.00 68.58  ? 2073 PHE A CZ    1 
ATOM   4946  N  N     . LYS A 1 2074 ? 188.135 181.338 194.643 1.00 82.13  ? 2074 LYS A N     1 
ATOM   4947  C  CA    . LYS A 1 2074 ? 187.828 179.925 194.859 1.00 83.66  ? 2074 LYS A CA    1 
ATOM   4948  C  C     . LYS A 1 2074 ? 186.797 179.747 195.972 1.00 87.37  ? 2074 LYS A C     1 
ATOM   4949  O  O     . LYS A 1 2074 ? 185.877 178.924 195.860 1.00 87.62  ? 2074 LYS A O     1 
ATOM   4950  C  CB    . LYS A 1 2074 ? 189.106 179.151 195.175 1.00 82.54  ? 2074 LYS A CB    1 
ATOM   4951  C  CG    . LYS A 1 2074 ? 189.770 178.543 193.952 1.00 85.73  ? 2074 LYS A CG    1 
ATOM   4952  C  CD    . LYS A 1 2074 ? 191.235 178.240 194.209 1.00 92.63  ? 2074 LYS A CD    1 
ATOM   4953  C  CE    . LYS A 1 2074 ? 192.027 178.219 192.912 1.00 86.82  ? 2074 LYS A CE    1 
ATOM   4954  N  NZ    . LYS A 1 2074 ? 193.488 178.373 193.149 1.00 83.97  ? 2074 LYS A NZ    1 
ATOM   4955  N  N     . LEU A 1 2075 ? 186.935 180.521 197.051 1.00 87.51  ? 2075 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 2075 ? 185.969 180.491 198.142 1.00 81.21  ? 2075 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 2075 ? 184.582 180.892 197.660 1.00 83.80  ? 2075 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 2075 ? 183.581 180.287 198.055 1.00 96.84  ? 2075 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 2075 ? 186.441 181.423 199.259 1.00 86.29  ? 2075 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 2075 ? 187.427 180.887 200.295 1.00 85.53  ? 2075 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 2075 ? 188.214 182.026 200.911 1.00 87.16  ? 2075 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 2075 ? 186.669 180.154 201.377 1.00 89.95  ? 2075 LEU A CD2   1 
ATOM   4963  N  N     . CYS A 1 2076 ? 184.503 181.920 196.815 1.00 82.44  ? 2076 CYS A N     1 
ATOM   4964  C  CA    . CYS A 1 2076 ? 183.218 182.320 196.254 1.00 83.83  ? 2076 CYS A CA    1 
ATOM   4965  C  C     . CYS A 1 2076 ? 182.629 181.217 195.388 1.00 89.35  ? 2076 CYS A C     1 
ATOM   4966  O  O     . CYS A 1 2076 ? 181.425 180.944 195.448 1.00 92.53  ? 2076 CYS A O     1 
ATOM   4967  C  CB    . CYS A 1 2076 ? 183.376 183.605 195.445 1.00 86.65  ? 2076 CYS A CB    1 
ATOM   4968  S  SG    . CYS A 1 2076 ? 183.355 185.101 196.441 1.00 110.27 ? 2076 CYS A SG    1 
ATOM   4969  N  N     . ASP A 1 2077 ? 183.464 180.569 194.576 1.00 90.83  ? 2077 ASP A N     1 
ATOM   4970  C  CA    . ASP A 1 2077 ? 182.966 179.507 193.710 1.00 86.45  ? 2077 ASP A CA    1 
ATOM   4971  C  C     . ASP A 1 2077 ? 182.422 178.340 194.523 1.00 90.77  ? 2077 ASP A C     1 
ATOM   4972  O  O     . ASP A 1 2077 ? 181.419 177.725 194.144 1.00 94.04  ? 2077 ASP A O     1 
ATOM   4973  C  CB    . ASP A 1 2077 ? 184.070 179.033 192.767 1.00 88.12  ? 2077 ASP A CB    1 
ATOM   4974  C  CG    . ASP A 1 2077 ? 183.632 177.870 191.901 1.00 93.56  ? 2077 ASP A CG    1 
ATOM   4975  O  OD1   . ASP A 1 2077 ? 182.754 178.070 191.036 1.00 97.40  ? 2077 ASP A OD1   1 
ATOM   4976  O  OD2   . ASP A 1 2077 ? 184.162 176.755 192.087 1.00 94.63  ? 2077 ASP A OD2   1 
ATOM   4977  N  N     . GLU A 1 2078 ? 183.069 178.018 195.642 1.00 100.51 ? 2078 GLU A N     1 
ATOM   4978  C  CA    . GLU A 1 2078 ? 182.704 176.838 196.418 1.00 97.98  ? 2078 GLU A CA    1 
ATOM   4979  C  C     . GLU A 1 2078 ? 181.772 177.121 197.593 1.00 98.34  ? 2078 GLU A C     1 
ATOM   4980  O  O     . GLU A 1 2078 ? 181.339 176.173 198.253 1.00 100.46 ? 2078 GLU A O     1 
ATOM   4981  C  CB    . GLU A 1 2078 ? 183.965 176.138 196.931 1.00 92.29  ? 2078 GLU A CB    1 
ATOM   4982  C  CG    . GLU A 1 2078 ? 184.687 175.321 195.877 1.00 95.64  ? 2078 GLU A CG    1 
ATOM   4983  C  CD    . GLU A 1 2078 ? 186.138 175.071 196.230 1.00 102.77 ? 2078 GLU A CD    1 
ATOM   4984  O  OE1   . GLU A 1 2078 ? 187.021 175.482 195.449 1.00 104.80 ? 2078 GLU A OE1   1 
ATOM   4985  O  OE2   . GLU A 1 2078 ? 186.396 174.465 197.291 1.00 101.56 ? 2078 GLU A OE2   1 
ATOM   4986  N  N     . GLN A 1 2079 ? 181.442 178.382 197.874 1.00 95.57  ? 2079 GLN A N     1 
ATOM   4987  C  CA    . GLN A 1 2079 ? 180.681 178.674 199.085 1.00 90.15  ? 2079 GLN A CA    1 
ATOM   4988  C  C     . GLN A 1 2079 ? 179.332 179.327 198.809 1.00 97.37  ? 2079 GLN A C     1 
ATOM   4989  O  O     . GLN A 1 2079 ? 178.364 179.067 199.530 1.00 111.13 ? 2079 GLN A O     1 
ATOM   4990  C  CB    . GLN A 1 2079 ? 181.500 179.559 200.025 1.00 90.34  ? 2079 GLN A CB    1 
ATOM   4991  C  CG    . GLN A 1 2079 ? 182.645 178.834 200.708 1.00 94.73  ? 2079 GLN A CG    1 
ATOM   4992  C  CD    . GLN A 1 2079 ? 182.743 179.163 202.182 1.00 101.07 ? 2079 GLN A CD    1 
ATOM   4993  O  OE1   . GLN A 1 2079 ? 182.327 180.235 202.620 1.00 102.72 ? 2079 GLN A OE1   1 
ATOM   4994  N  NE2   . GLN A 1 2079 ? 183.299 178.240 202.958 1.00 103.15 ? 2079 GLN A NE2   1 
ATOM   4995  N  N     . LEU A 1 2080 ? 179.246 180.180 197.793 1.00 84.53  ? 2080 LEU A N     1 
ATOM   4996  C  CA    . LEU A 1 2080 ? 177.954 180.765 197.474 1.00 88.74  ? 2080 LEU A CA    1 
ATOM   4997  C  C     . LEU A 1 2080 ? 177.038 179.720 196.843 1.00 88.43  ? 2080 LEU A C     1 
ATOM   4998  O  O     . LEU A 1 2080 ? 177.487 178.725 196.268 1.00 80.69  ? 2080 LEU A O     1 
ATOM   4999  C  CB    . LEU A 1 2080 ? 178.106 181.971 196.545 1.00 83.12  ? 2080 LEU A CB    1 
ATOM   5000  C  CG    . LEU A 1 2080 ? 179.322 182.875 196.737 1.00 86.14  ? 2080 LEU A CG    1 
ATOM   5001  C  CD1   . LEU A 1 2080 ? 179.604 183.650 195.470 1.00 85.79  ? 2080 LEU A CD1   1 
ATOM   5002  C  CD2   . LEU A 1 2080 ? 179.098 183.830 197.891 1.00 92.68  ? 2080 LEU A CD2   1 
ATOM   5003  N  N     . SER A 1 2081 ? 175.734 179.956 196.975 1.00 93.27  ? 2081 SER A N     1 
ATOM   5004  C  CA    . SER A 1 2081 ? 174.745 179.013 196.469 1.00 91.60  ? 2081 SER A CA    1 
ATOM   5005  C  C     . SER A 1 2081 ? 174.883 178.848 194.962 1.00 89.58  ? 2081 SER A C     1 
ATOM   5006  O  O     . SER A 1 2081 ? 175.135 179.811 194.234 1.00 92.07  ? 2081 SER A O     1 
ATOM   5007  C  CB    . SER A 1 2081 ? 173.335 179.489 196.821 1.00 89.63  ? 2081 SER A CB    1 
ATOM   5008  O  OG    . SER A 1 2081 ? 172.963 180.605 196.032 1.00 89.35  ? 2081 SER A OG    1 
ATOM   5009  N  N     . SER A 1 2082 ? 174.722 177.613 194.496 1.00 84.90  ? 2082 SER A N     1 
ATOM   5010  C  CA    . SER A 1 2082 ? 174.877 177.315 193.078 1.00 85.14  ? 2082 SER A CA    1 
ATOM   5011  C  C     . SER A 1 2082 ? 173.747 177.954 192.282 1.00 88.47  ? 2082 SER A C     1 
ATOM   5012  O  O     . SER A 1 2082 ? 172.571 177.817 192.637 1.00 89.07  ? 2082 SER A O     1 
ATOM   5013  C  CB    . SER A 1 2082 ? 174.902 175.805 192.857 1.00 85.31  ? 2082 SER A CB    1 
ATOM   5014  O  OG    . SER A 1 2082 ? 174.939 175.494 191.475 1.00 86.83  ? 2082 SER A OG    1 
ATOM   5015  N  N     . GLN A 1 2083 ? 174.103 178.651 191.206 1.00 77.74  ? 2083 GLN A N     1 
ATOM   5016  C  CA    . GLN A 1 2083 ? 173.136 179.274 190.316 1.00 70.51  ? 2083 GLN A CA    1 
ATOM   5017  C  C     . GLN A 1 2083 ? 173.636 179.176 188.883 1.00 69.72  ? 2083 GLN A C     1 
ATOM   5018  O  O     . GLN A 1 2083 ? 174.834 179.017 188.635 1.00 65.83  ? 2083 GLN A O     1 
ATOM   5019  C  CB    . GLN A 1 2083 ? 172.883 180.743 190.689 1.00 71.20  ? 2083 GLN A CB    1 
ATOM   5020  C  CG    . GLN A 1 2083 ? 172.015 180.949 191.930 1.00 76.48  ? 2083 GLN A CG    1 
ATOM   5021  C  CD    . GLN A 1 2083 ? 170.541 180.644 191.702 1.00 78.10  ? 2083 GLN A CD    1 
ATOM   5022  O  OE1   . GLN A 1 2083 ? 170.178 179.844 190.842 1.00 73.01  ? 2083 GLN A OE1   1 
ATOM   5023  N  NE2   . GLN A 1 2083 ? 169.683 181.287 192.485 1.00 80.37  ? 2083 GLN A NE2   1 
ATOM   5024  N  N     . SER A 1 2084 ? 172.700 179.269 187.937 1.00 76.61  ? 2084 SER A N     1 
ATOM   5025  C  CA    . SER A 1 2084 ? 173.042 179.093 186.531 1.00 73.72  ? 2084 SER A CA    1 
ATOM   5026  C  C     . SER A 1 2084 ? 173.782 180.289 185.949 1.00 69.88  ? 2084 SER A C     1 
ATOM   5027  O  O     . SER A 1 2084 ? 174.520 180.126 184.973 1.00 72.17  ? 2084 SER A O     1 
ATOM   5028  C  CB    . SER A 1 2084 ? 171.777 178.822 185.715 1.00 72.10  ? 2084 SER A CB    1 
ATOM   5029  O  OG    . SER A 1 2084 ? 170.801 179.823 185.943 1.00 75.38  ? 2084 SER A OG    1 
ATOM   5030  N  N     . HIS A 1 2085 ? 173.604 181.482 186.517 1.00 53.98  ? 2085 HIS A N     1 
ATOM   5031  C  CA    . HIS A 1 2085 ? 174.226 182.690 185.995 1.00 57.59  ? 2085 HIS A CA    1 
ATOM   5032  C  C     . HIS A 1 2085 ? 175.519 183.047 186.720 1.00 66.04  ? 2085 HIS A C     1 
ATOM   5033  O  O     . HIS A 1 2085 ? 176.135 184.071 186.405 1.00 72.69  ? 2085 HIS A O     1 
ATOM   5034  C  CB    . HIS A 1 2085 ? 173.244 183.861 186.063 1.00 62.42  ? 2085 HIS A CB    1 
ATOM   5035  C  CG    . HIS A 1 2085 ? 172.808 184.205 187.452 1.00 55.96  ? 2085 HIS A CG    1 
ATOM   5036  N  ND1   . HIS A 1 2085 ? 171.974 183.396 188.193 1.00 63.43  ? 2085 HIS A ND1   1 
ATOM   5037  C  CD2   . HIS A 1 2085 ? 173.090 185.272 188.236 1.00 57.91  ? 2085 HIS A CD2   1 
ATOM   5038  C  CE1   . HIS A 1 2085 ? 171.762 183.949 189.373 1.00 65.84  ? 2085 HIS A CE1   1 
ATOM   5039  N  NE2   . HIS A 1 2085 ? 172.427 185.089 189.424 1.00 65.87  ? 2085 HIS A NE2   1 
ATOM   5040  N  N     . TYR A 1 2086 ? 175.947 182.227 187.675 1.00 73.23  ? 2086 TYR A N     1 
ATOM   5041  C  CA    . TYR A 1 2086 ? 177.161 182.482 188.439 1.00 67.04  ? 2086 TYR A CA    1 
ATOM   5042  C  C     . TYR A 1 2086 ? 178.379 182.057 187.633 1.00 69.34  ? 2086 TYR A C     1 
ATOM   5043  O  O     . TYR A 1 2086 ? 178.417 180.947 187.092 1.00 72.57  ? 2086 TYR A O     1 
ATOM   5044  C  CB    . TYR A 1 2086 ? 177.141 181.744 189.778 1.00 64.67  ? 2086 TYR A CB    1 
ATOM   5045  C  CG    . TYR A 1 2086 ? 176.309 182.409 190.851 1.00 58.95  ? 2086 TYR A CG    1 
ATOM   5046  C  CD1   . TYR A 1 2086 ? 176.444 182.043 192.181 1.00 64.93  ? 2086 TYR A CD1   1 
ATOM   5047  C  CD2   . TYR A 1 2086 ? 175.396 183.404 190.537 1.00 69.04  ? 2086 TYR A CD2   1 
ATOM   5048  C  CE1   . TYR A 1 2086 ? 175.693 182.645 193.166 1.00 70.62  ? 2086 TYR A CE1   1 
ATOM   5049  C  CE2   . TYR A 1 2086 ? 174.639 184.010 191.516 1.00 76.58  ? 2086 TYR A CE2   1 
ATOM   5050  C  CZ    . TYR A 1 2086 ? 174.791 183.627 192.829 1.00 75.69  ? 2086 TYR A CZ    1 
ATOM   5051  O  OH    . TYR A 1 2086 ? 174.039 184.229 193.811 1.00 81.57  ? 2086 TYR A OH    1 
ATOM   5052  N  N     . ASP A 1 2087 ? 179.372 182.940 187.560 1.00 78.19  ? 2087 ASP A N     1 
ATOM   5053  C  CA    . ASP A 1 2087 ? 180.645 182.637 186.922 1.00 76.76  ? 2087 ASP A CA    1 
ATOM   5054  C  C     . ASP A 1 2087 ? 181.767 183.265 187.730 1.00 79.29  ? 2087 ASP A C     1 
ATOM   5055  O  O     . ASP A 1 2087 ? 181.705 184.453 188.063 1.00 78.27  ? 2087 ASP A O     1 
ATOM   5056  C  CB    . ASP A 1 2087 ? 180.689 183.151 185.482 1.00 80.29  ? 2087 ASP A CB    1 
ATOM   5057  C  CG    . ASP A 1 2087 ? 182.103 183.281 184.960 1.00 88.11  ? 2087 ASP A CG    1 
ATOM   5058  O  OD1   . ASP A 1 2087 ? 182.802 182.249 184.875 1.00 84.21  ? 2087 ASP A OD1   1 
ATOM   5059  O  OD2   . ASP A 1 2087 ? 182.520 184.414 184.643 1.00 87.93  ? 2087 ASP A OD2   1 
ATOM   5060  N  N     . PHE A 1 2088 ? 182.789 182.472 188.039 1.00 79.12  ? 2088 PHE A N     1 
ATOM   5061  C  CA    . PHE A 1 2088 ? 183.943 182.943 188.796 1.00 75.10  ? 2088 PHE A CA    1 
ATOM   5062  C  C     . PHE A 1 2088 ? 185.228 182.406 188.185 1.00 75.10  ? 2088 PHE A C     1 
ATOM   5063  O  O     . PHE A 1 2088 ? 186.173 182.045 188.893 1.00 80.41  ? 2088 PHE A O     1 
ATOM   5064  C  CB    . PHE A 1 2088 ? 183.828 182.554 190.268 1.00 74.06  ? 2088 PHE A CB    1 
ATOM   5065  C  CG    . PHE A 1 2088 ? 182.583 183.068 190.926 1.00 73.50  ? 2088 PHE A CG    1 
ATOM   5066  C  CD1   . PHE A 1 2088 ? 182.418 184.422 191.156 1.00 77.31  ? 2088 PHE A CD1   1 
ATOM   5067  C  CD2   . PHE A 1 2088 ? 181.571 182.202 191.299 1.00 74.21  ? 2088 PHE A CD2   1 
ATOM   5068  C  CE1   . PHE A 1 2088 ? 181.273 184.902 191.755 1.00 76.60  ? 2088 PHE A CE1   1 
ATOM   5069  C  CE2   . PHE A 1 2088 ? 180.423 182.678 191.898 1.00 77.97  ? 2088 PHE A CE2   1 
ATOM   5070  C  CZ    . PHE A 1 2088 ? 180.274 184.030 192.124 1.00 80.72  ? 2088 PHE A CZ    1 
ATOM   5071  N  N     . GLY A 1 2089 ? 185.278 182.351 186.856 1.00 70.04  ? 2089 GLY A N     1 
ATOM   5072  C  CA    . GLY A 1 2089 ? 186.444 181.877 186.145 1.00 68.92  ? 2089 GLY A CA    1 
ATOM   5073  C  C     . GLY A 1 2089 ? 187.501 182.954 185.993 1.00 69.85  ? 2089 GLY A C     1 
ATOM   5074  O  O     . GLY A 1 2089 ? 187.549 183.938 186.732 1.00 72.81  ? 2089 GLY A O     1 
ATOM   5075  N  N     . LEU A 1 2090 ? 188.370 182.749 185.002 1.00 65.43  ? 2090 LEU A N     1 
ATOM   5076  C  CA    . LEU A 1 2090 ? 189.467 183.684 184.777 1.00 64.77  ? 2090 LEU A CA    1 
ATOM   5077  C  C     . LEU A 1 2090 ? 188.964 185.010 184.219 1.00 65.46  ? 2090 LEU A C     1 
ATOM   5078  O  O     . LEU A 1 2090 ? 189.558 186.063 184.476 1.00 73.40  ? 2090 LEU A O     1 
ATOM   5079  C  CB    . LEU A 1 2090 ? 190.502 183.060 183.843 1.00 61.59  ? 2090 LEU A CB    1 
ATOM   5080  C  CG    . LEU A 1 2090 ? 191.718 183.915 183.489 1.00 60.78  ? 2090 LEU A CG    1 
ATOM   5081  C  CD1   . LEU A 1 2090 ? 192.487 184.297 184.738 1.00 63.49  ? 2090 LEU A CD1   1 
ATOM   5082  C  CD2   . LEU A 1 2090 ? 192.614 183.167 182.524 1.00 70.88  ? 2090 LEU A CD2   1 
ATOM   5083  N  N     . ARG A 1 2091 ? 187.873 184.981 183.449 1.00 61.15  ? 2091 ARG A N     1 
ATOM   5084  C  CA    . ARG A 1 2091 ? 187.335 186.218 182.890 1.00 60.15  ? 2091 ARG A CA    1 
ATOM   5085  C  C     . ARG A 1 2091 ? 186.837 187.149 183.988 1.00 64.60  ? 2091 ARG A C     1 
ATOM   5086  O  O     . ARG A 1 2091 ? 187.034 188.370 183.918 1.00 75.65  ? 2091 ARG A O     1 
ATOM   5087  C  CB    . ARG A 1 2091 ? 186.211 185.903 181.905 1.00 61.01  ? 2091 ARG A CB    1 
ATOM   5088  C  CG    . ARG A 1 2091 ? 186.324 186.645 180.585 1.00 64.97  ? 2091 ARG A CG    1 
ATOM   5089  C  CD    . ARG A 1 2091 ? 185.136 186.351 179.689 1.00 68.64  ? 2091 ARG A CD    1 
ATOM   5090  N  NE    . ARG A 1 2091 ? 184.999 184.927 179.411 1.00 69.46  ? 2091 ARG A NE    1 
ATOM   5091  C  CZ    . ARG A 1 2091 ? 185.497 184.321 178.343 1.00 66.63  ? 2091 ARG A CZ    1 
ATOM   5092  N  NH1   . ARG A 1 2091 ? 186.185 184.986 177.430 1.00 64.46  ? 2091 ARG A NH1   1 
ATOM   5093  N  NH2   . ARG A 1 2091 ? 185.299 183.016 178.186 1.00 61.48  ? 2091 ARG A NH2   1 
ATOM   5094  N  N     . ALA A 1 2092 ? 186.183 186.591 185.007 1.00 56.51  ? 2092 ALA A N     1 
ATOM   5095  C  CA    . ALA A 1 2092 ? 185.714 187.404 186.123 1.00 58.27  ? 2092 ALA A CA    1 
ATOM   5096  C  C     . ALA A 1 2092 ? 186.882 188.048 186.858 1.00 61.17  ? 2092 ALA A C     1 
ATOM   5097  O  O     . ALA A 1 2092 ? 186.827 189.229 187.223 1.00 66.86  ? 2092 ALA A O     1 
ATOM   5098  C  CB    . ALA A 1 2092 ? 184.881 186.545 187.074 1.00 62.44  ? 2092 ALA A CB    1 
ATOM   5099  N  N     . LEU A 1 2093 ? 187.954 187.285 187.078 1.00 62.98  ? 2093 LEU A N     1 
ATOM   5100  C  CA    . LEU A 1 2093 ? 189.134 187.838 187.734 1.00 58.27  ? 2093 LEU A CA    1 
ATOM   5101  C  C     . LEU A 1 2093 ? 189.776 188.927 186.884 1.00 58.38  ? 2093 LEU A C     1 
ATOM   5102  O  O     . LEU A 1 2093 ? 190.244 189.942 187.411 1.00 65.33  ? 2093 LEU A O     1 
ATOM   5103  C  CB    . LEU A 1 2093 ? 190.135 186.724 188.034 1.00 49.55  ? 2093 LEU A CB    1 
ATOM   5104  C  CG    . LEU A 1 2093 ? 191.400 187.130 188.787 1.00 49.57  ? 2093 LEU A CG    1 
ATOM   5105  C  CD1   . LEU A 1 2093 ? 191.077 187.456 190.234 1.00 59.00  ? 2093 LEU A CD1   1 
ATOM   5106  C  CD2   . LEU A 1 2093 ? 192.442 186.030 188.705 1.00 57.70  ? 2093 LEU A CD2   1 
ATOM   5107  N  N     . LYS A 1 2094 ? 189.813 188.729 185.565 1.00 61.82  ? 2094 LYS A N     1 
ATOM   5108  C  CA    . LYS A 1 2094 ? 190.348 189.749 184.668 1.00 56.45  ? 2094 LYS A CA    1 
ATOM   5109  C  C     . LYS A 1 2094 ? 189.545 191.040 184.764 1.00 63.07  ? 2094 LYS A C     1 
ATOM   5110  O  O     . LYS A 1 2094 ? 190.111 192.138 184.846 1.00 70.30  ? 2094 LYS A O     1 
ATOM   5111  C  CB    . LYS A 1 2094 ? 190.346 189.220 183.234 1.00 52.74  ? 2094 LYS A CB    1 
ATOM   5112  C  CG    . LYS A 1 2094 ? 190.988 190.140 182.216 1.00 56.47  ? 2094 LYS A CG    1 
ATOM   5113  C  CD    . LYS A 1 2094 ? 192.487 190.228 182.402 1.00 58.95  ? 2094 LYS A CD    1 
ATOM   5114  C  CE    . LYS A 1 2094 ? 193.094 191.189 181.396 1.00 68.53  ? 2094 LYS A CE    1 
ATOM   5115  N  NZ    . LYS A 1 2094 ? 192.858 190.755 179.993 1.00 68.47  ? 2094 LYS A NZ    1 
ATOM   5116  N  N     . SER A 1 2095 ? 188.215 190.923 184.755 1.00 61.44  ? 2095 SER A N     1 
ATOM   5117  C  CA    . SER A 1 2095 ? 187.371 192.105 184.885 1.00 61.57  ? 2095 SER A CA    1 
ATOM   5118  C  C     . SER A 1 2095 ? 187.589 192.786 186.230 1.00 65.60  ? 2095 SER A C     1 
ATOM   5119  O  O     . SER A 1 2095 ? 187.645 194.019 186.309 1.00 68.35  ? 2095 SER A O     1 
ATOM   5120  C  CB    . SER A 1 2095 ? 185.901 191.727 184.706 1.00 60.38  ? 2095 SER A CB    1 
ATOM   5121  O  OG    . SER A 1 2095 ? 185.445 190.929 185.783 1.00 69.40  ? 2095 SER A OG    1 
ATOM   5122  N  N     . VAL A 1 2096 ? 187.722 191.995 187.297 1.00 60.86  ? 2096 VAL A N     1 
ATOM   5123  C  CA    . VAL A 1 2096 ? 187.958 192.557 188.624 1.00 59.52  ? 2096 VAL A CA    1 
ATOM   5124  C  C     . VAL A 1 2096 ? 189.269 193.331 188.655 1.00 58.08  ? 2096 VAL A C     1 
ATOM   5125  O  O     . VAL A 1 2096 ? 189.337 194.440 189.193 1.00 68.33  ? 2096 VAL A O     1 
ATOM   5126  C  CB    . VAL A 1 2096 ? 187.930 191.444 189.688 1.00 58.58  ? 2096 VAL A CB    1 
ATOM   5127  C  CG1   . VAL A 1 2096 ? 188.752 191.841 190.902 1.00 53.40  ? 2096 VAL A CG1   1 
ATOM   5128  C  CG2   . VAL A 1 2096 ? 186.502 191.140 190.093 1.00 59.96  ? 2096 VAL A CG2   1 
ATOM   5129  N  N     . LEU A 1 2097 ? 190.330 192.763 188.077 1.00 52.56  ? 2097 LEU A N     1 
ATOM   5130  C  CA    . LEU A 1 2097 ? 191.627 193.435 188.090 1.00 50.49  ? 2097 LEU A CA    1 
ATOM   5131  C  C     . LEU A 1 2097 ? 191.605 194.714 187.260 1.00 60.94  ? 2097 LEU A C     1 
ATOM   5132  O  O     . LEU A 1 2097 ? 192.175 195.736 187.668 1.00 69.48  ? 2097 LEU A O     1 
ATOM   5133  C  CB    . LEU A 1 2097 ? 192.713 192.487 187.588 1.00 48.24  ? 2097 LEU A CB    1 
ATOM   5134  C  CG    . LEU A 1 2097 ? 192.923 191.218 188.413 1.00 52.37  ? 2097 LEU A CG    1 
ATOM   5135  C  CD1   . LEU A 1 2097 ? 193.834 190.252 187.680 1.00 51.68  ? 2097 LEU A CD1   1 
ATOM   5136  C  CD2   . LEU A 1 2097 ? 193.476 191.549 189.787 1.00 62.45  ? 2097 LEU A CD2   1 
ATOM   5137  N  N     . VAL A 1 2098 ? 190.961 194.681 186.091 1.00 61.06  ? 2098 VAL A N     1 
ATOM   5138  C  CA    . VAL A 1 2098 ? 190.872 195.886 185.268 1.00 62.37  ? 2098 VAL A CA    1 
ATOM   5139  C  C     . VAL A 1 2098 ? 190.090 196.973 185.998 1.00 67.14  ? 2098 VAL A C     1 
ATOM   5140  O  O     . VAL A 1 2098 ? 190.488 198.148 186.014 1.00 76.18  ? 2098 VAL A O     1 
ATOM   5141  C  CB    . VAL A 1 2098 ? 190.246 195.553 183.901 1.00 57.54  ? 2098 VAL A CB    1 
ATOM   5142  C  CG1   . VAL A 1 2098 ? 189.881 196.826 183.158 1.00 59.97  ? 2098 VAL A CG1   1 
ATOM   5143  C  CG2   . VAL A 1 2098 ? 191.203 194.709 183.077 1.00 62.73  ? 2098 VAL A CG2   1 
ATOM   5144  N  N     . SER A 1 2099 ? 188.970 196.597 186.622 1.00 57.31  ? 2099 SER A N     1 
ATOM   5145  C  CA    . SER A 1 2099 ? 188.190 197.564 187.383 1.00 64.26  ? 2099 SER A CA    1 
ATOM   5146  C  C     . SER A 1 2099 ? 188.985 198.108 188.562 1.00 67.78  ? 2099 SER A C     1 
ATOM   5147  O  O     . SER A 1 2099 ? 188.868 199.287 188.903 1.00 75.14  ? 2099 SER A O     1 
ATOM   5148  C  CB    . SER A 1 2099 ? 186.887 196.926 187.862 1.00 72.20  ? 2099 SER A CB    1 
ATOM   5149  O  OG    . SER A 1 2099 ? 186.310 197.678 188.914 1.00 76.64  ? 2099 SER A OG    1 
ATOM   5150  N  N     . ALA A 1 2100 ? 189.798 197.261 189.198 1.00 56.41  ? 2100 ALA A N     1 
ATOM   5151  C  CA    . ALA A 1 2100 ? 190.628 197.722 190.305 1.00 60.12  ? 2100 ALA A CA    1 
ATOM   5152  C  C     . ALA A 1 2100 ? 191.653 198.744 189.837 1.00 64.45  ? 2100 ALA A C     1 
ATOM   5153  O  O     . ALA A 1 2100 ? 191.889 199.751 190.513 1.00 76.79  ? 2100 ALA A O     1 
ATOM   5154  C  CB    . ALA A 1 2100 ? 191.321 196.535 190.972 1.00 59.73  ? 2100 ALA A CB    1 
ATOM   5155  N  N     . GLY A 1 2101 ? 192.276 198.498 188.684 1.00 62.78  ? 2101 GLY A N     1 
ATOM   5156  C  CA    . GLY A 1 2101 ? 193.200 199.481 188.139 1.00 58.88  ? 2101 GLY A CA    1 
ATOM   5157  C  C     . GLY A 1 2101 ? 192.520 200.803 187.836 1.00 67.21  ? 2101 GLY A C     1 
ATOM   5158  O  O     . GLY A 1 2101 ? 193.038 201.879 188.160 1.00 76.39  ? 2101 GLY A O     1 
ATOM   5159  N  N     . ASN A 1 2102 ? 191.335 200.738 187.223 1.00 71.85  ? 2102 ASN A N     1 
ATOM   5160  C  CA    . ASN A 1 2102 ? 190.595 201.961 186.921 1.00 69.42  ? 2102 ASN A CA    1 
ATOM   5161  C  C     . ASN A 1 2102 ? 190.213 202.707 188.196 1.00 76.67  ? 2102 ASN A C     1 
ATOM   5162  O  O     . ASN A 1 2102 ? 190.302 203.940 188.256 1.00 84.92  ? 2102 ASN A O     1 
ATOM   5163  C  CB    . ASN A 1 2102 ? 189.350 201.633 186.098 1.00 67.73  ? 2102 ASN A CB    1 
ATOM   5164  C  CG    . ASN A 1 2102 ? 189.685 201.184 184.690 1.00 78.92  ? 2102 ASN A CG    1 
ATOM   5165  O  OD1   . ASN A 1 2102 ? 190.800 201.387 184.211 1.00 82.93  ? 2102 ASN A OD1   1 
ATOM   5166  N  ND2   . ASN A 1 2102 ? 188.719 200.568 184.019 1.00 78.26  ? 2102 ASN A ND2   1 
ATOM   5167  N  N     . VAL A 1 2103 ? 189.788 201.973 189.226 1.00 72.52  ? 2103 VAL A N     1 
ATOM   5168  C  CA    . VAL A 1 2103 ? 189.399 202.596 190.487 1.00 71.26  ? 2103 VAL A CA    1 
ATOM   5169  C  C     . VAL A 1 2103 ? 190.603 203.242 191.160 1.00 75.84  ? 2103 VAL A C     1 
ATOM   5170  O  O     . VAL A 1 2103 ? 190.498 204.334 191.728 1.00 84.00  ? 2103 VAL A O     1 
ATOM   5171  C  CB    . VAL A 1 2103 ? 188.718 201.563 191.402 1.00 68.10  ? 2103 VAL A CB    1 
ATOM   5172  C  CG1   . VAL A 1 2103 ? 188.654 202.069 192.832 1.00 71.29  ? 2103 VAL A CG1   1 
ATOM   5173  C  CG2   . VAL A 1 2103 ? 187.323 201.247 190.891 1.00 76.92  ? 2103 VAL A CG2   1 
ATOM   5174  N  N     . LYS A 1 2104 ? 191.762 202.581 191.116 1.00 70.92  ? 2104 LYS A N     1 
ATOM   5175  C  CA    . LYS A 1 2104 ? 192.964 203.183 191.684 1.00 67.29  ? 2104 LYS A CA    1 
ATOM   5176  C  C     . LYS A 1 2104 ? 193.326 204.471 190.958 1.00 70.87  ? 2104 LYS A C     1 
ATOM   5177  O  O     . LYS A 1 2104 ? 193.682 205.472 191.593 1.00 81.64  ? 2104 LYS A O     1 
ATOM   5178  C  CB    . LYS A 1 2104 ? 194.130 202.198 191.631 1.00 66.41  ? 2104 LYS A CB    1 
ATOM   5179  C  CG    . LYS A 1 2104 ? 195.365 202.691 192.364 1.00 67.91  ? 2104 LYS A CG    1 
ATOM   5180  C  CD    . LYS A 1 2104 ? 196.492 201.680 192.308 1.00 71.47  ? 2104 LYS A CD    1 
ATOM   5181  C  CE    . LYS A 1 2104 ? 197.282 201.817 191.019 1.00 75.79  ? 2104 LYS A CE    1 
ATOM   5182  N  NZ    . LYS A 1 2104 ? 198.043 203.096 190.970 1.00 69.63  ? 2104 LYS A NZ    1 
ATOM   5183  N  N     . ARG A 1 2105 ? 193.240 204.467 189.625 1.00 77.28  ? 2105 ARG A N     1 
ATOM   5184  C  CA    . ARG A 1 2105 ? 193.535 205.686 188.877 1.00 81.38  ? 2105 ARG A CA    1 
ATOM   5185  C  C     . ARG A 1 2105 ? 192.561 206.804 189.234 1.00 84.63  ? 2105 ARG A C     1 
ATOM   5186  O  O     . ARG A 1 2105 ? 192.969 207.958 189.428 1.00 94.55  ? 2105 ARG A O     1 
ATOM   5187  C  CB    . ARG A 1 2105 ? 193.508 205.406 187.375 1.00 84.22  ? 2105 ARG A CB    1 
ATOM   5188  C  CG    . ARG A 1 2105 ? 194.884 205.407 186.726 1.00 81.97  ? 2105 ARG A CG    1 
ATOM   5189  C  CD    . ARG A 1 2105 ? 194.791 205.190 185.224 1.00 87.13  ? 2105 ARG A CD    1 
ATOM   5190  N  NE    . ARG A 1 2105 ? 193.937 204.060 184.878 1.00 80.89  ? 2105 ARG A NE    1 
ATOM   5191  C  CZ    . ARG A 1 2105 ? 194.265 202.787 185.055 1.00 84.91  ? 2105 ARG A CZ    1 
ATOM   5192  N  NH1   . ARG A 1 2105 ? 195.436 202.439 185.564 1.00 85.30  ? 2105 ARG A NH1   1 
ATOM   5193  N  NH2   . ARG A 1 2105 ? 193.398 201.840 184.709 1.00 86.05  ? 2105 ARG A NH2   1 
ATOM   5194  N  N     . GLU A 1 2106 ? 191.270 206.480 189.342 1.00 82.00  ? 2106 GLU A N     1 
ATOM   5195  C  CA    . GLU A 1 2106 ? 190.285 207.509 189.663 1.00 83.40  ? 2106 GLU A CA    1 
ATOM   5196  C  C     . GLU A 1 2106 ? 190.476 208.037 191.082 1.00 86.12  ? 2106 GLU A C     1 
ATOM   5197  O  O     . GLU A 1 2106 ? 190.283 209.230 191.336 1.00 88.71  ? 2106 GLU A O     1 
ATOM   5198  C  CB    . GLU A 1 2106 ? 188.865 206.972 189.457 1.00 86.16  ? 2106 GLU A CB    1 
ATOM   5199  C  CG    . GLU A 1 2106 ? 188.241 206.279 190.659 1.00 91.15  ? 2106 GLU A CG    1 
ATOM   5200  C  CD    . GLU A 1 2106 ? 186.746 206.086 190.512 1.00 95.64  ? 2106 GLU A CD    1 
ATOM   5201  O  OE1   . GLU A 1 2106 ? 186.041 206.093 191.543 1.00 93.55  ? 2106 GLU A OE1   1 
ATOM   5202  O  OE2   . GLU A 1 2106 ? 186.275 205.928 189.366 1.00 96.49  ? 2106 GLU A OE2   1 
ATOM   5203  N  N     . ARG A 1 2107 ? 190.877 207.171 192.017 1.00 84.99  ? 2107 ARG A N     1 
ATOM   5204  C  CA    . ARG A 1 2107 ? 191.127 207.625 193.382 1.00 86.36  ? 2107 ARG A CA    1 
ATOM   5205  C  C     . ARG A 1 2107 ? 192.353 208.524 193.445 1.00 89.97  ? 2107 ARG A C     1 
ATOM   5206  O  O     . ARG A 1 2107 ? 192.358 209.526 194.172 1.00 94.87  ? 2107 ARG A O     1 
ATOM   5207  C  CB    . ARG A 1 2107 ? 191.290 206.429 194.317 1.00 83.06  ? 2107 ARG A CB    1 
ATOM   5208  C  CG    . ARG A 1 2107 ? 189.985 205.741 194.670 1.00 86.15  ? 2107 ARG A CG    1 
ATOM   5209  C  CD    . ARG A 1 2107 ? 190.053 205.100 196.044 1.00 85.26  ? 2107 ARG A CD    1 
ATOM   5210  N  NE    . ARG A 1 2107 ? 188.883 204.274 196.314 1.00 91.18  ? 2107 ARG A NE    1 
ATOM   5211  C  CZ    . ARG A 1 2107 ? 188.642 203.673 197.470 1.00 94.17  ? 2107 ARG A CZ    1 
ATOM   5212  N  NH1   . ARG A 1 2107 ? 189.473 203.782 198.493 1.00 91.54  ? 2107 ARG A NH1   1 
ATOM   5213  N  NH2   . ARG A 1 2107 ? 187.538 202.943 197.604 1.00 90.19  ? 2107 ARG A NH2   1 
ATOM   5214  N  N     . ILE A 1 2108 ? 193.401 208.184 192.692 1.00 89.16  ? 2108 ILE A N     1 
ATOM   5215  C  CA    . ILE A 1 2108 ? 194.573 209.052 192.627 1.00 87.50  ? 2108 ILE A CA    1 
ATOM   5216  C  C     . ILE A 1 2108 ? 194.189 210.414 192.065 1.00 89.70  ? 2108 ILE A C     1 
ATOM   5217  O  O     . ILE A 1 2108 ? 194.592 211.459 192.594 1.00 96.56  ? 2108 ILE A O     1 
ATOM   5218  C  CB    . ILE A 1 2108 ? 195.688 208.385 191.800 1.00 84.27  ? 2108 ILE A CB    1 
ATOM   5219  C  CG1   . ILE A 1 2108 ? 196.511 207.442 192.677 1.00 84.63  ? 2108 ILE A CG1   1 
ATOM   5220  C  CG2   . ILE A 1 2108 ? 196.587 209.428 191.159 1.00 90.85  ? 2108 ILE A CG2   1 
ATOM   5221  C  CD1   . ILE A 1 2108 ? 197.158 206.312 191.911 1.00 89.15  ? 2108 ILE A CD1   1 
ATOM   5222  N  N     . GLN A 1 2109 ? 193.390 210.426 190.994 1.00 93.79  ? 2109 GLN A N     1 
ATOM   5223  C  CA    . GLN A 1 2109 ? 192.962 211.693 190.408 1.00 94.98  ? 2109 GLN A CA    1 
ATOM   5224  C  C     . GLN A 1 2109 ? 192.122 212.504 191.390 1.00 95.24  ? 2109 GLN A C     1 
ATOM   5225  O  O     . GLN A 1 2109 ? 192.273 213.728 191.483 1.00 98.25  ? 2109 GLN A O     1 
ATOM   5226  C  CB    . GLN A 1 2109 ? 192.184 211.438 189.118 1.00 98.70  ? 2109 GLN A CB    1 
ATOM   5227  C  CG    . GLN A 1 2109 ? 193.043 210.945 187.965 1.00 102.13 ? 2109 GLN A CG    1 
ATOM   5228  C  CD    . GLN A 1 2109 ? 194.037 211.987 187.493 1.00 101.13 ? 2109 GLN A CD    1 
ATOM   5229  O  OE1   . GLN A 1 2109 ? 195.246 211.832 187.668 1.00 99.36  ? 2109 GLN A OE1   1 
ATOM   5230  N  NE2   . GLN A 1 2109 ? 193.532 213.057 186.892 1.00 99.00  ? 2109 GLN A NE2   1 
ATOM   5231  N  N     . LYS A 1 2110 ? 191.227 211.840 192.127 1.00 99.26  ? 2110 LYS A N     1 
ATOM   5232  C  CA    . LYS A 1 2110 ? 190.393 212.542 193.097 1.00 101.08 ? 2110 LYS A CA    1 
ATOM   5233  C  C     . LYS A 1 2110 ? 191.232 213.140 194.221 1.00 100.62 ? 2110 LYS A C     1 
ATOM   5234  O  O     . LYS A 1 2110 ? 190.987 214.273 194.655 1.00 105.54 ? 2110 LYS A O     1 
ATOM   5235  C  CB    . LYS A 1 2110 ? 189.338 211.592 193.661 1.00 101.10 ? 2110 LYS A CB    1 
ATOM   5236  C  CG    . LYS A 1 2110 ? 188.000 212.247 193.953 1.00 103.28 ? 2110 LYS A CG    1 
ATOM   5237  C  CD    . LYS A 1 2110 ? 186.893 211.211 194.054 1.00 102.92 ? 2110 LYS A CD    1 
ATOM   5238  C  CE    . LYS A 1 2110 ? 187.169 210.213 195.166 1.00 101.34 ? 2110 LYS A CE    1 
ATOM   5239  N  NZ    . LYS A 1 2110 ? 187.201 210.867 196.503 1.00 101.28 ? 2110 LYS A NZ    1 
ATOM   5240  N  N     . ILE A 1 2111 ? 192.224 212.390 194.708 1.00 100.63 ? 2111 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 2111 ? 193.107 212.914 195.746 1.00 102.86 ? 2111 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 2111 ? 193.881 214.117 195.227 1.00 103.34 ? 2111 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 2111 ? 194.037 215.126 195.928 1.00 102.73 ? 2111 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 2111 ? 194.051 211.809 196.257 1.00 104.88 ? 2111 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 2111 ? 193.268 210.770 197.059 1.00 103.28 ? 2111 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 2111 ? 195.165 212.401 197.103 1.00 104.43 ? 2111 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 2111 ? 194.118 209.626 197.565 1.00 102.07 ? 2111 ILE A CD1   1 
ATOM   5248  N  N     . LYS A 1 2112 ? 194.372 214.036 193.988 1.00 112.75 ? 2112 LYS A N     1 
ATOM   5249  C  CA    . LYS A 1 2112 ? 195.092 215.167 193.412 1.00 112.56 ? 2112 LYS A CA    1 
ATOM   5250  C  C     . LYS A 1 2112 ? 194.195 216.392 193.296 1.00 114.19 ? 2112 LYS A C     1 
ATOM   5251  O  O     . LYS A 1 2112 ? 194.628 217.513 193.586 1.00 116.26 ? 2112 LYS A O     1 
ATOM   5252  C  CB    . LYS A 1 2112 ? 195.664 214.791 192.047 1.00 112.53 ? 2112 LYS A CB    1 
ATOM   5253  C  CG    . LYS A 1 2112 ? 196.727 213.715 192.105 1.00 111.97 ? 2112 LYS A CG    1 
ATOM   5254  C  CD    . LYS A 1 2112 ? 197.733 213.874 190.984 1.00 112.53 ? 2112 LYS A CD    1 
ATOM   5255  C  CE    . LYS A 1 2112 ? 198.461 212.570 190.733 1.00 112.99 ? 2112 LYS A CE    1 
ATOM   5256  N  NZ    . LYS A 1 2112 ? 199.036 212.507 189.363 1.00 114.36 ? 2112 LYS A NZ    1 
ATOM   5257  N  N     . ARG A 1 2113 ? 192.947 216.202 192.858 1.00 120.58 ? 2113 ARG A N     1 
ATOM   5258  C  CA    . ARG A 1 2113 ? 192.025 217.329 192.744 1.00 119.40 ? 2113 ARG A CA    1 
ATOM   5259  C  C     . ARG A 1 2113 ? 191.739 217.946 194.106 1.00 121.57 ? 2113 ARG A C     1 
ATOM   5260  O  O     . ARG A 1 2113 ? 191.704 219.177 194.247 1.00 123.51 ? 2113 ARG A O     1 
ATOM   5261  C  CB    . ARG A 1 2113 ? 190.727 216.886 192.072 1.00 118.88 ? 2113 ARG A CB    1 
ATOM   5262  C  CG    . ARG A 1 2113 ? 190.884 216.465 190.620 1.00 117.83 ? 2113 ARG A CG    1 
ATOM   5263  C  CD    . ARG A 1 2113 ? 189.736 215.599 190.055 1.00 121.42 ? 2113 ARG A CD    1 
ATOM   5264  N  NE    . ARG A 1 2113 ? 188.384 216.116 190.261 1.00 124.79 ? 2113 ARG A NE    1 
ATOM   5265  C  CZ    . ARG A 1 2113 ? 187.677 216.017 191.381 1.00 123.18 ? 2113 ARG A CZ    1 
ATOM   5266  N  NH1   . ARG A 1 2113 ? 188.112 215.321 192.419 1.00 121.37 ? 2113 ARG A NH1   1 
ATOM   5267  N  NH2   . ARG A 1 2113 ? 186.487 216.606 191.450 1.00 121.72 ? 2113 ARG A NH2   1 
ATOM   5268  N  N     . GLU A 1 2114 ? 191.536 217.106 195.123 1.00 126.78 ? 2114 GLU A N     1 
ATOM   5269  C  CA    . GLU A 1 2114 ? 191.333 217.616 196.474 1.00 126.84 ? 2114 GLU A CA    1 
ATOM   5270  C  C     . GLU A 1 2114 ? 192.547 218.403 196.950 1.00 127.18 ? 2114 GLU A C     1 
ATOM   5271  O  O     . GLU A 1 2114 ? 192.408 219.421 197.639 1.00 127.08 ? 2114 GLU A O     1 
ATOM   5272  C  CB    . GLU A 1 2114 ? 191.028 216.460 197.428 1.00 126.69 ? 2114 GLU A CB    1 
ATOM   5273  C  CG    . GLU A 1 2114 ? 191.258 216.776 198.899 1.00 128.43 ? 2114 GLU A CG    1 
ATOM   5274  C  CD    . GLU A 1 2114 ? 191.076 215.563 199.790 1.00 128.24 ? 2114 GLU A CD    1 
ATOM   5275  O  OE1   . GLU A 1 2114 ? 190.153 214.765 199.526 1.00 127.33 ? 2114 GLU A OE1   1 
ATOM   5276  O  OE2   . GLU A 1 2114 ? 191.857 215.407 200.752 1.00 126.30 ? 2114 GLU A OE2   1 
ATOM   5277  N  N     . LYS A 1 2115 ? 193.748 217.955 196.580 1.00 132.65 ? 2115 LYS A N     1 
ATOM   5278  C  CA    . LYS A 1 2115 ? 194.953 218.650 197.017 1.00 131.41 ? 2115 LYS A CA    1 
ATOM   5279  C  C     . LYS A 1 2115 ? 195.131 219.981 196.293 1.00 132.35 ? 2115 LYS A C     1 
ATOM   5280  O  O     . LYS A 1 2115 ? 195.539 220.973 196.907 1.00 134.62 ? 2115 LYS A O     1 
ATOM   5281  C  CB    . LYS A 1 2115 ? 196.178 217.757 196.826 1.00 133.80 ? 2115 LYS A CB    1 
ATOM   5282  C  CG    . LYS A 1 2115 ? 196.378 216.756 197.954 1.00 133.87 ? 2115 LYS A CG    1 
ATOM   5283  C  CD    . LYS A 1 2115 ? 197.517 215.798 197.661 1.00 134.18 ? 2115 LYS A CD    1 
ATOM   5284  C  CE    . LYS A 1 2115 ? 198.010 215.131 198.934 1.00 132.10 ? 2115 LYS A CE    1 
ATOM   5285  N  NZ    . LYS A 1 2115 ? 196.910 214.443 199.664 1.00 132.99 ? 2115 LYS A NZ    1 
ATOM   5286  N  N     . GLU A 1 2116 ? 194.845 220.029 194.987 1.00 135.60 ? 2116 GLU A N     1 
ATOM   5287  C  CA    . GLU A 1 2116 ? 194.991 221.302 194.283 1.00 135.77 ? 2116 GLU A CA    1 
ATOM   5288  C  C     . GLU A 1 2116 ? 193.934 222.304 194.732 1.00 137.57 ? 2116 GLU A C     1 
ATOM   5289  O  O     . GLU A 1 2116 ? 194.219 223.502 194.844 1.00 136.66 ? 2116 GLU A O     1 
ATOM   5290  C  CB    . GLU A 1 2116 ? 194.942 221.141 192.757 1.00 134.48 ? 2116 GLU A CB    1 
ATOM   5291  C  CG    . GLU A 1 2116 ? 193.760 220.389 192.166 1.00 137.43 ? 2116 GLU A CG    1 
ATOM   5292  C  CD    . GLU A 1 2116 ? 194.150 219.538 190.963 1.00 139.29 ? 2116 GLU A CD    1 
ATOM   5293  O  OE1   . GLU A 1 2116 ? 194.110 220.070 189.835 1.00 138.43 ? 2116 GLU A OE1   1 
ATOM   5294  O  OE2   . GLU A 1 2116 ? 194.507 218.355 191.123 1.00 139.45 ? 2116 GLU A OE2   1 
ATOM   5295  N  N     . GLU A 1 2117 ? 192.708 221.843 194.985 1.00 138.72 ? 2117 GLU A N     1 
ATOM   5296  C  CA    . GLU A 1 2117 ? 191.672 222.755 195.452 1.00 138.38 ? 2117 GLU A CA    1 
ATOM   5297  C  C     . GLU A 1 2117 ? 191.888 223.204 196.893 1.00 138.75 ? 2117 GLU A C     1 
ATOM   5298  O  O     . GLU A 1 2117 ? 191.546 224.344 197.229 1.00 139.93 ? 2117 GLU A O     1 
ATOM   5299  C  CB    . GLU A 1 2117 ? 190.293 222.105 195.296 1.00 137.14 ? 2117 GLU A CB    1 
ATOM   5300  C  CG    . GLU A 1 2117 ? 189.262 222.528 196.330 1.00 138.43 ? 2117 GLU A CG    1 
ATOM   5301  C  CD    . GLU A 1 2117 ? 187.848 222.179 195.915 1.00 138.73 ? 2117 GLU A CD    1 
ATOM   5302  O  OE1   . GLU A 1 2117 ? 187.547 220.975 195.777 1.00 137.70 ? 2117 GLU A OE1   1 
ATOM   5303  O  OE2   . GLU A 1 2117 ? 187.039 223.111 195.722 1.00 139.09 ? 2117 GLU A OE2   1 
ATOM   5304  N  N     . ARG A 1 2118 ? 192.473 222.356 197.740 1.00 137.73 ? 2118 ARG A N     1 
ATOM   5305  C  CA    . ARG A 1 2118 ? 192.784 222.689 199.131 1.00 137.30 ? 2118 ARG A CA    1 
ATOM   5306  C  C     . ARG A 1 2118 ? 194.297 222.868 199.231 1.00 139.85 ? 2118 ARG A C     1 
ATOM   5307  O  O     . ARG A 1 2118 ? 195.034 221.900 199.434 1.00 142.57 ? 2118 ARG A O     1 
ATOM   5308  C  CB    . ARG A 1 2118 ? 192.273 221.609 200.085 1.00 137.65 ? 2118 ARG A CB    1 
ATOM   5309  C  CG    . ARG A 1 2118 ? 192.628 221.838 201.549 1.00 136.96 ? 2118 ARG A CG    1 
ATOM   5310  C  CD    . ARG A 1 2118 ? 193.275 220.602 202.163 1.00 137.67 ? 2118 ARG A CD    1 
ATOM   5311  N  NE    . ARG A 1 2118 ? 194.565 220.290 201.559 1.00 140.74 ? 2118 ARG A NE    1 
ATOM   5312  C  CZ    . ARG A 1 2118 ? 195.738 220.650 202.064 1.00 139.07 ? 2118 ARG A CZ    1 
ATOM   5313  N  NH1   . ARG A 1 2118 ? 195.824 221.332 203.194 1.00 138.88 ? 2118 ARG A NH1   1 
ATOM   5314  N  NH2   . ARG A 1 2118 ? 196.852 220.317 201.418 1.00 136.75 ? 2118 ARG A NH2   1 
ATOM   5315  N  N     . GLY A 1 2119 ? 194.756 224.106 199.086 1.00 143.88 ? 2119 GLY A N     1 
ATOM   5316  C  CA    . GLY A 1 2119 ? 196.174 224.388 199.135 1.00 145.41 ? 2119 GLY A CA    1 
ATOM   5317  C  C     . GLY A 1 2119 ? 196.895 223.959 197.870 1.00 147.09 ? 2119 GLY A C     1 
ATOM   5318  O  O     . GLY A 1 2119 ? 196.295 223.693 196.825 1.00 147.02 ? 2119 GLY A O     1 
ATOM   5319  N  N     . GLU A 1 2120 ? 198.224 223.900 197.977 1.00 161.10 ? 2120 GLU A N     1 
ATOM   5320  C  CA    . GLU A 1 2120 ? 199.087 223.482 196.867 1.00 161.17 ? 2120 GLU A CA    1 
ATOM   5321  C  C     . GLU A 1 2120 ? 200.182 222.582 197.438 1.00 160.47 ? 2120 GLU A C     1 
ATOM   5322  O  O     . GLU A 1 2120 ? 201.251 223.057 197.829 1.00 160.41 ? 2120 GLU A O     1 
ATOM   5323  C  CB    . GLU A 1 2120 ? 199.671 224.684 196.136 1.00 160.46 ? 2120 GLU A CB    1 
ATOM   5324  C  CG    . GLU A 1 2120 ? 198.681 225.417 195.247 1.00 160.62 ? 2120 GLU A CG    1 
ATOM   5325  C  CD    . GLU A 1 2120 ? 199.238 226.719 194.707 1.00 161.17 ? 2120 GLU A CD    1 
ATOM   5326  O  OE1   . GLU A 1 2120 ? 200.292 226.684 194.037 1.00 161.40 ? 2120 GLU A OE1   1 
ATOM   5327  O  OE2   . GLU A 1 2120 ? 198.624 227.778 194.955 1.00 161.61 ? 2120 GLU A OE2   1 
ATOM   5328  N  N     . ALA A 1 2121 ? 199.908 221.279 197.477 1.00 150.62 ? 2121 ALA A N     1 
ATOM   5329  C  CA    . ALA A 1 2121 ? 200.894 220.306 197.939 1.00 149.60 ? 2121 ALA A CA    1 
ATOM   5330  C  C     . ALA A 1 2121 ? 200.536 218.956 197.334 1.00 149.22 ? 2121 ALA A C     1 
ATOM   5331  O  O     . ALA A 1 2121 ? 199.567 218.325 197.766 1.00 149.58 ? 2121 ALA A O     1 
ATOM   5332  C  CB    . ALA A 1 2121 ? 200.923 220.239 199.462 1.00 148.31 ? 2121 ALA A CB    1 
ATOM   5333  N  N     . VAL A 1 2122 ? 201.312 218.518 196.346 1.00 148.00 ? 2122 VAL A N     1 
ATOM   5334  C  CA    . VAL A 1 2122 ? 201.080 217.250 195.664 1.00 148.42 ? 2122 VAL A CA    1 
ATOM   5335  C  C     . VAL A 1 2122 ? 202.404 216.507 195.562 1.00 148.30 ? 2122 VAL A C     1 
ATOM   5336  O  O     . VAL A 1 2122 ? 203.392 217.055 195.060 1.00 147.18 ? 2122 VAL A O     1 
ATOM   5337  C  CB    . VAL A 1 2122 ? 200.466 217.458 194.265 1.00 147.34 ? 2122 VAL A CB    1 
ATOM   5338  C  CG1   . VAL A 1 2122 ? 200.697 216.234 193.390 1.00 145.49 ? 2122 VAL A CG1   1 
ATOM   5339  C  CG2   . VAL A 1 2122 ? 198.981 217.766 194.380 1.00 146.60 ? 2122 VAL A CG2   1 
ATOM   5340  N  N     . ASP A 1 2123 ? 202.423 215.265 196.040 1.00 147.90 ? 2123 ASP A N     1 
ATOM   5341  C  CA    . ASP A 1 2123 ? 203.593 214.401 195.926 1.00 147.57 ? 2123 ASP A CA    1 
ATOM   5342  C  C     . ASP A 1 2123 ? 203.127 213.027 195.476 1.00 148.70 ? 2123 ASP A C     1 
ATOM   5343  O  O     . ASP A 1 2123 ? 202.273 212.418 196.128 1.00 147.02 ? 2123 ASP A O     1 
ATOM   5344  C  CB    . ASP A 1 2123 ? 204.353 214.307 197.253 1.00 145.06 ? 2123 ASP A CB    1 
ATOM   5345  C  CG    . ASP A 1 2123 ? 205.510 213.331 197.191 1.00 147.47 ? 2123 ASP A CG    1 
ATOM   5346  O  OD1   . ASP A 1 2123 ? 206.319 213.426 196.245 1.00 147.72 ? 2123 ASP A OD1   1 
ATOM   5347  O  OD2   . ASP A 1 2123 ? 205.613 212.469 198.089 1.00 148.03 ? 2123 ASP A OD2   1 
ATOM   5348  N  N     . GLU A 1 2124 ? 203.684 212.545 194.362 1.00 137.56 ? 2124 GLU A N     1 
ATOM   5349  C  CA    . GLU A 1 2124 ? 203.266 211.253 193.827 1.00 133.33 ? 2124 GLU A CA    1 
ATOM   5350  C  C     . GLU A 1 2124 ? 203.565 210.125 194.806 1.00 132.09 ? 2124 GLU A C     1 
ATOM   5351  O  O     . GLU A 1 2124 ? 202.732 209.234 195.012 1.00 131.23 ? 2124 GLU A O     1 
ATOM   5352  C  CB    . GLU A 1 2124 ? 203.956 210.993 192.489 1.00 132.77 ? 2124 GLU A CB    1 
ATOM   5353  C  CG    . GLU A 1 2124 ? 203.339 211.729 191.315 1.00 132.54 ? 2124 GLU A CG    1 
ATOM   5354  C  CD    . GLU A 1 2124 ? 202.038 211.107 190.851 1.00 133.79 ? 2124 GLU A CD    1 
ATOM   5355  O  OE1   . GLU A 1 2124 ? 201.694 210.006 191.328 1.00 134.29 ? 2124 GLU A OE1   1 
ATOM   5356  O  OE2   . GLU A 1 2124 ? 201.363 211.719 189.999 1.00 134.43 ? 2124 GLU A OE2   1 
ATOM   5357  N  N     . GLY A 1 2125 ? 204.750 210.147 195.418 1.00 136.66 ? 2125 GLY A N     1 
ATOM   5358  C  CA    . GLY A 1 2125 ? 205.092 209.116 196.383 1.00 137.35 ? 2125 GLY A CA    1 
ATOM   5359  C  C     . GLY A 1 2125 ? 204.193 209.135 197.603 1.00 136.48 ? 2125 GLY A C     1 
ATOM   5360  O  O     . GLY A 1 2125 ? 203.798 208.083 198.112 1.00 137.75 ? 2125 GLY A O     1 
ATOM   5361  N  N     . GLU A 1 2126 ? 203.858 210.332 198.090 1.00 140.27 ? 2126 GLU A N     1 
ATOM   5362  C  CA    . GLU A 1 2126 ? 202.986 210.440 199.256 1.00 141.86 ? 2126 GLU A CA    1 
ATOM   5363  C  C     . GLU A 1 2126 ? 201.616 209.836 198.976 1.00 143.46 ? 2126 GLU A C     1 
ATOM   5364  O  O     . GLU A 1 2126 ? 201.053 209.134 199.825 1.00 143.69 ? 2126 GLU A O     1 
ATOM   5365  C  CB    . GLU A 1 2126 ? 202.853 211.903 199.676 1.00 143.46 ? 2126 GLU A CB    1 
ATOM   5366  C  CG    . GLU A 1 2126 ? 202.231 212.106 201.046 1.00 145.16 ? 2126 GLU A CG    1 
ATOM   5367  C  CD    . GLU A 1 2126 ? 202.018 213.571 201.373 1.00 145.16 ? 2126 GLU A CD    1 
ATOM   5368  O  OE1   . GLU A 1 2126 ? 202.188 214.414 200.468 1.00 145.10 ? 2126 GLU A OE1   1 
ATOM   5369  O  OE2   . GLU A 1 2126 ? 201.683 213.879 202.536 1.00 144.82 ? 2126 GLU A OE2   1 
ATOM   5370  N  N     . ILE A 1 2127 ? 201.062 210.100 197.792 1.00 130.95 ? 2127 ILE A N     1 
ATOM   5371  C  CA    . ILE A 1 2127 ? 199.780 209.510 197.424 1.00 129.12 ? 2127 ILE A CA    1 
ATOM   5372  C  C     . ILE A 1 2127 ? 199.912 208.001 197.258 1.00 128.05 ? 2127 ILE A C     1 
ATOM   5373  O  O     . ILE A 1 2127 ? 199.046 207.237 197.702 1.00 128.11 ? 2127 ILE A O     1 
ATOM   5374  C  CB    . ILE A 1 2127 ? 199.233 210.176 196.149 1.00 126.94 ? 2127 ILE A CB    1 
ATOM   5375  C  CG1   . ILE A 1 2127 ? 199.070 211.682 196.363 1.00 127.31 ? 2127 ILE A CG1   1 
ATOM   5376  C  CG2   . ILE A 1 2127 ? 197.907 209.554 195.747 1.00 125.99 ? 2127 ILE A CG2   1 
ATOM   5377  C  CD1   . ILE A 1 2127 ? 198.710 212.440 195.106 1.00 126.26 ? 2127 ILE A CD1   1 
ATOM   5378  N  N     . ALA A 1 2128 ? 200.995 207.547 196.619 1.00 125.23 ? 2128 ALA A N     1 
ATOM   5379  C  CA    . ALA A 1 2128 ? 201.157 206.120 196.353 1.00 122.75 ? 2128 ALA A CA    1 
ATOM   5380  C  C     . ALA A 1 2128 ? 201.268 205.316 197.643 1.00 124.89 ? 2128 ALA A C     1 
ATOM   5381  O  O     . ALA A 1 2128 ? 200.599 204.288 197.800 1.00 125.35 ? 2128 ALA A O     1 
ATOM   5382  C  CB    . ALA A 1 2128 ? 202.382 205.888 195.470 1.00 120.52 ? 2128 ALA A CB    1 
ATOM   5383  N  N     . GLU A 1 2129 ? 202.111 205.763 198.578 1.00 128.76 ? 2129 GLU A N     1 
ATOM   5384  C  CA    . GLU A 1 2129 ? 202.250 205.044 199.842 1.00 125.97 ? 2129 GLU A CA    1 
ATOM   5385  C  C     . GLU A 1 2129 ? 200.975 205.127 200.672 1.00 125.88 ? 2129 GLU A C     1 
ATOM   5386  O  O     . GLU A 1 2129 ? 200.564 204.138 201.289 1.00 126.70 ? 2129 GLU A O     1 
ATOM   5387  C  CB    . GLU A 1 2129 ? 203.444 205.581 200.633 1.00 126.08 ? 2129 GLU A CB    1 
ATOM   5388  C  CG    . GLU A 1 2129 ? 204.749 205.694 199.846 1.00 129.15 ? 2129 GLU A CG    1 
ATOM   5389  C  CD    . GLU A 1 2129 ? 205.443 204.358 199.615 1.00 130.60 ? 2129 GLU A CD    1 
ATOM   5390  O  OE1   . GLU A 1 2129 ? 204.760 203.315 199.534 1.00 126.59 ? 2129 GLU A OE1   1 
ATOM   5391  O  OE2   . GLU A 1 2129 ? 206.687 204.355 199.513 1.00 131.45 ? 2129 GLU A OE2   1 
ATOM   5392  N  N     . ASN A 1 2130 ? 200.338 206.295 200.703 1.00 130.18 ? 2130 ASN A N     1 
ATOM   5393  C  CA    . ASN A 1 2130 ? 199.105 206.485 201.465 1.00 131.97 ? 2130 ASN A CA    1 
ATOM   5394  C  C     . ASN A 1 2130 ? 197.900 206.271 200.550 1.00 130.83 ? 2130 ASN A C     1 
ATOM   5395  O  O     . ASN A 1 2130 ? 197.233 207.205 200.105 1.00 132.00 ? 2130 ASN A O     1 
ATOM   5396  C  CB    . ASN A 1 2130 ? 199.088 207.867 202.109 1.00 132.73 ? 2130 ASN A CB    1 
ATOM   5397  C  CG    . ASN A 1 2130 ? 200.293 208.112 202.995 1.00 133.98 ? 2130 ASN A CG    1 
ATOM   5398  O  OD1   . ASN A 1 2130 ? 200.640 207.281 203.834 1.00 133.82 ? 2130 ASN A OD1   1 
ATOM   5399  N  ND2   . ASN A 1 2130 ? 200.937 209.259 202.813 1.00 132.42 ? 2130 ASN A ND2   1 
ATOM   5400  N  N     . LEU A 1 2131 ? 197.631 204.993 200.272 1.00 111.15 ? 2131 LEU A N     1 
ATOM   5401  C  CA    . LEU A 1 2131 ? 196.524 204.606 199.415 1.00 108.39 ? 2131 LEU A CA    1 
ATOM   5402  C  C     . LEU A 1 2131 ? 195.985 203.255 199.873 1.00 111.73 ? 2131 LEU A C     1 
ATOM   5403  O  O     . LEU A 1 2131 ? 196.761 202.288 199.991 1.00 108.42 ? 2131 LEU A O     1 
ATOM   5404  C  CB    . LEU A 1 2131 ? 196.959 204.542 197.949 1.00 107.24 ? 2131 LEU A CB    1 
ATOM   5405  C  CG    . LEU A 1 2131 ? 195.845 204.475 196.906 1.00 104.37 ? 2131 LEU A CG    1 
ATOM   5406  C  CD1   . LEU A 1 2131 ? 195.224 205.845 196.706 1.00 108.04 ? 2131 LEU A CD1   1 
ATOM   5407  C  CD2   . LEU A 1 2131 ? 196.392 203.943 195.597 1.00 104.90 ? 2131 LEU A CD2   1 
ATOM   5408  N  N     . PRO A 1 2132 ? 194.684 203.148 200.140 1.00 111.83 ? 2132 PRO A N     1 
ATOM   5409  C  CA    . PRO A 1 2132 ? 194.084 201.861 200.555 1.00 107.34 ? 2132 PRO A CA    1 
ATOM   5410  C  C     . PRO A 1 2132 ? 193.844 200.920 199.376 1.00 105.93 ? 2132 PRO A C     1 
ATOM   5411  O  O     . PRO A 1 2132 ? 192.762 200.833 198.797 1.00 108.15 ? 2132 PRO A O     1 
ATOM   5412  C  CB    . PRO A 1 2132 ? 192.778 202.301 201.219 1.00 103.50 ? 2132 PRO A CB    1 
ATOM   5413  C  CG    . PRO A 1 2132 ? 192.411 203.560 200.511 1.00 102.36 ? 2132 PRO A CG    1 
ATOM   5414  C  CD    . PRO A 1 2132 ? 193.702 204.247 200.147 1.00 106.13 ? 2132 PRO A CD    1 
ATOM   5415  N  N     . GLU A 1 2133 ? 194.899 200.193 199.001 1.00 93.27  ? 2133 GLU A N     1 
ATOM   5416  C  CA    . GLU A 1 2133 ? 194.802 199.268 197.876 1.00 93.20  ? 2133 GLU A CA    1 
ATOM   5417  C  C     . GLU A 1 2133 ? 193.815 198.144 198.166 1.00 96.77  ? 2133 GLU A C     1 
ATOM   5418  O  O     . GLU A 1 2133 ? 193.093 197.692 197.268 1.00 102.93 ? 2133 GLU A O     1 
ATOM   5419  C  CB    . GLU A 1 2133 ? 196.181 198.704 197.544 1.00 90.31  ? 2133 GLU A CB    1 
ATOM   5420  C  CG    . GLU A 1 2133 ? 197.154 199.743 197.017 1.00 94.51  ? 2133 GLU A CG    1 
ATOM   5421  C  CD    . GLU A 1 2133 ? 198.532 199.173 196.761 1.00 96.95  ? 2133 GLU A CD    1 
ATOM   5422  O  OE1   . GLU A 1 2133 ? 198.755 197.988 197.085 1.00 98.73  ? 2133 GLU A OE1   1 
ATOM   5423  O  OE2   . GLU A 1 2133 ? 199.393 199.911 196.238 1.00 96.67  ? 2133 GLU A OE2   1 
ATOM   5424  N  N     . GLN A 1 2134 ? 193.774 197.677 199.416 1.00 81.38  ? 2134 GLN A N     1 
ATOM   5425  C  CA    . GLN A 1 2134 ? 192.790 196.672 199.801 1.00 78.91  ? 2134 GLN A CA    1 
ATOM   5426  C  C     . GLN A 1 2134 ? 191.375 197.190 199.584 1.00 82.25  ? 2134 GLN A C     1 
ATOM   5427  O  O     . GLN A 1 2134 ? 190.511 196.478 199.061 1.00 89.28  ? 2134 GLN A O     1 
ATOM   5428  C  CB    . GLN A 1 2134 ? 192.997 196.272 201.262 1.00 86.07  ? 2134 GLN A CB    1 
ATOM   5429  C  CG    . GLN A 1 2134 ? 194.330 195.603 201.548 1.00 88.16  ? 2134 GLN A CG    1 
ATOM   5430  C  CD    . GLN A 1 2134 ? 194.192 194.118 201.808 1.00 89.52  ? 2134 GLN A CD    1 
ATOM   5431  O  OE1   . GLN A 1 2134 ? 194.084 193.321 200.878 1.00 87.89  ? 2134 GLN A OE1   1 
ATOM   5432  N  NE2   . GLN A 1 2134 ? 194.192 193.738 203.080 1.00 88.04  ? 2134 GLN A NE2   1 
ATOM   5433  N  N     . GLU A 1 2135 ? 191.124 198.441 199.979 1.00 85.07  ? 2135 GLU A N     1 
ATOM   5434  C  CA    . GLU A 1 2135 ? 189.809 199.037 199.767 1.00 81.81  ? 2135 GLU A CA    1 
ATOM   5435  C  C     . GLU A 1 2135 ? 189.485 199.148 198.284 1.00 83.17  ? 2135 GLU A C     1 
ATOM   5436  O  O     . GLU A 1 2135 ? 188.339 198.936 197.879 1.00 83.77  ? 2135 GLU A O     1 
ATOM   5437  C  CB    . GLU A 1 2135 ? 189.739 200.409 200.436 1.00 89.74  ? 2135 GLU A CB    1 
ATOM   5438  C  CG    . GLU A 1 2135 ? 188.326 200.941 200.608 1.00 90.06  ? 2135 GLU A CG    1 
ATOM   5439  C  CD    . GLU A 1 2135 ? 188.221 201.979 201.707 1.00 93.27  ? 2135 GLU A CD    1 
ATOM   5440  O  OE1   . GLU A 1 2135 ? 189.044 202.918 201.721 1.00 88.50  ? 2135 GLU A OE1   1 
ATOM   5441  O  OE2   . GLU A 1 2135 ? 187.314 201.858 202.556 1.00 95.96  ? 2135 GLU A OE2   1 
ATOM   5442  N  N     . ILE A 1 2136 ? 190.480 199.484 197.461 1.00 76.88  ? 2136 ILE A N     1 
ATOM   5443  C  CA    . ILE A 1 2136 ? 190.262 199.582 196.019 1.00 72.64  ? 2136 ILE A CA    1 
ATOM   5444  C  C     . ILE A 1 2136 ? 189.865 198.226 195.448 1.00 74.05  ? 2136 ILE A C     1 
ATOM   5445  O  O     . ILE A 1 2136 ? 188.919 198.112 194.655 1.00 81.42  ? 2136 ILE A O     1 
ATOM   5446  C  CB    . ILE A 1 2136 ? 191.520 200.137 195.329 1.00 70.78  ? 2136 ILE A CB    1 
ATOM   5447  C  CG1   . ILE A 1 2136 ? 191.734 201.602 195.711 1.00 73.92  ? 2136 ILE A CG1   1 
ATOM   5448  C  CG2   . ILE A 1 2136 ? 191.425 199.970 193.823 1.00 76.38  ? 2136 ILE A CG2   1 
ATOM   5449  C  CD1   . ILE A 1 2136 ? 193.126 202.106 195.421 1.00 78.20  ? 2136 ILE A CD1   1 
ATOM   5450  N  N     . LEU A 1 2137 ? 190.588 197.176 195.842 1.00 72.34  ? 2137 LEU A N     1 
ATOM   5451  C  CA    . LEU A 1 2137 ? 190.274 195.841 195.345 1.00 69.17  ? 2137 LEU A CA    1 
ATOM   5452  C  C     . LEU A 1 2137 ? 188.896 195.389 195.810 1.00 68.73  ? 2137 LEU A C     1 
ATOM   5453  O  O     . LEU A 1 2137 ? 188.142 194.782 195.039 1.00 77.13  ? 2137 LEU A O     1 
ATOM   5454  C  CB    . LEU A 1 2137 ? 191.348 194.849 195.788 1.00 68.86  ? 2137 LEU A CB    1 
ATOM   5455  C  CG    . LEU A 1 2137 ? 191.434 193.571 194.956 1.00 73.46  ? 2137 LEU A CG    1 
ATOM   5456  C  CD1   . LEU A 1 2137 ? 191.973 193.882 193.573 1.00 73.96  ? 2137 LEU A CD1   1 
ATOM   5457  C  CD2   . LEU A 1 2137 ? 192.304 192.542 195.651 1.00 77.36  ? 2137 LEU A CD2   1 
ATOM   5458  N  N     . ILE A 1 2138 ? 188.545 195.678 197.065 1.00 71.27  ? 2138 ILE A N     1 
ATOM   5459  C  CA    . ILE A 1 2138 ? 187.222 195.316 197.565 1.00 72.62  ? 2138 ILE A CA    1 
ATOM   5460  C  C     . ILE A 1 2138 ? 186.138 196.071 196.807 1.00 74.69  ? 2138 ILE A C     1 
ATOM   5461  O  O     . ILE A 1 2138 ? 185.086 195.509 196.480 1.00 78.27  ? 2138 ILE A O     1 
ATOM   5462  C  CB    . ILE A 1 2138 ? 187.129 195.566 199.081 1.00 76.19  ? 2138 ILE A CB    1 
ATOM   5463  C  CG1   . ILE A 1 2138 ? 188.126 194.680 199.822 1.00 77.21  ? 2138 ILE A CG1   1 
ATOM   5464  C  CG2   . ILE A 1 2138 ? 185.721 195.300 199.583 1.00 70.09  ? 2138 ILE A CG2   1 
ATOM   5465  C  CD1   . ILE A 1 2138 ? 187.965 193.223 199.511 1.00 75.38  ? 2138 ILE A CD1   1 
ATOM   5466  N  N     . GLN A 1 2139 ? 186.369 197.355 196.524 1.00 72.97  ? 2139 GLN A N     1 
ATOM   5467  C  CA    . GLN A 1 2139 ? 185.391 198.134 195.775 1.00 70.42  ? 2139 GLN A CA    1 
ATOM   5468  C  C     . GLN A 1 2139 ? 185.185 197.559 194.382 1.00 72.62  ? 2139 GLN A C     1 
ATOM   5469  O  O     . GLN A 1 2139 ? 184.046 197.430 193.920 1.00 82.31  ? 2139 GLN A O     1 
ATOM   5470  C  CB    . GLN A 1 2139 ? 185.838 199.593 195.694 1.00 74.65  ? 2139 GLN A CB    1 
ATOM   5471  C  CG    . GLN A 1 2139 ? 184.838 200.509 195.014 1.00 76.01  ? 2139 GLN A CG    1 
ATOM   5472  C  CD    . GLN A 1 2139 ? 185.481 201.763 194.458 1.00 81.20  ? 2139 GLN A CD    1 
ATOM   5473  O  OE1   . GLN A 1 2139 ? 186.293 202.404 195.123 1.00 79.55  ? 2139 GLN A OE1   1 
ATOM   5474  N  NE2   . GLN A 1 2139 ? 185.113 202.124 193.235 1.00 79.08  ? 2139 GLN A NE2   1 
ATOM   5475  N  N     . SER A 1 2140 ? 186.275 197.193 193.703 1.00 72.66  ? 2140 SER A N     1 
ATOM   5476  C  CA    . SER A 1 2140 ? 186.142 196.594 192.377 1.00 69.92  ? 2140 SER A CA    1 
ATOM   5477  C  C     . SER A 1 2140 ? 185.413 195.257 192.444 1.00 73.39  ? 2140 SER A C     1 
ATOM   5478  O  O     . SER A 1 2140 ? 184.537 194.973 191.613 1.00 78.91  ? 2140 SER A O     1 
ATOM   5479  C  CB    . SER A 1 2140 ? 187.519 196.422 191.739 1.00 72.58  ? 2140 SER A CB    1 
ATOM   5480  O  OG    . SER A 1 2140 ? 187.972 195.087 191.866 1.00 83.87  ? 2140 SER A OG    1 
ATOM   5481  N  N     . VAL A 1 2141 ? 185.749 194.429 193.436 1.00 72.20  ? 2141 VAL A N     1 
ATOM   5482  C  CA    . VAL A 1 2141 ? 185.120 193.117 193.568 1.00 61.61  ? 2141 VAL A CA    1 
ATOM   5483  C  C     . VAL A 1 2141 ? 183.625 193.268 193.812 1.00 65.61  ? 2141 VAL A C     1 
ATOM   5484  O  O     . VAL A 1 2141 ? 182.807 192.546 193.232 1.00 74.72  ? 2141 VAL A O     1 
ATOM   5485  C  CB    . VAL A 1 2141 ? 185.797 192.310 194.691 1.00 67.00  ? 2141 VAL A CB    1 
ATOM   5486  C  CG1   . VAL A 1 2141 ? 184.847 191.263 195.249 1.00 63.06  ? 2141 VAL A CG1   1 
ATOM   5487  C  CG2   . VAL A 1 2141 ? 187.065 191.656 194.178 1.00 74.12  ? 2141 VAL A CG2   1 
ATOM   5488  N  N     . CYS A 1 2142 ? 183.245 194.208 194.678 1.00 78.79  ? 2142 CYS A N     1 
ATOM   5489  C  CA    . CYS A 1 2142 ? 181.832 194.415 194.970 1.00 81.83  ? 2142 CYS A CA    1 
ATOM   5490  C  C     . CYS A 1 2142 ? 181.099 194.992 193.765 1.00 81.25  ? 2142 CYS A C     1 
ATOM   5491  O  O     . CYS A 1 2142 ? 179.955 194.618 193.484 1.00 87.29  ? 2142 CYS A O     1 
ATOM   5492  C  CB    . CYS A 1 2142 ? 181.679 195.327 196.185 1.00 83.61  ? 2142 CYS A CB    1 
ATOM   5493  S  SG    . CYS A 1 2142 ? 182.120 194.556 197.757 1.00 100.41 ? 2142 CYS A SG    1 
ATOM   5494  N  N     . GLU A 1 2143 ? 181.741 195.909 193.038 1.00 74.87  ? 2143 GLU A N     1 
ATOM   5495  C  CA    . GLU A 1 2143 ? 181.102 196.483 191.860 1.00 72.93  ? 2143 GLU A CA    1 
ATOM   5496  C  C     . GLU A 1 2143 ? 180.909 195.444 190.764 1.00 77.57  ? 2143 GLU A C     1 
ATOM   5497  O  O     . GLU A 1 2143 ? 179.973 195.555 189.965 1.00 77.28  ? 2143 GLU A O     1 
ATOM   5498  C  CB    . GLU A 1 2143 ? 181.923 197.661 191.338 1.00 72.45  ? 2143 GLU A CB    1 
ATOM   5499  C  CG    . GLU A 1 2143 ? 181.769 198.931 192.156 1.00 80.97  ? 2143 GLU A CG    1 
ATOM   5500  C  CD    . GLU A 1 2143 ? 182.534 200.100 191.568 1.00 87.51  ? 2143 GLU A CD    1 
ATOM   5501  O  OE1   . GLU A 1 2143 ? 183.131 199.935 190.483 1.00 85.13  ? 2143 GLU A OE1   1 
ATOM   5502  O  OE2   . GLU A 1 2143 ? 182.540 201.182 192.191 1.00 84.66  ? 2143 GLU A OE2   1 
ATOM   5503  N  N     . THR A 1 2144 ? 181.775 194.433 190.707 1.00 76.61  ? 2144 THR A N     1 
ATOM   5504  C  CA    . THR A 1 2144 ? 181.678 193.438 189.645 1.00 67.59  ? 2144 THR A CA    1 
ATOM   5505  C  C     . THR A 1 2144 ? 180.829 192.225 190.017 1.00 75.20  ? 2144 THR A C     1 
ATOM   5506  O  O     . THR A 1 2144 ? 180.147 191.671 189.147 1.00 82.38  ? 2144 THR A O     1 
ATOM   5507  C  CB    . THR A 1 2144 ? 183.078 192.970 189.237 1.00 75.27  ? 2144 THR A CB    1 
ATOM   5508  O  OG1   . THR A 1 2144 ? 183.923 194.110 189.043 1.00 80.10  ? 2144 THR A OG1   1 
ATOM   5509  C  CG2   . THR A 1 2144 ? 183.020 192.172 187.945 1.00 75.05  ? 2144 THR A CG2   1 
ATOM   5510  N  N     . MET A 1 2145 ? 180.834 191.804 191.283 1.00 71.21  ? 2145 MET A N     1 
ATOM   5511  C  CA    . MET A 1 2145 ? 180.226 190.539 191.680 1.00 66.53  ? 2145 MET A CA    1 
ATOM   5512  C  C     . MET A 1 2145 ? 178.923 190.677 192.450 1.00 76.20  ? 2145 MET A C     1 
ATOM   5513  O  O     . MET A 1 2145 ? 178.063 189.804 192.331 1.00 86.68  ? 2145 MET A O     1 
ATOM   5514  C  CB    . MET A 1 2145 ? 181.205 189.725 192.532 1.00 67.08  ? 2145 MET A CB    1 
ATOM   5515  C  CG    . MET A 1 2145 ? 182.567 189.558 191.900 1.00 75.70  ? 2145 MET A CG    1 
ATOM   5516  S  SD    . MET A 1 2145 ? 182.625 188.166 190.764 1.00 83.19  ? 2145 MET A SD    1 
ATOM   5517  C  CE    . MET A 1 2145 ? 183.750 188.814 189.535 1.00 75.70  ? 2145 MET A CE    1 
ATOM   5518  N  N     . VAL A 1 2146 ? 178.764 191.735 193.250 1.00 70.43  ? 2146 VAL A N     1 
ATOM   5519  C  CA    . VAL A 1 2146 ? 177.536 191.889 194.039 1.00 69.62  ? 2146 VAL A CA    1 
ATOM   5520  C  C     . VAL A 1 2146 ? 176.285 191.904 193.172 1.00 78.12  ? 2146 VAL A C     1 
ATOM   5521  O  O     . VAL A 1 2146 ? 175.295 191.260 193.550 1.00 84.21  ? 2146 VAL A O     1 
ATOM   5522  C  CB    . VAL A 1 2146 ? 177.649 193.112 194.959 1.00 69.94  ? 2146 VAL A CB    1 
ATOM   5523  C  CG1   . VAL A 1 2146 ? 176.282 193.527 195.478 1.00 72.02  ? 2146 VAL A CG1   1 
ATOM   5524  C  CG2   . VAL A 1 2146 ? 178.591 192.817 196.114 1.00 74.51  ? 2146 VAL A CG2   1 
ATOM   5525  N  N     . PRO A 1 2147 ? 176.235 192.599 192.026 1.00 61.92  ? 2147 PRO A N     1 
ATOM   5526  C  CA    . PRO A 1 2147 ? 174.985 192.609 191.246 1.00 64.02  ? 2147 PRO A CA    1 
ATOM   5527  C  C     . PRO A 1 2147 ? 174.470 191.232 190.866 1.00 60.31  ? 2147 PRO A C     1 
ATOM   5528  O  O     . PRO A 1 2147 ? 173.251 191.020 190.869 1.00 73.15  ? 2147 PRO A O     1 
ATOM   5529  C  CB    . PRO A 1 2147 ? 175.363 193.426 190.005 1.00 63.48  ? 2147 PRO A CB    1 
ATOM   5530  C  CG    . PRO A 1 2147 ? 176.403 194.348 190.487 1.00 61.22  ? 2147 PRO A CG    1 
ATOM   5531  C  CD    . PRO A 1 2147 ? 177.209 193.562 191.478 1.00 58.31  ? 2147 PRO A CD    1 
ATOM   5532  N  N     . LYS A 1 2148 ? 175.349 190.285 190.545 1.00 42.50  ? 2148 LYS A N     1 
ATOM   5533  C  CA    . LYS A 1 2148 ? 174.897 188.978 190.085 1.00 57.44  ? 2148 LYS A CA    1 
ATOM   5534  C  C     . LYS A 1 2148 ? 174.414 188.074 191.211 1.00 57.81  ? 2148 LYS A C     1 
ATOM   5535  O  O     . LYS A 1 2148 ? 173.796 187.043 190.927 1.00 61.91  ? 2148 LYS A O     1 
ATOM   5536  C  CB    . LYS A 1 2148 ? 176.018 188.273 189.320 1.00 62.76  ? 2148 LYS A CB    1 
ATOM   5537  C  CG    . LYS A 1 2148 ? 176.947 187.454 190.197 1.00 57.32  ? 2148 LYS A CG    1 
ATOM   5538  C  CD    . LYS A 1 2148 ? 177.789 186.504 189.368 1.00 53.99  ? 2148 LYS A CD    1 
ATOM   5539  C  CE    . LYS A 1 2148 ? 178.911 187.239 188.662 1.00 57.83  ? 2148 LYS A CE    1 
ATOM   5540  N  NZ    . LYS A 1 2148 ? 179.911 186.294 188.097 1.00 62.23  ? 2148 LYS A NZ    1 
ATOM   5541  N  N     . LEU A 1 2149 ? 174.669 188.427 192.466 1.00 65.07  ? 2149 LEU A N     1 
ATOM   5542  C  CA    . LEU A 1 2149 ? 174.362 187.539 193.578 1.00 61.92  ? 2149 LEU A CA    1 
ATOM   5543  C  C     . LEU A 1 2149 ? 172.886 187.589 193.946 1.00 63.43  ? 2149 LEU A C     1 
ATOM   5544  O  O     . LEU A 1 2149 ? 172.228 188.625 193.817 1.00 67.42  ? 2149 LEU A O     1 
ATOM   5545  C  CB    . LEU A 1 2149 ? 175.207 187.902 194.797 1.00 63.79  ? 2149 LEU A CB    1 
ATOM   5546  C  CG    . LEU A 1 2149 ? 176.701 187.600 194.709 1.00 56.02  ? 2149 LEU A CG    1 
ATOM   5547  C  CD1   . LEU A 1 2149 ? 177.267 187.494 196.104 1.00 66.50  ? 2149 LEU A CD1   1 
ATOM   5548  C  CD2   . LEU A 1 2149 ? 176.952 186.320 193.933 1.00 56.62  ? 2149 LEU A CD2   1 
ATOM   5549  N  N     . VAL A 1 2150 ? 172.372 186.452 194.415 1.00 66.00  ? 2150 VAL A N     1 
ATOM   5550  C  CA    . VAL A 1 2150 ? 171.009 186.346 194.919 1.00 71.77  ? 2150 VAL A CA    1 
ATOM   5551  C  C     . VAL A 1 2150 ? 170.935 186.992 196.296 1.00 74.44  ? 2150 VAL A C     1 
ATOM   5552  O  O     . VAL A 1 2150 ? 171.964 187.337 196.887 1.00 80.64  ? 2150 VAL A O     1 
ATOM   5553  C  CB    . VAL A 1 2150 ? 170.542 184.881 194.968 1.00 69.30  ? 2150 VAL A CB    1 
ATOM   5554  C  CG1   . VAL A 1 2150 ? 170.583 184.271 193.580 1.00 65.99  ? 2150 VAL A CG1   1 
ATOM   5555  C  CG2   . VAL A 1 2150 ? 171.404 184.086 195.926 1.00 72.78  ? 2150 VAL A CG2   1 
ATOM   5556  N  N     . ALA A 1 2151 ? 169.715 187.168 196.809 1.00 80.34  ? 2151 ALA A N     1 
ATOM   5557  C  CA    . ALA A 1 2151 ? 169.530 187.878 198.071 1.00 84.43  ? 2151 ALA A CA    1 
ATOM   5558  C  C     . ALA A 1 2151 ? 170.235 187.176 199.226 1.00 86.09  ? 2151 ALA A C     1 
ATOM   5559  O  O     . ALA A 1 2151 ? 170.809 187.834 200.101 1.00 87.84  ? 2151 ALA A O     1 
ATOM   5560  C  CB    . ALA A 1 2151 ? 168.039 188.032 198.369 1.00 86.57  ? 2151 ALA A CB    1 
ATOM   5561  N  N     . GLU A 1 2152 ? 170.201 185.843 199.252 1.00 91.43  ? 2152 GLU A N     1 
ATOM   5562  C  CA    . GLU A 1 2152 ? 170.785 185.109 200.369 1.00 92.56  ? 2152 GLU A CA    1 
ATOM   5563  C  C     . GLU A 1 2152 ? 172.298 184.965 200.267 1.00 96.07  ? 2152 GLU A C     1 
ATOM   5564  O  O     . GLU A 1 2152 ? 172.926 184.516 201.232 1.00 100.92 ? 2152 GLU A O     1 
ATOM   5565  C  CB    . GLU A 1 2152 ? 170.149 183.722 200.487 1.00 92.68  ? 2152 GLU A CB    1 
ATOM   5566  C  CG    . GLU A 1 2152 ? 170.034 182.970 199.174 1.00 94.05  ? 2152 GLU A CG    1 
ATOM   5567  C  CD    . GLU A 1 2152 ? 168.618 182.955 198.634 1.00 99.29  ? 2152 GLU A CD    1 
ATOM   5568  O  OE1   . GLU A 1 2152 ? 167.818 183.825 199.037 1.00 101.80 ? 2152 GLU A OE1   1 
ATOM   5569  O  OE2   . GLU A 1 2152 ? 168.304 182.072 197.808 1.00 96.10  ? 2152 GLU A OE2   1 
ATOM   5570  N  N     . ASP A 1 2153 ? 172.898 185.327 199.132 1.00 84.68  ? 2153 ASP A N     1 
ATOM   5571  C  CA    . ASP A 1 2153 ? 174.340 185.185 198.975 1.00 81.63  ? 2153 ASP A CA    1 
ATOM   5572  C  C     . ASP A 1 2153 ? 175.099 186.479 199.237 1.00 76.09  ? 2153 ASP A C     1 
ATOM   5573  O  O     . ASP A 1 2153 ? 176.321 186.437 199.413 1.00 80.60  ? 2153 ASP A O     1 
ATOM   5574  C  CB    . ASP A 1 2153 ? 174.670 184.674 197.573 1.00 76.95  ? 2153 ASP A CB    1 
ATOM   5575  C  CG    . ASP A 1 2153 ? 174.447 183.185 197.431 1.00 79.85  ? 2153 ASP A CG    1 
ATOM   5576  O  OD1   . ASP A 1 2153 ? 174.226 182.517 198.463 1.00 83.33  ? 2153 ASP A OD1   1 
ATOM   5577  O  OD2   . ASP A 1 2153 ? 174.490 182.680 196.290 1.00 80.89  ? 2153 ASP A OD2   1 
ATOM   5578  N  N     . ILE A 1 2154 ? 174.411 187.622 199.258 1.00 75.36  ? 2154 ILE A N     1 
ATOM   5579  C  CA    . ILE A 1 2154 ? 175.088 188.888 199.545 1.00 80.56  ? 2154 ILE A CA    1 
ATOM   5580  C  C     . ILE A 1 2154 ? 175.729 188.902 200.929 1.00 91.21  ? 2154 ILE A C     1 
ATOM   5581  O  O     . ILE A 1 2154 ? 176.919 189.248 201.029 1.00 95.25  ? 2154 ILE A O     1 
ATOM   5582  C  CB    . ILE A 1 2154 ? 174.119 190.065 199.330 1.00 86.96  ? 2154 ILE A CB    1 
ATOM   5583  C  CG1   . ILE A 1 2154 ? 173.560 190.042 197.907 1.00 84.72  ? 2154 ILE A CG1   1 
ATOM   5584  C  CG2   . ILE A 1 2154 ? 174.813 191.385 199.611 1.00 90.17  ? 2154 ILE A CG2   1 
ATOM   5585  C  CD1   . ILE A 1 2154 ? 172.549 191.132 197.632 1.00 85.70  ? 2154 ILE A CD1   1 
ATOM   5586  N  N     . PRO A 1 2155 ? 175.027 188.561 202.021 1.00 100.88 ? 2155 PRO A N     1 
ATOM   5587  C  CA    . PRO A 1 2155 ? 175.712 188.560 203.325 1.00 98.56  ? 2155 PRO A CA    1 
ATOM   5588  C  C     . PRO A 1 2155 ? 176.789 187.498 203.425 1.00 97.40  ? 2155 PRO A C     1 
ATOM   5589  O  O     . PRO A 1 2155 ? 177.797 187.708 204.109 1.00 99.58  ? 2155 PRO A O     1 
ATOM   5590  C  CB    . PRO A 1 2155 ? 174.571 188.323 204.331 1.00 97.61  ? 2155 PRO A CB    1 
ATOM   5591  C  CG    . PRO A 1 2155 ? 173.299 188.385 203.537 1.00 98.48  ? 2155 PRO A CG    1 
ATOM   5592  C  CD    . PRO A 1 2155 ? 173.661 188.028 202.144 1.00 97.52  ? 2155 PRO A CD    1 
ATOM   5593  N  N     . LEU A 1 2156 ? 176.612 186.364 202.744 1.00 84.60  ? 2156 LEU A N     1 
ATOM   5594  C  CA    . LEU A 1 2156 ? 177.650 185.340 202.738 1.00 89.81  ? 2156 LEU A CA    1 
ATOM   5595  C  C     . LEU A 1 2156 ? 178.924 185.863 202.085 1.00 95.72  ? 2156 LEU A C     1 
ATOM   5596  O  O     . LEU A 1 2156 ? 180.024 185.694 202.626 1.00 98.37  ? 2156 LEU A O     1 
ATOM   5597  C  CB    . LEU A 1 2156 ? 177.140 184.089 202.020 1.00 88.29  ? 2156 LEU A CB    1 
ATOM   5598  C  CG    . LEU A 1 2156 ? 177.897 182.769 202.193 1.00 89.76  ? 2156 LEU A CG    1 
ATOM   5599  C  CD1   . LEU A 1 2156 ? 176.949 181.597 201.998 1.00 87.82  ? 2156 LEU A CD1   1 
ATOM   5600  C  CD2   . LEU A 1 2156 ? 179.081 182.650 201.251 1.00 91.17  ? 2156 LEU A CD2   1 
ATOM   5601  N  N     . LEU A 1 2157 ? 178.794 186.522 200.931 1.00 90.14  ? 2157 LEU A N     1 
ATOM   5602  C  CA    . LEU A 1 2157 ? 179.968 187.072 200.261 1.00 83.48  ? 2157 LEU A CA    1 
ATOM   5603  C  C     . LEU A 1 2157 ? 180.585 188.210 201.063 1.00 86.62  ? 2157 LEU A C     1 
ATOM   5604  O  O     . LEU A 1 2157 ? 181.810 188.368 201.080 1.00 94.91  ? 2157 LEU A O     1 
ATOM   5605  C  CB    . LEU A 1 2157 ? 179.606 187.541 198.851 1.00 84.58  ? 2157 LEU A CB    1 
ATOM   5606  C  CG    . LEU A 1 2157 ? 180.747 188.143 198.025 1.00 84.61  ? 2157 LEU A CG    1 
ATOM   5607  C  CD1   . LEU A 1 2157 ? 180.782 187.557 196.627 1.00 80.99  ? 2157 LEU A CD1   1 
ATOM   5608  C  CD2   . LEU A 1 2157 ? 180.615 189.656 197.954 1.00 88.61  ? 2157 LEU A CD2   1 
ATOM   5609  N  N     . PHE A 1 2158 ? 179.761 189.021 201.732 1.00 81.04  ? 2158 PHE A N     1 
ATOM   5610  C  CA    . PHE A 1 2158 ? 180.325 190.093 202.548 1.00 82.66  ? 2158 PHE A CA    1 
ATOM   5611  C  C     . PHE A 1 2158 ? 181.078 189.547 203.756 1.00 90.95  ? 2158 PHE A C     1 
ATOM   5612  O  O     . PHE A 1 2158 ? 182.140 190.072 204.112 1.00 92.73  ? 2158 PHE A O     1 
ATOM   5613  C  CB    . PHE A 1 2158 ? 179.226 191.062 202.980 1.00 86.95  ? 2158 PHE A CB    1 
ATOM   5614  C  CG    . PHE A 1 2158 ? 179.031 192.208 202.029 1.00 92.19  ? 2158 PHE A CG    1 
ATOM   5615  C  CD1   . PHE A 1 2158 ? 179.916 193.272 202.019 1.00 93.57  ? 2158 PHE A CD1   1 
ATOM   5616  C  CD2   . PHE A 1 2158 ? 177.973 192.216 201.137 1.00 92.55  ? 2158 PHE A CD2   1 
ATOM   5617  C  CE1   . PHE A 1 2158 ? 179.745 194.327 201.144 1.00 91.53  ? 2158 PHE A CE1   1 
ATOM   5618  C  CE2   . PHE A 1 2158 ? 177.796 193.269 200.259 1.00 92.56  ? 2158 PHE A CE2   1 
ATOM   5619  C  CZ    . PHE A 1 2158 ? 178.684 194.325 200.263 1.00 93.16  ? 2158 PHE A CZ    1 
ATOM   5620  N  N     . SER A 1 2159 ? 180.561 188.491 204.388 1.00 92.16  ? 2159 SER A N     1 
ATOM   5621  C  CA    . SER A 1 2159 ? 181.304 187.838 205.460 1.00 92.81  ? 2159 SER A CA    1 
ATOM   5622  C  C     . SER A 1 2159 ? 182.592 187.221 204.933 1.00 91.62  ? 2159 SER A C     1 
ATOM   5623  O  O     . SER A 1 2159 ? 183.625 187.251 205.610 1.00 96.54  ? 2159 SER A O     1 
ATOM   5624  C  CB    . SER A 1 2159 ? 180.438 186.776 206.134 1.00 95.82  ? 2159 SER A CB    1 
ATOM   5625  O  OG    . SER A 1 2159 ? 180.575 185.525 205.485 1.00 95.45  ? 2159 SER A OG    1 
ATOM   5626  N  N     . LEU A 1 2160 ? 182.547 186.652 203.727 1.00 78.73  ? 2160 LEU A N     1 
ATOM   5627  C  CA    . LEU A 1 2160 ? 183.757 186.115 203.114 1.00 80.62  ? 2160 LEU A CA    1 
ATOM   5628  C  C     . LEU A 1 2160 ? 184.795 187.212 202.896 1.00 83.54  ? 2160 LEU A C     1 
ATOM   5629  O  O     . LEU A 1 2160 ? 185.988 187.014 203.158 1.00 86.49  ? 2160 LEU A O     1 
ATOM   5630  C  CB    . LEU A 1 2160 ? 183.398 185.439 201.792 1.00 82.56  ? 2160 LEU A CB    1 
ATOM   5631  C  CG    . LEU A 1 2160 ? 184.463 184.658 201.028 1.00 81.81  ? 2160 LEU A CG    1 
ATOM   5632  C  CD1   . LEU A 1 2160 ? 185.441 184.007 201.984 1.00 83.79  ? 2160 LEU A CD1   1 
ATOM   5633  C  CD2   . LEU A 1 2160 ? 183.793 183.620 200.149 1.00 85.34  ? 2160 LEU A CD2   1 
ATOM   5634  N  N     . LEU A 1 2161 ? 184.354 188.375 202.414 1.00 86.32  ? 2161 LEU A N     1 
ATOM   5635  C  CA    . LEU A 1 2161 ? 185.259 189.506 202.230 1.00 78.72  ? 2161 LEU A CA    1 
ATOM   5636  C  C     . LEU A 1 2161 ? 185.845 189.964 203.557 1.00 82.24  ? 2161 LEU A C     1 
ATOM   5637  O  O     . LEU A 1 2161 ? 187.038 190.277 203.642 1.00 84.65  ? 2161 LEU A O     1 
ATOM   5638  C  CB    . LEU A 1 2161 ? 184.526 190.660 201.548 1.00 80.70  ? 2161 LEU A CB    1 
ATOM   5639  C  CG    . LEU A 1 2161 ? 184.251 190.523 200.053 1.00 83.89  ? 2161 LEU A CG    1 
ATOM   5640  C  CD1   . LEU A 1 2161 ? 183.315 191.621 199.588 1.00 86.38  ? 2161 LEU A CD1   1 
ATOM   5641  C  CD2   . LEU A 1 2161 ? 185.554 190.583 199.289 1.00 80.17  ? 2161 LEU A CD2   1 
ATOM   5642  N  N     . SER A 1 2162 ? 185.019 190.020 204.603 1.00 90.27  ? 2162 SER A N     1 
ATOM   5643  C  CA    . SER A 1 2162 ? 185.532 190.369 205.923 1.00 89.40  ? 2162 SER A CA    1 
ATOM   5644  C  C     . SER A 1 2162 ? 186.531 189.335 206.426 1.00 89.08  ? 2162 SER A C     1 
ATOM   5645  O  O     . SER A 1 2162 ? 187.464 189.681 207.160 1.00 93.09  ? 2162 SER A O     1 
ATOM   5646  C  CB    . SER A 1 2162 ? 184.379 190.518 206.915 1.00 89.56  ? 2162 SER A CB    1 
ATOM   5647  O  OG    . SER A 1 2162 ? 183.985 189.258 207.430 1.00 90.92  ? 2162 SER A OG    1 
ATOM   5648  N  N     . ASP A 1 2163 ? 186.353 188.069 206.044 1.00 91.06  ? 2163 ASP A N     1 
ATOM   5649  C  CA    . ASP A 1 2163 ? 187.272 187.024 206.482 1.00 94.27  ? 2163 ASP A CA    1 
ATOM   5650  C  C     . ASP A 1 2163 ? 188.611 187.119 205.761 1.00 89.75  ? 2163 ASP A C     1 
ATOM   5651  O  O     . ASP A 1 2163 ? 189.668 186.975 206.386 1.00 89.93  ? 2163 ASP A O     1 
ATOM   5652  C  CB    . ASP A 1 2163 ? 186.645 185.648 206.261 1.00 94.00  ? 2163 ASP A CB    1 
ATOM   5653  C  CG    . ASP A 1 2163 ? 185.744 185.227 207.405 1.00 98.77  ? 2163 ASP A CG    1 
ATOM   5654  O  OD1   . ASP A 1 2163 ? 185.220 186.115 208.109 1.00 96.51  ? 2163 ASP A OD1   1 
ATOM   5655  O  OD2   . ASP A 1 2163 ? 185.560 184.008 207.599 1.00 97.40  ? 2163 ASP A OD2   1 
ATOM   5656  N  N     . VAL A 1 2164 ? 188.591 187.357 204.452 1.00 79.23  ? 2164 VAL A N     1 
ATOM   5657  C  CA    . VAL A 1 2164 ? 189.836 187.402 203.692 1.00 79.27  ? 2164 VAL A CA    1 
ATOM   5658  C  C     . VAL A 1 2164 ? 190.450 188.801 203.678 1.00 80.14  ? 2164 VAL A C     1 
ATOM   5659  O  O     . VAL A 1 2164 ? 191.673 188.937 203.566 1.00 77.47  ? 2164 VAL A O     1 
ATOM   5660  C  CB    . VAL A 1 2164 ? 189.606 186.885 202.262 1.00 73.08  ? 2164 VAL A CB    1 
ATOM   5661  C  CG1   . VAL A 1 2164 ? 190.932 186.623 201.574 1.00 72.41  ? 2164 VAL A CG1   1 
ATOM   5662  C  CG2   . VAL A 1 2164 ? 188.772 185.619 202.289 1.00 78.44  ? 2164 VAL A CG2   1 
ATOM   5663  N  N     . PHE A 1 2165 ? 189.634 189.845 203.805 1.00 84.41  ? 2165 PHE A N     1 
ATOM   5664  C  CA    . PHE A 1 2165 ? 190.105 191.230 203.830 1.00 79.82  ? 2165 PHE A CA    1 
ATOM   5665  C  C     . PHE A 1 2165 ? 189.546 191.897 205.079 1.00 89.22  ? 2165 PHE A C     1 
ATOM   5666  O  O     . PHE A 1 2165 ? 188.571 192.658 205.010 1.00 91.75  ? 2165 PHE A O     1 
ATOM   5667  C  CB    . PHE A 1 2165 ? 189.688 191.990 202.570 1.00 76.26  ? 2165 PHE A CB    1 
ATOM   5668  C  CG    . PHE A 1 2165 ? 190.178 191.375 201.290 1.00 78.54  ? 2165 PHE A CG    1 
ATOM   5669  C  CD1   . PHE A 1 2165 ? 189.529 190.288 200.730 1.00 84.63  ? 2165 PHE A CD1   1 
ATOM   5670  C  CD2   . PHE A 1 2165 ? 191.277 191.901 200.635 1.00 85.37  ? 2165 PHE A CD2   1 
ATOM   5671  C  CE1   . PHE A 1 2165 ? 189.976 189.730 199.549 1.00 85.68  ? 2165 PHE A CE1   1 
ATOM   5672  C  CE2   . PHE A 1 2165 ? 191.729 191.347 199.454 1.00 85.42  ? 2165 PHE A CE2   1 
ATOM   5673  C  CZ    . PHE A 1 2165 ? 191.077 190.261 198.910 1.00 84.55  ? 2165 PHE A CZ    1 
ATOM   5674  N  N     . PRO A 1 2166 ? 190.132 191.626 206.243 1.00 84.84  ? 2166 PRO A N     1 
ATOM   5675  C  CA    . PRO A 1 2166 ? 189.619 192.230 207.477 1.00 84.05  ? 2166 PRO A CA    1 
ATOM   5676  C  C     . PRO A 1 2166 ? 190.008 193.696 207.588 1.00 85.88  ? 2166 PRO A C     1 
ATOM   5677  O  O     . PRO A 1 2166 ? 191.095 194.105 207.175 1.00 87.41  ? 2166 PRO A O     1 
ATOM   5678  C  CB    . PRO A 1 2166 ? 190.278 191.393 208.577 1.00 85.94  ? 2166 PRO A CB    1 
ATOM   5679  C  CG    . PRO A 1 2166 ? 191.557 190.933 207.964 1.00 80.89  ? 2166 PRO A CG    1 
ATOM   5680  C  CD    . PRO A 1 2166 ? 191.290 190.751 206.492 1.00 78.21  ? 2166 PRO A CD    1 
ATOM   5681  N  N     . GLY A 1 2167 ? 189.100 194.489 208.155 1.00 98.09  ? 2167 GLY A N     1 
ATOM   5682  C  CA    . GLY A 1 2167 ? 189.363 195.879 208.460 1.00 100.83 ? 2167 GLY A CA    1 
ATOM   5683  C  C     . GLY A 1 2167 ? 189.011 196.864 207.366 1.00 104.66 ? 2167 GLY A C     1 
ATOM   5684  O  O     . GLY A 1 2167 ? 189.069 198.076 207.611 1.00 104.83 ? 2167 GLY A O     1 
ATOM   5685  N  N     . VAL A 1 2168 ? 188.648 196.393 206.176 1.00 100.03 ? 2168 VAL A N     1 
ATOM   5686  C  CA    . VAL A 1 2168 ? 188.314 197.258 205.050 1.00 99.86  ? 2168 VAL A CA    1 
ATOM   5687  C  C     . VAL A 1 2168 ? 186.828 197.114 204.753 1.00 99.98  ? 2168 VAL A C     1 
ATOM   5688  O  O     . VAL A 1 2168 ? 186.280 196.006 204.805 1.00 97.11  ? 2168 VAL A O     1 
ATOM   5689  C  CB    . VAL A 1 2168 ? 189.165 196.932 203.810 1.00 97.22  ? 2168 VAL A CB    1 
ATOM   5690  C  CG1   . VAL A 1 2168 ? 190.600 197.381 204.026 1.00 97.63  ? 2168 VAL A CG1   1 
ATOM   5691  C  CG2   . VAL A 1 2168 ? 189.116 195.448 203.505 1.00 98.16  ? 2168 VAL A CG2   1 
ATOM   5692  N  N     . GLN A 1 2169 ? 186.177 198.235 204.456 1.00 104.73 ? 2169 GLN A N     1 
ATOM   5693  C  CA    . GLN A 1 2169 ? 184.745 198.273 204.204 1.00 104.53 ? 2169 GLN A CA    1 
ATOM   5694  C  C     . GLN A 1 2169 ? 184.469 198.948 202.868 1.00 105.31 ? 2169 GLN A C     1 
ATOM   5695  O  O     . GLN A 1 2169 ? 185.278 199.739 202.372 1.00 105.61 ? 2169 GLN A O     1 
ATOM   5696  C  CB    . GLN A 1 2169 ? 183.997 199.021 205.318 1.00 105.62 ? 2169 GLN A CB    1 
ATOM   5697  C  CG    . GLN A 1 2169 ? 184.278 198.517 206.726 1.00 108.91 ? 2169 GLN A CG    1 
ATOM   5698  C  CD    . GLN A 1 2169 ? 185.534 199.121 207.327 1.00 110.37 ? 2169 GLN A CD    1 
ATOM   5699  O  OE1   . GLN A 1 2169 ? 186.377 199.667 206.616 1.00 108.02 ? 2169 GLN A OE1   1 
ATOM   5700  N  NE2   . GLN A 1 2169 ? 185.662 199.028 208.645 1.00 107.65 ? 2169 GLN A NE2   1 
ATOM   5701  N  N     . TYR A 1 2170 ? 183.317 198.625 202.287 1.00 108.11 ? 2170 TYR A N     1 
ATOM   5702  C  CA    . TYR A 1 2170 ? 182.862 199.233 201.042 1.00 106.73 ? 2170 TYR A CA    1 
ATOM   5703  C  C     . TYR A 1 2170 ? 181.811 200.286 201.376 1.00 110.49 ? 2170 TYR A C     1 
ATOM   5704  O  O     . TYR A 1 2170 ? 180.814 199.989 202.043 1.00 109.91 ? 2170 TYR A O     1 
ATOM   5705  C  CB    . TYR A 1 2170 ? 182.293 198.181 200.093 1.00 106.33 ? 2170 TYR A CB    1 
ATOM   5706  C  CG    . TYR A 1 2170 ? 181.863 198.729 198.748 1.00 107.23 ? 2170 TYR A CG    1 
ATOM   5707  C  CD1   . TYR A 1 2170 ? 182.409 199.902 198.242 1.00 105.86 ? 2170 TYR A CD1   1 
ATOM   5708  C  CD2   . TYR A 1 2170 ? 180.889 198.088 197.997 1.00 107.16 ? 2170 TYR A CD2   1 
ATOM   5709  C  CE1   . TYR A 1 2170 ? 182.011 200.408 197.022 1.00 108.66 ? 2170 TYR A CE1   1 
ATOM   5710  C  CE2   . TYR A 1 2170 ? 180.485 198.586 196.773 1.00 108.92 ? 2170 TYR A CE2   1 
ATOM   5711  C  CZ    . TYR A 1 2170 ? 181.050 199.746 196.291 1.00 111.00 ? 2170 TYR A CZ    1 
ATOM   5712  O  OH    . TYR A 1 2170 ? 180.650 200.247 195.074 1.00 108.63 ? 2170 TYR A OH    1 
ATOM   5713  N  N     . HIS A 1 2171 ? 182.036 201.511 200.912 1.00 114.03 ? 2171 HIS A N     1 
ATOM   5714  C  CA    . HIS A 1 2171 ? 181.054 202.584 201.005 1.00 113.67 ? 2171 HIS A CA    1 
ATOM   5715  C  C     . HIS A 1 2171 ? 180.700 203.016 199.587 1.00 113.26 ? 2171 HIS A C     1 
ATOM   5716  O  O     . HIS A 1 2171 ? 181.436 203.790 198.965 1.00 115.02 ? 2171 HIS A O     1 
ATOM   5717  C  CB    . HIS A 1 2171 ? 181.596 203.753 201.823 1.00 113.75 ? 2171 HIS A CB    1 
ATOM   5718  C  CG    . HIS A 1 2171 ? 182.169 203.349 203.145 1.00 115.03 ? 2171 HIS A CG    1 
ATOM   5719  N  ND1   . HIS A 1 2171 ? 181.565 202.419 203.963 1.00 114.52 ? 2171 HIS A ND1   1 
ATOM   5720  C  CD2   . HIS A 1 2171 ? 183.288 203.750 203.793 1.00 113.36 ? 2171 HIS A CD2   1 
ATOM   5721  C  CE1   . HIS A 1 2171 ? 182.289 202.263 205.058 1.00 112.52 ? 2171 HIS A CE1   1 
ATOM   5722  N  NE2   . HIS A 1 2171 ? 183.340 203.059 204.979 1.00 112.62 ? 2171 HIS A NE2   1 
ATOM   5723  N  N     . ARG A 1 2172 ? 179.582 202.507 199.076 1.00 100.10 ? 2172 ARG A N     1 
ATOM   5724  C  CA    . ARG A 1 2172 ? 179.167 202.826 197.719 1.00 99.93  ? 2172 ARG A CA    1 
ATOM   5725  C  C     . ARG A 1 2172 ? 178.867 204.315 197.588 1.00 99.61  ? 2172 ARG A C     1 
ATOM   5726  O  O     . ARG A 1 2172 ? 178.233 204.924 198.454 1.00 98.19  ? 2172 ARG A O     1 
ATOM   5727  C  CB    . ARG A 1 2172 ? 177.941 201.998 197.328 1.00 97.37  ? 2172 ARG A CB    1 
ATOM   5728  C  CG    . ARG A 1 2172 ? 176.953 202.719 196.423 1.00 97.97  ? 2172 ARG A CG    1 
ATOM   5729  C  CD    . ARG A 1 2172 ? 175.932 201.762 195.832 1.00 98.22  ? 2172 ARG A CD    1 
ATOM   5730  N  NE    . ARG A 1 2172 ? 176.564 200.697 195.063 1.00 97.85  ? 2172 ARG A NE    1 
ATOM   5731  C  CZ    . ARG A 1 2172 ? 175.913 199.869 194.257 1.00 97.46  ? 2172 ARG A CZ    1 
ATOM   5732  N  NH1   . ARG A 1 2172 ? 174.604 199.955 194.089 1.00 96.33  ? 2172 ARG A NH1   1 
ATOM   5733  N  NH2   . ARG A 1 2172 ? 176.593 198.931 193.604 1.00 98.66  ? 2172 ARG A NH2   1 
ATOM   5734  N  N     . GLY A 1 2173 ? 179.342 204.901 196.492 1.00 109.49 ? 2173 GLY A N     1 
ATOM   5735  C  CA    . GLY A 1 2173 ? 179.153 206.321 196.282 1.00 109.72 ? 2173 GLY A CA    1 
ATOM   5736  C  C     . GLY A 1 2173 ? 177.693 206.679 196.081 1.00 113.28 ? 2173 GLY A C     1 
ATOM   5737  O  O     . GLY A 1 2173 ? 176.875 205.864 195.655 1.00 117.09 ? 2173 GLY A O     1 
ATOM   5738  N  N     . GLU A 1 2174 ? 177.365 207.926 196.403 1.00 114.50 ? 2174 GLU A N     1 
ATOM   5739  C  CA    . GLU A 1 2174 ? 176.002 208.440 196.281 1.00 114.16 ? 2174 GLU A CA    1 
ATOM   5740  C  C     . GLU A 1 2174 ? 175.933 209.271 195.005 1.00 118.05 ? 2174 GLU A C     1 
ATOM   5741  O  O     . GLU A 1 2174 ? 176.291 210.449 194.988 1.00 122.49 ? 2174 GLU A O     1 
ATOM   5742  C  CB    . GLU A 1 2174 ? 175.621 209.254 197.511 1.00 114.43 ? 2174 GLU A CB    1 
ATOM   5743  C  CG    . GLU A 1 2174 ? 176.166 208.693 198.815 1.00 115.63 ? 2174 GLU A CG    1 
ATOM   5744  C  CD    . GLU A 1 2174 ? 175.909 209.607 199.997 1.00 117.37 ? 2174 GLU A CD    1 
ATOM   5745  O  OE1   . GLU A 1 2174 ? 174.769 209.617 200.507 1.00 115.73 ? 2174 GLU A OE1   1 
ATOM   5746  O  OE2   . GLU A 1 2174 ? 176.848 210.315 200.418 1.00 116.39 ? 2174 GLU A OE2   1 
ATOM   5747  N  N     . MET A 1 2175 ? 175.464 208.648 193.923 1.00 101.38 ? 2175 MET A N     1 
ATOM   5748  C  CA    . MET A 1 2175 ? 175.317 209.335 192.640 1.00 100.92 ? 2175 MET A CA    1 
ATOM   5749  C  C     . MET A 1 2175 ? 174.101 210.252 192.734 1.00 98.98  ? 2175 MET A C     1 
ATOM   5750  O  O     . MET A 1 2175 ? 173.005 209.946 192.258 1.00 100.48 ? 2175 MET A O     1 
ATOM   5751  C  CB    . MET A 1 2175 ? 175.185 208.336 191.498 1.00 101.19 ? 2175 MET A CB    1 
ATOM   5752  C  CG    . MET A 1 2175 ? 176.356 207.378 191.362 1.00 100.67 ? 2175 MET A CG    1 
ATOM   5753  S  SD    . MET A 1 2175 ? 175.831 205.677 191.078 1.00 117.52 ? 2175 MET A SD    1 
ATOM   5754  C  CE    . MET A 1 2175 ? 175.770 205.051 192.753 1.00 101.50 ? 2175 MET A CE    1 
ATOM   5755  N  N     . THR A 1 2176 ? 174.312 211.406 193.370 1.00 90.45  ? 2176 THR A N     1 
ATOM   5756  C  CA    . THR A 1 2176 ? 173.208 212.318 193.652 1.00 90.48  ? 2176 THR A CA    1 
ATOM   5757  C  C     . THR A 1 2176 ? 172.567 212.829 192.367 1.00 97.06  ? 2176 THR A C     1 
ATOM   5758  O  O     . THR A 1 2176 ? 171.338 212.895 192.258 1.00 100.40 ? 2176 THR A O     1 
ATOM   5759  C  CB    . THR A 1 2176 ? 173.699 213.483 194.511 1.00 93.13  ? 2176 THR A CB    1 
ATOM   5760  O  OG1   . THR A 1 2176 ? 174.202 212.980 195.755 1.00 92.40  ? 2176 THR A OG1   1 
ATOM   5761  C  CG2   . THR A 1 2176 ? 172.565 214.458 194.787 1.00 91.67  ? 2176 THR A CG2   1 
ATOM   5762  N  N     . ALA A 1 2177 ? 173.386 213.197 191.379 1.00 91.28  ? 2177 ALA A N     1 
ATOM   5763  C  CA    . ALA A 1 2177 ? 172.837 213.654 190.106 1.00 85.75  ? 2177 ALA A CA    1 
ATOM   5764  C  C     . ALA A 1 2177 ? 172.065 212.542 189.408 1.00 90.22  ? 2177 ALA A C     1 
ATOM   5765  O  O     . ALA A 1 2177 ? 170.944 212.757 188.927 1.00 92.31  ? 2177 ALA A O     1 
ATOM   5766  C  CB    . ALA A 1 2177 ? 173.957 214.177 189.208 1.00 83.62  ? 2177 ALA A CB    1 
ATOM   5767  N  N     . LEU A 1 2178 ? 172.644 211.340 189.355 1.00 88.68  ? 2178 LEU A N     1 
ATOM   5768  C  CA    . LEU A 1 2178 ? 171.952 210.219 188.731 1.00 84.41  ? 2178 LEU A CA    1 
ATOM   5769  C  C     . LEU A 1 2178 ? 170.696 209.847 189.505 1.00 84.35  ? 2178 LEU A C     1 
ATOM   5770  O  O     . LEU A 1 2178 ? 169.680 209.486 188.906 1.00 89.71  ? 2178 LEU A O     1 
ATOM   5771  C  CB    . LEU A 1 2178 ? 172.884 209.015 188.611 1.00 79.99  ? 2178 LEU A CB    1 
ATOM   5772  C  CG    . LEU A 1 2178 ? 172.298 207.838 187.829 1.00 76.42  ? 2178 LEU A CG    1 
ATOM   5773  C  CD1   . LEU A 1 2178 ? 172.008 208.244 186.395 1.00 82.31  ? 2178 LEU A CD1   1 
ATOM   5774  C  CD2   . LEU A 1 2178 ? 173.233 206.646 187.870 1.00 74.84  ? 2178 LEU A CD2   1 
ATOM   5775  N  N     . ARG A 1 2179 ? 170.744 209.922 190.837 1.00 76.99  ? 2179 ARG A N     1 
ATOM   5776  C  CA    . ARG A 1 2179 ? 169.551 209.636 191.626 1.00 70.22  ? 2179 ARG A CA    1 
ATOM   5777  C  C     . ARG A 1 2179 ? 168.454 210.661 191.364 1.00 77.61  ? 2179 ARG A C     1 
ATOM   5778  O  O     . ARG A 1 2179 ? 167.273 210.305 191.292 1.00 86.06  ? 2179 ARG A O     1 
ATOM   5779  C  CB    . ARG A 1 2179 ? 169.899 209.580 193.111 1.00 72.06  ? 2179 ARG A CB    1 
ATOM   5780  C  CG    . ARG A 1 2179 ? 170.547 208.273 193.535 1.00 75.26  ? 2179 ARG A CG    1 
ATOM   5781  C  CD    . ARG A 1 2179 ? 170.574 208.132 195.045 1.00 80.69  ? 2179 ARG A CD    1 
ATOM   5782  N  NE    . ARG A 1 2179 ? 171.195 206.883 195.467 1.00 82.93  ? 2179 ARG A NE    1 
ATOM   5783  C  CZ    . ARG A 1 2179 ? 170.524 205.794 195.815 1.00 81.30  ? 2179 ARG A CZ    1 
ATOM   5784  N  NH1   . ARG A 1 2179 ? 169.202 205.761 195.793 1.00 79.55  ? 2179 ARG A NH1   1 
ATOM   5785  N  NH2   . ARG A 1 2179 ? 171.195 204.712 196.198 1.00 77.88  ? 2179 ARG A NH2   1 
ATOM   5786  N  N     . GLU A 1 2180 ? 168.820 211.936 191.218 1.00 81.29  ? 2180 GLU A N     1 
ATOM   5787  C  CA    . GLU A 1 2180 ? 167.828 212.952 190.876 1.00 82.58  ? 2180 GLU A CA    1 
ATOM   5788  C  C     . GLU A 1 2180 ? 167.217 212.687 189.505 1.00 86.97  ? 2180 GLU A C     1 
ATOM   5789  O  O     . GLU A 1 2180 ? 166.000 212.823 189.322 1.00 95.57  ? 2180 GLU A O     1 
ATOM   5790  C  CB    . GLU A 1 2180 ? 168.459 214.343 190.920 1.00 85.96  ? 2180 GLU A CB    1 
ATOM   5791  C  CG    . GLU A 1 2180 ? 168.718 214.868 192.320 1.00 91.68  ? 2180 GLU A CG    1 
ATOM   5792  C  CD    . GLU A 1 2180 ? 168.897 216.373 192.352 1.00 95.98  ? 2180 GLU A CD    1 
ATOM   5793  O  OE1   . GLU A 1 2180 ? 169.990 216.851 191.984 1.00 94.86  ? 2180 GLU A OE1   1 
ATOM   5794  O  OE2   . GLU A 1 2180 ? 167.943 217.078 192.742 1.00 93.48  ? 2180 GLU A OE2   1 
ATOM   5795  N  N     . GLU A 1 2181 ? 168.047 212.315 188.527 1.00 75.40  ? 2181 GLU A N     1 
ATOM   5796  C  CA    . GLU A 1 2181 ? 167.515 211.998 187.204 1.00 74.28  ? 2181 GLU A CA    1 
ATOM   5797  C  C     . GLU A 1 2181 ? 166.598 210.781 187.251 1.00 81.87  ? 2181 GLU A C     1 
ATOM   5798  O  O     . GLU A 1 2181 ? 165.557 210.756 186.585 1.00 87.75  ? 2181 GLU A O     1 
ATOM   5799  C  CB    . GLU A 1 2181 ? 168.650 211.780 186.204 1.00 74.11  ? 2181 GLU A CB    1 
ATOM   5800  C  CG    . GLU A 1 2181 ? 169.654 212.917 186.133 1.00 84.78  ? 2181 GLU A CG    1 
ATOM   5801  C  CD    . GLU A 1 2181 ? 169.006 214.286 186.237 1.00 86.49  ? 2181 GLU A CD    1 
ATOM   5802  O  OE1   . GLU A 1 2181 ? 168.069 214.568 185.459 1.00 85.68  ? 2181 GLU A OE1   1 
ATOM   5803  O  OE2   . GLU A 1 2181 ? 169.435 215.082 187.098 1.00 89.23  ? 2181 GLU A OE2   1 
ATOM   5804  N  N     . LEU A 1 2182 ? 166.967 209.762 188.030 1.00 68.98  ? 2182 LEU A N     1 
ATOM   5805  C  CA    . LEU A 1 2182 ? 166.102 208.595 188.181 1.00 62.72  ? 2182 LEU A CA    1 
ATOM   5806  C  C     . LEU A 1 2182 ? 164.779 208.973 188.832 1.00 71.85  ? 2182 LEU A C     1 
ATOM   5807  O  O     . LEU A 1 2182 ? 163.719 208.488 188.423 1.00 89.28  ? 2182 LEU A O     1 
ATOM   5808  C  CB    . LEU A 1 2182 ? 166.804 207.511 188.999 1.00 58.86  ? 2182 LEU A CB    1 
ATOM   5809  C  CG    . LEU A 1 2182 ? 168.040 206.843 188.400 1.00 61.61  ? 2182 LEU A CG    1 
ATOM   5810  C  CD1   . LEU A 1 2182 ? 168.582 205.789 189.346 1.00 68.10  ? 2182 LEU A CD1   1 
ATOM   5811  C  CD2   . LEU A 1 2182 ? 167.716 206.227 187.057 1.00 62.47  ? 2182 LEU A CD2   1 
ATOM   5812  N  N     . LYS A 1 2183 ? 164.822 209.833 189.852 1.00 63.78  ? 2183 LYS A N     1 
ATOM   5813  C  CA    . LYS A 1 2183 ? 163.591 210.287 190.490 1.00 69.25  ? 2183 LYS A CA    1 
ATOM   5814  C  C     . LYS A 1 2183 ? 162.696 211.015 189.498 1.00 76.00  ? 2183 LYS A C     1 
ATOM   5815  O  O     . LYS A 1 2183 ? 161.487 210.760 189.436 1.00 77.14  ? 2183 LYS A O     1 
ATOM   5816  C  CB    . LYS A 1 2183 ? 163.921 211.194 191.676 1.00 70.37  ? 2183 LYS A CB    1 
ATOM   5817  C  CG    . LYS A 1 2183 ? 162.737 211.501 192.579 1.00 75.99  ? 2183 LYS A CG    1 
ATOM   5818  C  CD    . LYS A 1 2183 ? 163.147 211.563 194.044 1.00 73.62  ? 2183 LYS A CD    1 
ATOM   5819  C  CE    . LYS A 1 2183 ? 164.471 212.291 194.226 1.00 72.63  ? 2183 LYS A CE    1 
ATOM   5820  N  NZ    . LYS A 1 2183 ? 164.931 212.268 195.642 1.00 73.63  ? 2183 LYS A NZ    1 
ATOM   5821  N  N     . LYS A 1 2184 ? 163.275 211.917 188.702 1.00 71.22  ? 2184 LYS A N     1 
ATOM   5822  C  CA    . LYS A 1 2184 ? 162.480 212.642 187.716 1.00 65.63  ? 2184 LYS A CA    1 
ATOM   5823  C  C     . LYS A 1 2184 ? 161.883 211.695 186.682 1.00 71.46  ? 2184 LYS A C     1 
ATOM   5824  O  O     . LYS A 1 2184 ? 160.693 211.789 186.356 1.00 78.81  ? 2184 LYS A O     1 
ATOM   5825  C  CB    . LYS A 1 2184 ? 163.333 213.709 187.033 1.00 65.57  ? 2184 LYS A CB    1 
ATOM   5826  C  CG    . LYS A 1 2184 ? 163.537 214.964 187.859 1.00 72.20  ? 2184 LYS A CG    1 
ATOM   5827  C  CD    . LYS A 1 2184 ? 164.054 216.099 186.996 1.00 79.07  ? 2184 LYS A CD    1 
ATOM   5828  C  CE    . LYS A 1 2184 ? 165.557 216.258 187.135 1.00 78.95  ? 2184 LYS A CE    1 
ATOM   5829  N  NZ    . LYS A 1 2184 ? 165.927 216.981 188.381 1.00 78.17  ? 2184 LYS A NZ    1 
ATOM   5830  N  N     . VAL A 1 2185 ? 162.691 210.762 186.171 1.00 68.33  ? 2185 VAL A N     1 
ATOM   5831  C  CA    . VAL A 1 2185 ? 162.211 209.833 185.152 1.00 69.84  ? 2185 VAL A CA    1 
ATOM   5832  C  C     . VAL A 1 2185 ? 161.092 208.961 185.707 1.00 75.70  ? 2185 VAL A C     1 
ATOM   5833  O  O     . VAL A 1 2185 ? 160.078 208.727 185.038 1.00 87.28  ? 2185 VAL A O     1 
ATOM   5834  C  CB    . VAL A 1 2185 ? 163.378 208.988 184.609 1.00 64.60  ? 2185 VAL A CB    1 
ATOM   5835  C  CG1   . VAL A 1 2185 ? 162.857 207.827 183.789 1.00 73.38  ? 2185 VAL A CG1   1 
ATOM   5836  C  CG2   . VAL A 1 2185 ? 164.304 209.851 183.770 1.00 69.42  ? 2185 VAL A CG2   1 
ATOM   5837  N  N     . CYS A 1 2186 ? 161.251 208.474 186.939 1.00 67.65  ? 2186 CYS A N     1 
ATOM   5838  C  CA    . CYS A 1 2186 ? 160.197 207.685 187.564 1.00 66.79  ? 2186 CYS A CA    1 
ATOM   5839  C  C     . CYS A 1 2186 ? 158.931 208.510 187.745 1.00 66.26  ? 2186 CYS A C     1 
ATOM   5840  O  O     . CYS A 1 2186 ? 157.818 207.998 187.576 1.00 67.95  ? 2186 CYS A O     1 
ATOM   5841  C  CB    . CYS A 1 2186 ? 160.677 207.138 188.907 1.00 67.61  ? 2186 CYS A CB    1 
ATOM   5842  S  SG    . CYS A 1 2186 ? 161.902 205.820 188.778 1.00 79.35  ? 2186 CYS A SG    1 
ATOM   5843  N  N     . GLN A 1 2187 ? 159.079 209.790 188.095 1.00 79.61  ? 2187 GLN A N     1 
ATOM   5844  C  CA    . GLN A 1 2187 ? 157.910 210.649 188.241 1.00 87.21  ? 2187 GLN A CA    1 
ATOM   5845  C  C     . GLN A 1 2187 ? 157.175 210.818 186.917 1.00 88.32  ? 2187 GLN A C     1 
ATOM   5846  O  O     . GLN A 1 2187 ? 155.939 210.815 186.882 1.00 89.32  ? 2187 GLN A O     1 
ATOM   5847  C  CB    . GLN A 1 2187 ? 158.321 212.008 188.806 1.00 90.10  ? 2187 GLN A CB    1 
ATOM   5848  C  CG    . GLN A 1 2187 ? 157.257 212.668 189.673 1.00 89.44  ? 2187 GLN A CG    1 
ATOM   5849  C  CD    . GLN A 1 2187 ? 156.841 211.812 190.857 1.00 93.32  ? 2187 GLN A CD    1 
ATOM   5850  O  OE1   . GLN A 1 2187 ? 157.611 210.984 191.344 1.00 94.88  ? 2187 GLN A OE1   1 
ATOM   5851  N  NE2   . GLN A 1 2187 ? 155.612 212.006 191.322 1.00 88.94  ? 2187 GLN A NE2   1 
ATOM   5852  N  N     . GLU A 1 2188 ? 157.912 210.968 185.813 1.00 87.66  ? 2188 GLU A N     1 
ATOM   5853  C  CA    . GLU A 1 2188 ? 157.252 211.124 184.520 1.00 83.69  ? 2188 GLU A CA    1 
ATOM   5854  C  C     . GLU A 1 2188 ? 156.692 209.820 183.965 1.00 87.78  ? 2188 GLU A C     1 
ATOM   5855  O  O     . GLU A 1 2188 ? 155.859 209.865 183.054 1.00 93.30  ? 2188 GLU A O     1 
ATOM   5856  C  CB    . GLU A 1 2188 ? 158.199 211.740 183.487 1.00 82.65  ? 2188 GLU A CB    1 
ATOM   5857  C  CG    . GLU A 1 2188 ? 159.099 212.829 184.024 1.00 87.49  ? 2188 GLU A CG    1 
ATOM   5858  C  CD    . GLU A 1 2188 ? 159.536 213.801 182.949 1.00 96.07  ? 2188 GLU A CD    1 
ATOM   5859  O  OE1   . GLU A 1 2188 ? 160.118 214.850 183.298 1.00 96.38  ? 2188 GLU A OE1   1 
ATOM   5860  O  OE2   . GLU A 1 2188 ? 159.294 213.520 181.757 1.00 95.75  ? 2188 GLU A OE2   1 
ATOM   5861  N  N     . MET A 1 2189 ? 157.121 208.666 184.475 1.00 77.64  ? 2189 MET A N     1 
ATOM   5862  C  CA    . MET A 1 2189 ? 156.615 207.384 184.001 1.00 78.19  ? 2189 MET A CA    1 
ATOM   5863  C  C     . MET A 1 2189 ? 155.737 206.674 185.023 1.00 79.18  ? 2189 MET A C     1 
ATOM   5864  O  O     . MET A 1 2189 ? 155.459 205.483 184.858 1.00 74.50  ? 2189 MET A O     1 
ATOM   5865  C  CB    . MET A 1 2189 ? 157.769 206.469 183.587 1.00 72.26  ? 2189 MET A CB    1 
ATOM   5866  C  CG    . MET A 1 2189 ? 158.779 207.112 182.657 1.00 79.21  ? 2189 MET A CG    1 
ATOM   5867  S  SD    . MET A 1 2189 ? 160.175 206.028 182.303 1.00 90.24  ? 2189 MET A SD    1 
ATOM   5868  C  CE    . MET A 1 2189 ? 159.360 204.438 182.195 1.00 81.07  ? 2189 MET A CE    1 
ATOM   5869  N  N     . TYR A 1 2190 ? 155.289 207.378 186.065 1.00 78.84  ? 2190 TYR A N     1 
ATOM   5870  C  CA    . TYR A 1 2190 ? 154.387 206.821 187.075 1.00 73.17  ? 2190 TYR A CA    1 
ATOM   5871  C  C     . TYR A 1 2190 ? 154.991 205.608 187.776 1.00 71.77  ? 2190 TYR A C     1 
ATOM   5872  O  O     . TYR A 1 2190 ? 154.293 204.632 188.060 1.00 72.10  ? 2190 TYR A O     1 
ATOM   5873  C  CB    . TYR A 1 2190 ? 153.030 206.460 186.465 1.00 66.30  ? 2190 TYR A CB    1 
ATOM   5874  C  CG    . TYR A 1 2190 ? 152.498 207.501 185.511 1.00 70.78  ? 2190 TYR A CG    1 
ATOM   5875  C  CD1   . TYR A 1 2190 ? 152.077 208.740 185.969 1.00 71.24  ? 2190 TYR A CD1   1 
ATOM   5876  C  CD2   . TYR A 1 2190 ? 152.427 207.248 184.148 1.00 70.85  ? 2190 TYR A CD2   1 
ATOM   5877  C  CE1   . TYR A 1 2190 ? 151.594 209.696 185.098 1.00 74.57  ? 2190 TYR A CE1   1 
ATOM   5878  C  CE2   . TYR A 1 2190 ? 151.948 208.197 183.270 1.00 74.01  ? 2190 TYR A CE2   1 
ATOM   5879  C  CZ    . TYR A 1 2190 ? 151.531 209.418 183.750 1.00 78.59  ? 2190 TYR A CZ    1 
ATOM   5880  O  OH    . TYR A 1 2190 ? 151.051 210.366 182.876 1.00 83.96  ? 2190 TYR A OH    1 
ATOM   5881  N  N     . LEU A 1 2191 ? 156.287 205.656 188.060 1.00 71.43  ? 2191 LEU A N     1 
ATOM   5882  C  CA    . LEU A 1 2191 ? 156.982 204.573 188.739 1.00 66.29  ? 2191 LEU A CA    1 
ATOM   5883  C  C     . LEU A 1 2191 ? 157.284 204.956 190.182 1.00 69.10  ? 2191 LEU A C     1 
ATOM   5884  O  O     . LEU A 1 2191 ? 157.408 206.136 190.521 1.00 75.54  ? 2191 LEU A O     1 
ATOM   5885  C  CB    . LEU A 1 2191 ? 158.281 204.215 188.014 1.00 65.29  ? 2191 LEU A CB    1 
ATOM   5886  C  CG    . LEU A 1 2191 ? 158.250 202.984 187.106 1.00 62.72  ? 2191 LEU A CG    1 
ATOM   5887  C  CD1   . LEU A 1 2191 ? 157.294 203.179 185.949 1.00 67.53  ? 2191 LEU A CD1   1 
ATOM   5888  C  CD2   . LEU A 1 2191 ? 159.641 202.674 186.592 1.00 62.36  ? 2191 LEU A CD2   1 
ATOM   5889  N  N     . THR A 1 2192 ? 157.398 203.940 191.033 1.00 72.32  ? 2192 THR A N     1 
ATOM   5890  C  CA    . THR A 1 2192 ? 157.668 204.158 192.447 1.00 78.58  ? 2192 THR A CA    1 
ATOM   5891  C  C     . THR A 1 2192 ? 159.170 204.212 192.691 1.00 75.81  ? 2192 THR A C     1 
ATOM   5892  O  O     . THR A 1 2192 ? 159.898 203.270 192.363 1.00 72.75  ? 2192 THR A O     1 
ATOM   5893  C  CB    . THR A 1 2192 ? 157.039 203.050 193.290 1.00 77.91  ? 2192 THR A CB    1 
ATOM   5894  O  OG1   . THR A 1 2192 ? 155.614 203.087 193.143 1.00 81.44  ? 2192 THR A OG1   1 
ATOM   5895  C  CG2   . THR A 1 2192 ? 157.396 203.229 194.756 1.00 73.97  ? 2192 THR A CG2   1 
ATOM   5896  N  N     . TYR A 1 2193 ? 159.629 205.316 193.270 1.00 87.44  ? 2193 TYR A N     1 
ATOM   5897  C  CA    . TYR A 1 2193 ? 161.038 205.533 193.558 1.00 87.16  ? 2193 TYR A CA    1 
ATOM   5898  C  C     . TYR A 1 2193 ? 161.242 205.599 195.065 1.00 87.99  ? 2193 TYR A C     1 
ATOM   5899  O  O     . TYR A 1 2193 ? 160.426 206.180 195.787 1.00 94.15  ? 2193 TYR A O     1 
ATOM   5900  C  CB    . TYR A 1 2193 ? 161.533 206.823 192.896 1.00 86.12  ? 2193 TYR A CB    1 
ATOM   5901  C  CG    . TYR A 1 2193 ? 162.946 207.219 193.263 1.00 88.96  ? 2193 TYR A CG    1 
ATOM   5902  C  CD1   . TYR A 1 2193 ? 163.202 208.042 194.350 1.00 89.39  ? 2193 TYR A CD1   1 
ATOM   5903  C  CD2   . TYR A 1 2193 ? 164.023 206.782 192.507 1.00 88.37  ? 2193 TYR A CD2   1 
ATOM   5904  C  CE1   . TYR A 1 2193 ? 164.491 208.406 194.682 1.00 86.90  ? 2193 TYR A CE1   1 
ATOM   5905  C  CE2   . TYR A 1 2193 ? 165.314 207.144 192.829 1.00 89.44  ? 2193 TYR A CE2   1 
ATOM   5906  C  CZ    . TYR A 1 2193 ? 165.542 207.956 193.916 1.00 90.64  ? 2193 TYR A CZ    1 
ATOM   5907  O  OH    . TYR A 1 2193 ? 166.828 208.316 194.241 1.00 93.48  ? 2193 TYR A OH    1 
ATOM   5908  N  N     . GLY A 1 2194 ? 162.328 205.003 195.534 1.00 81.64  ? 2194 GLY A N     1 
ATOM   5909  C  CA    . GLY A 1 2194 ? 162.646 205.021 196.952 1.00 88.27  ? 2194 GLY A CA    1 
ATOM   5910  C  C     . GLY A 1 2194 ? 164.137 204.928 197.164 1.00 89.38  ? 2194 GLY A C     1 
ATOM   5911  O  O     . GLY A 1 2194 ? 164.830 204.156 196.495 1.00 87.31  ? 2194 GLY A O     1 
ATOM   5912  N  N     . ASP A 1 2195 ? 164.635 205.717 198.111 1.00 99.65  ? 2195 ASP A N     1 
ATOM   5913  C  CA    . ASP A 1 2195 ? 166.059 205.787 198.416 1.00 97.61  ? 2195 ASP A CA    1 
ATOM   5914  C  C     . ASP A 1 2195 ? 166.346 204.959 199.661 1.00 96.78  ? 2195 ASP A C     1 
ATOM   5915  O  O     . ASP A 1 2195 ? 165.865 205.286 200.751 1.00 103.30 ? 2195 ASP A O     1 
ATOM   5916  C  CB    . ASP A 1 2195 ? 166.502 207.235 198.624 1.00 100.00 ? 2195 ASP A CB    1 
ATOM   5917  C  CG    . ASP A 1 2195 ? 166.849 207.930 197.325 1.00 100.99 ? 2195 ASP A CG    1 
ATOM   5918  O  OD1   . ASP A 1 2195 ? 167.139 207.227 196.335 1.00 100.95 ? 2195 ASP A OD1   1 
ATOM   5919  O  OD2   . ASP A 1 2195 ? 166.832 209.179 197.292 1.00 98.09  ? 2195 ASP A OD2   1 
ATOM   5920  N  N     . GLY A 1 2196 ? 167.130 203.898 199.498 1.00 92.74  ? 2196 GLY A N     1 
ATOM   5921  C  CA    . GLY A 1 2196 ? 167.541 203.086 200.626 1.00 96.89  ? 2196 GLY A CA    1 
ATOM   5922  C  C     . GLY A 1 2196 ? 166.538 202.024 201.024 1.00 98.75  ? 2196 GLY A C     1 
ATOM   5923  O  O     . GLY A 1 2196 ? 166.365 201.027 200.317 1.00 102.65 ? 2196 GLY A O     1 
ATOM   5924  N  N     . GLU A 1 2197 ? 165.875 202.221 202.161 1.00 104.30 ? 2197 GLU A N     1 
ATOM   5925  C  CA    . GLU A 1 2197 ? 164.909 201.260 202.675 1.00 101.06 ? 2197 GLU A CA    1 
ATOM   5926  C  C     . GLU A 1 2197 ? 163.465 201.647 202.387 1.00 99.91  ? 2197 GLU A C     1 
ATOM   5927  O  O     . GLU A 1 2197 ? 162.554 200.913 202.781 1.00 102.17 ? 2197 GLU A O     1 
ATOM   5928  C  CB    . GLU A 1 2197 ? 165.099 201.074 204.184 1.00 101.09 ? 2197 GLU A CB    1 
ATOM   5929  C  CG    . GLU A 1 2197 ? 166.377 200.339 204.577 1.00 103.67 ? 2197 GLU A CG    1 
ATOM   5930  C  CD    . GLU A 1 2197 ? 166.320 198.840 204.316 1.00 105.98 ? 2197 GLU A CD    1 
ATOM   5931  O  OE1   . GLU A 1 2197 ? 165.416 198.378 203.588 1.00 107.37 ? 2197 GLU A OE1   1 
ATOM   5932  O  OE2   . GLU A 1 2197 ? 167.189 198.117 204.847 1.00 105.38 ? 2197 GLU A OE2   1 
ATOM   5933  N  N     . GLU A 1 2198 ? 163.232 202.772 201.716 1.00 93.05  ? 2198 GLU A N     1 
ATOM   5934  C  CA    . GLU A 1 2198 ? 161.880 203.145 201.335 1.00 95.24  ? 2198 GLU A CA    1 
ATOM   5935  C  C     . GLU A 1 2198 ? 161.334 202.169 200.295 1.00 97.29  ? 2198 GLU A C     1 
ATOM   5936  O  O     . GLU A 1 2198 ? 162.038 201.287 199.793 1.00 97.28  ? 2198 GLU A O     1 
ATOM   5937  C  CB    . GLU A 1 2198 ? 161.848 204.574 200.791 1.00 94.54  ? 2198 GLU A CB    1 
ATOM   5938  C  CG    . GLU A 1 2198 ? 161.684 205.663 201.847 1.00 96.02  ? 2198 GLU A CG    1 
ATOM   5939  C  CD    . GLU A 1 2198 ? 162.762 205.642 202.916 1.00 100.12 ? 2198 GLU A CD    1 
ATOM   5940  O  OE1   . GLU A 1 2198 ? 163.862 205.111 202.659 1.00 102.87 ? 2198 GLU A OE1   1 
ATOM   5941  O  OE2   . GLU A 1 2198 ? 162.506 206.162 204.023 1.00 101.84 ? 2198 GLU A OE2   1 
ATOM   5942  N  N     . VAL A 1 2199 ? 160.053 202.333 199.974 1.00 90.25  ? 2199 VAL A N     1 
ATOM   5943  C  CA    . VAL A 1 2199 ? 159.414 201.499 198.965 1.00 83.05  ? 2199 VAL A CA    1 
ATOM   5944  C  C     . VAL A 1 2199 ? 160.082 201.770 197.625 1.00 86.09  ? 2199 VAL A C     1 
ATOM   5945  O  O     . VAL A 1 2199 ? 159.928 202.854 197.050 1.00 93.67  ? 2199 VAL A O     1 
ATOM   5946  C  CB    . VAL A 1 2199 ? 157.899 201.762 198.896 1.00 86.00  ? 2199 VAL A CB    1 
ATOM   5947  C  CG1   . VAL A 1 2199 ? 157.233 200.773 197.957 1.00 88.19  ? 2199 VAL A CG1   1 
ATOM   5948  C  CG2   . VAL A 1 2199 ? 157.286 201.684 200.285 1.00 86.81  ? 2199 VAL A CG2   1 
ATOM   5949  N  N     . GLY A 1 2200 ? 160.822 200.788 197.117 1.00 77.12  ? 2200 GLY A N     1 
ATOM   5950  C  CA    . GLY A 1 2200 ? 161.548 200.936 195.875 1.00 81.28  ? 2200 GLY A CA    1 
ATOM   5951  C  C     . GLY A 1 2200 ? 163.045 201.103 196.009 1.00 79.88  ? 2200 GLY A C     1 
ATOM   5952  O  O     . GLY A 1 2200 ? 163.705 201.409 195.009 1.00 86.60  ? 2200 GLY A O     1 
ATOM   5953  N  N     . GLY A 1 2201 ? 163.601 200.922 197.208 1.00 70.92  ? 2201 GLY A N     1 
ATOM   5954  C  CA    . GLY A 1 2201 ? 165.040 201.049 197.367 1.00 75.28  ? 2201 GLY A CA    1 
ATOM   5955  C  C     . GLY A 1 2201 ? 165.811 199.965 196.638 1.00 74.06  ? 2201 GLY A C     1 
ATOM   5956  O  O     . GLY A 1 2201 ? 166.840 200.236 196.013 1.00 82.06  ? 2201 GLY A O     1 
ATOM   5957  N  N     . MET A 1 2202 ? 165.326 198.724 196.708 1.00 64.80  ? 2202 MET A N     1 
ATOM   5958  C  CA    . MET A 1 2202 ? 166.009 197.623 196.038 1.00 70.51  ? 2202 MET A CA    1 
ATOM   5959  C  C     . MET A 1 2202 ? 166.010 197.811 194.527 1.00 70.98  ? 2202 MET A C     1 
ATOM   5960  O  O     . MET A 1 2202 ? 167.010 197.524 193.860 1.00 77.76  ? 2202 MET A O     1 
ATOM   5961  C  CB    . MET A 1 2202 ? 165.356 196.295 196.414 1.00 72.78  ? 2202 MET A CB    1 
ATOM   5962  C  CG    . MET A 1 2202 ? 165.382 195.996 197.902 1.00 76.74  ? 2202 MET A CG    1 
ATOM   5963  S  SD    . MET A 1 2202 ? 165.362 194.230 198.256 1.00 94.46  ? 2202 MET A SD    1 
ATOM   5964  C  CE    . MET A 1 2202 ? 163.845 194.097 199.197 1.00 80.69  ? 2202 MET A CE    1 
ATOM   5965  N  N     . TRP A 1 2203 ? 164.898 198.291 193.968 1.00 52.06  ? 2203 TRP A N     1 
ATOM   5966  C  CA    . TRP A 1 2203 ? 164.822 198.471 192.522 1.00 55.92  ? 2203 TRP A CA    1 
ATOM   5967  C  C     . TRP A 1 2203 ? 165.799 199.538 192.041 1.00 60.15  ? 2203 TRP A C     1 
ATOM   5968  O  O     . TRP A 1 2203 ? 166.502 199.342 191.042 1.00 73.26  ? 2203 TRP A O     1 
ATOM   5969  C  CB    . TRP A 1 2203 ? 163.394 198.825 192.115 1.00 59.87  ? 2203 TRP A CB    1 
ATOM   5970  C  CG    . TRP A 1 2203 ? 163.227 199.004 190.644 1.00 52.35  ? 2203 TRP A CG    1 
ATOM   5971  C  CD1   . TRP A 1 2203 ? 163.169 198.022 189.702 1.00 46.22  ? 2203 TRP A CD1   1 
ATOM   5972  C  CD2   . TRP A 1 2203 ? 163.102 200.244 189.942 1.00 49.94  ? 2203 TRP A CD2   1 
ATOM   5973  N  NE1   . TRP A 1 2203 ? 163.012 198.573 188.455 1.00 52.62  ? 2203 TRP A NE1   1 
ATOM   5974  C  CE2   . TRP A 1 2203 ? 162.968 199.936 188.576 1.00 52.11  ? 2203 TRP A CE2   1 
ATOM   5975  C  CE3   . TRP A 1 2203 ? 163.089 201.584 190.336 1.00 57.69  ? 2203 TRP A CE3   1 
ATOM   5976  C  CZ2   . TRP A 1 2203 ? 162.824 200.919 187.602 1.00 60.47  ? 2203 TRP A CZ2   1 
ATOM   5977  C  CZ3   . TRP A 1 2203 ? 162.946 202.556 189.369 1.00 57.83  ? 2203 TRP A CZ3   1 
ATOM   5978  C  CH2   . TRP A 1 2203 ? 162.816 202.220 188.018 1.00 58.29  ? 2203 TRP A CH2   1 
ATOM   5979  N  N     . VAL A 1 2204 ? 165.867 200.673 192.739 1.00 48.21  ? 2204 VAL A N     1 
ATOM   5980  C  CA    . VAL A 1 2204 ? 166.787 201.725 192.319 1.00 42.68  ? 2204 VAL A CA    1 
ATOM   5981  C  C     . VAL A 1 2204 ? 168.230 201.304 192.568 1.00 52.47  ? 2204 VAL A C     1 
ATOM   5982  O  O     . VAL A 1 2204 ? 169.140 201.691 191.826 1.00 64.98  ? 2204 VAL A O     1 
ATOM   5983  C  CB    . VAL A 1 2204 ? 166.446 203.057 193.013 1.00 50.69  ? 2204 VAL A CB    1 
ATOM   5984  C  CG1   . VAL A 1 2204 ? 166.922 203.060 194.452 1.00 64.03  ? 2204 VAL A CG1   1 
ATOM   5985  C  CG2   . VAL A 1 2204 ? 167.059 204.211 192.250 1.00 54.15  ? 2204 VAL A CG2   1 
ATOM   5986  N  N     . GLU A 1 2205 ? 168.466 200.498 193.606 1.00 62.59  ? 2205 GLU A N     1 
ATOM   5987  C  CA    . GLU A 1 2205 ? 169.806 199.968 193.829 1.00 61.17  ? 2205 GLU A CA    1 
ATOM   5988  C  C     . GLU A 1 2205 ? 170.213 199.040 192.691 1.00 64.66  ? 2205 GLU A C     1 
ATOM   5989  O  O     . GLU A 1 2205 ? 171.362 199.066 192.232 1.00 67.17  ? 2205 GLU A O     1 
ATOM   5990  C  CB    . GLU A 1 2205 ? 169.860 199.252 195.179 1.00 56.42  ? 2205 GLU A CB    1 
ATOM   5991  C  CG    . GLU A 1 2205 ? 170.699 197.991 195.210 1.00 63.61  ? 2205 GLU A CG    1 
ATOM   5992  C  CD    . GLU A 1 2205 ? 172.181 198.285 195.338 1.00 77.11  ? 2205 GLU A CD    1 
ATOM   5993  O  OE1   . GLU A 1 2205 ? 172.969 197.325 195.448 1.00 82.77  ? 2205 GLU A OE1   1 
ATOM   5994  O  OE2   . GLU A 1 2205 ? 172.559 199.475 195.334 1.00 74.17  ? 2205 GLU A OE2   1 
ATOM   5995  N  N     . LYS A 1 2206 ? 169.272 198.223 192.211 1.00 49.95  ? 2206 LYS A N     1 
ATOM   5996  C  CA    . LYS A 1 2206 ? 169.529 197.390 191.041 1.00 49.00  ? 2206 LYS A CA    1 
ATOM   5997  C  C     . LYS A 1 2206 ? 169.796 198.240 189.806 1.00 52.56  ? 2206 LYS A C     1 
ATOM   5998  O  O     . LYS A 1 2206 ? 170.642 197.893 188.977 1.00 61.87  ? 2206 LYS A O     1 
ATOM   5999  C  CB    . LYS A 1 2206 ? 168.348 196.452 190.798 1.00 42.20  ? 2206 LYS A CB    1 
ATOM   6000  C  CG    . LYS A 1 2206 ? 168.336 195.214 191.673 1.00 50.89  ? 2206 LYS A CG    1 
ATOM   6001  C  CD    . LYS A 1 2206 ? 169.533 194.325 191.395 1.00 48.86  ? 2206 LYS A CD    1 
ATOM   6002  C  CE    . LYS A 1 2206 ? 169.937 193.550 192.636 1.00 50.92  ? 2206 LYS A CE    1 
ATOM   6003  N  NZ    . LYS A 1 2206 ? 170.848 192.420 192.311 1.00 48.14  ? 2206 LYS A NZ    1 
ATOM   6004  N  N     . VAL A 1 2207 ? 169.071 199.351 189.659 1.00 46.33  ? 2207 VAL A N     1 
ATOM   6005  C  CA    . VAL A 1 2207 ? 169.307 200.247 188.527 1.00 36.83  ? 2207 VAL A CA    1 
ATOM   6006  C  C     . VAL A 1 2207 ? 170.718 200.824 188.586 1.00 52.43  ? 2207 VAL A C     1 
ATOM   6007  O  O     . VAL A 1 2207 ? 171.418 200.908 187.568 1.00 63.33  ? 2207 VAL A O     1 
ATOM   6008  C  CB    . VAL A 1 2207 ? 168.242 201.358 188.492 1.00 38.87  ? 2207 VAL A CB    1 
ATOM   6009  C  CG1   . VAL A 1 2207 ? 168.626 202.431 187.489 1.00 40.17  ? 2207 VAL A CG1   1 
ATOM   6010  C  CG2   . VAL A 1 2207 ? 166.884 200.779 188.151 1.00 47.80  ? 2207 VAL A CG2   1 
ATOM   6011  N  N     . LEU A 1 2208 ? 171.155 201.239 189.777 1.00 58.15  ? 2208 LEU A N     1 
ATOM   6012  C  CA    . LEU A 1 2208 ? 172.507 201.772 189.923 1.00 54.52  ? 2208 LEU A CA    1 
ATOM   6013  C  C     . LEU A 1 2208 ? 173.556 200.702 189.640 1.00 57.69  ? 2208 LEU A C     1 
ATOM   6014  O  O     . LEU A 1 2208 ? 174.589 200.982 189.017 1.00 66.87  ? 2208 LEU A O     1 
ATOM   6015  C  CB    . LEU A 1 2208 ? 172.694 202.358 191.321 1.00 48.31  ? 2208 LEU A CB    1 
ATOM   6016  C  CG    . LEU A 1 2208 ? 171.778 203.533 191.663 1.00 47.08  ? 2208 LEU A CG    1 
ATOM   6017  C  CD1   . LEU A 1 2208 ? 172.088 204.075 193.046 1.00 57.38  ? 2208 LEU A CD1   1 
ATOM   6018  C  CD2   . LEU A 1 2208 ? 171.893 204.624 190.616 1.00 50.24  ? 2208 LEU A CD2   1 
ATOM   6019  N  N     . GLN A 1 2209 ? 173.312 199.470 190.093 1.00 49.14  ? 2209 GLN A N     1 
ATOM   6020  C  CA    . GLN A 1 2209 ? 174.222 198.375 189.770 1.00 51.02  ? 2209 GLN A CA    1 
ATOM   6021  C  C     . GLN A 1 2209 ? 174.279 198.137 188.267 1.00 59.74  ? 2209 GLN A C     1 
ATOM   6022  O  O     . GLN A 1 2209 ? 175.351 197.870 187.712 1.00 69.55  ? 2209 GLN A O     1 
ATOM   6023  C  CB    . GLN A 1 2209 ? 173.797 197.100 190.495 1.00 49.34  ? 2209 GLN A CB    1 
ATOM   6024  C  CG    . GLN A 1 2209 ? 174.076 197.098 191.984 1.00 54.64  ? 2209 GLN A CG    1 
ATOM   6025  C  CD    . GLN A 1 2209 ? 173.526 195.864 192.667 1.00 56.56  ? 2209 GLN A CD    1 
ATOM   6026  O  OE1   . GLN A 1 2209 ? 172.969 194.981 192.018 1.00 57.13  ? 2209 GLN A OE1   1 
ATOM   6027  N  NE2   . GLN A 1 2209 ? 173.690 195.791 193.981 1.00 55.03  ? 2209 GLN A NE2   1 
ATOM   6028  N  N     . LEU A 1 2210 ? 173.131 198.220 187.595 1.00 59.23  ? 2210 LEU A N     1 
ATOM   6029  C  CA    . LEU A 1 2210 ? 173.101 198.074 186.144 1.00 51.14  ? 2210 LEU A CA    1 
ATOM   6030  C  C     . LEU A 1 2210 ? 173.912 199.170 185.467 1.00 49.13  ? 2210 LEU A C     1 
ATOM   6031  O  O     . LEU A 1 2210 ? 174.626 198.911 184.493 1.00 58.49  ? 2210 LEU A O     1 
ATOM   6032  C  CB    . LEU A 1 2210 ? 171.655 198.092 185.651 1.00 49.06  ? 2210 LEU A CB    1 
ATOM   6033  C  CG    . LEU A 1 2210 ? 171.439 197.856 184.158 1.00 49.22  ? 2210 LEU A CG    1 
ATOM   6034  C  CD1   . LEU A 1 2210 ? 171.618 196.389 183.835 1.00 53.21  ? 2210 LEU A CD1   1 
ATOM   6035  C  CD2   . LEU A 1 2210 ? 170.062 198.333 183.736 1.00 54.79  ? 2210 LEU A CD2   1 
ATOM   6036  N  N     . TYR A 1 2211 ? 173.808 200.402 185.966 1.00 50.63  ? 2211 TYR A N     1 
ATOM   6037  C  CA    . TYR A 1 2211 ? 174.618 201.488 185.420 1.00 56.10  ? 2211 TYR A CA    1 
ATOM   6038  C  C     . TYR A 1 2211 ? 176.105 201.212 185.602 1.00 59.67  ? 2211 TYR A C     1 
ATOM   6039  O  O     . TYR A 1 2211 ? 176.905 201.408 184.675 1.00 70.77  ? 2211 TYR A O     1 
ATOM   6040  C  CB    . TYR A 1 2211 ? 174.240 202.813 186.081 1.00 61.48  ? 2211 TYR A CB    1 
ATOM   6041  C  CG    . TYR A 1 2211 ? 175.148 203.959 185.699 1.00 65.97  ? 2211 TYR A CG    1 
ATOM   6042  C  CD1   . TYR A 1 2211 ? 175.276 204.357 184.376 1.00 56.25  ? 2211 TYR A CD1   1 
ATOM   6043  C  CD2   . TYR A 1 2211 ? 175.879 204.640 186.662 1.00 66.25  ? 2211 TYR A CD2   1 
ATOM   6044  C  CE1   . TYR A 1 2211 ? 176.104 205.403 184.023 1.00 59.96  ? 2211 TYR A CE1   1 
ATOM   6045  C  CE2   . TYR A 1 2211 ? 176.709 205.688 186.318 1.00 66.42  ? 2211 TYR A CE2   1 
ATOM   6046  C  CZ    . TYR A 1 2211 ? 176.818 206.065 184.997 1.00 67.24  ? 2211 TYR A CZ    1 
ATOM   6047  O  OH    . TYR A 1 2211 ? 177.645 207.108 184.649 1.00 67.20  ? 2211 TYR A OH    1 
ATOM   6048  N  N     . GLN A 1 2212 ? 176.492 200.751 186.793 1.00 64.14  ? 2212 GLN A N     1 
ATOM   6049  C  CA    . GLN A 1 2212 ? 177.899 200.466 187.050 1.00 63.82  ? 2212 GLN A CA    1 
ATOM   6050  C  C     . GLN A 1 2212 ? 178.410 199.348 186.149 1.00 56.38  ? 2212 GLN A C     1 
ATOM   6051  O  O     . GLN A 1 2212 ? 179.546 199.403 185.665 1.00 62.55  ? 2212 GLN A O     1 
ATOM   6052  C  CB    . GLN A 1 2212 ? 178.104 200.111 188.522 1.00 61.66  ? 2212 GLN A CB    1 
ATOM   6053  C  CG    . GLN A 1 2212 ? 178.003 201.305 189.455 1.00 68.58  ? 2212 GLN A CG    1 
ATOM   6054  C  CD    . GLN A 1 2212 ? 178.457 200.986 190.864 1.00 71.80  ? 2212 GLN A CD    1 
ATOM   6055  O  OE1   . GLN A 1 2212 ? 177.928 200.081 191.509 1.00 77.86  ? 2212 GLN A OE1   1 
ATOM   6056  N  NE2   . GLN A 1 2212 ? 179.440 201.733 191.351 1.00 65.21  ? 2212 GLN A NE2   1 
ATOM   6057  N  N     . ILE A 1 2213 ? 177.587 198.324 185.914 1.00 49.78  ? 2213 ILE A N     1 
ATOM   6058  C  CA    . ILE A 1 2213 ? 178.004 197.237 185.032 1.00 48.10  ? 2213 ILE A CA    1 
ATOM   6059  C  C     . ILE A 1 2213 ? 178.087 197.711 183.584 1.00 50.36  ? 2213 ILE A C     1 
ATOM   6060  O  O     . ILE A 1 2213 ? 178.995 197.307 182.847 1.00 57.31  ? 2213 ILE A O     1 
ATOM   6061  C  CB    . ILE A 1 2213 ? 177.065 196.026 185.180 1.00 45.03  ? 2213 ILE A CB    1 
ATOM   6062  C  CG1   . ILE A 1 2213 ? 177.074 195.518 186.620 1.00 46.68  ? 2213 ILE A CG1   1 
ATOM   6063  C  CG2   . ILE A 1 2213 ? 177.500 194.903 184.260 1.00 49.08  ? 2213 ILE A CG2   1 
ATOM   6064  C  CD1   . ILE A 1 2213 ? 178.399 194.943 187.053 1.00 55.04  ? 2213 ILE A CD1   1 
ATOM   6065  N  N     . THR A 1 2214 ? 177.156 198.565 183.146 1.00 59.89  ? 2214 THR A N     1 
ATOM   6066  C  CA    . THR A 1 2214 ? 177.238 199.108 181.792 1.00 57.56  ? 2214 THR A CA    1 
ATOM   6067  C  C     . THR A 1 2214 ? 178.516 199.911 181.606 1.00 61.43  ? 2214 THR A C     1 
ATOM   6068  O  O     . THR A 1 2214 ? 179.126 199.881 180.531 1.00 63.78  ? 2214 THR A O     1 
ATOM   6069  C  CB    . THR A 1 2214 ? 176.025 199.986 181.479 1.00 56.72  ? 2214 THR A CB    1 
ATOM   6070  O  OG1   . THR A 1 2214 ? 175.790 200.888 182.564 1.00 68.08  ? 2214 THR A OG1   1 
ATOM   6071  C  CG2   . THR A 1 2214 ? 174.788 199.144 181.242 1.00 60.91  ? 2214 THR A CG2   1 
ATOM   6072  N  N     . GLN A 1 2215 ? 178.930 200.647 182.639 1.00 71.20  ? 2215 GLN A N     1 
ATOM   6073  C  CA    . GLN A 1 2215 ? 180.180 201.394 182.548 1.00 64.35  ? 2215 GLN A CA    1 
ATOM   6074  C  C     . GLN A 1 2215 ? 181.391 200.489 182.353 1.00 64.68  ? 2215 GLN A C     1 
ATOM   6075  O  O     . GLN A 1 2215 ? 182.394 200.936 181.788 1.00 67.06  ? 2215 GLN A O     1 
ATOM   6076  C  CB    . GLN A 1 2215 ? 180.380 202.255 183.794 1.00 64.38  ? 2215 GLN A CB    1 
ATOM   6077  C  CG    . GLN A 1 2215 ? 179.629 203.571 183.762 1.00 68.15  ? 2215 GLN A CG    1 
ATOM   6078  C  CD    . GLN A 1 2215 ? 180.405 204.694 184.418 1.00 74.73  ? 2215 GLN A CD    1 
ATOM   6079  O  OE1   . GLN A 1 2215 ? 180.575 205.767 183.839 1.00 74.99  ? 2215 GLN A OE1   1 
ATOM   6080  N  NE2   . GLN A 1 2215 ? 180.887 204.450 185.631 1.00 75.82  ? 2215 GLN A NE2   1 
ATOM   6081  N  N     . ILE A 1 2216 ? 181.325 199.238 182.801 1.00 63.99  ? 2216 ILE A N     1 
ATOM   6082  C  CA    . ILE A 1 2216 ? 182.475 198.342 182.715 1.00 64.04  ? 2216 ILE A CA    1 
ATOM   6083  C  C     . ILE A 1 2216 ? 182.401 197.441 181.488 1.00 71.09  ? 2216 ILE A C     1 
ATOM   6084  O  O     . ILE A 1 2216 ? 183.349 197.377 180.703 1.00 77.12  ? 2216 ILE A O     1 
ATOM   6085  C  CB    . ILE A 1 2216 ? 182.594 197.513 184.008 1.00 59.55  ? 2216 ILE A CB    1 
ATOM   6086  C  CG1   . ILE A 1 2216 ? 182.577 198.424 185.235 1.00 68.66  ? 2216 ILE A CG1   1 
ATOM   6087  C  CG2   . ILE A 1 2216 ? 183.856 196.667 183.985 1.00 59.89  ? 2216 ILE A CG2   1 
ATOM   6088  C  CD1   . ILE A 1 2216 ? 182.571 197.674 186.548 1.00 68.80  ? 2216 ILE A CD1   1 
ATOM   6089  N  N     . ASN A 1 2217 ? 181.289 196.738 181.300 1.00 68.03  ? 2217 ASN A N     1 
ATOM   6090  C  CA    . ASN A 1 2217 ? 181.171 195.710 180.276 1.00 60.40  ? 2217 ASN A CA    1 
ATOM   6091  C  C     . ASN A 1 2217 ? 180.347 196.214 179.100 1.00 64.49  ? 2217 ASN A C     1 
ATOM   6092  O  O     . ASN A 1 2217 ? 179.469 197.066 179.262 1.00 71.29  ? 2217 ASN A O     1 
ATOM   6093  C  CB    . ASN A 1 2217 ? 180.524 194.444 180.844 1.00 54.48  ? 2217 ASN A CB    1 
ATOM   6094  C  CG    . ASN A 1 2217 ? 181.355 193.805 181.934 1.00 64.82  ? 2217 ASN A CG    1 
ATOM   6095  O  OD1   . ASN A 1 2217 ? 181.029 193.901 183.116 1.00 66.09  ? 2217 ASN A OD1   1 
ATOM   6096  N  ND2   . ASN A 1 2217 ? 182.438 193.146 181.541 1.00 75.41  ? 2217 ASN A ND2   1 
ATOM   6097  N  N     . HIS A 1 2218 ? 180.638 195.681 177.915 1.00 56.77  ? 2218 HIS A N     1 
ATOM   6098  C  CA    . HIS A 1 2218 ? 179.825 195.925 176.733 1.00 60.87  ? 2218 HIS A CA    1 
ATOM   6099  C  C     . HIS A 1 2218 ? 178.784 194.837 176.507 1.00 59.71  ? 2218 HIS A C     1 
ATOM   6100  O  O     . HIS A 1 2218 ? 178.079 194.873 175.494 1.00 64.08  ? 2218 HIS A O     1 
ATOM   6101  C  CB    . HIS A 1 2218 ? 180.715 196.066 175.493 1.00 57.48  ? 2218 HIS A CB    1 
ATOM   6102  C  CG    . HIS A 1 2218 ? 181.608 194.890 175.248 1.00 58.22  ? 2218 HIS A CG    1 
ATOM   6103  N  ND1   . HIS A 1 2218 ? 182.797 194.706 175.918 1.00 61.36  ? 2218 HIS A ND1   1 
ATOM   6104  C  CD2   . HIS A 1 2218 ? 181.491 193.844 174.396 1.00 61.29  ? 2218 HIS A CD2   1 
ATOM   6105  C  CE1   . HIS A 1 2218 ? 183.372 193.595 175.496 1.00 57.76  ? 2218 HIS A CE1   1 
ATOM   6106  N  NE2   . HIS A 1 2218 ? 182.599 193.052 174.572 1.00 59.64  ? 2218 HIS A NE2   1 
ATOM   6107  N  N     . GLY A 1 2219 ? 178.678 193.875 177.419 1.00 57.94  ? 2219 GLY A N     1 
ATOM   6108  C  CA    . GLY A 1 2219 ? 177.649 192.857 177.358 1.00 50.74  ? 2219 GLY A CA    1 
ATOM   6109  C  C     . GLY A 1 2219 ? 177.047 192.592 178.722 1.00 65.11  ? 2219 GLY A C     1 
ATOM   6110  O  O     . GLY A 1 2219 ? 177.775 192.317 179.680 1.00 76.89  ? 2219 GLY A O     1 
ATOM   6111  N  N     . LEU A 1 2220 ? 175.723 192.673 178.830 1.00 63.52  ? 2220 LEU A N     1 
ATOM   6112  C  CA    . LEU A 1 2220 ? 175.038 192.530 180.105 1.00 51.67  ? 2220 LEU A CA    1 
ATOM   6113  C  C     . LEU A 1 2220 ? 173.933 191.491 179.996 1.00 59.27  ? 2220 LEU A C     1 
ATOM   6114  O  O     . LEU A 1 2220 ? 173.438 191.188 178.909 1.00 78.00  ? 2220 LEU A O     1 
ATOM   6115  C  CB    . LEU A 1 2220 ? 174.436 193.854 180.579 1.00 46.40  ? 2220 LEU A CB    1 
ATOM   6116  C  CG    . LEU A 1 2220 ? 175.407 194.928 181.051 1.00 58.31  ? 2220 LEU A CG    1 
ATOM   6117  C  CD1   . LEU A 1 2220 ? 175.819 195.822 179.896 1.00 64.80  ? 2220 LEU A CD1   1 
ATOM   6118  C  CD2   . LEU A 1 2220 ? 174.762 195.731 182.158 1.00 62.46  ? 2220 LEU A CD2   1 
ATOM   6119  N  N     . MET A 1 2221 ? 173.544 190.954 181.150 1.00 56.67  ? 2221 MET A N     1 
ATOM   6120  C  CA    . MET A 1 2221 ? 172.438 190.008 181.236 1.00 61.58  ? 2221 MET A CA    1 
ATOM   6121  C  C     . MET A 1 2221 ? 171.616 190.333 182.471 1.00 65.78  ? 2221 MET A C     1 
ATOM   6122  O  O     . MET A 1 2221 ? 172.064 190.093 183.596 1.00 72.14  ? 2221 MET A O     1 
ATOM   6123  C  CB    . MET A 1 2221 ? 172.941 188.563 181.293 1.00 60.83  ? 2221 MET A CB    1 
ATOM   6124  C  CG    . MET A 1 2221 ? 173.195 187.943 179.934 1.00 64.23  ? 2221 MET A CG    1 
ATOM   6125  S  SD    . MET A 1 2221 ? 173.237 186.143 179.982 1.00 89.08  ? 2221 MET A SD    1 
ATOM   6126  C  CE    . MET A 1 2221 ? 173.233 185.758 178.235 1.00 70.04  ? 2221 MET A CE    1 
ATOM   6127  N  N     . MET A 1 2222 ? 170.420 190.877 182.264 1.00 57.93  ? 2222 MET A N     1 
ATOM   6128  C  CA    . MET A 1 2222 ? 169.485 191.141 183.355 1.00 45.99  ? 2222 MET A CA    1 
ATOM   6129  C  C     . MET A 1 2222 ? 168.668 189.875 183.572 1.00 54.51  ? 2222 MET A C     1 
ATOM   6130  O  O     . MET A 1 2222 ? 167.639 189.667 182.925 1.00 69.25  ? 2222 MET A O     1 
ATOM   6131  C  CB    . MET A 1 2222 ? 168.596 192.335 183.033 1.00 45.27  ? 2222 MET A CB    1 
ATOM   6132  C  CG    . MET A 1 2222 ? 169.261 193.681 183.239 1.00 48.72  ? 2222 MET A CG    1 
ATOM   6133  S  SD    . MET A 1 2222 ? 168.710 194.917 182.051 1.00 73.37  ? 2222 MET A SD    1 
ATOM   6134  C  CE    . MET A 1 2222 ? 169.259 194.176 180.519 1.00 53.72  ? 2222 MET A CE    1 
ATOM   6135  N  N     . VAL A 1 2223 ? 169.123 189.027 184.487 1.00 47.08  ? 2223 VAL A N     1 
ATOM   6136  C  CA    . VAL A 1 2223 ? 168.514 187.725 184.731 1.00 46.92  ? 2223 VAL A CA    1 
ATOM   6137  C  C     . VAL A 1 2223 ? 167.610 187.829 185.949 1.00 50.24  ? 2223 VAL A C     1 
ATOM   6138  O  O     . VAL A 1 2223 ? 168.018 188.350 186.993 1.00 61.60  ? 2223 VAL A O     1 
ATOM   6139  C  CB    . VAL A 1 2223 ? 169.583 186.640 184.932 1.00 46.05  ? 2223 VAL A CB    1 
ATOM   6140  C  CG1   . VAL A 1 2223 ? 168.949 185.262 184.904 1.00 60.85  ? 2223 VAL A CG1   1 
ATOM   6141  C  CG2   . VAL A 1 2223 ? 170.661 186.758 183.870 1.00 49.34  ? 2223 VAL A CG2   1 
ATOM   6142  N  N     . GLY A 1 2224 ? 166.381 187.339 185.817 1.00 52.56  ? 2224 GLY A N     1 
ATOM   6143  C  CA    . GLY A 1 2224 ? 165.437 187.351 186.906 1.00 56.98  ? 2224 GLY A CA    1 
ATOM   6144  C  C     . GLY A 1 2224 ? 164.049 186.938 186.469 1.00 55.52  ? 2224 GLY A C     1 
ATOM   6145  O  O     . GLY A 1 2224 ? 163.667 187.096 185.307 1.00 61.32  ? 2224 GLY A O     1 
ATOM   6146  N  N     . PRO A 1 2225 ? 163.258 186.413 187.404 1.00 47.63  ? 2225 PRO A N     1 
ATOM   6147  C  CA    . PRO A 1 2225 ? 161.924 185.918 187.053 1.00 54.81  ? 2225 PRO A CA    1 
ATOM   6148  C  C     . PRO A 1 2225 ? 161.043 187.022 186.491 1.00 62.18  ? 2225 PRO A C     1 
ATOM   6149  O  O     . PRO A 1 2225 ? 161.279 188.214 186.701 1.00 63.39  ? 2225 PRO A O     1 
ATOM   6150  C  CB    . PRO A 1 2225 ? 161.376 185.395 188.386 1.00 58.95  ? 2225 PRO A CB    1 
ATOM   6151  C  CG    . PRO A 1 2225 ? 162.586 185.132 189.217 1.00 59.56  ? 2225 PRO A CG    1 
ATOM   6152  C  CD    . PRO A 1 2225 ? 163.579 186.177 188.820 1.00 51.29  ? 2225 PRO A CD    1 
ATOM   6153  N  N     . SER A 1 2226 ? 160.020 186.602 185.748 1.00 67.94  ? 2226 SER A N     1 
ATOM   6154  C  CA    . SER A 1 2226 ? 159.113 187.546 185.112 1.00 63.98  ? 2226 SER A CA    1 
ATOM   6155  C  C     . SER A 1 2226 ? 158.468 188.453 186.152 1.00 65.21  ? 2226 SER A C     1 
ATOM   6156  O  O     . SER A 1 2226 ? 158.083 188.009 187.237 1.00 71.37  ? 2226 SER A O     1 
ATOM   6157  C  CB    . SER A 1 2226 ? 158.036 186.799 184.328 1.00 70.33  ? 2226 SER A CB    1 
ATOM   6158  O  OG    . SER A 1 2226 ? 157.218 186.033 185.194 1.00 80.35  ? 2226 SER A OG    1 
ATOM   6159  N  N     . GLY A 1 2227 ? 158.348 189.730 185.811 1.00 55.14  ? 2227 GLY A N     1 
ATOM   6160  C  CA    . GLY A 1 2227 ? 157.821 190.701 186.751 1.00 61.38  ? 2227 GLY A CA    1 
ATOM   6161  C  C     . GLY A 1 2227 ? 158.769 191.059 187.873 1.00 68.24  ? 2227 GLY A C     1 
ATOM   6162  O  O     . GLY A 1 2227 ? 158.340 191.175 189.028 1.00 70.47  ? 2227 GLY A O     1 
ATOM   6163  N  N     . SER A 1 2228 ? 160.055 191.223 187.567 1.00 58.83  ? 2228 SER A N     1 
ATOM   6164  C  CA    . SER A 1 2228 ? 161.032 191.694 188.536 1.00 45.45  ? 2228 SER A CA    1 
ATOM   6165  C  C     . SER A 1 2228 ? 161.568 193.079 188.204 1.00 56.35  ? 2228 SER A C     1 
ATOM   6166  O  O     . SER A 1 2228 ? 162.504 193.541 188.865 1.00 69.20  ? 2228 SER A O     1 
ATOM   6167  C  CB    . SER A 1 2228 ? 162.193 190.700 188.646 1.00 47.04  ? 2228 SER A CB    1 
ATOM   6168  O  OG    . SER A 1 2228 ? 162.675 190.341 187.365 1.00 65.90  ? 2228 SER A OG    1 
ATOM   6169  N  N     . GLY A 1 2229 ? 161.008 193.749 187.201 1.00 53.57  ? 2229 GLY A N     1 
ATOM   6170  C  CA    . GLY A 1 2229 ? 161.370 195.120 186.909 1.00 51.73  ? 2229 GLY A CA    1 
ATOM   6171  C  C     . GLY A 1 2229 ? 162.576 195.316 186.022 1.00 58.41  ? 2229 GLY A C     1 
ATOM   6172  O  O     . GLY A 1 2229 ? 163.143 196.413 186.018 1.00 67.23  ? 2229 GLY A O     1 
ATOM   6173  N  N     . LYS A 1 2230 ? 162.989 194.297 185.266 1.00 49.58  ? 2230 LYS A N     1 
ATOM   6174  C  CA    . LYS A 1 2230 ? 164.177 194.430 184.425 1.00 42.66  ? 2230 LYS A CA    1 
ATOM   6175  C  C     . LYS A 1 2230 ? 163.958 195.446 183.309 1.00 47.48  ? 2230 LYS A C     1 
ATOM   6176  O  O     . LYS A 1 2230 ? 164.777 196.355 183.109 1.00 57.19  ? 2230 LYS A O     1 
ATOM   6177  C  CB    . LYS A 1 2230 ? 164.553 193.067 183.845 1.00 40.65  ? 2230 LYS A CB    1 
ATOM   6178  C  CG    . LYS A 1 2230 ? 165.012 192.061 184.884 1.00 50.92  ? 2230 LYS A CG    1 
ATOM   6179  C  CD    . LYS A 1 2230 ? 164.863 190.638 184.383 1.00 36.61  ? 2230 LYS A CD    1 
ATOM   6180  C  CE    . LYS A 1 2230 ? 163.405 190.280 184.176 1.00 30.80  ? 2230 LYS A CE    1 
ATOM   6181  N  NZ    . LYS A 1 2230 ? 163.247 189.127 183.254 1.00 45.64  ? 2230 LYS A NZ    1 
ATOM   6182  N  N     . SER A 1 2231 ? 162.852 195.306 182.573 1.00 53.83  ? 2231 SER A N     1 
ATOM   6183  C  CA    . SER A 1 2231 ? 162.577 196.209 181.460 1.00 47.60  ? 2231 SER A CA    1 
ATOM   6184  C  C     . SER A 1 2231 ? 162.461 197.646 181.943 1.00 51.09  ? 2231 SER A C     1 
ATOM   6185  O  O     . SER A 1 2231 ? 163.061 198.560 181.363 1.00 62.07  ? 2231 SER A O     1 
ATOM   6186  C  CB    . SER A 1 2231 ? 161.296 195.784 180.741 1.00 47.61  ? 2231 SER A CB    1 
ATOM   6187  O  OG    . SER A 1 2231 ? 161.409 194.475 180.214 1.00 53.80  ? 2231 SER A OG    1 
ATOM   6188  N  N     . MET A 1 2232 ? 161.697 197.862 183.014 1.00 46.03  ? 2232 MET A N     1 
ATOM   6189  C  CA    . MET A 1 2232 ? 161.559 199.205 183.562 1.00 48.25  ? 2232 MET A CA    1 
ATOM   6190  C  C     . MET A 1 2232 ? 162.893 199.727 184.070 1.00 55.96  ? 2232 MET A C     1 
ATOM   6191  O  O     . MET A 1 2232 ? 163.209 200.907 183.896 1.00 63.72  ? 2232 MET A O     1 
ATOM   6192  C  CB    . MET A 1 2232 ? 160.513 199.216 184.674 1.00 40.59  ? 2232 MET A CB    1 
ATOM   6193  C  CG    . MET A 1 2232 ? 159.087 199.297 184.163 1.00 56.31  ? 2232 MET A CG    1 
ATOM   6194  S  SD    . MET A 1 2232 ? 158.892 200.522 182.857 1.00 66.32  ? 2232 MET A SD    1 
ATOM   6195  C  CE    . MET A 1 2232 ? 157.116 200.505 182.641 1.00 61.18  ? 2232 MET A CE    1 
ATOM   6196  N  N     . ALA A 1 2233 ? 163.697 198.859 184.690 1.00 57.03  ? 2233 ALA A N     1 
ATOM   6197  C  CA    . ALA A 1 2233 ? 165.000 199.286 185.189 1.00 58.38  ? 2233 ALA A CA    1 
ATOM   6198  C  C     . ALA A 1 2233 ? 165.868 199.827 184.062 1.00 53.31  ? 2233 ALA A C     1 
ATOM   6199  O  O     . ALA A 1 2233 ? 166.388 200.947 184.149 1.00 62.51  ? 2233 ALA A O     1 
ATOM   6200  C  CB    . ALA A 1 2233 ? 165.704 198.128 185.896 1.00 49.52  ? 2233 ALA A CB    1 
ATOM   6201  N  N     . TRP A 1 2234 ? 166.023 199.058 182.981 1.00 46.94  ? 2234 TRP A N     1 
ATOM   6202  C  CA    . TRP A 1 2234 ? 166.934 199.517 181.938 1.00 50.32  ? 2234 TRP A CA    1 
ATOM   6203  C  C     . TRP A 1 2234 ? 166.337 200.664 181.128 1.00 60.27  ? 2234 TRP A C     1 
ATOM   6204  O  O     . TRP A 1 2234 ? 167.080 201.547 180.686 1.00 66.06  ? 2234 TRP A O     1 
ATOM   6205  C  CB    . TRP A 1 2234 ? 167.370 198.354 181.039 1.00 46.74  ? 2234 TRP A CB    1 
ATOM   6206  C  CG    . TRP A 1 2234 ? 166.384 197.881 180.020 1.00 49.70  ? 2234 TRP A CG    1 
ATOM   6207  C  CD1   . TRP A 1 2234 ? 165.575 196.791 180.115 1.00 57.88  ? 2234 TRP A CD1   1 
ATOM   6208  C  CD2   . TRP A 1 2234 ? 166.142 198.447 178.727 1.00 55.65  ? 2234 TRP A CD2   1 
ATOM   6209  N  NE1   . TRP A 1 2234 ? 164.822 196.656 178.975 1.00 51.87  ? 2234 TRP A NE1   1 
ATOM   6210  C  CE2   . TRP A 1 2234 ? 165.154 197.661 178.106 1.00 54.51  ? 2234 TRP A CE2   1 
ATOM   6211  C  CE3   . TRP A 1 2234 ? 166.656 199.549 178.040 1.00 54.42  ? 2234 TRP A CE3   1 
ATOM   6212  C  CZ2   . TRP A 1 2234 ? 164.668 197.941 176.833 1.00 53.31  ? 2234 TRP A CZ2   1 
ATOM   6213  C  CZ3   . TRP A 1 2234 ? 166.173 199.826 176.778 1.00 50.81  ? 2234 TRP A CZ3   1 
ATOM   6214  C  CH2   . TRP A 1 2234 ? 165.190 199.026 176.187 1.00 47.27  ? 2234 TRP A CH2   1 
ATOM   6215  N  N     . ARG A 1 2235 ? 165.011 200.706 180.957 1.00 54.62  ? 2235 ARG A N     1 
ATOM   6216  C  CA    . ARG A 1 2235 ? 164.401 201.851 180.285 1.00 49.08  ? 2235 ARG A CA    1 
ATOM   6217  C  C     . ARG A 1 2235 ? 164.603 203.133 181.086 1.00 58.84  ? 2235 ARG A C     1 
ATOM   6218  O  O     . ARG A 1 2235 ? 164.961 204.179 180.528 1.00 70.38  ? 2235 ARG A O     1 
ATOM   6219  C  CB    . ARG A 1 2235 ? 162.911 201.599 180.058 1.00 51.52  ? 2235 ARG A CB    1 
ATOM   6220  C  CG    . ARG A 1 2235 ? 162.587 200.618 178.947 1.00 54.54  ? 2235 ARG A CG    1 
ATOM   6221  C  CD    . ARG A 1 2235 ? 161.087 200.571 178.709 1.00 59.17  ? 2235 ARG A CD    1 
ATOM   6222  N  NE    . ARG A 1 2235 ? 160.688 199.443 177.877 1.00 62.03  ? 2235 ARG A NE    1 
ATOM   6223  C  CZ    . ARG A 1 2235 ? 160.746 199.433 176.553 1.00 70.42  ? 2235 ARG A CZ    1 
ATOM   6224  N  NH1   . ARG A 1 2235 ? 161.188 200.477 175.872 1.00 62.26  ? 2235 ARG A NH1   1 
ATOM   6225  N  NH2   . ARG A 1 2235 ? 160.346 198.348 175.895 1.00 66.38  ? 2235 ARG A NH2   1 
ATOM   6226  N  N     . VAL A 1 2236 ? 164.373 203.070 182.400 1.00 55.42  ? 2236 VAL A N     1 
ATOM   6227  C  CA    . VAL A 1 2236 ? 164.549 204.239 183.251 1.00 50.03  ? 2236 VAL A CA    1 
ATOM   6228  C  C     . VAL A 1 2236 ? 166.006 204.672 183.264 1.00 57.17  ? 2236 VAL A C     1 
ATOM   6229  O  O     . VAL A 1 2236 ? 166.310 205.869 183.214 1.00 65.12  ? 2236 VAL A O     1 
ATOM   6230  C  CB    . VAL A 1 2236 ? 164.024 203.943 184.668 1.00 45.01  ? 2236 VAL A CB    1 
ATOM   6231  C  CG1   . VAL A 1 2236 ? 164.665 204.864 185.686 1.00 53.75  ? 2236 VAL A CG1   1 
ATOM   6232  C  CG2   . VAL A 1 2236 ? 162.513 204.077 184.707 1.00 58.77  ? 2236 VAL A CG2   1 
ATOM   6233  N  N     . LEU A 1 2237 ? 166.932 203.710 183.320 1.00 57.10  ? 2237 LEU A N     1 
ATOM   6234  C  CA    . LEU A 1 2237 ? 168.348 204.057 183.271 1.00 53.65  ? 2237 LEU A CA    1 
ATOM   6235  C  C     . LEU A 1 2237 ? 168.705 204.741 181.958 1.00 56.85  ? 2237 LEU A C     1 
ATOM   6236  O  O     . LEU A 1 2237 ? 169.445 205.731 181.949 1.00 68.51  ? 2237 LEU A O     1 
ATOM   6237  C  CB    . LEU A 1 2237 ? 169.203 202.808 183.472 1.00 51.87  ? 2237 LEU A CB    1 
ATOM   6238  C  CG    . LEU A 1 2237 ? 170.710 203.052 183.459 1.00 48.70  ? 2237 LEU A CG    1 
ATOM   6239  C  CD1   . LEU A 1 2237 ? 171.103 204.009 184.569 1.00 54.55  ? 2237 LEU A CD1   1 
ATOM   6240  C  CD2   . LEU A 1 2237 ? 171.461 201.741 183.583 1.00 55.42  ? 2237 LEU A CD2   1 
ATOM   6241  N  N     . LEU A 1 2238 ? 168.186 204.231 180.838 1.00 54.10  ? 2238 LEU A N     1 
ATOM   6242  C  CA    . LEU A 1 2238 ? 168.477 204.839 179.544 1.00 53.11  ? 2238 LEU A CA    1 
ATOM   6243  C  C     . LEU A 1 2238 ? 167.955 206.269 179.477 1.00 58.92  ? 2238 LEU A C     1 
ATOM   6244  O  O     . LEU A 1 2238 ? 168.667 207.183 179.042 1.00 66.31  ? 2238 LEU A O     1 
ATOM   6245  C  CB    . LEU A 1 2238 ? 167.875 203.992 178.424 1.00 57.22  ? 2238 LEU A CB    1 
ATOM   6246  C  CG    . LEU A 1 2238 ? 168.198 204.422 176.993 1.00 57.57  ? 2238 LEU A CG    1 
ATOM   6247  C  CD1   . LEU A 1 2238 ? 169.696 204.531 176.792 1.00 59.98  ? 2238 LEU A CD1   1 
ATOM   6248  C  CD2   . LEU A 1 2238 ? 167.592 203.450 175.995 1.00 62.88  ? 2238 LEU A CD2   1 
ATOM   6249  N  N     . LYS A 1 2239 ? 166.710 206.485 179.909 1.00 68.06  ? 2239 LYS A N     1 
ATOM   6250  C  CA    . LYS A 1 2239 ? 166.148 207.833 179.862 1.00 62.12  ? 2239 LYS A CA    1 
ATOM   6251  C  C     . LYS A 1 2239 ? 166.891 208.781 180.796 1.00 65.10  ? 2239 LYS A C     1 
ATOM   6252  O  O     . LYS A 1 2239 ? 167.141 209.941 180.442 1.00 72.89  ? 2239 LYS A O     1 
ATOM   6253  C  CB    . LYS A 1 2239 ? 164.657 207.803 180.195 1.00 64.04  ? 2239 LYS A CB    1 
ATOM   6254  C  CG    . LYS A 1 2239 ? 163.847 206.864 179.317 1.00 71.95  ? 2239 LYS A CG    1 
ATOM   6255  C  CD    . LYS A 1 2239 ? 162.357 206.992 179.586 1.00 69.45  ? 2239 LYS A CD    1 
ATOM   6256  C  CE    . LYS A 1 2239 ? 161.936 208.448 179.696 1.00 67.65  ? 2239 LYS A CE    1 
ATOM   6257  N  NZ    . LYS A 1 2239 ? 160.463 208.610 179.564 1.00 70.98  ? 2239 LYS A NZ    1 
ATOM   6258  N  N     . ALA A 1 2240 ? 167.253 208.311 181.993 1.00 55.95  ? 2240 ALA A N     1 
ATOM   6259  C  CA    . ALA A 1 2240 ? 167.995 209.154 182.923 1.00 57.54  ? 2240 ALA A CA    1 
ATOM   6260  C  C     . ALA A 1 2240 ? 169.362 209.524 182.367 1.00 63.20  ? 2240 ALA A C     1 
ATOM   6261  O  O     . ALA A 1 2240 ? 169.790 210.677 182.482 1.00 66.72  ? 2240 ALA A O     1 
ATOM   6262  C  CB    . ALA A 1 2240 ? 168.137 208.450 184.270 1.00 59.88  ? 2240 ALA A CB    1 
ATOM   6263  N  N     . LEU A 1 2241 ? 170.063 208.563 181.760 1.00 72.01  ? 2241 LEU A N     1 
ATOM   6264  C  CA    . LEU A 1 2241 ? 171.357 208.869 181.161 1.00 66.77  ? 2241 LEU A CA    1 
ATOM   6265  C  C     . LEU A 1 2241 ? 171.209 209.852 180.008 1.00 69.72  ? 2241 LEU A C     1 
ATOM   6266  O  O     . LEU A 1 2241 ? 172.033 210.760 179.847 1.00 78.16  ? 2241 LEU A O     1 
ATOM   6267  C  CB    . LEU A 1 2241 ? 172.035 207.583 180.690 1.00 65.87  ? 2241 LEU A CB    1 
ATOM   6268  C  CG    . LEU A 1 2241 ? 172.561 206.667 181.795 1.00 67.44  ? 2241 LEU A CG    1 
ATOM   6269  C  CD1   . LEU A 1 2241 ? 173.369 205.527 181.204 1.00 68.25  ? 2241 LEU A CD1   1 
ATOM   6270  C  CD2   . LEU A 1 2241 ? 173.389 207.456 182.792 1.00 73.50  ? 2241 LEU A CD2   1 
ATOM   6271  N  N     . GLU A 1 2242 ? 170.160 209.690 179.198 1.00 83.44  ? 2242 GLU A N     1 
ATOM   6272  C  CA    . GLU A 1 2242 ? 169.918 210.627 178.106 1.00 86.40  ? 2242 GLU A CA    1 
ATOM   6273  C  C     . GLU A 1 2242 ? 169.680 212.037 178.629 1.00 89.13  ? 2242 GLU A C     1 
ATOM   6274  O  O     . GLU A 1 2242 ? 170.206 213.010 178.077 1.00 87.75  ? 2242 GLU A O     1 
ATOM   6275  C  CB    . GLU A 1 2242 ? 168.727 210.162 177.268 1.00 87.93  ? 2242 GLU A CB    1 
ATOM   6276  C  CG    . GLU A 1 2242 ? 168.183 211.221 176.323 1.00 89.36  ? 2242 GLU A CG    1 
ATOM   6277  C  CD    . GLU A 1 2242 ? 167.081 210.693 175.426 1.00 93.16  ? 2242 GLU A CD    1 
ATOM   6278  O  OE1   . GLU A 1 2242 ? 166.677 209.524 175.601 1.00 91.67  ? 2242 GLU A OE1   1 
ATOM   6279  O  OE2   . GLU A 1 2242 ? 166.618 211.448 174.546 1.00 92.85  ? 2242 GLU A OE2   1 
ATOM   6280  N  N     . ARG A 1 2243 ? 168.892 212.168 179.699 1.00 82.04  ? 2243 ARG A N     1 
ATOM   6281  C  CA    . ARG A 1 2243 ? 168.564 213.500 180.198 1.00 80.55  ? 2243 ARG A CA    1 
ATOM   6282  C  C     . ARG A 1 2243 ? 169.682 214.080 181.057 1.00 76.36  ? 2243 ARG A C     1 
ATOM   6283  O  O     . ARG A 1 2243 ? 169.693 215.288 181.320 1.00 80.03  ? 2243 ARG A O     1 
ATOM   6284  C  CB    . ARG A 1 2243 ? 167.251 213.459 180.980 1.00 74.04  ? 2243 ARG A CB    1 
ATOM   6285  C  CG    . ARG A 1 2243 ? 167.410 213.274 182.478 1.00 74.55  ? 2243 ARG A CG    1 
ATOM   6286  C  CD    . ARG A 1 2243 ? 166.058 213.246 183.174 1.00 74.06  ? 2243 ARG A CD    1 
ATOM   6287  N  NE    . ARG A 1 2243 ? 165.141 214.246 182.640 1.00 77.80  ? 2243 ARG A NE    1 
ATOM   6288  C  CZ    . ARG A 1 2243 ? 164.017 213.965 181.996 1.00 76.13  ? 2243 ARG A CZ    1 
ATOM   6289  N  NH1   . ARG A 1 2243 ? 163.637 212.716 181.781 1.00 72.45  ? 2243 ARG A NH1   1 
ATOM   6290  N  NH2   . ARG A 1 2243 ? 163.255 214.961 181.555 1.00 76.08  ? 2243 ARG A NH2   1 
ATOM   6291  N  N     . LEU A 1 2244 ? 170.628 213.251 181.499 1.00 71.18  ? 2244 LEU A N     1 
ATOM   6292  C  CA    . LEU A 1 2244 ? 171.729 213.734 182.327 1.00 74.97  ? 2244 LEU A CA    1 
ATOM   6293  C  C     . LEU A 1 2244 ? 172.962 214.077 181.495 1.00 84.95  ? 2244 LEU A C     1 
ATOM   6294  O  O     . LEU A 1 2244 ? 173.429 215.220 181.509 1.00 92.29  ? 2244 LEU A O     1 
ATOM   6295  C  CB    . LEU A 1 2244 ? 172.078 212.690 183.394 1.00 76.43  ? 2244 LEU A CB    1 
ATOM   6296  C  CG    . LEU A 1 2244 ? 173.383 212.919 184.157 1.00 74.78  ? 2244 LEU A CG    1 
ATOM   6297  C  CD1   . LEU A 1 2244 ? 173.183 213.948 185.255 1.00 76.17  ? 2244 LEU A CD1   1 
ATOM   6298  C  CD2   . LEU A 1 2244 ? 173.905 211.614 184.733 1.00 75.01  ? 2244 LEU A CD2   1 
ATOM   6299  N  N     . GLU A 1 2245 ? 173.501 213.097 180.765 1.00 92.58  ? 2245 GLU A N     1 
ATOM   6300  C  CA    . GLU A 1 2245 ? 174.718 213.325 179.997 1.00 87.13  ? 2245 GLU A CA    1 
ATOM   6301  C  C     . GLU A 1 2245 ? 174.472 214.112 178.718 1.00 91.37  ? 2245 GLU A C     1 
ATOM   6302  O  O     . GLU A 1 2245 ? 175.433 214.603 178.116 1.00 94.79  ? 2245 GLU A O     1 
ATOM   6303  C  CB    . GLU A 1 2245 ? 175.387 211.992 179.657 1.00 86.68  ? 2245 GLU A CB    1 
ATOM   6304  C  CG    . GLU A 1 2245 ? 175.808 211.180 180.868 1.00 91.52  ? 2245 GLU A CG    1 
ATOM   6305  C  CD    . GLU A 1 2245 ? 176.358 209.819 180.493 1.00 96.36  ? 2245 GLU A CD    1 
ATOM   6306  O  OE1   . GLU A 1 2245 ? 176.151 209.391 179.338 1.00 97.73  ? 2245 GLU A OE1   1 
ATOM   6307  O  OE2   . GLU A 1 2245 ? 177.001 209.178 181.350 1.00 94.11  ? 2245 GLU A OE2   1 
ATOM   6308  N  N     . GLY A 1 2246 ? 173.220 214.242 178.290 1.00 89.42  ? 2246 GLY A N     1 
ATOM   6309  C  CA    . GLY A 1 2246 ? 172.911 214.973 177.080 1.00 89.22  ? 2246 GLY A CA    1 
ATOM   6310  C  C     . GLY A 1 2246 ? 173.095 214.201 175.796 1.00 91.99  ? 2246 GLY A C     1 
ATOM   6311  O  O     . GLY A 1 2246 ? 172.885 214.767 174.717 1.00 96.44  ? 2246 GLY A O     1 
ATOM   6312  N  N     . VAL A 1 2247 ? 173.478 212.930 175.870 1.00 87.60  ? 2247 VAL A N     1 
ATOM   6313  C  CA    . VAL A 1 2247 ? 173.633 212.081 174.695 1.00 88.57  ? 2247 VAL A CA    1 
ATOM   6314  C  C     . VAL A 1 2247 ? 172.353 211.278 174.524 1.00 88.41  ? 2247 VAL A C     1 
ATOM   6315  O  O     . VAL A 1 2247 ? 171.936 210.555 175.437 1.00 85.03  ? 2247 VAL A O     1 
ATOM   6316  C  CB    . VAL A 1 2247 ? 174.857 211.160 174.820 1.00 84.97  ? 2247 VAL A CB    1 
ATOM   6317  C  CG1   . VAL A 1 2247 ? 176.118 211.902 174.411 1.00 86.86  ? 2247 VAL A CG1   1 
ATOM   6318  C  CG2   . VAL A 1 2247 ? 174.989 210.640 176.241 1.00 81.38  ? 2247 VAL A CG2   1 
ATOM   6319  N  N     . GLU A 1 2248 ? 171.721 211.417 173.361 1.00 91.09  ? 2248 GLU A N     1 
ATOM   6320  C  CA    . GLU A 1 2248 ? 170.474 210.713 173.099 1.00 90.88  ? 2248 GLU A CA    1 
ATOM   6321  C  C     . GLU A 1 2248 ? 170.692 209.208 173.150 1.00 92.29  ? 2248 GLU A C     1 
ATOM   6322  O  O     . GLU A 1 2248 ? 171.647 208.686 172.568 1.00 96.10  ? 2248 GLU A O     1 
ATOM   6323  C  CB    . GLU A 1 2248 ? 169.915 211.123 171.737 1.00 91.84  ? 2248 GLU A CB    1 
ATOM   6324  C  CG    . GLU A 1 2248 ? 168.793 210.233 171.233 1.00 93.91  ? 2248 GLU A CG    1 
ATOM   6325  C  CD    . GLU A 1 2248 ? 167.822 210.972 170.338 1.00 96.63  ? 2248 GLU A CD    1 
ATOM   6326  O  OE1   . GLU A 1 2248 ? 167.088 210.307 169.579 1.00 97.12  ? 2248 GLU A OE1   1 
ATOM   6327  O  OE2   . GLU A 1 2248 ? 167.794 212.220 170.393 1.00 99.32  ? 2248 GLU A OE2   1 
ATOM   6328  N  N     . GLY A 1 2249 ? 169.805 208.510 173.857 1.00 72.63  ? 2249 GLY A N     1 
ATOM   6329  C  CA    . GLY A 1 2249 ? 169.875 207.074 173.976 1.00 72.12  ? 2249 GLY A CA    1 
ATOM   6330  C  C     . GLY A 1 2249 ? 168.717 206.410 173.263 1.00 73.21  ? 2249 GLY A C     1 
ATOM   6331  O  O     . GLY A 1 2249 ? 167.552 206.699 173.546 1.00 79.67  ? 2249 GLY A O     1 
ATOM   6332  N  N     . VAL A 1 2250 ? 169.043 205.519 172.332 1.00 56.76  ? 2250 VAL A N     1 
ATOM   6333  C  CA    . VAL A 1 2250 ? 168.055 204.742 171.595 1.00 61.04  ? 2250 VAL A CA    1 
ATOM   6334  C  C     . VAL A 1 2250 ? 168.291 203.272 171.902 1.00 59.50  ? 2250 VAL A C     1 
ATOM   6335  O  O     . VAL A 1 2250 ? 169.410 202.877 172.251 1.00 67.97  ? 2250 VAL A O     1 
ATOM   6336  C  CB    . VAL A 1 2250 ? 168.123 205.011 170.081 1.00 61.86  ? 2250 VAL A CB    1 
ATOM   6337  C  CG1   . VAL A 1 2250 ? 168.239 206.501 169.815 1.00 67.22  ? 2250 VAL A CG1   1 
ATOM   6338  C  CG2   . VAL A 1 2250 ? 169.288 204.266 169.453 1.00 55.90  ? 2250 VAL A CG2   1 
ATOM   6339  N  N     . ALA A 1 2251 ? 167.238 202.470 171.794 1.00 58.90  ? 2251 ALA A N     1 
ATOM   6340  C  CA    . ALA A 1 2251 ? 167.296 201.052 172.114 1.00 57.84  ? 2251 ALA A CA    1 
ATOM   6341  C  C     . ALA A 1 2251 ? 166.616 200.251 171.016 1.00 63.11  ? 2251 ALA A C     1 
ATOM   6342  O  O     . ALA A 1 2251 ? 165.534 200.623 170.549 1.00 71.46  ? 2251 ALA A O     1 
ATOM   6343  C  CB    . ALA A 1 2251 ? 166.635 200.768 173.462 1.00 59.79  ? 2251 ALA A CB    1 
ATOM   6344  N  N     . HIS A 1 2252 ? 167.249 199.155 170.609 1.00 42.51  ? 2252 HIS A N     1 
ATOM   6345  C  CA    . HIS A 1 2252 ? 166.693 198.233 169.627 1.00 45.54  ? 2252 HIS A CA    1 
ATOM   6346  C  C     . HIS A 1 2252 ? 166.360 196.933 170.345 1.00 50.05  ? 2252 HIS A C     1 
ATOM   6347  O  O     . HIS A 1 2252 ? 167.255 196.135 170.644 1.00 58.74  ? 2252 HIS A O     1 
ATOM   6348  C  CB    . HIS A 1 2252 ? 167.672 197.997 168.480 1.00 53.35  ? 2252 HIS A CB    1 
ATOM   6349  C  CG    . HIS A 1 2252 ? 168.312 199.248 167.967 1.00 56.46  ? 2252 HIS A CG    1 
ATOM   6350  N  ND1   . HIS A 1 2252 ? 167.841 199.925 166.863 1.00 61.93  ? 2252 HIS A ND1   1 
ATOM   6351  C  CD2   . HIS A 1 2252 ? 169.388 199.944 168.405 1.00 58.22  ? 2252 HIS A CD2   1 
ATOM   6352  C  CE1   . HIS A 1 2252 ? 168.598 200.986 166.644 1.00 64.34  ? 2252 HIS A CE1   1 
ATOM   6353  N  NE2   . HIS A 1 2252 ? 169.543 201.021 167.565 1.00 61.11  ? 2252 HIS A NE2   1 
ATOM   6354  N  N     . ILE A 1 2253 ? 165.078 196.719 170.615 1.00 54.53  ? 2253 ILE A N     1 
ATOM   6355  C  CA    . ILE A 1 2253 ? 164.609 195.536 171.324 1.00 46.39  ? 2253 ILE A CA    1 
ATOM   6356  C  C     . ILE A 1 2253 ? 164.374 194.437 170.300 1.00 44.64  ? 2253 ILE A C     1 
ATOM   6357  O  O     . ILE A 1 2253 ? 163.540 194.582 169.398 1.00 61.64  ? 2253 ILE A O     1 
ATOM   6358  C  CB    . ILE A 1 2253 ? 163.333 195.831 172.126 1.00 47.14  ? 2253 ILE A CB    1 
ATOM   6359  C  CG1   . ILE A 1 2253 ? 163.676 196.610 173.394 1.00 54.89  ? 2253 ILE A CG1   1 
ATOM   6360  C  CG2   . ILE A 1 2253 ? 162.621 194.541 172.480 1.00 55.57  ? 2253 ILE A CG2   1 
ATOM   6361  C  CD1   . ILE A 1 2253 ? 162.750 197.770 173.662 1.00 52.71  ? 2253 ILE A CD1   1 
ATOM   6362  N  N     . ILE A 1 2254 ? 165.113 193.340 170.433 1.00 42.29  ? 2254 ILE A N     1 
ATOM   6363  C  CA    . ILE A 1 2254 ? 165.053 192.223 169.500 1.00 50.31  ? 2254 ILE A CA    1 
ATOM   6364  C  C     . ILE A 1 2254 ? 164.644 190.977 170.270 1.00 55.27  ? 2254 ILE A C     1 
ATOM   6365  O  O     . ILE A 1 2254 ? 165.229 190.669 171.314 1.00 66.73  ? 2254 ILE A O     1 
ATOM   6366  C  CB    . ILE A 1 2254 ? 166.402 192.006 168.790 1.00 46.11  ? 2254 ILE A CB    1 
ATOM   6367  C  CG1   . ILE A 1 2254 ? 166.810 193.264 168.025 1.00 42.77  ? 2254 ILE A CG1   1 
ATOM   6368  C  CG2   . ILE A 1 2254 ? 166.326 190.817 167.850 1.00 53.92  ? 2254 ILE A CG2   1 
ATOM   6369  C  CD1   . ILE A 1 2254 ? 168.226 193.226 167.509 1.00 48.84  ? 2254 ILE A CD1   1 
ATOM   6370  N  N     . ASP A 1 2255 ? 163.635 190.273 169.763 1.00 55.47  ? 2255 ASP A N     1 
ATOM   6371  C  CA    . ASP A 1 2255 ? 163.276 188.973 170.313 1.00 55.89  ? 2255 ASP A CA    1 
ATOM   6372  C  C     . ASP A 1 2255 ? 164.015 187.901 169.523 1.00 60.86  ? 2255 ASP A C     1 
ATOM   6373  O  O     . ASP A 1 2255 ? 163.585 187.529 168.424 1.00 71.28  ? 2255 ASP A O     1 
ATOM   6374  C  CB    . ASP A 1 2255 ? 161.765 188.748 170.261 1.00 62.04  ? 2255 ASP A CB    1 
ATOM   6375  C  CG    . ASP A 1 2255 ? 161.284 187.776 171.320 1.00 71.20  ? 2255 ASP A CG    1 
ATOM   6376  O  OD1   . ASP A 1 2255 ? 161.937 186.728 171.508 1.00 70.81  ? 2255 ASP A OD1   1 
ATOM   6377  O  OD2   . ASP A 1 2255 ? 160.255 188.059 171.968 1.00 70.52  ? 2255 ASP A OD2   1 
ATOM   6378  N  N     . PRO A 1 2256 ? 165.134 187.392 170.046 1.00 47.09  ? 2256 PRO A N     1 
ATOM   6379  C  CA    . PRO A 1 2256 ? 165.977 186.489 169.248 1.00 49.96  ? 2256 PRO A CA    1 
ATOM   6380  C  C     . PRO A 1 2256 ? 165.300 185.191 168.851 1.00 57.55  ? 2256 PRO A C     1 
ATOM   6381  O  O     . PRO A 1 2256 ? 165.583 184.677 167.763 1.00 55.72  ? 2256 PRO A O     1 
ATOM   6382  C  CB    . PRO A 1 2256 ? 167.172 186.229 170.170 1.00 52.80  ? 2256 PRO A CB    1 
ATOM   6383  C  CG    . PRO A 1 2256 ? 166.610 186.396 171.540 1.00 49.98  ? 2256 PRO A CG    1 
ATOM   6384  C  CD    . PRO A 1 2256 ? 165.601 187.500 171.437 1.00 46.65  ? 2256 PRO A CD    1 
ATOM   6385  N  N     . LYS A 1 2257 ? 164.424 184.643 169.689 1.00 59.32  ? 2257 LYS A N     1 
ATOM   6386  C  CA    . LYS A 1 2257 ? 163.804 183.357 169.411 1.00 52.37  ? 2257 LYS A CA    1 
ATOM   6387  C  C     . LYS A 1 2257 ? 162.439 183.477 168.750 1.00 65.65  ? 2257 LYS A C     1 
ATOM   6388  O  O     . LYS A 1 2257 ? 161.820 182.449 168.455 1.00 73.05  ? 2257 LYS A O     1 
ATOM   6389  C  CB    . LYS A 1 2257 ? 163.685 182.541 170.702 1.00 59.83  ? 2257 LYS A CB    1 
ATOM   6390  C  CG    . LYS A 1 2257 ? 165.017 182.332 171.400 1.00 65.37  ? 2257 LYS A CG    1 
ATOM   6391  C  CD    . LYS A 1 2257 ? 165.670 181.041 170.946 1.00 58.35  ? 2257 LYS A CD    1 
ATOM   6392  C  CE    . LYS A 1 2257 ? 165.253 179.886 171.828 1.00 62.02  ? 2257 LYS A CE    1 
ATOM   6393  N  NZ    . LYS A 1 2257 ? 165.828 178.595 171.369 1.00 64.73  ? 2257 LYS A NZ    1 
ATOM   6394  N  N     . ALA A 1 2258 ? 161.955 184.695 168.510 1.00 59.33  ? 2258 ALA A N     1 
ATOM   6395  C  CA    . ALA A 1 2258 ? 160.735 184.884 167.739 1.00 52.15  ? 2258 ALA A CA    1 
ATOM   6396  C  C     . ALA A 1 2258 ? 160.979 184.823 166.239 1.00 54.07  ? 2258 ALA A C     1 
ATOM   6397  O  O     . ALA A 1 2258 ? 160.014 184.830 165.469 1.00 66.46  ? 2258 ALA A O     1 
ATOM   6398  C  CB    . ALA A 1 2258 ? 160.082 186.219 168.099 1.00 52.32  ? 2258 ALA A CB    1 
ATOM   6399  N  N     . ILE A 1 2259 ? 162.240 184.767 165.812 1.00 55.01  ? 2259 ILE A N     1 
ATOM   6400  C  CA    . ILE A 1 2259 ? 162.605 184.671 164.407 1.00 54.92  ? 2259 ILE A CA    1 
ATOM   6401  C  C     . ILE A 1 2259 ? 163.677 183.601 164.260 1.00 62.06  ? 2259 ILE A C     1 
ATOM   6402  O  O     . ILE A 1 2259 ? 164.364 183.240 165.218 1.00 71.69  ? 2259 ILE A O     1 
ATOM   6403  C  CB    . ILE A 1 2259 ? 163.111 186.014 163.842 1.00 52.08  ? 2259 ILE A CB    1 
ATOM   6404  C  CG1   . ILE A 1 2259 ? 164.217 186.574 164.736 1.00 49.14  ? 2259 ILE A CG1   1 
ATOM   6405  C  CG2   . ILE A 1 2259 ? 161.968 187.004 163.712 1.00 62.86  ? 2259 ILE A CG2   1 
ATOM   6406  C  CD1   . ILE A 1 2259 ? 164.612 187.988 164.402 1.00 56.35  ? 2259 ILE A CD1   1 
ATOM   6407  N  N     . SER A 1 2260 ? 163.813 183.093 163.039 1.00 69.89  ? 2260 SER A N     1 
ATOM   6408  C  CA    . SER A 1 2260 ? 164.843 182.106 162.762 1.00 67.13  ? 2260 SER A CA    1 
ATOM   6409  C  C     . SER A 1 2260 ? 166.224 182.751 162.817 1.00 69.70  ? 2260 SER A C     1 
ATOM   6410  O  O     . SER A 1 2260 ? 166.390 183.952 162.587 1.00 78.93  ? 2260 SER A O     1 
ATOM   6411  C  CB    . SER A 1 2260 ? 164.616 181.460 161.396 1.00 70.31  ? 2260 SER A CB    1 
ATOM   6412  O  OG    . SER A 1 2260 ? 164.786 182.404 160.355 1.00 75.40  ? 2260 SER A OG    1 
ATOM   6413  N  N     . LYS A 1 2261 ? 167.227 181.930 163.137 1.00 66.44  ? 2261 LYS A N     1 
ATOM   6414  C  CA    . LYS A 1 2261 ? 168.590 182.437 163.254 1.00 63.73  ? 2261 LYS A CA    1 
ATOM   6415  C  C     . LYS A 1 2261 ? 169.096 182.989 161.927 1.00 64.31  ? 2261 LYS A C     1 
ATOM   6416  O  O     . LYS A 1 2261 ? 169.880 183.947 161.910 1.00 73.03  ? 2261 LYS A O     1 
ATOM   6417  C  CB    . LYS A 1 2261 ? 169.512 181.333 163.775 1.00 65.25  ? 2261 LYS A CB    1 
ATOM   6418  C  CG    . LYS A 1 2261 ? 170.979 181.714 163.857 1.00 64.65  ? 2261 LYS A CG    1 
ATOM   6419  C  CD    . LYS A 1 2261 ? 171.849 180.484 164.042 1.00 66.32  ? 2261 LYS A CD    1 
ATOM   6420  C  CE    . LYS A 1 2261 ? 173.326 180.839 164.029 1.00 68.47  ? 2261 LYS A CE    1 
ATOM   6421  N  NZ    . LYS A 1 2261 ? 173.797 181.193 162.663 1.00 67.75  ? 2261 LYS A NZ    1 
ATOM   6422  N  N     . ASP A 1 2262 ? 168.651 182.410 160.809 1.00 64.01  ? 2262 ASP A N     1 
ATOM   6423  C  CA    . ASP A 1 2262 ? 168.998 182.959 159.503 1.00 64.68  ? 2262 ASP A CA    1 
ATOM   6424  C  C     . ASP A 1 2262 ? 168.458 184.374 159.344 1.00 71.02  ? 2262 ASP A C     1 
ATOM   6425  O  O     . ASP A 1 2262 ? 169.127 185.242 158.774 1.00 78.72  ? 2262 ASP A O     1 
ATOM   6426  C  CB    . ASP A 1 2262 ? 168.468 182.055 158.391 1.00 68.70  ? 2262 ASP A CB    1 
ATOM   6427  C  CG    . ASP A 1 2262 ? 168.502 180.587 158.766 1.00 83.22  ? 2262 ASP A CG    1 
ATOM   6428  O  OD1   . ASP A 1 2262 ? 167.422 179.964 158.835 1.00 83.01  ? 2262 ASP A OD1   1 
ATOM   6429  O  OD2   . ASP A 1 2262 ? 169.610 180.055 158.990 1.00 88.28  ? 2262 ASP A OD2   1 
ATOM   6430  N  N     . HIS A 1 2263 ? 167.243 184.624 159.833 1.00 64.38  ? 2263 HIS A N     1 
ATOM   6431  C  CA    . HIS A 1 2263 ? 166.690 185.971 159.831 1.00 60.99  ? 2263 HIS A CA    1 
ATOM   6432  C  C     . HIS A 1 2263 ? 167.317 186.868 160.889 1.00 65.05  ? 2263 HIS A C     1 
ATOM   6433  O  O     . HIS A 1 2263 ? 167.267 188.094 160.744 1.00 69.85  ? 2263 HIS A O     1 
ATOM   6434  C  CB    . HIS A 1 2263 ? 165.175 185.924 160.042 1.00 57.85  ? 2263 HIS A CB    1 
ATOM   6435  C  CG    . HIS A 1 2263 ? 164.419 185.368 158.876 1.00 62.59  ? 2263 HIS A CG    1 
ATOM   6436  N  ND1   . HIS A 1 2263 ? 164.798 185.589 157.570 1.00 69.97  ? 2263 HIS A ND1   1 
ATOM   6437  C  CD2   . HIS A 1 2263 ? 163.301 184.606 158.820 1.00 65.62  ? 2263 HIS A CD2   1 
ATOM   6438  C  CE1   . HIS A 1 2263 ? 163.950 184.982 156.759 1.00 66.96  ? 2263 HIS A CE1   1 
ATOM   6439  N  NE2   . HIS A 1 2263 ? 163.032 184.379 157.492 1.00 71.05  ? 2263 HIS A NE2   1 
ATOM   6440  N  N     . LEU A 1 2264 ? 167.900 186.294 161.940 1.00 55.66  ? 2264 LEU A N     1 
ATOM   6441  C  CA    . LEU A 1 2264 ? 168.467 187.086 163.024 1.00 50.73  ? 2264 LEU A CA    1 
ATOM   6442  C  C     . LEU A 1 2264 ? 169.870 187.588 162.708 1.00 57.66  ? 2264 LEU A C     1 
ATOM   6443  O  O     . LEU A 1 2264 ? 170.179 188.755 162.970 1.00 67.62  ? 2264 LEU A O     1 
ATOM   6444  C  CB    . LEU A 1 2264 ? 168.484 186.268 164.318 1.00 53.70  ? 2264 LEU A CB    1 
ATOM   6445  C  CG    . LEU A 1 2264 ? 169.260 186.859 165.496 1.00 54.32  ? 2264 LEU A CG    1 
ATOM   6446  C  CD1   . LEU A 1 2264 ? 168.629 188.161 165.951 1.00 54.02  ? 2264 LEU A CD1   1 
ATOM   6447  C  CD2   . LEU A 1 2264 ? 169.321 185.867 166.644 1.00 57.62  ? 2264 LEU A CD2   1 
ATOM   6448  N  N     . TYR A 1 2265 ? 170.728 186.737 162.146 1.00 55.90  ? 2265 TYR A N     1 
ATOM   6449  C  CA    . TYR A 1 2265 ? 172.092 187.132 161.818 1.00 51.52  ? 2265 TYR A CA    1 
ATOM   6450  C  C     . TYR A 1 2265 ? 172.349 187.306 160.332 1.00 56.09  ? 2265 TYR A C     1 
ATOM   6451  O  O     . TYR A 1 2265 ? 173.225 188.087 159.960 1.00 59.45  ? 2265 TYR A O     1 
ATOM   6452  C  CB    . TYR A 1 2265 ? 173.096 186.113 162.371 1.00 49.86  ? 2265 TYR A CB    1 
ATOM   6453  C  CG    . TYR A 1 2265 ? 173.163 186.078 163.877 1.00 49.54  ? 2265 TYR A CG    1 
ATOM   6454  C  CD1   . TYR A 1 2265 ? 173.465 187.222 164.600 1.00 47.71  ? 2265 TYR A CD1   1 
ATOM   6455  C  CD2   . TYR A 1 2265 ? 172.934 184.903 164.575 1.00 60.69  ? 2265 TYR A CD2   1 
ATOM   6456  C  CE1   . TYR A 1 2265 ? 173.531 187.198 165.975 1.00 61.07  ? 2265 TYR A CE1   1 
ATOM   6457  C  CE2   . TYR A 1 2265 ? 172.998 184.869 165.952 1.00 56.45  ? 2265 TYR A CE2   1 
ATOM   6458  C  CZ    . TYR A 1 2265 ? 173.296 186.019 166.646 1.00 64.07  ? 2265 TYR A CZ    1 
ATOM   6459  O  OH    . TYR A 1 2265 ? 173.362 185.992 168.018 1.00 71.69  ? 2265 TYR A OH    1 
ATOM   6460  N  N     . GLY A 1 2266 ? 171.620 186.602 159.477 1.00 70.21  ? 2266 GLY A N     1 
ATOM   6461  C  CA    . GLY A 1 2266 ? 171.827 186.665 158.045 1.00 66.32  ? 2266 GLY A CA    1 
ATOM   6462  C  C     . GLY A 1 2266 ? 171.943 185.282 157.437 1.00 65.25  ? 2266 GLY A C     1 
ATOM   6463  O  O     . GLY A 1 2266 ? 172.096 184.274 158.123 1.00 73.95  ? 2266 GLY A O     1 
ATOM   6464  N  N     . THR A 1 2267 ? 171.865 185.260 156.110 1.00 74.41  ? 2267 THR A N     1 
ATOM   6465  C  CA    . THR A 1 2267 ? 171.938 184.018 155.354 1.00 80.63  ? 2267 THR A CA    1 
ATOM   6466  C  C     . THR A 1 2267 ? 172.884 184.195 154.177 1.00 82.19  ? 2267 THR A C     1 
ATOM   6467  O  O     . THR A 1 2267 ? 173.084 185.314 153.694 1.00 86.64  ? 2267 THR A O     1 
ATOM   6468  C  CB    . THR A 1 2267 ? 170.549 183.575 154.870 1.00 88.32  ? 2267 THR A CB    1 
ATOM   6469  O  OG1   . THR A 1 2267 ? 170.530 182.151 154.712 1.00 85.08  ? 2267 THR A OG1   1 
ATOM   6470  C  CG2   . THR A 1 2267 ? 170.189 184.234 153.545 1.00 85.46  ? 2267 THR A CG2   1 
ATOM   6471  N  N     . LEU A 1 2268 ? 173.485 183.092 153.745 1.00 88.87  ? 2268 LEU A N     1 
ATOM   6472  C  CA    . LEU A 1 2268 ? 174.348 183.062 152.573 1.00 85.09  ? 2268 LEU A CA    1 
ATOM   6473  C  C     . LEU A 1 2268 ? 173.735 182.104 151.561 1.00 94.29  ? 2268 LEU A C     1 
ATOM   6474  O  O     . LEU A 1 2268 ? 173.577 180.913 151.851 1.00 102.85 ? 2268 LEU A O     1 
ATOM   6475  C  CB    . LEU A 1 2268 ? 175.760 182.617 152.953 1.00 86.72  ? 2268 LEU A CB    1 
ATOM   6476  C  CG    . LEU A 1 2268 ? 176.937 183.140 152.129 1.00 89.93  ? 2268 LEU A CG    1 
ATOM   6477  C  CD1   . LEU A 1 2268 ? 176.796 184.627 151.871 1.00 94.37  ? 2268 LEU A CD1   1 
ATOM   6478  C  CD2   . LEU A 1 2268 ? 178.251 182.838 152.828 1.00 88.16  ? 2268 LEU A CD2   1 
ATOM   6479  N  N     . ASP A 1 2269 ? 173.387 182.616 150.389 1.00 103.04 ? 2269 ASP A N     1 
ATOM   6480  C  CA    . ASP A 1 2269 ? 172.758 181.774 149.378 1.00 101.54 ? 2269 ASP A CA    1 
ATOM   6481  C  C     . ASP A 1 2269 ? 173.752 180.733 148.883 1.00 103.94 ? 2269 ASP A C     1 
ATOM   6482  O  O     . ASP A 1 2269 ? 174.836 181.100 148.411 1.00 106.71 ? 2269 ASP A O     1 
ATOM   6483  C  CB    . ASP A 1 2269 ? 172.242 182.612 148.211 1.00 101.66 ? 2269 ASP A CB    1 
ATOM   6484  C  CG    . ASP A 1 2269 ? 171.723 183.966 148.646 1.00 108.88 ? 2269 ASP A CG    1 
ATOM   6485  O  OD1   . ASP A 1 2269 ? 172.384 184.981 148.347 1.00 110.14 ? 2269 ASP A OD1   1 
ATOM   6486  O  OD2   . ASP A 1 2269 ? 170.651 184.016 149.285 1.00 108.53 ? 2269 ASP A OD2   1 
ATOM   6487  N  N     . PRO A 1 2270 ? 173.437 179.440 148.972 1.00 111.00 ? 2270 PRO A N     1 
ATOM   6488  C  CA    . PRO A 1 2270 ? 174.384 178.420 148.496 1.00 114.01 ? 2270 PRO A CA    1 
ATOM   6489  C  C     . PRO A 1 2270 ? 174.647 178.488 147.005 1.00 115.82 ? 2270 PRO A C     1 
ATOM   6490  O  O     . PRO A 1 2270 ? 175.658 177.944 146.544 1.00 114.23 ? 2270 PRO A O     1 
ATOM   6491  C  CB    . PRO A 1 2270 ? 173.705 177.099 148.886 1.00 111.24 ? 2270 PRO A CB    1 
ATOM   6492  C  CG    . PRO A 1 2270 ? 172.255 177.439 149.014 1.00 107.25 ? 2270 PRO A CG    1 
ATOM   6493  C  CD    . PRO A 1 2270 ? 172.207 178.846 149.523 1.00 107.78 ? 2270 PRO A CD    1 
ATOM   6494  N  N     . ASN A 1 2271 ? 173.774 179.136 146.235 1.00 122.26 ? 2271 ASN A N     1 
ATOM   6495  C  CA    . ASN A 1 2271 ? 173.912 179.184 144.784 1.00 121.62 ? 2271 ASN A CA    1 
ATOM   6496  C  C     . ASN A 1 2271 ? 174.807 180.340 144.340 1.00 120.98 ? 2271 ASN A C     1 
ATOM   6497  O  O     . ASN A 1 2271 ? 175.827 180.124 143.679 1.00 119.97 ? 2271 ASN A O     1 
ATOM   6498  C  CB    . ASN A 1 2271 ? 172.526 179.288 144.136 1.00 119.43 ? 2271 ASN A CB    1 
ATOM   6499  C  CG    . ASN A 1 2271 ? 172.593 179.571 142.646 1.00 123.02 ? 2271 ASN A CG    1 
ATOM   6500  O  OD1   . ASN A 1 2271 ? 173.540 179.175 141.966 1.00 125.35 ? 2271 ASN A OD1   1 
ATOM   6501  N  ND2   . ASN A 1 2271 ? 171.583 180.261 142.132 1.00 122.07 ? 2271 ASN A ND2   1 
ATOM   6502  N  N     . THR A 1 2272 ? 174.438 181.568 144.696 1.00 110.36 ? 2272 THR A N     1 
ATOM   6503  C  CA    . THR A 1 2272 ? 175.136 182.753 144.213 1.00 109.44 ? 2272 THR A CA    1 
ATOM   6504  C  C     . THR A 1 2272 ? 176.124 183.331 145.218 1.00 111.55 ? 2272 THR A C     1 
ATOM   6505  O  O     . THR A 1 2272 ? 176.836 184.282 144.878 1.00 111.58 ? 2272 THR A O     1 
ATOM   6506  C  CB    . THR A 1 2272 ? 174.125 183.833 143.815 1.00 108.82 ? 2272 THR A CB    1 
ATOM   6507  O  OG1   . THR A 1 2272 ? 174.823 185.018 143.411 1.00 111.90 ? 2272 THR A OG1   1 
ATOM   6508  C  CG2   . THR A 1 2272 ? 173.210 184.162 144.982 1.00 107.19 ? 2272 THR A CG2   1 
ATOM   6509  N  N     . ARG A 1 2273 ? 176.190 182.783 146.434 1.00 104.72 ? 2273 ARG A N     1 
ATOM   6510  C  CA    . ARG A 1 2273 ? 177.136 183.233 147.459 1.00 100.20 ? 2273 ARG A CA    1 
ATOM   6511  C  C     . ARG A 1 2273 ? 177.018 184.733 147.721 1.00 98.00  ? 2273 ARG A C     1 
ATOM   6512  O  O     . ARG A 1 2273 ? 178.015 185.456 147.768 1.00 97.61  ? 2273 ARG A O     1 
ATOM   6513  C  CB    . ARG A 1 2273 ? 178.572 182.856 147.088 1.00 98.86  ? 2273 ARG A CB    1 
ATOM   6514  C  CG    . ARG A 1 2273 ? 178.829 181.360 147.077 1.00 99.93  ? 2273 ARG A CG    1 
ATOM   6515  C  CD    . ARG A 1 2273 ? 179.027 180.830 148.488 1.00 98.27  ? 2273 ARG A CD    1 
ATOM   6516  N  NE    . ARG A 1 2273 ? 178.390 179.534 148.683 1.00 101.69 ? 2273 ARG A NE    1 
ATOM   6517  C  CZ    . ARG A 1 2273 ? 178.066 179.030 149.866 1.00 103.06 ? 2273 ARG A CZ    1 
ATOM   6518  N  NH1   . ARG A 1 2273 ? 178.310 179.689 150.988 1.00 101.32 ? 2273 ARG A NH1   1 
ATOM   6519  N  NH2   . ARG A 1 2273 ? 177.485 177.836 149.926 1.00 98.76  ? 2273 ARG A NH2   1 
ATOM   6520  N  N     . GLU A 1 2274 ? 175.787 185.205 147.892 1.00 101.63 ? 2274 GLU A N     1 
ATOM   6521  C  CA    . GLU A 1 2274 ? 175.512 186.597 148.215 1.00 99.74  ? 2274 GLU A CA    1 
ATOM   6522  C  C     . GLU A 1 2274 ? 175.014 186.697 149.651 1.00 98.60  ? 2274 GLU A C     1 
ATOM   6523  O  O     . GLU A 1 2274 ? 174.252 185.844 150.114 1.00 99.48  ? 2274 GLU A O     1 
ATOM   6524  C  CB    . GLU A 1 2274 ? 174.482 187.185 147.246 1.00 97.40  ? 2274 GLU A CB    1 
ATOM   6525  C  CG    . GLU A 1 2274 ? 173.611 188.283 147.833 1.00 98.66  ? 2274 GLU A CG    1 
ATOM   6526  C  CD    . GLU A 1 2274 ? 172.520 188.732 146.882 1.00 107.50 ? 2274 GLU A CD    1 
ATOM   6527  O  OE1   . GLU A 1 2274 ? 172.120 189.913 146.951 1.00 108.90 ? 2274 GLU A OE1   1 
ATOM   6528  O  OE2   . GLU A 1 2274 ? 172.063 187.904 146.067 1.00 106.47 ? 2274 GLU A OE2   1 
ATOM   6529  N  N     . TRP A 1 2275 ? 175.454 187.735 150.357 1.00 74.91  ? 2275 TRP A N     1 
ATOM   6530  C  CA    . TRP A 1 2275 ? 175.120 187.897 151.764 1.00 73.50  ? 2275 TRP A CA    1 
ATOM   6531  C  C     . TRP A 1 2275 ? 173.909 188.805 151.927 1.00 77.76  ? 2275 TRP A C     1 
ATOM   6532  O  O     . TRP A 1 2275 ? 173.876 189.914 151.384 1.00 83.71  ? 2275 TRP A O     1 
ATOM   6533  C  CB    . TRP A 1 2275 ? 176.306 188.464 152.542 1.00 67.33  ? 2275 TRP A CB    1 
ATOM   6534  C  CG    . TRP A 1 2275 ? 175.988 188.730 153.977 1.00 66.37  ? 2275 TRP A CG    1 
ATOM   6535  C  CD1   . TRP A 1 2275 ? 175.796 189.945 154.562 1.00 72.49  ? 2275 TRP A CD1   1 
ATOM   6536  C  CD2   . TRP A 1 2275 ? 175.807 187.755 155.009 1.00 70.80  ? 2275 TRP A CD2   1 
ATOM   6537  N  NE1   . TRP A 1 2275 ? 175.515 189.789 155.897 1.00 75.72  ? 2275 TRP A NE1   1 
ATOM   6538  C  CE2   . TRP A 1 2275 ? 175.516 188.452 156.196 1.00 72.67  ? 2275 TRP A CE2   1 
ATOM   6539  C  CE3   . TRP A 1 2275 ? 175.867 186.359 155.045 1.00 74.68  ? 2275 TRP A CE3   1 
ATOM   6540  C  CZ2   . TRP A 1 2275 ? 175.285 187.802 157.404 1.00 74.46  ? 2275 TRP A CZ2   1 
ATOM   6541  C  CZ3   . TRP A 1 2275 ? 175.637 185.717 156.244 1.00 72.74  ? 2275 TRP A CZ3   1 
ATOM   6542  C  CH2   . TRP A 1 2275 ? 175.350 186.438 157.408 1.00 74.85  ? 2275 TRP A CH2   1 
ATOM   6543  N  N     . THR A 1 2276 ? 172.919 188.328 152.676 1.00 80.60  ? 2276 THR A N     1 
ATOM   6544  C  CA    . THR A 1 2276 ? 171.742 189.106 153.039 1.00 74.68  ? 2276 THR A CA    1 
ATOM   6545  C  C     . THR A 1 2276 ? 171.772 189.340 154.543 1.00 78.43  ? 2276 THR A C     1 
ATOM   6546  O  O     . THR A 1 2276 ? 171.863 188.384 155.320 1.00 86.14  ? 2276 THR A O     1 
ATOM   6547  C  CB    . THR A 1 2276 ? 170.458 188.385 152.631 1.00 76.85  ? 2276 THR A CB    1 
ATOM   6548  O  OG1   . THR A 1 2276 ? 170.438 188.209 151.210 1.00 83.54  ? 2276 THR A OG1   1 
ATOM   6549  C  CG2   . THR A 1 2276 ? 169.239 189.187 153.055 1.00 82.63  ? 2276 THR A CG2   1 
ATOM   6550  N  N     . ASP A 1 2277 ? 171.698 190.605 154.948 1.00 71.92  ? 2277 ASP A N     1 
ATOM   6551  C  CA    . ASP A 1 2277 ? 171.800 190.946 156.359 1.00 69.35  ? 2277 ASP A CA    1 
ATOM   6552  C  C     . ASP A 1 2277 ? 170.612 190.407 157.145 1.00 75.27  ? 2277 ASP A C     1 
ATOM   6553  O  O     . ASP A 1 2277 ? 169.472 190.424 156.674 1.00 80.63  ? 2277 ASP A O     1 
ATOM   6554  C  CB    . ASP A 1 2277 ? 171.891 192.460 156.535 1.00 70.72  ? 2277 ASP A CB    1 
ATOM   6555  C  CG    . ASP A 1 2277 ? 173.273 192.999 156.235 1.00 80.55  ? 2277 ASP A CG    1 
ATOM   6556  O  OD1   . ASP A 1 2277 ? 173.443 194.236 156.229 1.00 80.01  ? 2277 ASP A OD1   1 
ATOM   6557  O  OD2   . ASP A 1 2277 ? 174.192 192.185 156.008 1.00 85.69  ? 2277 ASP A OD2   1 
ATOM   6558  N  N     . GLY A 1 2278 ? 170.887 189.927 158.353 1.00 68.23  ? 2278 GLY A N     1 
ATOM   6559  C  CA    . GLY A 1 2278 ? 169.847 189.527 159.276 1.00 66.89  ? 2278 GLY A CA    1 
ATOM   6560  C  C     . GLY A 1 2278 ? 169.267 190.734 159.981 1.00 64.71  ? 2278 GLY A C     1 
ATOM   6561  O  O     . GLY A 1 2278 ? 169.260 191.849 159.457 1.00 68.74  ? 2278 GLY A O     1 
ATOM   6562  N  N     . LEU A 1 2279 ? 168.771 190.505 161.197 1.00 57.00  ? 2279 LEU A N     1 
ATOM   6563  C  CA    . LEU A 1 2279 ? 168.223 191.606 161.981 1.00 55.31  ? 2279 LEU A CA    1 
ATOM   6564  C  C     . LEU A 1 2279 ? 169.310 192.282 162.810 1.00 56.91  ? 2279 LEU A C     1 
ATOM   6565  O  O     . LEU A 1 2279 ? 169.569 193.483 162.661 1.00 64.81  ? 2279 LEU A O     1 
ATOM   6566  C  CB    . LEU A 1 2279 ? 167.094 191.099 162.878 1.00 49.55  ? 2279 LEU A CB    1 
ATOM   6567  C  CG    . LEU A 1 2279 ? 166.326 192.171 163.648 1.00 52.63  ? 2279 LEU A CG    1 
ATOM   6568  C  CD1   . LEU A 1 2279 ? 165.990 193.341 162.743 1.00 65.95  ? 2279 LEU A CD1   1 
ATOM   6569  C  CD2   . LEU A 1 2279 ? 165.066 191.586 164.253 1.00 59.02  ? 2279 LEU A CD2   1 
ATOM   6570  N  N     . PHE A 1 2280 ? 169.961 191.518 163.692 1.00 51.47  ? 2280 PHE A N     1 
ATOM   6571  C  CA    . PHE A 1 2280 ? 171.013 192.089 164.525 1.00 45.24  ? 2280 PHE A CA    1 
ATOM   6572  C  C     . PHE A 1 2280 ? 172.185 192.563 163.680 1.00 52.74  ? 2280 PHE A C     1 
ATOM   6573  O  O     . PHE A 1 2280 ? 172.784 193.606 163.966 1.00 64.80  ? 2280 PHE A O     1 
ATOM   6574  C  CB    . PHE A 1 2280 ? 171.485 191.070 165.559 1.00 45.95  ? 2280 PHE A CB    1 
ATOM   6575  C  CG    . PHE A 1 2280 ? 172.744 191.475 166.267 1.00 55.36  ? 2280 PHE A CG    1 
ATOM   6576  C  CD1   . PHE A 1 2280 ? 172.742 192.532 167.159 1.00 58.34  ? 2280 PHE A CD1   1 
ATOM   6577  C  CD2   . PHE A 1 2280 ? 173.933 190.809 166.029 1.00 57.25  ? 2280 PHE A CD2   1 
ATOM   6578  C  CE1   . PHE A 1 2280 ? 173.899 192.910 167.809 1.00 56.28  ? 2280 PHE A CE1   1 
ATOM   6579  C  CE2   . PHE A 1 2280 ? 175.092 191.185 166.674 1.00 57.19  ? 2280 PHE A CE2   1 
ATOM   6580  C  CZ    . PHE A 1 2280 ? 175.075 192.236 167.566 1.00 51.33  ? 2280 PHE A CZ    1 
ATOM   6581  N  N     . THR A 1 2281 ? 172.537 191.801 162.642 1.00 55.77  ? 2281 THR A N     1 
ATOM   6582  C  CA    . THR A 1 2281 ? 173.609 192.226 161.749 1.00 46.92  ? 2281 THR A CA    1 
ATOM   6583  C  C     . THR A 1 2281 ? 173.261 193.539 161.064 1.00 58.41  ? 2281 THR A C     1 
ATOM   6584  O  O     . THR A 1 2281 ? 174.109 194.429 160.951 1.00 68.84  ? 2281 THR A O     1 
ATOM   6585  C  CB    . THR A 1 2281 ? 173.895 191.143 160.711 1.00 58.65  ? 2281 THR A CB    1 
ATOM   6586  O  OG1   . THR A 1 2281 ? 173.993 189.870 161.360 1.00 71.17  ? 2281 THR A OG1   1 
ATOM   6587  C  CG2   . THR A 1 2281 ? 175.195 191.435 159.986 1.00 64.08  ? 2281 THR A CG2   1 
ATOM   6588  N  N     . HIS A 1 2282 ? 172.015 193.680 160.604 1.00 59.74  ? 2282 HIS A N     1 
ATOM   6589  C  CA    . HIS A 1 2282 ? 171.600 194.927 159.968 1.00 58.55  ? 2282 HIS A CA    1 
ATOM   6590  C  C     . HIS A 1 2282 ? 171.660 196.093 160.944 1.00 62.59  ? 2282 HIS A C     1 
ATOM   6591  O  O     . HIS A 1 2282 ? 172.131 197.180 160.592 1.00 73.91  ? 2282 HIS A O     1 
ATOM   6592  C  CB    . HIS A 1 2282 ? 170.192 194.783 159.396 1.00 63.68  ? 2282 HIS A CB    1 
ATOM   6593  C  CG    . HIS A 1 2282 ? 169.512 196.089 159.126 1.00 64.94  ? 2282 HIS A CG    1 
ATOM   6594  N  ND1   . HIS A 1 2282 ? 169.826 196.883 158.045 1.00 67.55  ? 2282 HIS A ND1   1 
ATOM   6595  C  CD2   . HIS A 1 2282 ? 168.529 196.736 159.795 1.00 70.03  ? 2282 HIS A CD2   1 
ATOM   6596  C  CE1   . HIS A 1 2282 ? 169.069 197.965 158.061 1.00 65.35  ? 2282 HIS A CE1   1 
ATOM   6597  N  NE2   . HIS A 1 2282 ? 168.273 197.900 159.113 1.00 70.65  ? 2282 HIS A NE2   1 
ATOM   6598  N  N     . VAL A 1 2283 ? 171.190 195.887 162.177 1.00 54.63  ? 2283 VAL A N     1 
ATOM   6599  C  CA    . VAL A 1 2283 ? 171.210 196.963 163.166 1.00 50.36  ? 2283 VAL A CA    1 
ATOM   6600  C  C     . VAL A 1 2283 ? 172.645 197.379 163.470 1.00 60.67  ? 2283 VAL A C     1 
ATOM   6601  O  O     . VAL A 1 2283 ? 172.975 198.573 163.501 1.00 68.59  ? 2283 VAL A O     1 
ATOM   6602  C  CB    . VAL A 1 2283 ? 170.464 196.532 164.441 1.00 46.35  ? 2283 VAL A CB    1 
ATOM   6603  C  CG1   . VAL A 1 2283 ? 170.783 197.473 165.588 1.00 53.91  ? 2283 VAL A CG1   1 
ATOM   6604  C  CG2   . VAL A 1 2283 ? 168.969 196.486 164.188 1.00 57.15  ? 2283 VAL A CG2   1 
ATOM   6605  N  N     . LEU A 1 2284 ? 173.522 196.397 163.689 1.00 55.33  ? 2284 LEU A N     1 
ATOM   6606  C  CA    . LEU A 1 2284 ? 174.913 196.700 164.005 1.00 43.14  ? 2284 LEU A CA    1 
ATOM   6607  C  C     . LEU A 1 2284 ? 175.610 197.388 162.839 1.00 55.05  ? 2284 LEU A C     1 
ATOM   6608  O  O     . LEU A 1 2284 ? 176.390 198.323 163.043 1.00 65.42  ? 2284 LEU A O     1 
ATOM   6609  C  CB    . LEU A 1 2284 ? 175.651 195.421 164.397 1.00 54.08  ? 2284 LEU A CB    1 
ATOM   6610  C  CG    . LEU A 1 2284 ? 177.087 195.605 164.885 1.00 57.09  ? 2284 LEU A CG    1 
ATOM   6611  C  CD1   . LEU A 1 2284 ? 177.123 196.576 166.049 1.00 57.67  ? 2284 LEU A CD1   1 
ATOM   6612  C  CD2   . LEU A 1 2284 ? 177.691 194.270 165.281 1.00 57.29  ? 2284 LEU A CD2   1 
ATOM   6613  N  N     . ARG A 1 2285 ? 175.345 196.941 161.609 1.00 54.81  ? 2285 ARG A N     1 
ATOM   6614  C  CA    . ARG A 1 2285 ? 175.954 197.570 160.443 1.00 56.45  ? 2285 ARG A CA    1 
ATOM   6615  C  C     . ARG A 1 2285 ? 175.459 198.998 160.265 1.00 61.12  ? 2285 ARG A C     1 
ATOM   6616  O  O     . ARG A 1 2285 ? 176.237 199.890 159.907 1.00 69.78  ? 2285 ARG A O     1 
ATOM   6617  C  CB    . ARG A 1 2285 ? 175.665 196.738 159.196 1.00 62.32  ? 2285 ARG A CB    1 
ATOM   6618  C  CG    . ARG A 1 2285 ? 176.431 197.168 157.962 1.00 62.93  ? 2285 ARG A CG    1 
ATOM   6619  C  CD    . ARG A 1 2285 ? 175.872 196.497 156.720 1.00 69.50  ? 2285 ARG A CD    1 
ATOM   6620  N  NE    . ARG A 1 2285 ? 175.885 195.044 156.833 1.00 63.31  ? 2285 ARG A NE    1 
ATOM   6621  C  CZ    . ARG A 1 2285 ? 176.941 194.282 156.584 1.00 60.35  ? 2285 ARG A CZ    1 
ATOM   6622  N  NH1   . ARG A 1 2285 ? 178.097 194.804 156.208 1.00 64.86  ? 2285 ARG A NH1   1 
ATOM   6623  N  NH2   . ARG A 1 2285 ? 176.835 192.963 156.716 1.00 61.76  ? 2285 ARG A NH2   1 
ATOM   6624  N  N     . LYS A 1 2286 ? 174.167 199.234 160.506 1.00 64.07  ? 2286 LYS A N     1 
ATOM   6625  C  CA    . LYS A 1 2286 ? 173.634 200.588 160.423 1.00 64.51  ? 2286 LYS A CA    1 
ATOM   6626  C  C     . LYS A 1 2286 ? 174.278 201.494 161.464 1.00 65.88  ? 2286 LYS A C     1 
ATOM   6627  O  O     . LYS A 1 2286 ? 174.601 202.652 161.175 1.00 66.62  ? 2286 LYS A O     1 
ATOM   6628  C  CB    . LYS A 1 2286 ? 172.115 200.562 160.595 1.00 65.17  ? 2286 LYS A CB    1 
ATOM   6629  C  CG    . LYS A 1 2286 ? 171.489 201.922 160.849 1.00 70.46  ? 2286 LYS A CG    1 
ATOM   6630  C  CD    . LYS A 1 2286 ? 169.978 201.817 160.982 1.00 71.90  ? 2286 LYS A CD    1 
ATOM   6631  C  CE    . LYS A 1 2286 ? 169.306 201.756 159.620 1.00 73.37  ? 2286 LYS A CE    1 
ATOM   6632  N  NZ    . LYS A 1 2286 ? 169.411 203.050 158.892 1.00 73.40  ? 2286 LYS A NZ    1 
ATOM   6633  N  N     . ILE A 1 2287 ? 174.471 200.985 162.682 1.00 66.79  ? 2287 ILE A N     1 
ATOM   6634  C  CA    . ILE A 1 2287 ? 175.129 201.781 163.716 1.00 63.80  ? 2287 ILE A CA    1 
ATOM   6635  C  C     . ILE A 1 2287 ? 176.579 202.062 163.338 1.00 63.02  ? 2287 ILE A C     1 
ATOM   6636  O  O     . ILE A 1 2287 ? 177.076 203.182 163.512 1.00 69.74  ? 2287 ILE A O     1 
ATOM   6637  C  CB    . ILE A 1 2287 ? 175.027 201.081 165.083 1.00 60.26  ? 2287 ILE A CB    1 
ATOM   6638  C  CG1   . ILE A 1 2287 ? 173.571 201.019 165.542 1.00 59.68  ? 2287 ILE A CG1   1 
ATOM   6639  C  CG2   . ILE A 1 2287 ? 175.864 201.810 166.112 1.00 58.97  ? 2287 ILE A CG2   1 
ATOM   6640  C  CD1   . ILE A 1 2287 ? 173.346 200.108 166.725 1.00 63.04  ? 2287 ILE A CD1   1 
ATOM   6641  N  N     . ILE A 1 2288 ? 177.281 201.053 162.817 1.00 66.72  ? 2288 ILE A N     1 
ATOM   6642  C  CA    . ILE A 1 2288 ? 178.690 201.216 162.465 1.00 65.48  ? 2288 ILE A CA    1 
ATOM   6643  C  C     . ILE A 1 2288 ? 178.851 202.239 161.349 1.00 66.78  ? 2288 ILE A C     1 
ATOM   6644  O  O     . ILE A 1 2288 ? 179.736 203.102 161.401 1.00 69.65  ? 2288 ILE A O     1 
ATOM   6645  C  CB    . ILE A 1 2288 ? 179.304 199.858 162.079 1.00 60.71  ? 2288 ILE A CB    1 
ATOM   6646  C  CG1   . ILE A 1 2288 ? 179.512 198.992 163.319 1.00 60.12  ? 2288 ILE A CG1   1 
ATOM   6647  C  CG2   . ILE A 1 2288 ? 180.619 200.051 161.343 1.00 63.49  ? 2288 ILE A CG2   1 
ATOM   6648  C  CD1   . ILE A 1 2288 ? 179.677 197.528 163.004 1.00 63.89  ? 2288 ILE A CD1   1 
ATOM   6649  N  N     . ASP A 1 2289 ? 178.003 202.160 160.321 1.00 75.80  ? 2289 ASP A N     1 
ATOM   6650  C  CA    . ASP A 1 2289 ? 178.104 203.099 159.208 1.00 78.93  ? 2289 ASP A CA    1 
ATOM   6651  C  C     . ASP A 1 2289 ? 177.854 204.529 159.668 1.00 83.71  ? 2289 ASP A C     1 
ATOM   6652  O  O     . ASP A 1 2289 ? 178.540 205.459 159.227 1.00 88.90  ? 2289 ASP A O     1 
ATOM   6653  C  CB    . ASP A 1 2289 ? 177.125 202.710 158.101 1.00 84.52  ? 2289 ASP A CB    1 
ATOM   6654  C  CG    . ASP A 1 2289 ? 177.546 201.452 157.367 1.00 91.64  ? 2289 ASP A CG    1 
ATOM   6655  O  OD1   . ASP A 1 2289 ? 178.661 200.955 157.630 1.00 89.38  ? 2289 ASP A OD1   1 
ATOM   6656  O  OD2   . ASP A 1 2289 ? 176.763 200.960 156.528 1.00 93.09  ? 2289 ASP A OD2   1 
ATOM   6657  N  N     . SER A 1 2290 ? 176.880 204.722 160.560 1.00 83.82  ? 2290 SER A N     1 
ATOM   6658  C  CA    . SER A 1 2290 ? 176.569 206.032 161.134 1.00 84.22  ? 2290 SER A CA    1 
ATOM   6659  C  C     . SER A 1 2290 ? 176.288 207.065 160.043 1.00 85.64  ? 2290 SER A C     1 
ATOM   6660  O  O     . SER A 1 2290 ? 176.750 208.206 160.099 1.00 86.62  ? 2290 SER A O     1 
ATOM   6661  C  CB    . SER A 1 2290 ? 177.691 206.505 162.061 1.00 84.65  ? 2290 SER A CB    1 
ATOM   6662  O  OG    . SER A 1 2290 ? 177.331 207.704 162.724 1.00 89.87  ? 2290 SER A OG    1 
ATOM   6663  N  N     . VAL A 1 2291 ? 175.523 206.647 159.034 1.00 97.65  ? 2291 VAL A N     1 
ATOM   6664  C  CA    . VAL A 1 2291 ? 175.189 207.548 157.936 1.00 97.99  ? 2291 VAL A CA    1 
ATOM   6665  C  C     . VAL A 1 2291 ? 174.286 208.678 158.420 1.00 99.06  ? 2291 VAL A C     1 
ATOM   6666  O  O     . VAL A 1 2291 ? 174.287 209.776 157.852 1.00 99.26  ? 2291 VAL A O     1 
ATOM   6667  C  CB    . VAL A 1 2291 ? 174.561 206.760 156.771 1.00 98.06  ? 2291 VAL A CB    1 
ATOM   6668  C  CG1   . VAL A 1 2291 ? 173.114 206.408 157.068 1.00 97.24  ? 2291 VAL A CG1   1 
ATOM   6669  C  CG2   . VAL A 1 2291 ? 174.667 207.552 155.477 1.00 97.24  ? 2291 VAL A CG2   1 
ATOM   6670  N  N     . ARG A 1 2292 ? 173.509 208.435 159.474 1.00 101.96 ? 2292 ARG A N     1 
ATOM   6671  C  CA    . ARG A 1 2292 ? 172.628 209.439 160.062 1.00 99.20  ? 2292 ARG A CA    1 
ATOM   6672  C  C     . ARG A 1 2292 ? 173.079 209.821 161.469 1.00 98.97  ? 2292 ARG A C     1 
ATOM   6673  O  O     . ARG A 1 2292 ? 172.263 210.149 162.333 1.00 95.83  ? 2292 ARG A O     1 
ATOM   6674  C  CB    . ARG A 1 2292 ? 171.182 208.951 160.080 1.00 100.21 ? 2292 ARG A CB    1 
ATOM   6675  C  CG    . ARG A 1 2292 ? 170.618 208.617 158.709 1.00 100.76 ? 2292 ARG A CG    1 
ATOM   6676  C  CD    . ARG A 1 2292 ? 169.213 208.038 158.817 1.00 101.40 ? 2292 ARG A CD    1 
ATOM   6677  N  NE    . ARG A 1 2292 ? 168.518 207.993 157.535 1.00 100.65 ? 2292 ARG A NE    1 
ATOM   6678  C  CZ    . ARG A 1 2292 ? 168.867 207.230 156.507 1.00 101.73 ? 2292 ARG A CZ    1 
ATOM   6679  N  NH1   . ARG A 1 2292 ? 169.888 206.393 156.580 1.00 98.82  ? 2292 ARG A NH1   1 
ATOM   6680  N  NH2   . ARG A 1 2292 ? 168.165 207.300 155.380 1.00 105.21 ? 2292 ARG A NH2   1 
ATOM   6681  N  N     . GLY A 1 2293 ? 174.385 209.786 161.710 1.00 90.28  ? 2293 GLY A N     1 
ATOM   6682  C  CA    . GLY A 1 2293 ? 174.929 210.170 163.002 1.00 89.97  ? 2293 GLY A CA    1 
ATOM   6683  C  C     . GLY A 1 2293 ? 174.536 209.270 164.154 1.00 89.32  ? 2293 GLY A C     1 
ATOM   6684  O  O     . GLY A 1 2293 ? 174.224 209.767 165.244 1.00 86.09  ? 2293 GLY A O     1 
ATOM   6685  N  N     . GLU A 1 2294 ? 174.543 207.953 163.942 1.00 84.20  ? 2294 GLU A N     1 
ATOM   6686  C  CA    . GLU A 1 2294 ? 174.206 207.021 165.010 1.00 78.82  ? 2294 GLU A CA    1 
ATOM   6687  C  C     . GLU A 1 2294 ? 175.380 206.737 165.937 1.00 82.05  ? 2294 GLU A C     1 
ATOM   6688  O  O     . GLU A 1 2294 ? 175.177 206.160 167.010 1.00 88.18  ? 2294 GLU A O     1 
ATOM   6689  C  CB    . GLU A 1 2294 ? 173.692 205.706 164.422 1.00 73.92  ? 2294 GLU A CB    1 
ATOM   6690  C  CG    . GLU A 1 2294 ? 172.253 205.763 163.942 1.00 84.67  ? 2294 GLU A CG    1 
ATOM   6691  C  CD    . GLU A 1 2294 ? 172.142 205.731 162.432 1.00 88.19  ? 2294 GLU A CD    1 
ATOM   6692  O  OE1   . GLU A 1 2294 ? 173.188 205.822 161.757 1.00 87.22  ? 2294 GLU A OE1   1 
ATOM   6693  O  OE2   . GLU A 1 2294 ? 171.009 205.617 161.920 1.00 85.65  ? 2294 GLU A OE2   1 
ATOM   6694  N  N     . LEU A 1 2295 ? 176.595 207.125 165.552 1.00 77.50  ? 2295 LEU A N     1 
ATOM   6695  C  CA    . LEU A 1 2295 ? 177.771 206.876 166.376 1.00 75.31  ? 2295 LEU A CA    1 
ATOM   6696  C  C     . LEU A 1 2295 ? 177.880 207.821 167.565 1.00 74.19  ? 2295 LEU A C     1 
ATOM   6697  O  O     . LEU A 1 2295 ? 178.593 207.502 168.521 1.00 74.07  ? 2295 LEU A O     1 
ATOM   6698  C  CB    . LEU A 1 2295 ? 179.038 206.978 165.525 1.00 77.89  ? 2295 LEU A CB    1 
ATOM   6699  C  CG    . LEU A 1 2295 ? 179.678 205.653 165.110 1.00 76.68  ? 2295 LEU A CG    1 
ATOM   6700  C  CD1   . LEU A 1 2295 ? 180.775 205.884 164.084 1.00 71.31  ? 2295 LEU A CD1   1 
ATOM   6701  C  CD2   . LEU A 1 2295 ? 180.224 204.924 166.326 1.00 74.41  ? 2295 LEU A CD2   1 
ATOM   6702  N  N     . GLN A 1 2296 ? 177.199 208.963 167.533 1.00 82.51  ? 2296 GLN A N     1 
ATOM   6703  C  CA    . GLN A 1 2296 ? 177.239 209.923 168.627 1.00 85.94  ? 2296 GLN A CA    1 
ATOM   6704  C  C     . GLN A 1 2296 ? 176.185 209.652 169.691 1.00 86.20  ? 2296 GLN A C     1 
ATOM   6705  O  O     . GLN A 1 2296 ? 176.152 210.358 170.704 1.00 81.12  ? 2296 GLN A O     1 
ATOM   6706  C  CB    . GLN A 1 2296 ? 177.064 211.348 168.088 1.00 84.98  ? 2296 GLN A CB    1 
ATOM   6707  C  CG    . GLN A 1 2296 ? 177.623 211.570 166.691 1.00 83.11  ? 2296 GLN A CG    1 
ATOM   6708  C  CD    . GLN A 1 2296 ? 179.103 211.257 166.593 1.00 86.57  ? 2296 GLN A CD    1 
ATOM   6709  O  OE1   . GLN A 1 2296 ? 179.550 210.607 165.649 1.00 84.17  ? 2296 GLN A OE1   1 
ATOM   6710  N  NE2   . GLN A 1 2296 ? 179.872 211.723 167.570 1.00 88.68  ? 2296 GLN A NE2   1 
ATOM   6711  N  N     . LYS A 1 2297 ? 175.331 208.656 169.488 1.00 76.15  ? 2297 LYS A N     1 
ATOM   6712  C  CA    . LYS A 1 2297 ? 174.255 208.332 170.410 1.00 70.44  ? 2297 LYS A CA    1 
ATOM   6713  C  C     . LYS A 1 2297 ? 174.578 207.051 171.165 1.00 67.53  ? 2297 LYS A C     1 
ATOM   6714  O  O     . LYS A 1 2297 ? 175.362 206.214 170.710 1.00 76.54  ? 2297 LYS A O     1 
ATOM   6715  C  CB    . LYS A 1 2297 ? 172.927 208.176 169.662 1.00 66.09  ? 2297 LYS A CB    1 
ATOM   6716  C  CG    . LYS A 1 2297 ? 172.220 209.484 169.364 1.00 72.46  ? 2297 LYS A CG    1 
ATOM   6717  C  CD    . LYS A 1 2297 ? 171.663 209.491 167.951 1.00 77.45  ? 2297 LYS A CD    1 
ATOM   6718  C  CE    . LYS A 1 2297 ? 170.518 208.505 167.806 1.00 73.23  ? 2297 LYS A CE    1 
ATOM   6719  N  NZ    . LYS A 1 2297 ? 169.728 208.745 166.568 1.00 76.38  ? 2297 LYS A NZ    1 
ATOM   6720  N  N     . ARG A 1 2298 ? 173.961 206.905 172.334 1.00 58.29  ? 2298 ARG A N     1 
ATOM   6721  C  CA    . ARG A 1 2298 ? 174.114 205.704 173.147 1.00 58.43  ? 2298 ARG A CA    1 
ATOM   6722  C  C     . ARG A 1 2298 ? 173.186 204.631 172.590 1.00 66.28  ? 2298 ARG A C     1 
ATOM   6723  O  O     . ARG A 1 2298 ? 171.964 204.713 172.748 1.00 74.89  ? 2298 ARG A O     1 
ATOM   6724  C  CB    . ARG A 1 2298 ? 173.804 205.995 174.613 1.00 61.03  ? 2298 ARG A CB    1 
ATOM   6725  C  CG    . ARG A 1 2298 ? 173.626 204.750 175.463 1.00 61.67  ? 2298 ARG A CG    1 
ATOM   6726  C  CD    . ARG A 1 2298 ? 173.334 205.096 176.913 1.00 64.75  ? 2298 ARG A CD    1 
ATOM   6727  N  NE    . ARG A 1 2298 ? 174.541 205.453 177.647 1.00 69.84  ? 2298 ARG A NE    1 
ATOM   6728  C  CZ    . ARG A 1 2298 ? 174.880 206.693 177.969 1.00 70.09  ? 2298 ARG A CZ    1 
ATOM   6729  N  NH1   . ARG A 1 2298 ? 174.121 207.724 177.639 1.00 68.76  ? 2298 ARG A NH1   1 
ATOM   6730  N  NH2   . ARG A 1 2298 ? 176.008 206.904 178.641 1.00 67.78  ? 2298 ARG A NH2   1 
ATOM   6731  N  N     . GLN A 1 2299 ? 173.763 203.630 171.932 1.00 57.10  ? 2299 GLN A N     1 
ATOM   6732  C  CA    . GLN A 1 2299 ? 173.003 202.551 171.317 1.00 50.26  ? 2299 GLN A CA    1 
ATOM   6733  C  C     . GLN A 1 2299 ? 173.031 201.333 172.229 1.00 57.36  ? 2299 GLN A C     1 
ATOM   6734  O  O     . GLN A 1 2299 ? 174.108 200.846 172.588 1.00 64.38  ? 2299 GLN A O     1 
ATOM   6735  C  CB    . GLN A 1 2299 ? 173.571 202.198 169.943 1.00 57.62  ? 2299 GLN A CB    1 
ATOM   6736  C  CG    . GLN A 1 2299 ? 173.946 203.394 169.092 1.00 60.09  ? 2299 GLN A CG    1 
ATOM   6737  C  CD    . GLN A 1 2299 ? 172.774 203.931 168.300 1.00 70.75  ? 2299 GLN A CD    1 
ATOM   6738  O  OE1   . GLN A 1 2299 ? 171.947 203.168 167.803 1.00 71.17  ? 2299 GLN A OE1   1 
ATOM   6739  N  NE2   . GLN A 1 2299 ? 172.701 205.249 168.171 1.00 69.61  ? 2299 GLN A NE2   1 
ATOM   6740  N  N     . TRP A 1 2300 ? 171.851 200.844 172.597 1.00 50.73  ? 2300 TRP A N     1 
ATOM   6741  C  CA    . TRP A 1 2300 ? 171.706 199.633 173.395 1.00 42.02  ? 2300 TRP A CA    1 
ATOM   6742  C  C     . TRP A 1 2300 ? 170.884 198.632 172.601 1.00 52.79  ? 2300 TRP A C     1 
ATOM   6743  O  O     . TRP A 1 2300 ? 169.759 198.934 172.193 1.00 67.15  ? 2300 TRP A O     1 
ATOM   6744  C  CB    . TRP A 1 2300 ? 171.035 199.931 174.737 1.00 46.23  ? 2300 TRP A CB    1 
ATOM   6745  C  CG    . TRP A 1 2300 ? 171.925 200.608 175.728 1.00 49.34  ? 2300 TRP A CG    1 
ATOM   6746  C  CD1   . TRP A 1 2300 ? 173.172 201.109 175.503 1.00 57.74  ? 2300 TRP A CD1   1 
ATOM   6747  C  CD2   . TRP A 1 2300 ? 171.634 200.862 177.106 1.00 54.18  ? 2300 TRP A CD2   1 
ATOM   6748  N  NE1   . TRP A 1 2300 ? 173.677 201.657 176.656 1.00 57.59  ? 2300 TRP A NE1   1 
ATOM   6749  C  CE2   . TRP A 1 2300 ? 172.751 201.519 177.655 1.00 55.19  ? 2300 TRP A CE2   1 
ATOM   6750  C  CE3   . TRP A 1 2300 ? 170.536 200.597 177.930 1.00 52.53  ? 2300 TRP A CE3   1 
ATOM   6751  C  CZ2   . TRP A 1 2300 ? 172.803 201.914 178.988 1.00 52.07  ? 2300 TRP A CZ2   1 
ATOM   6752  C  CZ3   . TRP A 1 2300 ? 170.590 200.990 179.252 1.00 59.04  ? 2300 TRP A CZ3   1 
ATOM   6753  C  CH2   . TRP A 1 2300 ? 171.715 201.641 179.769 1.00 52.31  ? 2300 TRP A CH2   1 
ATOM   6754  N  N     . ILE A 1 2301 ? 171.442 197.447 172.382 1.00 40.32  ? 2301 ILE A N     1 
ATOM   6755  C  CA    . ILE A 1 2301 ? 170.757 196.374 171.673 1.00 37.80  ? 2301 ILE A CA    1 
ATOM   6756  C  C     . ILE A 1 2301 ? 170.328 195.346 172.709 1.00 45.68  ? 2301 ILE A C     1 
ATOM   6757  O  O     . ILE A 1 2301 ? 171.144 194.549 173.184 1.00 64.69  ? 2301 ILE A O     1 
ATOM   6758  C  CB    . ILE A 1 2301 ? 171.650 195.749 170.594 1.00 35.88  ? 2301 ILE A CB    1 
ATOM   6759  C  CG1   . ILE A 1 2301 ? 172.208 196.838 169.677 1.00 39.84  ? 2301 ILE A CG1   1 
ATOM   6760  C  CG2   . ILE A 1 2301 ? 170.871 194.725 169.791 1.00 35.35  ? 2301 ILE A CG2   1 
ATOM   6761  C  CD1   . ILE A 1 2301 ? 173.170 196.325 168.636 1.00 43.48  ? 2301 ILE A CD1   1 
ATOM   6762  N  N     . VAL A 1 2302 ? 169.046 195.357 173.059 1.00 39.92  ? 2302 VAL A N     1 
ATOM   6763  C  CA    . VAL A 1 2302 ? 168.508 194.514 174.120 1.00 36.02  ? 2302 VAL A CA    1 
ATOM   6764  C  C     . VAL A 1 2302 ? 167.906 193.267 173.491 1.00 52.17  ? 2302 VAL A C     1 
ATOM   6765  O  O     . VAL A 1 2302 ? 166.966 193.356 172.693 1.00 63.41  ? 2302 VAL A O     1 
ATOM   6766  C  CB    . VAL A 1 2302 ? 167.464 195.267 174.958 1.00 32.41  ? 2302 VAL A CB    1 
ATOM   6767  C  CG1   . VAL A 1 2302 ? 167.043 194.430 176.151 1.00 46.86  ? 2302 VAL A CG1   1 
ATOM   6768  C  CG2   . VAL A 1 2302 ? 168.019 196.607 175.408 1.00 43.10  ? 2302 VAL A CG2   1 
ATOM   6769  N  N     . PHE A 1 2303 ? 168.445 192.103 173.852 1.00 45.73  ? 2303 PHE A N     1 
ATOM   6770  C  CA    . PHE A 1 2303 ? 167.952 190.825 173.340 1.00 38.94  ? 2303 PHE A CA    1 
ATOM   6771  C  C     . PHE A 1 2303 ? 166.920 190.249 174.311 1.00 51.14  ? 2303 PHE A C     1 
ATOM   6772  O  O     . PHE A 1 2303 ? 167.162 189.291 175.045 1.00 67.53  ? 2303 PHE A O     1 
ATOM   6773  C  CB    . PHE A 1 2303 ? 169.109 189.861 173.117 1.00 38.59  ? 2303 PHE A CB    1 
ATOM   6774  C  CG    . PHE A 1 2303 ? 169.852 190.092 171.836 1.00 34.50  ? 2303 PHE A CG    1 
ATOM   6775  C  CD1   . PHE A 1 2303 ? 169.241 189.864 170.618 1.00 49.89  ? 2303 PHE A CD1   1 
ATOM   6776  C  CD2   . PHE A 1 2303 ? 171.163 190.530 171.851 1.00 41.32  ? 2303 PHE A CD2   1 
ATOM   6777  C  CE1   . PHE A 1 2303 ? 169.921 190.073 169.438 1.00 54.02  ? 2303 PHE A CE1   1 
ATOM   6778  C  CE2   . PHE A 1 2303 ? 171.848 190.740 170.674 1.00 42.49  ? 2303 PHE A CE2   1 
ATOM   6779  C  CZ    . PHE A 1 2303 ? 171.226 190.510 169.466 1.00 50.68  ? 2303 PHE A CZ    1 
ATOM   6780  N  N     . ASP A 1 2304 ? 165.742 190.866 174.300 1.00 47.49  ? 2304 ASP A N     1 
ATOM   6781  C  CA    . ASP A 1 2304 ? 164.643 190.442 175.161 1.00 55.57  ? 2304 ASP A CA    1 
ATOM   6782  C  C     . ASP A 1 2304 ? 164.095 189.119 174.641 1.00 63.06  ? 2304 ASP A C     1 
ATOM   6783  O  O     . ASP A 1 2304 ? 163.370 189.089 173.642 1.00 75.01  ? 2304 ASP A O     1 
ATOM   6784  C  CB    . ASP A 1 2304 ? 163.558 191.514 175.201 1.00 62.85  ? 2304 ASP A CB    1 
ATOM   6785  C  CG    . ASP A 1 2304 ? 162.528 191.267 176.288 1.00 66.50  ? 2304 ASP A CG    1 
ATOM   6786  O  OD1   . ASP A 1 2304 ? 162.505 190.159 176.862 1.00 60.18  ? 2304 ASP A OD1   1 
ATOM   6787  O  OD2   . ASP A 1 2304 ? 161.736 192.191 176.570 1.00 65.02  ? 2304 ASP A OD2   1 
ATOM   6788  N  N     . GLY A 1 2305 ? 164.436 188.029 175.313 1.00 49.89  ? 2305 GLY A N     1 
ATOM   6789  C  CA    . GLY A 1 2305 ? 163.962 186.722 174.913 1.00 54.99  ? 2305 GLY A CA    1 
ATOM   6790  C  C     . GLY A 1 2305 ? 164.822 185.632 175.523 1.00 57.74  ? 2305 GLY A C     1 
ATOM   6791  O  O     . GLY A 1 2305 ? 165.814 185.901 176.197 1.00 64.77  ? 2305 GLY A O     1 
ATOM   6792  N  N     . ASP A 1 2306 ? 164.414 184.394 175.262 1.00 71.61  ? 2306 ASP A N     1 
ATOM   6793  C  CA    . ASP A 1 2306 ? 165.124 183.234 175.778 1.00 69.50  ? 2306 ASP A CA    1 
ATOM   6794  C  C     . ASP A 1 2306 ? 166.489 183.098 175.113 1.00 78.10  ? 2306 ASP A C     1 
ATOM   6795  O  O     . ASP A 1 2306 ? 166.694 183.522 173.973 1.00 80.91  ? 2306 ASP A O     1 
ATOM   6796  C  CB    . ASP A 1 2306 ? 164.305 181.962 175.556 1.00 77.44  ? 2306 ASP A CB    1 
ATOM   6797  C  CG    . ASP A 1 2306 ? 163.262 181.746 176.635 1.00 86.18  ? 2306 ASP A CG    1 
ATOM   6798  O  OD1   . ASP A 1 2306 ? 162.900 180.578 176.889 1.00 86.62  ? 2306 ASP A OD1   1 
ATOM   6799  O  OD2   . ASP A 1 2306 ? 162.805 182.744 177.229 1.00 85.82  ? 2306 ASP A OD2   1 
ATOM   6800  N  N     . VAL A 1 2307 ? 167.427 182.501 175.844 1.00 76.11  ? 2307 VAL A N     1 
ATOM   6801  C  CA    . VAL A 1 2307 ? 168.808 182.355 175.396 1.00 71.01  ? 2307 VAL A CA    1 
ATOM   6802  C  C     . VAL A 1 2307 ? 169.151 180.873 175.365 1.00 71.61  ? 2307 VAL A C     1 
ATOM   6803  O  O     . VAL A 1 2307 ? 168.963 180.165 176.362 1.00 76.46  ? 2307 VAL A O     1 
ATOM   6804  C  CB    . VAL A 1 2307 ? 169.783 183.127 176.299 1.00 64.60  ? 2307 VAL A CB    1 
ATOM   6805  C  CG1   . VAL A 1 2307 ? 171.172 182.513 176.237 1.00 65.78  ? 2307 VAL A CG1   1 
ATOM   6806  C  CG2   . VAL A 1 2307 ? 169.833 184.588 175.892 1.00 66.95  ? 2307 VAL A CG2   1 
ATOM   6807  N  N     . ASP A 1 2308 ? 169.645 180.408 174.226 1.00 66.39  ? 2308 ASP A N     1 
ATOM   6808  C  CA    . ASP A 1 2308 ? 170.161 179.061 174.050 1.00 68.46  ? 2308 ASP A CA    1 
ATOM   6809  C  C     . ASP A 1 2308 ? 171.448 179.126 173.243 1.00 70.22  ? 2308 ASP A C     1 
ATOM   6810  O  O     . ASP A 1 2308 ? 171.705 180.119 172.554 1.00 74.97  ? 2308 ASP A O     1 
ATOM   6811  C  CB    . ASP A 1 2308 ? 169.128 178.145 173.369 1.00 70.85  ? 2308 ASP A CB    1 
ATOM   6812  C  CG    . ASP A 1 2308 ? 168.816 178.547 171.938 1.00 76.40  ? 2308 ASP A CG    1 
ATOM   6813  O  OD1   . ASP A 1 2308 ? 169.309 179.584 171.464 1.00 79.07  ? 2308 ASP A OD1   1 
ATOM   6814  O  OD2   . ASP A 1 2308 ? 168.055 177.812 171.275 1.00 79.21  ? 2308 ASP A OD2   1 
ATOM   6815  N  N     . PRO A 1 2309 ? 172.293 178.095 173.324 1.00 60.96  ? 2309 PRO A N     1 
ATOM   6816  C  CA    . PRO A 1 2309 ? 173.584 178.159 172.617 1.00 58.40  ? 2309 PRO A CA    1 
ATOM   6817  C  C     . PRO A 1 2309 ? 173.462 178.253 171.106 1.00 65.21  ? 2309 PRO A C     1 
ATOM   6818  O  O     . PRO A 1 2309 ? 174.433 178.635 170.444 1.00 75.09  ? 2309 PRO A O     1 
ATOM   6819  C  CB    . PRO A 1 2309 ? 174.284 176.860 173.042 1.00 60.12  ? 2309 PRO A CB    1 
ATOM   6820  C  CG    . PRO A 1 2309 ? 173.201 175.983 173.573 1.00 66.01  ? 2309 PRO A CG    1 
ATOM   6821  C  CD    . PRO A 1 2309 ? 172.203 176.904 174.184 1.00 66.36  ? 2309 PRO A CD    1 
ATOM   6822  N  N     . GLU A 1 2310 ? 172.310 177.907 170.531 1.00 68.21  ? 2310 GLU A N     1 
ATOM   6823  C  CA    . GLU A 1 2310 ? 172.199 177.900 169.075 1.00 67.08  ? 2310 GLU A CA    1 
ATOM   6824  C  C     . GLU A 1 2310 ? 172.359 179.299 168.491 1.00 70.09  ? 2310 GLU A C     1 
ATOM   6825  O  O     . GLU A 1 2310 ? 173.022 179.475 167.462 1.00 70.66  ? 2310 GLU A O     1 
ATOM   6826  C  CB    . GLU A 1 2310 ? 170.868 177.284 168.651 1.00 71.87  ? 2310 GLU A CB    1 
ATOM   6827  C  CG    . GLU A 1 2310 ? 170.744 175.814 169.010 1.00 79.38  ? 2310 GLU A CG    1 
ATOM   6828  C  CD    . GLU A 1 2310 ? 171.353 174.904 167.963 1.00 80.50  ? 2310 GLU A CD    1 
ATOM   6829  O  OE1   . GLU A 1 2310 ? 171.694 175.399 166.869 1.00 81.73  ? 2310 GLU A OE1   1 
ATOM   6830  O  OE2   . GLU A 1 2310 ? 171.496 173.693 168.235 1.00 74.33  ? 2310 GLU A OE2   1 
ATOM   6831  N  N     . TRP A 1 2311 ? 171.766 180.309 169.128 1.00 61.46  ? 2311 TRP A N     1 
ATOM   6832  C  CA    . TRP A 1 2311 ? 171.848 181.664 168.596 1.00 55.96  ? 2311 TRP A CA    1 
ATOM   6833  C  C     . TRP A 1 2311 ? 172.818 182.551 169.365 1.00 61.90  ? 2311 TRP A C     1 
ATOM   6834  O  O     . TRP A 1 2311 ? 173.374 183.490 168.784 1.00 68.29  ? 2311 TRP A O     1 
ATOM   6835  C  CB    . TRP A 1 2311 ? 170.457 182.314 168.572 1.00 55.37  ? 2311 TRP A CB    1 
ATOM   6836  C  CG    . TRP A 1 2311 ? 170.000 182.902 169.883 1.00 53.61  ? 2311 TRP A CG    1 
ATOM   6837  C  CD1   . TRP A 1 2311 ? 169.173 182.319 170.792 1.00 58.57  ? 2311 TRP A CD1   1 
ATOM   6838  C  CD2   . TRP A 1 2311 ? 170.309 184.202 170.403 1.00 55.74  ? 2311 TRP A CD2   1 
ATOM   6839  N  NE1   . TRP A 1 2311 ? 168.969 183.158 171.859 1.00 54.61  ? 2311 TRP A NE1   1 
ATOM   6840  C  CE2   . TRP A 1 2311 ? 169.654 184.322 171.643 1.00 53.78  ? 2311 TRP A CE2   1 
ATOM   6841  C  CE3   . TRP A 1 2311 ? 171.085 185.270 169.946 1.00 59.29  ? 2311 TRP A CE3   1 
ATOM   6842  C  CZ2   . TRP A 1 2311 ? 169.753 185.464 172.430 1.00 57.41  ? 2311 TRP A CZ2   1 
ATOM   6843  C  CZ3   . TRP A 1 2311 ? 171.181 186.401 170.728 1.00 54.96  ? 2311 TRP A CZ3   1 
ATOM   6844  C  CH2   . TRP A 1 2311 ? 170.516 186.491 171.954 1.00 59.59  ? 2311 TRP A CH2   1 
ATOM   6845  N  N     . VAL A 1 2312 ? 173.042 182.279 170.651 1.00 58.95  ? 2312 VAL A N     1 
ATOM   6846  C  CA    . VAL A 1 2312 ? 173.833 183.204 171.457 1.00 51.05  ? 2312 VAL A CA    1 
ATOM   6847  C  C     . VAL A 1 2312 ? 175.326 182.923 171.331 1.00 55.07  ? 2312 VAL A C     1 
ATOM   6848  O  O     . VAL A 1 2312 ? 176.148 183.787 171.654 1.00 68.78  ? 2312 VAL A O     1 
ATOM   6849  C  CB    . VAL A 1 2312 ? 173.380 183.156 172.926 1.00 55.92  ? 2312 VAL A CB    1 
ATOM   6850  C  CG1   . VAL A 1 2312 ? 174.036 181.995 173.652 1.00 56.35  ? 2312 VAL A CG1   1 
ATOM   6851  C  CG2   . VAL A 1 2312 ? 173.688 184.473 173.619 1.00 55.02  ? 2312 VAL A CG2   1 
ATOM   6852  N  N     . GLU A 1 2313 ? 175.708 181.732 170.867 1.00 67.16  ? 2313 GLU A N     1 
ATOM   6853  C  CA    . GLU A 1 2313 ? 177.129 181.417 170.750 1.00 64.88  ? 2313 GLU A CA    1 
ATOM   6854  C  C     . GLU A 1 2313 ? 177.768 182.173 169.593 1.00 72.30  ? 2313 GLU A C     1 
ATOM   6855  O  O     . GLU A 1 2313 ? 178.995 182.308 169.531 1.00 79.84  ? 2313 GLU A O     1 
ATOM   6856  C  CB    . GLU A 1 2313 ? 177.327 179.911 170.583 1.00 67.05  ? 2313 GLU A CB    1 
ATOM   6857  C  CG    . GLU A 1 2313 ? 177.135 179.108 171.864 1.00 73.98  ? 2313 GLU A CG    1 
ATOM   6858  C  CD    . GLU A 1 2313 ? 178.283 179.254 172.841 1.00 80.32  ? 2313 GLU A CD    1 
ATOM   6859  O  OE1   . GLU A 1 2313 ? 179.286 179.912 172.497 1.00 77.24  ? 2313 GLU A OE1   1 
ATOM   6860  O  OE2   . GLU A 1 2313 ? 178.183 178.705 173.958 1.00 81.82  ? 2313 GLU A OE2   1 
ATOM   6861  N  N     . ASN A 1 2314 ? 176.954 182.673 168.665 1.00 67.42  ? 2314 ASN A N     1 
ATOM   6862  C  CA    . ASN A 1 2314 ? 177.463 183.458 167.547 1.00 58.62  ? 2314 ASN A CA    1 
ATOM   6863  C  C     . ASN A 1 2314 ? 177.910 184.837 168.013 1.00 63.92  ? 2314 ASN A C     1 
ATOM   6864  O  O     . ASN A 1 2314 ? 178.547 185.579 167.259 1.00 67.86  ? 2314 ASN A O     1 
ATOM   6865  C  CB    . ASN A 1 2314 ? 176.405 183.588 166.453 1.00 58.80  ? 2314 ASN A CB    1 
ATOM   6866  C  CG    . ASN A 1 2314 ? 177.013 183.728 165.077 1.00 65.59  ? 2314 ASN A CG    1 
ATOM   6867  O  OD1   . ASN A 1 2314 ? 177.368 182.739 164.441 1.00 65.34  ? 2314 ASN A OD1   1 
ATOM   6868  N  ND2   . ASN A 1 2314 ? 177.147 184.964 164.611 1.00 71.62  ? 2314 ASN A ND2   1 
ATOM   6869  N  N     . LEU A 1 2315 ? 177.572 185.189 169.252 1.00 57.88  ? 2315 LEU A N     1 
ATOM   6870  C  CA    . LEU A 1 2315 ? 177.963 186.459 169.845 1.00 56.25  ? 2315 LEU A CA    1 
ATOM   6871  C  C     . LEU A 1 2315 ? 179.178 186.331 170.752 1.00 58.03  ? 2315 LEU A C     1 
ATOM   6872  O  O     . LEU A 1 2315 ? 179.503 187.281 171.469 1.00 65.91  ? 2315 LEU A O     1 
ATOM   6873  C  CB    . LEU A 1 2315 ? 176.792 187.059 170.625 1.00 51.49  ? 2315 LEU A CB    1 
ATOM   6874  C  CG    . LEU A 1 2315 ? 175.630 187.580 169.784 1.00 45.03  ? 2315 LEU A CG    1 
ATOM   6875  C  CD1   . LEU A 1 2315 ? 174.477 188.007 170.672 1.00 53.85  ? 2315 LEU A CD1   1 
ATOM   6876  C  CD2   . LEU A 1 2315 ? 176.096 188.733 168.923 1.00 51.00  ? 2315 LEU A CD2   1 
ATOM   6877  N  N     . ASN A 1 2316 ? 179.857 185.181 170.739 1.00 52.51  ? 2316 ASN A N     1 
ATOM   6878  C  CA    . ASN A 1 2316 ? 181.005 184.994 171.619 1.00 51.69  ? 2316 ASN A CA    1 
ATOM   6879  C  C     . ASN A 1 2316 ? 182.107 185.999 171.313 1.00 58.91  ? 2316 ASN A C     1 
ATOM   6880  O  O     . ASN A 1 2316 ? 182.716 186.562 172.229 1.00 70.24  ? 2316 ASN A O     1 
ATOM   6881  C  CB    . ASN A 1 2316 ? 181.537 183.568 171.493 1.00 59.56  ? 2316 ASN A CB    1 
ATOM   6882  C  CG    . ASN A 1 2316 ? 180.723 182.572 172.286 1.00 71.95  ? 2316 ASN A CG    1 
ATOM   6883  O  OD1   . ASN A 1 2316 ? 179.778 182.940 172.983 1.00 68.60  ? 2316 ASN A OD1   1 
ATOM   6884  N  ND2   . ASN A 1 2316 ? 181.087 181.300 172.187 1.00 70.66  ? 2316 ASN A ND2   1 
ATOM   6885  N  N     . SER A 1 2317 ? 182.378 186.239 170.029 1.00 58.30  ? 2317 SER A N     1 
ATOM   6886  C  CA    . SER A 1 2317 ? 183.406 187.208 169.665 1.00 57.64  ? 2317 SER A CA    1 
ATOM   6887  C  C     . SER A 1 2317 ? 182.968 188.634 169.970 1.00 57.85  ? 2317 SER A C     1 
ATOM   6888  O  O     . SER A 1 2317 ? 183.803 189.475 170.317 1.00 62.92  ? 2317 SER A O     1 
ATOM   6889  C  CB    . SER A 1 2317 ? 183.762 187.065 168.187 1.00 54.77  ? 2317 SER A CB    1 
ATOM   6890  O  OG    . SER A 1 2317 ? 182.596 187.078 167.383 1.00 58.23  ? 2317 SER A OG    1 
ATOM   6891  N  N     . VAL A 1 2318 ? 181.673 188.927 169.838 1.00 49.89  ? 2318 VAL A N     1 
ATOM   6892  C  CA    . VAL A 1 2318 ? 181.174 190.262 170.154 1.00 45.61  ? 2318 VAL A CA    1 
ATOM   6893  C  C     . VAL A 1 2318 ? 181.337 190.554 171.640 1.00 51.87  ? 2318 VAL A C     1 
ATOM   6894  O  O     . VAL A 1 2318 ? 181.783 191.638 172.033 1.00 55.10  ? 2318 VAL A O     1 
ATOM   6895  C  CB    . VAL A 1 2318 ? 179.708 190.404 169.710 1.00 42.37  ? 2318 VAL A CB    1 
ATOM   6896  C  CG1   . VAL A 1 2318 ? 179.196 191.797 170.016 1.00 48.33  ? 2318 VAL A CG1   1 
ATOM   6897  C  CG2   . VAL A 1 2318 ? 179.572 190.098 168.231 1.00 55.29  ? 2318 VAL A CG2   1 
ATOM   6898  N  N     . LEU A 1 2319 ? 180.979 189.589 172.488 1.00 58.42  ? 2319 LEU A N     1 
ATOM   6899  C  CA    . LEU A 1 2319 ? 181.081 189.779 173.930 1.00 53.57  ? 2319 LEU A CA    1 
ATOM   6900  C  C     . LEU A 1 2319 ? 182.516 189.657 174.426 1.00 55.48  ? 2319 LEU A C     1 
ATOM   6901  O  O     . LEU A 1 2319 ? 182.825 190.113 175.532 1.00 59.67  ? 2319 LEU A O     1 
ATOM   6902  C  CB    . LEU A 1 2319 ? 180.184 188.772 174.648 1.00 55.89  ? 2319 LEU A CB    1 
ATOM   6903  C  CG    . LEU A 1 2319 ? 178.736 188.748 174.160 1.00 46.28  ? 2319 LEU A CG    1 
ATOM   6904  C  CD1   . LEU A 1 2319 ? 177.976 187.586 174.773 1.00 45.97  ? 2319 LEU A CD1   1 
ATOM   6905  C  CD2   . LEU A 1 2319 ? 178.048 190.066 174.468 1.00 56.39  ? 2319 LEU A CD2   1 
ATOM   6906  N  N     . ASP A 1 2320 ? 183.398 189.050 173.636 1.00 66.62  ? 2320 ASP A N     1 
ATOM   6907  C  CA    . ASP A 1 2320 ? 184.794 188.919 174.019 1.00 63.40  ? 2320 ASP A CA    1 
ATOM   6908  C  C     . ASP A 1 2320 ? 185.517 190.256 173.878 1.00 71.44  ? 2320 ASP A C     1 
ATOM   6909  O  O     . ASP A 1 2320 ? 184.925 191.292 173.563 1.00 84.60  ? 2320 ASP A O     1 
ATOM   6910  C  CB    . ASP A 1 2320 ? 185.489 187.859 173.167 1.00 70.89  ? 2320 ASP A CB    1 
ATOM   6911  C  CG    . ASP A 1 2320 ? 185.473 186.491 173.813 1.00 84.83  ? 2320 ASP A CG    1 
ATOM   6912  O  OD1   . ASP A 1 2320 ? 185.054 186.392 174.985 1.00 88.14  ? 2320 ASP A OD1   1 
ATOM   6913  O  OD2   . ASP A 1 2320 ? 185.878 185.514 173.149 1.00 83.60  ? 2320 ASP A OD2   1 
ATOM   6914  N  N     . ASP A 1 2321 ? 186.829 190.221 174.118 1.00 75.82  ? 2321 ASP A N     1 
ATOM   6915  C  CA    . ASP A 1 2321 ? 187.640 191.420 173.942 1.00 80.02  ? 2321 ASP A CA    1 
ATOM   6916  C  C     . ASP A 1 2321 ? 187.817 191.754 172.467 1.00 77.30  ? 2321 ASP A C     1 
ATOM   6917  O  O     . ASP A 1 2321 ? 188.216 192.871 172.118 1.00 80.77  ? 2321 ASP A O     1 
ATOM   6918  C  CB    . ASP A 1 2321 ? 188.997 191.239 174.620 1.00 82.33  ? 2321 ASP A CB    1 
ATOM   6919  C  CG    . ASP A 1 2321 ? 188.871 190.916 176.096 1.00 87.82  ? 2321 ASP A CG    1 
ATOM   6920  O  OD1   . ASP A 1 2321 ? 187.908 191.397 176.730 1.00 87.63  ? 2321 ASP A OD1   1 
ATOM   6921  O  OD2   . ASP A 1 2321 ? 189.734 190.182 176.622 1.00 83.46  ? 2321 ASP A OD2   1 
ATOM   6922  N  N     . ASN A 1 2322 ? 187.534 190.794 171.586 1.00 72.68  ? 2322 ASN A N     1 
ATOM   6923  C  CA    . ASN A 1 2322 ? 187.636 191.011 170.148 1.00 74.76  ? 2322 ASN A CA    1 
ATOM   6924  C  C     . ASN A 1 2322 ? 186.645 192.071 169.685 1.00 75.33  ? 2322 ASN A C     1 
ATOM   6925  O  O     . ASN A 1 2322 ? 186.989 192.939 168.877 1.00 79.21  ? 2322 ASN A O     1 
ATOM   6926  C  CB    . ASN A 1 2322 ? 187.402 189.702 169.391 1.00 74.70  ? 2322 ASN A CB    1 
ATOM   6927  C  CG    . ASN A 1 2322 ? 188.461 188.661 169.685 1.00 78.24  ? 2322 ASN A CG    1 
ATOM   6928  O  OD1   . ASN A 1 2322 ? 189.635 188.845 169.365 1.00 79.78  ? 2322 ASN A OD1   1 
ATOM   6929  N  ND2   . ASN A 1 2322 ? 188.052 187.557 170.298 1.00 74.84  ? 2322 ASN A ND2   1 
ATOM   6930  N  N     . LYS A 1 2323 ? 185.417 192.006 170.201 1.00 61.46  ? 2323 LYS A N     1 
ATOM   6931  C  CA    . LYS A 1 2323 ? 184.340 192.917 169.815 1.00 59.51  ? 2323 LYS A CA    1 
ATOM   6932  C  C     . LYS A 1 2323 ? 184.130 192.909 168.302 1.00 61.89  ? 2323 LYS A C     1 
ATOM   6933  O  O     . LYS A 1 2323 ? 184.004 193.951 167.657 1.00 67.93  ? 2323 LYS A O     1 
ATOM   6934  C  CB    . LYS A 1 2323 ? 184.607 194.334 170.327 1.00 64.33  ? 2323 LYS A CB    1 
ATOM   6935  C  CG    . LYS A 1 2323 ? 184.350 194.513 171.815 1.00 64.83  ? 2323 LYS A CG    1 
ATOM   6936  C  CD    . LYS A 1 2323 ? 184.482 195.969 172.233 1.00 65.25  ? 2323 LYS A CD    1 
ATOM   6937  C  CE    . LYS A 1 2323 ? 185.937 196.386 172.347 1.00 65.06  ? 2323 LYS A CE    1 
ATOM   6938  N  NZ    . LYS A 1 2323 ? 186.625 195.675 173.459 1.00 69.16  ? 2323 LYS A NZ    1 
ATOM   6939  N  N     . LEU A 1 2324 ? 184.095 191.706 167.734 1.00 62.10  ? 2324 LEU A N     1 
ATOM   6940  C  CA    . LEU A 1 2324 ? 183.891 191.508 166.306 1.00 59.34  ? 2324 LEU A CA    1 
ATOM   6941  C  C     . LEU A 1 2324 ? 182.686 190.607 166.090 1.00 66.93  ? 2324 LEU A C     1 
ATOM   6942  O  O     . LEU A 1 2324 ? 182.508 189.619 166.809 1.00 78.39  ? 2324 LEU A O     1 
ATOM   6943  C  CB    . LEU A 1 2324 ? 185.127 190.886 165.650 1.00 53.31  ? 2324 LEU A CB    1 
ATOM   6944  C  CG    . LEU A 1 2324 ? 186.376 191.754 165.509 1.00 61.04  ? 2324 LEU A CG    1 
ATOM   6945  C  CD1   . LEU A 1 2324 ? 187.498 190.957 164.868 1.00 60.26  ? 2324 LEU A CD1   1 
ATOM   6946  C  CD2   . LEU A 1 2324 ? 186.070 192.995 164.695 1.00 64.60  ? 2324 LEU A CD2   1 
ATOM   6947  N  N     . LEU A 1 2325 ? 181.858 190.951 165.107 1.00 51.23  ? 2325 LEU A N     1 
ATOM   6948  C  CA    . LEU A 1 2325 ? 180.770 190.078 164.671 1.00 50.68  ? 2325 LEU A CA    1 
ATOM   6949  C  C     . LEU A 1 2325 ? 181.217 189.404 163.381 1.00 59.45  ? 2325 LEU A C     1 
ATOM   6950  O  O     . LEU A 1 2325 ? 181.114 189.980 162.296 1.00 69.69  ? 2325 LEU A O     1 
ATOM   6951  C  CB    . LEU A 1 2325 ? 179.479 190.864 164.479 1.00 57.70  ? 2325 LEU A CB    1 
ATOM   6952  C  CG    . LEU A 1 2325 ? 178.304 190.068 163.907 1.00 58.73  ? 2325 LEU A CG    1 
ATOM   6953  C  CD1   . LEU A 1 2325 ? 177.963 188.891 164.807 1.00 56.91  ? 2325 LEU A CD1   1 
ATOM   6954  C  CD2   . LEU A 1 2325 ? 177.094 190.961 163.707 1.00 63.43  ? 2325 LEU A CD2   1 
ATOM   6955  N  N     . THR A 1 2326 ? 181.723 188.181 163.498 1.00 59.52  ? 2326 THR A N     1 
ATOM   6956  C  CA    . THR A 1 2326 ? 182.253 187.468 162.345 1.00 55.53  ? 2326 THR A CA    1 
ATOM   6957  C  C     . THR A 1 2326 ? 181.126 186.797 161.573 1.00 62.76  ? 2326 THR A C     1 
ATOM   6958  O  O     . THR A 1 2326 ? 180.337 186.036 162.141 1.00 71.21  ? 2326 THR A O     1 
ATOM   6959  C  CB    . THR A 1 2326 ? 183.280 186.428 162.784 1.00 66.45  ? 2326 THR A CB    1 
ATOM   6960  O  OG1   . THR A 1 2326 ? 184.032 186.936 163.893 1.00 66.90  ? 2326 THR A OG1   1 
ATOM   6961  C  CG2   . THR A 1 2326 ? 184.222 186.111 161.641 1.00 71.33  ? 2326 THR A CG2   1 
ATOM   6962  N  N     . LEU A 1 2327 ? 181.058 187.077 160.275 1.00 58.24  ? 2327 LEU A N     1 
ATOM   6963  C  CA    . LEU A 1 2327 ? 180.047 186.520 159.396 1.00 57.51  ? 2327 LEU A CA    1 
ATOM   6964  C  C     . LEU A 1 2327 ? 180.648 185.430 158.514 1.00 68.62  ? 2327 LEU A C     1 
ATOM   6965  O  O     . LEU A 1 2327 ? 181.857 185.427 158.262 1.00 73.02  ? 2327 LEU A O     1 
ATOM   6966  C  CB    . LEU A 1 2327 ? 179.428 187.610 158.513 1.00 61.01  ? 2327 LEU A CB    1 
ATOM   6967  C  CG    . LEU A 1 2327 ? 178.803 188.789 159.259 1.00 66.36  ? 2327 LEU A CG    1 
ATOM   6968  C  CD1   . LEU A 1 2327 ? 178.381 189.874 158.285 1.00 68.29  ? 2327 LEU A CD1   1 
ATOM   6969  C  CD2   . LEU A 1 2327 ? 177.626 188.328 160.102 1.00 64.38  ? 2327 LEU A CD2   1 
ATOM   6970  N  N     . PRO A 1 2328 ? 179.834 184.484 158.037 1.00 72.67  ? 2328 PRO A N     1 
ATOM   6971  C  CA    . PRO A 1 2328 ? 180.383 183.385 157.224 1.00 67.73  ? 2328 PRO A CA    1 
ATOM   6972  C  C     . PRO A 1 2328 ? 181.063 183.838 155.945 1.00 68.11  ? 2328 PRO A C     1 
ATOM   6973  O  O     . PRO A 1 2328 ? 181.927 183.113 155.436 1.00 77.82  ? 2328 PRO A O     1 
ATOM   6974  C  CB    . PRO A 1 2328 ? 179.154 182.514 156.924 1.00 70.52  ? 2328 PRO A CB    1 
ATOM   6975  C  CG    . PRO A 1 2328 ? 177.969 183.353 157.274 1.00 70.45  ? 2328 PRO A CG    1 
ATOM   6976  C  CD    . PRO A 1 2328 ? 178.414 184.273 158.356 1.00 66.69  ? 2328 PRO A CD    1 
ATOM   6977  N  N     . ASN A 1 2329 ? 180.718 185.006 155.408 1.00 68.75  ? 2329 ASN A N     1 
ATOM   6978  C  CA    . ASN A 1 2329 ? 181.319 185.484 154.170 1.00 69.92  ? 2329 ASN A CA    1 
ATOM   6979  C  C     . ASN A 1 2329 ? 182.676 186.152 154.381 1.00 75.68  ? 2329 ASN A C     1 
ATOM   6980  O  O     . ASN A 1 2329 ? 183.143 186.873 153.491 1.00 77.02  ? 2329 ASN A O     1 
ATOM   6981  C  CB    . ASN A 1 2329 ? 180.362 186.442 153.455 1.00 71.08  ? 2329 ASN A CB    1 
ATOM   6982  C  CG    . ASN A 1 2329 ? 180.197 187.763 154.184 1.00 82.01  ? 2329 ASN A CG    1 
ATOM   6983  O  OD1   . ASN A 1 2329 ? 180.575 187.900 155.346 1.00 84.09  ? 2329 ASN A OD1   1 
ATOM   6984  N  ND2   . ASN A 1 2329 ? 179.632 188.747 153.496 1.00 86.27  ? 2329 ASN A ND2   1 
ATOM   6985  N  N     . GLY A 1 2330 ? 183.313 185.934 155.530 1.00 76.77  ? 2330 GLY A N     1 
ATOM   6986  C  CA    . GLY A 1 2330 ? 184.611 186.505 155.811 1.00 75.31  ? 2330 GLY A CA    1 
ATOM   6987  C  C     . GLY A 1 2330 ? 184.591 187.909 156.370 1.00 76.37  ? 2330 GLY A C     1 
ATOM   6988  O  O     . GLY A 1 2330 ? 185.655 188.430 156.726 1.00 87.26  ? 2330 GLY A O     1 
ATOM   6989  N  N     . GLU A 1 2331 ? 183.423 188.538 156.461 1.00 80.68  ? 2331 GLU A N     1 
ATOM   6990  C  CA    . GLU A 1 2331 ? 183.324 189.891 156.986 1.00 80.40  ? 2331 GLU A CA    1 
ATOM   6991  C  C     . GLU A 1 2331 ? 183.420 189.886 158.505 1.00 79.32  ? 2331 GLU A C     1 
ATOM   6992  O  O     . GLU A 1 2331 ? 183.070 188.902 159.162 1.00 83.72  ? 2331 GLU A O     1 
ATOM   6993  C  CB    . GLU A 1 2331 ? 182.006 190.532 156.551 1.00 78.13  ? 2331 GLU A CB    1 
ATOM   6994  C  CG    . GLU A 1 2331 ? 182.082 192.029 156.328 1.00 82.30  ? 2331 GLU A CG    1 
ATOM   6995  C  CD    . GLU A 1 2331 ? 180.727 192.635 156.025 1.00 85.62  ? 2331 GLU A CD    1 
ATOM   6996  O  OE1   . GLU A 1 2331 ? 179.832 191.891 155.571 1.00 79.71  ? 2331 GLU A OE1   1 
ATOM   6997  O  OE2   . GLU A 1 2331 ? 180.556 193.853 156.239 1.00 89.98  ? 2331 GLU A OE2   1 
ATOM   6998  N  N     . ARG A 1 2332 ? 183.902 190.995 159.061 1.00 70.71  ? 2332 ARG A N     1 
ATOM   6999  C  CA    . ARG A 1 2332 ? 183.945 191.197 160.503 1.00 71.82  ? 2332 ARG A CA    1 
ATOM   7000  C  C     . ARG A 1 2332 ? 183.496 192.617 160.806 1.00 73.46  ? 2332 ARG A C     1 
ATOM   7001  O  O     . ARG A 1 2332 ? 184.006 193.571 160.210 1.00 79.64  ? 2332 ARG A O     1 
ATOM   7002  C  CB    . ARG A 1 2332 ? 185.346 190.942 161.065 1.00 76.55  ? 2332 ARG A CB    1 
ATOM   7003  C  CG    . ARG A 1 2332 ? 185.655 189.473 161.307 1.00 81.57  ? 2332 ARG A CG    1 
ATOM   7004  C  CD    . ARG A 1 2332 ? 186.401 188.853 160.138 1.00 78.45  ? 2332 ARG A CD    1 
ATOM   7005  N  NE    . ARG A 1 2332 ? 187.588 189.620 159.781 1.00 76.37  ? 2332 ARG A NE    1 
ATOM   7006  C  CZ    . ARG A 1 2332 ? 188.695 189.673 160.510 1.00 80.67  ? 2332 ARG A CZ    1 
ATOM   7007  N  NH1   . ARG A 1 2332 ? 188.811 188.999 161.642 1.00 78.26  ? 2332 ARG A NH1   1 
ATOM   7008  N  NH2   . ARG A 1 2332 ? 189.712 190.419 160.090 1.00 82.70  ? 2332 ARG A NH2   1 
ATOM   7009  N  N     . LEU A 1 2333 ? 182.547 192.755 161.726 1.00 62.33  ? 2333 LEU A N     1 
ATOM   7010  C  CA    . LEU A 1 2333 ? 182.007 194.048 162.123 1.00 64.67  ? 2333 LEU A CA    1 
ATOM   7011  C  C     . LEU A 1 2333 ? 182.520 194.386 163.516 1.00 68.10  ? 2333 LEU A C     1 
ATOM   7012  O  O     . LEU A 1 2333 ? 182.273 193.639 164.469 1.00 71.77  ? 2333 LEU A O     1 
ATOM   7013  C  CB    . LEU A 1 2333 ? 180.478 194.036 162.102 1.00 63.67  ? 2333 LEU A CB    1 
ATOM   7014  C  CG    . LEU A 1 2333 ? 179.784 194.103 160.741 1.00 63.85  ? 2333 LEU A CG    1 
ATOM   7015  C  CD1   . LEU A 1 2333 ? 179.739 192.737 160.084 1.00 67.53  ? 2333 LEU A CD1   1 
ATOM   7016  C  CD2   . LEU A 1 2333 ? 178.383 194.667 160.889 1.00 63.92  ? 2333 LEU A CD2   1 
ATOM   7017  N  N     . SER A 1 2334 ? 183.224 195.508 163.632 1.00 60.85  ? 2334 SER A N     1 
ATOM   7018  C  CA    . SER A 1 2334 ? 183.770 195.930 164.914 1.00 55.00  ? 2334 SER A CA    1 
ATOM   7019  C  C     . SER A 1 2334 ? 182.690 196.612 165.741 1.00 58.76  ? 2334 SER A C     1 
ATOM   7020  O  O     . SER A 1 2334 ? 181.988 197.500 165.249 1.00 69.22  ? 2334 SER A O     1 
ATOM   7021  C  CB    . SER A 1 2334 ? 184.952 196.874 164.705 1.00 57.70  ? 2334 SER A CB    1 
ATOM   7022  O  OG    . SER A 1 2334 ? 185.996 196.234 163.994 1.00 74.89  ? 2334 SER A OG    1 
ATOM   7023  N  N     . LEU A 1 2335 ? 182.559 196.199 166.992 1.00 57.48  ? 2335 LEU A N     1 
ATOM   7024  C  CA    . LEU A 1 2335 ? 181.562 196.791 167.873 1.00 56.19  ? 2335 LEU A CA    1 
ATOM   7025  C  C     . LEU A 1 2335 ? 181.998 198.196 168.269 1.00 61.64  ? 2335 LEU A C     1 
ATOM   7026  O  O     . LEU A 1 2335 ? 183.084 198.358 168.841 1.00 69.91  ? 2335 LEU A O     1 
ATOM   7027  C  CB    . LEU A 1 2335 ? 181.367 195.923 169.111 1.00 46.64  ? 2335 LEU A CB    1 
ATOM   7028  C  CG    . LEU A 1 2335 ? 180.044 196.096 169.857 1.00 50.17  ? 2335 LEU A CG    1 
ATOM   7029  C  CD1   . LEU A 1 2335 ? 178.928 195.370 169.128 1.00 55.48  ? 2335 LEU A CD1   1 
ATOM   7030  C  CD2   . LEU A 1 2335 ? 180.166 195.597 171.285 1.00 53.10  ? 2335 LEU A CD2   1 
ATOM   7031  N  N     . PRO A 1 2336 ? 181.204 199.230 167.984 1.00 50.45  ? 2336 PRO A N     1 
ATOM   7032  C  CA    . PRO A 1 2336 ? 181.603 200.580 168.370 1.00 45.45  ? 2336 PRO A CA    1 
ATOM   7033  C  C     . PRO A 1 2336 ? 181.629 200.724 169.880 1.00 51.14  ? 2336 PRO A C     1 
ATOM   7034  O  O     . PRO A 1 2336 ? 180.923 199.996 170.600 1.00 66.81  ? 2336 PRO A O     1 
ATOM   7035  C  CB    . PRO A 1 2336 ? 180.514 201.465 167.739 1.00 52.65  ? 2336 PRO A CB    1 
ATOM   7036  C  CG    . PRO A 1 2336 ? 179.909 200.625 166.665 1.00 53.66  ? 2336 PRO A CG    1 
ATOM   7037  C  CD    . PRO A 1 2336 ? 179.975 199.223 167.176 1.00 52.27  ? 2336 PRO A CD    1 
ATOM   7038  N  N     . PRO A 1 2337 ? 182.440 201.642 170.410 1.00 56.40  ? 2337 PRO A N     1 
ATOM   7039  C  CA    . PRO A 1 2337 ? 182.525 201.794 171.872 1.00 62.81  ? 2337 PRO A CA    1 
ATOM   7040  C  C     . PRO A 1 2337 ? 181.230 202.244 172.525 1.00 62.74  ? 2337 PRO A C     1 
ATOM   7041  O  O     . PRO A 1 2337 ? 181.071 202.057 173.737 1.00 64.86  ? 2337 PRO A O     1 
ATOM   7042  C  CB    . PRO A 1 2337 ? 183.633 202.840 172.052 1.00 62.45  ? 2337 PRO A CB    1 
ATOM   7043  C  CG    . PRO A 1 2337 ? 183.673 203.579 170.756 1.00 64.96  ? 2337 PRO A CG    1 
ATOM   7044  C  CD    . PRO A 1 2337 ? 183.338 202.569 169.703 1.00 63.84  ? 2337 PRO A CD    1 
ATOM   7045  N  N     . ASN A 1 2338 ? 180.303 202.831 171.773 1.00 59.14  ? 2338 ASN A N     1 
ATOM   7046  C  CA    . ASN A 1 2338 ? 179.056 203.336 172.331 1.00 54.81  ? 2338 ASN A CA    1 
ATOM   7047  C  C     . ASN A 1 2338 ? 177.912 202.336 172.247 1.00 56.70  ? 2338 ASN A C     1 
ATOM   7048  O  O     . ASN A 1 2338 ? 176.783 202.680 172.611 1.00 69.84  ? 2338 ASN A O     1 
ATOM   7049  C  CB    . ASN A 1 2338 ? 178.652 204.633 171.624 1.00 61.57  ? 2338 ASN A CB    1 
ATOM   7050  C  CG    . ASN A 1 2338 ? 178.328 204.421 170.161 1.00 68.72  ? 2338 ASN A CG    1 
ATOM   7051  O  OD1   . ASN A 1 2338 ? 179.178 203.998 169.380 1.00 74.70  ? 2338 ASN A OD1   1 
ATOM   7052  N  ND2   . ASN A 1 2338 ? 177.090 204.712 169.780 1.00 66.02  ? 2338 ASN A ND2   1 
ATOM   7053  N  N     . VAL A 1 2339 ? 178.167 201.116 171.784 1.00 41.37  ? 2339 VAL A N     1 
ATOM   7054  C  CA    . VAL A 1 2339 ? 177.134 200.100 171.620 1.00 43.23  ? 2339 VAL A CA    1 
ATOM   7055  C  C     . VAL A 1 2339 ? 177.228 199.112 172.773 1.00 53.10  ? 2339 VAL A C     1 
ATOM   7056  O  O     . VAL A 1 2339 ? 178.318 198.631 173.103 1.00 67.28  ? 2339 VAL A O     1 
ATOM   7057  C  CB    . VAL A 1 2339 ? 177.269 199.382 170.268 1.00 48.57  ? 2339 VAL A CB    1 
ATOM   7058  C  CG1   . VAL A 1 2339 ? 176.224 198.287 170.139 1.00 54.22  ? 2339 VAL A CG1   1 
ATOM   7059  C  CG2   . VAL A 1 2339 ? 177.138 200.376 169.136 1.00 55.98  ? 2339 VAL A CG2   1 
ATOM   7060  N  N     . ARG A 1 2340 ? 176.087 198.813 173.385 1.00 52.49  ? 2340 ARG A N     1 
ATOM   7061  C  CA    . ARG A 1 2340 ? 175.995 197.847 174.470 1.00 53.22  ? 2340 ARG A CA    1 
ATOM   7062  C  C     . ARG A 1 2340 ? 175.048 196.729 174.063 1.00 56.13  ? 2340 ARG A C     1 
ATOM   7063  O  O     . ARG A 1 2340 ? 173.963 196.992 173.535 1.00 65.68  ? 2340 ARG A O     1 
ATOM   7064  C  CB    . ARG A 1 2340 ? 175.502 198.511 175.756 1.00 55.37  ? 2340 ARG A CB    1 
ATOM   7065  C  CG    . ARG A 1 2340 ? 176.448 199.546 176.332 1.00 52.37  ? 2340 ARG A CG    1 
ATOM   7066  C  CD    . ARG A 1 2340 ? 177.662 198.892 176.962 1.00 55.17  ? 2340 ARG A CD    1 
ATOM   7067  N  NE    . ARG A 1 2340 ? 178.533 199.867 177.605 1.00 63.76  ? 2340 ARG A NE    1 
ATOM   7068  C  CZ    . ARG A 1 2340 ? 179.428 200.608 176.967 1.00 57.51  ? 2340 ARG A CZ    1 
ATOM   7069  N  NH1   . ARG A 1 2340 ? 179.601 200.509 175.660 1.00 57.46  ? 2340 ARG A NH1   1 
ATOM   7070  N  NH2   . ARG A 1 2340 ? 180.167 201.470 177.658 1.00 59.10  ? 2340 ARG A NH2   1 
ATOM   7071  N  N     . ILE A 1 2341 ? 175.458 195.488 174.306 1.00 44.09  ? 2341 ILE A N     1 
ATOM   7072  C  CA    . ILE A 1 2341 ? 174.624 194.320 174.052 1.00 43.66  ? 2341 ILE A CA    1 
ATOM   7073  C  C     . ILE A 1 2341 ? 174.004 193.899 175.375 1.00 43.18  ? 2341 ILE A C     1 
ATOM   7074  O  O     . ILE A 1 2341 ? 174.720 193.595 176.336 1.00 60.21  ? 2341 ILE A O     1 
ATOM   7075  C  CB    . ILE A 1 2341 ? 175.432 193.173 173.427 1.00 40.96  ? 2341 ILE A CB    1 
ATOM   7076  C  CG1   . ILE A 1 2341 ? 176.339 193.698 172.315 1.00 42.38  ? 2341 ILE A CG1   1 
ATOM   7077  C  CG2   . ILE A 1 2341 ? 174.500 192.103 172.885 1.00 31.11  ? 2341 ILE A CG2   1 
ATOM   7078  C  CD1   . ILE A 1 2341 ? 175.592 194.305 171.154 1.00 44.50  ? 2341 ILE A CD1   1 
ATOM   7079  N  N     . MET A 1 2342 ? 172.678 193.881 175.431 1.00 39.19  ? 2342 MET A N     1 
ATOM   7080  C  CA    . MET A 1 2342 ? 171.949 193.560 176.648 1.00 44.95  ? 2342 MET A CA    1 
ATOM   7081  C  C     . MET A 1 2342 ? 171.063 192.347 176.413 1.00 49.80  ? 2342 MET A C     1 
ATOM   7082  O  O     . MET A 1 2342 ? 170.447 192.212 175.353 1.00 65.48  ? 2342 MET A O     1 
ATOM   7083  C  CB    . MET A 1 2342 ? 171.097 194.745 177.105 1.00 51.92  ? 2342 MET A CB    1 
ATOM   7084  C  CG    . MET A 1 2342 ? 171.839 196.067 177.136 1.00 52.77  ? 2342 MET A CG    1 
ATOM   7085  S  SD    . MET A 1 2342 ? 171.175 197.191 178.374 1.00 69.79  ? 2342 MET A SD    1 
ATOM   7086  C  CE    . MET A 1 2342 ? 172.118 196.698 179.811 1.00 60.06  ? 2342 MET A CE    1 
ATOM   7087  N  N     . PHE A 1 2343 ? 171.008 191.464 177.405 1.00 38.72  ? 2343 PHE A N     1 
ATOM   7088  C  CA    . PHE A 1 2343 ? 170.138 190.293 177.375 1.00 43.07  ? 2343 PHE A CA    1 
ATOM   7089  C  C     . PHE A 1 2343 ? 169.173 190.402 178.547 1.00 54.77  ? 2343 PHE A C     1 
ATOM   7090  O  O     . PHE A 1 2343 ? 169.599 190.425 179.706 1.00 73.74  ? 2343 PHE A O     1 
ATOM   7091  C  CB    . PHE A 1 2343 ? 170.940 188.995 177.460 1.00 43.07  ? 2343 PHE A CB    1 
ATOM   7092  C  CG    . PHE A 1 2343 ? 171.930 188.810 176.348 1.00 50.96  ? 2343 PHE A CG    1 
ATOM   7093  C  CD1   . PHE A 1 2343 ? 173.193 189.368 176.428 1.00 53.53  ? 2343 PHE A CD1   1 
ATOM   7094  C  CD2   . PHE A 1 2343 ? 171.607 188.061 175.232 1.00 51.59  ? 2343 PHE A CD2   1 
ATOM   7095  C  CE1   . PHE A 1 2343 ? 174.109 189.194 175.414 1.00 47.55  ? 2343 PHE A CE1   1 
ATOM   7096  C  CE2   . PHE A 1 2343 ? 172.521 187.884 174.215 1.00 55.04  ? 2343 PHE A CE2   1 
ATOM   7097  C  CZ    . PHE A 1 2343 ? 173.772 188.451 174.306 1.00 52.24  ? 2343 PHE A CZ    1 
ATOM   7098  N  N     . GLU A 1 2344 ? 167.881 190.472 178.251 1.00 48.60  ? 2344 GLU A N     1 
ATOM   7099  C  CA    . GLU A 1 2344 ? 166.846 190.474 179.277 1.00 45.09  ? 2344 GLU A CA    1 
ATOM   7100  C  C     . GLU A 1 2344 ? 166.196 189.097 179.285 1.00 54.47  ? 2344 GLU A C     1 
ATOM   7101  O  O     . GLU A 1 2344 ? 165.292 188.825 178.490 1.00 73.10  ? 2344 GLU A O     1 
ATOM   7102  C  CB    . GLU A 1 2344 ? 165.819 191.573 179.020 1.00 44.42  ? 2344 GLU A CB    1 
ATOM   7103  C  CG    . GLU A 1 2344 ? 164.665 191.575 180.001 1.00 50.34  ? 2344 GLU A CG    1 
ATOM   7104  C  CD    . GLU A 1 2344 ? 163.658 192.662 179.704 1.00 58.75  ? 2344 GLU A CD    1 
ATOM   7105  O  OE1   . GLU A 1 2344 ? 164.067 193.836 179.595 1.00 65.09  ? 2344 GLU A OE1   1 
ATOM   7106  O  OE2   . GLU A 1 2344 ? 162.455 192.348 179.582 1.00 51.06  ? 2344 GLU A OE2   1 
ATOM   7107  N  N     . VAL A 1 2345 ? 166.660 188.230 180.183 1.00 45.09  ? 2345 VAL A N     1 
ATOM   7108  C  CA    . VAL A 1 2345 ? 166.213 186.847 180.236 1.00 47.39  ? 2345 VAL A CA    1 
ATOM   7109  C  C     . VAL A 1 2345 ? 165.609 186.579 181.606 1.00 59.41  ? 2345 VAL A C     1 
ATOM   7110  O  O     . VAL A 1 2345 ? 165.889 187.275 182.583 1.00 72.71  ? 2345 VAL A O     1 
ATOM   7111  C  CB    . VAL A 1 2345 ? 167.360 185.857 179.953 1.00 50.63  ? 2345 VAL A CB    1 
ATOM   7112  C  CG1   . VAL A 1 2345 ? 167.952 186.118 178.585 1.00 60.03  ? 2345 VAL A CG1   1 
ATOM   7113  C  CG2   . VAL A 1 2345 ? 168.427 185.969 181.022 1.00 51.70  ? 2345 VAL A CG2   1 
ATOM   7114  N  N     . GLN A 1 2346 ? 164.765 185.550 181.666 1.00 64.30  ? 2346 GLN A N     1 
ATOM   7115  C  CA    . GLN A 1 2346 ? 164.163 185.146 182.927 1.00 66.25  ? 2346 GLN A CA    1 
ATOM   7116  C  C     . GLN A 1 2346 ? 164.955 184.067 183.649 1.00 67.77  ? 2346 GLN A C     1 
ATOM   7117  O  O     . GLN A 1 2346 ? 164.953 184.047 184.883 1.00 74.09  ? 2346 GLN A O     1 
ATOM   7118  C  CB    . GLN A 1 2346 ? 162.724 184.665 182.704 1.00 63.58  ? 2346 GLN A CB    1 
ATOM   7119  C  CG    . GLN A 1 2346 ? 162.599 183.377 181.917 1.00 69.59  ? 2346 GLN A CG    1 
ATOM   7120  C  CD    . GLN A 1 2346 ? 161.228 182.751 182.050 1.00 79.67  ? 2346 GLN A CD    1 
ATOM   7121  O  OE1   . GLN A 1 2346 ? 160.476 183.070 182.970 1.00 74.88  ? 2346 GLN A OE1   1 
ATOM   7122  N  NE2   . GLN A 1 2346 ? 160.892 181.858 181.127 1.00 79.95  ? 2346 GLN A NE2   1 
ATOM   7123  N  N     . ASP A 1 2347 ? 165.647 183.200 182.915 1.00 76.49  ? 2347 ASP A N     1 
ATOM   7124  C  CA    . ASP A 1 2347 ? 166.501 182.166 183.483 1.00 72.79  ? 2347 ASP A CA    1 
ATOM   7125  C  C     . ASP A 1 2347 ? 167.641 181.907 182.512 1.00 75.51  ? 2347 ASP A C     1 
ATOM   7126  O  O     . ASP A 1 2347 ? 167.565 182.253 181.331 1.00 86.10  ? 2347 ASP A O     1 
ATOM   7127  C  CB    . ASP A 1 2347 ? 165.729 180.868 183.761 1.00 80.36  ? 2347 ASP A CB    1 
ATOM   7128  C  CG    . ASP A 1 2347 ? 165.340 180.708 185.223 1.00 91.40  ? 2347 ASP A CG    1 
ATOM   7129  O  OD1   . ASP A 1 2347 ? 165.342 181.707 185.969 1.00 91.71  ? 2347 ASP A OD1   1 
ATOM   7130  O  OD2   . ASP A 1 2347 ? 165.027 179.569 185.630 1.00 93.51  ? 2347 ASP A OD2   1 
ATOM   7131  N  N     . LEU A 1 2348 ? 168.703 181.293 183.029 1.00 67.43  ? 2348 LEU A N     1 
ATOM   7132  C  CA    . LEU A 1 2348 ? 169.868 180.941 182.227 1.00 70.30  ? 2348 LEU A CA    1 
ATOM   7133  C  C     . LEU A 1 2348 ? 170.110 179.438 182.260 1.00 71.73  ? 2348 LEU A C     1 
ATOM   7134  O  O     . LEU A 1 2348 ? 171.256 178.985 182.299 1.00 74.14  ? 2348 LEU A O     1 
ATOM   7135  C  CB    . LEU A 1 2348 ? 171.108 181.695 182.704 1.00 69.74  ? 2348 LEU A CB    1 
ATOM   7136  C  CG    . LEU A 1 2348 ? 171.519 182.923 181.892 1.00 61.50  ? 2348 LEU A CG    1 
ATOM   7137  C  CD1   . LEU A 1 2348 ? 172.879 183.425 182.342 1.00 67.36  ? 2348 LEU A CD1   1 
ATOM   7138  C  CD2   . LEU A 1 2348 ? 171.519 182.616 180.408 1.00 60.39  ? 2348 LEU A CD2   1 
ATOM   7139  N  N     . LYS A 1 2349 ? 169.032 178.652 182.248 1.00 83.32  ? 2349 LYS A N     1 
ATOM   7140  C  CA    . LYS A 1 2349 ? 169.129 177.210 182.428 1.00 86.18  ? 2349 LYS A CA    1 
ATOM   7141  C  C     . LYS A 1 2349 ? 169.726 176.492 181.225 1.00 81.97  ? 2349 LYS A C     1 
ATOM   7142  O  O     . LYS A 1 2349 ? 170.190 175.357 181.375 1.00 87.45  ? 2349 LYS A O     1 
ATOM   7143  C  CB    . LYS A 1 2349 ? 167.742 176.640 182.740 1.00 83.61  ? 2349 LYS A CB    1 
ATOM   7144  C  CG    . LYS A 1 2349 ? 167.750 175.243 183.339 1.00 86.68  ? 2349 LYS A CG    1 
ATOM   7145  C  CD    . LYS A 1 2349 ? 166.569 175.038 184.273 1.00 88.13  ? 2349 LYS A CD    1 
ATOM   7146  C  CE    . LYS A 1 2349 ? 165.421 174.338 183.567 1.00 89.97  ? 2349 LYS A CE    1 
ATOM   7147  N  NZ    . LYS A 1 2349 ? 165.566 172.857 183.612 1.00 90.36  ? 2349 LYS A NZ    1 
ATOM   7148  N  N     . TYR A 1 2350 ? 169.743 177.117 180.048 1.00 72.04  ? 2350 TYR A N     1 
ATOM   7149  C  CA    . TYR A 1 2350 ? 170.165 176.436 178.833 1.00 82.35  ? 2350 TYR A CA    1 
ATOM   7150  C  C     . TYR A 1 2350 ? 171.442 176.992 178.220 1.00 85.25  ? 2350 TYR A C     1 
ATOM   7151  O  O     . TYR A 1 2350 ? 172.011 176.345 177.335 1.00 82.55  ? 2350 TYR A O     1 
ATOM   7152  C  CB    . TYR A 1 2350 ? 169.040 176.477 177.789 1.00 77.84  ? 2350 TYR A CB    1 
ATOM   7153  C  CG    . TYR A 1 2350 ? 167.860 175.607 178.154 1.00 82.30  ? 2350 TYR A CG    1 
ATOM   7154  C  CD1   . TYR A 1 2350 ? 167.938 174.225 178.062 1.00 79.20  ? 2350 TYR A CD1   1 
ATOM   7155  C  CD2   . TYR A 1 2350 ? 166.675 176.168 178.607 1.00 84.69  ? 2350 TYR A CD2   1 
ATOM   7156  C  CE1   . TYR A 1 2350 ? 166.864 173.426 178.399 1.00 79.90  ? 2350 TYR A CE1   1 
ATOM   7157  C  CE2   . TYR A 1 2350 ? 165.596 175.377 178.949 1.00 80.68  ? 2350 TYR A CE2   1 
ATOM   7158  C  CZ    . TYR A 1 2350 ? 165.696 174.008 178.843 1.00 80.61  ? 2350 TYR A CZ    1 
ATOM   7159  O  OH    . TYR A 1 2350 ? 164.623 173.217 179.182 1.00 83.99  ? 2350 TYR A OH    1 
ATOM   7160  N  N     . ALA A 1 2351 ? 171.909 178.158 178.656 1.00 77.95  ? 2351 ALA A N     1 
ATOM   7161  C  CA    . ALA A 1 2351 ? 173.148 178.701 178.122 1.00 68.93  ? 2351 ALA A CA    1 
ATOM   7162  C  C     . ALA A 1 2351 ? 174.354 178.015 178.754 1.00 71.21  ? 2351 ALA A C     1 
ATOM   7163  O  O     . ALA A 1 2351 ? 174.343 177.641 179.930 1.00 72.15  ? 2351 ALA A O     1 
ATOM   7164  C  CB    . ALA A 1 2351 ? 173.221 180.208 178.360 1.00 65.95  ? 2351 ALA A CB    1 
ATOM   7165  N  N     . THR A 1 2352 ? 175.405 177.854 177.955 1.00 72.71  ? 2352 THR A N     1 
ATOM   7166  C  CA    . THR A 1 2352 ? 176.624 177.206 178.407 1.00 67.83  ? 2352 THR A CA    1 
ATOM   7167  C  C     . THR A 1 2352 ? 177.474 178.185 179.214 1.00 69.05  ? 2352 THR A C     1 
ATOM   7168  O  O     . THR A 1 2352 ? 177.140 179.362 179.369 1.00 74.55  ? 2352 THR A O     1 
ATOM   7169  C  CB    . THR A 1 2352 ? 177.407 176.655 177.217 1.00 67.66  ? 2352 THR A CB    1 
ATOM   7170  O  OG1   . THR A 1 2352 ? 177.624 177.699 176.261 1.00 68.12  ? 2352 THR A OG1   1 
ATOM   7171  C  CG2   . THR A 1 2352 ? 176.638 175.524 176.556 1.00 70.22  ? 2352 THR A CG2   1 
ATOM   7172  N  N     . LEU A 1 2353 ? 178.598 177.691 179.739 1.00 68.96  ? 2353 LEU A N     1 
ATOM   7173  C  CA    . LEU A 1 2353 ? 179.475 178.544 180.532 1.00 68.76  ? 2353 LEU A CA    1 
ATOM   7174  C  C     . LEU A 1 2353 ? 180.196 179.570 179.668 1.00 70.68  ? 2353 LEU A C     1 
ATOM   7175  O  O     . LEU A 1 2353 ? 180.719 180.560 180.191 1.00 72.65  ? 2353 LEU A O     1 
ATOM   7176  C  CB    . LEU A 1 2353 ? 180.486 177.693 181.299 1.00 73.14  ? 2353 LEU A CB    1 
ATOM   7177  C  CG    . LEU A 1 2353 ? 180.986 178.245 182.637 1.00 76.72  ? 2353 LEU A CG    1 
ATOM   7178  C  CD1   . LEU A 1 2353 ? 179.936 179.127 183.296 1.00 73.98  ? 2353 LEU A CD1   1 
ATOM   7179  C  CD2   . LEU A 1 2353 ? 181.394 177.111 183.564 1.00 78.91  ? 2353 LEU A CD2   1 
ATOM   7180  N  N     . ALA A 1 2354 ? 180.247 179.348 178.352 1.00 65.81  ? 2354 ALA A N     1 
ATOM   7181  C  CA    . ALA A 1 2354 ? 180.883 180.317 177.466 1.00 61.19  ? 2354 ALA A CA    1 
ATOM   7182  C  C     . ALA A 1 2354 ? 180.120 181.635 177.450 1.00 63.37  ? 2354 ALA A C     1 
ATOM   7183  O  O     . ALA A 1 2354 ? 180.726 182.711 177.497 1.00 74.36  ? 2354 ALA A O     1 
ATOM   7184  C  CB    . ALA A 1 2354 ? 180.994 179.743 176.055 1.00 62.29  ? 2354 ALA A CB    1 
ATOM   7185  N  N     . THR A 1 2355 ? 178.789 181.571 177.383 1.00 62.59  ? 2355 THR A N     1 
ATOM   7186  C  CA    . THR A 1 2355 ? 177.994 182.794 177.344 1.00 65.24  ? 2355 THR A CA    1 
ATOM   7187  C  C     . THR A 1 2355 ? 177.893 183.438 178.721 1.00 64.61  ? 2355 THR A C     1 
ATOM   7188  O  O     . THR A 1 2355 ? 177.927 184.668 178.840 1.00 71.37  ? 2355 THR A O     1 
ATOM   7189  C  CB    . THR A 1 2355 ? 176.601 182.497 176.792 1.00 65.44  ? 2355 THR A CB    1 
ATOM   7190  O  OG1   . THR A 1 2355 ? 176.718 181.739 175.583 1.00 67.18  ? 2355 THR A OG1   1 
ATOM   7191  C  CG2   . THR A 1 2355 ? 175.863 183.791 176.501 1.00 63.48  ? 2355 THR A CG2   1 
ATOM   7192  N  N     . VAL A 1 2356 ? 177.766 182.626 179.772 1.00 59.73  ? 2356 VAL A N     1 
ATOM   7193  C  CA    . VAL A 1 2356 ? 177.586 183.170 181.114 1.00 56.53  ? 2356 VAL A CA    1 
ATOM   7194  C  C     . VAL A 1 2356 ? 178.823 183.941 181.555 1.00 63.19  ? 2356 VAL A C     1 
ATOM   7195  O  O     . VAL A 1 2356 ? 178.719 184.996 182.192 1.00 68.68  ? 2356 VAL A O     1 
ATOM   7196  C  CB    . VAL A 1 2356 ? 177.238 182.042 182.102 1.00 63.60  ? 2356 VAL A CB    1 
ATOM   7197  C  CG1   . VAL A 1 2356 ? 177.087 182.594 183.508 1.00 67.67  ? 2356 VAL A CG1   1 
ATOM   7198  C  CG2   . VAL A 1 2356 ? 175.966 181.336 181.668 1.00 61.19  ? 2356 VAL A CG2   1 
ATOM   7199  N  N     . SER A 1 2357 ? 180.012 183.437 181.220 1.00 62.07  ? 2357 SER A N     1 
ATOM   7200  C  CA    . SER A 1 2357 ? 181.239 184.097 181.645 1.00 56.66  ? 2357 SER A CA    1 
ATOM   7201  C  C     . SER A 1 2357 ? 181.525 185.367 180.858 1.00 63.82  ? 2357 SER A C     1 
ATOM   7202  O  O     . SER A 1 2357 ? 182.295 186.211 181.328 1.00 73.60  ? 2357 SER A O     1 
ATOM   7203  C  CB    . SER A 1 2357 ? 182.422 183.137 181.518 1.00 57.23  ? 2357 SER A CB    1 
ATOM   7204  O  OG    . SER A 1 2357 ? 182.604 182.734 180.173 1.00 68.17  ? 2357 SER A OG    1 
ATOM   7205  N  N     . ARG A 1 2358 ? 180.924 185.528 179.682 1.00 60.29  ? 2358 ARG A N     1 
ATOM   7206  C  CA    . ARG A 1 2358 ? 181.234 186.636 178.791 1.00 60.57  ? 2358 ARG A CA    1 
ATOM   7207  C  C     . ARG A 1 2358 ? 180.463 187.910 179.121 1.00 61.23  ? 2358 ARG A C     1 
ATOM   7208  O  O     . ARG A 1 2358 ? 180.822 188.979 178.618 1.00 63.08  ? 2358 ARG A O     1 
ATOM   7209  C  CB    . ARG A 1 2358 ? 180.956 186.229 177.342 1.00 62.48  ? 2358 ARG A CB    1 
ATOM   7210  C  CG    . ARG A 1 2358 ? 182.200 185.931 176.527 1.00 57.02  ? 2358 ARG A CG    1 
ATOM   7211  C  CD    . ARG A 1 2358 ? 181.899 184.930 175.425 1.00 55.54  ? 2358 ARG A CD    1 
ATOM   7212  N  NE    . ARG A 1 2358 ? 183.074 184.625 174.620 1.00 61.60  ? 2358 ARG A NE    1 
ATOM   7213  C  CZ    . ARG A 1 2358 ? 183.827 183.545 174.773 1.00 70.35  ? 2358 ARG A CZ    1 
ATOM   7214  N  NH1   . ARG A 1 2358 ? 183.558 182.641 175.700 1.00 65.67  ? 2358 ARG A NH1   1 
ATOM   7215  N  NH2   . ARG A 1 2358 ? 184.877 183.367 173.977 1.00 70.13  ? 2358 ARG A NH2   1 
ATOM   7216  N  N     . CYS A 1 2359 ? 179.426 187.828 179.951 1.00 60.27  ? 2359 CYS A N     1 
ATOM   7217  C  CA    . CYS A 1 2359 ? 178.571 188.980 180.211 1.00 59.54  ? 2359 CYS A CA    1 
ATOM   7218  C  C     . CYS A 1 2359 ? 178.486 189.245 181.705 1.00 66.64  ? 2359 CYS A C     1 
ATOM   7219  O  O     . CYS A 1 2359 ? 178.356 188.307 182.496 1.00 70.57  ? 2359 CYS A O     1 
ATOM   7220  C  CB    . CYS A 1 2359 ? 177.165 188.760 179.645 1.00 64.27  ? 2359 CYS A CB    1 
ATOM   7221  S  SG    . CYS A 1 2359 ? 177.030 188.962 177.861 1.00 88.45  ? 2359 CYS A SG    1 
ATOM   7222  N  N     . GLY A 1 2360 ? 178.561 190.519 182.082 1.00 65.57  ? 2360 GLY A N     1 
ATOM   7223  C  CA    . GLY A 1 2360 ? 178.237 190.892 183.444 1.00 64.47  ? 2360 GLY A CA    1 
ATOM   7224  C  C     . GLY A 1 2360 ? 176.760 190.697 183.729 1.00 66.21  ? 2360 GLY A C     1 
ATOM   7225  O  O     . GLY A 1 2360 ? 175.901 190.962 182.887 1.00 70.99  ? 2360 GLY A O     1 
ATOM   7226  N  N     . MET A 1 2361 ? 176.462 190.229 184.937 1.00 58.25  ? 2361 MET A N     1 
ATOM   7227  C  CA    . MET A 1 2361 ? 175.114 189.821 185.302 1.00 53.45  ? 2361 MET A CA    1 
ATOM   7228  C  C     . MET A 1 2361 ? 174.550 190.760 186.356 1.00 58.51  ? 2361 MET A C     1 
ATOM   7229  O  O     . MET A 1 2361 ? 175.273 191.197 187.257 1.00 76.68  ? 2361 MET A O     1 
ATOM   7230  C  CB    . MET A 1 2361 ? 175.101 188.386 185.831 1.00 53.66  ? 2361 MET A CB    1 
ATOM   7231  C  CG    . MET A 1 2361 ? 175.742 187.380 184.902 1.00 62.28  ? 2361 MET A CG    1 
ATOM   7232  S  SD    . MET A 1 2361 ? 174.548 186.541 183.852 1.00 72.98  ? 2361 MET A SD    1 
ATOM   7233  C  CE    . MET A 1 2361 ? 175.632 185.942 182.562 1.00 63.17  ? 2361 MET A CE    1 
ATOM   7234  N  N     . VAL A 1 2362 ? 173.261 191.068 186.235 1.00 45.18  ? 2362 VAL A N     1 
ATOM   7235  C  CA    . VAL A 1 2362 ? 172.499 191.745 187.277 1.00 46.41  ? 2362 VAL A CA    1 
ATOM   7236  C  C     . VAL A 1 2362 ? 171.277 190.885 187.564 1.00 49.50  ? 2362 VAL A C     1 
ATOM   7237  O  O     . VAL A 1 2362 ? 170.426 190.698 186.686 1.00 61.85  ? 2362 VAL A O     1 
ATOM   7238  C  CB    . VAL A 1 2362 ? 172.086 193.166 186.864 1.00 47.13  ? 2362 VAL A CB    1 
ATOM   7239  C  CG1   . VAL A 1 2362 ? 171.655 193.962 188.082 1.00 49.80  ? 2362 VAL A CG1   1 
ATOM   7240  C  CG2   . VAL A 1 2362 ? 173.224 193.867 186.144 1.00 52.01  ? 2362 VAL A CG2   1 
ATOM   7241  N  N     . TRP A 1 2363 ? 171.190 190.362 188.782 1.00 41.19  ? 2363 TRP A N     1 
ATOM   7242  C  CA    . TRP A 1 2363 ? 170.137 189.429 189.157 1.00 39.50  ? 2363 TRP A CA    1 
ATOM   7243  C  C     . TRP A 1 2363 ? 168.994 190.188 189.816 1.00 57.46  ? 2363 TRP A C     1 
ATOM   7244  O  O     . TRP A 1 2363 ? 169.182 190.814 190.865 1.00 65.32  ? 2363 TRP A O     1 
ATOM   7245  C  CB    . TRP A 1 2363 ? 170.673 188.347 190.093 1.00 53.34  ? 2363 TRP A CB    1 
ATOM   7246  C  CG    . TRP A 1 2363 ? 169.598 187.519 190.723 1.00 56.66  ? 2363 TRP A CG    1 
ATOM   7247  C  CD1   . TRP A 1 2363 ? 169.116 187.633 191.992 1.00 61.01  ? 2363 TRP A CD1   1 
ATOM   7248  C  CD2   . TRP A 1 2363 ? 168.868 186.450 190.111 1.00 50.74  ? 2363 TRP A CD2   1 
ATOM   7249  N  NE1   . TRP A 1 2363 ? 168.131 186.702 192.210 1.00 59.98  ? 2363 TRP A NE1   1 
ATOM   7250  C  CE2   . TRP A 1 2363 ? 167.960 185.963 191.070 1.00 53.15  ? 2363 TRP A CE2   1 
ATOM   7251  C  CE3   . TRP A 1 2363 ? 168.894 185.858 188.846 1.00 58.57  ? 2363 TRP A CE3   1 
ATOM   7252  C  CZ2   . TRP A 1 2363 ? 167.087 184.912 190.804 1.00 58.52  ? 2363 TRP A CZ2   1 
ATOM   7253  C  CZ3   . TRP A 1 2363 ? 168.026 184.816 188.584 1.00 56.83  ? 2363 TRP A CZ3   1 
ATOM   7254  C  CH2   . TRP A 1 2363 ? 167.136 184.353 189.558 1.00 57.38  ? 2363 TRP A CH2   1 
ATOM   7255  N  N     . PHE A 1 2364 ? 167.816 190.129 189.202 1.00 50.02  ? 2364 PHE A N     1 
ATOM   7256  C  CA    . PHE A 1 2364 ? 166.616 190.767 189.727 1.00 43.14  ? 2364 PHE A CA    1 
ATOM   7257  C  C     . PHE A 1 2364 ? 165.717 189.702 190.341 1.00 48.73  ? 2364 PHE A C     1 
ATOM   7258  O  O     . PHE A 1 2364 ? 165.170 188.860 189.623 1.00 64.29  ? 2364 PHE A O     1 
ATOM   7259  C  CB    . PHE A 1 2364 ? 165.864 191.513 188.627 1.00 41.94  ? 2364 PHE A CB    1 
ATOM   7260  C  CG    . PHE A 1 2364 ? 166.581 192.723 188.102 1.00 34.94  ? 2364 PHE A CG    1 
ATOM   7261  C  CD1   . PHE A 1 2364 ? 167.661 192.591 187.249 1.00 38.06  ? 2364 PHE A CD1   1 
ATOM   7262  C  CD2   . PHE A 1 2364 ? 166.158 193.993 188.445 1.00 44.45  ? 2364 PHE A CD2   1 
ATOM   7263  C  CE1   . PHE A 1 2364 ? 168.312 193.704 186.760 1.00 46.04  ? 2364 PHE A CE1   1 
ATOM   7264  C  CE2   . PHE A 1 2364 ? 166.804 195.108 187.958 1.00 51.55  ? 2364 PHE A CE2   1 
ATOM   7265  C  CZ    . PHE A 1 2364 ? 167.883 194.964 187.116 1.00 54.20  ? 2364 PHE A CZ    1 
ATOM   7266  N  N     . SER A 1 2365 ? 165.553 189.746 191.657 1.00 60.04  ? 2365 SER A N     1 
ATOM   7267  C  CA    . SER A 1 2365 ? 164.657 188.835 192.350 1.00 67.14  ? 2365 SER A CA    1 
ATOM   7268  C  C     . SER A 1 2365 ? 163.241 189.396 192.347 1.00 70.17  ? 2365 SER A C     1 
ATOM   7269  O  O     . SER A 1 2365 ? 163.020 190.583 192.096 1.00 73.62  ? 2365 SER A O     1 
ATOM   7270  C  CB    . SER A 1 2365 ? 165.129 188.595 193.786 1.00 67.75  ? 2365 SER A CB    1 
ATOM   7271  O  OG    . SER A 1 2365 ? 166.543 188.582 193.861 1.00 65.43  ? 2365 SER A OG    1 
ATOM   7272  N  N     . GLU A 1 2366 ? 162.272 188.522 192.622 1.00 79.54  ? 2366 GLU A N     1 
ATOM   7273  C  CA    . GLU A 1 2366 ? 160.887 188.973 192.679 1.00 82.32  ? 2366 GLU A CA    1 
ATOM   7274  C  C     . GLU A 1 2366 ? 160.622 189.870 193.879 1.00 87.19  ? 2366 GLU A C     1 
ATOM   7275  O  O     . GLU A 1 2366 ? 159.596 190.557 193.907 1.00 89.81  ? 2366 GLU A O     1 
ATOM   7276  C  CB    . GLU A 1 2366 ? 159.934 187.779 192.695 1.00 85.97  ? 2366 GLU A CB    1 
ATOM   7277  C  CG    . GLU A 1 2366 ? 159.986 186.938 191.433 1.00 88.53  ? 2366 GLU A CG    1 
ATOM   7278  C  CD    . GLU A 1 2366 ? 158.609 186.525 190.952 1.00 92.15  ? 2366 GLU A CD    1 
ATOM   7279  O  OE1   . GLU A 1 2366 ? 157.730 187.405 190.841 1.00 91.97  ? 2366 GLU A OE1   1 
ATOM   7280  O  OE2   . GLU A 1 2366 ? 158.406 185.323 190.683 1.00 89.70  ? 2366 GLU A OE2   1 
ATOM   7281  N  N     . ASP A 1 2367 ? 161.519 189.882 194.866 1.00 85.05  ? 2367 ASP A N     1 
ATOM   7282  C  CA    . ASP A 1 2367 ? 161.397 190.815 195.977 1.00 82.90  ? 2367 ASP A CA    1 
ATOM   7283  C  C     . ASP A 1 2367 ? 161.849 192.219 195.605 1.00 87.00  ? 2367 ASP A C     1 
ATOM   7284  O  O     . ASP A 1 2367 ? 161.573 193.163 196.352 1.00 88.72  ? 2367 ASP A O     1 
ATOM   7285  C  CB    . ASP A 1 2367 ? 162.198 190.313 197.178 1.00 85.80  ? 2367 ASP A CB    1 
ATOM   7286  C  CG    . ASP A 1 2367 ? 161.491 189.198 197.923 1.00 94.50  ? 2367 ASP A CG    1 
ATOM   7287  O  OD1   . ASP A 1 2367 ? 160.485 189.484 198.606 1.00 92.68  ? 2367 ASP A OD1   1 
ATOM   7288  O  OD2   . ASP A 1 2367 ? 161.939 188.037 197.824 1.00 95.90  ? 2367 ASP A OD2   1 
ATOM   7289  N  N     . VAL A 1 2368 ? 162.544 192.374 194.476 1.00 74.28  ? 2368 VAL A N     1 
ATOM   7290  C  CA    . VAL A 1 2368 ? 162.883 193.707 193.986 1.00 67.67  ? 2368 VAL A CA    1 
ATOM   7291  C  C     . VAL A 1 2368 ? 161.614 194.473 193.635 1.00 69.10  ? 2368 VAL A C     1 
ATOM   7292  O  O     . VAL A 1 2368 ? 161.468 195.657 193.960 1.00 72.12  ? 2368 VAL A O     1 
ATOM   7293  C  CB    . VAL A 1 2368 ? 163.837 193.607 192.782 1.00 55.71  ? 2368 VAL A CB    1 
ATOM   7294  C  CG1   . VAL A 1 2368 ? 163.904 194.929 192.038 1.00 60.51  ? 2368 VAL A CG1   1 
ATOM   7295  C  CG2   . VAL A 1 2368 ? 165.220 193.173 193.237 1.00 66.22  ? 2368 VAL A CG2   1 
ATOM   7296  N  N     . LEU A 1 2369 ? 160.673 193.803 192.975 1.00 62.50  ? 2369 LEU A N     1 
ATOM   7297  C  CA    . LEU A 1 2369 ? 159.400 194.402 192.586 1.00 60.52  ? 2369 LEU A CA    1 
ATOM   7298  C  C     . LEU A 1 2369 ? 158.358 194.019 193.629 1.00 66.60  ? 2369 LEU A C     1 
ATOM   7299  O  O     . LEU A 1 2369 ? 157.652 193.019 193.480 1.00 72.55  ? 2369 LEU A O     1 
ATOM   7300  C  CB    . LEU A 1 2369 ? 158.985 193.942 191.194 1.00 61.92  ? 2369 LEU A CB    1 
ATOM   7301  C  CG    . LEU A 1 2369 ? 158.064 194.895 190.432 1.00 63.71  ? 2369 LEU A CG    1 
ATOM   7302  C  CD1   . LEU A 1 2369 ? 158.875 195.998 189.785 1.00 60.16  ? 2369 LEU A CD1   1 
ATOM   7303  C  CD2   . LEU A 1 2369 ? 157.247 194.150 189.394 1.00 72.94  ? 2369 LEU A CD2   1 
ATOM   7304  N  N     . SER A 1 2370 ? 158.264 194.816 194.688 1.00 68.09  ? 2370 SER A N     1 
ATOM   7305  C  CA    . SER A 1 2370 ? 157.261 194.579 195.711 1.00 65.94  ? 2370 SER A CA    1 
ATOM   7306  C  C     . SER A 1 2370 ? 155.871 194.918 195.179 1.00 74.05  ? 2370 SER A C     1 
ATOM   7307  O  O     . SER A 1 2370 ? 155.706 195.736 194.271 1.00 84.64  ? 2370 SER A O     1 
ATOM   7308  C  CB    . SER A 1 2370 ? 157.564 195.399 196.964 1.00 67.38  ? 2370 SER A CB    1 
ATOM   7309  O  OG    . SER A 1 2370 ? 157.528 196.787 196.687 1.00 72.26  ? 2370 SER A OG    1 
ATOM   7310  N  N     . THR A 1 2371 ? 154.862 194.266 195.761 1.00 65.84  ? 2371 THR A N     1 
ATOM   7311  C  CA    . THR A 1 2371 ? 153.491 194.448 195.296 1.00 64.52  ? 2371 THR A CA    1 
ATOM   7312  C  C     . THR A 1 2371 ? 153.010 195.880 195.497 1.00 66.81  ? 2371 THR A C     1 
ATOM   7313  O  O     . THR A 1 2371 ? 152.194 196.378 194.708 1.00 75.61  ? 2371 THR A O     1 
ATOM   7314  C  CB    . THR A 1 2371 ? 152.566 193.468 196.015 1.00 69.30  ? 2371 THR A CB    1 
ATOM   7315  O  OG1   . THR A 1 2371 ? 153.168 192.168 196.030 1.00 72.68  ? 2371 THR A OG1   1 
ATOM   7316  C  CG2   . THR A 1 2371 ? 151.232 193.378 195.302 1.00 68.03  ? 2371 THR A CG2   1 
ATOM   7317  N  N     . ASP A 1 2372 ? 153.503 196.557 196.537 1.00 67.69  ? 2372 ASP A N     1 
ATOM   7318  C  CA    . ASP A 1 2372 ? 153.099 197.937 196.781 1.00 73.43  ? 2372 ASP A CA    1 
ATOM   7319  C  C     . ASP A 1 2372 ? 153.515 198.844 195.631 1.00 78.77  ? 2372 ASP A C     1 
ATOM   7320  O  O     . ASP A 1 2372 ? 152.799 199.790 195.287 1.00 85.09  ? 2372 ASP A O     1 
ATOM   7321  C  CB    . ASP A 1 2372 ? 153.697 198.435 198.095 1.00 74.43  ? 2372 ASP A CB    1 
ATOM   7322  C  CG    . ASP A 1 2372 ? 153.641 197.392 199.189 1.00 85.66  ? 2372 ASP A CG    1 
ATOM   7323  O  OD1   . ASP A 1 2372 ? 154.531 197.400 200.064 1.00 87.38  ? 2372 ASP A OD1   1 
ATOM   7324  O  OD2   . ASP A 1 2372 ? 152.710 196.560 199.172 1.00 87.64  ? 2372 ASP A OD2   1 
ATOM   7325  N  N     . MET A 1 2373 ? 154.675 198.576 195.028 1.00 67.26  ? 2373 MET A N     1 
ATOM   7326  C  CA    . MET A 1 2373 ? 155.113 199.379 193.891 1.00 65.46  ? 2373 MET A CA    1 
ATOM   7327  C  C     . MET A 1 2373 ? 154.178 199.210 192.701 1.00 71.21  ? 2373 MET A C     1 
ATOM   7328  O  O     . MET A 1 2373 ? 153.838 200.190 192.028 1.00 74.29  ? 2373 MET A O     1 
ATOM   7329  C  CB    . MET A 1 2373 ? 156.542 199.011 193.502 1.00 63.76  ? 2373 MET A CB    1 
ATOM   7330  C  CG    . MET A 1 2373 ? 157.573 199.357 194.553 1.00 69.66  ? 2373 MET A CG    1 
ATOM   7331  S  SD    . MET A 1 2373 ? 159.233 199.405 193.863 1.00 81.65  ? 2373 MET A SD    1 
ATOM   7332  C  CE    . MET A 1 2373 ? 159.143 198.074 192.676 1.00 71.82  ? 2373 MET A CE    1 
ATOM   7333  N  N     . ILE A 1 2374 ? 153.754 197.976 192.422 1.00 62.52  ? 2374 ILE A N     1 
ATOM   7334  C  CA    . ILE A 1 2374 ? 152.816 197.754 191.327 1.00 61.69  ? 2374 ILE A CA    1 
ATOM   7335  C  C     . ILE A 1 2374 ? 151.486 198.432 191.622 1.00 71.06  ? 2374 ILE A C     1 
ATOM   7336  O  O     . ILE A 1 2374 ? 150.860 199.015 190.729 1.00 76.46  ? 2374 ILE A O     1 
ATOM   7337  C  CB    . ILE A 1 2374 ? 152.636 196.249 191.062 1.00 59.42  ? 2374 ILE A CB    1 
ATOM   7338  C  CG1   . ILE A 1 2374 ? 153.989 195.539 191.069 1.00 61.77  ? 2374 ILE A CG1   1 
ATOM   7339  C  CG2   . ILE A 1 2374 ? 151.934 196.031 189.733 1.00 62.98  ? 2374 ILE A CG2   1 
ATOM   7340  C  CD1   . ILE A 1 2374 ? 153.885 194.041 190.913 1.00 61.17  ? 2374 ILE A CD1   1 
ATOM   7341  N  N     . PHE A 1 2375 ? 151.031 198.365 192.876 1.00 65.20  ? 2375 PHE A N     1 
ATOM   7342  C  CA    . PHE A 1 2375 ? 149.794 199.045 193.246 1.00 57.14  ? 2375 PHE A CA    1 
ATOM   7343  C  C     . PHE A 1 2375 ? 149.906 200.553 193.044 1.00 63.82  ? 2375 PHE A C     1 
ATOM   7344  O  O     . PHE A 1 2375 ? 148.982 201.186 192.522 1.00 73.54  ? 2375 PHE A O     1 
ATOM   7345  C  CB    . PHE A 1 2375 ? 149.432 198.722 194.694 1.00 56.25  ? 2375 PHE A CB    1 
ATOM   7346  C  CG    . PHE A 1 2375 ? 148.938 197.320 194.896 1.00 62.79  ? 2375 PHE A CG    1 
ATOM   7347  C  CD1   . PHE A 1 2375 ? 148.584 196.533 193.816 1.00 61.38  ? 2375 PHE A CD1   1 
ATOM   7348  C  CD2   . PHE A 1 2375 ? 148.829 196.788 196.169 1.00 69.87  ? 2375 PHE A CD2   1 
ATOM   7349  C  CE1   . PHE A 1 2375 ? 148.130 195.244 194.000 1.00 64.25  ? 2375 PHE A CE1   1 
ATOM   7350  C  CE2   . PHE A 1 2375 ? 148.377 195.498 196.359 1.00 64.37  ? 2375 PHE A CE2   1 
ATOM   7351  C  CZ    . PHE A 1 2375 ? 148.025 194.727 195.274 1.00 62.28  ? 2375 PHE A CZ    1 
ATOM   7352  N  N     . ASN A 1 2376 ? 151.030 201.144 193.455 1.00 61.27  ? 2376 ASN A N     1 
ATOM   7353  C  CA    . ASN A 1 2376 ? 151.220 202.582 193.281 1.00 68.65  ? 2376 ASN A CA    1 
ATOM   7354  C  C     . ASN A 1 2376 ? 151.286 202.958 191.807 1.00 73.38  ? 2376 ASN A C     1 
ATOM   7355  O  O     . ASN A 1 2376 ? 150.736 203.987 191.397 1.00 74.72  ? 2376 ASN A O     1 
ATOM   7356  C  CB    . ASN A 1 2376 ? 152.484 203.039 194.007 1.00 66.03  ? 2376 ASN A CB    1 
ATOM   7357  C  CG    . ASN A 1 2376 ? 152.322 203.042 195.511 1.00 71.95  ? 2376 ASN A CG    1 
ATOM   7358  O  OD1   . ASN A 1 2376 ? 151.212 202.913 196.027 1.00 74.04  ? 2376 ASN A OD1   1 
ATOM   7359  N  ND2   . ASN A 1 2376 ? 153.430 203.194 196.225 1.00 73.94  ? 2376 ASN A ND2   1 
ATOM   7360  N  N     . ASN A 1 2377 ? 151.967 202.145 190.997 1.00 61.87  ? 2377 ASN A N     1 
ATOM   7361  C  CA    . ASN A 1 2377 ? 152.019 202.399 189.561 1.00 60.64  ? 2377 ASN A CA    1 
ATOM   7362  C  C     . ASN A 1 2377 ? 150.625 202.353 188.951 1.00 63.89  ? 2377 ASN A C     1 
ATOM   7363  O  O     . ASN A 1 2377 ? 150.252 203.221 188.152 1.00 74.79  ? 2377 ASN A O     1 
ATOM   7364  C  CB    . ASN A 1 2377 ? 152.937 201.382 188.884 1.00 53.80  ? 2377 ASN A CB    1 
ATOM   7365  C  CG    . ASN A 1 2377 ? 153.009 201.572 187.384 1.00 60.16  ? 2377 ASN A CG    1 
ATOM   7366  O  OD1   . ASN A 1 2377 ? 152.642 200.682 186.617 1.00 66.09  ? 2377 ASN A OD1   1 
ATOM   7367  N  ND2   . ASN A 1 2377 ? 153.486 202.733 186.956 1.00 63.95  ? 2377 ASN A ND2   1 
ATOM   7368  N  N     . PHE A 1 2378 ? 149.835 201.346 189.331 1.00 54.76  ? 2378 PHE A N     1 
ATOM   7369  C  CA    . PHE A 1 2378 ? 148.478 201.233 188.811 1.00 61.91  ? 2378 PHE A CA    1 
ATOM   7370  C  C     . PHE A 1 2378 ? 147.637 202.432 189.225 1.00 67.79  ? 2378 PHE A C     1 
ATOM   7371  O  O     . PHE A 1 2378 ? 146.882 202.980 188.418 1.00 74.91  ? 2378 PHE A O     1 
ATOM   7372  C  CB    . PHE A 1 2378 ? 147.832 199.938 189.299 1.00 61.96  ? 2378 PHE A CB    1 
ATOM   7373  C  CG    . PHE A 1 2378 ? 146.333 199.931 189.190 1.00 60.22  ? 2378 PHE A CG    1 
ATOM   7374  C  CD1   . PHE A 1 2378 ? 145.714 200.131 187.968 1.00 64.95  ? 2378 PHE A CD1   1 
ATOM   7375  C  CD2   . PHE A 1 2378 ? 145.544 199.743 190.310 1.00 56.06  ? 2378 PHE A CD2   1 
ATOM   7376  C  CE1   . PHE A 1 2378 ? 144.339 200.130 187.865 1.00 68.04  ? 2378 PHE A CE1   1 
ATOM   7377  C  CE2   . PHE A 1 2378 ? 144.168 199.740 190.210 1.00 58.51  ? 2378 PHE A CE2   1 
ATOM   7378  C  CZ    . PHE A 1 2378 ? 143.566 199.934 188.987 1.00 69.12  ? 2378 PHE A CZ    1 
ATOM   7379  N  N     . LEU A 1 2379 ? 147.753 202.851 190.487 1.00 69.77  ? 2379 LEU A N     1 
ATOM   7380  C  CA    . LEU A 1 2379 ? 146.964 203.984 190.963 1.00 67.54  ? 2379 LEU A CA    1 
ATOM   7381  C  C     . LEU A 1 2379 ? 147.359 205.276 190.259 1.00 71.91  ? 2379 LEU A C     1 
ATOM   7382  O  O     . LEU A 1 2379 ? 146.493 206.078 189.895 1.00 81.58  ? 2379 LEU A O     1 
ATOM   7383  C  CB    . LEU A 1 2379 ? 147.109 204.125 192.476 1.00 63.89  ? 2379 LEU A CB    1 
ATOM   7384  C  CG    . LEU A 1 2379 ? 146.368 203.059 193.283 1.00 60.90  ? 2379 LEU A CG    1 
ATOM   7385  C  CD1   . LEU A 1 2379 ? 146.594 203.252 194.770 1.00 64.87  ? 2379 LEU A CD1   1 
ATOM   7386  C  CD2   . LEU A 1 2379 ? 144.886 203.088 192.954 1.00 61.63  ? 2379 LEU A CD2   1 
ATOM   7387  N  N     . ALA A 1 2380 ? 148.660 205.497 190.055 1.00 58.77  ? 2380 ALA A N     1 
ATOM   7388  C  CA    . ALA A 1 2380 ? 149.098 206.697 189.350 1.00 65.38  ? 2380 ALA A CA    1 
ATOM   7389  C  C     . ALA A 1 2380 ? 148.608 206.698 187.908 1.00 68.05  ? 2380 ALA A C     1 
ATOM   7390  O  O     . ALA A 1 2380 ? 148.121 207.721 187.409 1.00 76.80  ? 2380 ALA A O     1 
ATOM   7391  C  CB    . ALA A 1 2380 ? 150.620 206.812 189.403 1.00 70.64  ? 2380 ALA A CB    1 
ATOM   7392  N  N     . ARG A 1 2381 ? 148.716 205.556 187.224 1.00 58.87  ? 2381 ARG A N     1 
ATOM   7393  C  CA    . ARG A 1 2381 ? 148.225 205.474 185.852 1.00 69.13  ? 2381 ARG A CA    1 
ATOM   7394  C  C     . ARG A 1 2381 ? 146.715 205.671 185.795 1.00 74.86  ? 2381 ARG A C     1 
ATOM   7395  O  O     . ARG A 1 2381 ? 146.194 206.281 184.853 1.00 80.90  ? 2381 ARG A O     1 
ATOM   7396  C  CB    . ARG A 1 2381 ? 148.621 204.135 185.233 1.00 64.47  ? 2381 ARG A CB    1 
ATOM   7397  C  CG    . ARG A 1 2381 ? 150.105 204.004 184.954 1.00 66.03  ? 2381 ARG A CG    1 
ATOM   7398  C  CD    . ARG A 1 2381 ? 150.418 202.699 184.251 1.00 69.10  ? 2381 ARG A CD    1 
ATOM   7399  N  NE    . ARG A 1 2381 ? 149.711 202.586 182.982 1.00 71.30  ? 2381 ARG A NE    1 
ATOM   7400  C  CZ    . ARG A 1 2381 ? 150.128 203.118 181.842 1.00 74.88  ? 2381 ARG A CZ    1 
ATOM   7401  N  NH1   . ARG A 1 2381 ? 151.251 203.813 181.774 1.00 72.27  ? 2381 ARG A NH1   1 
ATOM   7402  N  NH2   . ARG A 1 2381 ? 149.400 202.948 180.742 1.00 73.72  ? 2381 ARG A NH2   1 
ATOM   7403  N  N     . LEU A 1 2382 ? 145.995 205.154 186.792 1.00 67.37  ? 2382 LEU A N     1 
ATOM   7404  C  CA    . LEU A 1 2382 ? 144.551 205.338 186.856 1.00 65.10  ? 2382 LEU A CA    1 
ATOM   7405  C  C     . LEU A 1 2382 ? 144.200 206.806 187.054 1.00 72.90  ? 2382 LEU A C     1 
ATOM   7406  O  O     . LEU A 1 2382 ? 143.250 207.316 186.449 1.00 78.40  ? 2382 LEU A O     1 
ATOM   7407  C  CB    . LEU A 1 2382 ? 143.988 204.486 187.996 1.00 66.27  ? 2382 LEU A CB    1 
ATOM   7408  C  CG    . LEU A 1 2382 ? 142.517 204.503 188.420 1.00 72.89  ? 2382 LEU A CG    1 
ATOM   7409  C  CD1   . LEU A 1 2382 ? 141.585 204.730 187.251 1.00 75.29  ? 2382 LEU A CD1   1 
ATOM   7410  C  CD2   . LEU A 1 2382 ? 142.156 203.219 189.147 1.00 71.60  ? 2382 LEU A CD2   1 
ATOM   7411  N  N     . ARG A 1 2383 ? 144.969 207.504 187.892 1.00 67.55  ? 2383 ARG A N     1 
ATOM   7412  C  CA    . ARG A 1 2383 ? 144.674 208.897 188.200 1.00 69.24  ? 2383 ARG A CA    1 
ATOM   7413  C  C     . ARG A 1 2383 ? 145.144 209.853 187.113 1.00 69.56  ? 2383 ARG A C     1 
ATOM   7414  O  O     . ARG A 1 2383 ? 144.693 211.003 187.085 1.00 70.99  ? 2383 ARG A O     1 
ATOM   7415  C  CB    . ARG A 1 2383 ? 145.319 209.283 189.531 1.00 64.30  ? 2383 ARG A CB    1 
ATOM   7416  C  CG    . ARG A 1 2383 ? 144.622 208.713 190.752 1.00 66.56  ? 2383 ARG A CG    1 
ATOM   7417  C  CD    . ARG A 1 2383 ? 145.363 209.081 192.025 1.00 69.83  ? 2383 ARG A CD    1 
ATOM   7418  N  NE    . ARG A 1 2383 ? 144.562 208.841 193.218 1.00 74.59  ? 2383 ARG A NE    1 
ATOM   7419  C  CZ    . ARG A 1 2383 ? 144.936 208.061 194.223 1.00 75.13  ? 2383 ARG A CZ    1 
ATOM   7420  N  NH1   . ARG A 1 2383 ? 146.098 207.429 194.211 1.00 68.08  ? 2383 ARG A NH1   1 
ATOM   7421  N  NH2   . ARG A 1 2383 ? 144.124 207.910 195.265 1.00 77.04  ? 2383 ARG A NH2   1 
ATOM   7422  N  N     . SER A 1 2384 ? 146.035 209.417 186.223 1.00 71.39  ? 2384 SER A N     1 
ATOM   7423  C  CA    . SER A 1 2384 ? 146.591 210.313 185.215 1.00 70.93  ? 2384 SER A CA    1 
ATOM   7424  C  C     . SER A 1 2384 ? 146.045 210.066 183.812 1.00 73.50  ? 2384 SER A C     1 
ATOM   7425  O  O     . SER A 1 2384 ? 145.506 210.987 183.192 1.00 82.52  ? 2384 SER A O     1 
ATOM   7426  C  CB    . SER A 1 2384 ? 148.119 210.199 185.201 1.00 76.72  ? 2384 SER A CB    1 
ATOM   7427  O  OG    . SER A 1 2384 ? 148.671 210.633 186.431 1.00 82.42  ? 2384 SER A OG    1 
ATOM   7428  N  N     . ILE A 1 2385 ? 146.171 208.849 183.297 1.00 69.16  ? 2385 ILE A N     1 
ATOM   7429  C  CA    . ILE A 1 2385 ? 145.866 208.554 181.900 1.00 71.48  ? 2385 ILE A CA    1 
ATOM   7430  C  C     . ILE A 1 2385 ? 144.355 208.397 181.758 1.00 76.05  ? 2385 ILE A C     1 
ATOM   7431  O  O     . ILE A 1 2385 ? 143.757 207.599 182.496 1.00 74.24  ? 2385 ILE A O     1 
ATOM   7432  C  CB    . ILE A 1 2385 ? 146.593 207.294 181.416 1.00 72.27  ? 2385 ILE A CB    1 
ATOM   7433  C  CG1   . ILE A 1 2385 ? 148.105 207.516 181.417 1.00 71.15  ? 2385 ILE A CG1   1 
ATOM   7434  C  CG2   . ILE A 1 2385 ? 146.120 206.910 180.024 1.00 78.27  ? 2385 ILE A CG2   1 
ATOM   7435  C  CD1   . ILE A 1 2385 ? 148.820 206.795 182.525 1.00 72.86  ? 2385 ILE A CD1   1 
ATOM   7436  N  N     . PRO A 1 2386 ? 143.710 209.125 180.850 1.00 91.88  ? 2386 PRO A N     1 
ATOM   7437  C  CA    . PRO A 1 2386 ? 142.291 208.877 180.578 1.00 90.20  ? 2386 PRO A CA    1 
ATOM   7438  C  C     . PRO A 1 2386 ? 142.089 207.527 179.911 1.00 92.54  ? 2386 PRO A C     1 
ATOM   7439  O  O     . PRO A 1 2386 ? 142.932 207.052 179.146 1.00 98.41  ? 2386 PRO A O     1 
ATOM   7440  C  CB    . PRO A 1 2386 ? 141.901 210.021 179.632 1.00 92.83  ? 2386 PRO A CB    1 
ATOM   7441  C  CG    . PRO A 1 2386 ? 143.036 211.008 179.693 1.00 91.38  ? 2386 PRO A CG    1 
ATOM   7442  C  CD    . PRO A 1 2386 ? 144.252 210.214 180.023 1.00 91.49  ? 2386 PRO A CD    1 
ATOM   7443  N  N     . LEU A 1 2387 ? 140.949 206.904 180.210 1.00 83.41  ? 2387 LEU A N     1 
ATOM   7444  C  CA    . LEU A 1 2387 ? 140.628 205.630 179.577 1.00 83.25  ? 2387 LEU A CA    1 
ATOM   7445  C  C     . LEU A 1 2387 ? 140.014 205.810 178.195 1.00 88.38  ? 2387 LEU A C     1 
ATOM   7446  O  O     . LEU A 1 2387 ? 140.248 204.982 177.308 1.00 93.07  ? 2387 LEU A O     1 
ATOM   7447  C  CB    . LEU A 1 2387 ? 139.688 204.815 180.464 1.00 81.01  ? 2387 LEU A CB    1 
ATOM   7448  C  CG    . LEU A 1 2387 ? 140.319 204.259 181.740 1.00 80.64  ? 2387 LEU A CG    1 
ATOM   7449  C  CD1   . LEU A 1 2387 ? 139.310 204.230 182.873 1.00 83.91  ? 2387 LEU A CD1   1 
ATOM   7450  C  CD2   . LEU A 1 2387 ? 140.897 202.879 181.490 1.00 85.07  ? 2387 LEU A CD2   1 
ATOM   7451  N  N     . ASP A 1 2388 ? 139.225 206.869 177.994 1.00 97.19  ? 2388 ASP A N     1 
ATOM   7452  C  CA    . ASP A 1 2388 ? 138.620 207.096 176.685 1.00 99.13  ? 2388 ASP A CA    1 
ATOM   7453  C  C     . ASP A 1 2388 ? 139.678 207.393 175.628 1.00 104.30 ? 2388 ASP A C     1 
ATOM   7454  O  O     . ASP A 1 2388 ? 139.595 206.890 174.502 1.00 107.44 ? 2388 ASP A O     1 
ATOM   7455  C  CB    . ASP A 1 2388 ? 137.597 208.228 176.769 1.00 98.01  ? 2388 ASP A CB    1 
ATOM   7456  C  CG    . ASP A 1 2388 ? 138.172 209.493 177.371 1.00 102.25 ? 2388 ASP A CG    1 
ATOM   7457  O  OD1   . ASP A 1 2388 ? 139.341 209.465 177.807 1.00 104.74 ? 2388 ASP A OD1   1 
ATOM   7458  O  OD2   . ASP A 1 2388 ? 137.456 210.515 177.408 1.00 103.32 ? 2388 ASP A OD2   1 
ATOM   7459  N  N     . GLU A 1 2389 ? 140.678 208.200 175.972 1.00 93.48  ? 2389 GLU A N     1 
ATOM   7460  C  CA    . GLU A 1 2389 ? 141.779 208.505 175.062 1.00 91.07  ? 2389 GLU A CA    1 
ATOM   7461  C  C     . GLU A 1 2389 ? 143.009 208.977 175.827 1.00 85.51  ? 2389 GLU A C     1 
ATOM   7462  O  O     . GLU A 1 2389 ? 142.946 209.933 176.598 0.00 93.30  ? 2389 GLU A O     1 
ATOM   7463  C  CB    . GLU A 1 2389 ? 141.364 209.566 174.039 1.00 92.98  ? 2389 GLU A CB    1 
ATOM   7464  C  CG    . GLU A 1 2389 ? 141.039 209.020 172.655 1.00 92.70  ? 2389 GLU A CG    1 
ATOM   7465  C  CD    . GLU A 1 2389 ? 142.266 208.532 171.902 1.00 95.53  ? 2389 GLU A CD    1 
ATOM   7466  O  OE1   . GLU A 1 2389 ? 142.099 207.955 170.807 1.00 97.46  ? 2389 GLU A OE1   1 
ATOM   7467  O  OE2   . GLU A 1 2389 ? 143.398 208.732 172.393 1.00 96.23  ? 2389 GLU A OE2   1 
ATOM   7468  N  N     . SER A 1 2410 ? 138.049 216.564 182.212 1.00 99.21  ? 2410 SER A N     1 
ATOM   7469  C  CA    . SER A 1 2410 ? 137.331 215.473 181.566 1.00 100.65 ? 2410 SER A CA    1 
ATOM   7470  C  C     . SER A 1 2410 ? 136.571 214.636 182.589 1.00 97.61  ? 2410 SER A C     1 
ATOM   7471  O  O     . SER A 1 2410 ? 137.138 214.235 183.605 1.00 94.62  ? 2410 SER A O     1 
ATOM   7472  C  CB    . SER A 1 2410 ? 138.299 214.589 180.777 1.00 96.82  ? 2410 SER A CB    1 
ATOM   7473  O  OG    . SER A 1 2410 ? 137.600 213.684 179.941 1.00 94.95  ? 2410 SER A OG    1 
ATOM   7474  N  N     . PRO A 1 2411 ? 135.282 214.393 182.326 1.00 102.14 ? 2411 PRO A N     1 
ATOM   7475  C  CA    . PRO A 1 2411 ? 134.517 213.503 183.216 1.00 103.11 ? 2411 PRO A CA    1 
ATOM   7476  C  C     . PRO A 1 2411 ? 135.184 212.155 183.418 1.00 105.97 ? 2411 PRO A C     1 
ATOM   7477  O  O     . PRO A 1 2411 ? 135.121 211.589 184.519 1.00 105.91 ? 2411 PRO A O     1 
ATOM   7478  C  CB    . PRO A 1 2411 ? 133.171 213.364 182.491 1.00 101.87 ? 2411 PRO A CB    1 
ATOM   7479  C  CG    . PRO A 1 2411 ? 133.081 214.551 181.558 1.00 102.99 ? 2411 PRO A CG    1 
ATOM   7480  C  CD    . PRO A 1 2411 ? 134.401 215.275 181.547 1.00 102.82 ? 2411 PRO A CD    1 
ATOM   7481  N  N     . MET A 1 2412 ? 135.825 211.628 182.371 1.00 97.95  ? 2412 MET A N     1 
ATOM   7482  C  CA    . MET A 1 2412 ? 136.612 210.408 182.507 1.00 94.45  ? 2412 MET A CA    1 
ATOM   7483  C  C     . MET A 1 2412 ? 137.626 210.533 183.637 1.00 95.34  ? 2412 MET A C     1 
ATOM   7484  O  O     . MET A 1 2412 ? 137.741 209.636 184.480 1.00 91.78  ? 2412 MET A O     1 
ATOM   7485  C  CB    . MET A 1 2412 ? 137.319 210.099 181.187 1.00 97.51  ? 2412 MET A CB    1 
ATOM   7486  C  CG    . MET A 1 2412 ? 137.958 208.720 181.104 1.00 101.72 ? 2412 MET A CG    1 
ATOM   7487  S  SD    . MET A 1 2412 ? 137.045 207.421 181.951 1.00 103.44 ? 2412 MET A SD    1 
ATOM   7488  C  CE    . MET A 1 2412 ? 135.745 207.113 180.760 1.00 97.22  ? 2412 MET A CE    1 
ATOM   7489  N  N     . LEU A 1 2413 ? 138.353 211.652 183.686 1.00 99.86  ? 2413 LEU A N     1 
ATOM   7490  C  CA    . LEU A 1 2413 ? 139.364 211.827 184.723 1.00 96.66  ? 2413 LEU A CA    1 
ATOM   7491  C  C     . LEU A 1 2413 ? 138.738 211.944 186.105 1.00 99.22  ? 2413 LEU A C     1 
ATOM   7492  O  O     . LEU A 1 2413 ? 139.278 211.412 187.079 1.00 102.03 ? 2413 LEU A O     1 
ATOM   7493  C  CB    . LEU A 1 2413 ? 140.227 213.052 184.428 1.00 98.44  ? 2413 LEU A CB    1 
ATOM   7494  C  CG    . LEU A 1 2413 ? 141.610 212.748 183.854 1.00 96.47  ? 2413 LEU A CG    1 
ATOM   7495  C  CD1   . LEU A 1 2413 ? 142.549 212.269 184.945 1.00 95.09  ? 2413 LEU A CD1   1 
ATOM   7496  C  CD2   . LEU A 1 2413 ? 141.494 211.709 182.767 1.00 92.47  ? 2413 LEU A CD2   1 
ATOM   7497  N  N     . GLN A 1 2414 ? 137.614 212.655 186.220 1.00 100.45 ? 2414 GLN A N     1 
ATOM   7498  C  CA    . GLN A 1 2414 ? 136.989 212.804 187.530 1.00 99.02  ? 2414 GLN A CA    1 
ATOM   7499  C  C     . GLN A 1 2414 ? 136.513 211.461 188.064 1.00 98.90  ? 2414 GLN A C     1 
ATOM   7500  O  O     . GLN A 1 2414 ? 136.750 211.129 189.234 1.00 94.20  ? 2414 GLN A O     1 
ATOM   7501  C  CB    . GLN A 1 2414 ? 135.831 213.797 187.456 1.00 97.64  ? 2414 GLN A CB    1 
ATOM   7502  C  CG    . GLN A 1 2414 ? 135.319 214.230 188.819 1.00 99.90  ? 2414 GLN A CG    1 
ATOM   7503  C  CD    . GLN A 1 2414 ? 136.444 214.637 189.753 1.00 100.84 ? 2414 GLN A CD    1 
ATOM   7504  O  OE1   . GLN A 1 2414 ? 137.225 215.536 189.445 1.00 101.56 ? 2414 GLN A OE1   1 
ATOM   7505  N  NE2   . GLN A 1 2414 ? 136.531 213.974 190.901 1.00 97.93  ? 2414 GLN A NE2   1 
ATOM   7506  N  N     . ILE A 1 2415 ? 135.862 210.662 187.213 1.00 94.83  ? 2415 ILE A N     1 
ATOM   7507  C  CA    . ILE A 1 2415 ? 135.440 209.327 187.628 1.00 95.21  ? 2415 ILE A CA    1 
ATOM   7508  C  C     . ILE A 1 2415 ? 136.649 208.475 187.985 1.00 94.82  ? 2415 ILE A C     1 
ATOM   7509  O  O     . ILE A 1 2415 ? 136.637 207.740 188.981 1.00 96.12  ? 2415 ILE A O     1 
ATOM   7510  C  CB    . ILE A 1 2415 ? 134.588 208.663 186.531 1.00 94.03  ? 2415 ILE A CB    1 
ATOM   7511  C  CG1   . ILE A 1 2415 ? 133.407 209.557 186.152 1.00 94.47  ? 2415 ILE A CG1   1 
ATOM   7512  C  CG2   . ILE A 1 2415 ? 134.110 207.295 186.987 1.00 91.65  ? 2415 ILE A CG2   1 
ATOM   7513  C  CD1   . ILE A 1 2415 ? 132.608 209.043 184.976 1.00 94.23  ? 2415 ILE A CD1   1 
ATOM   7514  N  N     . GLN A 1 2416 ? 137.710 208.559 187.180 1.00 92.12  ? 2416 GLN A N     1 
ATOM   7515  C  CA    . GLN A 1 2416 ? 138.901 207.756 187.426 1.00 86.40  ? 2416 GLN A CA    1 
ATOM   7516  C  C     . GLN A 1 2416 ? 139.523 208.093 188.775 1.00 88.53  ? 2416 GLN A C     1 
ATOM   7517  O  O     . GLN A 1 2416 ? 139.861 207.195 189.556 1.00 90.10  ? 2416 GLN A O     1 
ATOM   7518  C  CB    . GLN A 1 2416 ? 139.904 207.987 186.297 1.00 85.85  ? 2416 GLN A CB    1 
ATOM   7519  C  CG    . GLN A 1 2416 ? 139.893 206.923 185.220 1.00 87.42  ? 2416 GLN A CG    1 
ATOM   7520  C  CD    . GLN A 1 2416 ? 140.787 207.279 184.050 1.00 94.12  ? 2416 GLN A CD    1 
ATOM   7521  O  OE1   . GLN A 1 2416 ? 140.339 207.330 182.906 1.00 98.22  ? 2416 GLN A OE1   1 
ATOM   7522  N  NE2   . GLN A 1 2416 ? 142.056 207.539 184.334 1.00 89.34  ? 2416 GLN A NE2   1 
ATOM   7523  N  N     . ARG A 1 2417 ? 139.667 209.386 189.070 1.00 89.07  ? 2417 ARG A N     1 
ATOM   7524  C  CA    . ARG A 1 2417 ? 140.275 209.805 190.329 1.00 84.76  ? 2417 ARG A CA    1 
ATOM   7525  C  C     . ARG A 1 2417 ? 139.394 209.447 191.517 1.00 83.77  ? 2417 ARG A C     1 
ATOM   7526  O  O     . ARG A 1 2417 ? 139.898 209.021 192.563 1.00 88.26  ? 2417 ARG A O     1 
ATOM   7527  C  CB    . ARG A 1 2417 ? 140.557 211.307 190.301 1.00 89.53  ? 2417 ARG A CB    1 
ATOM   7528  C  CG    . ARG A 1 2417 ? 141.540 211.727 189.224 1.00 87.34  ? 2417 ARG A CG    1 
ATOM   7529  C  CD    . ARG A 1 2417 ? 142.144 213.086 189.519 1.00 86.38  ? 2417 ARG A CD    1 
ATOM   7530  N  NE    . ARG A 1 2417 ? 143.150 213.454 188.530 1.00 88.73  ? 2417 ARG A NE    1 
ATOM   7531  C  CZ    . ARG A 1 2417 ? 143.035 214.475 187.692 1.00 93.32  ? 2417 ARG A CZ    1 
ATOM   7532  N  NH1   . ARG A 1 2417 ? 141.964 215.252 187.692 1.00 91.35  ? 2417 ARG A NH1   1 
ATOM   7533  N  NH2   . ARG A 1 2417 ? 144.018 214.722 186.832 1.00 92.20  ? 2417 ARG A NH2   1 
ATOM   7534  N  N     . ASP A 1 2418 ? 138.076 209.614 191.381 1.00 86.67  ? 2418 ASP A N     1 
ATOM   7535  C  CA    . ASP A 1 2418 ? 137.180 209.238 192.470 1.00 92.81  ? 2418 ASP A CA    1 
ATOM   7536  C  C     . ASP A 1 2418 ? 137.263 207.744 192.756 1.00 91.18  ? 2418 ASP A C     1 
ATOM   7537  O  O     . ASP A 1 2418 ? 137.363 207.328 193.918 1.00 91.13  ? 2418 ASP A O     1 
ATOM   7538  C  CB    . ASP A 1 2418 ? 135.747 209.647 192.131 1.00 100.72 ? 2418 ASP A CB    1 
ATOM   7539  C  CG    . ASP A 1 2418 ? 135.086 210.431 193.246 1.00 104.95 ? 2418 ASP A CG    1 
ATOM   7540  O  OD1   . ASP A 1 2418 ? 134.032 211.052 192.994 1.00 102.13 ? 2418 ASP A OD1   1 
ATOM   7541  O  OD2   . ASP A 1 2418 ? 135.622 210.429 194.374 1.00 103.00 ? 2418 ASP A OD2   1 
ATOM   7542  N  N     . ALA A 1 2419 ? 137.250 206.919 191.705 1.00 83.37  ? 2419 ALA A N     1 
ATOM   7543  C  CA    . ALA A 1 2419 ? 137.357 205.478 191.897 1.00 81.45  ? 2419 ALA A CA    1 
ATOM   7544  C  C     . ALA A 1 2419 ? 138.692 205.103 192.525 1.00 81.70  ? 2419 ALA A C     1 
ATOM   7545  O  O     . ALA A 1 2419 ? 138.745 204.259 193.426 1.00 80.36  ? 2419 ALA A O     1 
ATOM   7546  C  CB    . ALA A 1 2419 ? 137.167 204.754 190.565 1.00 85.96  ? 2419 ALA A CB    1 
ATOM   7547  N  N     . ALA A 1 2420 ? 139.782 205.728 192.070 1.00 88.80  ? 2420 ALA A N     1 
ATOM   7548  C  CA    . ALA A 1 2420 ? 141.094 205.434 192.639 1.00 85.86  ? 2420 ALA A CA    1 
ATOM   7549  C  C     . ALA A 1 2420 ? 141.152 205.810 194.113 1.00 83.13  ? 2420 ALA A C     1 
ATOM   7550  O  O     . ALA A 1 2420 ? 141.758 205.094 194.918 1.00 85.44  ? 2420 ALA A O     1 
ATOM   7551  C  CB    . ALA A 1 2420 ? 142.183 206.163 191.854 1.00 85.58  ? 2420 ALA A CB    1 
ATOM   7552  N  N     . THR A 1 2421 ? 140.537 206.935 194.484 1.00 86.70  ? 2421 THR A N     1 
ATOM   7553  C  CA    . THR A 1 2421 ? 140.447 207.292 195.895 1.00 82.95  ? 2421 THR A CA    1 
ATOM   7554  C  C     . THR A 1 2421 ? 139.653 206.250 196.671 1.00 80.73  ? 2421 THR A C     1 
ATOM   7555  O  O     . THR A 1 2421 ? 139.991 205.926 197.816 1.00 80.82  ? 2421 THR A O     1 
ATOM   7556  C  CB    . THR A 1 2421 ? 139.812 208.675 196.049 1.00 86.90  ? 2421 THR A CB    1 
ATOM   7557  O  OG1   . THR A 1 2421 ? 140.566 209.635 195.300 1.00 87.87  ? 2421 THR A OG1   1 
ATOM   7558  C  CG2   . THR A 1 2421 ? 139.788 209.092 197.512 1.00 85.01  ? 2421 THR A CG2   1 
ATOM   7559  N  N     . ILE A 1 2422 ? 138.591 205.716 196.065 1.00 89.94  ? 2422 ILE A N     1 
ATOM   7560  C  CA    . ILE A 1 2422 ? 137.788 204.706 196.751 1.00 91.91  ? 2422 ILE A CA    1 
ATOM   7561  C  C     . ILE A 1 2422 ? 138.586 203.422 196.960 1.00 90.94  ? 2422 ILE A C     1 
ATOM   7562  O  O     . ILE A 1 2422 ? 138.501 202.792 198.021 1.00 88.28  ? 2422 ILE A O     1 
ATOM   7563  C  CB    . ILE A 1 2422 ? 136.477 204.443 195.987 1.00 91.28  ? 2422 ILE A CB    1 
ATOM   7564  C  CG1   . ILE A 1 2422 ? 135.645 205.723 195.895 1.00 90.30  ? 2422 ILE A CG1   1 
ATOM   7565  C  CG2   . ILE A 1 2422 ? 135.675 203.346 196.665 1.00 86.15  ? 2422 ILE A CG2   1 
ATOM   7566  C  CD1   . ILE A 1 2422 ? 135.613 206.530 197.177 1.00 90.31  ? 2422 ILE A CD1   1 
ATOM   7567  N  N     . MET A 1 2423 ? 139.375 203.011 195.964 1.00 86.93  ? 2423 MET A N     1 
ATOM   7568  C  CA    . MET A 1 2423 ? 140.118 201.760 196.079 1.00 83.62  ? 2423 MET A CA    1 
ATOM   7569  C  C     . MET A 1 2423 ? 141.428 201.905 196.843 1.00 84.41  ? 2423 MET A C     1 
ATOM   7570  O  O     . MET A 1 2423 ? 142.127 200.904 197.025 1.00 79.22  ? 2423 MET A O     1 
ATOM   7571  C  CB    . MET A 1 2423 ? 140.427 201.161 194.701 1.00 77.83  ? 2423 MET A CB    1 
ATOM   7572  C  CG    . MET A 1 2423 ? 139.275 200.395 194.077 1.00 84.24  ? 2423 MET A CG    1 
ATOM   7573  S  SD    . MET A 1 2423 ? 139.335 200.313 192.275 1.00 97.30  ? 2423 MET A SD    1 
ATOM   7574  C  CE    . MET A 1 2423 ? 139.998 201.917 191.855 1.00 82.48  ? 2423 MET A CE    1 
ATOM   7575  N  N     . GLN A 1 2424 ? 141.781 203.115 197.276 1.00 86.87  ? 2424 GLN A N     1 
ATOM   7576  C  CA    . GLN A 1 2424 ? 143.060 203.320 197.953 1.00 78.57  ? 2424 GLN A CA    1 
ATOM   7577  C  C     . GLN A 1 2424 ? 143.226 202.479 199.215 1.00 77.85  ? 2424 GLN A C     1 
ATOM   7578  O  O     . GLN A 1 2424 ? 144.299 201.873 199.381 1.00 81.40  ? 2424 GLN A O     1 
ATOM   7579  C  CB    . GLN A 1 2424 ? 143.250 204.811 198.252 1.00 82.18  ? 2424 GLN A CB    1 
ATOM   7580  C  CG    . GLN A 1 2424 ? 144.612 205.152 198.830 1.00 81.99  ? 2424 GLN A CG    1 
ATOM   7581  C  CD    . GLN A 1 2424 ? 145.723 205.042 197.807 1.00 87.13  ? 2424 GLN A CD    1 
ATOM   7582  O  OE1   . GLN A 1 2424 ? 145.758 205.787 196.828 1.00 88.34  ? 2424 GLN A OE1   1 
ATOM   7583  N  NE2   . GLN A 1 2424 ? 146.640 204.107 198.029 1.00 84.75  ? 2424 GLN A NE2   1 
ATOM   7584  N  N     . PRO A 1 2425 ? 142.255 202.403 200.138 1.00 79.03  ? 2425 PRO A N     1 
ATOM   7585  C  CA    . PRO A 1 2425 ? 142.491 201.603 201.355 1.00 80.65  ? 2425 PRO A CA    1 
ATOM   7586  C  C     . PRO A 1 2425 ? 142.789 200.138 201.084 1.00 82.72  ? 2425 PRO A C     1 
ATOM   7587  O  O     . PRO A 1 2425 ? 143.593 199.533 201.804 1.00 82.01  ? 2425 PRO A O     1 
ATOM   7588  C  CB    . PRO A 1 2425 ? 141.186 201.779 202.144 1.00 79.17  ? 2425 PRO A CB    1 
ATOM   7589  C  CG    . PRO A 1 2425 ? 140.625 203.060 201.659 1.00 81.10  ? 2425 PRO A CG    1 
ATOM   7590  C  CD    . PRO A 1 2425 ? 140.960 203.105 200.203 1.00 81.56  ? 2425 PRO A CD    1 
ATOM   7591  N  N     . TYR A 1 2426 ? 142.161 199.546 200.069 1.00 84.26  ? 2426 TYR A N     1 
ATOM   7592  C  CA    . TYR A 1 2426 ? 142.386 198.137 199.767 1.00 82.88  ? 2426 TYR A CA    1 
ATOM   7593  C  C     . TYR A 1 2426 ? 143.708 197.886 199.055 1.00 83.85  ? 2426 TYR A C     1 
ATOM   7594  O  O     . TYR A 1 2426 ? 144.295 196.814 199.231 1.00 82.15  ? 2426 TYR A O     1 
ATOM   7595  C  CB    . TYR A 1 2426 ? 141.232 197.592 198.924 1.00 79.92  ? 2426 TYR A CB    1 
ATOM   7596  C  CG    . TYR A 1 2426 ? 139.870 197.987 199.442 1.00 75.85  ? 2426 TYR A CG    1 
ATOM   7597  C  CD1   . TYR A 1 2426 ? 139.315 197.350 200.543 1.00 74.32  ? 2426 TYR A CD1   1 
ATOM   7598  C  CD2   . TYR A 1 2426 ? 139.144 199.003 198.839 1.00 77.83  ? 2426 TYR A CD2   1 
ATOM   7599  C  CE1   . TYR A 1 2426 ? 138.073 197.710 201.023 1.00 77.02  ? 2426 TYR A CE1   1 
ATOM   7600  C  CE2   . TYR A 1 2426 ? 137.902 199.370 199.312 1.00 82.02  ? 2426 TYR A CE2   1 
ATOM   7601  C  CZ    . TYR A 1 2426 ? 137.371 198.720 200.405 1.00 83.22  ? 2426 TYR A CZ    1 
ATOM   7602  O  OH    . TYR A 1 2426 ? 136.132 199.083 200.880 1.00 89.54  ? 2426 TYR A OH    1 
ATOM   7603  N  N     . PHE A 1 2427 ? 144.186 198.840 198.259 1.00 76.08  ? 2427 PHE A N     1 
ATOM   7604  C  CA    . PHE A 1 2427 ? 145.436 198.680 197.515 1.00 67.83  ? 2427 PHE A CA    1 
ATOM   7605  C  C     . PHE A 1 2427 ? 146.622 199.173 198.346 1.00 74.96  ? 2427 PHE A C     1 
ATOM   7606  O  O     . PHE A 1 2427 ? 147.406 200.027 197.934 1.00 81.88  ? 2427 PHE A O     1 
ATOM   7607  C  CB    . PHE A 1 2427 ? 145.347 199.410 196.181 1.00 71.84  ? 2427 PHE A CB    1 
ATOM   7608  C  CG    . PHE A 1 2427 ? 144.719 198.598 195.091 1.00 67.22  ? 2427 PHE A CG    1 
ATOM   7609  C  CD1   . PHE A 1 2427 ? 143.883 199.191 194.162 1.00 72.87  ? 2427 PHE A CD1   1 
ATOM   7610  C  CD2   . PHE A 1 2427 ? 144.974 197.244 194.986 1.00 64.42  ? 2427 PHE A CD2   1 
ATOM   7611  C  CE1   . PHE A 1 2427 ? 143.304 198.445 193.160 1.00 72.41  ? 2427 PHE A CE1   1 
ATOM   7612  C  CE2   . PHE A 1 2427 ? 144.402 196.495 193.982 1.00 66.06  ? 2427 PHE A CE2   1 
ATOM   7613  C  CZ    . PHE A 1 2427 ? 143.566 197.096 193.068 1.00 68.79  ? 2427 PHE A CZ    1 
ATOM   7614  N  N     . THR A 1 2428 ? 146.741 198.607 199.543 1.00 78.47  ? 2428 THR A N     1 
ATOM   7615  C  CA    . THR A 1 2428 ? 147.796 198.957 200.480 1.00 81.92  ? 2428 THR A CA    1 
ATOM   7616  C  C     . THR A 1 2428 ? 148.461 197.685 200.989 1.00 83.55  ? 2428 THR A C     1 
ATOM   7617  O  O     . THR A 1 2428 ? 147.974 196.572 200.774 1.00 85.41  ? 2428 THR A O     1 
ATOM   7618  C  CB    . THR A 1 2428 ? 147.254 199.786 201.655 1.00 80.40  ? 2428 THR A CB    1 
ATOM   7619  O  OG1   . THR A 1 2428 ? 148.317 200.555 202.231 1.00 84.90  ? 2428 THR A OG1   1 
ATOM   7620  C  CG2   . THR A 1 2428 ? 146.652 198.881 202.721 1.00 78.14  ? 2428 THR A CG2   1 
ATOM   7621  N  N     . SER A 1 2429 ? 149.598 197.862 201.658 1.00 93.62  ? 2429 SER A N     1 
ATOM   7622  C  CA    . SER A 1 2429 ? 150.308 196.735 202.246 1.00 90.68  ? 2429 SER A CA    1 
ATOM   7623  C  C     . SER A 1 2429 ? 149.433 196.049 203.287 1.00 92.32  ? 2429 SER A C     1 
ATOM   7624  O  O     . SER A 1 2429 ? 148.792 196.713 204.108 1.00 95.02  ? 2429 SER A O     1 
ATOM   7625  C  CB    . SER A 1 2429 ? 151.616 197.203 202.880 1.00 94.60  ? 2429 SER A CB    1 
ATOM   7626  O  OG    . SER A 1 2429 ? 152.426 197.883 201.937 1.00 98.60  ? 2429 SER A OG    1 
ATOM   7627  N  N     . ASN A 1 2430 ? 149.407 194.716 203.246 1.00 96.98  ? 2430 ASN A N     1 
ATOM   7628  C  CA    . ASN A 1 2430 ? 148.577 193.909 204.142 1.00 101.07 ? 2430 ASN A CA    1 
ATOM   7629  C  C     . ASN A 1 2430 ? 147.105 194.298 204.023 1.00 103.51 ? 2430 ASN A C     1 
ATOM   7630  O  O     . ASN A 1 2430 ? 146.357 194.309 205.003 1.00 103.88 ? 2430 ASN A O     1 
ATOM   7631  C  CB    . ASN A 1 2430 ? 149.061 194.018 205.590 1.00 101.70 ? 2430 ASN A CB    1 
ATOM   7632  C  CG    . ASN A 1 2430 ? 148.517 192.910 206.472 1.00 103.80 ? 2430 ASN A CG    1 
ATOM   7633  O  OD1   . ASN A 1 2430 ? 147.857 191.988 205.994 1.00 101.77 ? 2430 ASN A OD1   1 
ATOM   7634  N  ND2   . ASN A 1 2430 ? 148.787 193.000 207.769 1.00 103.22 ? 2430 ASN A ND2   1 
ATOM   7635  N  N     . GLY A 1 2431 ? 146.686 194.630 202.803 1.00 93.37  ? 2431 GLY A N     1 
ATOM   7636  C  CA    . GLY A 1 2431 ? 145.305 194.947 202.518 1.00 89.66  ? 2431 GLY A CA    1 
ATOM   7637  C  C     . GLY A 1 2431 ? 144.516 193.725 202.082 1.00 89.81  ? 2431 GLY A C     1 
ATOM   7638  O  O     . GLY A 1 2431 ? 144.991 192.588 202.120 1.00 90.63  ? 2431 GLY A O     1 
ATOM   7639  N  N     . LEU A 1 2432 ? 143.276 193.978 201.661 1.00 81.68  ? 2432 LEU A N     1 
ATOM   7640  C  CA    . LEU A 1 2432 ? 142.436 192.898 201.155 1.00 80.08  ? 2432 LEU A CA    1 
ATOM   7641  C  C     . LEU A 1 2432 ? 143.056 192.258 199.920 1.00 83.56  ? 2432 LEU A C     1 
ATOM   7642  O  O     . LEU A 1 2432 ? 143.117 191.027 199.805 1.00 88.77  ? 2432 LEU A O     1 
ATOM   7643  C  CB    . LEU A 1 2432 ? 141.037 193.430 200.841 1.00 81.51  ? 2432 LEU A CB    1 
ATOM   7644  C  CG    . LEU A 1 2432 ? 140.156 192.562 199.941 1.00 78.77  ? 2432 LEU A CG    1 
ATOM   7645  C  CD1   . LEU A 1 2432 ? 139.651 191.348 200.695 1.00 80.03  ? 2432 LEU A CD1   1 
ATOM   7646  C  CD2   . LEU A 1 2432 ? 138.995 193.370 199.384 1.00 78.66  ? 2432 LEU A CD2   1 
ATOM   7647  N  N     . VAL A 1 2433 ? 143.543 193.084 198.992 1.00 66.02  ? 2433 VAL A N     1 
ATOM   7648  C  CA    . VAL A 1 2433 ? 144.077 192.569 197.736 1.00 61.34  ? 2433 VAL A CA    1 
ATOM   7649  C  C     . VAL A 1 2433 ? 145.339 191.752 197.977 1.00 65.89  ? 2433 VAL A C     1 
ATOM   7650  O  O     . VAL A 1 2433 ? 145.509 190.671 197.405 1.00 69.14  ? 2433 VAL A O     1 
ATOM   7651  C  CB    . VAL A 1 2433 ? 144.332 193.724 196.754 1.00 62.86  ? 2433 VAL A CB    1 
ATOM   7652  C  CG1   . VAL A 1 2433 ? 144.582 193.181 195.360 1.00 65.96  ? 2433 VAL A CG1   1 
ATOM   7653  C  CG2   . VAL A 1 2433 ? 143.160 194.686 196.761 1.00 66.59  ? 2433 VAL A CG2   1 
ATOM   7654  N  N     . THR A 1 2434 ? 146.246 192.255 198.817 1.00 73.30  ? 2434 THR A N     1 
ATOM   7655  C  CA    . THR A 1 2434 ? 147.502 191.549 199.059 1.00 74.90  ? 2434 THR A CA    1 
ATOM   7656  C  C     . THR A 1 2434 ? 147.261 190.212 199.748 1.00 74.10  ? 2434 THR A C     1 
ATOM   7657  O  O     . THR A 1 2434 ? 147.848 189.192 199.369 1.00 76.76  ? 2434 THR A O     1 
ATOM   7658  C  CB    . THR A 1 2434 ? 148.442 192.420 199.890 1.00 75.81  ? 2434 THR A CB    1 
ATOM   7659  O  OG1   . THR A 1 2434 ? 148.664 193.664 199.214 1.00 79.53  ? 2434 THR A OG1   1 
ATOM   7660  C  CG2   . THR A 1 2434 ? 149.773 191.716 200.094 1.00 73.95  ? 2434 THR A CG2   1 
ATOM   7661  N  N     . LYS A 1 2435 ? 146.397 190.196 200.765 1.00 79.09  ? 2435 LYS A N     1 
ATOM   7662  C  CA    . LYS A 1 2435 ? 146.101 188.948 201.462 1.00 79.88  ? 2435 LYS A CA    1 
ATOM   7663  C  C     . LYS A 1 2435 ? 145.399 187.955 200.544 1.00 79.47  ? 2435 LYS A C     1 
ATOM   7664  O  O     . LYS A 1 2435 ? 145.704 186.756 200.565 1.00 81.81  ? 2435 LYS A O     1 
ATOM   7665  C  CB    . LYS A 1 2435 ? 145.258 189.233 202.705 1.00 80.52  ? 2435 LYS A CB    1 
ATOM   7666  C  CG    . LYS A 1 2435 ? 145.980 190.072 203.749 1.00 82.15  ? 2435 LYS A CG    1 
ATOM   7667  C  CD    . LYS A 1 2435 ? 145.028 190.605 204.806 1.00 80.51  ? 2435 LYS A CD    1 
ATOM   7668  C  CE    . LYS A 1 2435 ? 144.300 189.481 205.520 1.00 87.83  ? 2435 LYS A CE    1 
ATOM   7669  N  NZ    . LYS A 1 2435 ? 143.448 189.996 206.628 1.00 86.60  ? 2435 LYS A NZ    1 
ATOM   7670  N  N     . ALA A 1 2436 ? 144.459 188.436 199.725 1.00 75.31  ? 2436 ALA A N     1 
ATOM   7671  C  CA    . ALA A 1 2436 ? 143.782 187.551 198.783 1.00 73.84  ? 2436 ALA A CA    1 
ATOM   7672  C  C     . ALA A 1 2436 ? 144.760 186.974 197.767 1.00 73.00  ? 2436 ALA A C     1 
ATOM   7673  O  O     . ALA A 1 2436 ? 144.687 185.788 197.429 1.00 82.45  ? 2436 ALA A O     1 
ATOM   7674  C  CB    . ALA A 1 2436 ? 142.651 188.300 198.079 1.00 76.63  ? 2436 ALA A CB    1 
ATOM   7675  N  N     . LEU A 1 2437 ? 145.683 187.800 197.269 1.00 62.64  ? 2437 LEU A N     1 
ATOM   7676  C  CA    . LEU A 1 2437 ? 146.686 187.319 196.326 1.00 66.34  ? 2437 LEU A CA    1 
ATOM   7677  C  C     . LEU A 1 2437 ? 147.604 186.294 196.978 1.00 71.83  ? 2437 LEU A C     1 
ATOM   7678  O  O     . LEU A 1 2437 ? 147.990 185.305 196.343 1.00 77.18  ? 2437 LEU A O     1 
ATOM   7679  C  CB    . LEU A 1 2437 ? 147.486 188.500 195.773 1.00 63.44  ? 2437 LEU A CB    1 
ATOM   7680  C  CG    . LEU A 1 2437 ? 148.541 188.261 194.691 1.00 60.91  ? 2437 LEU A CG    1 
ATOM   7681  C  CD1   . LEU A 1 2437 ? 148.639 189.484 193.801 1.00 65.84  ? 2437 LEU A CD1   1 
ATOM   7682  C  CD2   . LEU A 1 2437 ? 149.903 187.954 195.295 1.00 65.46  ? 2437 LEU A CD2   1 
ATOM   7683  N  N     . GLU A 1 2438 ? 147.974 186.519 198.239 1.00 86.73  ? 2438 GLU A N     1 
ATOM   7684  C  CA    . GLU A 1 2438 ? 148.800 185.550 198.949 1.00 84.45  ? 2438 GLU A CA    1 
ATOM   7685  C  C     . GLU A 1 2438 ? 148.066 184.226 199.107 1.00 83.90  ? 2438 GLU A C     1 
ATOM   7686  O  O     . GLU A 1 2438 ? 148.658 183.155 198.929 1.00 85.40  ? 2438 GLU A O     1 
ATOM   7687  C  CB    . GLU A 1 2438 ? 149.235 186.140 200.300 1.00 86.03  ? 2438 GLU A CB    1 
ATOM   7688  C  CG    . GLU A 1 2438 ? 149.780 185.187 201.390 1.00 84.49  ? 2438 GLU A CG    1 
ATOM   7689  C  CD    . GLU A 1 2438 ? 148.769 184.184 201.922 1.00 89.63  ? 2438 GLU A CD    1 
ATOM   7690  O  OE1   . GLU A 1 2438 ? 149.093 182.979 201.964 1.00 94.05  ? 2438 GLU A OE1   1 
ATOM   7691  O  OE2   . GLU A 1 2438 ? 147.651 184.603 202.291 1.00 87.29  ? 2438 GLU A OE2   1 
ATOM   7692  N  N     . HIS A 1 2439 ? 146.775 184.274 199.447 1.00 82.36  ? 2439 HIS A N     1 
ATOM   7693  C  CA    . HIS A 1 2439 ? 146.015 183.037 199.594 1.00 78.88  ? 2439 HIS A CA    1 
ATOM   7694  C  C     . HIS A 1 2439 ? 145.793 182.356 198.249 1.00 84.20  ? 2439 HIS A C     1 
ATOM   7695  O  O     . HIS A 1 2439 ? 145.840 181.124 198.158 1.00 91.13  ? 2439 HIS A O     1 
ATOM   7696  C  CB    . HIS A 1 2439 ? 144.677 183.305 200.274 1.00 80.17  ? 2439 HIS A CB    1 
ATOM   7697  C  CG    . HIS A 1 2439 ? 143.913 182.060 200.596 1.00 85.61  ? 2439 HIS A CG    1 
ATOM   7698  N  ND1   . HIS A 1 2439 ? 142.539 181.987 200.521 1.00 87.33  ? 2439 HIS A ND1   1 
ATOM   7699  C  CD2   . HIS A 1 2439 ? 144.333 180.835 200.992 1.00 85.42  ? 2439 HIS A CD2   1 
ATOM   7700  C  CE1   . HIS A 1 2439 ? 142.146 180.772 200.858 1.00 87.84  ? 2439 HIS A CE1   1 
ATOM   7701  N  NE2   . HIS A 1 2439 ? 143.215 180.053 201.149 1.00 84.67  ? 2439 HIS A NE2   1 
ATOM   7702  N  N     . ALA A 1 2440 ? 145.537 183.139 197.197 1.00 79.11  ? 2440 ALA A N     1 
ATOM   7703  C  CA    . ALA A 1 2440 ? 145.289 182.555 195.883 1.00 74.28  ? 2440 ALA A CA    1 
ATOM   7704  C  C     . ALA A 1 2440 ? 146.503 181.800 195.364 1.00 76.79  ? 2440 ALA A C     1 
ATOM   7705  O  O     . ALA A 1 2440 ? 146.363 180.906 194.522 1.00 81.96  ? 2440 ALA A O     1 
ATOM   7706  C  CB    . ALA A 1 2440 ? 144.878 183.641 194.892 1.00 76.61  ? 2440 ALA A CB    1 
ATOM   7707  N  N     . PHE A 1 2441 ? 147.697 182.142 195.849 1.00 76.84  ? 2441 PHE A N     1 
ATOM   7708  C  CA    . PHE A 1 2441 ? 148.896 181.408 195.468 1.00 78.10  ? 2441 PHE A CA    1 
ATOM   7709  C  C     . PHE A 1 2441 ? 148.908 180.001 196.045 1.00 78.43  ? 2441 PHE A C     1 
ATOM   7710  O  O     . PHE A 1 2441 ? 149.645 179.143 195.547 1.00 75.09  ? 2441 PHE A O     1 
ATOM   7711  C  CB    . PHE A 1 2441 ? 150.139 182.171 195.927 1.00 80.38  ? 2441 PHE A CB    1 
ATOM   7712  C  CG    . PHE A 1 2441 ? 150.833 182.918 194.826 1.00 83.66  ? 2441 PHE A CG    1 
ATOM   7713  C  CD1   . PHE A 1 2441 ? 150.513 184.239 194.563 1.00 78.12  ? 2441 PHE A CD1   1 
ATOM   7714  C  CD2   . PHE A 1 2441 ? 151.808 182.305 194.060 1.00 84.44  ? 2441 PHE A CD2   1 
ATOM   7715  C  CE1   . PHE A 1 2441 ? 151.148 184.932 193.556 1.00 77.74  ? 2441 PHE A CE1   1 
ATOM   7716  C  CE2   . PHE A 1 2441 ? 152.448 182.994 193.050 1.00 82.91  ? 2441 PHE A CE2   1 
ATOM   7717  C  CZ    . PHE A 1 2441 ? 152.117 184.310 192.798 1.00 81.66  ? 2441 PHE A CZ    1 
ATOM   7718  N  N     . GLN A 1 2442 ? 148.112 179.746 197.083 1.00 86.91  ? 2442 GLN A N     1 
ATOM   7719  C  CA    . GLN A 1 2442 ? 148.071 178.450 197.744 1.00 82.99  ? 2442 GLN A CA    1 
ATOM   7720  C  C     . GLN A 1 2442 ? 147.040 177.501 197.148 1.00 80.48  ? 2442 GLN A C     1 
ATOM   7721  O  O     . GLN A 1 2442 ? 147.017 176.324 197.522 1.00 82.69  ? 2442 GLN A O     1 
ATOM   7722  C  CB    . GLN A 1 2442 ? 147.782 178.633 199.237 1.00 82.73  ? 2442 GLN A CB    1 
ATOM   7723  C  CG    . GLN A 1 2442 ? 149.024 178.736 200.103 1.00 85.08  ? 2442 GLN A CG    1 
ATOM   7724  C  CD    . GLN A 1 2442 ? 148.785 179.542 201.364 1.00 88.93  ? 2442 GLN A CD    1 
ATOM   7725  O  OE1   . GLN A 1 2442 ? 147.679 179.558 201.904 1.00 93.60  ? 2442 GLN A OE1   1 
ATOM   7726  N  NE2   . GLN A 1 2442 ? 149.824 180.219 201.839 1.00 86.99  ? 2442 GLN A NE2   1 
ATOM   7727  N  N     . LEU A 1 2443 ? 146.191 177.976 196.241 1.00 83.01  ? 2443 LEU A N     1 
ATOM   7728  C  CA    . LEU A 1 2443 ? 145.184 177.127 195.627 1.00 82.79  ? 2443 LEU A CA    1 
ATOM   7729  C  C     . LEU A 1 2443 ? 145.791 176.350 194.460 1.00 89.46  ? 2443 LEU A C     1 
ATOM   7730  O  O     . LEU A 1 2443 ? 146.999 176.382 194.214 1.00 91.90  ? 2443 LEU A O     1 
ATOM   7731  C  CB    . LEU A 1 2443 ? 143.992 177.962 195.166 1.00 77.98  ? 2443 LEU A CB    1 
ATOM   7732  C  CG    . LEU A 1 2443 ? 143.384 178.921 196.188 1.00 79.57  ? 2443 LEU A CG    1 
ATOM   7733  C  CD1   . LEU A 1 2443 ? 142.229 179.690 195.569 1.00 82.81  ? 2443 LEU A CD1   1 
ATOM   7734  C  CD2   . LEU A 1 2443 ? 142.929 178.167 197.424 1.00 85.39  ? 2443 LEU A CD2   1 
ATOM   7735  N  N     . GLU A 1 2444 ? 144.937 175.640 193.730 1.00 91.88  ? 2444 GLU A N     1 
ATOM   7736  C  CA    . GLU A 1 2444 ? 145.341 174.883 192.554 1.00 89.76  ? 2444 GLU A CA    1 
ATOM   7737  C  C     . GLU A 1 2444 ? 144.747 175.532 191.314 1.00 90.56  ? 2444 GLU A C     1 
ATOM   7738  O  O     . GLU A 1 2444 ? 143.523 175.663 191.202 1.00 93.92  ? 2444 GLU A O     1 
ATOM   7739  C  CB    . GLU A 1 2444 ? 144.889 173.425 192.655 1.00 91.08  ? 2444 GLU A CB    1 
ATOM   7740  C  CG    . GLU A 1 2444 ? 145.886 172.508 193.338 1.00 91.50  ? 2444 GLU A CG    1 
ATOM   7741  C  CD    . GLU A 1 2444 ? 145.484 171.049 193.255 1.00 95.03  ? 2444 GLU A CD    1 
ATOM   7742  O  OE1   . GLU A 1 2444 ? 144.400 170.700 193.768 1.00 92.18  ? 2444 GLU A OE1   1 
ATOM   7743  O  OE2   . GLU A 1 2444 ? 146.250 170.251 192.676 1.00 96.01  ? 2444 GLU A OE2   1 
ATOM   7744  N  N     . HIS A 1 2445 ? 145.611 175.930 190.387 1.00 76.43  ? 2445 HIS A N     1 
ATOM   7745  C  CA    . HIS A 1 2445 ? 145.199 176.582 189.156 1.00 72.00  ? 2445 HIS A CA    1 
ATOM   7746  C  C     . HIS A 1 2445 ? 145.594 175.726 187.963 1.00 76.53  ? 2445 HIS A C     1 
ATOM   7747  O  O     . HIS A 1 2445 ? 146.589 174.996 188.005 1.00 84.34  ? 2445 HIS A O     1 
ATOM   7748  C  CB    . HIS A 1 2445 ? 145.824 177.975 189.026 1.00 65.33  ? 2445 HIS A CB    1 
ATOM   7749  C  CG    . HIS A 1 2445 ? 145.627 178.840 190.230 1.00 69.16  ? 2445 HIS A CG    1 
ATOM   7750  N  ND1   . HIS A 1 2445 ? 144.588 179.739 190.338 1.00 71.65  ? 2445 HIS A ND1   1 
ATOM   7751  C  CD2   . HIS A 1 2445 ? 146.335 178.944 191.378 1.00 69.46  ? 2445 HIS A CD2   1 
ATOM   7752  C  CE1   . HIS A 1 2445 ? 144.665 180.360 191.501 1.00 77.73  ? 2445 HIS A CE1   1 
ATOM   7753  N  NE2   . HIS A 1 2445 ? 145.717 179.896 192.152 1.00 79.07  ? 2445 HIS A NE2   1 
ATOM   7754  N  N     . ILE A 1 2446 ? 144.796 175.817 186.896 1.00 66.54  ? 2446 ILE A N     1 
ATOM   7755  C  CA    . ILE A 1 2446 ? 145.084 175.061 185.684 1.00 65.88  ? 2446 ILE A CA    1 
ATOM   7756  C  C     . ILE A 1 2446 ? 146.424 175.463 185.086 1.00 71.01  ? 2446 ILE A C     1 
ATOM   7757  O  O     . ILE A 1 2446 ? 147.214 174.593 184.701 1.00 74.02  ? 2446 ILE A O     1 
ATOM   7758  C  CB    . ILE A 1 2446 ? 143.940 175.239 184.669 1.00 64.27  ? 2446 ILE A CB    1 
ATOM   7759  C  CG1   . ILE A 1 2446 ? 142.847 174.203 184.925 1.00 68.54  ? 2446 ILE A CG1   1 
ATOM   7760  C  CG2   . ILE A 1 2446 ? 144.453 175.115 183.248 1.00 71.42  ? 2446 ILE A CG2   1 
ATOM   7761  C  CD1   . ILE A 1 2446 ? 143.317 172.775 184.777 1.00 71.95  ? 2446 ILE A CD1   1 
ATOM   7762  N  N     . MET A 1 2447 ? 146.709 176.760 185.011 1.00 65.68  ? 2447 MET A N     1 
ATOM   7763  C  CA    . MET A 1 2447 ? 148.013 177.256 184.606 1.00 66.17  ? 2447 MET A CA    1 
ATOM   7764  C  C     . MET A 1 2447 ? 148.728 177.806 185.831 1.00 73.41  ? 2447 MET A C     1 
ATOM   7765  O  O     . MET A 1 2447 ? 148.097 178.224 186.804 1.00 77.27  ? 2447 MET A O     1 
ATOM   7766  C  CB    . MET A 1 2447 ? 147.901 178.341 183.528 1.00 70.30  ? 2447 MET A CB    1 
ATOM   7767  C  CG    . MET A 1 2447 ? 147.169 177.900 182.275 1.00 75.78  ? 2447 MET A CG    1 
ATOM   7768  S  SD    . MET A 1 2447 ? 148.026 178.410 180.776 1.00 83.28  ? 2447 MET A SD    1 
ATOM   7769  C  CE    . MET A 1 2447 ? 147.178 177.421 179.551 1.00 67.26  ? 2447 MET A CE    1 
ATOM   7770  N  N     . ASP A 1 2448 ? 150.058 177.790 185.775 1.00 76.53  ? 2448 ASP A N     1 
ATOM   7771  C  CA    . ASP A 1 2448 ? 150.859 178.267 186.895 1.00 73.01  ? 2448 ASP A CA    1 
ATOM   7772  C  C     . ASP A 1 2448 ? 150.513 179.714 187.218 1.00 72.90  ? 2448 ASP A C     1 
ATOM   7773  O  O     . ASP A 1 2448 ? 150.387 180.551 186.321 1.00 76.92  ? 2448 ASP A O     1 
ATOM   7774  C  CB    . ASP A 1 2448 ? 152.346 178.133 186.571 1.00 78.60  ? 2448 ASP A CB    1 
ATOM   7775  C  CG    . ASP A 1 2448 ? 152.731 176.719 186.187 1.00 87.12  ? 2448 ASP A CG    1 
ATOM   7776  O  OD1   . ASP A 1 2448 ? 151.900 176.024 185.565 1.00 88.14  ? 2448 ASP A OD1   1 
ATOM   7777  O  OD2   . ASP A 1 2448 ? 153.862 176.300 186.509 1.00 83.55  ? 2448 ASP A OD2   1 
ATOM   7778  N  N     . LEU A 1 2449 ? 150.353 180.004 188.506 1.00 75.72  ? 2449 LEU A N     1 
ATOM   7779  C  CA    . LEU A 1 2449 ? 149.914 181.319 188.951 1.00 82.60  ? 2449 LEU A CA    1 
ATOM   7780  C  C     . LEU A 1 2449 ? 151.105 182.255 189.094 1.00 83.67  ? 2449 LEU A C     1 
ATOM   7781  O  O     . LEU A 1 2449 ? 152.076 181.938 189.787 1.00 87.38  ? 2449 LEU A O     1 
ATOM   7782  C  CB    . LEU A 1 2449 ? 149.163 181.223 190.278 1.00 80.36  ? 2449 LEU A CB    1 
ATOM   7783  C  CG    . LEU A 1 2449 ? 148.245 182.411 190.573 1.00 73.28  ? 2449 LEU A CG    1 
ATOM   7784  C  CD1   . LEU A 1 2449 ? 146.987 182.338 189.725 1.00 73.89  ? 2449 LEU A CD1   1 
ATOM   7785  C  CD2   . LEU A 1 2449 ? 147.899 182.477 192.051 1.00 75.58  ? 2449 LEU A CD2   1 
ATOM   7786  N  N     . THR A 1 2450 ? 151.021 183.407 188.436 1.00 71.55  ? 2450 THR A N     1 
ATOM   7787  C  CA    . THR A 1 2450 ? 152.012 184.462 188.557 1.00 69.20  ? 2450 THR A CA    1 
ATOM   7788  C  C     . THR A 1 2450 ? 151.340 185.716 189.096 1.00 70.88  ? 2450 THR A C     1 
ATOM   7789  O  O     . THR A 1 2450 ? 150.165 185.976 188.822 1.00 75.68  ? 2450 THR A O     1 
ATOM   7790  C  CB    . THR A 1 2450 ? 152.682 184.762 187.213 1.00 77.62  ? 2450 THR A CB    1 
ATOM   7791  O  OG1   . THR A 1 2450 ? 151.689 184.804 186.182 1.00 78.21  ? 2450 THR A OG1   1 
ATOM   7792  C  CG2   . THR A 1 2450 ? 153.705 183.690 186.879 1.00 71.54  ? 2450 THR A CG2   1 
ATOM   7793  N  N     . ARG A 1 2451 ? 152.098 186.487 189.876 1.00 67.20  ? 2451 ARG A N     1 
ATOM   7794  C  CA    . ARG A 1 2451 ? 151.546 187.687 190.495 1.00 65.02  ? 2451 ARG A CA    1 
ATOM   7795  C  C     . ARG A 1 2451 ? 151.081 188.691 189.448 1.00 67.21  ? 2451 ARG A C     1 
ATOM   7796  O  O     . ARG A 1 2451 ? 149.994 189.272 189.570 1.00 79.41  ? 2451 ARG A O     1 
ATOM   7797  C  CB    . ARG A 1 2451 ? 152.589 188.318 191.414 1.00 66.50  ? 2451 ARG A CB    1 
ATOM   7798  C  CG    . ARG A 1 2451 ? 152.214 189.687 191.941 1.00 71.97  ? 2451 ARG A CG    1 
ATOM   7799  C  CD    . ARG A 1 2451 ? 153.355 190.281 192.746 1.00 72.83  ? 2451 ARG A CD    1 
ATOM   7800  N  NE    . ARG A 1 2451 ? 154.578 190.368 191.958 1.00 79.76  ? 2451 ARG A NE    1 
ATOM   7801  C  CZ    . ARG A 1 2451 ? 155.719 190.878 192.399 1.00 78.50  ? 2451 ARG A CZ    1 
ATOM   7802  N  NH1   . ARG A 1 2451 ? 155.831 191.360 193.625 1.00 78.45  ? 2451 ARG A NH1   1 
ATOM   7803  N  NH2   . ARG A 1 2451 ? 156.773 190.907 191.589 1.00 72.24  ? 2451 ARG A NH2   1 
ATOM   7804  N  N     . LEU A 1 2452 ? 151.882 188.898 188.403 1.00 49.09  ? 2452 LEU A N     1 
ATOM   7805  C  CA    . LEU A 1 2452 ? 151.567 189.941 187.436 1.00 55.50  ? 2452 LEU A CA    1 
ATOM   7806  C  C     . LEU A 1 2452 ? 150.376 189.586 186.559 1.00 65.05  ? 2452 LEU A C     1 
ATOM   7807  O  O     . LEU A 1 2452 ? 149.655 190.488 186.128 1.00 68.28  ? 2452 LEU A O     1 
ATOM   7808  C  CB    . LEU A 1 2452 ? 152.786 190.252 186.570 1.00 58.65  ? 2452 LEU A CB    1 
ATOM   7809  C  CG    . LEU A 1 2452 ? 153.653 191.386 187.118 1.00 59.19  ? 2452 LEU A CG    1 
ATOM   7810  C  CD1   . LEU A 1 2452 ? 154.587 191.905 186.048 1.00 56.32  ? 2452 LEU A CD1   1 
ATOM   7811  C  CD2   . LEU A 1 2452 ? 152.787 192.511 187.662 1.00 55.33  ? 2452 LEU A CD2   1 
ATOM   7812  N  N     . ARG A 1 2453 ? 150.139 188.302 186.288 1.00 59.21  ? 2453 ARG A N     1 
ATOM   7813  C  CA    . ARG A 1 2453 ? 148.937 187.925 185.548 1.00 59.66  ? 2453 ARG A CA    1 
ATOM   7814  C  C     . ARG A 1 2453 ? 147.681 188.309 186.322 1.00 59.76  ? 2453 ARG A C     1 
ATOM   7815  O  O     . ARG A 1 2453 ? 146.755 188.922 185.773 1.00 69.86  ? 2453 ARG A O     1 
ATOM   7816  C  CB    . ARG A 1 2453 ? 148.949 186.425 185.253 1.00 54.59  ? 2453 ARG A CB    1 
ATOM   7817  C  CG    . ARG A 1 2453 ? 147.659 185.913 184.636 1.00 55.32  ? 2453 ARG A CG    1 
ATOM   7818  C  CD    . ARG A 1 2453 ? 147.828 184.524 184.044 1.00 56.05  ? 2453 ARG A CD    1 
ATOM   7819  N  NE    . ARG A 1 2453 ? 148.218 183.537 185.042 1.00 53.05  ? 2453 ARG A NE    1 
ATOM   7820  C  CZ    . ARG A 1 2453 ? 147.457 182.520 185.422 1.00 60.48  ? 2453 ARG A CZ    1 
ATOM   7821  N  NH1   . ARG A 1 2453 ? 146.249 182.336 184.918 1.00 65.41  ? 2453 ARG A NH1   1 
ATOM   7822  N  NH2   . ARG A 1 2453 ? 147.920 181.665 186.329 1.00 60.10  ? 2453 ARG A NH2   1 
ATOM   7823  N  N     . CYS A 1 2454 ? 147.645 187.968 187.613 1.00 52.29  ? 2454 CYS A N     1 
ATOM   7824  C  CA    . CYS A 1 2454 ? 146.506 188.325 188.449 1.00 52.84  ? 2454 CYS A CA    1 
ATOM   7825  C  C     . CYS A 1 2454 ? 146.354 189.836 188.555 1.00 60.27  ? 2454 CYS A C     1 
ATOM   7826  O  O     . CYS A 1 2454 ? 145.238 190.364 188.470 1.00 70.31  ? 2454 CYS A O     1 
ATOM   7827  C  CB    . CYS A 1 2454 ? 146.668 187.706 189.836 1.00 63.46  ? 2454 CYS A CB    1 
ATOM   7828  S  SG    . CYS A 1 2454 ? 147.011 185.935 189.825 1.00 84.04  ? 2454 CYS A SG    1 
ATOM   7829  N  N     . LEU A 1 2455 ? 147.467 190.550 188.740 1.00 51.34  ? 2455 LEU A N     1 
ATOM   7830  C  CA    . LEU A 1 2455 ? 147.390 192.002 188.859 1.00 50.91  ? 2455 LEU A CA    1 
ATOM   7831  C  C     . LEU A 1 2455 ? 146.906 192.647 187.565 1.00 61.16  ? 2455 LEU A C     1 
ATOM   7832  O  O     . LEU A 1 2455 ? 146.106 193.587 187.601 1.00 70.92  ? 2455 LEU A O     1 
ATOM   7833  C  CB    . LEU A 1 2455 ? 148.746 192.566 189.279 1.00 58.47  ? 2455 LEU A CB    1 
ATOM   7834  C  CG    . LEU A 1 2455 ? 149.161 192.207 190.708 1.00 57.28  ? 2455 LEU A CG    1 
ATOM   7835  C  CD1   . LEU A 1 2455 ? 150.314 193.074 191.175 1.00 64.53  ? 2455 LEU A CD1   1 
ATOM   7836  C  CD2   . LEU A 1 2455 ? 147.980 192.338 191.653 1.00 52.57  ? 2455 LEU A CD2   1 
ATOM   7837  N  N     . GLY A 1 2456 ? 147.371 192.159 186.414 1.00 55.86  ? 2456 GLY A N     1 
ATOM   7838  C  CA    . GLY A 1 2456 ? 146.897 192.697 185.150 1.00 53.48  ? 2456 GLY A CA    1 
ATOM   7839  C  C     . GLY A 1 2456 ? 145.423 192.433 184.924 1.00 57.81  ? 2456 GLY A C     1 
ATOM   7840  O  O     . GLY A 1 2456 ? 144.690 193.311 184.457 1.00 64.14  ? 2456 GLY A O     1 
ATOM   7841  N  N     . SER A 1 2457 ? 144.965 191.222 185.256 1.00 57.57  ? 2457 SER A N     1 
ATOM   7842  C  CA    . SER A 1 2457 ? 143.540 190.921 185.157 1.00 50.85  ? 2457 SER A CA    1 
ATOM   7843  C  C     . SER A 1 2457 ? 142.726 191.861 186.035 1.00 58.36  ? 2457 SER A C     1 
ATOM   7844  O  O     . SER A 1 2457 ? 141.708 192.416 185.601 1.00 70.49  ? 2457 SER A O     1 
ATOM   7845  C  CB    . SER A 1 2457 ? 143.284 189.469 185.558 1.00 53.31  ? 2457 SER A CB    1 
ATOM   7846  O  OG    . SER A 1 2457 ? 144.056 188.578 184.777 1.00 67.00  ? 2457 SER A OG    1 
ATOM   7847  N  N     . LEU A 1 2458 ? 143.171 192.059 187.279 1.00 54.85  ? 2458 LEU A N     1 
ATOM   7848  C  CA    . LEU A 1 2458 ? 142.448 192.927 188.200 1.00 48.17  ? 2458 LEU A CA    1 
ATOM   7849  C  C     . LEU A 1 2458 ? 142.419 194.367 187.703 1.00 57.22  ? 2458 LEU A C     1 
ATOM   7850  O  O     . LEU A 1 2458 ? 141.379 195.034 187.768 1.00 70.94  ? 2458 LEU A O     1 
ATOM   7851  C  CB    . LEU A 1 2458 ? 143.083 192.846 189.587 1.00 41.95  ? 2458 LEU A CB    1 
ATOM   7852  C  CG    . LEU A 1 2458 ? 142.523 193.754 190.678 1.00 52.96  ? 2458 LEU A CG    1 
ATOM   7853  C  CD1   . LEU A 1 2458 ? 141.136 193.305 191.090 1.00 58.23  ? 2458 LEU A CD1   1 
ATOM   7854  C  CD2   . LEU A 1 2458 ? 143.459 193.756 191.871 1.00 57.26  ? 2458 LEU A CD2   1 
ATOM   7855  N  N     . PHE A 1 2459 ? 143.550 194.864 187.200 1.00 45.57  ? 2459 PHE A N     1 
ATOM   7856  C  CA    . PHE A 1 2459 ? 143.600 196.242 186.725 1.00 46.44  ? 2459 PHE A CA    1 
ATOM   7857  C  C     . PHE A 1 2459 ? 142.702 196.436 185.510 1.00 59.56  ? 2459 PHE A C     1 
ATOM   7858  O  O     . PHE A 1 2459 ? 141.997 197.447 185.407 1.00 72.70  ? 2459 PHE A O     1 
ATOM   7859  C  CB    . PHE A 1 2459 ? 145.042 196.635 186.400 1.00 50.62  ? 2459 PHE A CB    1 
ATOM   7860  C  CG    . PHE A 1 2459 ? 145.975 196.554 187.578 1.00 58.66  ? 2459 PHE A CG    1 
ATOM   7861  C  CD1   . PHE A 1 2459 ? 145.489 196.594 188.874 1.00 56.96  ? 2459 PHE A CD1   1 
ATOM   7862  C  CD2   . PHE A 1 2459 ? 147.341 196.437 187.387 1.00 63.83  ? 2459 PHE A CD2   1 
ATOM   7863  C  CE1   . PHE A 1 2459 ? 146.347 196.512 189.954 1.00 57.75  ? 2459 PHE A CE1   1 
ATOM   7864  C  CE2   . PHE A 1 2459 ? 148.202 196.358 188.464 1.00 56.55  ? 2459 PHE A CE2   1 
ATOM   7865  C  CZ    . PHE A 1 2459 ? 147.703 196.396 189.748 1.00 53.58  ? 2459 PHE A CZ    1 
ATOM   7866  N  N     . SER A 1 2460 ? 142.710 195.476 184.580 1.00 55.29  ? 2460 SER A N     1 
ATOM   7867  C  CA    . SER A 1 2460 ? 141.828 195.574 183.423 1.00 55.11  ? 2460 SER A CA    1 
ATOM   7868  C  C     . SER A 1 2460 ? 140.364 195.534 183.844 1.00 54.29  ? 2460 SER A C     1 
ATOM   7869  O  O     . SER A 1 2460 ? 139.530 196.273 183.299 1.00 62.18  ? 2460 SER A O     1 
ATOM   7870  C  CB    . SER A 1 2460 ? 142.140 194.457 182.429 1.00 56.14  ? 2460 SER A CB    1 
ATOM   7871  O  OG    . SER A 1 2460 ? 143.485 194.538 181.991 1.00 70.48  ? 2460 SER A OG    1 
ATOM   7872  N  N     . MET A 1 2461 ? 140.029 194.693 184.826 1.00 53.12  ? 2461 MET A N     1 
ATOM   7873  C  CA    . MET A 1 2461 ? 138.634 194.618 185.241 1.00 56.47  ? 2461 MET A CA    1 
ATOM   7874  C  C     . MET A 1 2461 ? 138.204 195.910 185.927 1.00 65.98  ? 2461 MET A C     1 
ATOM   7875  O  O     . MET A 1 2461 ? 137.073 196.372 185.742 1.00 76.60  ? 2461 MET A O     1 
ATOM   7876  C  CB    . MET A 1 2461 ? 138.401 193.416 186.157 1.00 54.15  ? 2461 MET A CB    1 
ATOM   7877  C  CG    . MET A 1 2461 ? 138.070 192.160 185.366 1.00 60.12  ? 2461 MET A CG    1 
ATOM   7878  S  SD    . MET A 1 2461 ? 138.148 190.591 186.239 1.00 71.53  ? 2461 MET A SD    1 
ATOM   7879  C  CE    . MET A 1 2461 ? 136.594 190.670 187.111 1.00 66.18  ? 2461 MET A CE    1 
ATOM   7880  N  N     . LEU A 1 2462 ? 139.105 196.523 186.701 1.00 57.27  ? 2462 LEU A N     1 
ATOM   7881  C  CA    . LEU A 1 2462 ? 138.773 197.785 187.357 1.00 58.82  ? 2462 LEU A CA    1 
ATOM   7882  C  C     . LEU A 1 2462 ? 138.632 198.917 186.343 1.00 61.30  ? 2462 LEU A C     1 
ATOM   7883  O  O     . LEU A 1 2462 ? 137.777 199.800 186.499 1.00 72.84  ? 2462 LEU A O     1 
ATOM   7884  C  CB    . LEU A 1 2462 ? 139.831 198.125 188.405 1.00 52.13  ? 2462 LEU A CB    1 
ATOM   7885  C  CG    . LEU A 1 2462 ? 139.860 197.194 189.619 1.00 53.66  ? 2462 LEU A CG    1 
ATOM   7886  C  CD1   . LEU A 1 2462 ? 141.076 197.469 190.489 1.00 59.62  ? 2462 LEU A CD1   1 
ATOM   7887  C  CD2   . LEU A 1 2462 ? 138.577 197.296 190.424 1.00 53.53  ? 2462 LEU A CD2   1 
ATOM   7888  N  N     . HIS A 1 2463 ? 139.461 198.908 185.297 1.00 56.21  ? 2463 HIS A N     1 
ATOM   7889  C  CA    . HIS A 1 2463 ? 139.279 199.870 184.216 1.00 59.19  ? 2463 HIS A CA    1 
ATOM   7890  C  C     . HIS A 1 2463 ? 137.918 199.695 183.557 1.00 66.38  ? 2463 HIS A C     1 
ATOM   7891  O  O     . HIS A 1 2463 ? 137.234 200.680 183.251 1.00 69.53  ? 2463 HIS A O     1 
ATOM   7892  C  CB    . HIS A 1 2463 ? 140.395 199.720 183.184 1.00 58.72  ? 2463 HIS A CB    1 
ATOM   7893  C  CG    . HIS A 1 2463 ? 141.754 200.047 183.714 1.00 63.47  ? 2463 HIS A CG    1 
ATOM   7894  N  ND1   . HIS A 1 2463 ? 142.909 199.811 183.000 1.00 68.40  ? 2463 HIS A ND1   1 
ATOM   7895  C  CD2   . HIS A 1 2463 ? 142.143 200.594 184.890 1.00 62.30  ? 2463 HIS A CD2   1 
ATOM   7896  C  CE1   . HIS A 1 2463 ? 143.951 200.198 183.714 1.00 69.64  ? 2463 HIS A CE1   1 
ATOM   7897  N  NE2   . HIS A 1 2463 ? 143.514 200.677 184.864 1.00 65.74  ? 2463 HIS A NE2   1 
ATOM   7898  N  N     . GLN A 1 2464 ? 137.506 198.445 183.334 1.00 71.83  ? 2464 GLN A N     1 
ATOM   7899  C  CA    . GLN A 1 2464 ? 136.184 198.205 182.762 1.00 68.65  ? 2464 GLN A CA    1 
ATOM   7900  C  C     . GLN A 1 2464 ? 135.079 198.672 183.703 1.00 71.29  ? 2464 GLN A C     1 
ATOM   7901  O  O     . GLN A 1 2464 ? 134.028 199.135 183.252 1.00 84.35  ? 2464 GLN A O     1 
ATOM   7902  C  CB    . GLN A 1 2464 ? 136.011 196.728 182.422 1.00 70.74  ? 2464 GLN A CB    1 
ATOM   7903  C  CG    . GLN A 1 2464 ? 134.780 196.433 181.580 1.00 79.61  ? 2464 GLN A CG    1 
ATOM   7904  C  CD    . GLN A 1 2464 ? 134.633 197.375 180.400 1.00 80.85  ? 2464 GLN A CD    1 
ATOM   7905  O  OE1   . GLN A 1 2464 ? 135.590 197.630 179.669 1.00 77.49  ? 2464 GLN A OE1   1 
ATOM   7906  N  NE2   . GLN A 1 2464 ? 133.427 197.897 180.208 1.00 71.94  ? 2464 GLN A NE2   1 
ATOM   7907  N  N     . ALA A 1 2465 ? 135.295 198.552 185.014 1.00 63.32  ? 2465 ALA A N     1 
ATOM   7908  C  CA    . ALA A 1 2465 ? 134.329 199.091 185.970 1.00 71.52  ? 2465 ALA A CA    1 
ATOM   7909  C  C     . ALA A 1 2465 ? 134.218 200.606 185.847 1.00 74.55  ? 2465 ALA A C     1 
ATOM   7910  O  O     . ALA A 1 2465 ? 133.116 201.169 185.907 1.00 75.97  ? 2465 ALA A O     1 
ATOM   7911  C  CB    . ALA A 1 2465 ? 134.721 198.704 187.394 1.00 62.45  ? 2465 ALA A CB    1 
ATOM   7912  N  N     . CYS A 1 2466 ? 135.355 201.284 185.687 1.00 77.82  ? 2466 CYS A N     1 
ATOM   7913  C  CA    . CYS A 1 2466 ? 135.326 202.731 185.489 1.00 74.78  ? 2466 CYS A CA    1 
ATOM   7914  C  C     . CYS A 1 2466 ? 134.580 203.096 184.209 1.00 77.63  ? 2466 CYS A C     1 
ATOM   7915  O  O     . CYS A 1 2466 ? 133.796 204.055 184.187 1.00 87.31  ? 2466 CYS A O     1 
ATOM   7916  C  CB    . CYS A 1 2466 ? 136.748 203.287 185.464 1.00 77.84  ? 2466 CYS A CB    1 
ATOM   7917  S  SG    . CYS A 1 2466 ? 137.634 203.112 187.029 1.00 96.83  ? 2466 CYS A SG    1 
ATOM   7918  N  N     . ARG A 1 2467 ? 134.806 202.339 183.132 1.00 75.39  ? 2467 ARG A N     1 
ATOM   7919  C  CA    . ARG A 1 2467 ? 134.066 202.592 181.897 1.00 75.65  ? 2467 ARG A CA    1 
ATOM   7920  C  C     . ARG A 1 2467 ? 132.577 202.312 182.070 1.00 78.09  ? 2467 ARG A C     1 
ATOM   7921  O  O     . ARG A 1 2467 ? 131.741 202.977 181.453 1.00 83.47  ? 2467 ARG A O     1 
ATOM   7922  C  CB    . ARG A 1 2467 ? 134.631 201.765 180.742 1.00 79.36  ? 2467 ARG A CB    1 
ATOM   7923  C  CG    . ARG A 1 2467 ? 136.139 201.786 180.623 1.00 79.83  ? 2467 ARG A CG    1 
ATOM   7924  C  CD    . ARG A 1 2467 ? 136.613 200.770 179.597 1.00 74.89  ? 2467 ARG A CD    1 
ATOM   7925  N  NE    . ARG A 1 2467 ? 137.855 201.171 178.946 1.00 75.98  ? 2467 ARG A NE    1 
ATOM   7926  C  CZ    . ARG A 1 2467 ? 137.967 202.179 178.092 1.00 82.84  ? 2467 ARG A CZ    1 
ATOM   7927  N  NH1   . ARG A 1 2467 ? 136.921 202.908 177.738 1.00 78.88  ? 2467 ARG A NH1   1 
ATOM   7928  N  NH2   . ARG A 1 2467 ? 139.160 202.459 177.574 1.00 86.32  ? 2467 ARG A NH2   1 
ATOM   7929  N  N     . ASN A 1 2468 ? 132.227 201.321 182.893 1.00 76.74  ? 2468 ASN A N     1 
ATOM   7930  C  CA    . ASN A 1 2468 ? 130.820 201.065 183.186 1.00 75.10  ? 2468 ASN A CA    1 
ATOM   7931  C  C     . ASN A 1 2468 ? 130.189 202.250 183.903 1.00 76.09  ? 2468 ASN A C     1 
ATOM   7932  O  O     . ASN A 1 2468 ? 129.057 202.644 183.598 1.00 80.71  ? 2468 ASN A O     1 
ATOM   7933  C  CB    . ASN A 1 2468 ? 130.678 199.797 184.027 1.00 70.57  ? 2468 ASN A CB    1 
ATOM   7934  C  CG    . ASN A 1 2468 ? 130.904 198.534 183.223 1.00 77.41  ? 2468 ASN A CG    1 
ATOM   7935  O  OD1   . ASN A 1 2468 ? 131.047 198.578 182.001 1.00 83.35  ? 2468 ASN A OD1   1 
ATOM   7936  N  ND2   . ASN A 1 2468 ? 130.936 197.396 183.907 1.00 79.35  ? 2468 ASN A ND2   1 
ATOM   7937  N  N     . VAL A 1 2469 ? 130.911 202.829 184.864 1.00 71.95  ? 2469 VAL A N     1 
ATOM   7938  C  CA    . VAL A 1 2469 ? 130.414 204.019 185.552 1.00 77.25  ? 2469 VAL A CA    1 
ATOM   7939  C  C     . VAL A 1 2469 ? 130.238 205.170 184.567 1.00 83.19  ? 2469 VAL A C     1 
ATOM   7940  O  O     . VAL A 1 2469 ? 129.238 205.900 184.607 1.00 85.70  ? 2469 VAL A O     1 
ATOM   7941  C  CB    . VAL A 1 2469 ? 131.358 204.404 186.705 1.00 75.99  ? 2469 VAL A CB    1 
ATOM   7942  C  CG1   . VAL A 1 2469 ? 130.913 205.707 187.338 1.00 76.50  ? 2469 VAL A CG1   1 
ATOM   7943  C  CG2   . VAL A 1 2469 ? 131.408 203.297 187.737 1.00 74.27  ? 2469 VAL A CG2   1 
ATOM   7944  N  N     . ALA A 1 2470 ? 131.211 205.353 183.672 1.00 84.76  ? 2470 ALA A N     1 
ATOM   7945  C  CA    . ALA A 1 2470 ? 131.110 206.418 182.679 1.00 79.37  ? 2470 ALA A CA    1 
ATOM   7946  C  C     . ALA A 1 2470 ? 129.920 206.203 181.751 1.00 89.95  ? 2470 ALA A C     1 
ATOM   7947  O  O     . ALA A 1 2470 ? 129.221 207.158 181.394 1.00 92.38  ? 2470 ALA A O     1 
ATOM   7948  C  CB    . ALA A 1 2470 ? 132.403 206.512 181.875 1.00 83.19  ? 2470 ALA A CB    1 
ATOM   7949  N  N     . GLN A 1 2471 ? 129.683 204.956 181.339 1.00 103.07 ? 2471 GLN A N     1 
ATOM   7950  C  CA    . GLN A 1 2471 ? 128.538 204.660 180.485 1.00 99.58  ? 2471 GLN A CA    1 
ATOM   7951  C  C     . GLN A 1 2471 ? 127.227 204.917 181.216 1.00 99.58  ? 2471 GLN A C     1 
ATOM   7952  O  O     . GLN A 1 2471 ? 126.268 205.428 180.626 1.00 106.07 ? 2471 GLN A O     1 
ATOM   7953  C  CB    . GLN A 1 2471 ? 128.612 203.214 179.993 1.00 97.40  ? 2471 GLN A CB    1 
ATOM   7954  C  CG    . GLN A 1 2471 ? 127.262 202.567 179.725 1.00 101.04 ? 2471 GLN A CG    1 
ATOM   7955  C  CD    . GLN A 1 2471 ? 127.379 201.094 179.386 1.00 107.16 ? 2471 GLN A CD    1 
ATOM   7956  O  OE1   . GLN A 1 2471 ? 127.998 200.723 178.389 1.00 106.04 ? 2471 GLN A OE1   1 
ATOM   7957  N  NE2   . GLN A 1 2471 ? 126.781 200.246 180.215 1.00 107.10 ? 2471 GLN A NE2   1 
ATOM   7958  N  N     . TYR A 1 2472 ? 127.167 204.570 182.505 1.00 91.27  ? 2472 TYR A N     1 
ATOM   7959  C  CA    . TYR A 1 2472 ? 125.975 204.868 183.292 1.00 92.25  ? 2472 TYR A CA    1 
ATOM   7960  C  C     . TYR A 1 2472 ? 125.729 206.369 183.360 1.00 94.38  ? 2472 TYR A C     1 
ATOM   7961  O  O     . TYR A 1 2472 ? 124.586 206.825 183.243 1.00 102.17 ? 2472 TYR A O     1 
ATOM   7962  C  CB    . TYR A 1 2472 ? 126.109 204.271 184.696 1.00 93.36  ? 2472 TYR A CB    1 
ATOM   7963  C  CG    . TYR A 1 2472 ? 125.115 204.794 185.721 1.00 94.82  ? 2472 TYR A CG    1 
ATOM   7964  C  CD1   . TYR A 1 2472 ? 123.961 204.082 186.017 1.00 96.90  ? 2472 TYR A CD1   1 
ATOM   7965  C  CD2   . TYR A 1 2472 ? 125.354 205.969 186.426 1.00 95.49  ? 2472 TYR A CD2   1 
ATOM   7966  C  CE1   . TYR A 1 2472 ? 123.055 204.541 186.956 1.00 97.45  ? 2472 TYR A CE1   1 
ATOM   7967  C  CE2   . TYR A 1 2472 ? 124.452 206.436 187.365 1.00 98.27  ? 2472 TYR A CE2   1 
ATOM   7968  C  CZ    . TYR A 1 2472 ? 123.308 205.717 187.628 1.00 98.94  ? 2472 TYR A CZ    1 
ATOM   7969  O  OH    . TYR A 1 2472 ? 122.412 206.179 188.566 1.00 99.93  ? 2472 TYR A OH    1 
ATOM   7970  N  N     . ASN A 1 2473 ? 126.792 207.151 183.558 1.00 96.41  ? 2473 ASN A N     1 
ATOM   7971  C  CA    . ASN A 1 2473 ? 126.642 208.604 183.563 1.00 100.86 ? 2473 ASN A CA    1 
ATOM   7972  C  C     . ASN A 1 2473 ? 126.164 209.115 182.209 1.00 100.41 ? 2473 ASN A C     1 
ATOM   7973  O  O     . ASN A 1 2473 ? 125.318 210.014 182.140 1.00 102.64 ? 2473 ASN A O     1 
ATOM   7974  C  CB    . ASN A 1 2473 ? 127.961 209.271 183.951 1.00 102.45 ? 2473 ASN A CB    1 
ATOM   7975  C  CG    . ASN A 1 2473 ? 128.100 209.458 185.447 1.00 102.22 ? 2473 ASN A CG    1 
ATOM   7976  O  OD1   . ASN A 1 2473 ? 127.249 209.018 186.221 1.00 100.84 ? 2473 ASN A OD1   1 
ATOM   7977  N  ND2   . ASN A 1 2473 ? 129.175 210.115 185.864 1.00 102.37 ? 2473 ASN A ND2   1 
ATOM   7978  N  N     . ALA A 1 2474 ? 126.701 208.557 181.122 1.00 101.69 ? 2474 ALA A N     1 
ATOM   7979  C  CA    . ALA A 1 2474 ? 126.295 208.987 179.788 1.00 103.25 ? 2474 ALA A CA    1 
ATOM   7980  C  C     . ALA A 1 2474 ? 124.826 208.679 179.526 1.00 103.42 ? 2474 ALA A C     1 
ATOM   7981  O  O     . ALA A 1 2474 ? 124.112 209.486 178.920 1.00 104.92 ? 2474 ALA A O     1 
ATOM   7982  C  CB    . ALA A 1 2474 ? 127.178 208.325 178.731 1.00 103.98 ? 2474 ALA A CB    1 
ATOM   7983  N  N     . ASN A 1 2475 ? 124.355 207.512 179.973 1.00 105.38 ? 2475 ASN A N     1 
ATOM   7984  C  CA    . ASN A 1 2475 ? 122.959 207.145 179.762 1.00 105.00 ? 2475 ASN A CA    1 
ATOM   7985  C  C     . ASN A 1 2475 ? 122.007 207.938 180.646 1.00 106.15 ? 2475 ASN A C     1 
ATOM   7986  O  O     . ASN A 1 2475 ? 120.794 207.902 180.414 1.00 111.79 ? 2475 ASN A O     1 
ATOM   7987  C  CB    . ASN A 1 2475 ? 122.763 205.647 180.004 1.00 106.42 ? 2475 ASN A CB    1 
ATOM   7988  C  CG    . ASN A 1 2475 ? 123.403 204.794 178.927 1.00 110.70 ? 2475 ASN A CG    1 
ATOM   7989  O  OD1   . ASN A 1 2475 ? 123.738 205.284 177.848 1.00 112.56 ? 2475 ASN A OD1   1 
ATOM   7990  N  ND2   . ASN A 1 2475 ? 123.573 203.509 179.213 1.00 107.77 ? 2475 ASN A ND2   1 
ATOM   7991  N  N     . HIS A 1 2476 ? 122.521 208.649 181.647 1.00 101.33 ? 2476 HIS A N     1 
ATOM   7992  C  CA    . HIS A 1 2476 ? 121.706 209.444 182.565 1.00 103.61 ? 2476 HIS A CA    1 
ATOM   7993  C  C     . HIS A 1 2476 ? 122.266 210.860 182.624 1.00 105.21 ? 2476 HIS A C     1 
ATOM   7994  O  O     . HIS A 1 2476 ? 122.878 211.259 183.622 1.00 105.34 ? 2476 HIS A O     1 
ATOM   7995  C  CB    . HIS A 1 2476 ? 121.670 208.813 183.958 1.00 103.81 ? 2476 HIS A CB    1 
ATOM   7996  C  CG    . HIS A 1 2476 ? 121.008 207.471 184.003 1.00 103.91 ? 2476 HIS A CG    1 
ATOM   7997  N  ND1   . HIS A 1 2476 ? 121.431 206.404 183.239 1.00 103.89 ? 2476 HIS A ND1   1 
ATOM   7998  C  CD2   . HIS A 1 2476 ? 119.958 207.020 184.729 1.00 102.89 ? 2476 HIS A CD2   1 
ATOM   7999  C  CE1   . HIS A 1 2476 ? 120.667 205.356 183.488 1.00 104.48 ? 2476 HIS A CE1   1 
ATOM   8000  N  NE2   . HIS A 1 2476 ? 119.765 205.703 184.389 1.00 104.03 ? 2476 HIS A NE2   1 
ATOM   8001  N  N     . PRO A 1 2477 ? 122.082 211.646 181.558 1.00 110.62 ? 2477 PRO A N     1 
ATOM   8002  C  CA    . PRO A 1 2477 ? 122.643 213.009 181.556 1.00 111.43 ? 2477 PRO A CA    1 
ATOM   8003  C  C     . PRO A 1 2477 ? 122.091 213.895 182.658 1.00 109.86 ? 2477 PRO A C     1 
ATOM   8004  O  O     . PRO A 1 2477 ? 122.822 214.734 183.199 1.00 110.24 ? 2477 PRO A O     1 
ATOM   8005  C  CB    . PRO A 1 2477 ? 122.270 213.539 180.162 1.00 108.44 ? 2477 PRO A CB    1 
ATOM   8006  C  CG    . PRO A 1 2477 ? 121.917 212.325 179.356 1.00 107.21 ? 2477 PRO A CG    1 
ATOM   8007  C  CD    . PRO A 1 2477 ? 121.328 211.360 180.328 1.00 107.13 ? 2477 PRO A CD    1 
ATOM   8008  N  N     . ASP A 1 2478 ? 120.813 213.736 183.006 1.00 119.24 ? 2478 ASP A N     1 
ATOM   8009  C  CA    . ASP A 1 2478 ? 120.211 214.603 184.012 1.00 122.26 ? 2478 ASP A CA    1 
ATOM   8010  C  C     . ASP A 1 2478 ? 120.664 214.228 185.417 1.00 120.05 ? 2478 ASP A C     1 
ATOM   8011  O  O     . ASP A 1 2478 ? 120.880 215.106 186.261 1.00 119.18 ? 2478 ASP A O     1 
ATOM   8012  C  CB    . ASP A 1 2478 ? 118.688 214.548 183.910 1.00 120.38 ? 2478 ASP A CB    1 
ATOM   8013  C  CG    . ASP A 1 2478 ? 118.013 215.648 184.704 1.00 121.92 ? 2478 ASP A CG    1 
ATOM   8014  O  OD1   . ASP A 1 2478 ? 118.227 216.835 184.377 1.00 121.89 ? 2478 ASP A OD1   1 
ATOM   8015  O  OD2   . ASP A 1 2478 ? 117.272 215.327 185.656 1.00 120.47 ? 2478 ASP A OD2   1 
ATOM   8016  N  N     . PHE A 1 2479 ? 120.808 212.932 185.691 1.00 118.71 ? 2479 PHE A N     1 
ATOM   8017  C  CA    . PHE A 1 2479 ? 121.135 212.429 187.023 1.00 119.02 ? 2479 PHE A CA    1 
ATOM   8018  C  C     . PHE A 1 2479 ? 122.424 211.626 186.911 1.00 122.63 ? 2479 PHE A C     1 
ATOM   8019  O  O     . PHE A 1 2479 ? 122.391 210.416 186.634 1.00 122.01 ? 2479 PHE A O     1 
ATOM   8020  C  CB    . PHE A 1 2479 ? 119.989 211.581 187.577 1.00 119.42 ? 2479 PHE A CB    1 
ATOM   8021  C  CG    . PHE A 1 2479 ? 120.293 210.901 188.890 1.00 120.71 ? 2479 PHE A CG    1 
ATOM   8022  C  CD1   . PHE A 1 2479 ? 119.556 209.798 189.287 1.00 120.75 ? 2479 PHE A CD1   1 
ATOM   8023  C  CD2   . PHE A 1 2479 ? 121.260 211.396 189.753 1.00 119.83 ? 2479 PHE A CD2   1 
ATOM   8024  C  CE1   . PHE A 1 2479 ? 119.812 209.171 190.489 1.00 119.77 ? 2479 PHE A CE1   1 
ATOM   8025  C  CE2   . PHE A 1 2479 ? 121.520 210.772 190.957 1.00 120.58 ? 2479 PHE A CE2   1 
ATOM   8026  C  CZ    . PHE A 1 2479 ? 120.793 209.660 191.327 1.00 120.40 ? 2479 PHE A CZ    1 
ATOM   8027  N  N     . PRO A 1 2480 ? 123.578 212.249 187.121 1.00 116.06 ? 2480 PRO A N     1 
ATOM   8028  C  CA    . PRO A 1 2480 ? 124.836 211.501 187.132 1.00 113.76 ? 2480 PRO A CA    1 
ATOM   8029  C  C     . PRO A 1 2480 ? 125.017 210.766 188.454 1.00 111.81 ? 2480 PRO A C     1 
ATOM   8030  O  O     . PRO A 1 2480 ? 124.359 211.050 189.455 1.00 110.45 ? 2480 PRO A O     1 
ATOM   8031  C  CB    . PRO A 1 2480 ? 125.908 212.582 186.940 1.00 110.90 ? 2480 PRO A CB    1 
ATOM   8032  C  CG    . PRO A 1 2480 ? 125.217 213.904 187.171 1.00 110.41 ? 2480 PRO A CG    1 
ATOM   8033  C  CD    . PRO A 1 2480 ? 123.765 213.667 187.460 1.00 112.40 ? 2480 PRO A CD    1 
ATOM   8034  N  N     . MET A 1 2481 ? 125.935 209.803 188.439 1.00 106.11 ? 2481 MET A N     1 
ATOM   8035  C  CA    . MET A 1 2481 ? 126.146 208.959 189.608 1.00 107.28 ? 2481 MET A CA    1 
ATOM   8036  C  C     . MET A 1 2481 ? 126.751 209.766 190.750 1.00 108.17 ? 2481 MET A C     1 
ATOM   8037  O  O     . MET A 1 2481 ? 127.705 210.525 190.560 1.00 107.55 ? 2481 MET A O     1 
ATOM   8038  C  CB    . MET A 1 2481 ? 127.052 207.781 189.254 1.00 107.00 ? 2481 MET A CB    1 
ATOM   8039  C  CG    . MET A 1 2481 ? 127.690 207.104 190.451 1.00 106.82 ? 2481 MET A CG    1 
ATOM   8040  S  SD    . MET A 1 2481 ? 128.634 205.645 189.983 1.00 109.87 ? 2481 MET A SD    1 
ATOM   8041  C  CE    . MET A 1 2481 ? 127.399 204.364 190.162 1.00 106.94 ? 2481 MET A CE    1 
ATOM   8042  N  N     . GLN A 1 2482 ? 126.190 209.595 191.943 1.00 112.05 ? 2482 GLN A N     1 
ATOM   8043  C  CA    . GLN A 1 2482 ? 126.633 210.316 193.123 1.00 110.51 ? 2482 GLN A CA    1 
ATOM   8044  C  C     . GLN A 1 2482 ? 127.819 209.598 193.762 1.00 111.80 ? 2482 GLN A C     1 
ATOM   8045  O  O     . GLN A 1 2482 ? 128.283 208.558 193.289 1.00 115.22 ? 2482 GLN A O     1 
ATOM   8046  C  CB    . GLN A 1 2482 ? 125.479 210.476 194.115 1.00 111.09 ? 2482 GLN A CB    1 
ATOM   8047  C  CG    . GLN A 1 2482 ? 124.593 211.678 193.834 1.00 112.25 ? 2482 GLN A CG    1 
ATOM   8048  C  CD    . GLN A 1 2482 ? 125.155 212.963 194.407 1.00 114.46 ? 2482 GLN A CD    1 
ATOM   8049  O  OE1   . GLN A 1 2482 ? 125.002 213.246 195.595 1.00 114.76 ? 2482 GLN A OE1   1 
ATOM   8050  N  NE2   . GLN A 1 2482 ? 125.811 213.750 193.562 1.00 113.85 ? 2482 GLN A NE2   1 
ATOM   8051  N  N     . ILE A 1 2483 ? 128.319 210.171 194.858 1.00 114.35 ? 2483 ILE A N     1 
ATOM   8052  C  CA    . ILE A 1 2483 ? 129.520 209.640 195.496 1.00 114.63 ? 2483 ILE A CA    1 
ATOM   8053  C  C     . ILE A 1 2483 ? 129.226 208.309 196.184 1.00 114.40 ? 2483 ILE A C     1 
ATOM   8054  O  O     . ILE A 1 2483 ? 130.031 207.373 196.122 1.00 115.50 ? 2483 ILE A O     1 
ATOM   8055  C  CB    . ILE A 1 2483 ? 130.113 210.676 196.470 1.00 116.05 ? 2483 ILE A CB    1 
ATOM   8056  C  CG1   . ILE A 1 2483 ? 131.428 210.171 197.071 1.00 114.27 ? 2483 ILE A CG1   1 
ATOM   8057  C  CG2   . ILE A 1 2483 ? 129.107 211.067 197.551 1.00 113.97 ? 2483 ILE A CG2   1 
ATOM   8058  C  CD1   . ILE A 1 2483 ? 132.397 209.610 196.051 1.00 108.77 ? 2483 ILE A CD1   1 
ATOM   8059  N  N     . GLU A 1 2484 ? 128.073 208.201 196.850 1.00 113.40 ? 2484 GLU A N     1 
ATOM   8060  C  CA    . GLU A 1 2484 ? 127.762 206.985 197.599 1.00 115.46 ? 2484 GLU A CA    1 
ATOM   8061  C  C     . GLU A 1 2484 ? 127.557 205.794 196.670 1.00 116.83 ? 2484 GLU A C     1 
ATOM   8062  O  O     . GLU A 1 2484 ? 128.043 204.687 196.947 1.00 114.04 ? 2484 GLU A O     1 
ATOM   8063  C  CB    . GLU A 1 2484 ? 126.523 207.212 198.466 1.00 115.32 ? 2484 GLU A CB    1 
ATOM   8064  C  CG    . GLU A 1 2484 ? 126.052 205.991 199.249 1.00 117.37 ? 2484 GLU A CG    1 
ATOM   8065  C  CD    . GLU A 1 2484 ? 127.182 205.224 199.916 1.00 118.47 ? 2484 GLU A CD    1 
ATOM   8066  O  OE1   . GLU A 1 2484 ? 127.109 203.978 199.952 1.00 117.04 ? 2484 GLU A OE1   1 
ATOM   8067  O  OE2   . GLU A 1 2484 ? 128.124 205.861 200.433 1.00 119.56 ? 2484 GLU A OE2   1 
ATOM   8068  N  N     . GLN A 1 2485 ? 126.833 206.002 195.568 1.00 107.53 ? 2485 GLN A N     1 
ATOM   8069  C  CA    . GLN A 1 2485 ? 126.649 204.938 194.588 1.00 102.94 ? 2485 GLN A CA    1 
ATOM   8070  C  C     . GLN A 1 2485 ? 127.986 204.499 194.012 1.00 102.90 ? 2485 GLN A C     1 
ATOM   8071  O  O     . GLN A 1 2485 ? 128.235 203.300 193.836 1.00 105.68 ? 2485 GLN A O     1 
ATOM   8072  C  CB    . GLN A 1 2485 ? 125.714 205.413 193.476 1.00 103.52 ? 2485 GLN A CB    1 
ATOM   8073  C  CG    . GLN A 1 2485 ? 124.940 204.308 192.783 1.00 104.55 ? 2485 GLN A CG    1 
ATOM   8074  C  CD    . GLN A 1 2485 ? 123.541 204.147 193.338 1.00 110.33 ? 2485 GLN A CD    1 
ATOM   8075  O  OE1   . GLN A 1 2485 ? 123.253 204.570 194.457 1.00 109.70 ? 2485 GLN A OE1   1 
ATOM   8076  N  NE2   . GLN A 1 2485 ? 122.660 203.539 192.553 1.00 109.61 ? 2485 GLN A NE2   1 
ATOM   8077  N  N     . LEU A 1 2486 ? 128.863 205.463 193.720 1.00 96.10  ? 2486 LEU A N     1 
ATOM   8078  C  CA    . LEU A 1 2486 ? 130.187 205.134 193.206 1.00 93.21  ? 2486 LEU A CA    1 
ATOM   8079  C  C     . LEU A 1 2486 ? 130.981 204.317 194.214 1.00 93.00  ? 2486 LEU A C     1 
ATOM   8080  O  O     . LEU A 1 2486 ? 131.629 203.333 193.847 1.00 96.49  ? 2486 LEU A O     1 
ATOM   8081  C  CB    . LEU A 1 2486 ? 130.936 206.414 192.839 1.00 91.60  ? 2486 LEU A CB    1 
ATOM   8082  C  CG    . LEU A 1 2486 ? 132.264 206.252 192.099 1.00 93.26  ? 2486 LEU A CG    1 
ATOM   8083  C  CD1   . LEU A 1 2486 ? 132.124 205.260 190.958 1.00 97.62  ? 2486 LEU A CD1   1 
ATOM   8084  C  CD2   . LEU A 1 2486 ? 132.748 207.595 191.583 1.00 93.46  ? 2486 LEU A CD2   1 
ATOM   8085  N  N     . GLU A 1 2487 ? 130.932 204.700 195.492 1.00 104.28 ? 2487 GLU A N     1 
ATOM   8086  C  CA    . GLU A 1 2487 ? 131.650 203.951 196.519 1.00 104.55 ? 2487 GLU A CA    1 
ATOM   8087  C  C     . GLU A 1 2487 ? 131.153 202.514 196.596 1.00 106.36 ? 2487 GLU A C     1 
ATOM   8088  O  O     . GLU A 1 2487 ? 131.948 201.565 196.581 1.00 109.37 ? 2487 GLU A O     1 
ATOM   8089  C  CB    . GLU A 1 2487 ? 131.493 204.636 197.877 1.00 105.26 ? 2487 GLU A CB    1 
ATOM   8090  C  CG    . GLU A 1 2487 ? 132.155 205.994 197.987 1.00 110.19 ? 2487 GLU A CG    1 
ATOM   8091  C  CD    . GLU A 1 2487 ? 132.460 206.372 199.422 1.00 112.31 ? 2487 GLU A CD    1 
ATOM   8092  O  OE1   . GLU A 1 2487 ? 132.333 205.499 200.306 1.00 110.57 ? 2487 GLU A OE1   1 
ATOM   8093  O  OE2   . GLU A 1 2487 ? 132.823 207.542 199.666 1.00 110.44 ? 2487 GLU A OE2   1 
ATOM   8094  N  N     . ARG A 1 2488 ? 129.831 202.337 196.676 1.00 98.74  ? 2488 ARG A N     1 
ATOM   8095  C  CA    . ARG A 1 2488 ? 129.271 200.994 196.791 1.00 96.44  ? 2488 ARG A CA    1 
ATOM   8096  C  C     . ARG A 1 2488 ? 129.637 200.144 195.580 1.00 94.84  ? 2488 ARG A C     1 
ATOM   8097  O  O     . ARG A 1 2488 ? 130.108 199.004 195.719 1.00 93.24  ? 2488 ARG A O     1 
ATOM   8098  C  CB    . ARG A 1 2488 ? 127.753 201.074 196.954 1.00 97.50  ? 2488 ARG A CB    1 
ATOM   8099  C  CG    . ARG A 1 2488 ? 127.276 201.075 198.395 1.00 96.37  ? 2488 ARG A CG    1 
ATOM   8100  C  CD    . ARG A 1 2488 ? 125.763 200.932 198.471 1.00 99.93  ? 2488 ARG A CD    1 
ATOM   8101  N  NE    . ARG A 1 2488 ? 125.094 201.605 197.364 1.00 104.03 ? 2488 ARG A NE    1 
ATOM   8102  C  CZ    . ARG A 1 2488 ? 124.363 202.704 197.487 1.00 102.05 ? 2488 ARG A CZ    1 
ATOM   8103  N  NH1   . ARG A 1 2488 ? 124.179 203.284 198.661 1.00 99.34  ? 2488 ARG A NH1   1 
ATOM   8104  N  NH2   . ARG A 1 2488 ? 123.800 203.234 196.404 1.00 99.90  ? 2488 ARG A NH2   1 
ATOM   8105  N  N     . TYR A 1 2489 ? 129.440 200.696 194.378 1.00 79.69  ? 2489 TYR A N     1 
ATOM   8106  C  CA    . TYR A 1 2489 ? 129.727 199.945 193.163 1.00 77.41  ? 2489 TYR A CA    1 
ATOM   8107  C  C     . TYR A 1 2489 ? 131.201 199.584 193.073 1.00 76.88  ? 2489 TYR A C     1 
ATOM   8108  O  O     . TYR A 1 2489 ? 131.544 198.448 192.732 1.00 81.88  ? 2489 TYR A O     1 
ATOM   8109  C  CB    . TYR A 1 2489 ? 129.303 200.749 191.935 1.00 78.46  ? 2489 TYR A CB    1 
ATOM   8110  C  CG    . TYR A 1 2489 ? 129.610 200.059 190.627 1.00 73.78  ? 2489 TYR A CG    1 
ATOM   8111  C  CD1   . TYR A 1 2489 ? 128.879 198.955 190.217 1.00 77.01  ? 2489 TYR A CD1   1 
ATOM   8112  C  CD2   . TYR A 1 2489 ? 130.638 200.503 189.811 1.00 72.92  ? 2489 TYR A CD2   1 
ATOM   8113  C  CE1   . TYR A 1 2489 ? 129.156 198.318 189.025 1.00 76.18  ? 2489 TYR A CE1   1 
ATOM   8114  C  CE2   . TYR A 1 2489 ? 130.923 199.871 188.617 1.00 77.83  ? 2489 TYR A CE2   1 
ATOM   8115  C  CZ    . TYR A 1 2489 ? 130.180 198.779 188.230 1.00 77.83  ? 2489 TYR A CZ    1 
ATOM   8116  O  OH    . TYR A 1 2489 ? 130.458 198.145 187.041 1.00 82.52  ? 2489 TYR A OH    1 
ATOM   8117  N  N     . ILE A 1 2490 ? 132.088 200.531 193.383 1.00 80.30  ? 2490 ILE A N     1 
ATOM   8118  C  CA    . ILE A 1 2490 ? 133.517 200.278 193.252 1.00 75.43  ? 2490 ILE A CA    1 
ATOM   8119  C  C     . ILE A 1 2490 ? 133.972 199.221 194.247 1.00 77.98  ? 2490 ILE A C     1 
ATOM   8120  O  O     . ILE A 1 2490 ? 134.750 198.330 193.901 1.00 87.76  ? 2490 ILE A O     1 
ATOM   8121  C  CB    . ILE A 1 2490 ? 134.311 201.587 193.405 1.00 70.97  ? 2490 ILE A CB    1 
ATOM   8122  C  CG1   . ILE A 1 2490 ? 134.143 202.454 192.158 1.00 73.53  ? 2490 ILE A CG1   1 
ATOM   8123  C  CG2   . ILE A 1 2490 ? 135.779 201.295 193.635 1.00 69.74  ? 2490 ILE A CG2   1 
ATOM   8124  C  CD1   . ILE A 1 2490 ? 134.436 201.726 190.870 1.00 74.51  ? 2490 ILE A CD1   1 
ATOM   8125  N  N     . GLN A 1 2491 ? 133.488 199.284 195.490 1.00 82.90  ? 2491 GLN A N     1 
ATOM   8126  C  CA    . GLN A 1 2491 ? 133.889 198.283 196.477 1.00 83.27  ? 2491 GLN A CA    1 
ATOM   8127  C  C     . GLN A 1 2491 ? 133.402 196.891 196.083 1.00 88.62  ? 2491 GLN A C     1 
ATOM   8128  O  O     . GLN A 1 2491 ? 134.175 195.915 196.089 1.00 88.51  ? 2491 GLN A O     1 
ATOM   8129  C  CB    . GLN A 1 2491 ? 133.354 198.677 197.853 1.00 79.95  ? 2491 GLN A CB    1 
ATOM   8130  C  CG    . GLN A 1 2491 ? 133.952 199.960 198.403 1.00 86.31  ? 2491 GLN A CG    1 
ATOM   8131  C  CD    . GLN A 1 2491 ? 133.139 200.544 199.541 1.00 92.34  ? 2491 GLN A CD    1 
ATOM   8132  O  OE1   . GLN A 1 2491 ? 132.693 199.826 200.434 1.00 90.99  ? 2491 GLN A OE1   1 
ATOM   8133  N  NE2   . GLN A 1 2491 ? 132.939 201.857 199.511 1.00 90.30  ? 2491 GLN A NE2   1 
ATOM   8134  N  N     . ARG A 1 2492 ? 132.118 196.778 195.729 1.00 86.85  ? 2492 ARG A N     1 
ATOM   8135  C  CA    . ARG A 1 2492 ? 131.579 195.472 195.367 1.00 81.94  ? 2492 ARG A CA    1 
ATOM   8136  C  C     . ARG A 1 2492 ? 132.265 194.921 194.123 1.00 84.24  ? 2492 ARG A C     1 
ATOM   8137  O  O     . ARG A 1 2492 ? 132.599 193.731 194.065 1.00 93.32  ? 2492 ARG A O     1 
ATOM   8138  C  CB    . ARG A 1 2492 ? 130.068 195.567 195.164 1.00 84.97  ? 2492 ARG A CB    1 
ATOM   8139  C  CG    . ARG A 1 2492 ? 129.280 195.685 196.460 1.00 84.94  ? 2492 ARG A CG    1 
ATOM   8140  C  CD    . ARG A 1 2492 ? 128.005 196.486 196.254 1.00 93.40  ? 2492 ARG A CD    1 
ATOM   8141  N  NE    . ARG A 1 2492 ? 127.096 196.385 197.390 1.00 94.41  ? 2492 ARG A NE    1 
ATOM   8142  C  CZ    . ARG A 1 2492 ? 127.238 197.052 198.527 1.00 88.74  ? 2492 ARG A CZ    1 
ATOM   8143  N  NH1   . ARG A 1 2492 ? 128.255 197.875 198.723 1.00 85.78  ? 2492 ARG A NH1   1 
ATOM   8144  N  NH2   . ARG A 1 2492 ? 126.336 196.891 199.490 1.00 87.09  ? 2492 ARG A NH2   1 
ATOM   8145  N  N     . TYR A 1 2493 ? 132.506 195.773 193.123 1.00 64.10  ? 2493 TYR A N     1 
ATOM   8146  C  CA    . TYR A 1 2493 ? 133.180 195.315 191.917 1.00 58.32  ? 2493 TYR A CA    1 
ATOM   8147  C  C     . TYR A 1 2493 ? 134.641 194.990 192.177 1.00 61.04  ? 2493 TYR A C     1 
ATOM   8148  O  O     . TYR A 1 2493 ? 135.204 194.137 191.494 1.00 72.08  ? 2493 TYR A O     1 
ATOM   8149  C  CB    . TYR A 1 2493 ? 133.067 196.357 190.807 1.00 61.97  ? 2493 TYR A CB    1 
ATOM   8150  C  CG    . TYR A 1 2493 ? 133.284 195.783 189.425 1.00 58.98  ? 2493 TYR A CG    1 
ATOM   8151  C  CD1   . TYR A 1 2493 ? 134.561 195.644 188.901 1.00 54.63  ? 2493 TYR A CD1   1 
ATOM   8152  C  CD2   . TYR A 1 2493 ? 132.211 195.375 188.647 1.00 67.29  ? 2493 TYR A CD2   1 
ATOM   8153  C  CE1   . TYR A 1 2493 ? 134.763 195.119 187.641 1.00 63.70  ? 2493 TYR A CE1   1 
ATOM   8154  C  CE2   . TYR A 1 2493 ? 132.403 194.849 187.386 1.00 70.33  ? 2493 TYR A CE2   1 
ATOM   8155  C  CZ    . TYR A 1 2493 ? 133.681 194.723 186.888 1.00 72.89  ? 2493 TYR A CZ    1 
ATOM   8156  O  OH    . TYR A 1 2493 ? 133.874 194.199 185.631 1.00 76.20  ? 2493 TYR A OH    1 
ATOM   8157  N  N     . LEU A 1 2494 ? 135.277 195.649 193.146 1.00 70.29  ? 2494 LEU A N     1 
ATOM   8158  C  CA    . LEU A 1 2494 ? 136.641 195.275 193.500 1.00 67.46  ? 2494 LEU A CA    1 
ATOM   8159  C  C     . LEU A 1 2494 ? 136.684 193.869 194.072 1.00 62.73  ? 2494 LEU A C     1 
ATOM   8160  O  O     . LEU A 1 2494 ? 137.556 193.070 193.709 1.00 68.77  ? 2494 LEU A O     1 
ATOM   8161  C  CB    . LEU A 1 2494 ? 137.224 196.276 194.495 1.00 67.90  ? 2494 LEU A CB    1 
ATOM   8162  C  CG    . LEU A 1 2494 ? 138.653 195.975 194.949 1.00 62.79  ? 2494 LEU A CG    1 
ATOM   8163  C  CD1   . LEU A 1 2494 ? 139.658 196.615 194.008 1.00 70.58  ? 2494 LEU A CD1   1 
ATOM   8164  C  CD2   . LEU A 1 2494 ? 138.871 196.448 196.372 1.00 68.92  ? 2494 LEU A CD2   1 
ATOM   8165  N  N     . VAL A 1 2495 ? 135.740 193.541 194.958 1.00 64.44  ? 2495 VAL A N     1 
ATOM   8166  C  CA    . VAL A 1 2495 ? 135.682 192.173 195.475 1.00 66.51  ? 2495 VAL A CA    1 
ATOM   8167  C  C     . VAL A 1 2495 ? 135.388 191.187 194.348 1.00 66.66  ? 2495 VAL A C     1 
ATOM   8168  O  O     . VAL A 1 2495 ? 136.016 190.122 194.249 1.00 67.59  ? 2495 VAL A O     1 
ATOM   8169  C  CB    . VAL A 1 2495 ? 134.648 192.067 196.608 1.00 67.07  ? 2495 VAL A CB    1 
ATOM   8170  C  CG1   . VAL A 1 2495 ? 134.390 190.611 196.954 1.00 59.50  ? 2495 VAL A CG1   1 
ATOM   8171  C  CG2   . VAL A 1 2495 ? 135.145 192.812 197.821 1.00 69.27  ? 2495 VAL A CG2   1 
ATOM   8172  N  N     . TYR A 1 2496 ? 134.437 191.534 193.477 1.00 70.23  ? 2496 TYR A N     1 
ATOM   8173  C  CA    . TYR A 1 2496 ? 134.092 190.672 192.350 1.00 65.71  ? 2496 TYR A CA    1 
ATOM   8174  C  C     . TYR A 1 2496 ? 135.294 190.444 191.441 1.00 65.18  ? 2496 TYR A C     1 
ATOM   8175  O  O     . TYR A 1 2496 ? 135.544 189.317 190.992 1.00 76.13  ? 2496 TYR A O     1 
ATOM   8176  C  CB    . TYR A 1 2496 ? 132.924 191.299 191.583 1.00 60.98  ? 2496 TYR A CB    1 
ATOM   8177  C  CG    . TYR A 1 2496 ? 132.750 190.859 190.147 1.00 59.77  ? 2496 TYR A CG    1 
ATOM   8178  C  CD1   . TYR A 1 2496 ? 133.278 191.605 189.102 1.00 68.96  ? 2496 TYR A CD1   1 
ATOM   8179  C  CD2   . TYR A 1 2496 ? 132.018 189.724 189.834 1.00 65.31  ? 2496 TYR A CD2   1 
ATOM   8180  C  CE1   . TYR A 1 2496 ? 133.107 191.217 187.788 1.00 68.27  ? 2496 TYR A CE1   1 
ATOM   8181  C  CE2   . TYR A 1 2496 ? 131.839 189.330 188.523 1.00 69.84  ? 2496 TYR A CE2   1 
ATOM   8182  C  CZ    . TYR A 1 2496 ? 132.387 190.078 187.505 1.00 66.90  ? 2496 TYR A CZ    1 
ATOM   8183  O  OH    . TYR A 1 2496 ? 132.212 189.686 186.199 1.00 69.21  ? 2496 TYR A OH    1 
ATOM   8184  N  N     . ALA A 1 2497 ? 136.067 191.499 191.185 1.00 54.89  ? 2497 ALA A N     1 
ATOM   8185  C  CA    . ALA A 1 2497 ? 137.214 191.400 190.294 1.00 54.61  ? 2497 ALA A CA    1 
ATOM   8186  C  C     . ALA A 1 2497 ? 138.336 190.597 190.924 1.00 54.99  ? 2497 ALA A C     1 
ATOM   8187  O  O     . ALA A 1 2497 ? 139.012 189.826 190.237 1.00 58.42  ? 2497 ALA A O     1 
ATOM   8188  C  CB    . ALA A 1 2497 ? 137.701 192.795 189.907 1.00 63.95  ? 2497 ALA A CB    1 
ATOM   8189  N  N     . ILE A 1 2498 ? 138.547 190.758 192.229 1.00 58.68  ? 2498 ILE A N     1 
ATOM   8190  C  CA    . ILE A 1 2498 ? 139.542 189.943 192.913 1.00 63.66  ? 2498 ILE A CA    1 
ATOM   8191  C  C     . ILE A 1 2498 ? 139.166 188.471 192.817 1.00 66.12  ? 2498 ILE A C     1 
ATOM   8192  O  O     . ILE A 1 2498 ? 140.005 187.618 192.498 1.00 74.74  ? 2498 ILE A O     1 
ATOM   8193  C  CB    . ILE A 1 2498 ? 139.688 190.406 194.373 1.00 62.60  ? 2498 ILE A CB    1 
ATOM   8194  C  CG1   . ILE A 1 2498 ? 140.573 191.648 194.439 1.00 68.58  ? 2498 ILE A CG1   1 
ATOM   8195  C  CG2   . ILE A 1 2498 ? 140.282 189.305 195.226 1.00 57.64  ? 2498 ILE A CG2   1 
ATOM   8196  C  CD1   . ILE A 1 2498 ? 140.565 192.322 195.784 1.00 71.37  ? 2498 ILE A CD1   1 
ATOM   8197  N  N     . LEU A 1 2499 ? 137.889 188.156 193.055 1.00 59.43  ? 2499 LEU A N     1 
ATOM   8198  C  CA    . LEU A 1 2499 ? 137.442 186.768 192.984 1.00 58.44  ? 2499 LEU A CA    1 
ATOM   8199  C  C     . LEU A 1 2499 ? 137.621 186.191 191.585 1.00 59.98  ? 2499 LEU A C     1 
ATOM   8200  O  O     . LEU A 1 2499 ? 138.092 185.060 191.423 1.00 66.37  ? 2499 LEU A O     1 
ATOM   8201  C  CB    . LEU A 1 2499 ? 135.983 186.661 193.421 1.00 59.30  ? 2499 LEU A CB    1 
ATOM   8202  C  CG    . LEU A 1 2499 ? 135.762 186.191 194.855 1.00 64.56  ? 2499 LEU A CG    1 
ATOM   8203  C  CD1   . LEU A 1 2499 ? 134.283 186.056 195.143 1.00 69.83  ? 2499 LEU A CD1   1 
ATOM   8204  C  CD2   . LEU A 1 2499 ? 136.477 184.873 195.086 1.00 65.96  ? 2499 LEU A CD2   1 
ATOM   8205  N  N     . TRP A 1 2500 ? 137.245 186.952 190.556 1.00 54.82  ? 2500 TRP A N     1 
ATOM   8206  C  CA    . TRP A 1 2500 ? 137.291 186.422 189.198 1.00 51.52  ? 2500 TRP A CA    1 
ATOM   8207  C  C     . TRP A 1 2500 ? 138.663 186.525 188.546 1.00 62.19  ? 2500 TRP A C     1 
ATOM   8208  O  O     . TRP A 1 2500 ? 138.861 185.942 187.474 1.00 67.38  ? 2500 TRP A O     1 
ATOM   8209  C  CB    . TRP A 1 2500 ? 136.250 187.123 188.327 1.00 47.85  ? 2500 TRP A CB    1 
ATOM   8210  C  CG    . TRP A 1 2500 ? 134.973 186.360 188.235 1.00 50.00  ? 2500 TRP A CG    1 
ATOM   8211  C  CD1   . TRP A 1 2500 ? 133.764 186.721 188.744 1.00 55.65  ? 2500 TRP A CD1   1 
ATOM   8212  C  CD2   . TRP A 1 2500 ? 134.775 185.102 187.581 1.00 53.90  ? 2500 TRP A CD2   1 
ATOM   8213  N  NE1   . TRP A 1 2500 ? 132.823 185.764 188.455 1.00 59.89  ? 2500 TRP A NE1   1 
ATOM   8214  C  CE2   . TRP A 1 2500 ? 133.420 184.759 187.740 1.00 56.19  ? 2500 TRP A CE2   1 
ATOM   8215  C  CE3   . TRP A 1 2500 ? 135.613 184.232 186.879 1.00 59.20  ? 2500 TRP A CE3   1 
ATOM   8216  C  CZ2   . TRP A 1 2500 ? 132.884 183.584 187.224 1.00 57.98  ? 2500 TRP A CZ2   1 
ATOM   8217  C  CZ3   . TRP A 1 2500 ? 135.079 183.067 186.367 1.00 56.91  ? 2500 TRP A CZ3   1 
ATOM   8218  C  CH2   . TRP A 1 2500 ? 133.728 182.753 186.542 1.00 61.27  ? 2500 TRP A CH2   1 
ATOM   8219  N  N     . SER A 1 2501 ? 139.609 187.241 189.148 1.00 59.18  ? 2501 SER A N     1 
ATOM   8220  C  CA    . SER A 1 2501 ? 140.960 187.316 188.610 1.00 54.49  ? 2501 SER A CA    1 
ATOM   8221  C  C     . SER A 1 2501 ? 141.940 186.402 189.324 1.00 60.60  ? 2501 SER A C     1 
ATOM   8222  O  O     . SER A 1 2501 ? 142.810 185.817 188.671 1.00 60.91  ? 2501 SER A O     1 
ATOM   8223  C  CB    . SER A 1 2501 ? 141.479 188.755 188.679 1.00 51.65  ? 2501 SER A CB    1 
ATOM   8224  O  OG    . SER A 1 2501 ? 142.877 188.779 188.898 1.00 58.42  ? 2501 SER A OG    1 
ATOM   8225  N  N     . LEU A 1 2502 ? 141.828 186.265 190.643 1.00 69.00  ? 2502 LEU A N     1 
ATOM   8226  C  CA    . LEU A 1 2502 ? 142.722 185.397 191.394 1.00 60.82  ? 2502 LEU A CA    1 
ATOM   8227  C  C     . LEU A 1 2502 ? 142.306 183.933 191.348 1.00 64.37  ? 2502 LEU A C     1 
ATOM   8228  O  O     . LEU A 1 2502 ? 143.111 183.066 191.700 1.00 70.79  ? 2502 LEU A O     1 
ATOM   8229  C  CB    . LEU A 1 2502 ? 142.801 185.859 192.853 1.00 57.37  ? 2502 LEU A CB    1 
ATOM   8230  C  CG    . LEU A 1 2502 ? 143.840 186.914 193.243 1.00 51.88  ? 2502 LEU A CG    1 
ATOM   8231  C  CD1   . LEU A 1 2502 ? 143.949 188.024 192.213 1.00 54.98  ? 2502 LEU A CD1   1 
ATOM   8232  C  CD2   . LEU A 1 2502 ? 143.489 187.493 194.597 1.00 63.16  ? 2502 LEU A CD2   1 
ATOM   8233  N  N     . SER A 1 2503 ? 141.074 183.638 190.921 1.00 64.05  ? 2503 SER A N     1 
ATOM   8234  C  CA    . SER A 1 2503 ? 140.610 182.257 190.854 1.00 58.34  ? 2503 SER A CA    1 
ATOM   8235  C  C     . SER A 1 2503 ? 139.850 181.964 189.564 1.00 69.36  ? 2503 SER A C     1 
ATOM   8236  O  O     . SER A 1 2503 ? 139.106 180.978 189.506 1.00 67.10  ? 2503 SER A O     1 
ATOM   8237  C  CB    . SER A 1 2503 ? 139.721 181.923 192.052 1.00 64.99  ? 2503 SER A CB    1 
ATOM   8238  O  OG    . SER A 1 2503 ? 138.527 182.683 192.024 1.00 78.59  ? 2503 SER A OG    1 
ATOM   8239  N  N     . GLY A 1 2504 ? 140.011 182.793 188.532 1.00 70.34  ? 2504 GLY A N     1 
ATOM   8240  C  CA    . GLY A 1 2504 ? 139.330 182.534 187.276 1.00 63.45  ? 2504 GLY A CA    1 
ATOM   8241  C  C     . GLY A 1 2504 ? 139.859 181.312 186.554 1.00 69.22  ? 2504 GLY A C     1 
ATOM   8242  O  O     . GLY A 1 2504 ? 139.138 180.688 185.771 1.00 76.08  ? 2504 GLY A O     1 
ATOM   8243  N  N     . ASP A 1 2505 ? 141.119 180.952 186.803 1.00 64.40  ? 2505 ASP A N     1 
ATOM   8244  C  CA    . ASP A 1 2505 ? 141.762 179.816 186.155 1.00 63.02  ? 2505 ASP A CA    1 
ATOM   8245  C  C     . ASP A 1 2505 ? 141.811 178.585 187.052 1.00 70.64  ? 2505 ASP A C     1 
ATOM   8246  O  O     . ASP A 1 2505 ? 142.770 177.808 186.988 1.00 81.39  ? 2505 ASP A O     1 
ATOM   8247  C  CB    . ASP A 1 2505 ? 143.169 180.198 185.700 1.00 66.93  ? 2505 ASP A CB    1 
ATOM   8248  C  CG    . ASP A 1 2505 ? 144.043 180.666 186.844 1.00 75.18  ? 2505 ASP A CG    1 
ATOM   8249  O  OD1   . ASP A 1 2505 ? 143.490 181.098 187.875 1.00 78.42  ? 2505 ASP A OD1   1 
ATOM   8250  O  OD2   . ASP A 1 2505 ? 145.283 180.607 186.710 1.00 77.06  ? 2505 ASP A OD2   1 
ATOM   8251  N  N     . SER A 1 2506 ? 140.795 178.390 187.888 1.00 68.81  ? 2506 SER A N     1 
ATOM   8252  C  CA    . SER A 1 2506 ? 140.723 177.250 188.788 1.00 64.41  ? 2506 SER A CA    1 
ATOM   8253  C  C     . SER A 1 2506 ? 139.321 176.659 188.742 1.00 66.58  ? 2506 SER A C     1 
ATOM   8254  O  O     . SER A 1 2506 ? 138.393 177.243 188.177 1.00 74.93  ? 2506 SER A O     1 
ATOM   8255  C  CB    . SER A 1 2506 ? 141.092 177.647 190.223 1.00 67.72  ? 2506 SER A CB    1 
ATOM   8256  O  OG    . SER A 1 2506 ? 140.348 178.776 190.645 1.00 75.47  ? 2506 SER A OG    1 
ATOM   8257  N  N     . ARG A 1 2507 ? 139.174 175.483 189.346 1.00 73.02  ? 2507 ARG A N     1 
ATOM   8258  C  CA    . ARG A 1 2507 ? 137.889 174.802 189.365 1.00 77.02  ? 2507 ARG A CA    1 
ATOM   8259  C  C     . ARG A 1 2507 ? 136.904 175.552 190.261 1.00 84.81  ? 2507 ARG A C     1 
ATOM   8260  O  O     . ARG A 1 2507 ? 137.231 176.559 190.895 1.00 92.15  ? 2507 ARG A O     1 
ATOM   8261  C  CB    . ARG A 1 2507 ? 138.061 173.359 189.830 1.00 86.33  ? 2507 ARG A CB    1 
ATOM   8262  C  CG    . ARG A 1 2507 ? 138.958 172.522 188.935 1.00 87.26  ? 2507 ARG A CG    1 
ATOM   8263  C  CD    . ARG A 1 2507 ? 139.079 171.098 189.451 1.00 85.85  ? 2507 ARG A CD    1 
ATOM   8264  N  NE    . ARG A 1 2507 ? 139.335 171.054 190.885 1.00 86.81  ? 2507 ARG A NE    1 
ATOM   8265  C  CZ    . ARG A 1 2507 ? 140.527 171.228 191.438 1.00 88.58  ? 2507 ARG A CZ    1 
ATOM   8266  N  NH1   . ARG A 1 2507 ? 141.602 171.467 190.704 1.00 89.26  ? 2507 ARG A NH1   1 
ATOM   8267  N  NH2   . ARG A 1 2507 ? 140.644 171.161 192.761 1.00 84.38  ? 2507 ARG A NH2   1 
ATOM   8268  N  N     . LEU A 1 2508 ? 135.671 175.044 190.311 1.00 94.86  ? 2508 LEU A N     1 
ATOM   8269  C  CA    . LEU A 1 2508 ? 134.633 175.689 191.108 1.00 96.38  ? 2508 LEU A CA    1 
ATOM   8270  C  C     . LEU A 1 2508 ? 134.947 175.610 192.598 1.00 97.79  ? 2508 LEU A C     1 
ATOM   8271  O  O     . LEU A 1 2508 ? 134.632 176.537 193.355 1.00 99.85  ? 2508 LEU A O     1 
ATOM   8272  C  CB    . LEU A 1 2508 ? 133.276 175.052 190.807 1.00 95.89  ? 2508 LEU A CB    1 
ATOM   8273  C  CG    . LEU A 1 2508 ? 132.074 175.547 191.612 1.00 98.17  ? 2508 LEU A CG    1 
ATOM   8274  C  CD1   . LEU A 1 2508 ? 131.890 177.046 191.437 1.00 94.17  ? 2508 LEU A CD1   1 
ATOM   8275  C  CD2   . LEU A 1 2508 ? 130.816 174.798 191.203 1.00 99.28  ? 2508 LEU A CD2   1 
ATOM   8276  N  N     . LYS A 1 2509 ? 135.564 174.509 193.036 1.00 85.24  ? 2509 LYS A N     1 
ATOM   8277  C  CA    . LYS A 1 2509 ? 135.879 174.351 194.452 1.00 82.95  ? 2509 LYS A CA    1 
ATOM   8278  C  C     . LYS A 1 2509 ? 136.849 175.425 194.930 1.00 85.54  ? 2509 LYS A C     1 
ATOM   8279  O  O     . LYS A 1 2509 ? 136.663 176.005 196.005 1.00 88.63  ? 2509 LYS A O     1 
ATOM   8280  C  CB    . LYS A 1 2509 ? 136.453 172.958 194.707 1.00 81.96  ? 2509 LYS A CB    1 
ATOM   8281  C  CG    . LYS A 1 2509 ? 136.717 172.655 196.173 1.00 84.65  ? 2509 LYS A CG    1 
ATOM   8282  C  CD    . LYS A 1 2509 ? 137.817 171.614 196.352 1.00 87.22  ? 2509 LYS A CD    1 
ATOM   8283  C  CE    . LYS A 1 2509 ? 137.947 170.705 195.138 1.00 90.15  ? 2509 LYS A CE    1 
ATOM   8284  N  NZ    . LYS A 1 2509 ? 139.202 169.905 195.173 1.00 89.00  ? 2509 LYS A NZ    1 
ATOM   8285  N  N     . MET A 1 2510 ? 137.888 175.710 194.141 1.00 80.67  ? 2510 MET A N     1 
ATOM   8286  C  CA    . MET A 1 2510 ? 138.835 176.748 194.531 1.00 78.02  ? 2510 MET A CA    1 
ATOM   8287  C  C     . MET A 1 2510 ? 138.207 178.134 194.474 1.00 82.73  ? 2510 MET A C     1 
ATOM   8288  O  O     . MET A 1 2510 ? 138.547 179.000 195.288 1.00 92.82  ? 2510 MET A O     1 
ATOM   8289  C  CB    . MET A 1 2510 ? 140.080 176.683 193.650 1.00 74.80  ? 2510 MET A CB    1 
ATOM   8290  C  CG    . MET A 1 2510 ? 140.652 175.285 193.530 1.00 80.65  ? 2510 MET A CG    1 
ATOM   8291  S  SD    . MET A 1 2510 ? 140.709 174.467 195.135 1.00 98.83  ? 2510 MET A SD    1 
ATOM   8292  C  CE    . MET A 1 2510 ? 142.078 173.341 194.900 1.00 86.87  ? 2510 MET A CE    1 
ATOM   8293  N  N     . ARG A 1 2511 ? 137.290 178.362 193.532 1.00 71.35  ? 2511 ARG A N     1 
ATOM   8294  C  CA    . ARG A 1 2511 ? 136.564 179.626 193.507 1.00 71.77  ? 2511 ARG A CA    1 
ATOM   8295  C  C     . ARG A 1 2511 ? 135.744 179.810 194.778 1.00 79.42  ? 2511 ARG A C     1 
ATOM   8296  O  O     . ARG A 1 2511 ? 135.751 180.890 195.381 1.00 80.50  ? 2511 ARG A O     1 
ATOM   8297  C  CB    . ARG A 1 2511 ? 135.670 179.686 192.269 1.00 72.93  ? 2511 ARG A CB    1 
ATOM   8298  C  CG    . ARG A 1 2511 ? 136.443 179.716 190.961 1.00 72.81  ? 2511 ARG A CG    1 
ATOM   8299  C  CD    . ARG A 1 2511 ? 135.539 179.482 189.765 1.00 74.11  ? 2511 ARG A CD    1 
ATOM   8300  N  NE    . ARG A 1 2511 ? 136.266 179.608 188.508 1.00 69.52  ? 2511 ARG A NE    1 
ATOM   8301  C  CZ    . ARG A 1 2511 ? 135.795 179.230 187.328 1.00 71.54  ? 2511 ARG A CZ    1 
ATOM   8302  N  NH1   . ARG A 1 2511 ? 134.594 178.690 187.204 1.00 77.84  ? 2511 ARG A NH1   1 
ATOM   8303  N  NH2   . ARG A 1 2511 ? 136.549 179.396 186.245 1.00 67.17  ? 2511 ARG A NH2   1 
ATOM   8304  N  N     . ALA A 1 2512 ? 135.047 178.757 195.212 1.00 80.34  ? 2512 ALA A N     1 
ATOM   8305  C  CA    . ALA A 1 2512 ? 134.290 178.832 196.458 1.00 74.07  ? 2512 ALA A CA    1 
ATOM   8306  C  C     . ALA A 1 2512 ? 135.212 179.035 197.655 1.00 78.47  ? 2512 ALA A C     1 
ATOM   8307  O  O     . ALA A 1 2512 ? 134.879 179.778 198.586 1.00 81.28  ? 2512 ALA A O     1 
ATOM   8308  C  CB    . ALA A 1 2512 ? 133.447 177.571 196.637 1.00 75.62  ? 2512 ALA A CB    1 
ATOM   8309  N  N     . GLU A 1 2513 ? 136.370 178.371 197.654 1.00 80.96  ? 2513 GLU A N     1 
ATOM   8310  C  CA    . GLU A 1 2513 ? 137.324 178.529 198.748 1.00 82.52  ? 2513 GLU A CA    1 
ATOM   8311  C  C     . GLU A 1 2513 ? 137.817 179.968 198.849 1.00 83.24  ? 2513 GLU A C     1 
ATOM   8312  O  O     . GLU A 1 2513 ? 137.865 180.551 199.941 1.00 86.53  ? 2513 GLU A O     1 
ATOM   8313  C  CB    . GLU A 1 2513 ? 138.498 177.570 198.549 1.00 79.68  ? 2513 GLU A CB    1 
ATOM   8314  C  CG    . GLU A 1 2513 ? 139.710 177.878 199.407 1.00 83.46  ? 2513 GLU A CG    1 
ATOM   8315  C  CD    . GLU A 1 2513 ? 140.465 176.629 199.810 1.00 90.52  ? 2513 GLU A CD    1 
ATOM   8316  O  OE1   . GLU A 1 2513 ? 140.455 175.652 199.033 1.00 86.12  ? 2513 GLU A OE1   1 
ATOM   8317  O  OE2   . GLU A 1 2513 ? 141.069 176.623 200.903 1.00 95.03  ? 2513 GLU A OE2   1 
ATOM   8318  N  N     . LEU A 1 2514 ? 138.193 180.559 197.712 1.00 71.64  ? 2514 LEU A N     1 
ATOM   8319  C  CA    . LEU A 1 2514 ? 138.652 181.943 197.721 1.00 69.72  ? 2514 LEU A CA    1 
ATOM   8320  C  C     . LEU A 1 2514 ? 137.528 182.889 198.119 1.00 74.30  ? 2514 LEU A C     1 
ATOM   8321  O  O     . LEU A 1 2514 ? 137.761 183.882 198.819 1.00 85.27  ? 2514 LEU A O     1 
ATOM   8322  C  CB    . LEU A 1 2514 ? 139.220 182.323 196.355 1.00 65.53  ? 2514 LEU A CB    1 
ATOM   8323  C  CG    . LEU A 1 2514 ? 139.987 183.645 196.335 1.00 67.54  ? 2514 LEU A CG    1 
ATOM   8324  C  CD1   . LEU A 1 2514 ? 141.187 183.575 197.260 1.00 70.98  ? 2514 LEU A CD1   1 
ATOM   8325  C  CD2   . LEU A 1 2514 ? 140.422 183.997 194.926 1.00 68.15  ? 2514 LEU A CD2   1 
ATOM   8326  N  N     . GLY A 1 2515 ? 136.299 182.599 197.684 1.00 82.02  ? 2515 GLY A N     1 
ATOM   8327  C  CA    . GLY A 1 2515 ? 135.169 183.402 198.117 1.00 84.63  ? 2515 GLY A CA    1 
ATOM   8328  C  C     . GLY A 1 2515 ? 134.970 183.360 199.619 1.00 85.09  ? 2515 GLY A C     1 
ATOM   8329  O  O     . GLY A 1 2515 ? 134.720 184.388 200.250 1.00 89.57  ? 2515 GLY A O     1 
ATOM   8330  N  N     . GLU A 1 2516 ? 135.084 182.170 200.213 1.00 88.28  ? 2516 GLU A N     1 
ATOM   8331  C  CA    . GLU A 1 2516 ? 134.947 182.049 201.662 1.00 88.80  ? 2516 GLU A CA    1 
ATOM   8332  C  C     . GLU A 1 2516 ? 136.061 182.794 202.387 1.00 90.84  ? 2516 GLU A C     1 
ATOM   8333  O  O     . GLU A 1 2516 ? 135.818 183.460 203.402 1.00 95.93  ? 2516 GLU A O     1 
ATOM   8334  C  CB    . GLU A 1 2516 ? 134.933 180.577 202.067 1.00 88.21  ? 2516 GLU A CB    1 
ATOM   8335  C  CG    . GLU A 1 2516 ? 133.660 179.844 201.685 1.00 91.83  ? 2516 GLU A CG    1 
ATOM   8336  C  CD    . GLU A 1 2516 ? 133.883 178.360 201.482 1.00 97.65  ? 2516 GLU A CD    1 
ATOM   8337  O  OE1   . GLU A 1 2516 ? 134.976 177.869 201.835 1.00 98.27  ? 2516 GLU A OE1   1 
ATOM   8338  O  OE2   . GLU A 1 2516 ? 132.966 177.685 200.971 1.00 97.49  ? 2516 GLU A OE2   1 
ATOM   8339  N  N     . TYR A 1 2517 ? 137.293 182.694 201.881 1.00 84.78  ? 2517 TYR A N     1 
ATOM   8340  C  CA    . TYR A 1 2517 ? 138.397 183.420 202.504 1.00 84.91  ? 2517 TYR A CA    1 
ATOM   8341  C  C     . TYR A 1 2517 ? 138.172 184.927 202.441 1.00 89.15  ? 2517 TYR A C     1 
ATOM   8342  O  O     . TYR A 1 2517 ? 138.376 185.638 203.435 1.00 94.32  ? 2517 TYR A O     1 
ATOM   8343  C  CB    . TYR A 1 2517 ? 139.717 183.047 201.835 1.00 80.55  ? 2517 TYR A CB    1 
ATOM   8344  C  CG    . TYR A 1 2517 ? 140.917 183.753 202.421 1.00 79.50  ? 2517 TYR A CG    1 
ATOM   8345  C  CD1   . TYR A 1 2517 ? 141.529 183.281 203.573 1.00 82.31  ? 2517 TYR A CD1   1 
ATOM   8346  C  CD2   . TYR A 1 2517 ? 141.445 184.884 201.816 1.00 87.09  ? 2517 TYR A CD2   1 
ATOM   8347  C  CE1   . TYR A 1 2517 ? 142.628 183.921 204.111 1.00 89.01  ? 2517 TYR A CE1   1 
ATOM   8348  C  CE2   . TYR A 1 2517 ? 142.544 185.531 202.346 1.00 91.88  ? 2517 TYR A CE2   1 
ATOM   8349  C  CZ    . TYR A 1 2517 ? 143.131 185.046 203.493 1.00 90.58  ? 2517 TYR A CZ    1 
ATOM   8350  O  OH    . TYR A 1 2517 ? 144.227 185.688 204.024 1.00 85.48  ? 2517 TYR A OH    1 
ATOM   8351  N  N     . ILE A 1 2518 ? 137.742 185.431 201.282 1.00 84.11  ? 2518 ILE A N     1 
ATOM   8352  C  CA    . ILE A 1 2518 ? 137.452 186.856 201.159 1.00 78.67  ? 2518 ILE A CA    1 
ATOM   8353  C  C     . ILE A 1 2518 ? 136.343 187.252 202.121 1.00 80.48  ? 2518 ILE A C     1 
ATOM   8354  O  O     . ILE A 1 2518 ? 136.454 188.254 202.836 1.00 83.91  ? 2518 ILE A O     1 
ATOM   8355  C  CB    . ILE A 1 2518 ? 137.098 187.209 199.704 1.00 77.43  ? 2518 ILE A CB    1 
ATOM   8356  C  CG1   . ILE A 1 2518 ? 138.348 187.143 198.828 1.00 79.01  ? 2518 ILE A CG1   1 
ATOM   8357  C  CG2   . ILE A 1 2518 ? 136.465 188.587 199.624 1.00 81.89  ? 2518 ILE A CG2   1 
ATOM   8358  C  CD1   . ILE A 1 2518 ? 138.078 187.417 197.376 1.00 82.14  ? 2518 ILE A CD1   1 
ATOM   8359  N  N     . ARG A 1 2519 ? 135.273 186.453 202.180 1.00 91.64  ? 2519 ARG A N     1 
ATOM   8360  C  CA    . ARG A 1 2519 ? 134.187 186.713 203.120 1.00 96.95  ? 2519 ARG A CA    1 
ATOM   8361  C  C     . ARG A 1 2519 ? 134.709 186.820 204.545 1.00 99.06  ? 2519 ARG A C     1 
ATOM   8362  O  O     . ARG A 1 2519 ? 134.251 187.665 205.323 1.00 100.69 ? 2519 ARG A O     1 
ATOM   8363  C  CB    . ARG A 1 2519 ? 133.140 185.603 203.020 1.00 96.63  ? 2519 ARG A CB    1 
ATOM   8364  C  CG    . ARG A 1 2519 ? 131.781 185.950 203.605 1.00 96.55  ? 2519 ARG A CG    1 
ATOM   8365  C  CD    . ARG A 1 2519 ? 130.866 184.735 203.591 1.00 96.26  ? 2519 ARG A CD    1 
ATOM   8366  N  NE    . ARG A 1 2519 ? 130.024 184.681 202.402 1.00 97.26  ? 2519 ARG A NE    1 
ATOM   8367  C  CZ    . ARG A 1 2519 ? 128.900 185.367 202.246 1.00 100.96 ? 2519 ARG A CZ    1 
ATOM   8368  N  NH1   . ARG A 1 2519 ? 128.447 186.175 203.190 1.00 101.81 ? 2519 ARG A NH1   1 
ATOM   8369  N  NH2   . ARG A 1 2519 ? 128.212 185.235 201.116 1.00 98.26  ? 2519 ARG A NH2   1 
ATOM   8370  N  N     . ARG A 1 2520 ? 135.750 186.045 204.856 1.00 97.22  ? 2520 ARG A N     1 
ATOM   8371  C  CA    . ARG A 1 2520 ? 136.369 186.123 206.207 1.00 97.59  ? 2520 ARG A CA    1 
ATOM   8372  C  C     . ARG A 1 2520 ? 137.185 187.413 206.343 1.00 100.14 ? 2520 ARG A C     1 
ATOM   8373  O  O     . ARG A 1 2520 ? 136.813 188.251 207.186 1.00 98.90  ? 2520 ARG A O     1 
ATOM   8374  C  CB    . ARG A 1 2520 ? 137.275 184.912 206.444 1.00 95.53  ? 2520 ARG A CB    1 
ATOM   8375  C  CG    . ARG A 1 2520 ? 136.551 183.574 206.438 1.00 95.68  ? 2520 ARG A CG    1 
ATOM   8376  C  CD    . ARG A 1 2520 ? 137.449 182.490 205.876 1.00 98.59  ? 2520 ARG A CD    1 
ATOM   8377  N  NE    . ARG A 1 2520 ? 138.801 182.574 206.410 1.00 102.73 ? 2520 ARG A NE    1 
ATOM   8378  C  CZ    . ARG A 1 2520 ? 139.802 181.780 206.049 1.00 104.84 ? 2520 ARG A CZ    1 
ATOM   8379  N  NH1   . ARG A 1 2520 ? 139.616 180.864 205.117 1.00 101.85 ? 2520 ARG A NH1   1 
ATOM   8380  N  NH2   . ARG A 1 2520 ? 140.988 181.910 206.619 1.00 101.90 ? 2520 ARG A NH2   1 
ATOM   8381  N  N     . ILE A 1 2521 ? 138.250 187.571 205.548 1.00 100.35 ? 2521 ILE A N     1 
ATOM   8382  C  CA    . ILE A 1 2521 ? 139.163 188.747 205.697 1.00 95.53  ? 2521 ILE A CA    1 
ATOM   8383  C  C     . ILE A 1 2521 ? 138.470 190.050 205.281 1.00 95.54  ? 2521 ILE A C     1 
ATOM   8384  O  O     . ILE A 1 2521 ? 138.634 191.047 206.008 1.00 98.41  ? 2521 ILE A O     1 
ATOM   8385  C  CB    . ILE A 1 2521 ? 140.463 188.529 204.896 1.00 93.84  ? 2521 ILE A CB    1 
ATOM   8386  C  CG1   . ILE A 1 2521 ? 140.219 188.572 203.386 1.00 97.96  ? 2521 ILE A CG1   1 
ATOM   8387  C  CG2   . ILE A 1 2521 ? 141.145 187.237 205.319 1.00 95.93  ? 2521 ILE A CG2   1 
ATOM   8388  C  CD1   . ILE A 1 2521 ? 141.482 188.647 202.561 1.00 96.16  ? 2521 ILE A CD1   1 
ATOM   8389  N  N     . THR A 1 2522 ? 137.731 190.054 204.167 1.00 101.49 ? 2522 THR A N     1 
ATOM   8390  C  CA    . THR A 1 2522 ? 137.143 191.326 203.659 1.00 103.97 ? 2522 THR A CA    1 
ATOM   8391  C  C     . THR A 1 2522 ? 136.161 191.910 204.677 1.00 107.15 ? 2522 THR A C     1 
ATOM   8392  O  O     . THR A 1 2522 ? 135.604 191.131 205.474 1.00 107.94 ? 2522 THR A O     1 
ATOM   8393  C  CB    . THR A 1 2522 ? 136.448 191.137 202.306 1.00 107.95 ? 2522 THR A CB    1 
ATOM   8394  O  OG1   . THR A 1 2522 ? 136.624 192.337 201.553 1.00 109.35 ? 2522 THR A OG1   1 
ATOM   8395  C  CG2   . THR A 1 2522 ? 134.973 190.825 202.437 1.00 106.36 ? 2522 THR A CG2   1 
ATOM   8396  N  N     . THR A 1 2523 ? 135.971 193.232 204.647 1.00 108.18 ? 2523 THR A N     1 
ATOM   8397  C  CA    . THR A 1 2523 ? 135.001 193.892 205.559 1.00 107.65 ? 2523 THR A CA    1 
ATOM   8398  C  C     . THR A 1 2523 ? 133.821 194.411 204.734 1.00 109.81 ? 2523 THR A C     1 
ATOM   8399  O  O     . THR A 1 2523 ? 132.732 194.589 205.312 1.00 111.92 ? 2523 THR A O     1 
ATOM   8400  C  CB    . THR A 1 2523 ? 135.667 195.030 206.338 1.00 109.23 ? 2523 THR A CB    1 
ATOM   8401  O  OG1   . THR A 1 2523 ? 136.051 196.035 205.399 1.00 108.85 ? 2523 THR A OG1   1 
ATOM   8402  C  CG2   . THR A 1 2523 ? 136.874 194.574 207.128 1.00 107.94 ? 2523 THR A CG2   1 
ATOM   8403  N  N     . VAL A 1 2524 ? 134.036 194.635 203.434 1.00 100.31 ? 2524 VAL A N     1 
ATOM   8404  C  CA    . VAL A 1 2524 ? 132.956 195.163 202.548 1.00 101.83 ? 2524 VAL A CA    1 
ATOM   8405  C  C     . VAL A 1 2524 ? 131.748 194.226 202.639 1.00 100.21 ? 2524 VAL A C     1 
ATOM   8406  O  O     . VAL A 1 2524 ? 131.951 192.997 202.656 1.00 99.32  ? 2524 VAL A O     1 
ATOM   8407  C  CB    . VAL A 1 2524 ? 133.444 195.305 201.094 1.00 97.50  ? 2524 VAL A CB    1 
ATOM   8408  C  CG1   . VAL A 1 2524 ? 134.329 196.527 200.913 1.00 97.59  ? 2524 VAL A CG1   1 
ATOM   8409  C  CG2   . VAL A 1 2524 ? 134.158 194.050 200.624 1.00 92.75  ? 2524 VAL A CG2   1 
ATOM   8410  N  N     . PRO A 1 2525 ? 130.506 194.752 202.701 1.00 104.99 ? 2525 PRO A N     1 
ATOM   8411  C  CA    . PRO A 1 2525 ? 129.316 193.908 202.750 1.00 103.63 ? 2525 PRO A CA    1 
ATOM   8412  C  C     . PRO A 1 2525 ? 129.316 192.940 201.560 1.00 105.98 ? 2525 PRO A C     1 
ATOM   8413  O  O     . PRO A 1 2525 ? 129.441 193.399 200.440 1.00 107.91 ? 2525 PRO A O     1 
ATOM   8414  C  CB    . PRO A 1 2525 ? 128.160 194.908 202.622 1.00 105.01 ? 2525 PRO A CB    1 
ATOM   8415  C  CG    . PRO A 1 2525 ? 128.733 196.203 203.149 1.00 106.53 ? 2525 PRO A CG    1 
ATOM   8416  C  CD    . PRO A 1 2525 ? 130.188 196.181 202.730 1.00 105.34 ? 2525 PRO A CD    1 
ATOM   8417  N  N     . LEU A 1 2526 ? 129.180 191.640 201.830 1.00 98.02  ? 2526 LEU A N     1 
ATOM   8418  C  CA    . LEU A 1 2526 ? 129.177 190.619 200.749 1.00 96.50  ? 2526 LEU A CA    1 
ATOM   8419  C  C     . LEU A 1 2526 ? 127.811 189.927 200.729 1.00 100.57 ? 2526 LEU A C     1 
ATOM   8420  O  O     . LEU A 1 2526 ? 127.078 190.051 201.729 1.00 101.37 ? 2526 LEU A O     1 
ATOM   8421  C  CB    . LEU A 1 2526 ? 130.310 189.623 201.014 1.00 92.83  ? 2526 LEU A CB    1 
ATOM   8422  C  CG    . LEU A 1 2526 ? 131.533 189.768 200.110 1.00 93.08  ? 2526 LEU A CG    1 
ATOM   8423  C  CD1   . LEU A 1 2526 ? 132.001 191.214 200.058 1.00 96.40  ? 2526 LEU A CD1   1 
ATOM   8424  C  CD2   . LEU A 1 2526 ? 132.661 188.866 200.582 1.00 96.25  ? 2526 LEU A CD2   1 
ATOM   8425  N  N     . PRO A 1 2527 ? 127.430 189.212 199.647 1.00 101.85 ? 2527 PRO A N     1 
ATOM   8426  C  CA    . PRO A 1 2527 ? 126.104 188.602 199.561 1.00 103.18 ? 2527 PRO A CA    1 
ATOM   8427  C  C     . PRO A 1 2527 ? 125.748 187.907 200.881 1.00 106.19 ? 2527 PRO A C     1 
ATOM   8428  O  O     . PRO A 1 2527 ? 126.560 187.150 201.372 1.00 104.33 ? 2527 PRO A O     1 
ATOM   8429  C  CB    . PRO A 1 2527 ? 126.289 187.559 198.455 1.00 100.33 ? 2527 PRO A CB    1 
ATOM   8430  C  CG    . PRO A 1 2527 ? 127.321 188.181 197.541 1.00 101.21 ? 2527 PRO A CG    1 
ATOM   8431  C  CD    . PRO A 1 2527 ? 128.247 188.951 198.459 1.00 98.15  ? 2527 PRO A CD    1 
ATOM   8432  N  N     . THR A 1 2528 ? 124.554 188.179 201.415 1.00 118.27 ? 2528 THR A N     1 
ATOM   8433  C  CA    . THR A 1 2528 ? 124.138 187.591 202.718 1.00 116.00 ? 2528 THR A CA    1 
ATOM   8434  C  C     . THR A 1 2528 ? 123.643 186.157 202.497 1.00 116.44 ? 2528 THR A C     1 
ATOM   8435  O  O     . THR A 1 2528 ? 123.309 185.489 203.494 1.00 114.34 ? 2528 THR A O     1 
ATOM   8436  C  CB    . THR A 1 2528 ? 123.077 188.468 203.395 1.00 117.04 ? 2528 THR A CB    1 
ATOM   8437  O  OG1   . THR A 1 2528 ? 123.515 189.825 203.317 1.00 114.69 ? 2528 THR A OG1   1 
ATOM   8438  C  CG2   . THR A 1 2528 ? 122.829 188.094 204.840 1.00 116.68 ? 2528 THR A CG2   1 
ATOM   8439  N  N     . ALA A 1 2529 ? 123.612 185.704 201.241 1.00 122.91 ? 2529 ALA A N     1 
ATOM   8440  C  CA    . ALA A 1 2529 ? 123.127 184.340 200.925 1.00 121.75 ? 2529 ALA A CA    1 
ATOM   8441  C  C     . ALA A 1 2529 ? 123.887 183.316 201.772 1.00 123.15 ? 2529 ALA A C     1 
ATOM   8442  O  O     . ALA A 1 2529 ? 125.101 183.502 201.985 1.00 122.63 ? 2529 ALA A O     1 
ATOM   8443  C  CB    . ALA A 1 2529 ? 123.298 184.062 199.454 1.00 119.52 ? 2529 ALA A CB    1 
ATOM   8444  N  N     . PRO A 1 2530 ? 123.227 182.244 202.261 1.00 123.93 ? 2530 PRO A N     1 
ATOM   8445  C  CA    . PRO A 1 2530 ? 123.884 181.263 203.127 1.00 123.52 ? 2530 PRO A CA    1 
ATOM   8446  C  C     . PRO A 1 2530 ? 124.842 180.351 202.349 1.00 121.82 ? 2530 PRO A C     1 
ATOM   8447  O  O     . PRO A 1 2530 ? 126.036 180.471 202.544 1.00 121.98 ? 2530 PRO A O     1 
ATOM   8448  C  CB    . PRO A 1 2530 ? 122.707 180.444 203.676 1.00 123.28 ? 2530 PRO A CB    1 
ATOM   8449  C  CG    . PRO A 1 2530 ? 121.652 180.540 202.596 1.00 123.03 ? 2530 PRO A CG    1 
ATOM   8450  C  CD    . PRO A 1 2530 ? 121.821 181.925 202.005 1.00 122.37 ? 2530 PRO A CD    1 
ATOM   8451  N  N     . ASN A 1 2531 ? 124.305 179.475 201.495 1.00 118.30 ? 2531 ASN A N     1 
ATOM   8452  C  CA    . ASN A 1 2531 ? 125.145 178.531 200.767 1.00 119.13 ? 2531 ASN A CA    1 
ATOM   8453  C  C     . ASN A 1 2531 ? 125.612 179.019 199.405 1.00 118.48 ? 2531 ASN A C     1 
ATOM   8454  O  O     . ASN A 1 2531 ? 126.600 178.481 198.892 1.00 116.39 ? 2531 ASN A O     1 
ATOM   8455  C  CB    . ASN A 1 2531 ? 124.415 177.193 200.575 1.00 119.99 ? 2531 ASN A CB    1 
ATOM   8456  C  CG    . ASN A 1 2531 ? 123.804 176.668 201.859 1.00 121.68 ? 2531 ASN A CG    1 
ATOM   8457  O  OD1   . ASN A 1 2531 ? 123.370 177.437 202.714 1.00 120.11 ? 2531 ASN A OD1   1 
ATOM   8458  N  ND2   . ASN A 1 2531 ? 123.768 175.349 201.998 1.00 122.12 ? 2531 ASN A ND2   1 
ATOM   8459  N  N     . ILE A 1 2532 ? 124.951 179.999 198.803 1.00 110.95 ? 2532 ILE A N     1 
ATOM   8460  C  CA    . ILE A 1 2532 ? 125.345 180.448 197.463 1.00 108.45 ? 2532 ILE A CA    1 
ATOM   8461  C  C     . ILE A 1 2532 ? 126.681 181.178 197.550 1.00 107.44 ? 2532 ILE A C     1 
ATOM   8462  O  O     . ILE A 1 2532 ? 126.803 182.154 198.312 1.00 109.33 ? 2532 ILE A O     1 
ATOM   8463  C  CB    . ILE A 1 2532 ? 124.264 181.347 196.864 1.00 106.38 ? 2532 ILE A CB    1 
ATOM   8464  C  CG1   . ILE A 1 2532 ? 122.962 180.561 196.686 1.00 106.44 ? 2532 ILE A CG1   1 
ATOM   8465  C  CG2   . ILE A 1 2532 ? 124.735 181.926 195.539 1.00 106.85 ? 2532 ILE A CG2   1 
ATOM   8466  C  CD1   . ILE A 1 2532 ? 122.039 181.119 195.620 1.00 106.39 ? 2532 ILE A CD1   1 
ATOM   8467  N  N     . PRO A 1 2533 ? 127.700 180.753 196.808 1.00 89.24  ? 2533 PRO A N     1 
ATOM   8468  C  CA    . PRO A 1 2533 ? 128.989 181.448 196.855 1.00 88.75  ? 2533 PRO A CA    1 
ATOM   8469  C  C     . PRO A 1 2533 ? 128.911 182.816 196.197 1.00 94.46  ? 2533 PRO A C     1 
ATOM   8470  O  O     . PRO A 1 2533 ? 128.006 183.116 195.414 1.00 96.91  ? 2533 PRO A O     1 
ATOM   8471  C  CB    . PRO A 1 2533 ? 129.927 180.514 196.085 1.00 90.09  ? 2533 PRO A CB    1 
ATOM   8472  C  CG    . PRO A 1 2533 ? 129.029 179.734 195.190 1.00 90.35  ? 2533 PRO A CG    1 
ATOM   8473  C  CD    . PRO A 1 2533 ? 127.735 179.570 195.932 1.00 88.65  ? 2533 PRO A CD    1 
ATOM   8474  N  N     . ILE A 1 2534 ? 129.891 183.657 196.536 1.00 86.39  ? 2534 ILE A N     1 
ATOM   8475  C  CA    . ILE A 1 2534 ? 129.924 185.021 196.026 1.00 84.10  ? 2534 ILE A CA    1 
ATOM   8476  C  C     . ILE A 1 2534 ? 130.091 185.064 194.514 1.00 84.87  ? 2534 ILE A C     1 
ATOM   8477  O  O     . ILE A 1 2534 ? 129.538 185.956 193.860 1.00 87.56  ? 2534 ILE A O     1 
ATOM   8478  C  CB    . ILE A 1 2534 ? 131.046 185.819 196.715 1.00 80.56  ? 2534 ILE A CB    1 
ATOM   8479  C  CG1   . ILE A 1 2534 ? 130.987 185.617 198.228 1.00 85.96  ? 2534 ILE A CG1   1 
ATOM   8480  C  CG2   . ILE A 1 2534 ? 130.943 187.295 196.377 1.00 83.72  ? 2534 ILE A CG2   1 
ATOM   8481  C  CD1   . ILE A 1 2534 ? 132.280 185.938 198.925 1.00 86.10  ? 2534 ILE A CD1   1 
ATOM   8482  N  N     . ILE A 1 2535 ? 130.835 184.120 193.934 1.00 76.46  ? 2535 ILE A N     1 
ATOM   8483  C  CA    . ILE A 1 2535 ? 131.087 184.137 192.496 1.00 76.81  ? 2535 ILE A CA    1 
ATOM   8484  C  C     . ILE A 1 2535 ? 129.824 183.963 191.668 1.00 80.85  ? 2535 ILE A C     1 
ATOM   8485  O  O     . ILE A 1 2535 ? 129.845 184.231 190.461 1.00 82.41  ? 2535 ILE A O     1 
ATOM   8486  C  CB    . ILE A 1 2535 ? 132.126 183.060 192.124 1.00 71.89  ? 2535 ILE A CB    1 
ATOM   8487  C  CG1   . ILE A 1 2535 ? 133.062 183.590 191.039 1.00 75.91  ? 2535 ILE A CG1   1 
ATOM   8488  C  CG2   . ILE A 1 2535 ? 131.446 181.771 191.684 1.00 71.81  ? 2535 ILE A CG2   1 
ATOM   8489  C  CD1   . ILE A 1 2535 ? 134.150 182.630 190.652 1.00 73.52  ? 2535 ILE A CD1   1 
ATOM   8490  N  N     . ASP A 1 2536 ? 128.722 183.537 192.281 1.00 87.09  ? 2536 ASP A N     1 
ATOM   8491  C  CA    . ASP A 1 2536 ? 127.431 183.469 191.614 1.00 82.64  ? 2536 ASP A CA    1 
ATOM   8492  C  C     . ASP A 1 2536 ? 126.745 184.827 191.534 1.00 87.19  ? 2536 ASP A C     1 
ATOM   8493  O  O     . ASP A 1 2536 ? 125.607 184.907 191.063 1.00 93.31  ? 2536 ASP A O     1 
ATOM   8494  C  CB    . ASP A 1 2536 ? 126.516 182.473 192.332 1.00 81.94  ? 2536 ASP A CB    1 
ATOM   8495  C  CG    . ASP A 1 2536 ? 126.955 181.036 192.143 1.00 90.13  ? 2536 ASP A CG    1 
ATOM   8496  O  OD1   . ASP A 1 2536 ? 127.979 180.810 191.465 1.00 94.57  ? 2536 ASP A OD1   1 
ATOM   8497  O  OD2   . ASP A 1 2536 ? 126.276 180.132 192.674 1.00 87.60  ? 2536 ASP A OD2   1 
ATOM   8498  N  N     . TYR A 1 2537 ? 127.410 185.888 191.983 1.00 82.59  ? 2537 TYR A N     1 
ATOM   8499  C  CA    . TYR A 1 2537 ? 126.825 187.217 192.069 1.00 80.11  ? 2537 TYR A CA    1 
ATOM   8500  C  C     . TYR A 1 2537 ? 127.592 188.192 191.189 1.00 78.03  ? 2537 TYR A C     1 
ATOM   8501  O  O     . TYR A 1 2537 ? 128.824 188.150 191.124 1.00 83.80  ? 2537 TYR A O     1 
ATOM   8502  C  CB    . TYR A 1 2537 ? 126.829 187.726 193.511 1.00 77.69  ? 2537 TYR A CB    1 
ATOM   8503  C  CG    . TYR A 1 2537 ? 125.792 187.082 194.394 1.00 79.75  ? 2537 TYR A CG    1 
ATOM   8504  C  CD1   . TYR A 1 2537 ? 126.104 185.977 195.172 1.00 78.30  ? 2537 TYR A CD1   1 
ATOM   8505  C  CD2   . TYR A 1 2537 ? 124.502 187.586 194.459 1.00 84.02  ? 2537 TYR A CD2   1 
ATOM   8506  C  CE1   . TYR A 1 2537 ? 125.157 185.388 195.983 1.00 81.81  ? 2537 TYR A CE1   1 
ATOM   8507  C  CE2   . TYR A 1 2537 ? 123.549 187.004 195.266 1.00 86.66  ? 2537 TYR A CE2   1 
ATOM   8508  C  CZ    . TYR A 1 2537 ? 123.882 185.906 196.026 1.00 86.84  ? 2537 TYR A CZ    1 
ATOM   8509  O  OH    . TYR A 1 2537 ? 122.933 185.324 196.831 1.00 90.14  ? 2537 TYR A OH    1 
ATOM   8510  N  N     . GLU A 1 2538 ? 126.855 189.066 190.514 1.00 76.74  ? 2538 GLU A N     1 
ATOM   8511  C  CA    . GLU A 1 2538 ? 127.424 190.193 189.795 1.00 79.60  ? 2538 GLU A CA    1 
ATOM   8512  C  C     . GLU A 1 2538 ? 127.161 191.473 190.574 1.00 84.23  ? 2538 GLU A C     1 
ATOM   8513  O  O     . GLU A 1 2538 ? 126.405 191.495 191.549 1.00 90.22  ? 2538 GLU A O     1 
ATOM   8514  C  CB    . GLU A 1 2538 ? 126.838 190.302 188.384 1.00 78.32  ? 2538 GLU A CB    1 
ATOM   8515  C  CG    . GLU A 1 2538 ? 125.392 190.762 188.353 1.00 84.58  ? 2538 GLU A CG    1 
ATOM   8516  C  CD    . GLU A 1 2538 ? 124.975 191.283 186.993 1.00 88.90  ? 2538 GLU A CD    1 
ATOM   8517  O  OE1   . GLU A 1 2538 ? 125.848 191.410 186.110 1.00 90.05  ? 2538 GLU A OE1   1 
ATOM   8518  O  OE2   . GLU A 1 2538 ? 123.773 191.569 186.807 1.00 87.78  ? 2538 GLU A OE2   1 
ATOM   8519  N  N     . VAL A 1 2539 ? 127.795 192.551 190.131 1.00 78.37  ? 2539 VAL A N     1 
ATOM   8520  C  CA    . VAL A 1 2539 ? 127.634 193.864 190.741 1.00 75.59  ? 2539 VAL A CA    1 
ATOM   8521  C  C     . VAL A 1 2539 ? 126.890 194.743 189.747 1.00 80.47  ? 2539 VAL A C     1 
ATOM   8522  O  O     . VAL A 1 2539 ? 127.465 195.193 188.748 1.00 84.52  ? 2539 VAL A O     1 
ATOM   8523  C  CB    . VAL A 1 2539 ? 128.981 194.482 191.133 1.00 77.50  ? 2539 VAL A CB    1 
ATOM   8524  C  CG1   . VAL A 1 2539 ? 128.762 195.811 191.829 1.00 79.67  ? 2539 VAL A CG1   1 
ATOM   8525  C  CG2   . VAL A 1 2539 ? 129.754 193.530 192.027 1.00 78.21  ? 2539 VAL A CG2   1 
ATOM   8526  N  N     . SER A 1 2540 ? 125.612 194.988 190.017 1.00 84.49  ? 2540 SER A N     1 
ATOM   8527  C  CA    . SER A 1 2540 ? 124.820 195.850 189.158 1.00 87.58  ? 2540 SER A CA    1 
ATOM   8528  C  C     . SER A 1 2540 ? 125.286 197.295 189.290 1.00 90.87  ? 2540 SER A C     1 
ATOM   8529  O  O     . SER A 1 2540 ? 125.894 197.692 190.288 1.00 91.00  ? 2540 SER A O     1 
ATOM   8530  C  CB    . SER A 1 2540 ? 123.335 195.739 189.501 1.00 90.23  ? 2540 SER A CB    1 
ATOM   8531  O  OG    . SER A 1 2540 ? 123.098 196.088 190.853 1.00 91.85  ? 2540 SER A OG    1 
ATOM   8532  N  N     . ILE A 1 2541 ? 124.993 198.088 188.257 1.00 94.24  ? 2541 ILE A N     1 
ATOM   8533  C  CA    . ILE A 1 2541 ? 125.432 199.478 188.222 1.00 91.81  ? 2541 ILE A CA    1 
ATOM   8534  C  C     . ILE A 1 2541 ? 124.842 200.314 189.347 1.00 92.03  ? 2541 ILE A C     1 
ATOM   8535  O  O     . ILE A 1 2541 ? 125.354 201.403 189.630 1.00 89.95  ? 2541 ILE A O     1 
ATOM   8536  C  CB    . ILE A 1 2541 ? 125.093 200.108 186.856 1.00 92.33  ? 2541 ILE A CB    1 
ATOM   8537  C  CG1   . ILE A 1 2541 ? 126.086 201.222 186.524 1.00 90.46  ? 2541 ILE A CG1   1 
ATOM   8538  C  CG2   . ILE A 1 2541 ? 123.662 200.629 186.839 1.00 93.28  ? 2541 ILE A CG2   1 
ATOM   8539  C  CD1   . ILE A 1 2541 ? 127.521 200.758 186.454 1.00 90.58  ? 2541 ILE A CD1   1 
ATOM   8540  N  N     . SER A 1 2542 ? 123.787 199.835 190.003 1.00 95.63  ? 2542 SER A N     1 
ATOM   8541  C  CA    . SER A 1 2542 ? 123.194 200.545 191.127 1.00 95.67  ? 2542 SER A CA    1 
ATOM   8542  C  C     . SER A 1 2542 ? 123.976 200.364 192.420 1.00 95.25  ? 2542 SER A C     1 
ATOM   8543  O  O     . SER A 1 2542 ? 123.647 201.012 193.419 1.00 96.94  ? 2542 SER A O     1 
ATOM   8544  C  CB    . SER A 1 2542 ? 121.747 200.090 191.335 1.00 96.09  ? 2542 SER A CB    1 
ATOM   8545  O  OG    . SER A 1 2542 ? 121.695 198.758 191.815 1.00 95.61  ? 2542 SER A OG    1 
ATOM   8546  N  N     . GLY A 1 2543 ? 124.994 199.508 192.429 1.00 89.21  ? 2543 GLY A N     1 
ATOM   8547  C  CA    . GLY A 1 2543 ? 125.791 199.310 193.623 1.00 87.66  ? 2543 GLY A CA    1 
ATOM   8548  C  C     . GLY A 1 2543 ? 125.247 198.285 194.589 1.00 92.55  ? 2543 GLY A C     1 
ATOM   8549  O  O     . GLY A 1 2543 ? 125.307 198.497 195.804 1.00 95.37  ? 2543 GLY A O     1 
ATOM   8550  N  N     . GLU A 1 2544 ? 124.710 197.176 194.086 1.00 97.11  ? 2544 GLU A N     1 
ATOM   8551  C  CA    . GLU A 1 2544 ? 124.177 196.115 194.926 1.00 94.16  ? 2544 GLU A CA    1 
ATOM   8552  C  C     . GLU A 1 2544 ? 124.448 194.764 194.281 1.00 92.83  ? 2544 GLU A C     1 
ATOM   8553  O  O     . GLU A 1 2544 ? 124.542 194.652 193.055 1.00 96.61  ? 2544 GLU A O     1 
ATOM   8554  C  CB    . GLU A 1 2544 ? 122.670 196.286 195.159 1.00 96.92  ? 2544 GLU A CB    1 
ATOM   8555  C  CG    . GLU A 1 2544 ? 122.314 197.004 196.450 1.00 98.51  ? 2544 GLU A CG    1 
ATOM   8556  C  CD    . GLU A 1 2544 ? 122.410 196.103 197.667 1.00 100.11 ? 2544 GLU A CD    1 
ATOM   8557  O  OE1   . GLU A 1 2544 ? 122.647 194.889 197.496 1.00 99.87  ? 2544 GLU A OE1   1 
ATOM   8558  O  OE2   . GLU A 1 2544 ? 122.248 196.611 198.796 1.00 101.30 ? 2544 GLU A OE2   1 
ATOM   8559  N  N     . TRP A 1 2545 ? 124.572 193.738 195.118 1.00 82.73  ? 2545 TRP A N     1 
ATOM   8560  C  CA    . TRP A 1 2545 ? 124.753 192.385 194.613 1.00 85.90  ? 2545 TRP A CA    1 
ATOM   8561  C  C     . TRP A 1 2545 ? 123.459 191.865 193.999 1.00 88.59  ? 2545 TRP A C     1 
ATOM   8562  O  O     . TRP A 1 2545 ? 122.379 191.991 194.583 1.00 94.60  ? 2545 TRP A O     1 
ATOM   8563  C  CB    . TRP A 1 2545 ? 125.202 191.445 195.730 1.00 84.84  ? 2545 TRP A CB    1 
ATOM   8564  C  CG    . TRP A 1 2545 ? 126.479 191.839 196.399 1.00 86.84  ? 2545 TRP A CG    1 
ATOM   8565  C  CD1   . TRP A 1 2545 ? 126.620 192.668 197.472 1.00 89.91  ? 2545 TRP A CD1   1 
ATOM   8566  C  CD2   . TRP A 1 2545 ? 127.798 191.408 196.048 1.00 83.92  ? 2545 TRP A CD2   1 
ATOM   8567  N  NE1   . TRP A 1 2545 ? 127.947 192.785 197.808 1.00 88.84  ? 2545 TRP A NE1   1 
ATOM   8568  C  CE2   . TRP A 1 2545 ? 128.691 192.020 196.948 1.00 82.95  ? 2545 TRP A CE2   1 
ATOM   8569  C  CE3   . TRP A 1 2545 ? 128.312 190.567 195.057 1.00 86.32  ? 2545 TRP A CE3   1 
ATOM   8570  C  CZ2   . TRP A 1 2545 ? 130.066 191.818 196.887 1.00 85.04  ? 2545 TRP A CZ2   1 
ATOM   8571  C  CZ3   . TRP A 1 2545 ? 129.677 190.367 194.999 1.00 83.99  ? 2545 TRP A CZ3   1 
ATOM   8572  C  CH2   . TRP A 1 2545 ? 130.539 190.990 195.908 1.00 83.23  ? 2545 TRP A CH2   1 
ATOM   8573  N  N     . SER A 1 2546 ? 123.575 191.273 192.813 1.00 81.95  ? 2546 SER A N     1 
ATOM   8574  C  CA    . SER A 1 2546 ? 122.458 190.606 192.170 1.00 83.05  ? 2546 SER A CA    1 
ATOM   8575  C  C     . SER A 1 2546 ? 122.926 189.263 191.629 1.00 85.23  ? 2546 SER A C     1 
ATOM   8576  O  O     . SER A 1 2546 ? 123.933 189.199 190.914 1.00 88.06  ? 2546 SER A O     1 
ATOM   8577  C  CB    . SER A 1 2546 ? 121.875 191.456 191.032 1.00 84.24  ? 2546 SER A CB    1 
ATOM   8578  O  OG    . SER A 1 2546 ? 122.621 191.297 189.840 1.00 89.74  ? 2546 SER A OG    1 
ATOM   8579  N  N     . PRO A 1 2547 ? 122.228 188.179 191.958 1.00 85.74  ? 2547 PRO A N     1 
ATOM   8580  C  CA    . PRO A 1 2547 ? 122.693 186.851 191.541 1.00 83.92  ? 2547 PRO A CA    1 
ATOM   8581  C  C     . PRO A 1 2547 ? 122.675 186.701 190.028 1.00 87.67  ? 2547 PRO A C     1 
ATOM   8582  O  O     . PRO A 1 2547 ? 121.859 187.309 189.332 1.00 89.97  ? 2547 PRO A O     1 
ATOM   8583  C  CB    . PRO A 1 2547 ? 121.701 185.899 192.217 1.00 81.41  ? 2547 PRO A CB    1 
ATOM   8584  C  CG    . PRO A 1 2547 ? 120.482 186.723 192.446 1.00 87.61  ? 2547 PRO A CG    1 
ATOM   8585  C  CD    . PRO A 1 2547 ? 120.971 188.113 192.721 1.00 86.72  ? 2547 PRO A CD    1 
ATOM   8586  N  N     . TRP A 1 2548 ? 123.599 185.882 189.522 1.00 80.79  ? 2548 TRP A N     1 
ATOM   8587  C  CA    . TRP A 1 2548 ? 123.671 185.642 188.085 1.00 76.96  ? 2548 TRP A CA    1 
ATOM   8588  C  C     . TRP A 1 2548 ? 122.467 184.853 187.587 1.00 82.78  ? 2548 TRP A C     1 
ATOM   8589  O  O     . TRP A 1 2548 ? 122.178 184.861 186.386 1.00 88.02  ? 2548 TRP A O     1 
ATOM   8590  C  CB    . TRP A 1 2548 ? 124.966 184.908 187.743 1.00 68.15  ? 2548 TRP A CB    1 
ATOM   8591  C  CG    . TRP A 1 2548 ? 126.126 185.812 187.468 1.00 75.38  ? 2548 TRP A CG    1 
ATOM   8592  C  CD1   . TRP A 1 2548 ? 127.310 185.848 188.143 1.00 78.94  ? 2548 TRP A CD1   1 
ATOM   8593  C  CD2   . TRP A 1 2548 ? 126.225 186.797 186.433 1.00 79.97  ? 2548 TRP A CD2   1 
ATOM   8594  N  NE1   . TRP A 1 2548 ? 128.136 186.800 187.599 1.00 83.48  ? 2548 TRP A NE1   1 
ATOM   8595  C  CE2   . TRP A 1 2548 ? 127.494 187.396 186.547 1.00 80.06  ? 2548 TRP A CE2   1 
ATOM   8596  C  CE3   . TRP A 1 2548 ? 125.362 187.232 185.424 1.00 80.53  ? 2548 TRP A CE3   1 
ATOM   8597  C  CZ2   . TRP A 1 2548 ? 127.920 188.407 185.692 1.00 72.95  ? 2548 TRP A CZ2   1 
ATOM   8598  C  CZ3   . TRP A 1 2548 ? 125.788 188.236 184.577 1.00 80.71  ? 2548 TRP A CZ3   1 
ATOM   8599  C  CH2   . TRP A 1 2548 ? 127.054 188.813 184.716 1.00 74.27  ? 2548 TRP A CH2   1 
ATOM   8600  N  N     . GLN A 1 2549 ? 121.758 184.169 188.489 1.00 82.27  ? 2549 GLN A N     1 
ATOM   8601  C  CA    . GLN A 1 2549 ? 120.580 183.408 188.090 1.00 78.54  ? 2549 GLN A CA    1 
ATOM   8602  C  C     . GLN A 1 2549 ? 119.459 184.304 187.583 1.00 81.86  ? 2549 GLN A C     1 
ATOM   8603  O  O     . GLN A 1 2549 ? 118.586 183.828 186.849 1.00 86.33  ? 2549 GLN A O     1 
ATOM   8604  C  CB    . GLN A 1 2549 ? 120.080 182.561 189.260 1.00 75.24  ? 2549 GLN A CB    1 
ATOM   8605  C  CG    . GLN A 1 2549 ? 121.032 181.453 189.666 1.00 78.56  ? 2549 GLN A CG    1 
ATOM   8606  C  CD    . GLN A 1 2549 ? 120.580 180.093 189.176 1.00 85.67  ? 2549 GLN A CD    1 
ATOM   8607  O  OE1   . GLN A 1 2549 ? 119.788 179.991 188.240 1.00 87.13  ? 2549 GLN A OE1   1 
ATOM   8608  N  NE2   . GLN A 1 2549 ? 121.085 179.039 189.806 1.00 85.41  ? 2549 GLN A NE2   1 
ATOM   8609  N  N     . ALA A 1 2550 ? 119.458 185.584 187.958 1.00 77.52  ? 2550 ALA A N     1 
ATOM   8610  C  CA    . ALA A 1 2550 ? 118.465 186.510 187.428 1.00 80.16  ? 2550 ALA A CA    1 
ATOM   8611  C  C     . ALA A 1 2550 ? 118.655 186.764 185.940 1.00 82.25  ? 2550 ALA A C     1 
ATOM   8612  O  O     . ALA A 1 2550 ? 117.717 187.218 185.276 1.00 88.05  ? 2550 ALA A O     1 
ATOM   8613  C  CB    . ALA A 1 2550 ? 118.514 187.832 188.193 1.00 83.22  ? 2550 ALA A CB    1 
ATOM   8614  N  N     . LYS A 1 2551 ? 119.841 186.483 185.404 1.00 73.03  ? 2551 LYS A N     1 
ATOM   8615  C  CA    . LYS A 1 2551 ? 120.126 186.641 183.986 1.00 75.78  ? 2551 LYS A CA    1 
ATOM   8616  C  C     . LYS A 1 2551 ? 120.130 185.312 183.241 1.00 78.30  ? 2551 LYS A C     1 
ATOM   8617  O  O     . LYS A 1 2551 ? 120.660 185.238 182.129 1.00 82.62  ? 2551 LYS A O     1 
ATOM   8618  C  CB    . LYS A 1 2551 ? 121.465 187.354 183.793 1.00 78.78  ? 2551 LYS A CB    1 
ATOM   8619  C  CG    . LYS A 1 2551 ? 121.409 188.850 184.049 1.00 81.67  ? 2551 LYS A CG    1 
ATOM   8620  C  CD    . LYS A 1 2551 ? 122.659 189.545 183.537 1.00 83.91  ? 2551 LYS A CD    1 
ATOM   8621  C  CE    . LYS A 1 2551 ? 122.559 191.052 183.697 1.00 85.45  ? 2551 LYS A CE    1 
ATOM   8622  N  NZ    . LYS A 1 2551 ? 123.760 191.747 183.159 1.00 78.45  ? 2551 LYS A NZ    1 
ATOM   8623  N  N     . VAL A 1 2552 ? 119.553 184.268 183.827 1.00 86.20  ? 2552 VAL A N     1 
ATOM   8624  C  CA    . VAL A 1 2552 ? 119.496 182.951 183.199 1.00 85.92  ? 2552 VAL A CA    1 
ATOM   8625  C  C     . VAL A 1 2552 ? 118.031 182.572 183.018 1.00 87.44  ? 2552 VAL A C     1 
ATOM   8626  O  O     . VAL A 1 2552 ? 117.442 181.928 183.898 1.00 87.38  ? 2552 VAL A O     1 
ATOM   8627  C  CB    . VAL A 1 2552 ? 120.247 181.900 184.031 1.00 82.62  ? 2552 VAL A CB    1 
ATOM   8628  C  CG1   . VAL A 1 2552 ? 120.210 180.546 183.342 1.00 84.97  ? 2552 VAL A CG1   1 
ATOM   8629  C  CG2   . VAL A 1 2552 ? 121.681 182.338 184.268 1.00 81.53  ? 2552 VAL A CG2   1 
ATOM   8630  N  N     . PRO A 1 2553 ? 117.403 182.957 181.912 1.00 93.11  ? 2553 PRO A N     1 
ATOM   8631  C  CA    . PRO A 1 2553 ? 115.996 182.620 181.692 1.00 94.54  ? 2553 PRO A CA    1 
ATOM   8632  C  C     . PRO A 1 2553 ? 115.823 181.237 181.077 1.00 93.38  ? 2553 PRO A C     1 
ATOM   8633  O  O     . PRO A 1 2553 ? 116.719 180.690 180.432 1.00 94.11  ? 2553 PRO A O     1 
ATOM   8634  C  CB    . PRO A 1 2553 ? 115.532 183.710 180.718 1.00 91.84  ? 2553 PRO A CB    1 
ATOM   8635  C  CG    . PRO A 1 2553 ? 116.757 184.031 179.929 1.00 91.96  ? 2553 PRO A CG    1 
ATOM   8636  C  CD    . PRO A 1 2553 ? 117.944 183.808 180.838 1.00 90.11  ? 2553 PRO A CD    1 
ATOM   8637  N  N     . GLN A 1 2554 ? 114.635 180.678 181.295 1.00 99.54  ? 2554 GLN A N     1 
ATOM   8638  C  CA    . GLN A 1 2554 ? 114.262 179.390 180.715 1.00 99.76  ? 2554 GLN A CA    1 
ATOM   8639  C  C     . GLN A 1 2554 ? 113.754 179.641 179.302 1.00 97.50  ? 2554 GLN A C     1 
ATOM   8640  O  O     . GLN A 1 2554 ? 112.551 179.692 179.047 1.00 101.98 ? 2554 GLN A O     1 
ATOM   8641  C  CB    . GLN A 1 2554 ? 113.213 178.693 181.574 1.00 102.87 ? 2554 GLN A CB    1 
ATOM   8642  C  CG    . GLN A 1 2554 ? 113.783 177.841 182.703 1.00 102.13 ? 2554 GLN A CG    1 
ATOM   8643  C  CD    . GLN A 1 2554 ? 114.330 178.661 183.861 1.00 101.99 ? 2554 GLN A CD    1 
ATOM   8644  O  OE1   . GLN A 1 2554 ? 114.469 179.881 183.770 1.00 101.49 ? 2554 GLN A OE1   1 
ATOM   8645  N  NE2   . GLN A 1 2554 ? 114.645 177.987 184.960 1.00 100.03 ? 2554 GLN A NE2   1 
ATOM   8646  N  N     . ILE A 1 2555 ? 114.691 179.802 178.370 1.00 92.57  ? 2555 ILE A N     1 
ATOM   8647  C  CA    . ILE A 1 2555 ? 114.333 180.132 176.997 1.00 95.67  ? 2555 ILE A CA    1 
ATOM   8648  C  C     . ILE A 1 2555 ? 113.713 178.918 176.312 1.00 101.03 ? 2555 ILE A C     1 
ATOM   8649  O  O     . ILE A 1 2555 ? 113.799 177.783 176.787 1.00 103.11 ? 2555 ILE A O     1 
ATOM   8650  C  CB    . ILE A 1 2555 ? 115.554 180.647 176.217 1.00 96.35  ? 2555 ILE A CB    1 
ATOM   8651  C  CG1   . ILE A 1 2555 ? 116.570 179.523 176.013 1.00 95.56  ? 2555 ILE A CG1   1 
ATOM   8652  C  CG2   . ILE A 1 2555 ? 116.192 181.819 176.942 1.00 98.32  ? 2555 ILE A CG2   1 
ATOM   8653  C  CD1   . ILE A 1 2555 ? 117.455 179.713 174.802 1.00 94.93  ? 2555 ILE A CD1   1 
ATOM   8654  N  N     . GLU A 1 2556 ? 113.073 179.173 175.174 1.00 103.14 ? 2556 GLU A N     1 
ATOM   8655  C  CA    . GLU A 1 2556 ? 112.471 178.134 174.342 1.00 100.85 ? 2556 GLU A CA    1 
ATOM   8656  C  C     . GLU A 1 2556 ? 113.027 178.303 172.933 1.00 101.21 ? 2556 GLU A C     1 
ATOM   8657  O  O     . GLU A 1 2556 ? 112.612 179.204 172.198 1.00 105.80 ? 2556 GLU A O     1 
ATOM   8658  C  CB    . GLU A 1 2556 ? 110.948 178.225 174.361 1.00 103.85 ? 2556 GLU A CB    1 
ATOM   8659  C  CG    . GLU A 1 2556 ? 110.332 177.993 175.730 1.00 104.45 ? 2556 GLU A CG    1 
ATOM   8660  C  CD    . GLU A 1 2556 ? 110.482 176.560 176.201 1.00 108.58 ? 2556 GLU A CD    1 
ATOM   8661  O  OE1   . GLU A 1 2556 ? 110.486 175.649 175.347 1.00 106.46 ? 2556 GLU A OE1   1 
ATOM   8662  O  OE2   . GLU A 1 2556 ? 110.597 176.345 177.426 1.00 106.60 ? 2556 GLU A OE2   1 
ATOM   8663  N  N     . VAL A 1 2557 ? 113.970 177.436 172.562 1.00 90.72  ? 2557 VAL A N     1 
ATOM   8664  C  CA    . VAL A 1 2557 ? 114.620 177.548 171.264 1.00 91.54  ? 2557 VAL A CA    1 
ATOM   8665  C  C     . VAL A 1 2557 ? 113.628 177.221 170.155 1.00 91.73  ? 2557 VAL A C     1 
ATOM   8666  O  O     . VAL A 1 2557 ? 112.716 176.399 170.321 1.00 94.87  ? 2557 VAL A O     1 
ATOM   8667  C  CB    . VAL A 1 2557 ? 115.851 176.626 171.196 1.00 89.50  ? 2557 VAL A CB    1 
ATOM   8668  C  CG1   . VAL A 1 2557 ? 116.813 177.101 170.120 1.00 90.73  ? 2557 VAL A CG1   1 
ATOM   8669  C  CG2   . VAL A 1 2557 ? 116.542 176.568 172.548 1.00 90.02  ? 2557 VAL A CG2   1 
ATOM   8670  N  N     . GLU A 1 2558 ? 113.798 177.880 169.012 1.00 97.03  ? 2558 GLU A N     1 
ATOM   8671  C  CA    . GLU A 1 2558 ? 112.966 177.591 167.855 1.00 99.66  ? 2558 GLU A CA    1 
ATOM   8672  C  C     . GLU A 1 2558 ? 113.234 176.180 167.349 1.00 100.12 ? 2558 GLU A C     1 
ATOM   8673  O  O     . GLU A 1 2558 ? 114.327 175.632 167.516 1.00 107.40 ? 2558 GLU A O     1 
ATOM   8674  C  CB    . GLU A 1 2558 ? 113.220 178.606 166.742 1.00 101.63 ? 2558 GLU A CB    1 
ATOM   8675  C  CG    . GLU A 1 2558 ? 113.324 180.042 167.222 1.00 103.07 ? 2558 GLU A CG    1 
ATOM   8676  C  CD    . GLU A 1 2558 ? 113.317 181.037 166.080 1.00 103.16 ? 2558 GLU A CD    1 
ATOM   8677  O  OE1   . GLU A 1 2558 ? 114.274 181.832 165.976 1.00 103.76 ? 2558 GLU A OE1   1 
ATOM   8678  O  OE2   . GLU A 1 2558 ? 112.353 181.023 165.286 1.00 100.77 ? 2558 GLU A OE2   1 
ATOM   8679  N  N     . THR A 1 2559 ? 112.211 175.587 166.732 1.00 90.99  ? 2559 THR A N     1 
ATOM   8680  C  CA    . THR A 1 2559 ? 112.323 174.208 166.269 1.00 90.74  ? 2559 THR A CA    1 
ATOM   8681  C  C     . THR A 1 2559 ? 113.423 174.057 165.225 1.00 92.52  ? 2559 THR A C     1 
ATOM   8682  O  O     . THR A 1 2559 ? 114.223 173.116 165.288 1.00 95.70  ? 2559 THR A O     1 
ATOM   8683  C  CB    . THR A 1 2559 ? 110.983 173.737 165.706 1.00 92.14  ? 2559 THR A CB    1 
ATOM   8684  O  OG1   . THR A 1 2559 ? 110.037 173.601 166.774 1.00 94.83  ? 2559 THR A OG1   1 
ATOM   8685  C  CG2   . THR A 1 2559 ? 111.142 172.404 165.010 1.00 90.67  ? 2559 THR A CG2   1 
ATOM   8686  N  N     . HIS A 1 2560 ? 113.490 174.979 164.264 1.00 92.71  ? 2560 HIS A N     1 
ATOM   8687  C  CA    . HIS A 1 2560 ? 114.498 174.891 163.215 1.00 94.60  ? 2560 HIS A CA    1 
ATOM   8688  C  C     . HIS A 1 2560 ? 115.891 175.275 163.697 1.00 97.03  ? 2560 HIS A C     1 
ATOM   8689  O  O     . HIS A 1 2560 ? 116.862 175.047 162.968 1.00 98.77  ? 2560 HIS A O     1 
ATOM   8690  C  CB    . HIS A 1 2560 ? 114.102 175.774 162.031 1.00 97.40  ? 2560 HIS A CB    1 
ATOM   8691  C  CG    . HIS A 1 2560 ? 114.257 177.240 162.292 1.00 100.48 ? 2560 HIS A CG    1 
ATOM   8692  N  ND1   . HIS A 1 2560 ? 113.538 177.903 163.263 1.00 99.89  ? 2560 HIS A ND1   1 
ATOM   8693  C  CD2   . HIS A 1 2560 ? 115.046 178.172 161.706 1.00 99.14  ? 2560 HIS A CD2   1 
ATOM   8694  C  CE1   . HIS A 1 2560 ? 113.879 179.179 163.266 1.00 99.95  ? 2560 HIS A CE1   1 
ATOM   8695  N  NE2   . HIS A 1 2560 ? 114.792 179.369 162.331 1.00 100.61 ? 2560 HIS A NE2   1 
ATOM   8696  N  N     . LYS A 1 2561 ? 116.015 175.843 164.896 1.00 92.67  ? 2561 LYS A N     1 
ATOM   8697  C  CA    . LYS A 1 2561 ? 117.298 176.261 165.445 1.00 90.90  ? 2561 LYS A CA    1 
ATOM   8698  C  C     . LYS A 1 2561 ? 117.775 175.329 166.554 1.00 88.64  ? 2561 LYS A C     1 
ATOM   8699  O  O     . LYS A 1 2561 ? 118.540 175.739 167.430 1.00 93.11  ? 2561 LYS A O     1 
ATOM   8700  C  CB    . LYS A 1 2561 ? 117.218 177.698 165.959 1.00 93.11  ? 2561 LYS A CB    1 
ATOM   8701  C  CG    . LYS A 1 2561 ? 117.034 178.739 164.869 1.00 94.05  ? 2561 LYS A CG    1 
ATOM   8702  C  CD    . LYS A 1 2561 ? 118.344 179.443 164.554 1.00 93.75  ? 2561 LYS A CD    1 
ATOM   8703  C  CE    . LYS A 1 2561 ? 118.163 180.485 163.463 1.00 97.69  ? 2561 LYS A CE    1 
ATOM   8704  N  NZ    . LYS A 1 2561 ? 117.876 179.861 162.141 1.00 97.19  ? 2561 LYS A NZ    1 
ATOM   8705  N  N     . VAL A 1 2562 ? 117.332 174.074 166.530 1.00 75.81  ? 2562 VAL A N     1 
ATOM   8706  C  CA    . VAL A 1 2562 ? 117.707 173.123 167.571 1.00 76.05  ? 2562 VAL A CA    1 
ATOM   8707  C  C     . VAL A 1 2562 ? 119.159 172.712 167.368 1.00 83.23  ? 2562 VAL A C     1 
ATOM   8708  O  O     . VAL A 1 2562 ? 119.532 172.206 166.303 1.00 84.26  ? 2562 VAL A O     1 
ATOM   8709  C  CB    . VAL A 1 2562 ? 116.775 171.905 167.561 1.00 70.45  ? 2562 VAL A CB    1 
ATOM   8710  C  CG1   . VAL A 1 2562 ? 117.428 170.733 168.267 1.00 71.63  ? 2562 VAL A CG1   1 
ATOM   8711  C  CG2   . VAL A 1 2562 ? 115.451 172.249 168.215 1.00 75.96  ? 2562 VAL A CG2   1 
ATOM   8712  N  N     . ALA A 1 2563 ? 119.984 172.936 168.393 1.00 91.56  ? 2563 ALA A N     1 
ATOM   8713  C  CA    . ALA A 1 2563 ? 121.400 172.562 168.383 1.00 87.83  ? 2563 ALA A CA    1 
ATOM   8714  C  C     . ALA A 1 2563 ? 122.139 173.187 167.201 1.00 92.43  ? 2563 ALA A C     1 
ATOM   8715  O  O     . ALA A 1 2563 ? 123.059 172.593 166.636 1.00 85.48  ? 2563 ALA A O     1 
ATOM   8716  C  CB    . ALA A 1 2563 ? 121.572 171.042 168.392 1.00 84.09  ? 2563 ALA A CB    1 
ATOM   8717  N  N     . ALA A 1 2564 ? 121.730 174.394 166.823 1.00 104.71 ? 2564 ALA A N     1 
ATOM   8718  C  CA    . ALA A 1 2564 ? 122.423 175.118 165.772 1.00 99.89  ? 2564 ALA A CA    1 
ATOM   8719  C  C     . ALA A 1 2564 ? 123.801 175.559 166.265 1.00 101.28 ? 2564 ALA A C     1 
ATOM   8720  O  O     . ALA A 1 2564 ? 124.015 175.718 167.470 1.00 103.42 ? 2564 ALA A O     1 
ATOM   8721  C  CB    . ALA A 1 2564 ? 121.608 176.331 165.331 1.00 99.73  ? 2564 ALA A CB    1 
ATOM   8722  N  N     . PRO A 1 2565 ? 124.760 175.746 165.353 1.00 102.86 ? 2565 PRO A N     1 
ATOM   8723  C  CA    . PRO A 1 2565 ? 126.116 176.122 165.791 1.00 105.06 ? 2565 PRO A CA    1 
ATOM   8724  C  C     . PRO A 1 2565 ? 126.172 177.422 166.574 1.00 103.09 ? 2565 PRO A C     1 
ATOM   8725  O  O     . PRO A 1 2565 ? 127.029 177.564 167.455 1.00 104.59 ? 2565 PRO A O     1 
ATOM   8726  C  CB    . PRO A 1 2565 ? 126.897 176.225 164.471 1.00 105.13 ? 2565 PRO A CB    1 
ATOM   8727  C  CG    . PRO A 1 2565 ? 125.856 176.320 163.398 1.00 102.98 ? 2565 PRO A CG    1 
ATOM   8728  C  CD    . PRO A 1 2565 ? 124.690 175.537 163.898 1.00 101.37 ? 2565 PRO A CD    1 
ATOM   8729  N  N     . ASP A 1 2566 ? 125.290 178.377 166.286 1.00 94.97  ? 2566 ASP A N     1 
ATOM   8730  C  CA    . ASP A 1 2566 ? 125.301 179.673 166.950 1.00 95.18  ? 2566 ASP A CA    1 
ATOM   8731  C  C     . ASP A 1 2566 ? 124.251 179.804 168.050 1.00 97.84  ? 2566 ASP A C     1 
ATOM   8732  O  O     . ASP A 1 2566 ? 124.051 180.906 168.571 1.00 98.85  ? 2566 ASP A O     1 
ATOM   8733  C  CB    . ASP A 1 2566 ? 125.174 180.795 165.905 1.00 96.38  ? 2566 ASP A CB    1 
ATOM   8734  C  CG    . ASP A 1 2566 ? 123.735 181.046 165.426 1.00 102.06 ? 2566 ASP A CG    1 
ATOM   8735  O  OD1   . ASP A 1 2566 ? 122.757 180.475 165.953 1.00 101.49 ? 2566 ASP A OD1   1 
ATOM   8736  O  OD2   . ASP A 1 2566 ? 123.586 181.851 164.483 1.00 101.30 ? 2566 ASP A OD2   1 
ATOM   8737  N  N     . VAL A 1 2567 ? 123.581 178.716 168.416 1.00 86.59  ? 2567 VAL A N     1 
ATOM   8738  C  CA    . VAL A 1 2567 ? 122.561 178.733 169.460 1.00 84.22  ? 2567 VAL A CA    1 
ATOM   8739  C  C     . VAL A 1 2567 ? 123.215 178.327 170.773 1.00 82.50  ? 2567 VAL A C     1 
ATOM   8740  O  O     . VAL A 1 2567 ? 123.815 177.250 170.871 1.00 86.27  ? 2567 VAL A O     1 
ATOM   8741  C  CB    . VAL A 1 2567 ? 121.387 177.805 169.115 1.00 86.02  ? 2567 VAL A CB    1 
ATOM   8742  C  CG1   . VAL A 1 2567 ? 120.564 177.508 170.358 1.00 82.58  ? 2567 VAL A CG1   1 
ATOM   8743  C  CG2   . VAL A 1 2567 ? 120.516 178.439 168.046 1.00 86.05  ? 2567 VAL A CG2   1 
ATOM   8744  N  N     . VAL A 1 2568 ? 123.100 179.187 171.780 1.00 64.14  ? 2568 VAL A N     1 
ATOM   8745  C  CA    . VAL A 1 2568 ? 123.687 178.958 173.095 1.00 60.40  ? 2568 VAL A CA    1 
ATOM   8746  C  C     . VAL A 1 2568 ? 122.570 179.011 174.126 1.00 63.76  ? 2568 VAL A C     1 
ATOM   8747  O  O     . VAL A 1 2568 ? 121.883 180.032 174.252 1.00 65.11  ? 2568 VAL A O     1 
ATOM   8748  C  CB    . VAL A 1 2568 ? 124.776 179.990 173.422 1.00 60.19  ? 2568 VAL A CB    1 
ATOM   8749  C  CG1   . VAL A 1 2568 ? 125.418 179.678 174.762 1.00 62.16  ? 2568 VAL A CG1   1 
ATOM   8750  C  CG2   . VAL A 1 2568 ? 125.816 180.034 172.317 1.00 64.55  ? 2568 VAL A CG2   1 
ATOM   8751  N  N     . VAL A 1 2569 ? 122.390 177.919 174.862 1.00 64.01  ? 2569 VAL A N     1 
ATOM   8752  C  CA    . VAL A 1 2569 ? 121.417 177.882 175.951 1.00 59.62  ? 2569 VAL A CA    1 
ATOM   8753  C  C     . VAL A 1 2569 ? 122.041 178.568 177.160 1.00 63.55  ? 2569 VAL A C     1 
ATOM   8754  O  O     . VAL A 1 2569 ? 123.101 178.138 177.635 1.00 76.17  ? 2569 VAL A O     1 
ATOM   8755  C  CB    . VAL A 1 2569 ? 120.990 176.444 176.279 1.00 59.43  ? 2569 VAL A CB    1 
ATOM   8756  C  CG1   . VAL A 1 2569 ? 120.151 176.420 177.543 1.00 59.85  ? 2569 VAL A CG1   1 
ATOM   8757  C  CG2   . VAL A 1 2569 ? 120.221 175.843 175.116 1.00 62.50  ? 2569 VAL A CG2   1 
ATOM   8758  N  N     . PRO A 1 2570 ? 121.430 179.629 177.686 1.00 67.28  ? 2570 PRO A N     1 
ATOM   8759  C  CA    . PRO A 1 2570 ? 122.058 180.369 178.788 1.00 64.38  ? 2570 PRO A CA    1 
ATOM   8760  C  C     . PRO A 1 2570 ? 122.024 179.572 180.084 1.00 64.15  ? 2570 PRO A C     1 
ATOM   8761  O  O     . PRO A 1 2570 ? 120.969 179.103 180.515 1.00 68.93  ? 2570 PRO A O     1 
ATOM   8762  C  CB    . PRO A 1 2570 ? 121.209 181.641 178.887 1.00 66.04  ? 2570 PRO A CB    1 
ATOM   8763  C  CG    . PRO A 1 2570 ? 119.882 181.238 178.342 1.00 67.63  ? 2570 PRO A CG    1 
ATOM   8764  C  CD    . PRO A 1 2570 ? 120.174 180.256 177.244 1.00 69.54  ? 2570 PRO A CD    1 
ATOM   8765  N  N     . THR A 1 2571 ? 123.194 179.417 180.696 1.00 65.12  ? 2571 THR A N     1 
ATOM   8766  C  CA    . THR A 1 2571 ? 123.341 178.829 182.020 1.00 68.72  ? 2571 THR A CA    1 
ATOM   8767  C  C     . THR A 1 2571 ? 124.201 179.758 182.867 1.00 73.18  ? 2571 THR A C     1 
ATOM   8768  O  O     . THR A 1 2571 ? 124.677 180.794 182.396 1.00 80.83  ? 2571 THR A O     1 
ATOM   8769  C  CB    . THR A 1 2571 ? 123.955 177.425 181.953 1.00 61.17  ? 2571 THR A CB    1 
ATOM   8770  O  OG1   . THR A 1 2571 ? 125.227 177.486 181.298 1.00 67.08  ? 2571 THR A OG1   1 
ATOM   8771  C  CG2   . THR A 1 2571 ? 123.042 176.479 181.196 1.00 63.66  ? 2571 THR A CG2   1 
ATOM   8772  N  N     . LEU A 1 2572 ? 124.405 179.377 184.130 1.00 65.69  ? 2572 LEU A N     1 
ATOM   8773  C  CA    . LEU A 1 2572 ? 125.171 180.217 185.046 1.00 64.72  ? 2572 LEU A CA    1 
ATOM   8774  C  C     . LEU A 1 2572 ? 126.600 180.410 184.552 1.00 71.63  ? 2572 LEU A C     1 
ATOM   8775  O  O     . LEU A 1 2572 ? 127.099 181.541 184.468 1.00 78.09  ? 2572 LEU A O     1 
ATOM   8776  C  CB    . LEU A 1 2572 ? 125.162 179.596 186.443 1.00 61.88  ? 2572 LEU A CB    1 
ATOM   8777  C  CG    . LEU A 1 2572 ? 125.568 180.492 187.610 1.00 67.41  ? 2572 LEU A CG    1 
ATOM   8778  C  CD1   . LEU A 1 2572 ? 124.401 181.361 188.032 1.00 70.31  ? 2572 LEU A CD1   1 
ATOM   8779  C  CD2   . LEU A 1 2572 ? 126.063 179.656 188.777 1.00 69.99  ? 2572 LEU A CD2   1 
ATOM   8780  N  N     . ASP A 1 2573 ? 127.269 179.310 184.201 1.00 63.80  ? 2573 ASP A N     1 
ATOM   8781  C  CA    . ASP A 1 2573 ? 128.633 179.407 183.695 1.00 66.01  ? 2573 ASP A CA    1 
ATOM   8782  C  C     . ASP A 1 2573 ? 128.678 180.217 182.409 1.00 68.86  ? 2573 ASP A C     1 
ATOM   8783  O  O     . ASP A 1 2573 ? 129.599 181.016 182.200 1.00 75.79  ? 2573 ASP A O     1 
ATOM   8784  C  CB    . ASP A 1 2573 ? 129.208 178.010 183.470 1.00 71.92  ? 2573 ASP A CB    1 
ATOM   8785  C  CG    . ASP A 1 2573 ? 129.470 177.271 184.766 1.00 77.28  ? 2573 ASP A CG    1 
ATOM   8786  O  OD1   . ASP A 1 2573 ? 130.243 177.786 185.600 1.00 80.51  ? 2573 ASP A OD1   1 
ATOM   8787  O  OD2   . ASP A 1 2573 ? 128.902 176.174 184.950 1.00 73.64  ? 2573 ASP A OD2   1 
ATOM   8788  N  N     . THR A 1 2574 ? 127.681 180.035 181.542 1.00 60.66  ? 2574 THR A N     1 
ATOM   8789  C  CA    . THR A 1 2574 ? 127.658 180.751 180.272 1.00 58.37  ? 2574 THR A CA    1 
ATOM   8790  C  C     . THR A 1 2574 ? 127.608 182.259 180.489 1.00 63.91  ? 2574 THR A C     1 
ATOM   8791  O  O     . THR A 1 2574 ? 128.403 183.002 179.905 1.00 69.55  ? 2574 THR A O     1 
ATOM   8792  C  CB    . THR A 1 2574 ? 126.472 180.286 179.426 1.00 61.28  ? 2574 THR A CB    1 
ATOM   8793  O  OG1   . THR A 1 2574 ? 126.782 179.024 178.822 1.00 66.78  ? 2574 THR A OG1   1 
ATOM   8794  C  CG2   . THR A 1 2574 ? 126.165 181.295 178.334 1.00 60.29  ? 2574 THR A CG2   1 
ATOM   8795  N  N     . VAL A 1 2575 ? 126.699 182.731 181.347 1.00 58.30  ? 2575 VAL A N     1 
ATOM   8796  C  CA    . VAL A 1 2575 ? 126.565 184.173 181.537 1.00 56.01  ? 2575 VAL A CA    1 
ATOM   8797  C  C     . VAL A 1 2575 ? 127.773 184.735 182.280 1.00 57.27  ? 2575 VAL A C     1 
ATOM   8798  O  O     . VAL A 1 2575 ? 128.261 185.825 181.956 1.00 65.18  ? 2575 VAL A O     1 
ATOM   8799  C  CB    . VAL A 1 2575 ? 125.245 184.520 182.251 1.00 57.59  ? 2575 VAL A CB    1 
ATOM   8800  C  CG1   . VAL A 1 2575 ? 124.071 184.364 181.295 1.00 61.61  ? 2575 VAL A CG1   1 
ATOM   8801  C  CG2   . VAL A 1 2575 ? 125.050 183.676 183.492 1.00 62.26  ? 2575 VAL A CG2   1 
ATOM   8802  N  N     . ARG A 1 2576 ? 128.280 184.006 183.281 1.00 48.16  ? 2576 ARG A N     1 
ATOM   8803  C  CA    . ARG A 1 2576 ? 129.458 184.483 184.002 1.00 53.74  ? 2576 ARG A CA    1 
ATOM   8804  C  C     . ARG A 1 2576 ? 130.648 184.642 183.063 1.00 58.47  ? 2576 ARG A C     1 
ATOM   8805  O  O     . ARG A 1 2576 ? 131.316 185.686 183.051 1.00 62.25  ? 2576 ARG A O     1 
ATOM   8806  C  CB    . ARG A 1 2576 ? 129.802 183.527 185.144 1.00 54.04  ? 2576 ARG A CB    1 
ATOM   8807  C  CG    . ARG A 1 2576 ? 128.765 183.472 186.246 1.00 63.99  ? 2576 ARG A CG    1 
ATOM   8808  C  CD    . ARG A 1 2576 ? 129.290 182.729 187.460 1.00 62.20  ? 2576 ARG A CD    1 
ATOM   8809  N  NE    . ARG A 1 2576 ? 130.067 181.554 187.086 1.00 50.73  ? 2576 ARG A NE    1 
ATOM   8810  C  CZ    . ARG A 1 2576 ? 130.230 180.489 187.858 1.00 58.83  ? 2576 ARG A CZ    1 
ATOM   8811  N  NH1   . ARG A 1 2576 ? 129.677 180.413 189.057 1.00 59.36  ? 2576 ARG A NH1   1 
ATOM   8812  N  NH2   . ARG A 1 2576 ? 130.967 179.474 187.416 1.00 64.12  ? 2576 ARG A NH2   1 
ATOM   8813  N  N     . HIS A 1 2577 ? 130.916 183.618 182.249 1.00 64.27  ? 2577 HIS A N     1 
ATOM   8814  C  CA    . HIS A 1 2577 ? 132.061 183.680 181.352 1.00 54.55  ? 2577 HIS A CA    1 
ATOM   8815  C  C     . HIS A 1 2577 ? 131.834 184.684 180.231 1.00 59.83  ? 2577 HIS A C     1 
ATOM   8816  O  O     . HIS A 1 2577 ? 132.784 185.318 179.768 1.00 65.37  ? 2577 HIS A O     1 
ATOM   8817  C  CB    . HIS A 1 2577 ? 132.362 182.291 180.796 1.00 48.00  ? 2577 HIS A CB    1 
ATOM   8818  C  CG    . HIS A 1 2577 ? 132.820 181.318 181.835 1.00 50.73  ? 2577 HIS A CG    1 
ATOM   8819  N  ND1   . HIS A 1 2577 ? 132.835 179.956 181.628 1.00 63.55  ? 2577 HIS A ND1   1 
ATOM   8820  C  CD2   . HIS A 1 2577 ? 133.282 181.513 183.093 1.00 53.77  ? 2577 HIS A CD2   1 
ATOM   8821  C  CE1   . HIS A 1 2577 ? 133.286 179.353 182.714 1.00 59.33  ? 2577 HIS A CE1   1 
ATOM   8822  N  NE2   . HIS A 1 2577 ? 133.564 180.275 183.617 1.00 53.59  ? 2577 HIS A NE2   1 
ATOM   8823  N  N     . GLU A 1 2578 ? 130.586 184.858 179.788 1.00 59.69  ? 2578 GLU A N     1 
ATOM   8824  C  CA    . GLU A 1 2578 ? 130.304 185.881 178.789 1.00 53.89  ? 2578 GLU A CA    1 
ATOM   8825  C  C     . GLU A 1 2578 ? 130.611 187.269 179.330 1.00 61.07  ? 2578 GLU A C     1 
ATOM   8826  O  O     . GLU A 1 2578 ? 131.231 188.088 178.641 1.00 72.99  ? 2578 GLU A O     1 
ATOM   8827  C  CB    . GLU A 1 2578 ? 128.846 185.793 178.341 1.00 60.63  ? 2578 GLU A CB    1 
ATOM   8828  C  CG    . GLU A 1 2578 ? 128.606 184.846 177.180 1.00 67.89  ? 2578 GLU A CG    1 
ATOM   8829  C  CD    . GLU A 1 2578 ? 127.131 184.633 176.899 1.00 77.22  ? 2578 GLU A CD    1 
ATOM   8830  O  OE1   . GLU A 1 2578 ? 126.309 185.431 177.394 1.00 80.05  ? 2578 GLU A OE1   1 
ATOM   8831  O  OE2   . GLU A 1 2578 ? 126.794 183.665 176.186 1.00 71.03  ? 2578 GLU A OE2   1 
ATOM   8832  N  N     . ALA A 1 2579 ? 130.191 187.551 180.565 1.00 57.99  ? 2579 ALA A N     1 
ATOM   8833  C  CA    . ALA A 1 2579 ? 130.488 188.850 181.159 1.00 61.06  ? 2579 ALA A CA    1 
ATOM   8834  C  C     . ALA A 1 2579 ? 131.988 189.045 181.337 1.00 55.42  ? 2579 ALA A C     1 
ATOM   8835  O  O     . ALA A 1 2579 ? 132.520 190.123 181.046 1.00 56.39  ? 2579 ALA A O     1 
ATOM   8836  C  CB    . ALA A 1 2579 ? 129.767 188.998 182.496 1.00 61.37  ? 2579 ALA A CB    1 
ATOM   8837  N  N     . LEU A 1 2580 ? 132.686 188.010 181.811 1.00 49.36  ? 2580 LEU A N     1 
ATOM   8838  C  CA    . LEU A 1 2580 ? 134.132 188.116 181.994 1.00 43.46  ? 2580 LEU A CA    1 
ATOM   8839  C  C     . LEU A 1 2580 ? 134.845 188.367 180.669 1.00 51.82  ? 2580 LEU A C     1 
ATOM   8840  O  O     . LEU A 1 2580 ? 135.737 189.222 180.583 1.00 55.31  ? 2580 LEU A O     1 
ATOM   8841  C  CB    . LEU A 1 2580 ? 134.663 186.847 182.659 1.00 43.85  ? 2580 LEU A CB    1 
ATOM   8842  C  CG    . LEU A 1 2580 ? 136.047 186.882 183.305 1.00 45.99  ? 2580 LEU A CG    1 
ATOM   8843  C  CD1   . LEU A 1 2580 ? 136.015 187.670 184.598 1.00 47.96  ? 2580 LEU A CD1   1 
ATOM   8844  C  CD2   . LEU A 1 2580 ? 136.530 185.471 183.568 1.00 51.32  ? 2580 LEU A CD2   1 
ATOM   8845  N  N     . LEU A 1 2581 ? 134.464 187.632 179.622 1.00 50.52  ? 2581 LEU A N     1 
ATOM   8846  C  CA    . LEU A 1 2581 ? 135.102 187.811 178.326 1.00 47.07  ? 2581 LEU A CA    1 
ATOM   8847  C  C     . LEU A 1 2581 ? 134.790 189.178 177.736 1.00 56.01  ? 2581 LEU A C     1 
ATOM   8848  O  O     . LEU A 1 2581 ? 135.663 189.800 177.127 1.00 54.70  ? 2581 LEU A O     1 
ATOM   8849  C  CB    . LEU A 1 2581 ? 134.678 186.703 177.364 1.00 46.85  ? 2581 LEU A CB    1 
ATOM   8850  C  CG    . LEU A 1 2581 ? 135.154 185.290 177.697 1.00 47.03  ? 2581 LEU A CG    1 
ATOM   8851  C  CD1   . LEU A 1 2581 ? 134.761 184.338 176.586 1.00 58.33  ? 2581 LEU A CD1   1 
ATOM   8852  C  CD2   . LEU A 1 2581 ? 136.649 185.262 177.935 1.00 40.74  ? 2581 LEU A CD2   1 
ATOM   8853  N  N     . TYR A 1 2582 ? 133.555 189.663 177.886 1.00 57.39  ? 2582 TYR A N     1 
ATOM   8854  C  CA    . TYR A 1 2582 ? 133.244 191.003 177.399 1.00 50.09  ? 2582 TYR A CA    1 
ATOM   8855  C  C     . TYR A 1 2582 ? 134.082 192.039 178.138 1.00 56.48  ? 2582 TYR A C     1 
ATOM   8856  O  O     . TYR A 1 2582 ? 134.621 192.968 177.523 1.00 69.57  ? 2582 TYR A O     1 
ATOM   8857  C  CB    . TYR A 1 2582 ? 131.739 191.271 177.543 1.00 48.75  ? 2582 TYR A CB    1 
ATOM   8858  C  CG    . TYR A 1 2582 ? 131.230 192.623 177.054 1.00 57.95  ? 2582 TYR A CG    1 
ATOM   8859  C  CD1   . TYR A 1 2582 ? 130.194 192.691 176.131 1.00 61.77  ? 2582 TYR A CD1   1 
ATOM   8860  C  CD2   . TYR A 1 2582 ? 131.730 193.821 177.553 1.00 64.59  ? 2582 TYR A CD2   1 
ATOM   8861  C  CE1   . TYR A 1 2582 ? 129.711 193.906 175.684 1.00 71.08  ? 2582 TYR A CE1   1 
ATOM   8862  C  CE2   . TYR A 1 2582 ? 131.255 195.037 177.112 1.00 67.72  ? 2582 TYR A CE2   1 
ATOM   8863  C  CZ    . TYR A 1 2582 ? 130.243 195.076 176.180 1.00 74.06  ? 2582 TYR A CZ    1 
ATOM   8864  O  OH    . TYR A 1 2582 ? 129.763 196.290 175.744 1.00 72.91  ? 2582 TYR A OH    1 
ATOM   8865  N  N     . THR A 1 2583 ? 134.227 191.876 179.456 1.00 52.36  ? 2583 THR A N     1 
ATOM   8866  C  CA    . THR A 1 2583 ? 135.040 192.803 180.237 1.00 50.59  ? 2583 THR A CA    1 
ATOM   8867  C  C     . THR A 1 2583 ? 136.486 192.810 179.761 1.00 47.95  ? 2583 THR A C     1 
ATOM   8868  O  O     . THR A 1 2583 ? 137.100 193.875 179.630 1.00 49.00  ? 2583 THR A O     1 
ATOM   8869  C  CB    . THR A 1 2583 ? 134.963 192.436 181.720 1.00 50.66  ? 2583 THR A CB    1 
ATOM   8870  O  OG1   . THR A 1 2583 ? 133.683 192.812 182.244 1.00 58.78  ? 2583 THR A OG1   1 
ATOM   8871  C  CG2   . THR A 1 2583 ? 136.057 193.127 182.508 1.00 47.68  ? 2583 THR A CG2   1 
ATOM   8872  N  N     . TRP A 1 2584 ? 137.049 191.632 179.488 1.00 50.93  ? 2584 TRP A N     1 
ATOM   8873  C  CA    . TRP A 1 2584 ? 138.445 191.584 179.063 1.00 50.58  ? 2584 TRP A CA    1 
ATOM   8874  C  C     . TRP A 1 2584 ? 138.642 192.057 177.625 1.00 57.18  ? 2584 TRP A C     1 
ATOM   8875  O  O     . TRP A 1 2584 ? 139.645 192.718 177.335 1.00 57.89  ? 2584 TRP A O     1 
ATOM   8876  C  CB    . TRP A 1 2584 ? 139.007 190.174 179.238 1.00 51.81  ? 2584 TRP A CB    1 
ATOM   8877  C  CG    . TRP A 1 2584 ? 139.274 189.829 180.667 1.00 50.46  ? 2584 TRP A CG    1 
ATOM   8878  C  CD1   . TRP A 1 2584 ? 139.381 190.699 181.711 1.00 47.83  ? 2584 TRP A CD1   1 
ATOM   8879  C  CD2   . TRP A 1 2584 ? 139.487 188.522 181.211 1.00 54.94  ? 2584 TRP A CD2   1 
ATOM   8880  N  NE1   . TRP A 1 2584 ? 139.638 190.015 182.873 1.00 55.86  ? 2584 TRP A NE1   1 
ATOM   8881  C  CE2   . TRP A 1 2584 ? 139.709 188.677 182.592 1.00 54.10  ? 2584 TRP A CE2   1 
ATOM   8882  C  CE3   . TRP A 1 2584 ? 139.508 187.236 180.664 1.00 56.53  ? 2584 TRP A CE3   1 
ATOM   8883  C  CZ2   . TRP A 1 2584 ? 139.949 187.595 183.435 1.00 49.80  ? 2584 TRP A CZ2   1 
ATOM   8884  C  CZ3   . TRP A 1 2584 ? 139.746 186.165 181.501 1.00 53.72  ? 2584 TRP A CZ3   1 
ATOM   8885  C  CH2   . TRP A 1 2584 ? 139.964 186.350 182.871 1.00 53.36  ? 2584 TRP A CH2   1 
ATOM   8886  N  N     . LEU A 1 2585 ? 137.716 191.741 176.716 1.00 59.29  ? 2585 LEU A N     1 
ATOM   8887  C  CA    . LEU A 1 2585 ? 137.879 192.146 175.322 1.00 53.44  ? 2585 LEU A CA    1 
ATOM   8888  C  C     . LEU A 1 2585 ? 137.594 193.628 175.119 1.00 46.55  ? 2585 LEU A C     1 
ATOM   8889  O  O     . LEU A 1 2585 ? 138.141 194.242 174.197 1.00 57.52  ? 2585 LEU A O     1 
ATOM   8890  C  CB    . LEU A 1 2585 ? 136.979 191.312 174.407 1.00 44.48  ? 2585 LEU A CB    1 
ATOM   8891  C  CG    . LEU A 1 2585 ? 137.187 189.799 174.354 1.00 41.57  ? 2585 LEU A CG    1 
ATOM   8892  C  CD1   . LEU A 1 2585 ? 135.875 189.076 174.098 1.00 48.50  ? 2585 LEU A CD1   1 
ATOM   8893  C  CD2   . LEU A 1 2585 ? 138.202 189.456 173.287 1.00 53.76  ? 2585 LEU A CD2   1 
ATOM   8894  N  N     . ALA A 1 2586 ? 136.736 194.221 175.954 1.00 56.40  ? 2586 ALA A N     1 
ATOM   8895  C  CA    . ALA A 1 2586 ? 136.461 195.648 175.821 1.00 59.38  ? 2586 ALA A CA    1 
ATOM   8896  C  C     . ALA A 1 2586 ? 137.710 196.482 176.074 1.00 65.61  ? 2586 ALA A C     1 
ATOM   8897  O  O     . ALA A 1 2586 ? 137.801 197.622 175.605 1.00 71.67  ? 2586 ALA A O     1 
ATOM   8898  C  CB    . ALA A 1 2586 ? 135.341 196.061 176.774 1.00 68.92  ? 2586 ALA A CB    1 
ATOM   8899  N  N     . GLU A 1 2587 ? 138.676 195.935 176.806 1.00 67.26  ? 2587 GLU A N     1 
ATOM   8900  C  CA    . GLU A 1 2587 ? 139.957 196.586 177.036 1.00 69.41  ? 2587 GLU A CA    1 
ATOM   8901  C  C     . GLU A 1 2587 ? 140.973 196.289 175.943 1.00 71.30  ? 2587 GLU A C     1 
ATOM   8902  O  O     . GLU A 1 2587 ? 142.101 196.786 176.019 1.00 74.29  ? 2587 GLU A O     1 
ATOM   8903  C  CB    . GLU A 1 2587 ? 140.535 196.154 178.387 1.00 72.99  ? 2587 GLU A CB    1 
ATOM   8904  C  CG    . GLU A 1 2587 ? 139.617 196.386 179.571 1.00 75.53  ? 2587 GLU A CG    1 
ATOM   8905  C  CD    . GLU A 1 2587 ? 139.698 197.802 180.097 1.00 85.23  ? 2587 GLU A CD    1 
ATOM   8906  O  OE1   . GLU A 1 2587 ? 138.637 198.436 180.264 1.00 81.39  ? 2587 GLU A OE1   1 
ATOM   8907  O  OE2   . GLU A 1 2587 ? 140.826 198.283 180.335 1.00 84.31  ? 2587 GLU A OE2   1 
ATOM   8908  N  N     . HIS A 1 2588 ? 140.604 195.488 174.940 1.00 60.70  ? 2588 HIS A N     1 
ATOM   8909  C  CA    . HIS A 1 2588 ? 141.535 195.000 173.923 1.00 56.91  ? 2588 HIS A CA    1 
ATOM   8910  C  C     . HIS A 1 2588 ? 142.701 194.249 174.557 1.00 62.47  ? 2588 HIS A C     1 
ATOM   8911  O  O     . HIS A 1 2588 ? 143.820 194.257 174.040 1.00 65.18  ? 2588 HIS A O     1 
ATOM   8912  C  CB    . HIS A 1 2588 ? 142.040 196.138 173.032 1.00 55.00  ? 2588 HIS A CB    1 
ATOM   8913  C  CG    . HIS A 1 2588 ? 140.952 197.032 172.528 1.00 61.21  ? 2588 HIS A CG    1 
ATOM   8914  N  ND1   . HIS A 1 2588 ? 139.858 196.556 171.839 1.00 60.17  ? 2588 HIS A ND1   1 
ATOM   8915  C  CD2   . HIS A 1 2588 ? 140.786 198.372 172.619 1.00 65.81  ? 2588 HIS A CD2   1 
ATOM   8916  C  CE1   . HIS A 1 2588 ? 139.066 197.565 171.524 1.00 62.73  ? 2588 HIS A CE1   1 
ATOM   8917  N  NE2   . HIS A 1 2588 ? 139.606 198.678 171.985 1.00 66.94  ? 2588 HIS A NE2   1 
ATOM   8918  N  N     . LYS A 1 2589 ? 142.435 193.600 175.681 1.00 60.96  ? 2589 LYS A N     1 
ATOM   8919  C  CA    . LYS A 1 2589 ? 143.451 192.863 176.418 1.00 57.93  ? 2589 LYS A CA    1 
ATOM   8920  C  C     . LYS A 1 2589 ? 143.517 191.427 175.912 1.00 56.03  ? 2589 LYS A C     1 
ATOM   8921  O  O     . LYS A 1 2589 ? 142.481 190.761 175.827 1.00 61.82  ? 2589 LYS A O     1 
ATOM   8922  C  CB    . LYS A 1 2589 ? 143.134 192.881 177.910 1.00 61.21  ? 2589 LYS A CB    1 
ATOM   8923  C  CG    . LYS A 1 2589 ? 144.080 192.071 178.775 1.00 60.87  ? 2589 LYS A CG    1 
ATOM   8924  C  CD    . LYS A 1 2589 ? 145.236 192.922 179.266 1.00 57.88  ? 2589 LYS A CD    1 
ATOM   8925  C  CE    . LYS A 1 2589 ? 145.973 192.242 180.405 1.00 61.79  ? 2589 LYS A CE    1 
ATOM   8926  N  NZ    . LYS A 1 2589 ? 147.266 192.910 180.709 1.00 65.99  ? 2589 LYS A NZ    1 
ATOM   8927  N  N     . PRO A 1 2590 ? 144.697 190.925 175.552 1.00 54.74  ? 2590 PRO A N     1 
ATOM   8928  C  CA    . PRO A 1 2590 ? 144.799 189.520 175.145 1.00 52.34  ? 2590 PRO A CA    1 
ATOM   8929  C  C     . PRO A 1 2590 ? 144.400 188.597 176.284 1.00 55.66  ? 2590 PRO A C     1 
ATOM   8930  O  O     . PRO A 1 2590 ? 144.691 188.861 177.451 1.00 63.31  ? 2590 PRO A O     1 
ATOM   8931  C  CB    . PRO A 1 2590 ? 146.279 189.365 174.781 1.00 44.09  ? 2590 PRO A CB    1 
ATOM   8932  C  CG    . PRO A 1 2590 ? 146.965 190.422 175.573 1.00 50.99  ? 2590 PRO A CG    1 
ATOM   8933  C  CD    . PRO A 1 2590 ? 146.013 191.581 175.604 1.00 56.10  ? 2590 PRO A CD    1 
ATOM   8934  N  N     . LEU A 1 2591 ? 143.726 187.504 175.936 1.00 52.95  ? 2591 LEU A N     1 
ATOM   8935  C  CA    . LEU A 1 2591 ? 143.223 186.568 176.929 1.00 47.69  ? 2591 LEU A CA    1 
ATOM   8936  C  C     . LEU A 1 2591 ? 143.275 185.159 176.360 1.00 49.25  ? 2591 LEU A C     1 
ATOM   8937  O  O     . LEU A 1 2591 ? 143.313 184.958 175.144 1.00 62.05  ? 2591 LEU A O     1 
ATOM   8938  C  CB    . LEU A 1 2591 ? 141.796 186.932 177.368 1.00 43.30  ? 2591 LEU A CB    1 
ATOM   8939  C  CG    . LEU A 1 2591 ? 140.630 186.672 176.411 1.00 45.08  ? 2591 LEU A CG    1 
ATOM   8940  C  CD1   . LEU A 1 2591 ? 140.013 185.301 176.633 1.00 52.75  ? 2591 LEU A CD1   1 
ATOM   8941  C  CD2   . LEU A 1 2591 ? 139.579 187.758 176.549 1.00 54.49  ? 2591 LEU A CD2   1 
ATOM   8942  N  N     . VAL A 1 2592 ? 143.278 184.180 177.260 1.00 37.28  ? 2592 VAL A N     1 
ATOM   8943  C  CA    . VAL A 1 2592 ? 143.346 182.771 176.896 1.00 36.57  ? 2592 VAL A CA    1 
ATOM   8944  C  C     . VAL A 1 2592 ? 142.285 182.015 177.682 1.00 49.39  ? 2592 VAL A C     1 
ATOM   8945  O  O     . VAL A 1 2592 ? 142.202 182.150 178.907 1.00 64.68  ? 2592 VAL A O     1 
ATOM   8946  C  CB    . VAL A 1 2592 ? 144.743 182.180 177.167 1.00 37.49  ? 2592 VAL A CB    1 
ATOM   8947  C  CG1   . VAL A 1 2592 ? 144.706 180.668 177.072 1.00 44.59  ? 2592 VAL A CG1   1 
ATOM   8948  C  CG2   . VAL A 1 2592 ? 145.758 182.750 176.192 1.00 45.42  ? 2592 VAL A CG2   1 
ATOM   8949  N  N     . LEU A 1 2593 ? 141.475 181.228 176.980 1.00 49.63  ? 2593 LEU A N     1 
ATOM   8950  C  CA    . LEU A 1 2593 ? 140.510 180.331 177.602 1.00 47.05  ? 2593 LEU A CA    1 
ATOM   8951  C  C     . LEU A 1 2593 ? 141.089 178.925 177.594 1.00 47.44  ? 2593 LEU A C     1 
ATOM   8952  O  O     . LEU A 1 2593 ? 141.339 178.360 176.524 1.00 62.48  ? 2593 LEU A O     1 
ATOM   8953  C  CB    . LEU A 1 2593 ? 139.169 180.354 176.869 1.00 47.06  ? 2593 LEU A CB    1 
ATOM   8954  C  CG    . LEU A 1 2593 ? 138.458 181.693 176.699 1.00 46.02  ? 2593 LEU A CG    1 
ATOM   8955  C  CD1   . LEU A 1 2593 ? 138.610 182.201 175.277 1.00 46.11  ? 2593 LEU A CD1   1 
ATOM   8956  C  CD2   . LEU A 1 2593 ? 136.995 181.537 177.065 1.00 49.78  ? 2593 LEU A CD2   1 
ATOM   8957  N  N     . CYS A 1 2594 ? 141.300 178.364 178.778 1.00 48.78  ? 2594 CYS A N     1 
ATOM   8958  C  CA    . CYS A 1 2594 ? 141.858 177.029 178.918 1.00 52.25  ? 2594 CYS A CA    1 
ATOM   8959  C  C     . CYS A 1 2594 ? 140.821 176.101 179.533 1.00 60.90  ? 2594 CYS A C     1 
ATOM   8960  O  O     . CYS A 1 2594 ? 140.181 176.444 180.531 1.00 70.61  ? 2594 CYS A O     1 
ATOM   8961  C  CB    . CYS A 1 2594 ? 143.122 177.049 179.778 1.00 58.95  ? 2594 CYS A CB    1 
ATOM   8962  S  SG    . CYS A 1 2594 ? 144.048 175.501 179.753 1.00 90.42  ? 2594 CYS A SG    1 
ATOM   8963  N  N     . GLY A 1 2595 ? 140.658 174.927 178.931 1.00 57.21  ? 2595 GLY A N     1 
ATOM   8964  C  CA    . GLY A 1 2595 ? 139.711 173.952 179.409 1.00 56.58  ? 2595 GLY A CA    1 
ATOM   8965  C  C     . GLY A 1 2595 ? 139.741 172.680 178.589 1.00 64.48  ? 2595 GLY A C     1 
ATOM   8966  O  O     . GLY A 1 2595 ? 140.403 172.600 177.549 1.00 69.34  ? 2595 GLY A O     1 
ATOM   8967  N  N     . PRO A 1 2596 ? 139.025 171.656 179.046 1.00 64.26  ? 2596 PRO A N     1 
ATOM   8968  C  CA    . PRO A 1 2596 ? 139.002 170.399 178.308 1.00 55.55  ? 2596 PRO A CA    1 
ATOM   8969  C  C     . PRO A 1 2596 ? 138.330 170.585 176.965 1.00 65.49  ? 2596 PRO A C     1 
ATOM   8970  O  O     . PRO A 1 2596 ? 137.528 171.519 176.775 1.00 78.24  ? 2596 PRO A O     1 
ATOM   8971  C  CB    . PRO A 1 2596 ? 138.192 169.469 179.221 1.00 56.61  ? 2596 PRO A CB    1 
ATOM   8972  C  CG    . PRO A 1 2596 ? 138.234 170.107 180.569 1.00 63.65  ? 2596 PRO A CG    1 
ATOM   8973  C  CD    . PRO A 1 2596 ? 138.267 171.574 180.303 1.00 65.12  ? 2596 PRO A CD    1 
ATOM   8974  N  N     . PRO A 1 2597 ? 138.641 169.731 175.989 1.00 54.22  ? 2597 PRO A N     1 
ATOM   8975  C  CA    . PRO A 1 2597 ? 138.029 169.878 174.663 1.00 56.40  ? 2597 PRO A CA    1 
ATOM   8976  C  C     . PRO A 1 2597 ? 136.516 169.739 174.730 1.00 64.55  ? 2597 PRO A C     1 
ATOM   8977  O  O     . PRO A 1 2597 ? 135.980 168.909 175.467 1.00 65.71  ? 2597 PRO A O     1 
ATOM   8978  C  CB    . PRO A 1 2597 ? 138.664 168.745 173.851 1.00 53.71  ? 2597 PRO A CB    1 
ATOM   8979  C  CG    . PRO A 1 2597 ? 139.110 167.753 174.867 1.00 57.37  ? 2597 PRO A CG    1 
ATOM   8980  C  CD    . PRO A 1 2597 ? 139.520 168.553 176.063 1.00 54.65  ? 2597 PRO A CD    1 
ATOM   8981  N  N     . GLY A 1 2598 ? 135.827 170.568 173.949 1.00 60.87  ? 2598 GLY A N     1 
ATOM   8982  C  CA    . GLY A 1 2598 ? 134.381 170.552 173.919 1.00 58.24  ? 2598 GLY A CA    1 
ATOM   8983  C  C     . GLY A 1 2598 ? 133.706 171.194 175.107 1.00 60.08  ? 2598 GLY A C     1 
ATOM   8984  O  O     . GLY A 1 2598 ? 132.480 171.098 175.228 1.00 75.05  ? 2598 GLY A O     1 
ATOM   8985  N  N     . SER A 1 2599 ? 134.464 171.845 175.992 1.00 45.02  ? 2599 SER A N     1 
ATOM   8986  C  CA    . SER A 1 2599 ? 133.860 172.470 177.162 1.00 48.76  ? 2599 SER A CA    1 
ATOM   8987  C  C     . SER A 1 2599 ? 132.996 173.664 176.783 1.00 55.96  ? 2599 SER A C     1 
ATOM   8988  O  O     . SER A 1 2599 ? 132.005 173.951 177.464 1.00 59.91  ? 2599 SER A O     1 
ATOM   8989  C  CB    . SER A 1 2599 ? 134.944 172.894 178.149 1.00 58.94  ? 2599 SER A CB    1 
ATOM   8990  O  OG    . SER A 1 2599 ? 134.421 173.783 179.119 1.00 76.08  ? 2599 SER A OG    1 
ATOM   8991  N  N     . GLY A 1 2600 ? 133.351 174.370 175.714 1.00 60.78  ? 2600 GLY A N     1 
ATOM   8992  C  CA    . GLY A 1 2600 ? 132.576 175.513 175.281 1.00 59.49  ? 2600 GLY A CA    1 
ATOM   8993  C  C     . GLY A 1 2600 ? 133.383 176.790 175.178 1.00 64.93  ? 2600 GLY A C     1 
ATOM   8994  O  O     . GLY A 1 2600 ? 132.820 177.886 175.214 1.00 68.10  ? 2600 GLY A O     1 
ATOM   8995  N  N     . LYS A 1 2601 ? 134.705 176.660 175.053 1.00 61.83  ? 2601 LYS A N     1 
ATOM   8996  C  CA    . LYS A 1 2601 ? 135.561 177.840 174.964 1.00 53.87  ? 2601 LYS A CA    1 
ATOM   8997  C  C     . LYS A 1 2601 ? 135.242 178.658 173.718 1.00 49.76  ? 2601 LYS A C     1 
ATOM   8998  O  O     . LYS A 1 2601 ? 134.997 179.868 173.800 1.00 63.83  ? 2601 LYS A O     1 
ATOM   8999  C  CB    . LYS A 1 2601 ? 137.030 177.419 174.970 1.00 57.06  ? 2601 LYS A CB    1 
ATOM   9000  C  CG    . LYS A 1 2601 ? 137.434 176.602 176.184 1.00 60.45  ? 2601 LYS A CG    1 
ATOM   9001  C  CD    . LYS A 1 2601 ? 138.895 176.195 176.119 1.00 58.48  ? 2601 LYS A CD    1 
ATOM   9002  C  CE    . LYS A 1 2601 ? 139.130 175.140 175.056 1.00 54.03  ? 2601 LYS A CE    1 
ATOM   9003  N  NZ    . LYS A 1 2601 ? 138.370 173.895 175.344 1.00 54.71  ? 2601 LYS A NZ    1 
ATOM   9004  N  N     . THR A 1 2602 ? 135.233 178.008 172.552 1.00 45.90  ? 2602 THR A N     1 
ATOM   9005  C  CA    . THR A 1 2602 ? 134.935 178.718 171.313 1.00 48.15  ? 2602 THR A CA    1 
ATOM   9006  C  C     . THR A 1 2602 ? 133.509 179.253 171.314 1.00 55.22  ? 2602 THR A C     1 
ATOM   9007  O  O     . THR A 1 2602 ? 133.262 180.381 170.873 1.00 72.43  ? 2602 THR A O     1 
ATOM   9008  C  CB    . THR A 1 2602 ? 135.158 177.801 170.111 1.00 54.73  ? 2602 THR A CB    1 
ATOM   9009  O  OG1   . THR A 1 2602 ? 136.468 177.225 170.184 1.00 65.46  ? 2602 THR A OG1   1 
ATOM   9010  C  CG2   . THR A 1 2602 ? 135.030 178.581 168.815 1.00 56.83  ? 2602 THR A CG2   1 
ATOM   9011  N  N     . MET A 1 2603 ? 132.558 178.456 171.804 1.00 59.95  ? 2603 MET A N     1 
ATOM   9012  C  CA    . MET A 1 2603 ? 131.170 178.902 171.846 1.00 57.48  ? 2603 MET A CA    1 
ATOM   9013  C  C     . MET A 1 2603 ? 131.012 180.118 172.748 1.00 57.26  ? 2603 MET A C     1 
ATOM   9014  O  O     . MET A 1 2603 ? 130.352 181.097 172.382 1.00 66.63  ? 2603 MET A O     1 
ATOM   9015  C  CB    . MET A 1 2603 ? 130.269 177.762 172.319 1.00 60.23  ? 2603 MET A CB    1 
ATOM   9016  C  CG    . MET A 1 2603 ? 128.882 178.211 172.735 1.00 58.94  ? 2603 MET A CG    1 
ATOM   9017  S  SD    . MET A 1 2603 ? 128.087 177.072 173.880 1.00 79.32  ? 2603 MET A SD    1 
ATOM   9018  C  CE    . MET A 1 2603 ? 129.251 177.101 175.239 1.00 58.86  ? 2603 MET A CE    1 
ATOM   9019  N  N     . THR A 1 2604 ? 131.622 180.076 173.936 1.00 55.72  ? 2604 THR A N     1 
ATOM   9020  C  CA    . THR A 1 2604 ? 131.529 181.206 174.854 1.00 54.40  ? 2604 THR A CA    1 
ATOM   9021  C  C     . THR A 1 2604 ? 132.190 182.447 174.270 1.00 58.47  ? 2604 THR A C     1 
ATOM   9022  O  O     . THR A 1 2604 ? 131.656 183.557 174.387 1.00 66.21  ? 2604 THR A O     1 
ATOM   9023  C  CB    . THR A 1 2604 ? 132.160 180.850 176.200 1.00 45.50  ? 2604 THR A CB    1 
ATOM   9024  O  OG1   . THR A 1 2604 ? 131.519 179.686 176.736 1.00 59.91  ? 2604 THR A OG1   1 
ATOM   9025  C  CG2   . THR A 1 2604 ? 132.001 181.995 177.178 1.00 51.06  ? 2604 THR A CG2   1 
ATOM   9026  N  N     . LEU A 1 2605 ? 133.356 182.284 173.639 1.00 62.34  ? 2605 LEU A N     1 
ATOM   9027  C  CA    . LEU A 1 2605 ? 134.028 183.433 173.044 1.00 49.60  ? 2605 LEU A CA    1 
ATOM   9028  C  C     . LEU A 1 2605 ? 133.195 184.046 171.926 1.00 59.22  ? 2605 LEU A C     1 
ATOM   9029  O  O     . LEU A 1 2605 ? 133.061 185.273 171.845 1.00 73.51  ? 2605 LEU A O     1 
ATOM   9030  C  CB    . LEU A 1 2605 ? 135.405 183.031 172.521 1.00 44.92  ? 2605 LEU A CB    1 
ATOM   9031  C  CG    . LEU A 1 2605 ? 136.078 184.116 171.684 1.00 54.81  ? 2605 LEU A CG    1 
ATOM   9032  C  CD1   . LEU A 1 2605 ? 136.664 185.191 172.580 1.00 58.23  ? 2605 LEU A CD1   1 
ATOM   9033  C  CD2   . LEU A 1 2605 ? 137.143 183.519 170.790 1.00 62.43  ? 2605 LEU A CD2   1 
ATOM   9034  N  N     . PHE A 1 2606 ? 132.623 183.211 171.056 1.00 56.04  ? 2606 PHE A N     1 
ATOM   9035  C  CA    . PHE A 1 2606 ? 131.801 183.735 169.970 1.00 48.34  ? 2606 PHE A CA    1 
ATOM   9036  C  C     . PHE A 1 2606 ? 130.537 184.396 170.504 1.00 56.74  ? 2606 PHE A C     1 
ATOM   9037  O  O     . PHE A 1 2606 ? 130.061 185.385 169.935 1.00 67.84  ? 2606 PHE A O     1 
ATOM   9038  C  CB    . PHE A 1 2606 ? 131.455 182.622 168.983 1.00 46.99  ? 2606 PHE A CB    1 
ATOM   9039  C  CG    . PHE A 1 2606 ? 132.582 182.260 168.059 1.00 48.54  ? 2606 PHE A CG    1 
ATOM   9040  C  CD1   . PHE A 1 2606 ? 133.708 183.060 167.973 1.00 53.79  ? 2606 PHE A CD1   1 
ATOM   9041  C  CD2   . PHE A 1 2606 ? 132.512 181.126 167.271 1.00 59.79  ? 2606 PHE A CD2   1 
ATOM   9042  C  CE1   . PHE A 1 2606 ? 134.745 182.731 167.124 1.00 58.83  ? 2606 PHE A CE1   1 
ATOM   9043  C  CE2   . PHE A 1 2606 ? 133.546 180.793 166.417 1.00 66.96  ? 2606 PHE A CE2   1 
ATOM   9044  C  CZ    . PHE A 1 2606 ? 134.664 181.597 166.344 1.00 59.59  ? 2606 PHE A CZ    1 
ATOM   9045  N  N     . SER A 1 2607 ? 129.976 183.862 171.591 1.00 58.74  ? 2607 SER A N     1 
ATOM   9046  C  CA    . SER A 1 2607 ? 128.824 184.503 172.214 1.00 59.50  ? 2607 SER A CA    1 
ATOM   9047  C  C     . SER A 1 2607 ? 129.194 185.866 172.783 1.00 66.28  ? 2607 SER A C     1 
ATOM   9048  O  O     . SER A 1 2607 ? 128.422 186.825 172.671 1.00 70.62  ? 2607 SER A O     1 
ATOM   9049  C  CB    . SER A 1 2607 ? 128.251 183.602 173.307 1.00 63.28  ? 2607 SER A CB    1 
ATOM   9050  O  OG    . SER A 1 2607 ? 127.081 184.169 173.868 1.00 68.45  ? 2607 SER A OG    1 
ATOM   9051  N  N     . ALA A 1 2608 ? 130.371 185.969 173.403 1.00 69.16  ? 2608 ALA A N     1 
ATOM   9052  C  CA    . ALA A 1 2608 ? 130.820 187.257 173.923 1.00 62.88  ? 2608 ALA A CA    1 
ATOM   9053  C  C     . ALA A 1 2608 ? 131.123 188.233 172.795 1.00 61.87  ? 2608 ALA A C     1 
ATOM   9054  O  O     . ALA A 1 2608 ? 130.839 189.431 172.910 1.00 72.58  ? 2608 ALA A O     1 
ATOM   9055  C  CB    . ALA A 1 2608 ? 132.047 187.067 174.812 1.00 60.00  ? 2608 ALA A CB    1 
ATOM   9056  N  N     . LEU A 1 2609 ? 131.701 187.742 171.697 1.00 56.38  ? 2609 LEU A N     1 
ATOM   9057  C  CA    . LEU A 1 2609 ? 132.015 188.610 170.568 1.00 57.74  ? 2609 LEU A CA    1 
ATOM   9058  C  C     . LEU A 1 2609 ? 130.767 189.102 169.849 1.00 66.58  ? 2609 LEU A C     1 
ATOM   9059  O  O     . LEU A 1 2609 ? 130.824 190.136 169.176 1.00 76.03  ? 2609 LEU A O     1 
ATOM   9060  C  CB    . LEU A 1 2609 ? 132.930 187.883 169.583 1.00 57.74  ? 2609 LEU A CB    1 
ATOM   9061  C  CG    . LEU A 1 2609 ? 134.422 187.913 169.914 1.00 56.23  ? 2609 LEU A CG    1 
ATOM   9062  C  CD1   . LEU A 1 2609 ? 135.178 186.894 169.080 1.00 56.79  ? 2609 LEU A CD1   1 
ATOM   9063  C  CD2   . LEU A 1 2609 ? 134.986 189.306 169.704 1.00 65.66  ? 2609 LEU A CD2   1 
ATOM   9064  N  N     . ARG A 1 2610 ? 129.646 188.388 169.970 1.00 66.24  ? 2610 ARG A N     1 
ATOM   9065  C  CA    . ARG A 1 2610 ? 128.411 188.839 169.339 1.00 69.99  ? 2610 ARG A CA    1 
ATOM   9066  C  C     . ARG A 1 2610 ? 127.879 190.118 169.969 1.00 77.91  ? 2610 ARG A C     1 
ATOM   9067  O  O     . ARG A 1 2610 ? 127.090 190.826 169.335 1.00 85.40  ? 2610 ARG A O     1 
ATOM   9068  C  CB    . ARG A 1 2610 ? 127.349 187.741 169.409 1.00 71.24  ? 2610 ARG A CB    1 
ATOM   9069  C  CG    . ARG A 1 2610 ? 127.245 186.904 168.145 1.00 73.91  ? 2610 ARG A CG    1 
ATOM   9070  C  CD    . ARG A 1 2610 ? 125.935 186.134 168.097 1.00 76.88  ? 2610 ARG A CD    1 
ATOM   9071  N  NE    . ARG A 1 2610 ? 125.942 184.984 168.993 1.00 81.33  ? 2610 ARG A NE    1 
ATOM   9072  C  CZ    . ARG A 1 2610 ? 126.454 183.800 168.687 1.00 81.67  ? 2610 ARG A CZ    1 
ATOM   9073  N  NH1   . ARG A 1 2610 ? 127.016 183.574 167.511 1.00 79.11  ? 2610 ARG A NH1   1 
ATOM   9074  N  NH2   . ARG A 1 2610 ? 126.402 182.820 169.584 1.00 79.42  ? 2610 ARG A NH2   1 
ATOM   9075  N  N     . ALA A 1 2611 ? 128.289 190.429 171.196 1.00 75.95  ? 2611 ALA A N     1 
ATOM   9076  C  CA    . ALA A 1 2611 ? 127.899 191.665 171.858 1.00 79.28  ? 2611 ALA A CA    1 
ATOM   9077  C  C     . ALA A 1 2611 ? 128.815 192.832 171.515 1.00 84.48  ? 2611 ALA A C     1 
ATOM   9078  O  O     . ALA A 1 2611 ? 128.590 193.943 172.004 1.00 86.82  ? 2611 ALA A O     1 
ATOM   9079  C  CB    . ALA A 1 2611 ? 127.867 191.464 173.376 1.00 76.08  ? 2611 ALA A CB    1 
ATOM   9080  N  N     . LEU A 1 2612 ? 129.839 192.606 170.691 1.00 81.60  ? 2612 LEU A N     1 
ATOM   9081  C  CA    . LEU A 1 2612 ? 130.770 193.647 170.256 1.00 77.17  ? 2612 LEU A CA    1 
ATOM   9082  C  C     . LEU A 1 2612 ? 130.708 193.728 168.737 1.00 82.24  ? 2612 LEU A C     1 
ATOM   9083  O  O     . LEU A 1 2612 ? 131.413 192.985 168.036 1.00 85.10  ? 2612 LEU A O     1 
ATOM   9084  C  CB    . LEU A 1 2612 ? 132.188 193.353 170.739 1.00 73.98  ? 2612 LEU A CB    1 
ATOM   9085  C  CG    . LEU A 1 2612 ? 132.411 193.428 172.249 1.00 76.00  ? 2612 LEU A CG    1 
ATOM   9086  C  CD1   . LEU A 1 2612 ? 133.569 192.537 172.665 1.00 76.82  ? 2612 LEU A CD1   1 
ATOM   9087  C  CD2   . LEU A 1 2612 ? 132.655 194.864 172.680 1.00 83.64  ? 2612 LEU A CD2   1 
ATOM   9088  N  N     . PRO A 1 2613 ? 129.875 194.613 168.183 1.00 84.66  ? 2613 PRO A N     1 
ATOM   9089  C  CA    . PRO A 1 2613 ? 129.726 194.665 166.720 1.00 85.29  ? 2613 PRO A CA    1 
ATOM   9090  C  C     . PRO A 1 2613 ? 130.951 195.193 165.993 1.00 83.89  ? 2613 PRO A C     1 
ATOM   9091  O  O     . PRO A 1 2613 ? 131.029 195.044 164.768 1.00 77.16  ? 2613 PRO A O     1 
ATOM   9092  C  CB    . PRO A 1 2613 ? 128.521 195.593 166.524 1.00 84.24  ? 2613 PRO A CB    1 
ATOM   9093  C  CG    . PRO A 1 2613 ? 128.515 196.456 167.740 1.00 82.75  ? 2613 PRO A CG    1 
ATOM   9094  C  CD    . PRO A 1 2613 ? 129.030 195.606 168.868 1.00 83.41  ? 2613 PRO A CD    1 
ATOM   9095  N  N     . ASP A 1 2614 ? 131.903 195.802 166.697 1.00 91.03  ? 2614 ASP A N     1 
ATOM   9096  C  CA    . ASP A 1 2614 ? 133.085 196.378 166.072 1.00 91.11  ? 2614 ASP A CA    1 
ATOM   9097  C  C     . ASP A 1 2614 ? 134.304 195.467 166.160 1.00 88.93  ? 2614 ASP A C     1 
ATOM   9098  O  O     . ASP A 1 2614 ? 135.436 195.950 166.050 1.00 94.39  ? 2614 ASP A O     1 
ATOM   9099  C  CB    . ASP A 1 2614 ? 133.401 197.738 166.697 1.00 93.47  ? 2614 ASP A CB    1 
ATOM   9100  C  CG    . ASP A 1 2614 ? 132.414 198.811 166.284 1.00 98.55  ? 2614 ASP A CG    1 
ATOM   9101  O  OD1   . ASP A 1 2614 ? 131.896 198.740 165.150 1.00 100.54 ? 2614 ASP A OD1   1 
ATOM   9102  O  OD2   . ASP A 1 2614 ? 132.154 199.727 167.094 1.00 98.30  ? 2614 ASP A OD2   1 
ATOM   9103  N  N     . MET A 1 2615 ? 134.101 194.166 166.357 1.00 74.40  ? 2615 MET A N     1 
ATOM   9104  C  CA    . MET A 1 2615 ? 135.194 193.204 166.433 1.00 72.53  ? 2615 MET A CA    1 
ATOM   9105  C  C     . MET A 1 2615 ? 134.934 192.090 165.433 1.00 73.50  ? 2615 MET A C     1 
ATOM   9106  O  O     . MET A 1 2615 ? 133.880 191.448 165.476 1.00 73.22  ? 2615 MET A O     1 
ATOM   9107  C  CB    . MET A 1 2615 ? 135.332 192.630 167.845 1.00 69.34  ? 2615 MET A CB    1 
ATOM   9108  C  CG    . MET A 1 2615 ? 135.381 193.679 168.938 1.00 73.80  ? 2615 MET A CG    1 
ATOM   9109  S  SD    . MET A 1 2615 ? 136.682 193.379 170.145 1.00 81.06  ? 2615 MET A SD    1 
ATOM   9110  C  CE    . MET A 1 2615 ? 136.798 194.994 170.907 1.00 74.58  ? 2615 MET A CE    1 
ATOM   9111  N  N     . GLU A 1 2616 ? 135.890 191.861 164.539 1.00 76.49  ? 2616 GLU A N     1 
ATOM   9112  C  CA    . GLU A 1 2616 ? 135.821 190.769 163.578 1.00 72.88  ? 2616 GLU A CA    1 
ATOM   9113  C  C     . GLU A 1 2616 ? 136.789 189.679 164.018 1.00 77.69  ? 2616 GLU A C     1 
ATOM   9114  O  O     . GLU A 1 2616 ? 137.960 189.960 164.294 1.00 85.37  ? 2616 GLU A O     1 
ATOM   9115  C  CB    . GLU A 1 2616 ? 136.155 191.252 162.167 1.00 70.67  ? 2616 GLU A CB    1 
ATOM   9116  C  CG    . GLU A 1 2616 ? 136.502 190.129 161.205 1.00 80.96  ? 2616 GLU A CG    1 
ATOM   9117  C  CD    . GLU A 1 2616 ? 137.134 190.630 159.925 1.00 88.65  ? 2616 GLU A CD    1 
ATOM   9118  O  OE1   . GLU A 1 2616 ? 138.065 191.457 160.006 1.00 89.06  ? 2616 GLU A OE1   1 
ATOM   9119  O  OE2   . GLU A 1 2616 ? 136.700 190.195 158.837 1.00 86.15  ? 2616 GLU A OE2   1 
ATOM   9120  N  N     . VAL A 1 2617 ? 136.304 188.444 164.081 1.00 57.11  ? 2617 VAL A N     1 
ATOM   9121  C  CA    . VAL A 1 2617 ? 137.081 187.318 164.582 1.00 47.71  ? 2617 VAL A CA    1 
ATOM   9122  C  C     . VAL A 1 2617 ? 137.606 186.512 163.402 1.00 54.50  ? 2617 VAL A C     1 
ATOM   9123  O  O     . VAL A 1 2617 ? 136.864 186.213 162.459 1.00 65.02  ? 2617 VAL A O     1 
ATOM   9124  C  CB    . VAL A 1 2617 ? 136.242 186.442 165.530 1.00 57.17  ? 2617 VAL A CB    1 
ATOM   9125  C  CG1   . VAL A 1 2617 ? 134.936 186.022 164.869 1.00 62.27  ? 2617 VAL A CG1   1 
ATOM   9126  C  CG2   . VAL A 1 2617 ? 137.036 185.225 165.974 1.00 62.20  ? 2617 VAL A CG2   1 
ATOM   9127  N  N     . VAL A 1 2618 ? 138.894 186.182 163.444 1.00 56.81  ? 2618 VAL A N     1 
ATOM   9128  C  CA    . VAL A 1 2618 ? 139.533 185.328 162.450 1.00 59.52  ? 2618 VAL A CA    1 
ATOM   9129  C  C     . VAL A 1 2618 ? 140.087 184.111 163.179 1.00 65.26  ? 2618 VAL A C     1 
ATOM   9130  O  O     . VAL A 1 2618 ? 140.782 184.250 164.193 1.00 77.09  ? 2618 VAL A O     1 
ATOM   9131  C  CB    . VAL A 1 2618 ? 140.635 186.069 161.676 1.00 54.49  ? 2618 VAL A CB    1 
ATOM   9132  C  CG1   . VAL A 1 2618 ? 141.556 186.814 162.628 1.00 62.19  ? 2618 VAL A CG1   1 
ATOM   9133  C  CG2   . VAL A 1 2618 ? 141.427 185.096 160.821 1.00 62.56  ? 2618 VAL A CG2   1 
ATOM   9134  N  N     . GLY A 1 2619 ? 139.765 182.924 162.676 1.00 61.38  ? 2619 GLY A N     1 
ATOM   9135  C  CA    . GLY A 1 2619 ? 140.141 181.701 163.354 1.00 58.91  ? 2619 GLY A CA    1 
ATOM   9136  C  C     . GLY A 1 2619 ? 141.488 181.148 162.943 1.00 65.70  ? 2619 GLY A C     1 
ATOM   9137  O  O     . GLY A 1 2619 ? 141.743 180.925 161.756 1.00 73.58  ? 2619 GLY A O     1 
ATOM   9138  N  N     . LEU A 1 2620 ? 142.360 180.925 163.920 1.00 66.30  ? 2620 LEU A N     1 
ATOM   9139  C  CA    . LEU A 1 2620 ? 143.647 180.284 163.705 1.00 60.59  ? 2620 LEU A CA    1 
ATOM   9140  C  C     . LEU A 1 2620 ? 143.685 178.958 164.450 1.00 63.57  ? 2620 LEU A C     1 
ATOM   9141  O  O     . LEU A 1 2620 ? 143.180 178.851 165.571 1.00 71.81  ? 2620 LEU A O     1 
ATOM   9142  C  CB    . LEU A 1 2620 ? 144.798 181.176 164.168 1.00 63.68  ? 2620 LEU A CB    1 
ATOM   9143  C  CG    . LEU A 1 2620 ? 145.054 182.409 163.308 1.00 66.22  ? 2620 LEU A CG    1 
ATOM   9144  C  CD1   . LEU A 1 2620 ? 145.681 183.507 164.137 1.00 67.13  ? 2620 LEU A CD1   1 
ATOM   9145  C  CD2   . LEU A 1 2620 ? 145.945 182.039 162.142 1.00 68.91  ? 2620 LEU A CD2   1 
ATOM   9146  N  N     . ASN A 1 2621 ? 144.286 177.954 163.823 1.00 62.14  ? 2621 ASN A N     1 
ATOM   9147  C  CA    . ASN A 1 2621 ? 144.302 176.592 164.348 1.00 66.99  ? 2621 ASN A CA    1 
ATOM   9148  C  C     . ASN A 1 2621 ? 145.752 176.130 164.432 1.00 67.78  ? 2621 ASN A C     1 
ATOM   9149  O  O     . ASN A 1 2621 ? 146.315 175.639 163.449 1.00 74.43  ? 2621 ASN A O     1 
ATOM   9150  C  CB    . ASN A 1 2621 ? 143.458 175.679 163.472 1.00 63.11  ? 2621 ASN A CB    1 
ATOM   9151  C  CG    . ASN A 1 2621 ? 141.986 176.018 163.546 1.00 75.28  ? 2621 ASN A CG    1 
ATOM   9152  O  OD1   . ASN A 1 2621 ? 141.385 176.437 162.560 1.00 79.92  ? 2621 ASN A OD1   1 
ATOM   9153  N  ND2   . ASN A 1 2621 ? 141.395 175.834 164.720 1.00 78.05  ? 2621 ASN A ND2   1 
ATOM   9154  N  N     . PHE A 1 2622 ? 146.348 176.292 165.608 1.00 59.53  ? 2622 PHE A N     1 
ATOM   9155  C  CA    . PHE A 1 2622 ? 147.746 175.942 165.800 1.00 55.28  ? 2622 PHE A CA    1 
ATOM   9156  C  C     . PHE A 1 2622 ? 147.927 174.429 165.821 1.00 57.68  ? 2622 PHE A C     1 
ATOM   9157  O  O     . PHE A 1 2622 ? 147.051 173.679 166.258 1.00 67.53  ? 2622 PHE A O     1 
ATOM   9158  C  CB    . PHE A 1 2622 ? 148.273 176.546 167.101 1.00 55.36  ? 2622 PHE A CB    1 
ATOM   9159  C  CG    . PHE A 1 2622 ? 148.598 178.011 167.008 1.00 48.61  ? 2622 PHE A CG    1 
ATOM   9160  C  CD1   . PHE A 1 2622 ? 148.137 178.776 165.953 1.00 56.48  ? 2622 PHE A CD1   1 
ATOM   9161  C  CD2   . PHE A 1 2622 ? 149.365 178.621 167.984 1.00 47.44  ? 2622 PHE A CD2   1 
ATOM   9162  C  CE1   . PHE A 1 2622 ? 148.434 180.118 165.872 1.00 63.02  ? 2622 PHE A CE1   1 
ATOM   9163  C  CE2   . PHE A 1 2622 ? 149.665 179.963 167.908 1.00 51.68  ? 2622 PHE A CE2   1 
ATOM   9164  C  CZ    . PHE A 1 2622 ? 149.200 180.712 166.850 1.00 59.09  ? 2622 PHE A CZ    1 
ATOM   9165  N  N     . SER A 1 2623 ? 149.083 173.986 165.339 1.00 58.94  ? 2623 SER A N     1 
ATOM   9166  C  CA    . SER A 1 2623 ? 149.461 172.582 165.341 1.00 59.79  ? 2623 SER A CA    1 
ATOM   9167  C  C     . SER A 1 2623 ? 150.858 172.454 165.935 1.00 63.47  ? 2623 SER A C     1 
ATOM   9168  O  O     . SER A 1 2623 ? 151.471 173.441 166.350 1.00 79.14  ? 2623 SER A O     1 
ATOM   9169  C  CB    . SER A 1 2623 ? 149.407 171.990 163.928 1.00 60.15  ? 2623 SER A CB    1 
ATOM   9170  O  OG    . SER A 1 2623 ? 150.299 172.666 163.062 1.00 62.56  ? 2623 SER A OG    1 
ATOM   9171  N  N     . SER A 1 2624 ? 151.365 171.221 165.976 1.00 55.41  ? 2624 SER A N     1 
ATOM   9172  C  CA    . SER A 1 2624 ? 152.689 170.995 166.545 1.00 56.49  ? 2624 SER A CA    1 
ATOM   9173  C  C     . SER A 1 2624 ? 153.782 171.631 165.698 1.00 67.28  ? 2624 SER A C     1 
ATOM   9174  O  O     . SER A 1 2624 ? 154.868 171.927 166.208 1.00 79.10  ? 2624 SER A O     1 
ATOM   9175  C  CB    . SER A 1 2624 ? 152.946 169.497 166.703 1.00 64.57  ? 2624 SER A CB    1 
ATOM   9176  O  OG    . SER A 1 2624 ? 154.331 169.210 166.630 1.00 73.36  ? 2624 SER A OG    1 
ATOM   9177  N  N     . ALA A 1 2625 ? 153.520 171.851 164.412 1.00 64.71  ? 2625 ALA A N     1 
ATOM   9178  C  CA    . ALA A 1 2625 ? 154.493 172.442 163.505 1.00 70.03  ? 2625 ALA A CA    1 
ATOM   9179  C  C     . ALA A 1 2625 ? 154.208 173.908 163.209 1.00 62.78  ? 2625 ALA A C     1 
ATOM   9180  O  O     . ALA A 1 2625 ? 154.783 174.461 162.267 1.00 65.78  ? 2625 ALA A O     1 
ATOM   9181  C  CB    . ALA A 1 2625 ? 154.545 171.649 162.198 1.00 69.27  ? 2625 ALA A CB    1 
ATOM   9182  N  N     . THR A 1 2626 ? 153.333 174.544 163.984 1.00 64.66  ? 2626 THR A N     1 
ATOM   9183  C  CA    . THR A 1 2626 ? 152.959 175.925 163.713 1.00 63.25  ? 2626 THR A CA    1 
ATOM   9184  C  C     . THR A 1 2626 ? 154.138 176.858 163.962 1.00 67.62  ? 2626 THR A C     1 
ATOM   9185  O  O     . THR A 1 2626 ? 154.839 176.740 164.971 1.00 74.23  ? 2626 THR A O     1 
ATOM   9186  C  CB    . THR A 1 2626 ? 151.769 176.331 164.581 1.00 65.49  ? 2626 THR A CB    1 
ATOM   9187  O  OG1   . THR A 1 2626 ? 150.658 175.473 164.297 1.00 73.60  ? 2626 THR A OG1   1 
ATOM   9188  C  CG2   . THR A 1 2626 ? 151.367 177.768 164.296 1.00 59.85  ? 2626 THR A CG2   1 
ATOM   9189  N  N     . THR A 1 2627 ? 154.351 177.782 163.038 1.00 67.91  ? 2627 THR A N     1 
ATOM   9190  C  CA    . THR A 1 2627 ? 155.409 178.778 163.091 1.00 64.21  ? 2627 THR A CA    1 
ATOM   9191  C  C     . THR A 1 2627 ? 154.787 180.151 162.921 1.00 68.22  ? 2627 THR A C     1 
ATOM   9192  O  O     . THR A 1 2627 ? 153.636 180.272 162.489 1.00 77.55  ? 2627 THR A O     1 
ATOM   9193  C  CB    . THR A 1 2627 ? 156.453 178.522 161.990 1.00 66.21  ? 2627 THR A CB    1 
ATOM   9194  O  OG1   . THR A 1 2627 ? 155.791 178.338 160.733 1.00 72.54  ? 2627 THR A OG1   1 
ATOM   9195  C  CG2   . THR A 1 2627 ? 157.274 177.285 162.313 1.00 71.37  ? 2627 THR A CG2   1 
ATOM   9196  N  N     . PRO A 1 2628 ? 155.514 181.218 163.270 1.00 61.98  ? 2628 PRO A N     1 
ATOM   9197  C  CA    . PRO A 1 2628 ? 154.985 182.573 163.040 1.00 57.94  ? 2628 PRO A CA    1 
ATOM   9198  C  C     . PRO A 1 2628 ? 154.598 182.848 161.596 1.00 62.70  ? 2628 PRO A C     1 
ATOM   9199  O  O     . PRO A 1 2628 ? 153.942 183.866 161.336 1.00 68.97  ? 2628 PRO A O     1 
ATOM   9200  C  CB    . PRO A 1 2628 ? 156.139 183.480 163.484 1.00 58.59  ? 2628 PRO A CB    1 
ATOM   9201  C  CG    . PRO A 1 2628 ? 156.863 182.681 164.497 1.00 58.01  ? 2628 PRO A CG    1 
ATOM   9202  C  CD    . PRO A 1 2628 ? 156.753 181.244 164.069 1.00 67.29  ? 2628 PRO A CD    1 
ATOM   9203  N  N     . GLU A 1 2629 ? 154.980 181.983 160.653 1.00 71.80  ? 2629 GLU A N     1 
ATOM   9204  C  CA    . GLU A 1 2629 ? 154.576 182.172 159.266 1.00 71.45  ? 2629 GLU A CA    1 
ATOM   9205  C  C     . GLU A 1 2629 ? 153.064 182.105 159.104 1.00 73.24  ? 2629 GLU A C     1 
ATOM   9206  O  O     . GLU A 1 2629 ? 152.509 182.776 158.231 1.00 80.75  ? 2629 GLU A O     1 
ATOM   9207  C  CB    . GLU A 1 2629 ? 155.253 181.131 158.375 1.00 69.71  ? 2629 GLU A CB    1 
ATOM   9208  C  CG    . GLU A 1 2629 ? 156.764 181.068 158.531 1.00 74.37  ? 2629 GLU A CG    1 
ATOM   9209  C  CD    . GLU A 1 2629 ? 157.455 182.341 158.080 1.00 81.90  ? 2629 GLU A CD    1 
ATOM   9210  O  OE1   . GLU A 1 2629 ? 156.886 183.066 157.236 1.00 81.03  ? 2629 GLU A OE1   1 
ATOM   9211  O  OE2   . GLU A 1 2629 ? 158.569 182.618 158.572 1.00 83.61  ? 2629 GLU A OE2   1 
ATOM   9212  N  N     . LEU A 1 2630 ? 152.380 181.309 159.929 1.00 59.89  ? 2630 LEU A N     1 
ATOM   9213  C  CA    . LEU A 1 2630 ? 150.922 181.272 159.869 1.00 60.54  ? 2630 LEU A CA    1 
ATOM   9214  C  C     . LEU A 1 2630 ? 150.324 182.622 160.251 1.00 71.12  ? 2630 LEU A C     1 
ATOM   9215  O  O     . LEU A 1 2630 ? 149.426 183.134 159.567 1.00 82.12  ? 2630 LEU A O     1 
ATOM   9216  C  CB    . LEU A 1 2630 ? 150.394 180.165 160.781 1.00 64.34  ? 2630 LEU A CB    1 
ATOM   9217  C  CG    . LEU A 1 2630 ? 148.885 180.040 161.004 1.00 66.23  ? 2630 LEU A CG    1 
ATOM   9218  C  CD1   . LEU A 1 2630 ? 148.123 180.129 159.691 1.00 71.93  ? 2630 LEU A CD1   1 
ATOM   9219  C  CD2   . LEU A 1 2630 ? 148.566 178.738 161.720 1.00 66.71  ? 2630 LEU A CD2   1 
ATOM   9220  N  N     . LEU A 1 2631 ? 150.821 183.219 161.336 1.00 61.57  ? 2631 LEU A N     1 
ATOM   9221  C  CA    . LEU A 1 2631 ? 150.362 184.547 161.726 1.00 54.90  ? 2631 LEU A CA    1 
ATOM   9222  C  C     . LEU A 1 2631 ? 150.703 185.578 160.659 1.00 59.97  ? 2631 LEU A C     1 
ATOM   9223  O  O     . LEU A 1 2631 ? 149.918 186.498 160.401 1.00 74.49  ? 2631 LEU A O     1 
ATOM   9224  C  CB    . LEU A 1 2631 ? 150.976 184.943 163.069 1.00 67.56  ? 2631 LEU A CB    1 
ATOM   9225  C  CG    . LEU A 1 2631 ? 150.469 184.202 164.306 1.00 64.18  ? 2631 LEU A CG    1 
ATOM   9226  C  CD1   . LEU A 1 2631 ? 151.417 184.404 165.471 1.00 59.47  ? 2631 LEU A CD1   1 
ATOM   9227  C  CD2   . LEU A 1 2631 ? 149.078 184.676 164.670 1.00 62.73  ? 2631 LEU A CD2   1 
ATOM   9228  N  N     . LEU A 1 2632 ? 151.872 185.444 160.031 1.00 59.66  ? 2632 LEU A N     1 
ATOM   9229  C  CA    . LEU A 1 2632 ? 152.249 186.375 158.971 1.00 62.63  ? 2632 LEU A CA    1 
ATOM   9230  C  C     . LEU A 1 2632 ? 151.323 186.250 157.766 1.00 63.88  ? 2632 LEU A C     1 
ATOM   9231  O  O     . LEU A 1 2632 ? 150.952 187.259 157.158 1.00 68.77  ? 2632 LEU A O     1 
ATOM   9232  C  CB    . LEU A 1 2632 ? 153.703 186.145 158.565 1.00 66.33  ? 2632 LEU A CB    1 
ATOM   9233  C  CG    . LEU A 1 2632 ? 154.736 186.498 159.636 1.00 61.08  ? 2632 LEU A CG    1 
ATOM   9234  C  CD1   . LEU A 1 2632 ? 156.147 186.249 159.130 1.00 62.69  ? 2632 LEU A CD1   1 
ATOM   9235  C  CD2   . LEU A 1 2632 ? 154.569 187.939 160.088 1.00 63.82  ? 2632 LEU A CD2   1 
ATOM   9236  N  N     . LYS A 1 2633 ? 150.943 185.024 157.402 1.00 66.13  ? 2633 LYS A N     1 
ATOM   9237  C  CA    . LYS A 1 2633 ? 149.996 184.835 156.306 1.00 69.95  ? 2633 LYS A CA    1 
ATOM   9238  C  C     . LYS A 1 2633 ? 148.636 185.427 156.649 1.00 72.96  ? 2633 LYS A C     1 
ATOM   9239  O  O     . LYS A 1 2633 ? 147.985 186.049 155.799 1.00 77.52  ? 2633 LYS A O     1 
ATOM   9240  C  CB    . LYS A 1 2633 ? 149.861 183.349 155.972 1.00 72.61  ? 2633 LYS A CB    1 
ATOM   9241  C  CG    . LYS A 1 2633 ? 151.130 182.704 155.444 1.00 73.27  ? 2633 LYS A CG    1 
ATOM   9242  C  CD    . LYS A 1 2633 ? 151.386 183.072 153.995 1.00 79.63  ? 2633 LYS A CD    1 
ATOM   9243  C  CE    . LYS A 1 2633 ? 152.448 182.173 153.385 1.00 78.28  ? 2633 LYS A CE    1 
ATOM   9244  N  NZ    . LYS A 1 2633 ? 152.169 180.733 153.642 1.00 77.06  ? 2633 LYS A NZ    1 
ATOM   9245  N  N     . THR A 1 2634 ? 148.187 185.240 157.893 1.00 66.38  ? 2634 THR A N     1 
ATOM   9246  C  CA    . THR A 1 2634 ? 146.922 185.836 158.311 1.00 63.20  ? 2634 THR A CA    1 
ATOM   9247  C  C     . THR A 1 2634 ? 146.985 187.359 158.251 1.00 64.74  ? 2634 THR A C     1 
ATOM   9248  O  O     . THR A 1 2634 ? 146.028 188.011 157.820 1.00 68.91  ? 2634 THR A O     1 
ATOM   9249  C  CB    . THR A 1 2634 ? 146.557 185.361 159.717 1.00 64.30  ? 2634 THR A CB    1 
ATOM   9250  O  OG1   . THR A 1 2634 ? 146.163 183.985 159.661 1.00 62.20  ? 2634 THR A OG1   1 
ATOM   9251  C  CG2   . THR A 1 2634 ? 145.410 186.181 160.284 1.00 65.58  ? 2634 THR A CG2   1 
ATOM   9252  N  N     . PHE A 1 2635 ? 148.109 187.942 158.676 1.00 62.39  ? 2635 PHE A N     1 
ATOM   9253  C  CA    . PHE A 1 2635 ? 148.281 189.389 158.574 1.00 60.48  ? 2635 PHE A CA    1 
ATOM   9254  C  C     . PHE A 1 2635 ? 148.272 189.846 157.122 1.00 66.02  ? 2635 PHE A C     1 
ATOM   9255  O  O     . PHE A 1 2635 ? 147.675 190.877 156.791 1.00 72.40  ? 2635 PHE A O     1 
ATOM   9256  C  CB    . PHE A 1 2635 ? 149.580 189.814 159.256 1.00 66.47  ? 2635 PHE A CB    1 
ATOM   9257  C  CG    . PHE A 1 2635 ? 149.529 189.751 160.752 1.00 63.86  ? 2635 PHE A CG    1 
ATOM   9258  C  CD1   . PHE A 1 2635 ? 148.317 189.780 161.417 1.00 58.53  ? 2635 PHE A CD1   1 
ATOM   9259  C  CD2   . PHE A 1 2635 ? 150.692 189.659 161.493 1.00 63.81  ? 2635 PHE A CD2   1 
ATOM   9260  C  CE1   . PHE A 1 2635 ? 148.268 189.722 162.791 1.00 60.62  ? 2635 PHE A CE1   1 
ATOM   9261  C  CE2   . PHE A 1 2635 ? 150.648 189.600 162.867 1.00 59.92  ? 2635 PHE A CE2   1 
ATOM   9262  C  CZ    . PHE A 1 2635 ? 149.435 189.631 163.518 1.00 59.45  ? 2635 PHE A CZ    1 
ATOM   9263  N  N     . ASP A 1 2636 ? 148.938 189.098 156.242 1.00 81.19  ? 2636 ASP A N     1 
ATOM   9264  C  CA    . ASP A 1 2636 ? 148.952 189.455 154.828 1.00 84.42  ? 2636 ASP A CA    1 
ATOM   9265  C  C     . ASP A 1 2636 ? 147.555 189.408 154.227 1.00 83.57  ? 2636 ASP A C     1 
ATOM   9266  O  O     . ASP A 1 2636 ? 147.211 190.249 153.390 1.00 87.71  ? 2636 ASP A O     1 
ATOM   9267  C  CB    . ASP A 1 2636 ? 149.890 188.523 154.059 1.00 85.85  ? 2636 ASP A CB    1 
ATOM   9268  C  CG    . ASP A 1 2636 ? 151.343 188.950 154.152 1.00 92.70  ? 2636 ASP A CG    1 
ATOM   9269  O  OD1   . ASP A 1 2636 ? 151.845 189.119 155.282 1.00 91.31  ? 2636 ASP A OD1   1 
ATOM   9270  O  OD2   . ASP A 1 2636 ? 151.984 189.113 153.093 1.00 94.12  ? 2636 ASP A OD2   1 
ATOM   9271  N  N     . HIS A 1 2637 ? 146.739 188.437 154.638 1.00 78.14  ? 2637 HIS A N     1 
ATOM   9272  C  CA    . HIS A 1 2637 ? 145.406 188.306 154.061 1.00 78.99  ? 2637 HIS A CA    1 
ATOM   9273  C  C     . HIS A 1 2637 ? 144.440 189.346 154.621 1.00 78.30  ? 2637 HIS A C     1 
ATOM   9274  O  O     . HIS A 1 2637 ? 143.722 190.006 153.862 1.00 77.65  ? 2637 HIS A O     1 
ATOM   9275  C  CB    . HIS A 1 2637 ? 144.866 186.895 154.299 1.00 81.14  ? 2637 HIS A CB    1 
ATOM   9276  C  CG    . HIS A 1 2637 ? 143.598 186.601 153.560 1.00 79.36  ? 2637 HIS A CG    1 
ATOM   9277  N  ND1   . HIS A 1 2637 ? 142.396 187.198 153.874 1.00 82.51  ? 2637 HIS A ND1   1 
ATOM   9278  C  CD2   . HIS A 1 2637 ? 143.346 185.776 152.516 1.00 81.97  ? 2637 HIS A CD2   1 
ATOM   9279  C  CE1   . HIS A 1 2637 ? 141.458 186.753 153.058 1.00 85.25  ? 2637 HIS A CE1   1 
ATOM   9280  N  NE2   . HIS A 1 2637 ? 142.008 185.889 152.224 1.00 89.27  ? 2637 HIS A NE2   1 
ATOM   9281  N  N     . TYR A 1 2638 ? 144.405 189.507 155.944 1.00 73.02  ? 2638 TYR A N     1 
ATOM   9282  C  CA    . TYR A 1 2638 ? 143.394 190.327 156.600 1.00 68.24  ? 2638 TYR A CA    1 
ATOM   9283  C  C     . TYR A 1 2638 ? 143.859 191.739 156.935 1.00 69.15  ? 2638 TYR A C     1 
ATOM   9284  O  O     . TYR A 1 2638 ? 143.021 192.578 157.278 1.00 72.92  ? 2638 TYR A O     1 
ATOM   9285  C  CB    . TYR A 1 2638 ? 142.914 189.644 157.886 1.00 64.54  ? 2638 TYR A CB    1 
ATOM   9286  C  CG    . TYR A 1 2638 ? 142.026 188.444 157.654 1.00 64.74  ? 2638 TYR A CG    1 
ATOM   9287  C  CD1   . TYR A 1 2638 ? 140.651 188.587 157.542 1.00 68.22  ? 2638 TYR A CD1   1 
ATOM   9288  C  CD2   . TYR A 1 2638 ? 142.561 187.169 157.548 1.00 67.08  ? 2638 TYR A CD2   1 
ATOM   9289  C  CE1   . TYR A 1 2638 ? 139.834 187.495 157.332 1.00 68.61  ? 2638 TYR A CE1   1 
ATOM   9290  C  CE2   . TYR A 1 2638 ? 141.752 186.070 157.337 1.00 73.90  ? 2638 TYR A CE2   1 
ATOM   9291  C  CZ    . TYR A 1 2638 ? 140.389 186.239 157.230 1.00 72.55  ? 2638 TYR A CZ    1 
ATOM   9292  O  OH    . TYR A 1 2638 ? 139.579 185.148 157.019 1.00 74.23  ? 2638 TYR A OH    1 
ATOM   9293  N  N     . CYS A 1 2639 ? 145.155 192.025 156.855 1.00 75.57  ? 2639 CYS A N     1 
ATOM   9294  C  CA    . CYS A 1 2639 ? 145.682 193.335 157.210 1.00 69.02  ? 2639 CYS A CA    1 
ATOM   9295  C  C     . CYS A 1 2639 ? 146.556 193.861 156.080 1.00 77.39  ? 2639 CYS A C     1 
ATOM   9296  O  O     . CYS A 1 2639 ? 146.820 193.171 155.092 1.00 82.61  ? 2639 CYS A O     1 
ATOM   9297  C  CB    . CYS A 1 2639 ? 146.484 193.282 158.517 1.00 74.64  ? 2639 CYS A CB    1 
ATOM   9298  S  SG    . CYS A 1 2639 ? 145.671 192.399 159.862 1.00 99.68  ? 2639 CYS A SG    1 
ATOM   9299  N  N     . GLU A 1 2640 ? 147.006 195.104 156.236 1.00 81.87  ? 2640 GLU A N     1 
ATOM   9300  C  CA    . GLU A 1 2640 ? 147.860 195.747 155.250 1.00 83.83  ? 2640 GLU A CA    1 
ATOM   9301  C  C     . GLU A 1 2640 ? 148.882 196.627 155.955 1.00 83.94  ? 2640 GLU A C     1 
ATOM   9302  O  O     . GLU A 1 2640 ? 148.568 197.309 156.934 1.00 83.60  ? 2640 GLU A O     1 
ATOM   9303  C  CB    . GLU A 1 2640 ? 147.043 196.584 154.255 1.00 82.25  ? 2640 GLU A CB    1 
ATOM   9304  C  CG    . GLU A 1 2640 ? 146.188 197.661 154.902 1.00 89.36  ? 2640 GLU A CG    1 
ATOM   9305  C  CD    . GLU A 1 2640 ? 145.332 198.407 153.900 1.00 93.47  ? 2640 GLU A CD    1 
ATOM   9306  O  OE1   . GLU A 1 2640 ? 145.382 198.063 152.700 1.00 92.30  ? 2640 GLU A OE1   1 
ATOM   9307  O  OE2   . GLU A 1 2640 ? 144.609 199.338 154.312 1.00 92.53  ? 2640 GLU A OE2   1 
ATOM   9308  N  N     . TYR A 1 2641 ? 150.112 196.598 155.450 1.00 75.58  ? 2641 TYR A N     1 
ATOM   9309  C  CA    . TYR A 1 2641 ? 151.185 197.450 155.945 1.00 71.39  ? 2641 TYR A CA    1 
ATOM   9310  C  C     . TYR A 1 2641 ? 151.117 198.798 155.243 1.00 78.59  ? 2641 TYR A C     1 
ATOM   9311  O  O     . TYR A 1 2641 ? 151.012 198.857 154.014 1.00 86.90  ? 2641 TYR A O     1 
ATOM   9312  C  CB    . TYR A 1 2641 ? 152.558 196.817 155.709 1.00 72.13  ? 2641 TYR A CB    1 
ATOM   9313  C  CG    . TYR A 1 2641 ? 152.720 195.402 156.214 1.00 74.30  ? 2641 TYR A CG    1 
ATOM   9314  C  CD1   . TYR A 1 2641 ? 152.275 194.319 155.469 1.00 76.75  ? 2641 TYR A CD1   1 
ATOM   9315  C  CD2   . TYR A 1 2641 ? 153.346 195.148 157.426 1.00 73.21  ? 2641 TYR A CD2   1 
ATOM   9316  C  CE1   . TYR A 1 2641 ? 152.433 193.026 155.925 1.00 77.33  ? 2641 TYR A CE1   1 
ATOM   9317  C  CE2   . TYR A 1 2641 ? 153.509 193.858 157.889 1.00 68.91  ? 2641 TYR A CE2   1 
ATOM   9318  C  CZ    . TYR A 1 2641 ? 153.050 192.801 157.135 1.00 73.38  ? 2641 TYR A CZ    1 
ATOM   9319  O  OH    . TYR A 1 2641 ? 153.211 191.514 157.593 1.00 78.99  ? 2641 TYR A OH    1 
ATOM   9320  N  N     . ARG A 1 2642 ? 151.178 199.876 156.020 1.00 85.94  ? 2642 ARG A N     1 
ATOM   9321  C  CA    . ARG A 1 2642 ? 151.224 201.218 155.465 1.00 87.91  ? 2642 ARG A CA    1 
ATOM   9322  C  C     . ARG A 1 2642 ? 152.362 202.002 156.102 1.00 86.87  ? 2642 ARG A C     1 
ATOM   9323  O  O     . ARG A 1 2642 ? 152.616 201.900 157.305 1.00 86.69  ? 2642 ARG A O     1 
ATOM   9324  C  CB    . ARG A 1 2642 ? 149.884 201.954 155.648 1.00 85.19  ? 2642 ARG A CB    1 
ATOM   9325  C  CG    . ARG A 1 2642 ? 149.564 202.397 157.067 1.00 86.34  ? 2642 ARG A CG    1 
ATOM   9326  C  CD    . ARG A 1 2642 ? 148.347 203.310 157.081 1.00 88.84  ? 2642 ARG A CD    1 
ATOM   9327  N  NE    . ARG A 1 2642 ? 148.083 203.868 158.402 1.00 89.62  ? 2642 ARG A NE    1 
ATOM   9328  C  CZ    . ARG A 1 2642 ? 147.328 203.284 159.323 1.00 91.42  ? 2642 ARG A CZ    1 
ATOM   9329  N  NH1   . ARG A 1 2642 ? 146.741 202.120 159.098 1.00 86.59  ? 2642 ARG A NH1   1 
ATOM   9330  N  NH2   . ARG A 1 2642 ? 147.155 203.885 160.496 1.00 89.98  ? 2642 ARG A NH2   1 
ATOM   9331  N  N     . ARG A 1 2643 ? 153.053 202.778 155.272 1.00 101.00 ? 2643 ARG A N     1 
ATOM   9332  C  CA    . ARG A 1 2643 ? 154.152 203.617 155.726 1.00 99.95  ? 2643 ARG A CA    1 
ATOM   9333  C  C     . ARG A 1 2643 ? 153.583 204.878 156.361 1.00 102.76 ? 2643 ARG A C     1 
ATOM   9334  O  O     . ARG A 1 2643 ? 152.748 205.561 155.760 1.00 106.69 ? 2643 ARG A O     1 
ATOM   9335  C  CB    . ARG A 1 2643 ? 155.074 203.978 154.559 1.00 99.03  ? 2643 ARG A CB    1 
ATOM   9336  C  CG    . ARG A 1 2643 ? 156.178 204.973 154.898 1.00 100.89 ? 2643 ARG A CG    1 
ATOM   9337  C  CD    . ARG A 1 2643 ? 156.977 204.561 156.126 1.00 103.18 ? 2643 ARG A CD    1 
ATOM   9338  N  NE    . ARG A 1 2643 ? 157.444 203.182 156.040 1.00 106.27 ? 2643 ARG A NE    1 
ATOM   9339  C  CZ    . ARG A 1 2643 ? 158.715 202.833 155.888 1.00 104.71 ? 2643 ARG A CZ    1 
ATOM   9340  N  NH1   . ARG A 1 2643 ? 159.674 203.740 155.794 1.00 103.81 ? 2643 ARG A NH1   1 
ATOM   9341  N  NH2   . ARG A 1 2643 ? 159.032 201.543 155.826 1.00 99.84  ? 2643 ARG A NH2   1 
ATOM   9342  N  N     . THR A 1 2644 ? 154.024 205.173 157.573 1.00 100.00 ? 2644 THR A N     1 
ATOM   9343  C  CA    . THR A 1 2644 ? 153.636 206.363 158.312 1.00 99.10  ? 2644 THR A CA    1 
ATOM   9344  C  C     . THR A 1 2644 ? 154.895 207.070 158.783 1.00 101.74 ? 2644 THR A C     1 
ATOM   9345  O  O     . THR A 1 2644 ? 155.974 206.469 158.821 1.00 104.48 ? 2644 THR A O     1 
ATOM   9346  C  CB    . THR A 1 2644 ? 152.745 206.020 159.517 1.00 99.78  ? 2644 THR A CB    1 
ATOM   9347  O  OG1   . THR A 1 2644 ? 153.515 205.321 160.503 1.00 102.40 ? 2644 THR A OG1   1 
ATOM   9348  C  CG2   . THR A 1 2644 ? 151.563 205.164 159.090 1.00 98.37  ? 2644 THR A CG2   1 
ATOM   9349  N  N     . PRO A 1 2645 ? 154.798 208.357 159.127 1.00 109.64 ? 2645 PRO A N     1 
ATOM   9350  C  CA    . PRO A 1 2645 ? 155.985 209.060 159.641 1.00 111.25 ? 2645 PRO A CA    1 
ATOM   9351  C  C     . PRO A 1 2645 ? 156.597 208.403 160.865 1.00 111.72 ? 2645 PRO A C     1 
ATOM   9352  O  O     . PRO A 1 2645 ? 157.810 208.523 161.078 1.00 112.13 ? 2645 PRO A O     1 
ATOM   9353  C  CB    . PRO A 1 2645 ? 155.445 210.458 159.961 1.00 110.39 ? 2645 PRO A CB    1 
ATOM   9354  C  CG    . PRO A 1 2645 ? 154.318 210.640 159.011 1.00 112.31 ? 2645 PRO A CG    1 
ATOM   9355  C  CD    . PRO A 1 2645 ? 153.687 209.285 158.849 1.00 108.69 ? 2645 PRO A CD    1 
ATOM   9356  N  N     . ASN A 1 2646 ? 155.800 207.713 161.678 1.00 110.62 ? 2646 ASN A N     1 
ATOM   9357  C  CA    . ASN A 1 2646 ? 156.315 207.022 162.851 1.00 110.23 ? 2646 ASN A CA    1 
ATOM   9358  C  C     . ASN A 1 2646 ? 156.812 205.616 162.546 1.00 111.04 ? 2646 ASN A C     1 
ATOM   9359  O  O     . ASN A 1 2646 ? 157.360 204.963 163.440 1.00 113.34 ? 2646 ASN A O     1 
ATOM   9360  C  CB    . ASN A 1 2646 ? 155.238 206.957 163.937 1.00 109.40 ? 2646 ASN A CB    1 
ATOM   9361  C  CG    . ASN A 1 2646 ? 154.783 208.329 164.379 1.00 112.58 ? 2646 ASN A CG    1 
ATOM   9362  O  OD1   . ASN A 1 2646 ? 154.810 209.283 163.602 1.00 115.16 ? 2646 ASN A OD1   1 
ATOM   9363  N  ND2   . ASN A 1 2646 ? 154.366 208.440 165.634 1.00 112.76 ? 2646 ASN A ND2   1 
ATOM   9364  N  N     . GLY A 1 2647 ? 156.636 205.136 161.323 1.00 92.39  ? 2647 GLY A N     1 
ATOM   9365  C  CA    . GLY A 1 2647 ? 157.091 203.823 160.935 1.00 89.61  ? 2647 GLY A CA    1 
ATOM   9366  C  C     . GLY A 1 2647 ? 155.973 203.055 160.267 1.00 90.48  ? 2647 GLY A C     1 
ATOM   9367  O  O     . GLY A 1 2647 ? 154.915 203.605 159.970 1.00 96.85  ? 2647 GLY A O     1 
ATOM   9368  N  N     . VAL A 1 2648 ? 156.217 201.771 160.035 1.00 71.92  ? 2648 VAL A N     1 
ATOM   9369  C  CA    . VAL A 1 2648 ? 155.236 200.896 159.407 1.00 72.47  ? 2648 VAL A CA    1 
ATOM   9370  C  C     . VAL A 1 2648 ? 154.188 200.516 160.440 1.00 75.47  ? 2648 VAL A C     1 
ATOM   9371  O  O     . VAL A 1 2648 ? 154.523 200.113 161.559 1.00 78.52  ? 2648 VAL A O     1 
ATOM   9372  C  CB    . VAL A 1 2648 ? 155.908 199.644 158.821 1.00 69.48  ? 2648 VAL A CB    1 
ATOM   9373  C  CG1   . VAL A 1 2648 ? 154.860 198.686 158.282 1.00 75.42  ? 2648 VAL A CG1   1 
ATOM   9374  C  CG2   . VAL A 1 2648 ? 156.875 200.034 157.730 1.00 73.32  ? 2648 VAL A CG2   1 
ATOM   9375  N  N     . VAL A 1 2649 ? 152.920 200.651 160.069 1.00 64.12  ? 2649 VAL A N     1 
ATOM   9376  C  CA    . VAL A 1 2649 ? 151.802 200.286 160.928 1.00 61.30  ? 2649 VAL A CA    1 
ATOM   9377  C  C     . VAL A 1 2649 ? 150.957 199.259 160.191 1.00 63.87  ? 2649 VAL A C     1 
ATOM   9378  O  O     . VAL A 1 2649 ? 150.551 199.489 159.046 1.00 73.45  ? 2649 VAL A O     1 
ATOM   9379  C  CB    . VAL A 1 2649 ? 150.961 201.515 161.315 1.00 60.69  ? 2649 VAL A CB    1 
ATOM   9380  C  CG1   . VAL A 1 2649 ? 149.698 201.085 162.024 1.00 62.94  ? 2649 VAL A CG1   1 
ATOM   9381  C  CG2   . VAL A 1 2649 ? 151.773 202.454 162.187 1.00 66.69  ? 2649 VAL A CG2   1 
ATOM   9382  N  N     . LEU A 1 2650 ? 150.696 198.131 160.844 1.00 56.55  ? 2650 LEU A N     1 
ATOM   9383  C  CA    . LEU A 1 2650 ? 149.875 197.069 160.277 1.00 59.22  ? 2650 LEU A CA    1 
ATOM   9384  C  C     . LEU A 1 2650 ? 148.475 197.166 160.868 1.00 66.12  ? 2650 LEU A C     1 
ATOM   9385  O  O     . LEU A 1 2650 ? 148.298 197.022 162.082 1.00 67.97  ? 2650 LEU A O     1 
ATOM   9386  C  CB    . LEU A 1 2650 ? 150.486 195.697 160.556 1.00 53.53  ? 2650 LEU A CB    1 
ATOM   9387  C  CG    . LEU A 1 2650 ? 149.649 194.499 160.114 1.00 57.79  ? 2650 LEU A CG    1 
ATOM   9388  C  CD1   . LEU A 1 2650 ? 150.085 194.030 158.737 1.00 63.05  ? 2650 LEU A CD1   1 
ATOM   9389  C  CD2   . LEU A 1 2650 ? 149.754 193.372 161.121 1.00 63.97  ? 2650 LEU A CD2   1 
ATOM   9390  N  N     . ALA A 1 2651 ? 147.490 197.410 160.011 1.00 74.67  ? 2651 ALA A N     1 
ATOM   9391  C  CA    . ALA A 1 2651 ? 146.111 197.597 160.427 1.00 68.99  ? 2651 ALA A CA    1 
ATOM   9392  C  C     . ALA A 1 2651 ? 145.203 196.751 159.550 1.00 72.21  ? 2651 ALA A C     1 
ATOM   9393  O  O     . ALA A 1 2651 ? 145.547 196.458 158.398 1.00 75.16  ? 2651 ALA A O     1 
ATOM   9394  C  CB    . ALA A 1 2651 ? 145.692 199.073 160.335 1.00 70.56  ? 2651 ALA A CB    1 
ATOM   9395  N  N     . PRO A 1 2652 ? 144.045 196.340 160.066 1.00 65.98  ? 2652 PRO A N     1 
ATOM   9396  C  CA    . PRO A 1 2652 ? 143.105 195.575 159.241 1.00 70.88  ? 2652 PRO A CA    1 
ATOM   9397  C  C     . PRO A 1 2652 ? 142.605 196.397 158.064 1.00 76.45  ? 2652 PRO A C     1 
ATOM   9398  O  O     . PRO A 1 2652 ? 142.530 197.626 158.122 1.00 74.80  ? 2652 PRO A O     1 
ATOM   9399  C  CB    . PRO A 1 2652 ? 141.968 195.242 160.214 1.00 63.92  ? 2652 PRO A CB    1 
ATOM   9400  C  CG    . PRO A 1 2652 ? 142.592 195.324 161.562 1.00 66.67  ? 2652 PRO A CG    1 
ATOM   9401  C  CD    . PRO A 1 2652 ? 143.605 196.422 161.468 1.00 68.12  ? 2652 PRO A CD    1 
ATOM   9402  N  N     . VAL A 1 2653 ? 142.270 195.696 156.978 1.00 81.28  ? 2653 VAL A N     1 
ATOM   9403  C  CA    . VAL A 1 2653 ? 141.785 196.370 155.777 1.00 77.52  ? 2653 VAL A CA    1 
ATOM   9404  C  C     . VAL A 1 2653 ? 140.481 197.101 156.067 1.00 82.82  ? 2653 VAL A C     1 
ATOM   9405  O  O     . VAL A 1 2653 ? 140.278 198.239 155.627 1.00 85.41  ? 2653 VAL A O     1 
ATOM   9406  C  CB    . VAL A 1 2653 ? 141.627 195.362 154.625 1.00 77.40  ? 2653 VAL A CB    1 
ATOM   9407  C  CG1   . VAL A 1 2653 ? 141.487 196.093 153.300 1.00 80.23  ? 2653 VAL A CG1   1 
ATOM   9408  C  CG2   . VAL A 1 2653 ? 142.808 194.408 154.590 1.00 83.59  ? 2653 VAL A CG2   1 
ATOM   9409  N  N     . GLN A 1 2654 ? 139.576 196.461 156.803 1.00 86.87  ? 2654 GLN A N     1 
ATOM   9410  C  CA    . GLN A 1 2654 ? 138.332 197.110 157.192 1.00 86.51  ? 2654 GLN A CA    1 
ATOM   9411  C  C     . GLN A 1 2654 ? 138.619 198.255 158.154 1.00 82.42  ? 2654 GLN A C     1 
ATOM   9412  O  O     . GLN A 1 2654 ? 139.445 198.125 159.063 1.00 81.04  ? 2654 GLN A O     1 
ATOM   9413  C  CB    . GLN A 1 2654 ? 137.388 196.099 157.839 1.00 82.80  ? 2654 GLN A CB    1 
ATOM   9414  C  CG    . GLN A 1 2654 ? 137.163 194.845 157.016 1.00 80.64  ? 2654 GLN A CG    1 
ATOM   9415  C  CD    . GLN A 1 2654 ? 138.012 193.684 157.492 1.00 86.15  ? 2654 GLN A CD    1 
ATOM   9416  O  OE1   . GLN A 1 2654 ? 138.654 193.760 158.539 1.00 88.25  ? 2654 GLN A OE1   1 
ATOM   9417  N  NE2   . GLN A 1 2654 ? 138.019 192.600 156.725 1.00 85.25  ? 2654 GLN A NE2   1 
ATOM   9418  N  N     . LEU A 1 2655 ? 137.937 199.378 157.954 1.00 77.25  ? 2655 LEU A N     1 
ATOM   9419  C  CA    . LEU A 1 2655 ? 138.133 200.556 158.786 1.00 80.59  ? 2655 LEU A CA    1 
ATOM   9420  C  C     . LEU A 1 2655 ? 137.193 200.524 159.983 1.00 81.94  ? 2655 LEU A C     1 
ATOM   9421  O  O     . LEU A 1 2655 ? 136.002 200.229 159.848 1.00 81.24  ? 2655 LEU A O     1 
ATOM   9422  C  CB    . LEU A 1 2655 ? 137.904 201.833 157.976 1.00 84.05  ? 2655 LEU A CB    1 
ATOM   9423  C  CG    . LEU A 1 2655 ? 139.141 202.497 157.369 1.00 81.89  ? 2655 LEU A CG    1 
ATOM   9424  C  CD1   . LEU A 1 2655 ? 140.141 202.859 158.457 1.00 78.44  ? 2655 LEU A CD1   1 
ATOM   9425  C  CD2   . LEU A 1 2655 ? 139.783 201.604 156.319 1.00 77.83  ? 2655 LEU A CD2   1 
ATOM   9426  N  N     . GLY A 1 2656 ? 137.739 200.831 161.158 1.00 79.69  ? 2656 GLY A N     1 
ATOM   9427  C  CA    . GLY A 1 2656 ? 136.947 200.889 162.369 1.00 78.38  ? 2656 GLY A CA    1 
ATOM   9428  C  C     . GLY A 1 2656 ? 136.669 199.560 163.029 1.00 79.63  ? 2656 GLY A C     1 
ATOM   9429  O  O     . GLY A 1 2656 ? 135.943 199.525 164.028 1.00 78.78  ? 2656 GLY A O     1 
ATOM   9430  N  N     . LYS A 1 2657 ? 137.221 198.466 162.513 1.00 81.70  ? 2657 LYS A N     1 
ATOM   9431  C  CA    . LYS A 1 2657 ? 136.993 197.136 163.057 1.00 79.36  ? 2657 LYS A CA    1 
ATOM   9432  C  C     . LYS A 1 2657 ? 138.266 196.613 163.706 1.00 71.85  ? 2657 LYS A C     1 
ATOM   9433  O  O     . LYS A 1 2657 ? 139.373 196.870 163.223 1.00 76.56  ? 2657 LYS A O     1 
ATOM   9434  C  CB    . LYS A 1 2657 ? 136.530 196.167 161.967 1.00 78.04  ? 2657 LYS A CB    1 
ATOM   9435  C  CG    . LYS A 1 2657 ? 135.145 196.462 161.419 1.00 79.10  ? 2657 LYS A CG    1 
ATOM   9436  C  CD    . LYS A 1 2657 ? 134.093 195.598 162.092 1.00 82.39  ? 2657 LYS A CD    1 
ATOM   9437  C  CE    . LYS A 1 2657 ? 132.703 195.928 161.578 1.00 83.61  ? 2657 LYS A CE    1 
ATOM   9438  N  NZ    . LYS A 1 2657 ? 132.354 197.355 161.816 1.00 81.73  ? 2657 LYS A NZ    1 
ATOM   9439  N  N     . TRP A 1 2658 ? 138.101 195.877 164.800 1.00 54.55  ? 2658 TRP A N     1 
ATOM   9440  C  CA    . TRP A 1 2658 ? 139.213 195.288 165.531 1.00 55.90  ? 2658 TRP A CA    1 
ATOM   9441  C  C     . TRP A 1 2658 ? 139.336 193.817 165.160 1.00 62.34  ? 2658 TRP A C     1 
ATOM   9442  O  O     . TRP A 1 2658 ? 138.373 193.057 165.296 1.00 72.90  ? 2658 TRP A O     1 
ATOM   9443  C  CB    . TRP A 1 2658 ? 139.011 195.434 167.039 1.00 57.55  ? 2658 TRP A CB    1 
ATOM   9444  C  CG    . TRP A 1 2658 ? 139.477 196.741 167.587 1.00 60.48  ? 2658 TRP A CG    1 
ATOM   9445  C  CD1   . TRP A 1 2658 ? 138.840 197.942 167.490 1.00 61.48  ? 2658 TRP A CD1   1 
ATOM   9446  C  CD2   . TRP A 1 2658 ? 140.676 196.981 168.330 1.00 61.82  ? 2658 TRP A CD2   1 
ATOM   9447  N  NE1   . TRP A 1 2658 ? 139.572 198.918 168.121 1.00 62.71  ? 2658 TRP A NE1   1 
ATOM   9448  C  CE2   . TRP A 1 2658 ? 140.704 198.353 168.646 1.00 64.05  ? 2658 TRP A CE2   1 
ATOM   9449  C  CE3   . TRP A 1 2658 ? 141.730 196.170 168.758 1.00 56.74  ? 2658 TRP A CE3   1 
ATOM   9450  C  CZ2   . TRP A 1 2658 ? 141.743 198.931 169.368 1.00 60.70  ? 2658 TRP A CZ2   1 
ATOM   9451  C  CZ3   . TRP A 1 2658 ? 142.761 196.745 169.474 1.00 62.28  ? 2658 TRP A CZ3   1 
ATOM   9452  C  CH2   . TRP A 1 2658 ? 142.760 198.112 169.772 1.00 60.98  ? 2658 TRP A CH2   1 
ATOM   9453  N  N     . LEU A 1 2659 ? 140.517 193.420 164.697 1.00 52.66  ? 2659 LEU A N     1 
ATOM   9454  C  CA    . LEU A 1 2659 ? 140.758 192.039 164.306 1.00 50.11  ? 2659 LEU A CA    1 
ATOM   9455  C  C     . LEU A 1 2659 ? 141.123 191.217 165.534 1.00 53.20  ? 2659 LEU A C     1 
ATOM   9456  O  O     . LEU A 1 2659 ? 142.083 191.537 166.241 1.00 66.10  ? 2659 LEU A O     1 
ATOM   9457  C  CB    . LEU A 1 2659 ? 141.869 191.955 163.260 1.00 54.27  ? 2659 LEU A CB    1 
ATOM   9458  C  CG    . LEU A 1 2659 ? 141.945 190.634 162.495 1.00 50.00  ? 2659 LEU A CG    1 
ATOM   9459  C  CD1   . LEU A 1 2659 ? 140.761 190.498 161.557 1.00 50.29  ? 2659 LEU A CD1   1 
ATOM   9460  C  CD2   . LEU A 1 2659 ? 143.248 190.532 161.727 1.00 55.08  ? 2659 LEU A CD2   1 
ATOM   9461  N  N     . VAL A 1 2660 ? 140.357 190.161 165.781 1.00 45.97  ? 2660 VAL A N     1 
ATOM   9462  C  CA    . VAL A 1 2660 ? 140.556 189.283 166.927 1.00 41.24  ? 2660 VAL A CA    1 
ATOM   9463  C  C     . VAL A 1 2660 ? 141.109 187.966 166.404 1.00 47.07  ? 2660 VAL A C     1 
ATOM   9464  O  O     . VAL A 1 2660 ? 140.358 187.125 165.894 1.00 60.13  ? 2660 VAL A O     1 
ATOM   9465  C  CB    . VAL A 1 2660 ? 139.256 189.069 167.712 1.00 45.17  ? 2660 VAL A CB    1 
ATOM   9466  C  CG1   . VAL A 1 2660 ? 139.511 188.214 168.934 1.00 48.43  ? 2660 VAL A CG1   1 
ATOM   9467  C  CG2   . VAL A 1 2660 ? 138.657 190.405 168.112 1.00 57.83  ? 2660 VAL A CG2   1 
ATOM   9468  N  N     . LEU A 1 2661 ? 142.419 187.780 166.532 1.00 43.43  ? 2661 LEU A N     1 
ATOM   9469  C  CA    . LEU A 1 2661 ? 143.076 186.561 166.067 1.00 47.82  ? 2661 LEU A CA    1 
ATOM   9470  C  C     . LEU A 1 2661 ? 142.840 185.472 167.102 1.00 51.96  ? 2661 LEU A C     1 
ATOM   9471  O  O     . LEU A 1 2661 ? 143.394 185.513 168.203 1.00 67.63  ? 2661 LEU A O     1 
ATOM   9472  C  CB    . LEU A 1 2661 ? 144.563 186.805 165.840 1.00 54.56  ? 2661 LEU A CB    1 
ATOM   9473  C  CG    . LEU A 1 2661 ? 144.942 187.456 164.510 1.00 48.64  ? 2661 LEU A CG    1 
ATOM   9474  C  CD1   . LEU A 1 2661 ? 144.835 188.963 164.609 1.00 52.33  ? 2661 LEU A CD1   1 
ATOM   9475  C  CD2   . LEU A 1 2661 ? 146.342 187.054 164.097 1.00 52.81  ? 2661 LEU A CD2   1 
ATOM   9476  N  N     . PHE A 1 2662 ? 142.011 184.493 166.754 1.00 45.58  ? 2662 PHE A N     1 
ATOM   9477  C  CA    . PHE A 1 2662 ? 141.625 183.433 167.682 1.00 45.72  ? 2662 PHE A CA    1 
ATOM   9478  C  C     . PHE A 1 2662 ? 142.498 182.212 167.423 1.00 53.70  ? 2662 PHE A C     1 
ATOM   9479  O  O     . PHE A 1 2662 ? 142.268 181.458 166.475 1.00 67.34  ? 2662 PHE A O     1 
ATOM   9480  C  CB    . PHE A 1 2662 ? 140.144 183.106 167.532 1.00 50.08  ? 2662 PHE A CB    1 
ATOM   9481  C  CG    . PHE A 1 2662 ? 139.689 181.952 168.373 1.00 55.29  ? 2662 PHE A CG    1 
ATOM   9482  C  CD1   . PHE A 1 2662 ? 140.002 181.893 169.718 1.00 60.63  ? 2662 PHE A CD1   1 
ATOM   9483  C  CD2   . PHE A 1 2662 ? 138.943 180.927 167.819 1.00 55.61  ? 2662 PHE A CD2   1 
ATOM   9484  C  CE1   . PHE A 1 2662 ? 139.581 180.834 170.496 1.00 55.03  ? 2662 PHE A CE1   1 
ATOM   9485  C  CE2   . PHE A 1 2662 ? 138.521 179.865 168.591 1.00 55.02  ? 2662 PHE A CE2   1 
ATOM   9486  C  CZ    . PHE A 1 2662 ? 138.841 179.819 169.932 1.00 53.96  ? 2662 PHE A CZ    1 
ATOM   9487  N  N     . CYS A 1 2663 ? 143.505 182.015 168.270 1.00 47.60  ? 2663 CYS A N     1 
ATOM   9488  C  CA    . CYS A 1 2663 ? 144.368 180.844 168.194 1.00 49.44  ? 2663 CYS A CA    1 
ATOM   9489  C  C     . CYS A 1 2663 ? 143.766 179.723 169.029 1.00 61.46  ? 2663 CYS A C     1 
ATOM   9490  O  O     . CYS A 1 2663 ? 143.580 179.874 170.240 1.00 74.20  ? 2663 CYS A O     1 
ATOM   9491  C  CB    . CYS A 1 2663 ? 145.776 181.181 168.683 1.00 59.55  ? 2663 CYS A CB    1 
ATOM   9492  S  SG    . CYS A 1 2663 ? 146.446 182.716 168.004 1.00 79.31  ? 2663 CYS A SG    1 
ATOM   9493  N  N     . ASP A 1 2664 ? 143.466 178.598 168.380 1.00 56.70  ? 2664 ASP A N     1 
ATOM   9494  C  CA    . ASP A 1 2664 ? 142.667 177.550 169.000 1.00 57.86  ? 2664 ASP A CA    1 
ATOM   9495  C  C     . ASP A 1 2664 ? 143.485 176.529 169.779 1.00 58.75  ? 2664 ASP A C     1 
ATOM   9496  O  O     . ASP A 1 2664 ? 142.928 175.847 170.647 1.00 71.61  ? 2664 ASP A O     1 
ATOM   9497  C  CB    . ASP A 1 2664 ? 141.845 176.821 167.933 1.00 62.86  ? 2664 ASP A CB    1 
ATOM   9498  C  CG    . ASP A 1 2664 ? 140.600 176.171 168.499 1.00 74.12  ? 2664 ASP A CG    1 
ATOM   9499  O  OD1   . ASP A 1 2664 ? 140.287 176.411 169.683 1.00 72.89  ? 2664 ASP A OD1   1 
ATOM   9500  O  OD2   . ASP A 1 2664 ? 139.932 175.419 167.758 1.00 73.87  ? 2664 ASP A OD2   1 
ATOM   9501  N  N     . GLU A 1 2665 ? 144.775 176.390 169.488 1.00 61.81  ? 2665 GLU A N     1 
ATOM   9502  C  CA    . GLU A 1 2665 ? 145.629 175.399 170.143 1.00 66.59  ? 2665 GLU A CA    1 
ATOM   9503  C  C     . GLU A 1 2665 ? 146.956 176.037 170.539 1.00 75.14  ? 2665 GLU A C     1 
ATOM   9504  O  O     . GLU A 1 2665 ? 148.035 175.541 170.215 1.00 78.69  ? 2665 GLU A O     1 
ATOM   9505  C  CB    . GLU A 1 2665 ? 145.838 174.179 169.251 1.00 68.68  ? 2665 GLU A CB    1 
ATOM   9506  C  CG    . GLU A 1 2665 ? 144.555 173.434 168.911 1.00 73.09  ? 2665 GLU A CG    1 
ATOM   9507  C  CD    . GLU A 1 2665 ? 144.024 172.611 170.071 1.00 75.83  ? 2665 GLU A CD    1 
ATOM   9508  O  OE1   . GLU A 1 2665 ? 144.691 172.557 171.125 1.00 73.99  ? 2665 GLU A OE1   1 
ATOM   9509  O  OE2   . GLU A 1 2665 ? 142.934 172.019 169.930 1.00 72.91  ? 2665 GLU A OE2   1 
ATOM   9510  N  N     . ILE A 1 2666 ? 146.875 177.168 171.245 1.00 62.61  ? 2666 ILE A N     1 
ATOM   9511  C  CA    . ILE A 1 2666 ? 148.028 178.044 171.434 1.00 57.17  ? 2666 ILE A CA    1 
ATOM   9512  C  C     . ILE A 1 2666 ? 149.196 177.338 172.117 1.00 61.43  ? 2666 ILE A C     1 
ATOM   9513  O  O     . ILE A 1 2666 ? 150.355 177.717 171.912 1.00 73.38  ? 2666 ILE A O     1 
ATOM   9514  C  CB    . ILE A 1 2666 ? 147.596 179.310 172.204 1.00 55.05  ? 2666 ILE A CB    1 
ATOM   9515  C  CG1   . ILE A 1 2666 ? 148.461 180.503 171.796 1.00 63.71  ? 2666 ILE A CG1   1 
ATOM   9516  C  CG2   . ILE A 1 2666 ? 147.647 179.084 173.708 1.00 57.37  ? 2666 ILE A CG2   1 
ATOM   9517  C  CD1   . ILE A 1 2666 ? 148.255 181.725 172.657 1.00 67.56  ? 2666 ILE A CD1   1 
ATOM   9518  N  N     . ASN A 1 2667 ? 148.934 176.310 172.924 1.00 51.31  ? 2667 ASN A N     1 
ATOM   9519  C  CA    . ASN A 1 2667 ? 150.002 175.630 173.648 1.00 53.85  ? 2667 ASN A CA    1 
ATOM   9520  C  C     . ASN A 1 2667 ? 150.461 174.344 172.970 1.00 59.43  ? 2667 ASN A C     1 
ATOM   9521  O  O     . ASN A 1 2667 ? 151.305 173.633 173.523 1.00 65.87  ? 2667 ASN A O     1 
ATOM   9522  C  CB    . ASN A 1 2667 ? 149.574 175.337 175.088 1.00 56.73  ? 2667 ASN A CB    1 
ATOM   9523  C  CG    . ASN A 1 2667 ? 148.341 174.464 175.170 1.00 64.36  ? 2667 ASN A CG    1 
ATOM   9524  O  OD1   . ASN A 1 2667 ? 147.822 173.998 174.157 1.00 71.02  ? 2667 ASN A OD1   1 
ATOM   9525  N  ND2   . ASN A 1 2667 ? 147.866 174.234 176.387 1.00 63.35  ? 2667 ASN A ND2   1 
ATOM   9526  N  N     . LEU A 1 2668 ? 149.929 174.031 171.795 1.00 60.50  ? 2668 LEU A N     1 
ATOM   9527  C  CA    . LEU A 1 2668 ? 150.307 172.831 171.054 1.00 61.09  ? 2668 LEU A CA    1 
ATOM   9528  C  C     . LEU A 1 2668 ? 151.652 172.933 170.334 1.00 60.56  ? 2668 LEU A C     1 
ATOM   9529  O  O     . LEU A 1 2668 ? 152.383 171.935 170.302 1.00 66.67  ? 2668 LEU A O     1 
ATOM   9530  C  CB    . LEU A 1 2668 ? 149.216 172.467 170.045 1.00 58.94  ? 2668 LEU A CB    1 
ATOM   9531  C  CG    . LEU A 1 2668 ? 148.361 171.261 170.427 1.00 55.04  ? 2668 LEU A CG    1 
ATOM   9532  C  CD1   . LEU A 1 2668 ? 147.377 170.932 169.324 1.00 64.54  ? 2668 LEU A CD1   1 
ATOM   9533  C  CD2   . LEU A 1 2668 ? 149.248 170.068 170.717 1.00 58.21  ? 2668 LEU A CD2   1 
ATOM   9534  N  N     . PRO A 1 2669 ? 152.014 174.094 169.712 1.00 49.69  ? 2669 PRO A N     1 
ATOM   9535  C  CA    . PRO A 1 2669 ? 153.281 174.168 168.963 1.00 51.84  ? 2669 PRO A CA    1 
ATOM   9536  C  C     . PRO A 1 2669 ? 154.488 173.555 169.657 1.00 65.00  ? 2669 PRO A C     1 
ATOM   9537  O  O     . PRO A 1 2669 ? 154.611 173.600 170.884 1.00 67.27  ? 2669 PRO A O     1 
ATOM   9538  C  CB    . PRO A 1 2669 ? 153.465 175.675 168.769 1.00 49.06  ? 2669 PRO A CB    1 
ATOM   9539  C  CG    . PRO A 1 2669 ? 152.086 176.169 168.614 1.00 49.41  ? 2669 PRO A CG    1 
ATOM   9540  C  CD    . PRO A 1 2669 ? 151.205 175.306 169.481 1.00 48.93  ? 2669 PRO A CD    1 
ATOM   9541  N  N     . ASP A 1 2670 ? 155.382 172.978 168.855 1.00 79.22  ? 2670 ASP A N     1 
ATOM   9542  C  CA    . ASP A 1 2670 ? 156.489 172.192 169.382 1.00 72.69  ? 2670 ASP A CA    1 
ATOM   9543  C  C     . ASP A 1 2670 ? 157.423 173.046 170.226 1.00 77.33  ? 2670 ASP A C     1 
ATOM   9544  O  O     . ASP A 1 2670 ? 157.769 174.170 169.854 1.00 84.27  ? 2670 ASP A O     1 
ATOM   9545  C  CB    . ASP A 1 2670 ? 157.268 171.550 168.234 1.00 79.47  ? 2670 ASP A CB    1 
ATOM   9546  C  CG    . ASP A 1 2670 ? 157.082 170.049 168.170 1.00 83.70  ? 2670 ASP A CG    1 
ATOM   9547  O  OD1   . ASP A 1 2670 ? 156.259 169.517 168.944 1.00 80.10  ? 2670 ASP A OD1   1 
ATOM   9548  O  OD2   . ASP A 1 2670 ? 157.758 169.401 167.344 1.00 84.51  ? 2670 ASP A OD2   1 
ATOM   9549  N  N     . MET A 1 2671 ? 157.830 172.501 171.367 1.00 78.17  ? 2671 MET A N     1 
ATOM   9550  C  CA    . MET A 1 2671 ? 158.834 173.114 172.223 1.00 76.74  ? 2671 MET A CA    1 
ATOM   9551  C  C     . MET A 1 2671 ? 160.190 172.512 171.887 1.00 79.19  ? 2671 MET A C     1 
ATOM   9552  O  O     . MET A 1 2671 ? 160.350 171.287 171.900 1.00 84.97  ? 2671 MET A O     1 
ATOM   9553  C  CB    . MET A 1 2671 ? 158.505 172.892 173.699 1.00 76.32  ? 2671 MET A CB    1 
ATOM   9554  C  CG    . MET A 1 2671 ? 158.844 174.063 174.604 1.00 75.89  ? 2671 MET A CG    1 
ATOM   9555  S  SD    . MET A 1 2671 ? 157.596 174.305 175.883 1.00 95.90  ? 2671 MET A SD    1 
ATOM   9556  C  CE    . MET A 1 2671 ? 158.280 175.691 176.785 1.00 82.71  ? 2671 MET A CE    1 
ATOM   9557  N  N     . ASP A 1 2672 ? 161.160 173.370 171.582 1.00 87.71  ? 2672 ASP A N     1 
ATOM   9558  C  CA    . ASP A 1 2672 ? 162.489 172.898 171.232 1.00 89.71  ? 2672 ASP A CA    1 
ATOM   9559  C  C     . ASP A 1 2672 ? 163.161 172.266 172.450 1.00 94.76  ? 2672 ASP A C     1 
ATOM   9560  O  O     . ASP A 1 2672 ? 162.615 172.235 173.556 1.00 97.35  ? 2672 ASP A O     1 
ATOM   9561  C  CB    . ASP A 1 2672 ? 163.332 174.044 170.678 1.00 87.73  ? 2672 ASP A CB    1 
ATOM   9562  C  CG    . ASP A 1 2672 ? 162.611 174.831 169.605 1.00 94.42  ? 2672 ASP A CG    1 
ATOM   9563  O  OD1   . ASP A 1 2672 ? 162.899 176.036 169.455 1.00 94.70  ? 2672 ASP A OD1   1 
ATOM   9564  O  OD2   . ASP A 1 2672 ? 161.756 174.245 168.909 1.00 96.24  ? 2672 ASP A OD2   1 
ATOM   9565  N  N     . LYS A 1 2673 ? 164.375 171.756 172.240 1.00 88.67  ? 2673 LYS A N     1 
ATOM   9566  C  CA    . LYS A 1 2673 ? 165.135 171.169 173.336 1.00 87.55  ? 2673 LYS A CA    1 
ATOM   9567  C  C     . LYS A 1 2673 ? 165.526 172.195 174.389 1.00 86.57  ? 2673 LYS A C     1 
ATOM   9568  O  O     . LYS A 1 2673 ? 165.952 171.805 175.481 1.00 92.82  ? 2673 LYS A O     1 
ATOM   9569  C  CB    . LYS A 1 2673 ? 166.387 170.477 172.795 1.00 86.12  ? 2673 LYS A CB    1 
ATOM   9570  C  CG    . LYS A 1 2673 ? 167.108 171.259 171.714 1.00 85.34  ? 2673 LYS A CG    1 
ATOM   9571  C  CD    . LYS A 1 2673 ? 168.512 170.724 171.496 1.00 84.63  ? 2673 LYS A CD    1 
ATOM   9572  C  CE    . LYS A 1 2673 ? 168.489 169.386 170.780 1.00 84.80  ? 2673 LYS A CE    1 
ATOM   9573  N  NZ    . LYS A 1 2673 ? 169.864 168.906 170.471 1.00 89.02  ? 2673 LYS A NZ    1 
ATOM   9574  N  N     . TYR A 1 2674 ? 165.390 173.487 174.089 1.00 76.41  ? 2674 TYR A N     1 
ATOM   9575  C  CA    . TYR A 1 2674 ? 165.722 174.558 175.017 1.00 79.37  ? 2674 TYR A CA    1 
ATOM   9576  C  C     . TYR A 1 2674 ? 164.480 175.196 175.633 1.00 76.88  ? 2674 TYR A C     1 
ATOM   9577  O  O     . TYR A 1 2674 ? 164.552 176.318 176.143 1.00 78.10  ? 2674 TYR A O     1 
ATOM   9578  C  CB    . TYR A 1 2674 ? 166.574 175.610 174.311 1.00 79.31  ? 2674 TYR A CB    1 
ATOM   9579  C  CG    . TYR A 1 2674 ? 167.778 175.023 173.611 1.00 79.52  ? 2674 TYR A CG    1 
ATOM   9580  C  CD1   . TYR A 1 2674 ? 168.869 174.562 174.334 1.00 80.12  ? 2674 TYR A CD1   1 
ATOM   9581  C  CD2   . TYR A 1 2674 ? 167.815 174.914 172.230 1.00 75.84  ? 2674 TYR A CD2   1 
ATOM   9582  C  CE1   . TYR A 1 2674 ? 169.969 174.023 173.698 1.00 77.82  ? 2674 TYR A CE1   1 
ATOM   9583  C  CE2   . TYR A 1 2674 ? 168.909 174.376 171.586 1.00 75.01  ? 2674 TYR A CE2   1 
ATOM   9584  C  CZ    . TYR A 1 2674 ? 169.983 173.932 172.324 1.00 75.64  ? 2674 TYR A CZ    1 
ATOM   9585  O  OH    . TYR A 1 2674 ? 171.075 173.393 171.685 1.00 75.12  ? 2674 TYR A OH    1 
ATOM   9586  N  N     . GLY A 1 2675 ? 163.344 174.504 175.589 1.00 81.42  ? 2675 GLY A N     1 
ATOM   9587  C  CA    . GLY A 1 2675 ? 162.144 174.952 176.270 1.00 82.73  ? 2675 GLY A CA    1 
ATOM   9588  C  C     . GLY A 1 2675 ? 161.549 176.251 175.768 1.00 84.42  ? 2675 GLY A C     1 
ATOM   9589  O  O     . GLY A 1 2675 ? 161.218 177.131 176.568 1.00 88.91  ? 2675 GLY A O     1 
ATOM   9590  N  N     . THR A 1 2676 ? 161.411 176.394 174.452 1.00 79.96  ? 2676 THR A N     1 
ATOM   9591  C  CA    . THR A 1 2676 ? 160.805 177.586 173.874 1.00 77.13  ? 2676 THR A CA    1 
ATOM   9592  C  C     . THR A 1 2676 ? 159.829 177.188 172.778 1.00 85.15  ? 2676 THR A C     1 
ATOM   9593  O  O     . THR A 1 2676 ? 159.954 176.110 172.190 1.00 92.32  ? 2676 THR A O     1 
ATOM   9594  C  CB    . THR A 1 2676 ? 161.867 178.536 173.307 1.00 75.04  ? 2676 THR A CB    1 
ATOM   9595  O  OG1   . THR A 1 2676 ? 161.331 179.862 173.231 1.00 75.41  ? 2676 THR A OG1   1 
ATOM   9596  C  CG2   . THR A 1 2676 ? 162.286 178.093 171.917 1.00 73.62  ? 2676 THR A CG2   1 
ATOM   9597  N  N     . GLN A 1 2677 ? 158.849 178.050 172.525 1.00 69.98  ? 2677 GLN A N     1 
ATOM   9598  C  CA    . GLN A 1 2677 ? 157.951 177.916 171.387 1.00 62.05  ? 2677 GLN A CA    1 
ATOM   9599  C  C     . GLN A 1 2677 ? 158.040 179.195 170.565 1.00 63.69  ? 2677 GLN A C     1 
ATOM   9600  O  O     . GLN A 1 2677 ? 157.747 180.282 171.073 1.00 70.97  ? 2677 GLN A O     1 
ATOM   9601  C  CB    . GLN A 1 2677 ? 156.517 177.654 171.842 1.00 55.41  ? 2677 GLN A CB    1 
ATOM   9602  C  CG    . GLN A 1 2677 ? 156.327 176.316 172.534 1.00 53.49  ? 2677 GLN A CG    1 
ATOM   9603  C  CD    . GLN A 1 2677 ? 155.115 176.294 173.442 1.00 57.61  ? 2677 GLN A CD    1 
ATOM   9604  O  OE1   . GLN A 1 2677 ? 155.027 177.063 174.397 1.00 66.83  ? 2677 GLN A OE1   1 
ATOM   9605  N  NE2   . GLN A 1 2677 ? 154.175 175.405 173.151 1.00 61.14  ? 2677 GLN A NE2   1 
ATOM   9606  N  N     . ARG A 1 2678 ? 158.451 179.063 169.302 1.00 62.45  ? 2678 ARG A N     1 
ATOM   9607  C  CA    . ARG A 1 2678 ? 158.750 180.243 168.497 1.00 57.99  ? 2678 ARG A CA    1 
ATOM   9608  C  C     . ARG A 1 2678 ? 157.513 181.107 168.286 1.00 64.16  ? 2678 ARG A C     1 
ATOM   9609  O  O     . ARG A 1 2678 ? 157.583 182.337 168.388 1.00 70.84  ? 2678 ARG A O     1 
ATOM   9610  C  CB    . ARG A 1 2678 ? 159.350 179.825 167.157 1.00 58.97  ? 2678 ARG A CB    1 
ATOM   9611  C  CG    . ARG A 1 2678 ? 159.653 180.989 166.234 1.00 62.68  ? 2678 ARG A CG    1 
ATOM   9612  C  CD    . ARG A 1 2678 ? 160.265 180.516 164.930 1.00 65.93  ? 2678 ARG A CD    1 
ATOM   9613  N  NE    . ARG A 1 2678 ? 161.560 179.879 165.138 1.00 68.16  ? 2678 ARG A NE    1 
ATOM   9614  C  CZ    . ARG A 1 2678 ? 162.286 179.330 164.175 1.00 71.73  ? 2678 ARG A CZ    1 
ATOM   9615  N  NH1   . ARG A 1 2678 ? 161.874 179.324 162.918 1.00 70.35  ? 2678 ARG A NH1   1 
ATOM   9616  N  NH2   . ARG A 1 2678 ? 163.454 178.774 164.481 1.00 69.83  ? 2678 ARG A NH2   1 
ATOM   9617  N  N     . VAL A 1 2679 ? 156.369 180.485 167.993 1.00 51.76  ? 2679 VAL A N     1 
ATOM   9618  C  CA    . VAL A 1 2679 ? 155.152 181.264 167.794 1.00 46.09  ? 2679 VAL A CA    1 
ATOM   9619  C  C     . VAL A 1 2679 ? 154.700 181.906 169.100 1.00 51.38  ? 2679 VAL A C     1 
ATOM   9620  O  O     . VAL A 1 2679 ? 154.161 183.019 169.097 1.00 54.60  ? 2679 VAL A O     1 
ATOM   9621  C  CB    . VAL A 1 2679 ? 154.048 180.391 167.168 1.00 40.56  ? 2679 VAL A CB    1 
ATOM   9622  C  CG1   . VAL A 1 2679 ? 153.641 179.279 168.109 1.00 48.79  ? 2679 VAL A CG1   1 
ATOM   9623  C  CG2   . VAL A 1 2679 ? 152.848 181.242 166.785 1.00 43.75  ? 2679 VAL A CG2   1 
ATOM   9624  N  N     . ILE A 1 2680 ? 154.912 181.234 170.234 1.00 50.10  ? 2680 ILE A N     1 
ATOM   9625  C  CA    . ILE A 1 2680 ? 154.555 181.827 171.519 1.00 39.79  ? 2680 ILE A CA    1 
ATOM   9626  C  C     . ILE A 1 2680 ? 155.424 183.044 171.806 1.00 48.77  ? 2680 ILE A C     1 
ATOM   9627  O  O     . ILE A 1 2680 ? 154.935 184.072 172.287 1.00 54.54  ? 2680 ILE A O     1 
ATOM   9628  C  CB    . ILE A 1 2680 ? 154.653 180.777 172.639 1.00 44.83  ? 2680 ILE A CB    1 
ATOM   9629  C  CG1   . ILE A 1 2680 ? 153.563 179.720 172.463 1.00 48.08  ? 2680 ILE A CG1   1 
ATOM   9630  C  CG2   . ILE A 1 2680 ? 154.537 181.433 174.002 1.00 42.60  ? 2680 ILE A CG2   1 
ATOM   9631  C  CD1   . ILE A 1 2680 ? 152.184 180.305 172.287 1.00 40.57  ? 2680 ILE A CD1   1 
ATOM   9632  N  N     . SER A 1 2681 ? 156.723 182.953 171.514 1.00 58.47  ? 2681 SER A N     1 
ATOM   9633  C  CA    . SER A 1 2681 ? 157.595 184.112 171.672 1.00 49.00  ? 2681 SER A CA    1 
ATOM   9634  C  C     . SER A 1 2681 ? 157.188 185.237 170.729 1.00 60.55  ? 2681 SER A C     1 
ATOM   9635  O  O     . SER A 1 2681 ? 157.252 186.417 171.091 1.00 70.21  ? 2681 SER A O     1 
ATOM   9636  C  CB    . SER A 1 2681 ? 159.050 183.711 171.436 1.00 47.31  ? 2681 SER A CB    1 
ATOM   9637  O  OG    . SER A 1 2681 ? 159.502 182.821 172.440 1.00 58.13  ? 2681 SER A OG    1 
ATOM   9638  N  N     . PHE A 1 2682 ? 156.770 184.889 169.511 1.00 56.87  ? 2682 PHE A N     1 
ATOM   9639  C  CA    . PHE A 1 2682 ? 156.301 185.896 168.564 1.00 49.61  ? 2682 PHE A CA    1 
ATOM   9640  C  C     . PHE A 1 2682 ? 155.065 186.613 169.095 1.00 59.58  ? 2682 PHE A C     1 
ATOM   9641  O  O     . PHE A 1 2682 ? 154.962 187.843 169.018 1.00 71.45  ? 2682 PHE A O     1 
ATOM   9642  C  CB    . PHE A 1 2682 ? 156.011 185.233 167.218 1.00 48.20  ? 2682 PHE A CB    1 
ATOM   9643  C  CG    . PHE A 1 2682 ? 155.728 186.199 166.110 1.00 49.63  ? 2682 PHE A CG    1 
ATOM   9644  C  CD1   . PHE A 1 2682 ? 156.708 187.062 165.658 1.00 58.23  ? 2682 PHE A CD1   1 
ATOM   9645  C  CD2   . PHE A 1 2682 ? 154.485 186.230 165.505 1.00 47.17  ? 2682 PHE A CD2   1 
ATOM   9646  C  CE1   . PHE A 1 2682 ? 156.450 187.946 164.633 1.00 52.02  ? 2682 PHE A CE1   1 
ATOM   9647  C  CE2   . PHE A 1 2682 ? 154.221 187.110 164.480 1.00 51.04  ? 2682 PHE A CE2   1 
ATOM   9648  C  CZ    . PHE A 1 2682 ? 155.204 187.970 164.043 1.00 52.45  ? 2682 PHE A CZ    1 
ATOM   9649  N  N     . ILE A 1 2683 ? 154.118 185.855 169.649 1.00 50.21  ? 2683 ILE A N     1 
ATOM   9650  C  CA    . ILE A 1 2683 ? 152.913 186.457 170.210 1.00 41.92  ? 2683 ILE A CA    1 
ATOM   9651  C  C     . ILE A 1 2683 ? 153.257 187.312 171.423 1.00 51.54  ? 2683 ILE A C     1 
ATOM   9652  O  O     . ILE A 1 2683 ? 152.676 188.384 171.628 1.00 59.53  ? 2683 ILE A O     1 
ATOM   9653  C  CB    . ILE A 1 2683 ? 151.881 185.367 170.555 1.00 39.37  ? 2683 ILE A CB    1 
ATOM   9654  C  CG1   . ILE A 1 2683 ? 151.405 184.665 169.284 1.00 52.25  ? 2683 ILE A CG1   1 
ATOM   9655  C  CG2   . ILE A 1 2683 ? 150.696 185.964 171.289 1.00 46.39  ? 2683 ILE A CG2   1 
ATOM   9656  C  CD1   . ILE A 1 2683 ? 150.482 183.500 169.544 1.00 44.83  ? 2683 ILE A CD1   1 
ATOM   9657  N  N     . ARG A 1 2684 ? 154.208 186.860 172.243 1.00 53.80  ? 2684 ARG A N     1 
ATOM   9658  C  CA    . ARG A 1 2684 ? 154.622 187.651 173.398 1.00 47.14  ? 2684 ARG A CA    1 
ATOM   9659  C  C     . ARG A 1 2684 ? 155.251 188.968 172.965 1.00 46.47  ? 2684 ARG A C     1 
ATOM   9660  O  O     . ARG A 1 2684 ? 155.003 190.014 173.575 1.00 57.30  ? 2684 ARG A O     1 
ATOM   9661  C  CB    . ARG A 1 2684 ? 155.595 186.854 174.263 1.00 47.44  ? 2684 ARG A CB    1 
ATOM   9662  C  CG    . ARG A 1 2684 ? 155.984 187.560 175.548 1.00 57.09  ? 2684 ARG A CG    1 
ATOM   9663  C  CD    . ARG A 1 2684 ? 157.358 187.129 176.026 1.00 58.36  ? 2684 ARG A CD    1 
ATOM   9664  N  NE    . ARG A 1 2684 ? 158.031 188.193 176.761 1.00 53.22  ? 2684 ARG A NE    1 
ATOM   9665  C  CZ    . ARG A 1 2684 ? 158.972 188.973 176.252 1.00 62.48  ? 2684 ARG A CZ    1 
ATOM   9666  N  NH1   . ARG A 1 2684 ? 159.383 188.835 175.002 1.00 59.18  ? 2684 ARG A NH1   1 
ATOM   9667  N  NH2   . ARG A 1 2684 ? 159.515 189.918 177.014 1.00 64.07  ? 2684 ARG A NH2   1 
ATOM   9668  N  N     . GLN A 1 2685 ? 156.079 188.935 171.919 1.00 47.24  ? 2685 GLN A N     1 
ATOM   9669  C  CA    . GLN A 1 2685 ? 156.651 190.168 171.389 1.00 50.69  ? 2685 GLN A CA    1 
ATOM   9670  C  C     . GLN A 1 2685 ? 155.569 191.086 170.836 1.00 51.05  ? 2685 GLN A C     1 
ATOM   9671  O  O     . GLN A 1 2685 ? 155.606 192.302 171.057 1.00 65.88  ? 2685 GLN A O     1 
ATOM   9672  C  CB    . GLN A 1 2685 ? 157.680 189.849 170.306 1.00 44.46  ? 2685 GLN A CB    1 
ATOM   9673  C  CG    . GLN A 1 2685 ? 158.116 191.056 169.497 1.00 46.76  ? 2685 GLN A CG    1 
ATOM   9674  C  CD    . GLN A 1 2685 ? 159.046 190.691 168.361 1.00 56.64  ? 2685 GLN A CD    1 
ATOM   9675  O  OE1   . GLN A 1 2685 ? 158.710 189.870 167.508 1.00 59.67  ? 2685 GLN A OE1   1 
ATOM   9676  N  NE2   . GLN A 1 2685 ? 160.224 191.302 168.340 1.00 57.91  ? 2685 GLN A NE2   1 
ATOM   9677  N  N     . MET A 1 2686 ? 154.596 190.522 170.120 1.00 52.83  ? 2686 MET A N     1 
ATOM   9678  C  CA    . MET A 1 2686 ? 153.543 191.333 169.519 1.00 57.49  ? 2686 MET A CA    1 
ATOM   9679  C  C     . MET A 1 2686 ? 152.549 191.860 170.547 1.00 61.72  ? 2686 MET A C     1 
ATOM   9680  O  O     . MET A 1 2686 ? 151.825 192.817 170.255 1.00 67.48  ? 2686 MET A O     1 
ATOM   9681  C  CB    . MET A 1 2686 ? 152.826 190.521 168.442 1.00 55.06  ? 2686 MET A CB    1 
ATOM   9682  C  CG    . MET A 1 2686 ? 153.598 190.465 167.136 1.00 58.80  ? 2686 MET A CG    1 
ATOM   9683  S  SD    . MET A 1 2686 ? 152.631 189.884 165.734 1.00 92.74  ? 2686 MET A SD    1 
ATOM   9684  C  CE    . MET A 1 2686 ? 151.550 188.707 166.533 1.00 60.34  ? 2686 MET A CE    1 
ATOM   9685  N  N     . VAL A 1 2687 ? 152.495 191.262 171.732 1.00 56.00  ? 2687 VAL A N     1 
ATOM   9686  C  CA    . VAL A 1 2687 ? 151.612 191.746 172.789 1.00 54.93  ? 2687 VAL A CA    1 
ATOM   9687  C  C     . VAL A 1 2687 ? 152.318 192.751 173.689 1.00 57.75  ? 2687 VAL A C     1 
ATOM   9688  O  O     . VAL A 1 2687 ? 151.821 193.859 173.909 1.00 65.47  ? 2687 VAL A O     1 
ATOM   9689  C  CB    . VAL A 1 2687 ? 151.062 190.555 173.602 1.00 54.20  ? 2687 VAL A CB    1 
ATOM   9690  C  CG1   . VAL A 1 2687 ? 150.480 191.037 174.915 1.00 58.66  ? 2687 VAL A CG1   1 
ATOM   9691  C  CG2   . VAL A 1 2687 ? 150.013 189.807 172.800 1.00 58.51  ? 2687 VAL A CG2   1 
ATOM   9692  N  N     . GLU A 1 2688 ? 153.484 192.384 174.228 1.00 61.42  ? 2688 GLU A N     1 
ATOM   9693  C  CA    . GLU A 1 2688 ? 154.183 193.268 175.155 1.00 57.98  ? 2688 GLU A CA    1 
ATOM   9694  C  C     . GLU A 1 2688 ? 154.717 194.509 174.452 1.00 65.98  ? 2688 GLU A C     1 
ATOM   9695  O  O     . GLU A 1 2688 ? 154.509 195.633 174.925 1.00 80.85  ? 2688 GLU A O     1 
ATOM   9696  C  CB    . GLU A 1 2688 ? 155.325 192.515 175.835 1.00 56.81  ? 2688 GLU A CB    1 
ATOM   9697  C  CG    . GLU A 1 2688 ? 156.037 193.315 176.911 1.00 67.54  ? 2688 GLU A CG    1 
ATOM   9698  C  CD    . GLU A 1 2688 ? 157.350 192.686 177.332 1.00 75.93  ? 2688 GLU A CD    1 
ATOM   9699  O  OE1   . GLU A 1 2688 ? 157.426 191.440 177.379 1.00 74.50  ? 2688 GLU A OE1   1 
ATOM   9700  O  OE2   . GLU A 1 2688 ? 158.305 193.437 177.619 1.00 72.52  ? 2688 GLU A OE2   1 
ATOM   9701  N  N     . HIS A 1 2689 ? 155.404 194.330 173.327 1.00 52.01  ? 2689 HIS A N     1 
ATOM   9702  C  CA    . HIS A 1 2689 ? 156.006 195.442 172.607 1.00 47.53  ? 2689 HIS A CA    1 
ATOM   9703  C  C     . HIS A 1 2689 ? 155.066 196.075 171.592 1.00 53.35  ? 2689 HIS A C     1 
ATOM   9704  O  O     . HIS A 1 2689 ? 155.403 197.121 171.029 1.00 61.45  ? 2689 HIS A O     1 
ATOM   9705  C  CB    . HIS A 1 2689 ? 157.286 194.980 171.901 1.00 51.10  ? 2689 HIS A CB    1 
ATOM   9706  C  CG    . HIS A 1 2689 ? 158.327 194.447 172.834 1.00 59.51  ? 2689 HIS A CG    1 
ATOM   9707  N  ND1   . HIS A 1 2689 ? 158.603 195.030 174.051 1.00 63.11  ? 2689 HIS A ND1   1 
ATOM   9708  C  CD2   . HIS A 1 2689 ? 159.151 193.378 172.733 1.00 58.91  ? 2689 HIS A CD2   1 
ATOM   9709  C  CE1   . HIS A 1 2689 ? 159.556 194.346 174.658 1.00 66.45  ? 2689 HIS A CE1   1 
ATOM   9710  N  NE2   . HIS A 1 2689 ? 159.906 193.338 173.880 1.00 57.54  ? 2689 HIS A NE2   1 
ATOM   9711  N  N     . GLY A 1 2690 ? 153.905 195.474 171.347 1.00 54.33  ? 2690 GLY A N     1 
ATOM   9712  C  CA    . GLY A 1 2690 ? 152.955 196.043 170.415 1.00 52.75  ? 2690 GLY A CA    1 
ATOM   9713  C  C     . GLY A 1 2690 ? 153.389 196.018 168.969 1.00 54.87  ? 2690 GLY A C     1 
ATOM   9714  O  O     . GLY A 1 2690 ? 152.934 196.852 168.184 1.00 65.47  ? 2690 GLY A O     1 
ATOM   9715  N  N     . GLY A 1 2691 ? 154.256 195.088 168.592 1.00 47.35  ? 2691 GLY A N     1 
ATOM   9716  C  CA    . GLY A 1 2691 ? 154.702 195.021 167.216 1.00 47.15  ? 2691 GLY A CA    1 
ATOM   9717  C  C     . GLY A 1 2691 ? 155.686 193.891 167.018 1.00 61.31  ? 2691 GLY A C     1 
ATOM   9718  O  O     . GLY A 1 2691 ? 155.999 193.143 167.947 1.00 77.31  ? 2691 GLY A O     1 
ATOM   9719  N  N     . PHE A 1 2692 ? 156.170 193.775 165.785 1.00 58.25  ? 2692 PHE A N     1 
ATOM   9720  C  CA    . PHE A 1 2692 ? 157.133 192.744 165.426 1.00 51.01  ? 2692 PHE A CA    1 
ATOM   9721  C  C     . PHE A 1 2692 ? 158.067 193.309 164.362 1.00 54.94  ? 2692 PHE A C     1 
ATOM   9722  O  O     . PHE A 1 2692 ? 157.999 194.492 164.016 1.00 66.77  ? 2692 PHE A O     1 
ATOM   9723  C  CB    . PHE A 1 2692 ? 156.418 191.469 164.962 1.00 50.10  ? 2692 PHE A CB    1 
ATOM   9724  C  CG    . PHE A 1 2692 ? 155.630 191.637 163.694 1.00 54.28  ? 2692 PHE A CG    1 
ATOM   9725  C  CD1   . PHE A 1 2692 ? 154.347 192.153 163.723 1.00 58.07  ? 2692 PHE A CD1   1 
ATOM   9726  C  CD2   . PHE A 1 2692 ? 156.167 191.262 162.476 1.00 56.76  ? 2692 PHE A CD2   1 
ATOM   9727  C  CE1   . PHE A 1 2692 ? 153.620 192.303 162.559 1.00 51.62  ? 2692 PHE A CE1   1 
ATOM   9728  C  CE2   . PHE A 1 2692 ? 155.444 191.409 161.310 1.00 54.23  ? 2692 PHE A CE2   1 
ATOM   9729  C  CZ    . PHE A 1 2692 ? 154.169 191.930 161.352 1.00 50.17  ? 2692 PHE A CZ    1 
ATOM   9730  N  N     . TYR A 1 2693 ? 158.944 192.456 163.840 1.00 60.48  ? 2693 TYR A N     1 
ATOM   9731  C  CA    . TYR A 1 2693 ? 159.957 192.851 162.871 1.00 56.46  ? 2693 TYR A CA    1 
ATOM   9732  C  C     . TYR A 1 2693 ? 159.659 192.198 161.529 1.00 55.94  ? 2693 TYR A C     1 
ATOM   9733  O  O     . TYR A 1 2693 ? 159.473 190.979 161.457 1.00 66.77  ? 2693 TYR A O     1 
ATOM   9734  C  CB    . TYR A 1 2693 ? 161.355 192.448 163.345 1.00 52.56  ? 2693 TYR A CB    1 
ATOM   9735  C  CG    . TYR A 1 2693 ? 162.074 193.508 164.146 1.00 53.72  ? 2693 TYR A CG    1 
ATOM   9736  C  CD1   . TYR A 1 2693 ? 162.646 194.608 163.524 1.00 57.02  ? 2693 TYR A CD1   1 
ATOM   9737  C  CD2   . TYR A 1 2693 ? 162.188 193.405 165.524 1.00 57.37  ? 2693 TYR A CD2   1 
ATOM   9738  C  CE1   . TYR A 1 2693 ? 163.307 195.576 164.253 1.00 60.56  ? 2693 TYR A CE1   1 
ATOM   9739  C  CE2   . TYR A 1 2693 ? 162.846 194.367 166.261 1.00 57.64  ? 2693 TYR A CE2   1 
ATOM   9740  C  CZ    . TYR A 1 2693 ? 163.403 195.450 165.620 1.00 57.45  ? 2693 TYR A CZ    1 
ATOM   9741  O  OH    . TYR A 1 2693 ? 164.060 196.413 166.351 1.00 56.70  ? 2693 TYR A OH    1 
ATOM   9742  N  N     . ARG A 1 2694 ? 159.617 193.007 160.474 1.00 61.04  ? 2694 ARG A N     1 
ATOM   9743  C  CA    . ARG A 1 2694 ? 159.487 192.482 159.120 1.00 66.97  ? 2694 ARG A CA    1 
ATOM   9744  C  C     . ARG A 1 2694 ? 160.846 191.984 158.647 1.00 72.40  ? 2694 ARG A C     1 
ATOM   9745  O  O     . ARG A 1 2694 ? 161.744 192.786 158.373 1.00 78.91  ? 2694 ARG A O     1 
ATOM   9746  C  CB    . ARG A 1 2694 ? 158.950 193.550 158.172 1.00 67.90  ? 2694 ARG A CB    1 
ATOM   9747  C  CG    . ARG A 1 2694 ? 157.488 193.382 157.812 1.00 76.80  ? 2694 ARG A CG    1 
ATOM   9748  C  CD    . ARG A 1 2694 ? 157.176 194.038 156.478 1.00 77.17  ? 2694 ARG A CD    1 
ATOM   9749  N  NE    . ARG A 1 2694 ? 157.733 195.382 156.383 1.00 70.69  ? 2694 ARG A NE    1 
ATOM   9750  C  CZ    . ARG A 1 2694 ? 157.474 196.231 155.399 1.00 72.01  ? 2694 ARG A CZ    1 
ATOM   9751  N  NH1   . ARG A 1 2694 ? 156.665 195.908 154.403 1.00 72.55  ? 2694 ARG A NH1   1 
ATOM   9752  N  NH2   . ARG A 1 2694 ? 158.038 197.434 155.414 1.00 76.04  ? 2694 ARG A NH2   1 
ATOM   9753  N  N     . THR A 1 2695 ? 160.995 190.665 158.542 1.00 73.33  ? 2695 THR A N     1 
ATOM   9754  C  CA    . THR A 1 2695 ? 162.271 190.079 158.155 1.00 70.86  ? 2695 THR A CA    1 
ATOM   9755  C  C     . THR A 1 2695 ? 162.652 190.376 156.711 1.00 73.16  ? 2695 THR A C     1 
ATOM   9756  O  O     . THR A 1 2695 ? 163.803 190.136 156.333 1.00 78.83  ? 2695 THR A O     1 
ATOM   9757  C  CB    . THR A 1 2695 ? 162.240 188.564 158.369 1.00 80.40  ? 2695 THR A CB    1 
ATOM   9758  O  OG1   . THR A 1 2695 ? 161.281 187.976 157.483 1.00 80.86  ? 2695 THR A OG1   1 
ATOM   9759  C  CG2   . THR A 1 2695 ? 161.861 188.240 159.806 1.00 76.91  ? 2695 THR A CG2   1 
ATOM   9760  N  N     . SER A 1 2696 ? 161.722 190.883 155.900 1.00 74.09  ? 2696 SER A N     1 
ATOM   9761  C  CA    . SER A 1 2696 ? 162.048 191.208 154.516 1.00 75.78  ? 2696 SER A CA    1 
ATOM   9762  C  C     . SER A 1 2696 ? 163.014 192.384 154.433 1.00 72.42  ? 2696 SER A C     1 
ATOM   9763  O  O     . SER A 1 2696 ? 163.953 192.366 153.630 1.00 67.66  ? 2696 SER A O     1 
ATOM   9764  C  CB    . SER A 1 2696 ? 160.772 191.507 153.731 1.00 75.95  ? 2696 SER A CB    1 
ATOM   9765  O  OG    . SER A 1 2696 ? 160.395 192.864 153.878 1.00 77.21  ? 2696 SER A OG    1 
ATOM   9766  N  N     . ASP A 1 2697 ? 162.801 193.417 155.253 1.00 76.77  ? 2697 ASP A N     1 
ATOM   9767  C  CA    . ASP A 1 2697 ? 163.661 194.593 155.246 1.00 76.05  ? 2697 ASP A CA    1 
ATOM   9768  C  C     . ASP A 1 2697 ? 164.062 195.046 156.645 1.00 78.19  ? 2697 ASP A C     1 
ATOM   9769  O  O     . ASP A 1 2697 ? 164.531 196.180 156.800 1.00 74.48  ? 2697 ASP A O     1 
ATOM   9770  C  CB    . ASP A 1 2697 ? 162.984 195.751 154.505 1.00 78.55  ? 2697 ASP A CB    1 
ATOM   9771  C  CG    . ASP A 1 2697 ? 161.556 195.972 154.952 1.00 84.31  ? 2697 ASP A CG    1 
ATOM   9772  O  OD1   . ASP A 1 2697 ? 161.039 195.136 155.722 1.00 84.58  ? 2697 ASP A OD1   1 
ATOM   9773  O  OD2   . ASP A 1 2697 ? 160.950 196.982 154.537 1.00 86.29  ? 2697 ASP A OD2   1 
ATOM   9774  N  N     . GLN A 1 2698 ? 163.896 194.195 157.659 1.00 76.21  ? 2698 GLN A N     1 
ATOM   9775  C  CA    . GLN A 1 2698 ? 164.315 194.490 159.032 1.00 66.73  ? 2698 GLN A CA    1 
ATOM   9776  C  C     . GLN A 1 2698 ? 163.704 195.795 159.538 1.00 69.33  ? 2698 GLN A C     1 
ATOM   9777  O  O     . GLN A 1 2698 ? 164.368 196.618 160.171 1.00 73.27  ? 2698 GLN A O     1 
ATOM   9778  C  CB    . GLN A 1 2698 ? 165.841 194.520 159.144 1.00 62.68  ? 2698 GLN A CB    1 
ATOM   9779  C  CG    . GLN A 1 2698 ? 166.511 193.190 158.854 1.00 71.10  ? 2698 GLN A CG    1 
ATOM   9780  C  CD    . GLN A 1 2698 ? 166.692 192.929 157.372 1.00 74.23  ? 2698 GLN A CD    1 
ATOM   9781  O  OE1   . GLN A 1 2698 ? 166.870 193.856 156.584 1.00 77.45  ? 2698 GLN A OE1   1 
ATOM   9782  N  NE2   . GLN A 1 2698 ? 166.650 191.659 156.986 1.00 70.75  ? 2698 GLN A NE2   1 
ATOM   9783  N  N     . THR A 1 2699 ? 162.419 195.980 159.255 1.00 73.09  ? 2699 THR A N     1 
ATOM   9784  C  CA    . THR A 1 2699 ? 161.692 197.183 159.634 1.00 71.81  ? 2699 THR A CA    1 
ATOM   9785  C  C     . THR A 1 2699 ? 160.718 196.854 160.756 1.00 71.87  ? 2699 THR A C     1 
ATOM   9786  O  O     . THR A 1 2699 ? 159.984 195.864 160.675 1.00 76.24  ? 2699 THR A O     1 
ATOM   9787  C  CB    . THR A 1 2699 ? 160.939 197.767 158.436 1.00 70.15  ? 2699 THR A CB    1 
ATOM   9788  O  OG1   . THR A 1 2699 ? 161.872 198.099 157.401 1.00 74.99  ? 2699 THR A OG1   1 
ATOM   9789  C  CG2   . THR A 1 2699 ? 160.185 199.021 158.844 1.00 68.19  ? 2699 THR A CG2   1 
ATOM   9790  N  N     . TRP A 1 2700 ? 160.714 197.683 161.797 1.00 54.05  ? 2700 TRP A N     1 
ATOM   9791  C  CA    . TRP A 1 2700 ? 159.797 197.488 162.913 1.00 56.31  ? 2700 TRP A CA    1 
ATOM   9792  C  C     . TRP A 1 2700 ? 158.375 197.809 162.472 1.00 56.59  ? 2700 TRP A C     1 
ATOM   9793  O  O     . TRP A 1 2700 ? 158.114 198.886 161.926 1.00 64.96  ? 2700 TRP A O     1 
ATOM   9794  C  CB    . TRP A 1 2700 ? 160.206 198.366 164.091 1.00 53.61  ? 2700 TRP A CB    1 
ATOM   9795  C  CG    . TRP A 1 2700 ? 159.249 198.316 165.242 1.00 53.76  ? 2700 TRP A CG    1 
ATOM   9796  C  CD1   . TRP A 1 2700 ? 158.324 199.260 165.577 1.00 59.50  ? 2700 TRP A CD1   1 
ATOM   9797  C  CD2   . TRP A 1 2700 ? 159.127 197.273 166.216 1.00 56.83  ? 2700 TRP A CD2   1 
ATOM   9798  N  NE1   . TRP A 1 2700 ? 157.631 198.869 166.695 1.00 57.80  ? 2700 TRP A NE1   1 
ATOM   9799  C  CE2   . TRP A 1 2700 ? 158.106 197.652 167.108 1.00 54.59  ? 2700 TRP A CE2   1 
ATOM   9800  C  CE3   . TRP A 1 2700 ? 159.781 196.055 166.420 1.00 58.55  ? 2700 TRP A CE3   1 
ATOM   9801  C  CZ2   . TRP A 1 2700 ? 157.723 196.857 168.184 1.00 56.84  ? 2700 TRP A CZ2   1 
ATOM   9802  C  CZ3   . TRP A 1 2700 ? 159.400 195.269 167.490 1.00 50.82  ? 2700 TRP A CZ3   1 
ATOM   9803  C  CH2   . TRP A 1 2700 ? 158.381 195.672 168.357 1.00 55.32  ? 2700 TRP A CH2   1 
ATOM   9804  N  N     . VAL A 1 2701 ? 157.457 196.877 162.711 1.00 51.37  ? 2701 VAL A N     1 
ATOM   9805  C  CA    . VAL A 1 2701 ? 156.060 197.009 162.314 1.00 51.52  ? 2701 VAL A CA    1 
ATOM   9806  C  C     . VAL A 1 2701 ? 155.208 197.036 163.573 1.00 57.44  ? 2701 VAL A C     1 
ATOM   9807  O  O     . VAL A 1 2701 ? 155.235 196.088 164.365 1.00 72.86  ? 2701 VAL A O     1 
ATOM   9808  C  CB    . VAL A 1 2701 ? 155.631 195.861 161.387 1.00 56.41  ? 2701 VAL A CB    1 
ATOM   9809  C  CG1   . VAL A 1 2701 ? 154.131 195.893 161.165 1.00 65.05  ? 2701 VAL A CG1   1 
ATOM   9810  C  CG2   . VAL A 1 2701 ? 156.376 195.942 160.071 1.00 64.76  ? 2701 VAL A CG2   1 
ATOM   9811  N  N     . LYS A 1 2702 ? 154.445 198.109 163.750 1.00 56.66  ? 2702 LYS A N     1 
ATOM   9812  C  CA    . LYS A 1 2702 ? 153.635 198.303 164.945 1.00 57.45  ? 2702 LYS A CA    1 
ATOM   9813  C  C     . LYS A 1 2702 ? 152.194 197.898 164.663 1.00 64.52  ? 2702 LYS A C     1 
ATOM   9814  O  O     . LYS A 1 2702 ? 151.598 198.350 163.679 1.00 77.71  ? 2702 LYS A O     1 
ATOM   9815  C  CB    . LYS A 1 2702 ? 153.698 199.758 165.412 1.00 54.00  ? 2702 LYS A CB    1 
ATOM   9816  C  CG    . LYS A 1 2702 ? 152.489 200.210 166.212 1.00 61.36  ? 2702 LYS A CG    1 
ATOM   9817  C  CD    . LYS A 1 2702 ? 152.599 201.678 166.590 1.00 67.85  ? 2702 LYS A CD    1 
ATOM   9818  C  CE    . LYS A 1 2702 ? 151.226 202.315 166.726 1.00 72.15  ? 2702 LYS A CE    1 
ATOM   9819  N  NZ    . LYS A 1 2702 ? 150.524 201.858 167.957 1.00 69.60  ? 2702 LYS A NZ    1 
ATOM   9820  N  N     . LEU A 1 2703 ? 151.644 197.046 165.523 1.00 56.73  ? 2703 LEU A N     1 
ATOM   9821  C  CA    . LEU A 1 2703 ? 150.275 196.582 165.349 1.00 51.49  ? 2703 LEU A CA    1 
ATOM   9822  C  C     . LEU A 1 2703 ? 149.283 197.686 165.687 1.00 51.96  ? 2703 LEU A C     1 
ATOM   9823  O  O     . LEU A 1 2703 ? 149.513 198.499 166.586 1.00 59.08  ? 2703 LEU A O     1 
ATOM   9824  C  CB    . LEU A 1 2703 ? 150.011 195.360 166.227 1.00 54.94  ? 2703 LEU A CB    1 
ATOM   9825  C  CG    . LEU A 1 2703 ? 150.879 194.127 165.980 1.00 58.03  ? 2703 LEU A CG    1 
ATOM   9826  C  CD1   . LEU A 1 2703 ? 150.283 192.914 166.670 1.00 55.36  ? 2703 LEU A CD1   1 
ATOM   9827  C  CD2   . LEU A 1 2703 ? 151.034 193.874 164.494 1.00 51.31  ? 2703 LEU A CD2   1 
ATOM   9828  N  N     . GLU A 1 2704 ? 148.170 197.710 164.957 1.00 72.33  ? 2704 GLU A N     1 
ATOM   9829  C  CA    . GLU A 1 2704 ? 147.095 198.659 165.206 1.00 73.50  ? 2704 GLU A CA    1 
ATOM   9830  C  C     . GLU A 1 2704 ? 145.762 197.952 165.030 1.00 74.83  ? 2704 GLU A C     1 
ATOM   9831  O  O     . GLU A 1 2704 ? 145.553 197.262 164.028 1.00 81.22  ? 2704 GLU A O     1 
ATOM   9832  C  CB    . GLU A 1 2704 ? 147.182 199.863 164.261 1.00 74.37  ? 2704 GLU A CB    1 
ATOM   9833  C  CG    . GLU A 1 2704 ? 146.306 201.035 164.666 1.00 79.40  ? 2704 GLU A CG    1 
ATOM   9834  C  CD    . GLU A 1 2704 ? 145.951 201.931 163.495 1.00 84.98  ? 2704 GLU A CD    1 
ATOM   9835  O  OE1   . GLU A 1 2704 ? 146.871 202.360 162.771 1.00 82.71  ? 2704 GLU A OE1   1 
ATOM   9836  O  OE2   . GLU A 1 2704 ? 144.749 202.205 163.298 1.00 85.49  ? 2704 GLU A OE2   1 
ATOM   9837  N  N     . ARG A 1 2705 ? 144.867 198.131 166.003 1.00 56.88  ? 2705 ARG A N     1 
ATOM   9838  C  CA    . ARG A 1 2705 ? 143.524 197.551 165.961 1.00 57.36  ? 2705 ARG A CA    1 
ATOM   9839  C  C     . ARG A 1 2705 ? 143.572 196.033 165.804 1.00 62.88  ? 2705 ARG A C     1 
ATOM   9840  O  O     . ARG A 1 2705 ? 142.829 195.449 165.012 1.00 71.09  ? 2705 ARG A O     1 
ATOM   9841  C  CB    . ARG A 1 2705 ? 142.687 198.188 164.849 1.00 59.94  ? 2705 ARG A CB    1 
ATOM   9842  C  CG    . ARG A 1 2705 ? 142.102 199.539 165.214 1.00 62.30  ? 2705 ARG A CG    1 
ATOM   9843  C  CD    . ARG A 1 2705 ? 141.178 200.052 164.126 1.00 59.14  ? 2705 ARG A CD    1 
ATOM   9844  N  NE    . ARG A 1 2705 ? 141.920 200.539 162.969 1.00 63.13  ? 2705 ARG A NE    1 
ATOM   9845  C  CZ    . ARG A 1 2705 ? 141.871 199.990 161.763 1.00 69.10  ? 2705 ARG A CZ    1 
ATOM   9846  N  NH1   . ARG A 1 2705 ? 141.125 198.926 161.518 1.00 63.26  ? 2705 ARG A NH1   1 
ATOM   9847  N  NH2   . ARG A 1 2705 ? 142.589 200.523 160.779 1.00 73.44  ? 2705 ARG A NH2   1 
ATOM   9848  N  N     . ILE A 1 2706 ? 144.457 195.387 166.559 1.00 53.42  ? 2706 ILE A N     1 
ATOM   9849  C  CA    . ILE A 1 2706 ? 144.608 193.937 166.539 1.00 48.41  ? 2706 ILE A CA    1 
ATOM   9850  C  C     . ILE A 1 2706 ? 144.741 193.444 167.972 1.00 49.63  ? 2706 ILE A C     1 
ATOM   9851  O  O     . ILE A 1 2706 ? 145.527 193.994 168.751 1.00 55.59  ? 2706 ILE A O     1 
ATOM   9852  C  CB    . ILE A 1 2706 ? 145.824 193.502 165.699 1.00 45.29  ? 2706 ILE A CB    1 
ATOM   9853  C  CG1   . ILE A 1 2706 ? 145.530 193.665 164.207 1.00 48.58  ? 2706 ILE A CG1   1 
ATOM   9854  C  CG2   . ILE A 1 2706 ? 146.208 192.066 166.007 1.00 44.96  ? 2706 ILE A CG2   1 
ATOM   9855  C  CD1   . ILE A 1 2706 ? 146.735 193.458 163.323 1.00 43.03  ? 2706 ILE A CD1   1 
ATOM   9856  N  N     . GLN A 1 2707 ? 143.975 192.411 168.319 1.00 40.68  ? 2707 GLN A N     1 
ATOM   9857  C  CA    . GLN A 1 2707 ? 144.056 191.768 169.622 1.00 38.61  ? 2707 GLN A CA    1 
ATOM   9858  C  C     . GLN A 1 2707 ? 144.008 190.258 169.436 1.00 51.16  ? 2707 GLN A C     1 
ATOM   9859  O  O     . GLN A 1 2707 ? 143.570 189.751 168.401 1.00 68.48  ? 2707 GLN A O     1 
ATOM   9860  C  CB    . GLN A 1 2707 ? 142.929 192.227 170.555 1.00 46.19  ? 2707 GLN A CB    1 
ATOM   9861  C  CG    . GLN A 1 2707 ? 141.548 192.168 169.942 1.00 56.37  ? 2707 GLN A CG    1 
ATOM   9862  C  CD    . GLN A 1 2707 ? 140.456 192.356 170.972 1.00 54.69  ? 2707 GLN A CD    1 
ATOM   9863  O  OE1   . GLN A 1 2707 ? 140.661 192.116 172.160 1.00 55.09  ? 2707 GLN A OE1   1 
ATOM   9864  N  NE2   . GLN A 1 2707 ? 139.286 192.788 170.521 1.00 53.83  ? 2707 GLN A NE2   1 
ATOM   9865  N  N     . PHE A 1 2708 ? 144.464 189.536 170.457 1.00 45.89  ? 2708 PHE A N     1 
ATOM   9866  C  CA    . PHE A 1 2708 ? 144.642 188.093 170.373 1.00 43.76  ? 2708 PHE A CA    1 
ATOM   9867  C  C     . PHE A 1 2708 ? 143.810 187.408 171.443 1.00 53.27  ? 2708 PHE A C     1 
ATOM   9868  O  O     . PHE A 1 2708 ? 143.746 187.881 172.582 1.00 63.72  ? 2708 PHE A O     1 
ATOM   9869  C  CB    . PHE A 1 2708 ? 146.116 187.714 170.535 1.00 47.05  ? 2708 PHE A CB    1 
ATOM   9870  C  CG    . PHE A 1 2708 ? 147.036 188.483 169.636 1.00 53.21  ? 2708 PHE A CG    1 
ATOM   9871  C  CD1   . PHE A 1 2708 ? 147.349 188.011 168.376 1.00 55.50  ? 2708 PHE A CD1   1 
ATOM   9872  C  CD2   . PHE A 1 2708 ? 147.585 189.682 170.054 1.00 54.92  ? 2708 PHE A CD2   1 
ATOM   9873  C  CE1   . PHE A 1 2708 ? 148.190 188.724 167.550 1.00 53.08  ? 2708 PHE A CE1   1 
ATOM   9874  C  CE2   . PHE A 1 2708 ? 148.427 190.397 169.233 1.00 56.81  ? 2708 PHE A CE2   1 
ATOM   9875  C  CZ    . PHE A 1 2708 ? 148.728 189.919 167.980 1.00 54.40  ? 2708 PHE A CZ    1 
ATOM   9876  N  N     . VAL A 1 2709 ? 143.173 186.301 171.075 1.00 48.98  ? 2709 VAL A N     1 
ATOM   9877  C  CA    . VAL A 1 2709 ? 142.460 185.441 172.011 1.00 40.54  ? 2709 VAL A CA    1 
ATOM   9878  C  C     . VAL A 1 2709 ? 142.944 184.016 171.801 1.00 53.80  ? 2709 VAL A C     1 
ATOM   9879  O  O     . VAL A 1 2709 ? 142.956 183.521 170.669 1.00 68.96  ? 2709 VAL A O     1 
ATOM   9880  C  CB    . VAL A 1 2709 ? 140.935 185.534 171.830 1.00 41.31  ? 2709 VAL A CB    1 
ATOM   9881  C  CG1   . VAL A 1 2709 ? 140.242 184.510 172.708 1.00 47.42  ? 2709 VAL A CG1   1 
ATOM   9882  C  CG2   . VAL A 1 2709 ? 140.457 186.926 172.166 1.00 53.88  ? 2709 VAL A CG2   1 
ATOM   9883  N  N     . GLY A 1 2710 ? 143.339 183.360 172.886 1.00 60.19  ? 2710 GLY A N     1 
ATOM   9884  C  CA    . GLY A 1 2710 ? 143.882 182.020 172.818 1.00 57.18  ? 2710 GLY A CA    1 
ATOM   9885  C  C     . GLY A 1 2710 ? 142.922 180.998 173.395 1.00 56.33  ? 2710 GLY A C     1 
ATOM   9886  O  O     . GLY A 1 2710 ? 142.128 181.300 174.286 1.00 69.15  ? 2710 GLY A O     1 
ATOM   9887  N  N     . ALA A 1 2711 ? 142.997 179.782 172.866 1.00 38.90  ? 2711 ALA A N     1 
ATOM   9888  C  CA    . ALA A 1 2711 ? 142.269 178.642 173.396 1.00 40.84  ? 2711 ALA A CA    1 
ATOM   9889  C  C     . ALA A 1 2711 ? 143.221 177.462 173.475 1.00 49.77  ? 2711 ALA A C     1 
ATOM   9890  O  O     . ALA A 1 2711 ? 144.118 177.317 172.642 1.00 68.07  ? 2711 ALA A O     1 
ATOM   9891  C  CB    . ALA A 1 2711 ? 141.055 178.288 172.531 1.00 44.12  ? 2711 ALA A CB    1 
ATOM   9892  N  N     . CYS A 1 2712 ? 143.033 176.625 174.492 1.00 56.55  ? 2712 CYS A N     1 
ATOM   9893  C  CA    . CYS A 1 2712 ? 143.936 175.502 174.690 1.00 60.42  ? 2712 CYS A CA    1 
ATOM   9894  C  C     . CYS A 1 2712 ? 143.349 174.541 175.710 1.00 63.31  ? 2712 CYS A C     1 
ATOM   9895  O  O     . CYS A 1 2712 ? 142.548 174.922 176.566 1.00 66.85  ? 2712 CYS A O     1 
ATOM   9896  C  CB    . CYS A 1 2712 ? 145.319 175.973 175.149 1.00 58.02  ? 2712 CYS A CB    1 
ATOM   9897  S  SG    . CYS A 1 2712 ? 145.283 177.116 176.542 1.00 73.49  ? 2712 CYS A SG    1 
ATOM   9898  N  N     . ASN A 1 2713 ? 143.762 173.290 175.600 1.00 63.35  ? 2713 ASN A N     1 
ATOM   9899  C  CA    . ASN A 1 2713 ? 143.521 172.268 176.602 1.00 60.30  ? 2713 ASN A CA    1 
ATOM   9900  C  C     . ASN A 1 2713 ? 144.468 172.467 177.776 1.00 64.84  ? 2713 ASN A C     1 
ATOM   9901  O  O     . ASN A 1 2713 ? 145.473 173.176 177.658 1.00 69.31  ? 2713 ASN A O     1 
ATOM   9902  C  CB    . ASN A 1 2713 ? 143.715 170.882 175.990 1.00 55.91  ? 2713 ASN A CB    1 
ATOM   9903  C  CG    . ASN A 1 2713 ? 142.785 170.625 174.823 1.00 58.85  ? 2713 ASN A CG    1 
ATOM   9904  O  OD1   . ASN A 1 2713 ? 143.045 169.759 173.988 1.00 66.86  ? 2713 ASN A OD1   1 
ATOM   9905  N  ND2   . ASN A 1 2713 ? 141.689 171.371 174.763 1.00 63.64  ? 2713 ASN A ND2   1 
ATOM   9906  N  N     . PRO A 1 2714 ? 144.173 171.879 178.932 1.00 58.52  ? 2714 PRO A N     1 
ATOM   9907  C  CA    . PRO A 1 2714 ? 145.082 171.999 180.075 1.00 58.02  ? 2714 PRO A CA    1 
ATOM   9908  C  C     . PRO A 1 2714 ? 146.458 171.461 179.732 1.00 67.36  ? 2714 PRO A C     1 
ATOM   9909  O  O     . PRO A 1 2714 ? 146.583 170.494 178.966 1.00 75.56  ? 2714 PRO A O     1 
ATOM   9910  C  CB    . PRO A 1 2714 ? 144.403 171.147 181.155 1.00 63.07  ? 2714 PRO A CB    1 
ATOM   9911  C  CG    . PRO A 1 2714 ? 142.965 171.202 180.812 1.00 66.50  ? 2714 PRO A CG    1 
ATOM   9912  C  CD    . PRO A 1 2714 ? 142.902 171.235 179.311 1.00 65.80  ? 2714 PRO A CD    1 
ATOM   9913  N  N     . PRO A 1 2715 ? 147.517 172.071 180.267 1.00 68.66  ? 2715 PRO A N     1 
ATOM   9914  C  CA    . PRO A 1 2715 ? 148.875 171.605 179.943 1.00 72.51  ? 2715 PRO A CA    1 
ATOM   9915  C  C     . PRO A 1 2715 ? 149.155 170.183 180.394 1.00 73.64  ? 2715 PRO A C     1 
ATOM   9916  O  O     . PRO A 1 2715 ? 150.093 169.561 179.883 1.00 73.77  ? 2715 PRO A O     1 
ATOM   9917  C  CB    . PRO A 1 2715 ? 149.776 172.612 180.672 1.00 69.08  ? 2715 PRO A CB    1 
ATOM   9918  C  CG    . PRO A 1 2715 ? 148.914 173.186 181.746 1.00 70.02  ? 2715 PRO A CG    1 
ATOM   9919  C  CD    . PRO A 1 2715 ? 147.528 173.220 181.186 1.00 64.85  ? 2715 PRO A CD    1 
ATOM   9920  N  N     . THR A 1 2716 ? 148.377 169.650 181.336 1.00 75.74  ? 2716 THR A N     1 
ATOM   9921  C  CA    . THR A 1 2716 ? 148.554 168.274 181.779 1.00 75.86  ? 2716 THR A CA    1 
ATOM   9922  C  C     . THR A 1 2716 ? 148.068 167.254 180.757 1.00 79.71  ? 2716 THR A C     1 
ATOM   9923  O  O     . THR A 1 2716 ? 148.419 166.075 180.872 1.00 87.88  ? 2716 THR A O     1 
ATOM   9924  C  CB    . THR A 1 2716 ? 147.826 168.050 183.105 1.00 84.57  ? 2716 THR A CB    1 
ATOM   9925  O  OG1   . THR A 1 2716 ? 146.424 168.286 182.929 1.00 82.56  ? 2716 THR A OG1   1 
ATOM   9926  C  CG2   . THR A 1 2716 ? 148.361 168.994 184.169 1.00 83.37  ? 2716 THR A CG2   1 
ATOM   9927  N  N     . ASP A 1 2717 ? 147.268 167.667 179.778 1.00 75.43  ? 2717 ASP A N     1 
ATOM   9928  C  CA    . ASP A 1 2717 ? 146.839 166.750 178.736 1.00 73.70  ? 2717 ASP A CA    1 
ATOM   9929  C  C     . ASP A 1 2717 ? 148.011 166.418 177.813 1.00 75.45  ? 2717 ASP A C     1 
ATOM   9930  O  O     . ASP A 1 2717 ? 148.863 167.270 177.550 1.00 81.60  ? 2717 ASP A O     1 
ATOM   9931  C  CB    . ASP A 1 2717 ? 145.694 167.355 177.930 1.00 76.07  ? 2717 ASP A CB    1 
ATOM   9932  C  CG    . ASP A 1 2717 ? 144.341 167.107 178.566 1.00 79.74  ? 2717 ASP A CG    1 
ATOM   9933  O  OD1   . ASP A 1 2717 ? 144.305 166.654 179.729 1.00 80.21  ? 2717 ASP A OD1   1 
ATOM   9934  O  OD2   . ASP A 1 2717 ? 143.314 167.364 177.904 1.00 80.85  ? 2717 ASP A OD2   1 
ATOM   9935  N  N     . PRO A 1 2718 ? 148.073 165.186 177.307 1.00 69.45  ? 2718 PRO A N     1 
ATOM   9936  C  CA    . PRO A 1 2718 ? 149.222 164.784 176.485 1.00 73.24  ? 2718 PRO A CA    1 
ATOM   9937  C  C     . PRO A 1 2718 ? 149.344 165.627 175.225 1.00 70.41  ? 2718 PRO A C     1 
ATOM   9938  O  O     . PRO A 1 2718 ? 148.348 165.991 174.597 1.00 73.10  ? 2718 PRO A O     1 
ATOM   9939  C  CB    . PRO A 1 2718 ? 148.925 163.317 176.154 1.00 72.89  ? 2718 PRO A CB    1 
ATOM   9940  C  CG    . PRO A 1 2718 ? 147.454 163.176 176.330 1.00 70.71  ? 2718 PRO A CG    1 
ATOM   9941  C  CD    . PRO A 1 2718 ? 147.089 164.101 177.446 1.00 68.78  ? 2718 PRO A CD    1 
ATOM   9942  N  N     . GLY A 1 2719 ? 150.588 165.933 174.859 1.00 66.07  ? 2719 GLY A N     1 
ATOM   9943  C  CA    . GLY A 1 2719 ? 150.876 166.747 173.701 1.00 63.14  ? 2719 GLY A CA    1 
ATOM   9944  C  C     . GLY A 1 2719 ? 150.857 168.239 173.942 1.00 66.88  ? 2719 GLY A C     1 
ATOM   9945  O  O     . GLY A 1 2719 ? 151.225 168.998 173.037 1.00 75.31  ? 2719 GLY A O     1 
ATOM   9946  N  N     . ARG A 1 2720 ? 150.452 168.686 175.125 1.00 64.58  ? 2720 ARG A N     1 
ATOM   9947  C  CA    . ARG A 1 2720 ? 150.374 170.103 175.446 1.00 61.10  ? 2720 ARG A CA    1 
ATOM   9948  C  C     . ARG A 1 2720 ? 151.566 170.509 176.300 1.00 69.36  ? 2720 ARG A C     1 
ATOM   9949  O  O     . ARG A 1 2720 ? 151.996 169.761 177.182 1.00 70.41  ? 2720 ARG A O     1 
ATOM   9950  C  CB    . ARG A 1 2720 ? 149.073 170.425 176.184 1.00 59.04  ? 2720 ARG A CB    1 
ATOM   9951  C  CG    . ARG A 1 2720 ? 147.837 169.770 175.590 1.00 59.36  ? 2720 ARG A CG    1 
ATOM   9952  C  CD    . ARG A 1 2720 ? 147.570 170.261 174.178 1.00 64.02  ? 2720 ARG A CD    1 
ATOM   9953  N  NE    . ARG A 1 2720 ? 146.276 169.810 173.680 1.00 67.34  ? 2720 ARG A NE    1 
ATOM   9954  C  CZ    . ARG A 1 2720 ? 146.044 168.603 173.182 1.00 64.36  ? 2720 ARG A CZ    1 
ATOM   9955  N  NH1   . ARG A 1 2720 ? 147.000 167.694 173.099 1.00 65.37  ? 2720 ARG A NH1   1 
ATOM   9956  N  NH2   . ARG A 1 2720 ? 144.821 168.302 172.756 1.00 66.59  ? 2720 ARG A NH2   1 
ATOM   9957  N  N     . LYS A 1 2721 ? 152.096 171.697 176.032 1.00 73.24  ? 2721 LYS A N     1 
ATOM   9958  C  CA    . LYS A 1 2721 ? 153.223 172.212 176.787 1.00 70.84  ? 2721 LYS A CA    1 
ATOM   9959  C  C     . LYS A 1 2721 ? 152.811 173.440 177.591 1.00 72.98  ? 2721 LYS A C     1 
ATOM   9960  O  O     . LYS A 1 2721 ? 151.957 174.217 177.153 1.00 76.34  ? 2721 LYS A O     1 
ATOM   9961  C  CB    . LYS A 1 2721 ? 154.385 172.585 175.859 1.00 65.47  ? 2721 LYS A CB    1 
ATOM   9962  C  CG    . LYS A 1 2721 ? 155.359 171.450 175.598 1.00 70.92  ? 2721 LYS A CG    1 
ATOM   9963  C  CD    . LYS A 1 2721 ? 154.853 170.533 174.500 1.00 70.65  ? 2721 LYS A CD    1 
ATOM   9964  C  CE    . LYS A 1 2721 ? 154.738 171.272 173.179 1.00 72.25  ? 2721 LYS A CE    1 
ATOM   9965  N  NZ    . LYS A 1 2721 ? 154.291 170.375 172.078 1.00 74.36  ? 2721 LYS A NZ    1 
ATOM   9966  N  N     . PRO A 1 2722 ? 153.392 173.642 178.773 1.00 68.08  ? 2722 PRO A N     1 
ATOM   9967  C  CA    . PRO A 1 2722 ? 153.049 174.831 179.564 1.00 67.18  ? 2722 PRO A CA    1 
ATOM   9968  C  C     . PRO A 1 2722 ? 153.598 176.091 178.912 1.00 72.72  ? 2722 PRO A C     1 
ATOM   9969  O  O     . PRO A 1 2722 ? 154.746 176.126 178.465 1.00 75.37  ? 2722 PRO A O     1 
ATOM   9970  C  CB    . PRO A 1 2722 ? 153.710 174.559 180.919 1.00 67.86  ? 2722 PRO A CB    1 
ATOM   9971  C  CG    . PRO A 1 2722 ? 154.837 173.640 180.604 1.00 71.18  ? 2722 PRO A CG    1 
ATOM   9972  C  CD    . PRO A 1 2722 ? 154.375 172.785 179.457 1.00 69.18  ? 2722 PRO A CD    1 
ATOM   9973  N  N     . LEU A 1 2723 ? 152.765 177.125 178.858 1.00 67.92  ? 2723 LEU A N     1 
ATOM   9974  C  CA    . LEU A 1 2723 ? 153.182 178.388 178.270 1.00 64.90  ? 2723 LEU A CA    1 
ATOM   9975  C  C     . LEU A 1 2723 ? 154.226 179.066 179.150 1.00 65.35  ? 2723 LEU A C     1 
ATOM   9976  O  O     . LEU A 1 2723 ? 154.251 178.892 180.371 1.00 73.44  ? 2723 LEU A O     1 
ATOM   9977  C  CB    . LEU A 1 2723 ? 151.979 179.308 178.076 1.00 59.90  ? 2723 LEU A CB    1 
ATOM   9978  C  CG    . LEU A 1 2723 ? 150.928 178.822 177.077 1.00 55.90  ? 2723 LEU A CG    1 
ATOM   9979  C  CD1   . LEU A 1 2723 ? 149.677 179.678 177.158 1.00 59.29  ? 2723 LEU A CD1   1 
ATOM   9980  C  CD2   . LEU A 1 2723 ? 151.488 178.823 175.667 1.00 63.36  ? 2723 LEU A CD2   1 
ATOM   9981  N  N     . SER A 1 2724 ? 155.100 179.840 178.512 1.00 57.37  ? 2724 SER A N     1 
ATOM   9982  C  CA    . SER A 1 2724 ? 156.156 180.529 179.240 1.00 59.65  ? 2724 SER A CA    1 
ATOM   9983  C  C     . SER A 1 2724 ? 155.563 181.551 180.201 1.00 57.63  ? 2724 SER A C     1 
ATOM   9984  O  O     . SER A 1 2724 ? 154.544 182.182 179.912 1.00 63.47  ? 2724 SER A O     1 
ATOM   9985  C  CB    . SER A 1 2724 ? 157.110 181.214 178.264 1.00 67.45  ? 2724 SER A CB    1 
ATOM   9986  O  OG    . SER A 1 2724 ? 156.426 182.163 177.465 1.00 70.06  ? 2724 SER A OG    1 
ATOM   9987  N  N     . HIS A 1 2725 ? 156.210 181.708 181.359 1.00 65.33  ? 2725 HIS A N     1 
ATOM   9988  C  CA    . HIS A 1 2725 ? 155.710 182.641 182.363 1.00 64.08  ? 2725 HIS A CA    1 
ATOM   9989  C  C     . HIS A 1 2725 ? 155.759 184.080 181.870 1.00 62.27  ? 2725 HIS A C     1 
ATOM   9990  O  O     . HIS A 1 2725 ? 154.980 184.919 182.335 1.00 66.47  ? 2725 HIS A O     1 
ATOM   9991  C  CB    . HIS A 1 2725 ? 156.504 182.496 183.659 1.00 67.02  ? 2725 HIS A CB    1 
ATOM   9992  C  CG    . HIS A 1 2725 ? 156.080 181.333 184.498 1.00 69.95  ? 2725 HIS A CG    1 
ATOM   9993  N  ND1   . HIS A 1 2725 ? 156.684 181.018 185.696 1.00 72.48  ? 2725 HIS A ND1   1 
ATOM   9994  C  CD2   . HIS A 1 2725 ? 155.110 180.407 184.312 1.00 64.86  ? 2725 HIS A CD2   1 
ATOM   9995  C  CE1   . HIS A 1 2725 ? 156.105 179.949 186.211 1.00 70.05  ? 2725 HIS A CE1   1 
ATOM   9996  N  NE2   . HIS A 1 2725 ? 155.147 179.558 185.391 1.00 68.68  ? 2725 HIS A NE2   1 
ATOM   9997  N  N     . ARG A 1 2726 ? 156.663 184.387 180.939 1.00 50.09  ? 2726 ARG A N     1 
ATOM   9998  C  CA    . ARG A 1 2726 ? 156.699 185.726 180.364 1.00 59.16  ? 2726 ARG A CA    1 
ATOM   9999  C  C     . ARG A 1 2726 ? 155.481 185.975 179.483 1.00 61.40  ? 2726 ARG A C     1 
ATOM   10000 O  O     . ARG A 1 2726 ? 154.980 187.102 179.406 1.00 70.03  ? 2726 ARG A O     1 
ATOM   10001 C  CB    . ARG A 1 2726 ? 157.989 185.921 179.570 1.00 59.28  ? 2726 ARG A CB    1 
ATOM   10002 C  CG    . ARG A 1 2726 ? 159.248 185.632 180.369 1.00 60.04  ? 2726 ARG A CG    1 
ATOM   10003 C  CD    . ARG A 1 2726 ? 160.495 185.947 179.565 1.00 60.64  ? 2726 ARG A CD    1 
ATOM   10004 N  NE    . ARG A 1 2726 ? 161.048 187.251 179.905 1.00 56.97  ? 2726 ARG A NE    1 
ATOM   10005 C  CZ    . ARG A 1 2726 ? 162.067 187.817 179.275 1.00 57.40  ? 2726 ARG A CZ    1 
ATOM   10006 N  NH1   . ARG A 1 2726 ? 162.671 187.220 178.261 1.00 64.19  ? 2726 ARG A NH1   1 
ATOM   10007 N  NH2   . ARG A 1 2726 ? 162.492 189.013 179.673 1.00 58.25  ? 2726 ARG A NH2   1 
ATOM   10008 N  N     . PHE A 1 2727 ? 154.995 184.934 178.803 1.00 46.14  ? 2727 PHE A N     1 
ATOM   10009 C  CA    . PHE A 1 2727 ? 153.789 185.081 177.996 1.00 40.61  ? 2727 PHE A CA    1 
ATOM   10010 C  C     . PHE A 1 2727 ? 152.542 185.152 178.868 1.00 49.15  ? 2727 PHE A C     1 
ATOM   10011 O  O     . PHE A 1 2727 ? 151.644 185.960 178.609 1.00 61.33  ? 2727 PHE A O     1 
ATOM   10012 C  CB    . PHE A 1 2727 ? 153.677 183.930 176.999 1.00 47.80  ? 2727 PHE A CB    1 
ATOM   10013 C  CG    . PHE A 1 2727 ? 152.398 183.933 176.220 1.00 45.12  ? 2727 PHE A CG    1 
ATOM   10014 C  CD1   . PHE A 1 2727 ? 152.079 184.996 175.397 1.00 46.49  ? 2727 PHE A CD1   1 
ATOM   10015 C  CD2   . PHE A 1 2727 ? 151.512 182.876 176.313 1.00 47.19  ? 2727 PHE A CD2   1 
ATOM   10016 C  CE1   . PHE A 1 2727 ? 150.902 185.004 174.682 1.00 46.18  ? 2727 PHE A CE1   1 
ATOM   10017 C  CE2   . PHE A 1 2727 ? 150.334 182.879 175.599 1.00 46.99  ? 2727 PHE A CE2   1 
ATOM   10018 C  CZ    . PHE A 1 2727 ? 150.029 183.945 174.782 1.00 45.26  ? 2727 PHE A CZ    1 
ATOM   10019 N  N     . LEU A 1 2728 ? 152.468 184.315 179.905 1.00 58.30  ? 2728 LEU A N     1 
ATOM   10020 C  CA    . LEU A 1 2728 ? 151.301 184.306 180.780 1.00 51.29  ? 2728 LEU A CA    1 
ATOM   10021 C  C     . LEU A 1 2728 ? 151.173 185.587 181.592 1.00 55.50  ? 2728 LEU A C     1 
ATOM   10022 O  O     . LEU A 1 2728 ? 150.111 185.832 182.173 1.00 59.52  ? 2728 LEU A O     1 
ATOM   10023 C  CB    . LEU A 1 2728 ? 151.358 183.104 181.720 1.00 54.78  ? 2728 LEU A CB    1 
ATOM   10024 C  CG    . LEU A 1 2728 ? 150.945 181.758 181.128 1.00 59.10  ? 2728 LEU A CG    1 
ATOM   10025 C  CD1   . LEU A 1 2728 ? 150.946 180.687 182.204 1.00 60.73  ? 2728 LEU A CD1   1 
ATOM   10026 C  CD2   . LEU A 1 2728 ? 149.581 181.862 180.469 1.00 52.70  ? 2728 LEU A CD2   1 
ATOM   10027 N  N     . ARG A 1 2729 ? 152.228 186.400 181.650 1.00 57.45  ? 2729 ARG A N     1 
ATOM   10028 C  CA    . ARG A 1 2729 ? 152.161 187.653 182.394 1.00 55.83  ? 2729 ARG A CA    1 
ATOM   10029 C  C     . ARG A 1 2729 ? 151.127 188.602 181.803 1.00 58.97  ? 2729 ARG A C     1 
ATOM   10030 O  O     . ARG A 1 2729 ? 150.451 189.324 182.545 1.00 63.78  ? 2729 ARG A O     1 
ATOM   10031 C  CB    . ARG A 1 2729 ? 153.544 188.307 182.424 1.00 51.18  ? 2729 ARG A CB    1 
ATOM   10032 C  CG    . ARG A 1 2729 ? 153.548 189.778 182.795 1.00 55.83  ? 2729 ARG A CG    1 
ATOM   10033 C  CD    . ARG A 1 2729 ? 154.938 190.374 182.650 1.00 50.04  ? 2729 ARG A CD    1 
ATOM   10034 N  NE    . ARG A 1 2729 ? 154.927 191.822 182.810 1.00 54.18  ? 2729 ARG A NE    1 
ATOM   10035 C  CZ    . ARG A 1 2729 ? 155.424 192.678 181.928 1.00 62.58  ? 2729 ARG A CZ    1 
ATOM   10036 N  NH1   . ARG A 1 2729 ? 156.003 192.265 180.814 1.00 58.79  ? 2729 ARG A NH1   1 
ATOM   10037 N  NH2   . ARG A 1 2729 ? 155.343 193.983 182.174 1.00 64.01  ? 2729 ARG A NH2   1 
ATOM   10038 N  N     . HIS A 1 2730 ? 150.976 188.604 180.481 1.00 56.12  ? 2730 HIS A N     1 
ATOM   10039 C  CA    . HIS A 1 2730 ? 150.085 189.538 179.807 1.00 54.92  ? 2730 HIS A CA    1 
ATOM   10040 C  C     . HIS A 1 2730 ? 148.681 188.994 179.588 1.00 55.46  ? 2730 HIS A C     1 
ATOM   10041 O  O     . HIS A 1 2730 ? 147.756 189.788 179.385 1.00 66.13  ? 2730 HIS A O     1 
ATOM   10042 C  CB    . HIS A 1 2730 ? 150.675 189.941 178.453 1.00 52.23  ? 2730 HIS A CB    1 
ATOM   10043 C  CG    . HIS A 1 2730 ? 152.081 190.441 178.533 1.00 57.07  ? 2730 HIS A CG    1 
ATOM   10044 N  ND1   . HIS A 1 2730 ? 153.168 189.656 178.217 1.00 62.56  ? 2730 HIS A ND1   1 
ATOM   10045 C  CD2   . HIS A 1 2730 ? 152.579 191.648 178.891 1.00 59.43  ? 2730 HIS A CD2   1 
ATOM   10046 C  CE1   . HIS A 1 2730 ? 154.276 190.356 178.379 1.00 59.98  ? 2730 HIS A CE1   1 
ATOM   10047 N  NE2   . HIS A 1 2730 ? 153.946 191.568 178.787 1.00 59.30  ? 2730 HIS A NE2   1 
ATOM   10048 N  N     . VAL A 1 2731 ? 148.490 187.680 179.620 1.00 42.31  ? 2731 VAL A N     1 
ATOM   10049 C  CA    . VAL A 1 2731 ? 147.202 187.103 179.243 1.00 49.23  ? 2731 VAL A CA    1 
ATOM   10050 C  C     . VAL A 1 2731 ? 146.479 186.527 180.458 1.00 54.47  ? 2731 VAL A C     1 
ATOM   10051 O  O     . VAL A 1 2731 ? 146.975 185.590 181.100 1.00 61.98  ? 2731 VAL A O     1 
ATOM   10052 C  CB    . VAL A 1 2731 ? 147.375 186.055 178.129 1.00 48.95  ? 2731 VAL A CB    1 
ATOM   10053 C  CG1   . VAL A 1 2731 ? 147.884 186.724 176.867 1.00 57.86  ? 2731 VAL A CG1   1 
ATOM   10054 C  CG2   . VAL A 1 2731 ? 148.350 184.963 178.544 1.00 48.29  ? 2731 VAL A CG2   1 
ATOM   10055 N  N     . PRO A 1 2732 ? 145.329 187.083 180.834 1.00 44.37  ? 2732 PRO A N     1 
ATOM   10056 C  CA    . PRO A 1 2732 ? 144.479 186.412 181.822 1.00 43.71  ? 2732 PRO A CA    1 
ATOM   10057 C  C     . PRO A 1 2732 ? 143.989 185.073 181.295 1.00 50.61  ? 2732 PRO A C     1 
ATOM   10058 O  O     . PRO A 1 2732 ? 143.801 184.889 180.091 1.00 58.64  ? 2732 PRO A O     1 
ATOM   10059 C  CB    . PRO A 1 2732 ? 143.319 187.395 182.022 1.00 52.99  ? 2732 PRO A CB    1 
ATOM   10060 C  CG    . PRO A 1 2732 ? 143.410 188.360 180.879 1.00 53.23  ? 2732 PRO A CG    1 
ATOM   10061 C  CD    . PRO A 1 2732 ? 144.857 188.443 180.541 1.00 50.26  ? 2732 PRO A CD    1 
ATOM   10062 N  N     . VAL A 1 2733 ? 143.784 184.131 182.211 1.00 54.80  ? 2733 VAL A N     1 
ATOM   10063 C  CA    . VAL A 1 2733 ? 143.320 182.792 181.875 1.00 53.41  ? 2733 VAL A CA    1 
ATOM   10064 C  C     . VAL A 1 2733 ? 142.015 182.533 182.613 1.00 51.76  ? 2733 VAL A C     1 
ATOM   10065 O  O     . VAL A 1 2733 ? 141.942 182.702 183.835 1.00 63.26  ? 2733 VAL A O     1 
ATOM   10066 C  CB    . VAL A 1 2733 ? 144.369 181.722 182.227 1.00 46.78  ? 2733 VAL A CB    1 
ATOM   10067 C  CG1   . VAL A 1 2733 ? 143.769 180.332 182.110 1.00 46.59  ? 2733 VAL A CG1   1 
ATOM   10068 C  CG2   . VAL A 1 2733 ? 145.580 181.857 181.323 1.00 51.10  ? 2733 VAL A CG2   1 
ATOM   10069 N  N     . VAL A 1 2734 ? 140.989 182.127 181.870 1.00 36.12  ? 2734 VAL A N     1 
ATOM   10070 C  CA    . VAL A 1 2734 ? 139.703 181.734 182.430 1.00 37.53  ? 2734 VAL A CA    1 
ATOM   10071 C  C     . VAL A 1 2734 ? 139.506 180.250 182.158 1.00 47.52  ? 2734 VAL A C     1 
ATOM   10072 O  O     . VAL A 1 2734 ? 139.688 179.791 181.024 1.00 60.36  ? 2734 VAL A O     1 
ATOM   10073 C  CB    . VAL A 1 2734 ? 138.546 182.571 181.854 1.00 44.90  ? 2734 VAL A CB    1 
ATOM   10074 C  CG1   . VAL A 1 2734 ? 138.574 182.567 180.335 1.00 51.92  ? 2734 VAL A CG1   1 
ATOM   10075 C  CG2   . VAL A 1 2734 ? 137.212 182.052 182.361 1.00 47.78  ? 2734 VAL A CG2   1 
ATOM   10076 N  N     . TYR A 1 2735 ? 139.158 179.500 183.199 1.00 53.54  ? 2735 TYR A N     1 
ATOM   10077 C  CA    . TYR A 1 2735 ? 139.039 178.049 183.108 1.00 47.60  ? 2735 TYR A CA    1 
ATOM   10078 C  C     . TYR A 1 2735 ? 137.587 177.687 182.823 1.00 54.92  ? 2735 TYR A C     1 
ATOM   10079 O  O     . TYR A 1 2735 ? 136.720 177.835 183.690 1.00 67.10  ? 2735 TYR A O     1 
ATOM   10080 C  CB    . TYR A 1 2735 ? 139.527 177.391 184.395 1.00 55.68  ? 2735 TYR A CB    1 
ATOM   10081 C  CG    . TYR A 1 2735 ? 139.380 175.889 184.411 1.00 58.05  ? 2735 TYR A CG    1 
ATOM   10082 C  CD1   . TYR A 1 2735 ? 139.837 175.116 183.354 1.00 59.49  ? 2735 TYR A CD1   1 
ATOM   10083 C  CD2   . TYR A 1 2735 ? 138.794 175.242 185.489 1.00 63.67  ? 2735 TYR A CD2   1 
ATOM   10084 C  CE1   . TYR A 1 2735 ? 139.708 173.742 183.367 1.00 61.14  ? 2735 TYR A CE1   1 
ATOM   10085 C  CE2   . TYR A 1 2735 ? 138.661 173.869 185.510 1.00 63.94  ? 2735 TYR A CE2   1 
ATOM   10086 C  CZ    . TYR A 1 2735 ? 139.121 173.124 184.447 1.00 63.22  ? 2735 TYR A CZ    1 
ATOM   10087 O  OH    . TYR A 1 2735 ? 138.990 171.756 184.465 1.00 67.12  ? 2735 TYR A OH    1 
ATOM   10088 N  N     . VAL A 1 2736 ? 137.324 177.211 181.610 1.00 49.70  ? 2736 VAL A N     1 
ATOM   10089 C  CA    . VAL A 1 2736 ? 135.994 176.778 181.201 1.00 44.24  ? 2736 VAL A CA    1 
ATOM   10090 C  C     . VAL A 1 2736 ? 135.970 175.259 181.316 1.00 58.22  ? 2736 VAL A C     1 
ATOM   10091 O  O     . VAL A 1 2736 ? 136.521 174.550 180.470 1.00 61.49  ? 2736 VAL A O     1 
ATOM   10092 C  CB    . VAL A 1 2736 ? 135.653 177.247 179.785 1.00 39.02  ? 2736 VAL A CB    1 
ATOM   10093 C  CG1   . VAL A 1 2736 ? 134.178 177.036 179.504 1.00 47.02  ? 2736 VAL A CG1   1 
ATOM   10094 C  CG2   . VAL A 1 2736 ? 136.028 178.707 179.610 1.00 58.33  ? 2736 VAL A CG2   1 
ATOM   10095 N  N     . ASP A 1 2737 ? 135.331 174.755 182.365 1.00 66.30  ? 2737 ASP A N     1 
ATOM   10096 C  CA    . ASP A 1 2737 ? 135.255 173.325 182.612 1.00 60.06  ? 2737 ASP A CA    1 
ATOM   10097 C  C     . ASP A 1 2737 ? 133.977 172.750 182.006 1.00 64.61  ? 2737 ASP A C     1 
ATOM   10098 O  O     . ASP A 1 2737 ? 133.123 173.474 181.488 1.00 78.62  ? 2737 ASP A O     1 
ATOM   10099 C  CB    . ASP A 1 2737 ? 135.318 173.043 184.113 1.00 64.96  ? 2737 ASP A CB    1 
ATOM   10100 C  CG    . ASP A 1 2737 ? 135.771 171.631 184.424 1.00 77.08  ? 2737 ASP A CG    1 
ATOM   10101 O  OD1   . ASP A 1 2737 ? 136.001 170.858 183.471 1.00 77.80  ? 2737 ASP A OD1   1 
ATOM   10102 O  OD2   . ASP A 1 2737 ? 135.899 171.296 185.620 1.00 75.09  ? 2737 ASP A OD2   1 
ATOM   10103 N  N     . TYR A 1 2738 ? 133.856 171.427 182.067 1.00 57.30  ? 2738 TYR A N     1 
ATOM   10104 C  CA    . TYR A 1 2738 ? 132.678 170.767 181.527 1.00 56.81  ? 2738 TYR A CA    1 
ATOM   10105 C  C     . TYR A 1 2738 ? 131.429 171.234 182.269 1.00 65.60  ? 2738 TYR A C     1 
ATOM   10106 O  O     . TYR A 1 2738 ? 131.472 171.441 183.488 1.00 73.51  ? 2738 TYR A O     1 
ATOM   10107 C  CB    . TYR A 1 2738 ? 132.795 169.247 181.647 1.00 57.73  ? 2738 TYR A CB    1 
ATOM   10108 C  CG    . TYR A 1 2738 ? 133.685 168.591 180.622 1.00 57.90  ? 2738 TYR A CG    1 
ATOM   10109 C  CD1   . TYR A 1 2738 ? 133.336 168.576 179.281 1.00 60.11  ? 2738 TYR A CD1   1 
ATOM   10110 C  CD2   . TYR A 1 2738 ? 134.854 167.952 181.001 1.00 60.13  ? 2738 TYR A CD2   1 
ATOM   10111 C  CE1   . TYR A 1 2738 ? 134.141 167.966 178.343 1.00 59.52  ? 2738 TYR A CE1   1 
ATOM   10112 C  CE2   . TYR A 1 2738 ? 135.662 167.336 180.072 1.00 63.15  ? 2738 TYR A CE2   1 
ATOM   10113 C  CZ    . TYR A 1 2738 ? 135.303 167.348 178.744 1.00 62.13  ? 2738 TYR A CZ    1 
ATOM   10114 O  OH    . TYR A 1 2738 ? 136.110 166.735 177.814 1.00 69.99  ? 2738 TYR A OH    1 
ATOM   10115 N  N     . PRO A 1 2739 ? 130.312 171.425 181.572 1.00 65.76  ? 2739 PRO A N     1 
ATOM   10116 C  CA    . PRO A 1 2739 ? 129.053 171.696 182.272 1.00 64.37  ? 2739 PRO A CA    1 
ATOM   10117 C  C     . PRO A 1 2739 ? 128.689 170.538 183.188 1.00 65.03  ? 2739 PRO A C     1 
ATOM   10118 O  O     . PRO A 1 2739 ? 128.902 169.370 182.858 1.00 59.09  ? 2739 PRO A O     1 
ATOM   10119 C  CB    . PRO A 1 2739 ? 128.040 171.858 181.134 1.00 61.27  ? 2739 PRO A CB    1 
ATOM   10120 C  CG    . PRO A 1 2739 ? 128.861 172.220 179.942 1.00 61.33  ? 2739 PRO A CG    1 
ATOM   10121 C  CD    . PRO A 1 2739 ? 130.163 171.499 180.110 1.00 62.83  ? 2739 PRO A CD    1 
ATOM   10122 N  N     . GLY A 1 2740 ? 128.139 170.872 184.351 1.00 78.73  ? 2740 GLY A N     1 
ATOM   10123 C  CA    . GLY A 1 2740 ? 127.767 169.875 185.323 1.00 77.94  ? 2740 GLY A CA    1 
ATOM   10124 C  C     . GLY A 1 2740 ? 126.550 169.090 184.884 1.00 81.32  ? 2740 GLY A C     1 
ATOM   10125 O  O     . GLY A 1 2740 ? 125.882 169.435 183.905 1.00 83.45  ? 2740 GLY A O     1 
ATOM   10126 N  N     . PRO A 1 2741 ? 126.247 168.000 185.596 1.00 80.01  ? 2741 PRO A N     1 
ATOM   10127 C  CA    . PRO A 1 2741 ? 125.048 167.220 185.248 1.00 75.89  ? 2741 PRO A CA    1 
ATOM   10128 C  C     . PRO A 1 2741 ? 123.773 168.042 185.281 1.00 78.12  ? 2741 PRO A C     1 
ATOM   10129 O  O     . PRO A 1 2741 ? 122.888 167.833 184.444 1.00 84.99  ? 2741 PRO A O     1 
ATOM   10130 C  CB    . PRO A 1 2741 ? 125.041 166.107 186.304 1.00 76.44  ? 2741 PRO A CB    1 
ATOM   10131 C  CG    . PRO A 1 2741 ? 126.468 165.975 186.718 1.00 77.03  ? 2741 PRO A CG    1 
ATOM   10132 C  CD    . PRO A 1 2741 ? 127.033 167.365 186.666 1.00 79.12  ? 2741 PRO A CD    1 
ATOM   10133 N  N     . ALA A 1 2742 ? 123.656 168.983 186.219 1.00 77.41  ? 2742 ALA A N     1 
ATOM   10134 C  CA    . ALA A 1 2742 ? 122.496 169.867 186.232 1.00 81.27  ? 2742 ALA A CA    1 
ATOM   10135 C  C     . ALA A 1 2742 ? 122.510 170.814 185.038 1.00 85.62  ? 2742 ALA A C     1 
ATOM   10136 O  O     . ALA A 1 2742 ? 121.471 171.041 184.406 1.00 88.92  ? 2742 ALA A O     1 
ATOM   10137 C  CB    . ALA A 1 2742 ? 122.447 170.652 187.542 1.00 85.38  ? 2742 ALA A CB    1 
ATOM   10138 N  N     . SER A 1 2743 ? 123.677 171.377 184.715 1.00 75.00  ? 2743 SER A N     1 
ATOM   10139 C  CA    . SER A 1 2743 ? 123.774 172.260 183.556 1.00 74.47  ? 2743 SER A CA    1 
ATOM   10140 C  C     . SER A 1 2743 ? 123.499 171.505 182.262 1.00 81.20  ? 2743 SER A C     1 
ATOM   10141 O  O     . SER A 1 2743 ? 122.785 172.006 181.384 1.00 86.46  ? 2743 SER A O     1 
ATOM   10142 C  CB    . SER A 1 2743 ? 125.153 172.916 183.512 1.00 80.45  ? 2743 SER A CB    1 
ATOM   10143 O  OG    . SER A 1 2743 ? 125.272 173.772 182.389 1.00 85.96  ? 2743 SER A OG    1 
ATOM   10144 N  N     . LEU A 1 2744 ? 124.062 170.301 182.124 1.00 70.63  ? 2744 LEU A N     1 
ATOM   10145 C  CA    . LEU A 1 2744 ? 123.781 169.485 180.948 1.00 63.72  ? 2744 LEU A CA    1 
ATOM   10146 C  C     . LEU A 1 2744 ? 122.302 169.146 180.866 1.00 65.80  ? 2744 LEU A C     1 
ATOM   10147 O  O     . LEU A 1 2744 ? 121.703 169.193 179.783 1.00 73.10  ? 2744 LEU A O     1 
ATOM   10148 C  CB    . LEU A 1 2744 ? 124.618 168.208 180.980 1.00 63.24  ? 2744 LEU A CB    1 
ATOM   10149 C  CG    . LEU A 1 2744 ? 126.100 168.333 180.632 1.00 68.14  ? 2744 LEU A CG    1 
ATOM   10150 C  CD1   . LEU A 1 2744 ? 126.767 166.971 180.693 1.00 72.75  ? 2744 LEU A CD1   1 
ATOM   10151 C  CD2   . LEU A 1 2744 ? 126.283 168.961 179.263 1.00 61.01  ? 2744 LEU A CD2   1 
ATOM   10152 N  N     . THR A 1 2745 ? 121.696 168.799 182.004 1.00 68.50  ? 2745 THR A N     1 
ATOM   10153 C  CA    . THR A 1 2745 ? 120.271 168.500 182.025 1.00 66.00  ? 2745 THR A CA    1 
ATOM   10154 C  C     . THR A 1 2745 ? 119.463 169.694 181.545 1.00 66.84  ? 2745 THR A C     1 
ATOM   10155 O  O     . THR A 1 2745 ? 118.578 169.551 180.700 1.00 79.66  ? 2745 THR A O     1 
ATOM   10156 C  CB    . THR A 1 2745 ? 119.837 168.089 183.432 1.00 71.21  ? 2745 THR A CB    1 
ATOM   10157 O  OG1   . THR A 1 2745 ? 120.645 166.996 183.885 1.00 80.80  ? 2745 THR A OG1   1 
ATOM   10158 C  CG2   . THR A 1 2745 ? 118.377 167.670 183.435 1.00 71.30  ? 2745 THR A CG2   1 
ATOM   10159 N  N     . GLN A 1 2746 ? 119.782 170.889 182.043 1.00 64.67  ? 2746 GLN A N     1 
ATOM   10160 C  CA    . GLN A 1 2746 ? 119.059 172.084 181.616 1.00 69.39  ? 2746 GLN A CA    1 
ATOM   10161 C  C     . GLN A 1 2746 ? 119.208 172.310 180.116 1.00 71.05  ? 2746 GLN A C     1 
ATOM   10162 O  O     . GLN A 1 2746 ? 118.211 172.445 179.392 1.00 73.86  ? 2746 GLN A O     1 
ATOM   10163 C  CB    . GLN A 1 2746 ? 119.558 173.304 182.390 1.00 70.73  ? 2746 GLN A CB    1 
ATOM   10164 C  CG    . GLN A 1 2746 ? 119.119 174.632 181.793 1.00 78.08  ? 2746 GLN A CG    1 
ATOM   10165 C  CD    . GLN A 1 2746 ? 119.567 175.823 182.617 1.00 83.61  ? 2746 GLN A CD    1 
ATOM   10166 O  OE1   . GLN A 1 2746 ? 120.187 175.667 183.669 1.00 82.65  ? 2746 GLN A OE1   1 
ATOM   10167 N  NE2   . GLN A 1 2746 ? 119.254 177.023 182.142 1.00 78.97  ? 2746 GLN A NE2   1 
ATOM   10168 N  N     . ILE A 1 2747 ? 120.452 172.326 179.628 1.00 68.58  ? 2747 ILE A N     1 
ATOM   10169 C  CA    . ILE A 1 2747 ? 120.703 172.660 178.227 1.00 67.42  ? 2747 ILE A CA    1 
ATOM   10170 C  C     . ILE A 1 2747 ? 120.007 171.666 177.308 1.00 70.30  ? 2747 ILE A C     1 
ATOM   10171 O  O     . ILE A 1 2747 ? 119.267 172.047 176.391 1.00 76.26  ? 2747 ILE A O     1 
ATOM   10172 C  CB    . ILE A 1 2747 ? 122.215 172.709 177.944 1.00 58.58  ? 2747 ILE A CB    1 
ATOM   10173 C  CG1   . ILE A 1 2747 ? 122.897 173.761 178.814 1.00 67.14  ? 2747 ILE A CG1   1 
ATOM   10174 C  CG2   . ILE A 1 2747 ? 122.470 172.993 176.476 1.00 61.35  ? 2747 ILE A CG2   1 
ATOM   10175 C  CD1   . ILE A 1 2747 ? 124.392 173.574 178.923 1.00 59.19  ? 2747 ILE A CD1   1 
ATOM   10176 N  N     . TYR A 1 2748 ? 120.211 170.373 177.549 1.00 66.34  ? 2748 TYR A N     1 
ATOM   10177 C  CA    . TYR A 1 2748 ? 119.705 169.400 176.597 1.00 63.50  ? 2748 TYR A CA    1 
ATOM   10178 C  C     . TYR A 1 2748 ? 118.247 169.041 176.838 1.00 65.78  ? 2748 TYR A C     1 
ATOM   10179 O  O     . TYR A 1 2748 ? 117.590 168.571 175.908 1.00 75.50  ? 2748 TYR A O     1 
ATOM   10180 C  CB    . TYR A 1 2748 ? 120.610 168.172 176.597 1.00 56.87  ? 2748 TYR A CB    1 
ATOM   10181 C  CG    . TYR A 1 2748 ? 121.960 168.530 176.025 1.00 64.49  ? 2748 TYR A CG    1 
ATOM   10182 C  CD1   . TYR A 1 2748 ? 122.114 168.770 174.667 1.00 67.26  ? 2748 TYR A CD1   1 
ATOM   10183 C  CD2   . TYR A 1 2748 ? 123.067 168.685 176.845 1.00 73.14  ? 2748 TYR A CD2   1 
ATOM   10184 C  CE1   . TYR A 1 2748 ? 123.337 169.122 174.138 1.00 66.00  ? 2748 TYR A CE1   1 
ATOM   10185 C  CE2   . TYR A 1 2748 ? 124.296 169.038 176.323 1.00 70.28  ? 2748 TYR A CE2   1 
ATOM   10186 C  CZ    . TYR A 1 2748 ? 124.423 169.258 174.970 1.00 67.72  ? 2748 TYR A CZ    1 
ATOM   10187 O  OH    . TYR A 1 2748 ? 125.645 169.605 174.445 1.00 72.81  ? 2748 TYR A OH    1 
ATOM   10188 N  N     . GLY A 1 2749 ? 117.697 169.325 178.020 1.00 66.01  ? 2749 GLY A N     1 
ATOM   10189 C  CA    . GLY A 1 2749 ? 116.255 169.299 178.167 1.00 68.82  ? 2749 GLY A CA    1 
ATOM   10190 C  C     . GLY A 1 2749 ? 115.592 170.406 177.374 1.00 75.77  ? 2749 GLY A C     1 
ATOM   10191 O  O     . GLY A 1 2749 ? 114.558 170.188 176.739 1.00 78.37  ? 2749 GLY A O     1 
ATOM   10192 N  N     . THR A 1 2750 ? 116.184 171.604 177.383 1.00 72.83  ? 2750 THR A N     1 
ATOM   10193 C  CA    . THR A 1 2750 ? 115.679 172.674 176.528 1.00 73.17  ? 2750 THR A CA    1 
ATOM   10194 C  C     . THR A 1 2750 ? 115.772 172.282 175.058 1.00 75.82  ? 2750 THR A C     1 
ATOM   10195 O  O     . THR A 1 2750 ? 114.822 172.476 174.286 1.00 83.75  ? 2750 THR A O     1 
ATOM   10196 C  CB    . THR A 1 2750 ? 116.451 173.967 176.789 1.00 68.16  ? 2750 THR A CB    1 
ATOM   10197 O  OG1   . THR A 1 2750 ? 116.334 174.327 178.170 1.00 77.29  ? 2750 THR A OG1   1 
ATOM   10198 C  CG2   . THR A 1 2750 ? 115.904 175.094 175.930 1.00 69.72  ? 2750 THR A CG2   1 
ATOM   10199 N  N     . PHE A 1 2751 ? 116.910 171.711 174.659 1.00 60.43  ? 2751 PHE A N     1 
ATOM   10200 C  CA    . PHE A 1 2751 ? 117.083 171.302 173.267 1.00 55.79  ? 2751 PHE A CA    1 
ATOM   10201 C  C     . PHE A 1 2751 ? 116.076 170.229 172.868 1.00 62.04  ? 2751 PHE A C     1 
ATOM   10202 O  O     . PHE A 1 2751 ? 115.496 170.290 171.780 1.00 72.08  ? 2751 PHE A O     1 
ATOM   10203 C  CB    . PHE A 1 2751 ? 118.511 170.812 173.034 1.00 59.76  ? 2751 PHE A CB    1 
ATOM   10204 C  CG    . PHE A 1 2751 ? 119.471 171.904 172.669 1.00 63.04  ? 2751 PHE A CG    1 
ATOM   10205 C  CD1   . PHE A 1 2751 ? 119.055 172.978 171.903 1.00 67.72  ? 2751 PHE A CD1   1 
ATOM   10206 C  CD2   . PHE A 1 2751 ? 120.789 171.856 173.085 1.00 60.35  ? 2751 PHE A CD2   1 
ATOM   10207 C  CE1   . PHE A 1 2751 ? 119.932 173.985 171.562 1.00 64.95  ? 2751 PHE A CE1   1 
ATOM   10208 C  CE2   . PHE A 1 2751 ? 121.672 172.859 172.747 1.00 64.98  ? 2751 PHE A CE2   1 
ATOM   10209 C  CZ    . PHE A 1 2751 ? 121.242 173.925 171.984 1.00 68.23  ? 2751 PHE A CZ    1 
ATOM   10210 N  N     . ASN A 1 2752 ? 115.854 169.236 173.734 1.00 62.00  ? 2752 ASN A N     1 
ATOM   10211 C  CA    . ASN A 1 2752 ? 114.903 168.176 173.420 1.00 61.86  ? 2752 ASN A CA    1 
ATOM   10212 C  C     . ASN A 1 2752 ? 113.474 168.702 173.379 1.00 67.04  ? 2752 ASN A C     1 
ATOM   10213 O  O     . ASN A 1 2752 ? 112.694 168.321 172.500 1.00 77.59  ? 2752 ASN A O     1 
ATOM   10214 C  CB    . ASN A 1 2752 ? 115.030 167.043 174.437 1.00 63.61  ? 2752 ASN A CB    1 
ATOM   10215 C  CG    . ASN A 1 2752 ? 116.293 166.230 174.244 1.00 63.86  ? 2752 ASN A CG    1 
ATOM   10216 O  OD1   . ASN A 1 2752 ? 116.599 165.342 175.037 1.00 69.77  ? 2752 ASN A OD1   1 
ATOM   10217 N  ND2   . ASN A 1 2752 ? 117.034 166.530 173.185 1.00 64.43  ? 2752 ASN A ND2   1 
ATOM   10218 N  N     . ARG A 1 2753 ? 113.110 169.574 174.324 1.00 67.67  ? 2753 ARG A N     1 
ATOM   10219 C  CA    . ARG A 1 2753 ? 111.767 170.142 174.325 1.00 72.29  ? 2753 ARG A CA    1 
ATOM   10220 C  C     . ARG A 1 2753 ? 111.516 170.950 173.061 1.00 73.99  ? 2753 ARG A C     1 
ATOM   10221 O  O     . ARG A 1 2753 ? 110.421 170.899 172.490 1.00 78.89  ? 2753 ARG A O     1 
ATOM   10222 C  CB    . ARG A 1 2753 ? 111.566 171.007 175.568 1.00 71.41  ? 2753 ARG A CB    1 
ATOM   10223 C  CG    . ARG A 1 2753 ? 110.937 170.271 176.736 1.00 74.04  ? 2753 ARG A CG    1 
ATOM   10224 C  CD    . ARG A 1 2753 ? 110.639 171.218 177.883 1.00 76.87  ? 2753 ARG A CD    1 
ATOM   10225 N  NE    . ARG A 1 2753 ? 111.811 171.440 178.720 1.00 80.17  ? 2753 ARG A NE    1 
ATOM   10226 C  CZ    . ARG A 1 2753 ? 112.473 172.586 178.790 1.00 77.56  ? 2753 ARG A CZ    1 
ATOM   10227 N  NH1   . ARG A 1 2753 ? 112.103 173.642 178.083 1.00 73.58  ? 2753 ARG A NH1   1 
ATOM   10228 N  NH2   . ARG A 1 2753 ? 113.532 172.677 179.589 1.00 74.34  ? 2753 ARG A NH2   1 
ATOM   10229 N  N     . ALA A 1 2754 ? 112.518 171.707 172.609 1.00 75.07  ? 2754 ALA A N     1 
ATOM   10230 C  CA    . ALA A 1 2754 ? 112.386 172.405 171.335 1.00 77.41  ? 2754 ALA A CA    1 
ATOM   10231 C  C     . ALA A 1 2754 ? 112.299 171.420 170.174 1.00 79.41  ? 2754 ALA A C     1 
ATOM   10232 O  O     . ALA A 1 2754 ? 111.556 171.646 169.212 1.00 81.68  ? 2754 ALA A O     1 
ATOM   10233 C  CB    . ALA A 1 2754 ? 113.558 173.365 171.139 1.00 80.82  ? 2754 ALA A CB    1 
ATOM   10234 N  N     . MET A 1 2755 ? 113.054 170.322 170.247 1.00 76.14  ? 2755 MET A N     1 
ATOM   10235 C  CA    . MET A 1 2755 ? 113.098 169.367 169.144 1.00 72.69  ? 2755 MET A CA    1 
ATOM   10236 C  C     . MET A 1 2755 ? 111.831 168.522 169.078 1.00 74.25  ? 2755 MET A C     1 
ATOM   10237 O  O     . MET A 1 2755 ? 111.311 168.260 167.987 1.00 79.44  ? 2755 MET A O     1 
ATOM   10238 C  CB    . MET A 1 2755 ? 114.333 168.476 169.281 1.00 67.59  ? 2755 MET A CB    1 
ATOM   10239 C  CG    . MET A 1 2755 ? 114.189 167.094 168.672 1.00 68.09  ? 2755 MET A CG    1 
ATOM   10240 S  SD    . MET A 1 2755 ? 115.648 166.075 168.951 1.00 81.34  ? 2755 MET A SD    1 
ATOM   10241 C  CE    . MET A 1 2755 ? 115.239 165.327 170.526 1.00 74.08  ? 2755 MET A CE    1 
ATOM   10242 N  N     . LEU A 1 2756 ? 111.312 168.097 170.228 1.00 74.09  ? 2756 LEU A N     1 
ATOM   10243 C  CA    . LEU A 1 2756 ? 110.189 167.168 170.252 1.00 72.35  ? 2756 LEU A CA    1 
ATOM   10244 C  C     . LEU A 1 2756 ? 108.848 167.834 169.978 1.00 76.92  ? 2756 LEU A C     1 
ATOM   10245 O  O     . LEU A 1 2756 ? 107.815 167.163 170.072 1.00 83.15  ? 2756 LEU A O     1 
ATOM   10246 C  CB    . LEU A 1 2756 ? 110.138 166.439 171.597 1.00 69.15  ? 2756 LEU A CB    1 
ATOM   10247 C  CG    . LEU A 1 2756 ? 111.121 165.276 171.737 1.00 68.17  ? 2756 LEU A CG    1 
ATOM   10248 C  CD1   . LEU A 1 2756 ? 110.761 164.409 172.925 1.00 73.29  ? 2756 LEU A CD1   1 
ATOM   10249 C  CD2   . LEU A 1 2756 ? 111.159 164.449 170.464 1.00 71.28  ? 2756 LEU A CD2   1 
ATOM   10250 N  N     . ARG A 1 2757 ? 108.829 169.125 169.647 1.00 90.93  ? 2757 ARG A N     1 
ATOM   10251 C  CA    . ARG A 1 2757 ? 107.581 169.768 169.257 1.00 93.64  ? 2757 ARG A CA    1 
ATOM   10252 C  C     . ARG A 1 2757 ? 107.096 169.321 167.884 1.00 94.78  ? 2757 ARG A C     1 
ATOM   10253 O  O     . ARG A 1 2757 ? 105.948 169.612 167.530 1.00 96.30  ? 2757 ARG A O     1 
ATOM   10254 C  CB    . ARG A 1 2757 ? 107.738 171.289 169.286 1.00 92.73  ? 2757 ARG A CB    1 
ATOM   10255 C  CG    . ARG A 1 2757 ? 107.588 171.893 170.674 1.00 89.66  ? 2757 ARG A CG    1 
ATOM   10256 C  CD    . ARG A 1 2757 ? 107.253 173.373 170.605 1.00 90.50  ? 2757 ARG A CD    1 
ATOM   10257 N  NE    . ARG A 1 2757 ? 108.394 174.175 170.182 1.00 94.73  ? 2757 ARG A NE    1 
ATOM   10258 C  CZ    . ARG A 1 2757 ? 109.208 174.815 171.011 1.00 97.78  ? 2757 ARG A CZ    1 
ATOM   10259 N  NH1   . ARG A 1 2757 ? 109.034 174.769 172.321 1.00 96.03  ? 2757 ARG A NH1   1 
ATOM   10260 N  NH2   . ARG A 1 2757 ? 110.220 175.519 170.512 1.00 95.96  ? 2757 ARG A NH2   1 
ATOM   10261 N  N     . LEU A 1 2758 ? 107.938 168.635 167.106 1.00 89.32  ? 2758 LEU A N     1 
ATOM   10262 C  CA    . LEU A 1 2758 ? 107.494 168.096 165.824 1.00 93.87  ? 2758 LEU A CA    1 
ATOM   10263 C  C     . LEU A 1 2758 ? 106.379 167.076 166.008 1.00 96.04  ? 2758 LEU A C     1 
ATOM   10264 O  O     . LEU A 1 2758 ? 105.370 167.111 165.293 1.00 100.34 ? 2758 LEU A O     1 
ATOM   10265 C  CB    . LEU A 1 2758 ? 108.672 167.462 165.086 1.00 87.97  ? 2758 LEU A CB    1 
ATOM   10266 C  CG    . LEU A 1 2758 ? 109.900 168.343 164.881 1.00 87.76  ? 2758 LEU A CG    1 
ATOM   10267 C  CD1   . LEU A 1 2758 ? 111.061 167.522 164.355 1.00 91.09  ? 2758 LEU A CD1   1 
ATOM   10268 C  CD2   . LEU A 1 2758 ? 109.555 169.450 163.909 1.00 90.66  ? 2758 LEU A CD2   1 
ATOM   10269 N  N     . ILE A 1 2759 ? 106.539 166.163 166.960 1.00 93.42  ? 2759 ILE A N     1 
ATOM   10270 C  CA    . ILE A 1 2759 ? 105.534 165.138 167.227 1.00 92.03  ? 2759 ILE A CA    1 
ATOM   10271 C  C     . ILE A 1 2759 ? 104.850 165.475 168.545 1.00 95.10  ? 2759 ILE A C     1 
ATOM   10272 O  O     . ILE A 1 2759 ? 105.453 165.306 169.615 1.00 100.00 ? 2759 ILE A O     1 
ATOM   10273 C  CB    . ILE A 1 2759 ? 106.148 163.727 167.265 1.00 94.28  ? 2759 ILE A CB    1 
ATOM   10274 C  CG1   . ILE A 1 2759 ? 107.390 163.616 166.370 1.00 94.34  ? 2759 ILE A CG1   1 
ATOM   10275 C  CG2   . ILE A 1 2759 ? 105.113 162.691 166.855 1.00 98.00  ? 2759 ILE A CG2   1 
ATOM   10276 C  CD1   . ILE A 1 2759 ? 107.150 163.936 164.899 1.00 93.65  ? 2759 ILE A CD1   1 
ATOM   10277 N  N     . PRO A 1 2760 ? 103.606 165.962 168.518 1.00 104.83 ? 2760 PRO A N     1 
ATOM   10278 C  CA    . PRO A 1 2760 ? 102.930 166.303 169.782 1.00 106.98 ? 2760 PRO A CA    1 
ATOM   10279 C  C     . PRO A 1 2760 ? 102.782 165.125 170.728 1.00 104.43 ? 2760 PRO A C     1 
ATOM   10280 O  O     . PRO A 1 2760 ? 102.835 165.308 171.950 1.00 102.69 ? 2760 PRO A O     1 
ATOM   10281 C  CB    . PRO A 1 2760 ? 101.568 166.834 169.312 1.00 105.38 ? 2760 PRO A CB    1 
ATOM   10282 C  CG    . PRO A 1 2760 ? 101.793 167.267 167.899 1.00 103.84 ? 2760 PRO A CG    1 
ATOM   10283 C  CD    . PRO A 1 2760 ? 102.792 166.303 167.341 1.00 100.91 ? 2760 PRO A CD    1 
ATOM   10284 N  N     . SER A 1 2761 ? 102.596 163.915 170.197 1.00 99.95  ? 2761 SER A N     1 
ATOM   10285 C  CA    . SER A 1 2761 ? 102.440 162.744 171.052 1.00 99.80  ? 2761 SER A CA    1 
ATOM   10286 C  C     . SER A 1 2761 ? 103.722 162.396 171.796 1.00 99.72  ? 2761 SER A C     1 
ATOM   10287 O  O     . SER A 1 2761 ? 103.661 161.734 172.837 1.00 100.05 ? 2761 SER A O     1 
ATOM   10288 C  CB    . SER A 1 2761 ? 101.978 161.545 170.222 1.00 102.45 ? 2761 SER A CB    1 
ATOM   10289 O  OG    . SER A 1 2761 ? 102.971 161.155 169.291 1.00 99.47  ? 2761 SER A OG    1 
ATOM   10290 N  N     . LEU A 1 2762 ? 104.876 162.821 171.287 1.00 97.24  ? 2762 LEU A N     1 
ATOM   10291 C  CA    . LEU A 1 2762 ? 106.160 162.533 171.911 1.00 94.91  ? 2762 LEU A CA    1 
ATOM   10292 C  C     . LEU A 1 2762 ? 106.627 163.633 172.853 1.00 97.63  ? 2762 LEU A C     1 
ATOM   10293 O  O     . LEU A 1 2762 ? 107.724 163.524 173.409 1.00 96.07  ? 2762 LEU A O     1 
ATOM   10294 C  CB    . LEU A 1 2762 ? 107.226 162.300 170.836 1.00 91.63  ? 2762 LEU A CB    1 
ATOM   10295 C  CG    . LEU A 1 2762 ? 107.114 161.009 170.027 1.00 94.35  ? 2762 LEU A CG    1 
ATOM   10296 C  CD1   . LEU A 1 2762 ? 108.237 160.923 169.006 1.00 93.63  ? 2762 LEU A CD1   1 
ATOM   10297 C  CD2   . LEU A 1 2762 ? 107.123 159.801 170.947 1.00 95.61  ? 2762 LEU A CD2   1 
ATOM   10298 N  N     . ARG A 1 2763 ? 105.828 164.686 173.045 1.00 102.10 ? 2763 ARG A N     1 
ATOM   10299 C  CA    . ARG A 1 2763 ? 106.279 165.823 173.842 1.00 99.90  ? 2763 ARG A CA    1 
ATOM   10300 C  C     . ARG A 1 2763 ? 106.508 165.433 175.297 1.00 100.18 ? 2763 ARG A C     1 
ATOM   10301 O  O     . ARG A 1 2763 ? 107.382 165.995 175.967 1.00 103.76 ? 2763 ARG A O     1 
ATOM   10302 C  CB    . ARG A 1 2763 ? 105.265 166.963 173.745 1.00 99.04  ? 2763 ARG A CB    1 
ATOM   10303 C  CG    . ARG A 1 2763 ? 105.473 167.875 172.544 1.00 98.46  ? 2763 ARG A CG    1 
ATOM   10304 C  CD    . ARG A 1 2763 ? 105.045 169.324 172.797 1.00 105.77 ? 2763 ARG A CD    1 
ATOM   10305 N  NE    . ARG A 1 2763 ? 103.637 169.471 173.154 1.00 110.37 ? 2763 ARG A NE    1 
ATOM   10306 C  CZ    . ARG A 1 2763 ? 103.162 169.458 174.393 1.00 106.52 ? 2763 ARG A CZ    1 
ATOM   10307 N  NH1   . ARG A 1 2763 ? 103.962 169.342 175.440 1.00 101.43 ? 2763 ARG A NH1   1 
ATOM   10308 N  NH2   . ARG A 1 2763 ? 101.851 169.577 174.587 1.00 103.17 ? 2763 ARG A NH2   1 
ATOM   10309 N  N     . THR A 1 2764 ? 105.736 164.471 175.806 1.00 88.47  ? 2764 THR A N     1 
ATOM   10310 C  CA    . THR A 1 2764 ? 105.853 164.095 177.209 1.00 90.78  ? 2764 THR A CA    1 
ATOM   10311 C  C     . THR A 1 2764 ? 107.126 163.312 177.505 1.00 92.70  ? 2764 THR A C     1 
ATOM   10312 O  O     . THR A 1 2764 ? 107.470 163.135 178.679 1.00 91.67  ? 2764 THR A O     1 
ATOM   10313 C  CB    . THR A 1 2764 ? 104.636 163.275 177.640 1.00 92.71  ? 2764 THR A CB    1 
ATOM   10314 O  OG1   . THR A 1 2764 ? 104.802 162.850 178.999 1.00 94.03  ? 2764 THR A OG1   1 
ATOM   10315 C  CG2   . THR A 1 2764 ? 104.473 162.056 176.749 1.00 91.65  ? 2764 THR A CG2   1 
ATOM   10316 N  N     . TYR A 1 2765 ? 107.831 162.839 176.480 1.00 91.51  ? 2765 TYR A N     1 
ATOM   10317 C  CA    . TYR A 1 2765 ? 109.011 162.006 176.669 1.00 87.40  ? 2765 TYR A CA    1 
ATOM   10318 C  C     . TYR A 1 2765 ? 110.318 162.786 176.605 1.00 89.19  ? 2765 TYR A C     1 
ATOM   10319 O  O     . TYR A 1 2765 ? 111.387 162.172 176.653 1.00 91.27  ? 2765 TYR A O     1 
ATOM   10320 C  CB    . TYR A 1 2765 ? 109.034 160.881 175.631 1.00 85.53  ? 2765 TYR A CB    1 
ATOM   10321 C  CG    . TYR A 1 2765 ? 107.897 159.899 175.775 1.00 90.66  ? 2765 TYR A CG    1 
ATOM   10322 C  CD1   . TYR A 1 2765 ? 107.932 158.906 176.744 1.00 89.68  ? 2765 TYR A CD1   1 
ATOM   10323 C  CD2   . TYR A 1 2765 ? 106.788 159.964 174.943 1.00 91.56  ? 2765 TYR A CD2   1 
ATOM   10324 C  CE1   . TYR A 1 2765 ? 106.895 158.006 176.881 1.00 90.52  ? 2765 TYR A CE1   1 
ATOM   10325 C  CE2   . TYR A 1 2765 ? 105.746 159.068 175.073 1.00 93.07  ? 2765 TYR A CE2   1 
ATOM   10326 C  CZ    . TYR A 1 2765 ? 105.805 158.091 176.043 1.00 94.36  ? 2765 TYR A CZ    1 
ATOM   10327 O  OH    . TYR A 1 2765 ? 104.769 157.196 176.176 1.00 97.35  ? 2765 TYR A OH    1 
ATOM   10328 N  N     . ALA A 1 2766 ? 110.264 164.115 176.490 1.00 81.48  ? 2766 ALA A N     1 
ATOM   10329 C  CA    . ALA A 1 2766 ? 111.496 164.896 176.428 1.00 76.84  ? 2766 ALA A CA    1 
ATOM   10330 C  C     . ALA A 1 2766 ? 112.283 164.801 177.729 1.00 79.02  ? 2766 ALA A C     1 
ATOM   10331 O  O     . ALA A 1 2766 ? 113.510 164.639 177.709 1.00 80.17  ? 2766 ALA A O     1 
ATOM   10332 C  CB    . ALA A 1 2766 ? 111.177 166.353 176.099 1.00 76.30  ? 2766 ALA A CB    1 
ATOM   10333 N  N     . GLU A 1 2767 ? 111.595 164.902 178.867 1.00 87.14  ? 2767 GLU A N     1 
ATOM   10334 C  CA    . GLU A 1 2767 ? 112.278 164.862 180.158 1.00 86.79  ? 2767 GLU A CA    1 
ATOM   10335 C  C     . GLU A 1 2767 ? 112.985 163.536 180.418 1.00 86.05  ? 2767 GLU A C     1 
ATOM   10336 O  O     . GLU A 1 2767 ? 114.151 163.562 180.846 1.00 85.77  ? 2767 GLU A O     1 
ATOM   10337 C  CB    . GLU A 1 2767 ? 111.282 165.200 181.273 1.00 85.44  ? 2767 GLU A CB    1 
ATOM   10338 C  CG    . GLU A 1 2767 ? 111.887 165.962 182.438 1.00 87.37  ? 2767 GLU A CG    1 
ATOM   10339 C  CD    . GLU A 1 2767 ? 110.861 166.794 183.181 1.00 94.09  ? 2767 GLU A CD    1 
ATOM   10340 O  OE1   . GLU A 1 2767 ? 111.232 167.455 184.173 1.00 93.65  ? 2767 GLU A OE1   1 
ATOM   10341 O  OE2   . GLU A 1 2767 ? 109.681 166.788 182.770 1.00 96.84  ? 2767 GLU A OE2   1 
ATOM   10342 N  N     . PRO A 1 2768 ? 112.367 162.365 180.215 1.00 77.46  ? 2768 PRO A N     1 
ATOM   10343 C  CA    . PRO A 1 2768 ? 113.150 161.127 180.366 1.00 74.18  ? 2768 PRO A CA    1 
ATOM   10344 C  C     . PRO A 1 2768 ? 114.221 160.968 179.304 1.00 77.82  ? 2768 PRO A C     1 
ATOM   10345 O  O     . PRO A 1 2768 ? 115.276 160.383 179.579 1.00 80.44  ? 2768 PRO A O     1 
ATOM   10346 C  CB    . PRO A 1 2768 ? 112.085 160.025 180.280 1.00 72.76  ? 2768 PRO A CB    1 
ATOM   10347 C  CG    . PRO A 1 2768 ? 110.974 160.637 179.519 1.00 76.29  ? 2768 PRO A CG    1 
ATOM   10348 C  CD    . PRO A 1 2768 ? 110.949 162.074 179.933 1.00 78.87  ? 2768 PRO A CD    1 
ATOM   10349 N  N     . LEU A 1 2769 ? 113.984 161.480 178.094 1.00 77.77  ? 2769 LEU A N     1 
ATOM   10350 C  CA    . LEU A 1 2769 ? 114.948 161.308 177.012 1.00 69.41  ? 2769 LEU A CA    1 
ATOM   10351 C  C     . LEU A 1 2769 ? 116.243 162.058 177.297 1.00 70.90  ? 2769 LEU A C     1 
ATOM   10352 O  O     . LEU A 1 2769 ? 117.341 161.516 177.120 1.00 72.72  ? 2769 LEU A O     1 
ATOM   10353 C  CB    . LEU A 1 2769 ? 114.336 161.769 175.688 1.00 65.78  ? 2769 LEU A CB    1 
ATOM   10354 C  CG    . LEU A 1 2769 ? 115.288 161.924 174.504 1.00 67.27  ? 2769 LEU A CG    1 
ATOM   10355 C  CD1   . LEU A 1 2769 ? 115.700 160.563 173.981 1.00 68.21  ? 2769 LEU A CD1   1 
ATOM   10356 C  CD2   . LEU A 1 2769 ? 114.638 162.747 173.406 1.00 73.03  ? 2769 LEU A CD2   1 
ATOM   10357 N  N     . THR A 1 2770 ? 116.136 163.312 177.744 1.00 68.27  ? 2770 THR A N     1 
ATOM   10358 C  CA    . THR A 1 2770 ? 117.344 164.075 178.044 1.00 60.73  ? 2770 THR A CA    1 
ATOM   10359 C  C     . THR A 1 2770 ? 118.084 163.472 179.232 1.00 65.49  ? 2770 THR A C     1 
ATOM   10360 O  O     . THR A 1 2770 ? 119.319 163.463 179.271 1.00 71.43  ? 2770 THR A O     1 
ATOM   10361 C  CB    . THR A 1 2770 ? 117.011 165.548 178.299 1.00 65.62  ? 2770 THR A CB    1 
ATOM   10362 O  OG1   . THR A 1 2770 ? 118.194 166.237 178.718 1.00 69.94  ? 2770 THR A OG1   1 
ATOM   10363 C  CG2   . THR A 1 2770 ? 115.951 165.695 179.373 1.00 74.21  ? 2770 THR A CG2   1 
ATOM   10364 N  N     . ALA A 1 2771 ? 117.338 162.947 180.206 1.00 67.62  ? 2771 ALA A N     1 
ATOM   10365 C  CA    . ALA A 1 2771 ? 117.962 162.283 181.345 1.00 70.87  ? 2771 ALA A CA    1 
ATOM   10366 C  C     . ALA A 1 2771 ? 118.739 161.050 180.900 1.00 67.84  ? 2771 ALA A C     1 
ATOM   10367 O  O     . ALA A 1 2771 ? 119.865 160.813 181.350 1.00 67.81  ? 2771 ALA A O     1 
ATOM   10368 C  CB    . ALA A 1 2771 ? 116.900 161.907 182.379 1.00 67.12  ? 2771 ALA A CB    1 
ATOM   10369 N  N     . ALA A 1 2772 ? 118.149 160.254 180.005 1.00 64.08  ? 2772 ALA A N     1 
ATOM   10370 C  CA    . ALA A 1 2772 ? 118.835 159.074 179.490 1.00 64.18  ? 2772 ALA A CA    1 
ATOM   10371 C  C     . ALA A 1 2772 ? 120.090 159.462 178.719 1.00 68.93  ? 2772 ALA A C     1 
ATOM   10372 O  O     . ALA A 1 2772 ? 121.146 158.832 178.865 1.00 77.91  ? 2772 ALA A O     1 
ATOM   10373 C  CB    . ALA A 1 2772 ? 117.887 158.262 178.607 1.00 63.99  ? 2772 ALA A CB    1 
ATOM   10374 N  N     . MET A 1 2773 ? 119.990 160.505 177.892 1.00 65.58  ? 2773 MET A N     1 
ATOM   10375 C  CA    . MET A 1 2773 ? 121.146 160.971 177.133 1.00 58.59  ? 2773 MET A CA    1 
ATOM   10376 C  C     . MET A 1 2773 ? 122.273 161.395 178.068 1.00 63.29  ? 2773 MET A C     1 
ATOM   10377 O  O     . MET A 1 2773 ? 123.432 160.999 177.893 1.00 65.88  ? 2773 MET A O     1 
ATOM   10378 C  CB    . MET A 1 2773 ? 120.741 162.128 176.216 1.00 58.01  ? 2773 MET A CB    1 
ATOM   10379 C  CG    . MET A 1 2773 ? 119.800 161.734 175.091 1.00 67.41  ? 2773 MET A CG    1 
ATOM   10380 S  SD    . MET A 1 2773 ? 119.859 162.852 173.679 1.00 73.05  ? 2773 MET A SD    1 
ATOM   10381 C  CE    . MET A 1 2773 ? 119.875 164.441 174.501 1.00 57.99  ? 2773 MET A CE    1 
ATOM   10382 N  N     . VAL A 1 2774 ? 121.937 162.193 179.085 1.00 71.52  ? 2774 VAL A N     1 
ATOM   10383 C  CA    . VAL A 1 2774 ? 122.946 162.686 180.022 1.00 69.60  ? 2774 VAL A CA    1 
ATOM   10384 C  C     . VAL A 1 2774 ? 123.579 161.527 180.780 1.00 73.86  ? 2774 VAL A C     1 
ATOM   10385 O  O     . VAL A 1 2774 ? 124.800 161.477 180.965 1.00 76.34  ? 2774 VAL A O     1 
ATOM   10386 C  CB    . VAL A 1 2774 ? 122.329 163.718 180.982 1.00 66.60  ? 2774 VAL A CB    1 
ATOM   10387 C  CG1   . VAL A 1 2774 ? 123.277 164.010 182.132 1.00 67.80  ? 2774 VAL A CG1   1 
ATOM   10388 C  CG2   . VAL A 1 2774 ? 121.991 164.995 180.236 1.00 68.66  ? 2774 VAL A CG2   1 
ATOM   10389 N  N     . GLU A 1 2775 ? 122.757 160.576 181.230 1.00 72.74  ? 2775 GLU A N     1 
ATOM   10390 C  CA    . GLU A 1 2775 ? 123.278 159.448 181.995 1.00 70.19  ? 2775 GLU A CA    1 
ATOM   10391 C  C     . GLU A 1 2775 ? 124.234 158.608 181.158 1.00 71.14  ? 2775 GLU A C     1 
ATOM   10392 O  O     . GLU A 1 2775 ? 125.340 158.273 181.604 1.00 80.12  ? 2775 GLU A O     1 
ATOM   10393 C  CB    . GLU A 1 2775 ? 122.120 158.593 182.511 1.00 72.93  ? 2775 GLU A CB    1 
ATOM   10394 C  CG    . GLU A 1 2775 ? 122.536 157.239 183.055 1.00 76.65  ? 2775 GLU A CG    1 
ATOM   10395 C  CD    . GLU A 1 2775 ? 121.591 156.731 184.126 1.00 83.73  ? 2775 GLU A CD    1 
ATOM   10396 O  OE1   . GLU A 1 2775 ? 120.369 156.937 183.985 1.00 85.71  ? 2775 GLU A OE1   1 
ATOM   10397 O  OE2   . GLU A 1 2775 ? 122.069 156.126 185.108 1.00 84.25  ? 2775 GLU A OE2   1 
ATOM   10398 N  N     . PHE A 1 2776 ? 123.831 158.267 179.930 1.00 60.32  ? 2776 PHE A N     1 
ATOM   10399 C  CA    . PHE A 1 2776 ? 124.702 157.455 179.088 1.00 61.93  ? 2776 PHE A CA    1 
ATOM   10400 C  C     . PHE A 1 2776 ? 125.987 158.195 178.748 1.00 65.16  ? 2776 PHE A C     1 
ATOM   10401 O  O     . PHE A 1 2776 ? 127.069 157.596 178.733 1.00 69.78  ? 2776 PHE A O     1 
ATOM   10402 C  CB    . PHE A 1 2776 ? 123.987 157.033 177.807 1.00 59.02  ? 2776 PHE A CB    1 
ATOM   10403 C  CG    . PHE A 1 2776 ? 124.818 156.140 176.934 1.00 63.28  ? 2776 PHE A CG    1 
ATOM   10404 C  CD1   . PHE A 1 2776 ? 125.550 155.103 177.486 1.00 66.33  ? 2776 PHE A CD1   1 
ATOM   10405 C  CD2   . PHE A 1 2776 ? 124.896 156.353 175.570 1.00 67.96  ? 2776 PHE A CD2   1 
ATOM   10406 C  CE1   . PHE A 1 2776 ? 126.326 154.285 176.695 1.00 57.75  ? 2776 PHE A CE1   1 
ATOM   10407 C  CE2   . PHE A 1 2776 ? 125.673 155.537 174.773 1.00 69.64  ? 2776 PHE A CE2   1 
ATOM   10408 C  CZ    . PHE A 1 2776 ? 126.390 154.504 175.338 1.00 62.00  ? 2776 PHE A CZ    1 
ATOM   10409 N  N     . TYR A 1 2777 ? 125.892 159.495 178.463 1.00 63.91  ? 2777 TYR A N     1 
ATOM   10410 C  CA    . TYR A 1 2777 ? 127.089 160.265 178.152 1.00 61.34  ? 2777 TYR A CA    1 
ATOM   10411 C  C     . TYR A 1 2777 ? 128.031 160.320 179.348 1.00 73.10  ? 2777 TYR A C     1 
ATOM   10412 O  O     . TYR A 1 2777 ? 129.254 160.238 179.195 1.00 78.97  ? 2777 TYR A O     1 
ATOM   10413 C  CB    . TYR A 1 2777 ? 126.694 161.668 177.702 1.00 63.06  ? 2777 TYR A CB    1 
ATOM   10414 C  CG    . TYR A 1 2777 ? 127.786 162.701 177.825 1.00 64.22  ? 2777 TYR A CG    1 
ATOM   10415 C  CD1   . TYR A 1 2777 ? 128.880 162.686 176.974 1.00 62.86  ? 2777 TYR A CD1   1 
ATOM   10416 C  CD2   . TYR A 1 2777 ? 127.715 163.700 178.783 1.00 69.47  ? 2777 TYR A CD2   1 
ATOM   10417 C  CE1   . TYR A 1 2777 ? 129.876 163.632 177.079 1.00 66.82  ? 2777 TYR A CE1   1 
ATOM   10418 C  CE2   . TYR A 1 2777 ? 128.706 164.649 178.896 1.00 66.99  ? 2777 TYR A CE2   1 
ATOM   10419 C  CZ    . TYR A 1 2777 ? 129.782 164.613 178.041 1.00 67.15  ? 2777 TYR A CZ    1 
ATOM   10420 O  OH    . TYR A 1 2777 ? 130.772 165.559 178.154 1.00 65.91  ? 2777 TYR A OH    1 
ATOM   10421 N  N     . THR A 1 2778 ? 127.474 160.466 180.552 1.00 78.76  ? 2778 THR A N     1 
ATOM   10422 C  CA    . THR A 1 2778 ? 128.301 160.490 181.753 1.00 70.46  ? 2778 THR A CA    1 
ATOM   10423 C  C     . THR A 1 2778 ? 128.997 159.152 181.965 1.00 72.91  ? 2778 THR A C     1 
ATOM   10424 O  O     . THR A 1 2778 ? 130.184 159.106 182.307 1.00 78.68  ? 2778 THR A O     1 
ATOM   10425 C  CB    . THR A 1 2778 ? 127.449 160.852 182.969 1.00 71.82  ? 2778 THR A CB    1 
ATOM   10426 O  OG1   . THR A 1 2778 ? 126.728 162.061 182.703 1.00 81.90  ? 2778 THR A OG1   1 
ATOM   10427 C  CG2   . THR A 1 2778 ? 128.328 161.052 184.194 1.00 76.00  ? 2778 THR A CG2   1 
ATOM   10428 N  N     . MET A 1 2779 ? 128.273 158.048 181.763 1.00 81.46  ? 2779 MET A N     1 
ATOM   10429 C  CA    . MET A 1 2779 ? 128.892 156.732 181.908 1.00 82.05  ? 2779 MET A CA    1 
ATOM   10430 C  C     . MET A 1 2779 ? 129.979 156.516 180.862 1.00 81.02  ? 2779 MET A C     1 
ATOM   10431 O  O     . MET A 1 2779 ? 131.034 155.943 181.156 1.00 88.09  ? 2779 MET A O     1 
ATOM   10432 C  CB    . MET A 1 2779 ? 127.835 155.630 181.823 1.00 81.29  ? 2779 MET A CB    1 
ATOM   10433 C  CG    . MET A 1 2779 ? 127.583 154.929 183.150 1.00 86.14  ? 2779 MET A CG    1 
ATOM   10434 S  SD    . MET A 1 2779 ? 126.415 153.558 183.061 1.00 104.81 ? 2779 MET A SD    1 
ATOM   10435 C  CE    . MET A 1 2779 ? 124.891 154.423 182.719 1.00 85.86  ? 2779 MET A CE    1 
ATOM   10436 N  N     . SER A 1 2780 ? 129.734 156.964 179.628 1.00 68.98  ? 2780 SER A N     1 
ATOM   10437 C  CA    . SER A 1 2780 ? 130.712 156.767 178.563 1.00 67.73  ? 2780 SER A CA    1 
ATOM   10438 C  C     . SER A 1 2780 ? 132.000 157.530 178.841 1.00 73.66  ? 2780 SER A C     1 
ATOM   10439 O  O     . SER A 1 2780 ? 133.097 157.018 178.592 1.00 79.52  ? 2780 SER A O     1 
ATOM   10440 C  CB    . SER A 1 2780 ? 130.119 157.193 177.222 1.00 75.55  ? 2780 SER A CB    1 
ATOM   10441 O  OG    . SER A 1 2780 ? 129.178 156.243 176.756 1.00 84.82  ? 2780 SER A OG    1 
ATOM   10442 N  N     . GLN A 1 2781 ? 131.888 158.761 179.344 1.00 76.61  ? 2781 GLN A N     1 
ATOM   10443 C  CA    . GLN A 1 2781 ? 133.074 159.540 179.674 1.00 72.83  ? 2781 GLN A CA    1 
ATOM   10444 C  C     . GLN A 1 2781 ? 133.913 158.888 180.762 1.00 80.67  ? 2781 GLN A C     1 
ATOM   10445 O  O     . GLN A 1 2781 ? 135.141 158.842 180.639 1.00 87.02  ? 2781 GLN A O     1 
ATOM   10446 C  CB    . GLN A 1 2781 ? 132.677 160.947 180.114 1.00 74.07  ? 2781 GLN A CB    1 
ATOM   10447 C  CG    . GLN A 1 2781 ? 133.653 162.022 179.687 1.00 76.47  ? 2781 GLN A CG    1 
ATOM   10448 C  CD    . GLN A 1 2781 ? 133.055 163.407 179.761 1.00 81.99  ? 2781 GLN A CD    1 
ATOM   10449 O  OE1   . GLN A 1 2781 ? 131.840 163.565 179.861 1.00 83.59  ? 2781 GLN A OE1   1 
ATOM   10450 N  NE2   . GLN A 1 2781 ? 133.907 164.423 179.711 1.00 77.44  ? 2781 GLN A NE2   1 
ATOM   10451 N  N     . GLU A 1 2782 ? 133.280 158.390 181.822 1.00 85.63  ? 2782 GLU A N     1 
ATOM   10452 C  CA    . GLU A 1 2782 ? 133.996 157.724 182.899 1.00 81.92  ? 2782 GLU A CA    1 
ATOM   10453 C  C     . GLU A 1 2782 ? 134.665 156.434 182.445 1.00 81.12  ? 2782 GLU A C     1 
ATOM   10454 O  O     . GLU A 1 2782 ? 135.830 156.203 182.787 1.00 82.08  ? 2782 GLU A O     1 
ATOM   10455 C  CB    . GLU A 1 2782 ? 133.026 157.439 184.058 1.00 82.44  ? 2782 GLU A CB    1 
ATOM   10456 C  CG    . GLU A 1 2782 ? 133.381 156.300 185.032 1.00 85.80  ? 2782 GLU A CG    1 
ATOM   10457 C  CD    . GLU A 1 2782 ? 134.824 156.302 185.528 1.00 93.37  ? 2782 GLU A CD    1 
ATOM   10458 O  OE1   . GLU A 1 2782 ? 135.288 155.236 185.983 1.00 93.20  ? 2782 GLU A OE1   1 
ATOM   10459 O  OE2   . GLU A 1 2782 ? 135.482 157.364 185.502 1.00 93.58  ? 2782 GLU A OE2   1 
ATOM   10460 N  N     . ARG A 1 2783 ? 133.971 155.609 181.663 1.00 75.20  ? 2783 ARG A N     1 
ATOM   10461 C  CA    . ARG A 1 2783 ? 134.484 154.302 181.273 1.00 72.91  ? 2783 ARG A CA    1 
ATOM   10462 C  C     . ARG A 1 2783 ? 135.666 154.395 180.315 1.00 79.02  ? 2783 ARG A C     1 
ATOM   10463 O  O     . ARG A 1 2783 ? 136.671 153.704 180.510 1.00 83.31  ? 2783 ARG A O     1 
ATOM   10464 C  CB    . ARG A 1 2783 ? 133.364 153.473 180.640 1.00 76.88  ? 2783 ARG A CB    1 
ATOM   10465 C  CG    . ARG A 1 2783 ? 133.827 152.163 180.036 1.00 80.03  ? 2783 ARG A CG    1 
ATOM   10466 C  CD    . ARG A 1 2783 ? 134.159 151.154 181.120 1.00 82.26  ? 2783 ARG A CD    1 
ATOM   10467 N  NE    . ARG A 1 2783 ? 134.144 149.785 180.618 1.00 84.89  ? 2783 ARG A NE    1 
ATOM   10468 C  CZ    . ARG A 1 2783 ? 135.100 149.248 179.873 1.00 85.51  ? 2783 ARG A CZ    1 
ATOM   10469 N  NH1   . ARG A 1 2783 ? 136.176 149.935 179.528 1.00 84.03  ? 2783 ARG A NH1   1 
ATOM   10470 N  NH2   . ARG A 1 2783 ? 134.974 147.988 179.468 1.00 82.59  ? 2783 ARG A NH2   1 
ATOM   10471 N  N     . PHE A 1 2784 ? 135.573 155.237 179.288 1.00 77.87  ? 2784 PHE A N     1 
ATOM   10472 C  CA    . PHE A 1 2784 ? 136.637 155.404 178.305 1.00 72.40  ? 2784 PHE A CA    1 
ATOM   10473 C  C     . PHE A 1 2784 ? 137.320 156.746 178.529 1.00 71.74  ? 2784 PHE A C     1 
ATOM   10474 O  O     . PHE A 1 2784 ? 136.683 157.798 178.408 1.00 79.29  ? 2784 PHE A O     1 
ATOM   10475 C  CB    . PHE A 1 2784 ? 136.094 155.316 176.879 1.00 67.82  ? 2784 PHE A CB    1 
ATOM   10476 C  CG    . PHE A 1 2784 ? 135.110 154.203 176.670 1.00 65.25  ? 2784 PHE A CG    1 
ATOM   10477 C  CD1   . PHE A 1 2784 ? 135.494 152.884 176.829 1.00 67.69  ? 2784 PHE A CD1   1 
ATOM   10478 C  CD2   . PHE A 1 2784 ? 133.805 154.476 176.301 1.00 68.86  ? 2784 PHE A CD2   1 
ATOM   10479 C  CE1   . PHE A 1 2784 ? 134.593 151.858 176.630 1.00 72.51  ? 2784 PHE A CE1   1 
ATOM   10480 C  CE2   . PHE A 1 2784 ? 132.899 153.454 176.102 1.00 71.40  ? 2784 PHE A CE2   1 
ATOM   10481 C  CZ    . PHE A 1 2784 ? 133.294 152.144 176.268 1.00 74.69  ? 2784 PHE A CZ    1 
ATOM   10482 N  N     . THR A 1 2785 ? 138.609 156.706 178.847 1.00 76.23  ? 2785 THR A N     1 
ATOM   10483 C  CA    . THR A 1 2785 ? 139.413 157.899 179.057 1.00 79.81  ? 2785 THR A CA    1 
ATOM   10484 C  C     . THR A 1 2785 ? 140.571 157.919 178.068 1.00 78.69  ? 2785 THR A C     1 
ATOM   10485 O  O     . THR A 1 2785 ? 140.797 156.965 177.319 1.00 81.40  ? 2785 THR A O     1 
ATOM   10486 C  CB    . THR A 1 2785 ? 139.948 157.966 180.494 1.00 81.52  ? 2785 THR A CB    1 
ATOM   10487 O  OG1   . THR A 1 2785 ? 141.194 157.262 180.574 1.00 87.24  ? 2785 THR A OG1   1 
ATOM   10488 C  CG2   . THR A 1 2785 ? 138.960 157.342 181.466 1.00 83.81  ? 2785 THR A CG2   1 
ATOM   10489 N  N     . GLN A 1 2786 ? 141.315 159.026 178.076 1.00 79.68  ? 2786 GLN A N     1 
ATOM   10490 C  CA    . GLN A 1 2786 ? 142.472 159.161 177.199 1.00 80.82  ? 2786 GLN A CA    1 
ATOM   10491 C  C     . GLN A 1 2786 ? 143.604 158.212 177.564 1.00 84.38  ? 2786 GLN A C     1 
ATOM   10492 O  O     . GLN A 1 2786 ? 144.534 158.052 176.766 1.00 86.01  ? 2786 GLN A O     1 
ATOM   10493 C  CB    . GLN A 1 2786 ? 142.988 160.600 177.224 1.00 84.79  ? 2786 GLN A CB    1 
ATOM   10494 C  CG    . GLN A 1 2786 ? 142.289 161.531 176.252 1.00 86.09  ? 2786 GLN A CG    1 
ATOM   10495 C  CD    . GLN A 1 2786 ? 143.189 162.656 175.786 1.00 90.98  ? 2786 GLN A CD    1 
ATOM   10496 O  OE1   . GLN A 1 2786 ? 144.397 162.477 175.638 1.00 89.09  ? 2786 GLN A OE1   1 
ATOM   10497 N  NE2   . GLN A 1 2786 ? 142.607 163.827 175.560 1.00 90.69  ? 2786 GLN A NE2   1 
ATOM   10498 N  N     . ASP A 1 2787 ? 143.557 157.593 178.746 1.00 93.88  ? 2787 ASP A N     1 
ATOM   10499 C  CA    . ASP A 1 2787 ? 144.597 156.641 179.122 1.00 89.14  ? 2787 ASP A CA    1 
ATOM   10500 C  C     . ASP A 1 2787 ? 144.560 155.405 178.233 1.00 90.75  ? 2787 ASP A C     1 
ATOM   10501 O  O     . ASP A 1 2787 ? 145.607 154.840 177.898 1.00 93.94  ? 2787 ASP A O     1 
ATOM   10502 C  CB    . ASP A 1 2787 ? 144.443 156.250 180.592 1.00 91.94  ? 2787 ASP A CB    1 
ATOM   10503 C  CG    . ASP A 1 2787 ? 144.187 157.445 181.488 1.00 98.96  ? 2787 ASP A CG    1 
ATOM   10504 O  OD1   . ASP A 1 2787 ? 145.102 158.281 181.642 1.00 101.55 ? 2787 ASP A OD1   1 
ATOM   10505 O  OD2   . ASP A 1 2787 ? 143.072 157.547 182.040 1.00 97.95  ? 2787 ASP A OD2   1 
ATOM   10506 N  N     . THR A 1 2788 ? 143.361 154.968 177.843 1.00 80.92  ? 2788 THR A N     1 
ATOM   10507 C  CA    . THR A 1 2788 ? 143.241 153.791 176.990 1.00 78.39  ? 2788 THR A CA    1 
ATOM   10508 C  C     . THR A 1 2788 ? 143.681 154.100 175.563 1.00 79.57  ? 2788 THR A C     1 
ATOM   10509 O  O     . THR A 1 2788 ? 144.618 153.487 175.041 1.00 81.60  ? 2788 THR A O     1 
ATOM   10510 C  CB    . THR A 1 2788 ? 141.802 153.273 177.012 1.00 78.07  ? 2788 THR A CB    1 
ATOM   10511 O  OG1   . THR A 1 2788 ? 141.332 153.220 178.364 1.00 80.74  ? 2788 THR A OG1   1 
ATOM   10512 C  CG2   . THR A 1 2788 ? 141.731 151.882 176.405 1.00 78.28  ? 2788 THR A CG2   1 
ATOM   10513 N  N     . GLN A 1 2789 ? 143.014 155.051 174.916 1.00 77.10  ? 2789 GLN A N     1 
ATOM   10514 C  CA    . GLN A 1 2789 ? 143.332 155.444 173.553 1.00 70.59  ? 2789 GLN A CA    1 
ATOM   10515 C  C     . GLN A 1 2789 ? 143.374 156.960 173.441 1.00 69.52  ? 2789 GLN A C     1 
ATOM   10516 O  O     . GLN A 1 2789 ? 142.663 157.661 174.169 1.00 75.39  ? 2789 GLN A O     1 
ATOM   10517 C  CB    . GLN A 1 2789 ? 142.303 154.883 172.560 1.00 73.42  ? 2789 GLN A CB    1 
ATOM   10518 C  CG    . GLN A 1 2789 ? 142.204 153.367 172.554 1.00 74.98  ? 2789 GLN A CG    1 
ATOM   10519 C  CD    . GLN A 1 2789 ? 143.327 152.715 171.776 1.00 77.26  ? 2789 GLN A CD    1 
ATOM   10520 O  OE1   . GLN A 1 2789 ? 144.031 153.372 171.010 1.00 74.41  ? 2789 GLN A OE1   1 
ATOM   10521 N  NE2   . GLN A 1 2789 ? 143.500 151.413 171.968 1.00 78.03  ? 2789 GLN A NE2   1 
ATOM   10522 N  N     . PRO A 1 2790 ? 144.206 157.494 172.543 1.00 67.03  ? 2790 PRO A N     1 
ATOM   10523 C  CA    . PRO A 1 2790 ? 144.300 158.958 172.412 1.00 74.84  ? 2790 PRO A CA    1 
ATOM   10524 C  C     . PRO A 1 2790 ? 143.008 159.624 171.971 1.00 74.66  ? 2790 PRO A C     1 
ATOM   10525 O  O     . PRO A 1 2790 ? 142.757 160.774 172.351 1.00 75.73  ? 2790 PRO A O     1 
ATOM   10526 C  CB    . PRO A 1 2790 ? 145.413 159.143 171.371 1.00 79.02  ? 2790 PRO A CB    1 
ATOM   10527 C  CG    . PRO A 1 2790 ? 145.450 157.859 170.617 1.00 74.40  ? 2790 PRO A CG    1 
ATOM   10528 C  CD    . PRO A 1 2790 ? 145.113 156.797 171.616 1.00 73.51  ? 2790 PRO A CD    1 
ATOM   10529 N  N     . HIS A 1 2791 ? 142.181 158.945 171.181 1.00 71.33  ? 2791 HIS A N     1 
ATOM   10530 C  CA    . HIS A 1 2791 ? 140.966 159.540 170.641 1.00 69.89  ? 2791 HIS A CA    1 
ATOM   10531 C  C     . HIS A 1 2791 ? 139.757 159.358 171.547 1.00 73.84  ? 2791 HIS A C     1 
ATOM   10532 O  O     . HIS A 1 2791 ? 138.649 159.743 171.159 1.00 77.79  ? 2791 HIS A O     1 
ATOM   10533 C  CB    . HIS A 1 2791 ? 140.658 158.952 169.260 1.00 67.42  ? 2791 HIS A CB    1 
ATOM   10534 C  CG    . HIS A 1 2791 ? 140.491 157.465 169.260 1.00 68.25  ? 2791 HIS A CG    1 
ATOM   10535 N  ND1   . HIS A 1 2791 ? 141.560 156.595 169.260 1.00 73.10  ? 2791 HIS A ND1   1 
ATOM   10536 C  CD2   . HIS A 1 2791 ? 139.379 156.693 169.260 1.00 67.40  ? 2791 HIS A CD2   1 
ATOM   10537 C  CE1   . HIS A 1 2791 ? 141.114 155.352 169.260 1.00 70.98  ? 2791 HIS A CE1   1 
ATOM   10538 N  NE2   . HIS A 1 2791 ? 139.794 155.384 169.260 1.00 71.26  ? 2791 HIS A NE2   1 
ATOM   10539 N  N     . TYR A 1 2792 ? 139.937 158.784 172.736 1.00 73.29  ? 2792 TYR A N     1 
ATOM   10540 C  CA    . TYR A 1 2792 ? 138.826 158.499 173.645 1.00 61.36  ? 2792 TYR A CA    1 
ATOM   10541 C  C     . TYR A 1 2792 ? 138.476 159.755 174.446 1.00 70.33  ? 2792 TYR A C     1 
ATOM   10542 O  O     . TYR A 1 2792 ? 138.588 159.811 175.672 1.00 83.35  ? 2792 TYR A O     1 
ATOM   10543 C  CB    . TYR A 1 2792 ? 139.176 157.338 174.563 1.00 69.39  ? 2792 TYR A CB    1 
ATOM   10544 C  CG    . TYR A 1 2792 ? 138.935 155.975 173.960 1.00 68.50  ? 2792 TYR A CG    1 
ATOM   10545 C  CD1   . TYR A 1 2792 ? 138.368 155.841 172.703 1.00 67.78  ? 2792 TYR A CD1   1 
ATOM   10546 C  CD2   . TYR A 1 2792 ? 139.275 154.822 174.652 1.00 72.49  ? 2792 TYR A CD2   1 
ATOM   10547 C  CE1   . TYR A 1 2792 ? 138.146 154.596 172.152 1.00 73.48  ? 2792 TYR A CE1   1 
ATOM   10548 C  CE2   . TYR A 1 2792 ? 139.056 153.574 174.110 1.00 65.06  ? 2792 TYR A CE2   1 
ATOM   10549 C  CZ    . TYR A 1 2792 ? 138.492 153.466 172.860 1.00 68.68  ? 2792 TYR A CZ    1 
ATOM   10550 O  OH    . TYR A 1 2792 ? 138.273 152.222 172.317 1.00 77.06  ? 2792 TYR A OH    1 
ATOM   10551 N  N     . ILE A 1 2793 ? 138.041 160.780 173.722 1.00 63.11  ? 2793 ILE A N     1 
ATOM   10552 C  CA    . ILE A 1 2793 ? 137.608 162.039 174.317 1.00 59.57  ? 2793 ILE A CA    1 
ATOM   10553 C  C     . ILE A 1 2793 ? 136.107 162.173 174.098 1.00 66.33  ? 2793 ILE A C     1 
ATOM   10554 O  O     . ILE A 1 2793 ? 135.602 161.894 173.003 1.00 73.64  ? 2793 ILE A O     1 
ATOM   10555 C  CB    . ILE A 1 2793 ? 138.375 163.244 173.744 1.00 61.82  ? 2793 ILE A CB    1 
ATOM   10556 C  CG1   . ILE A 1 2793 ? 138.005 163.504 172.281 1.00 66.07  ? 2793 ILE A CG1   1 
ATOM   10557 C  CG2   . ILE A 1 2793 ? 139.872 163.029 173.876 1.00 67.60  ? 2793 ILE A CG2   1 
ATOM   10558 C  CD1   . ILE A 1 2793 ? 138.299 164.912 171.816 1.00 67.96  ? 2793 ILE A CD1   1 
ATOM   10559 N  N     . TYR A 1 2794 ? 135.391 162.550 175.152 1.00 67.89  ? 2794 TYR A N     1 
ATOM   10560 C  CA    . TYR A 1 2794 ? 133.953 162.767 175.094 1.00 64.87  ? 2794 TYR A CA    1 
ATOM   10561 C  C     . TYR A 1 2794 ? 133.640 164.131 175.688 1.00 69.60  ? 2794 TYR A C     1 
ATOM   10562 O  O     . TYR A 1 2794 ? 134.236 164.525 176.695 1.00 80.04  ? 2794 TYR A O     1 
ATOM   10563 C  CB    . TYR A 1 2794 ? 133.195 161.664 175.836 1.00 66.22  ? 2794 TYR A CB    1 
ATOM   10564 C  CG    . TYR A 1 2794 ? 133.339 160.303 175.194 1.00 72.36  ? 2794 TYR A CG    1 
ATOM   10565 C  CD1   . TYR A 1 2794 ? 132.651 159.987 174.032 1.00 67.31  ? 2794 TYR A CD1   1 
ATOM   10566 C  CD2   . TYR A 1 2794 ? 134.165 159.336 175.749 1.00 76.25  ? 2794 TYR A CD2   1 
ATOM   10567 C  CE1   . TYR A 1 2794 ? 132.783 158.747 173.439 1.00 65.94  ? 2794 TYR A CE1   1 
ATOM   10568 C  CE2   . TYR A 1 2794 ? 134.301 158.092 175.164 1.00 76.37  ? 2794 TYR A CE2   1 
ATOM   10569 C  CZ    . TYR A 1 2794 ? 133.608 157.803 174.011 1.00 72.36  ? 2794 TYR A CZ    1 
ATOM   10570 O  OH    . TYR A 1 2794 ? 133.740 156.566 173.425 1.00 74.16  ? 2794 TYR A OH    1 
ATOM   10571 N  N     . SER A 1 2795 ? 132.714 164.844 175.064 1.00 53.64  ? 2795 SER A N     1 
ATOM   10572 C  CA    . SER A 1 2795 ? 132.427 166.223 175.426 1.00 56.09  ? 2795 SER A CA    1 
ATOM   10573 C  C     . SER A 1 2795 ? 130.976 166.508 175.083 1.00 61.47  ? 2795 SER A C     1 
ATOM   10574 O  O     . SER A 1 2795 ? 130.318 165.704 174.412 1.00 80.08  ? 2795 SER A O     1 
ATOM   10575 C  CB    . SER A 1 2795 ? 133.362 167.190 174.692 1.00 61.74  ? 2795 SER A CB    1 
ATOM   10576 O  OG    . SER A 1 2795 ? 133.436 166.874 173.313 1.00 63.67  ? 2795 SER A OG    1 
ATOM   10577 N  N     . PRO A 1 2796 ? 130.437 167.644 175.540 1.00 47.50  ? 2796 PRO A N     1 
ATOM   10578 C  CA    . PRO A 1 2796 ? 129.094 168.048 175.093 1.00 50.62  ? 2796 PRO A CA    1 
ATOM   10579 C  C     . PRO A 1 2796 ? 128.949 168.146 173.582 1.00 55.15  ? 2796 PRO A C     1 
ATOM   10580 O  O     . PRO A 1 2796 ? 127.817 168.267 173.097 1.00 66.70  ? 2796 PRO A O     1 
ATOM   10581 C  CB    . PRO A 1 2796 ? 128.901 169.413 175.760 1.00 55.47  ? 2796 PRO A CB    1 
ATOM   10582 C  CG    . PRO A 1 2796 ? 129.703 169.315 177.003 1.00 55.25  ? 2796 PRO A CG    1 
ATOM   10583 C  CD    . PRO A 1 2796 ? 130.909 168.481 176.658 1.00 55.86  ? 2796 PRO A CD    1 
ATOM   10584 N  N     . ARG A 1 2797 ? 130.050 168.106 172.826 1.00 56.88  ? 2797 ARG A N     1 
ATOM   10585 C  CA    . ARG A 1 2797 ? 129.945 168.004 171.375 1.00 60.02  ? 2797 ARG A CA    1 
ATOM   10586 C  C     . ARG A 1 2797 ? 129.199 166.739 170.973 1.00 66.96  ? 2797 ARG A C     1 
ATOM   10587 O  O     . ARG A 1 2797 ? 128.412 166.749 170.020 1.00 74.78  ? 2797 ARG A O     1 
ATOM   10588 C  CB    . ARG A 1 2797 ? 131.336 168.024 170.745 1.00 60.00  ? 2797 ARG A CB    1 
ATOM   10589 C  CG    . ARG A 1 2797 ? 131.928 169.408 170.575 1.00 63.89  ? 2797 ARG A CG    1 
ATOM   10590 C  CD    . ARG A 1 2797 ? 132.974 169.413 169.477 1.00 63.36  ? 2797 ARG A CD    1 
ATOM   10591 N  NE    . ARG A 1 2797 ? 134.277 168.982 169.970 1.00 66.66  ? 2797 ARG A NE    1 
ATOM   10592 C  CZ    . ARG A 1 2797 ? 135.355 169.752 170.008 1.00 73.51  ? 2797 ARG A CZ    1 
ATOM   10593 N  NH1   . ARG A 1 2797 ? 135.325 171.004 169.581 1.00 64.92  ? 2797 ARG A NH1   1 
ATOM   10594 N  NH2   . ARG A 1 2797 ? 136.491 169.254 170.485 1.00 76.69  ? 2797 ARG A NH2   1 
ATOM   10595 N  N     . GLU A 1 2798 ? 129.439 165.638 171.689 1.00 64.59  ? 2798 GLU A N     1 
ATOM   10596 C  CA    . GLU A 1 2798 ? 128.723 164.401 171.401 1.00 53.56  ? 2798 GLU A CA    1 
ATOM   10597 C  C     . GLU A 1 2798 ? 127.233 164.547 171.675 1.00 65.18  ? 2798 GLU A C     1 
ATOM   10598 O  O     . GLU A 1 2798 ? 126.406 164.045 170.909 1.00 80.92  ? 2798 GLU A O     1 
ATOM   10599 C  CB    . GLU A 1 2798 ? 129.315 163.248 172.210 1.00 52.04  ? 2798 GLU A CB    1 
ATOM   10600 C  CG    . GLU A 1 2798 ? 130.830 163.278 172.298 1.00 68.19  ? 2798 GLU A CG    1 
ATOM   10601 C  CD    . GLU A 1 2798 ? 131.501 162.912 170.988 1.00 68.93  ? 2798 GLU A CD    1 
ATOM   10602 O  OE1   . GLU A 1 2798 ? 130.814 162.391 170.086 1.00 72.28  ? 2798 GLU A OE1   1 
ATOM   10603 O  OE2   . GLU A 1 2798 ? 132.720 163.148 170.859 1.00 65.70  ? 2798 GLU A OE2   1 
ATOM   10604 N  N     . MET A 1 2799 ? 126.866 165.236 172.758 1.00 56.82  ? 2799 MET A N     1 
ATOM   10605 C  CA    . MET A 1 2799 ? 125.450 165.491 173.018 1.00 61.05  ? 2799 MET A CA    1 
ATOM   10606 C  C     . MET A 1 2799 ? 124.830 166.376 171.944 1.00 61.96  ? 2799 MET A C     1 
ATOM   10607 O  O     . MET A 1 2799 ? 123.683 166.154 171.537 1.00 66.25  ? 2799 MET A O     1 
ATOM   10608 C  CB    . MET A 1 2799 ? 125.268 166.124 174.394 1.00 63.58  ? 2799 MET A CB    1 
ATOM   10609 C  CG    . MET A 1 2799 ? 125.985 165.414 175.509 1.00 61.30  ? 2799 MET A CG    1 
ATOM   10610 S  SD    . MET A 1 2799 ? 124.944 164.075 176.098 1.00 80.69  ? 2799 MET A SD    1 
ATOM   10611 C  CE    . MET A 1 2799 ? 123.674 164.997 176.957 1.00 67.51  ? 2799 MET A CE    1 
ATOM   10612 N  N     . THR A 1 2800 ? 125.556 167.400 171.492 1.00 53.91  ? 2800 THR A N     1 
ATOM   10613 C  CA    . THR A 1 2800 ? 125.032 168.253 170.432 1.00 53.17  ? 2800 THR A CA    1 
ATOM   10614 C  C     . THR A 1 2800 ? 124.823 167.460 169.148 1.00 64.63  ? 2800 THR A C     1 
ATOM   10615 O  O     . THR A 1 2800 ? 123.799 167.615 168.472 1.00 73.36  ? 2800 THR A O     1 
ATOM   10616 C  CB    . THR A 1 2800 ? 125.972 169.433 170.191 1.00 53.81  ? 2800 THR A CB    1 
ATOM   10617 O  OG1   . THR A 1 2800 ? 126.047 170.232 171.378 1.00 65.44  ? 2800 THR A OG1   1 
ATOM   10618 C  CG2   . THR A 1 2800 ? 125.466 170.293 169.046 1.00 57.73  ? 2800 THR A CG2   1 
ATOM   10619 N  N     . ARG A 1 2801 ? 125.779 166.593 168.806 1.00 63.01  ? 2801 ARG A N     1 
ATOM   10620 C  CA    . ARG A 1 2801 ? 125.619 165.731 167.639 1.00 56.18  ? 2801 ARG A CA    1 
ATOM   10621 C  C     . ARG A 1 2801 ? 124.450 164.772 167.822 1.00 63.45  ? 2801 ARG A C     1 
ATOM   10622 O  O     . ARG A 1 2801 ? 123.723 164.478 166.868 1.00 72.54  ? 2801 ARG A O     1 
ATOM   10623 C  CB    . ARG A 1 2801 ? 126.911 164.959 167.380 1.00 56.26  ? 2801 ARG A CB    1 
ATOM   10624 C  CG    . ARG A 1 2801 ? 127.918 165.706 166.529 1.00 65.04  ? 2801 ARG A CG    1 
ATOM   10625 C  CD    . ARG A 1 2801 ? 129.181 164.887 166.332 1.00 74.72  ? 2801 ARG A CD    1 
ATOM   10626 N  NE    . ARG A 1 2801 ? 130.381 165.653 166.647 1.00 75.53  ? 2801 ARG A NE    1 
ATOM   10627 C  CZ    . ARG A 1 2801 ? 131.596 165.132 166.746 1.00 74.20  ? 2801 ARG A CZ    1 
ATOM   10628 N  NH1   . ARG A 1 2801 ? 131.811 163.840 166.563 1.00 70.00  ? 2801 ARG A NH1   1 
ATOM   10629 N  NH2   . ARG A 1 2801 ? 132.622 165.928 167.036 1.00 68.30  ? 2801 ARG A NH2   1 
ATOM   10630 N  N     . TRP A 1 2802 ? 124.260 164.274 169.043 1.00 53.29  ? 2802 TRP A N     1 
ATOM   10631 C  CA    . TRP A 1 2802 ? 123.135 163.397 169.349 1.00 50.32  ? 2802 TRP A CA    1 
ATOM   10632 C  C     . TRP A 1 2802 ? 121.809 164.096 169.087 1.00 55.73  ? 2802 TRP A C     1 
ATOM   10633 O  O     . TRP A 1 2802 ? 120.920 163.551 168.420 1.00 69.99  ? 2802 TRP A O     1 
ATOM   10634 C  CB    . TRP A 1 2802 ? 123.233 162.968 170.811 1.00 47.64  ? 2802 TRP A CB    1 
ATOM   10635 C  CG    . TRP A 1 2802 ? 122.599 161.673 171.142 1.00 45.54  ? 2802 TRP A CG    1 
ATOM   10636 C  CD1   . TRP A 1 2802 ? 121.611 161.040 170.455 1.00 54.31  ? 2802 TRP A CD1   1 
ATOM   10637 C  CD2   . TRP A 1 2802 ? 122.905 160.845 172.265 1.00 46.01  ? 2802 TRP A CD2   1 
ATOM   10638 N  NE1   . TRP A 1 2802 ? 121.284 159.861 171.079 1.00 60.40  ? 2802 TRP A NE1   1 
ATOM   10639 C  CE2   . TRP A 1 2802 ? 122.066 159.720 172.195 1.00 55.05  ? 2802 TRP A CE2   1 
ATOM   10640 C  CE3   . TRP A 1 2802 ? 123.811 160.946 173.324 1.00 47.83  ? 2802 TRP A CE3   1 
ATOM   10641 C  CZ2   . TRP A 1 2802 ? 122.105 158.703 173.141 1.00 59.95  ? 2802 TRP A CZ2   1 
ATOM   10642 C  CZ3   . TRP A 1 2802 ? 123.847 159.937 174.262 1.00 57.41  ? 2802 TRP A CZ3   1 
ATOM   10643 C  CH2   . TRP A 1 2802 ? 123.000 158.829 174.165 1.00 63.19  ? 2802 TRP A CH2   1 
ATOM   10644 N  N     . VAL A 1 2803 ? 121.665 165.312 169.614 1.00 57.21  ? 2803 VAL A N     1 
ATOM   10645 C  CA    . VAL A 1 2803 ? 120.429 166.066 169.435 1.00 54.94  ? 2803 VAL A CA    1 
ATOM   10646 C  C     . VAL A 1 2803 ? 120.217 166.396 167.963 1.00 62.18  ? 2803 VAL A C     1 
ATOM   10647 O  O     . VAL A 1 2803 ? 119.098 166.294 167.446 1.00 67.62  ? 2803 VAL A O     1 
ATOM   10648 C  CB    . VAL A 1 2803 ? 120.445 167.333 170.308 1.00 53.61  ? 2803 VAL A CB    1 
ATOM   10649 C  CG1   . VAL A 1 2803 ? 119.190 168.147 170.080 1.00 55.57  ? 2803 VAL A CG1   1 
ATOM   10650 C  CG2   . VAL A 1 2803 ? 120.570 166.959 171.773 1.00 57.65  ? 2803 VAL A CG2   1 
ATOM   10651 N  N     . ARG A 1 2804 ? 121.286 166.787 167.264 1.00 65.24  ? 2804 ARG A N     1 
ATOM   10652 C  CA    . ARG A 1 2804 ? 121.168 167.086 165.840 1.00 62.54  ? 2804 ARG A CA    1 
ATOM   10653 C  C     . ARG A 1 2804 ? 120.723 165.861 165.053 1.00 70.11  ? 2804 ARG A C     1 
ATOM   10654 O  O     . ARG A 1 2804 ? 119.856 165.959 164.178 1.00 77.95  ? 2804 ARG A O     1 
ATOM   10655 C  CB    . ARG A 1 2804 ? 122.498 167.610 165.299 1.00 63.57  ? 2804 ARG A CB    1 
ATOM   10656 C  CG    . ARG A 1 2804 ? 122.715 169.099 165.501 1.00 70.84  ? 2804 ARG A CG    1 
ATOM   10657 C  CD    . ARG A 1 2804 ? 121.549 169.914 164.966 1.00 77.06  ? 2804 ARG A CD    1 
ATOM   10658 N  NE    . ARG A 1 2804 ? 121.216 169.572 163.589 1.00 77.56  ? 2804 ARG A NE    1 
ATOM   10659 C  CZ    . ARG A 1 2804 ? 120.255 170.154 162.886 1.00 75.94  ? 2804 ARG A CZ    1 
ATOM   10660 N  NH1   . ARG A 1 2804 ? 119.505 171.114 163.402 1.00 70.09  ? 2804 ARG A NH1   1 
ATOM   10661 N  NH2   . ARG A 1 2804 ? 120.040 169.764 161.633 1.00 74.05  ? 2804 ARG A NH2   1 
ATOM   10662 N  N     . GLY A 1 2805 ? 121.301 164.696 165.352 1.00 62.35  ? 2805 GLY A N     1 
ATOM   10663 C  CA    . GLY A 1 2805 ? 120.919 163.488 164.642 1.00 56.85  ? 2805 GLY A CA    1 
ATOM   10664 C  C     . GLY A 1 2805 ? 119.481 163.086 164.905 1.00 64.73  ? 2805 GLY A C     1 
ATOM   10665 O  O     . GLY A 1 2805 ? 118.748 162.732 163.976 1.00 74.95  ? 2805 GLY A O     1 
ATOM   10666 N  N     . ILE A 1 2806 ? 119.054 163.141 166.169 1.00 58.24  ? 2806 ILE A N     1 
ATOM   10667 C  CA    . ILE A 1 2806 ? 117.672 162.793 166.490 1.00 50.53  ? 2806 ILE A CA    1 
ATOM   10668 C  C     . ILE A 1 2806 ? 116.707 163.761 165.816 1.00 61.57  ? 2806 ILE A C     1 
ATOM   10669 O  O     . ILE A 1 2806 ? 115.677 163.351 165.266 1.00 64.65  ? 2806 ILE A O     1 
ATOM   10670 C  CB    . ILE A 1 2806 ? 117.464 162.750 168.015 1.00 47.85  ? 2806 ILE A CB    1 
ATOM   10671 C  CG1   . ILE A 1 2806 ? 118.355 161.678 168.641 1.00 55.09  ? 2806 ILE A CG1   1 
ATOM   10672 C  CG2   . ILE A 1 2806 ? 116.011 162.471 168.344 1.00 53.17  ? 2806 ILE A CG2   1 
ATOM   10673 C  CD1   . ILE A 1 2806 ? 118.138 161.496 170.124 1.00 59.41  ? 2806 ILE A CD1   1 
ATOM   10674 N  N     . PHE A 1 2807 ? 117.025 165.058 165.839 1.00 69.72  ? 2807 PHE A N     1 
ATOM   10675 C  CA    . PHE A 1 2807 ? 116.158 166.044 165.203 1.00 64.45  ? 2807 PHE A CA    1 
ATOM   10676 C  C     . PHE A 1 2807 ? 116.088 165.836 163.696 1.00 72.87  ? 2807 PHE A C     1 
ATOM   10677 O  O     . PHE A 1 2807 ? 115.009 165.927 163.100 1.00 84.35  ? 2807 PHE A O     1 
ATOM   10678 C  CB    . PHE A 1 2807 ? 116.647 167.454 165.531 1.00 66.25  ? 2807 PHE A CB    1 
ATOM   10679 C  CG    . PHE A 1 2807 ? 115.969 168.530 164.738 1.00 71.12  ? 2807 PHE A CG    1 
ATOM   10680 C  CD1   . PHE A 1 2807 ? 114.647 168.859 164.981 1.00 71.74  ? 2807 PHE A CD1   1 
ATOM   10681 C  CD2   . PHE A 1 2807 ? 116.656 169.220 163.755 1.00 72.46  ? 2807 PHE A CD2   1 
ATOM   10682 C  CE1   . PHE A 1 2807 ? 114.022 169.849 164.254 1.00 73.98  ? 2807 PHE A CE1   1 
ATOM   10683 C  CE2   . PHE A 1 2807 ? 116.036 170.212 163.025 1.00 71.86  ? 2807 PHE A CE2   1 
ATOM   10684 C  CZ    . PHE A 1 2807 ? 114.717 170.528 163.275 1.00 75.78  ? 2807 PHE A CZ    1 
ATOM   10685 N  N     . GLU A 1 2808 ? 117.229 165.558 163.059 1.00 70.62  ? 2808 GLU A N     1 
ATOM   10686 C  CA    . GLU A 1 2808 ? 117.236 165.340 161.617 1.00 71.03  ? 2808 GLU A CA    1 
ATOM   10687 C  C     . GLU A 1 2808 ? 116.460 164.084 161.245 1.00 73.57  ? 2808 GLU A C     1 
ATOM   10688 O  O     . GLU A 1 2808 ? 115.778 164.050 160.215 1.00 79.67  ? 2808 GLU A O     1 
ATOM   10689 C  CB    . GLU A 1 2808 ? 118.673 165.259 161.105 1.00 75.58  ? 2808 GLU A CB    1 
ATOM   10690 C  CG    . GLU A 1 2808 ? 119.266 166.606 160.727 1.00 78.68  ? 2808 GLU A CG    1 
ATOM   10691 C  CD    . GLU A 1 2808 ? 120.777 166.631 160.839 1.00 84.23  ? 2808 GLU A CD    1 
ATOM   10692 O  OE1   . GLU A 1 2808 ? 121.347 165.681 161.416 1.00 87.41  ? 2808 GLU A OE1   1 
ATOM   10693 O  OE2   . GLU A 1 2808 ? 121.394 167.600 160.351 1.00 79.83  ? 2808 GLU A OE2   1 
ATOM   10694 N  N     . ALA A 1 2809 ? 116.561 163.037 162.065 1.00 65.92  ? 2809 ALA A N     1 
ATOM   10695 C  CA    . ALA A 1 2809 ? 115.773 161.835 161.817 1.00 68.52  ? 2809 ALA A CA    1 
ATOM   10696 C  C     . ALA A 1 2809 ? 114.284 162.104 161.999 1.00 69.14  ? 2809 ALA A C     1 
ATOM   10697 O  O     . ALA A 1 2809 ? 113.456 161.570 161.251 1.00 74.30  ? 2809 ALA A O     1 
ATOM   10698 C  CB    . ALA A 1 2809 ? 116.233 160.706 162.737 1.00 69.86  ? 2809 ALA A CB    1 
ATOM   10699 N  N     . LEU A 1 2810 ? 113.924 162.926 162.986 1.00 64.89  ? 2810 LEU A N     1 
ATOM   10700 C  CA    . LEU A 1 2810 ? 112.520 163.172 163.295 1.00 67.78  ? 2810 LEU A CA    1 
ATOM   10701 C  C     . LEU A 1 2810 ? 111.906 164.294 162.468 1.00 77.45  ? 2810 LEU A C     1 
ATOM   10702 O  O     . LEU A 1 2810 ? 110.681 164.453 162.489 1.00 81.98  ? 2810 LEU A O     1 
ATOM   10703 C  CB    . LEU A 1 2810 ? 112.360 163.508 164.779 1.00 61.51  ? 2810 LEU A CB    1 
ATOM   10704 C  CG    . LEU A 1 2810 ? 112.483 162.350 165.767 1.00 66.49  ? 2810 LEU A CG    1 
ATOM   10705 C  CD1   . LEU A 1 2810 ? 112.147 162.807 167.176 1.00 70.11  ? 2810 LEU A CD1   1 
ATOM   10706 C  CD2   . LEU A 1 2810 ? 111.586 161.213 165.348 1.00 73.05  ? 2810 LEU A CD2   1 
ATOM   10707 N  N     . ARG A 1 2811 ? 112.717 165.079 161.758 1.00 84.01  ? 2811 ARG A N     1 
ATOM   10708 C  CA    . ARG A 1 2811 ? 112.188 166.261 161.079 1.00 76.74  ? 2811 ARG A CA    1 
ATOM   10709 C  C     . ARG A 1 2811 ? 111.169 165.935 159.992 1.00 82.49  ? 2811 ARG A C     1 
ATOM   10710 O  O     . ARG A 1 2811 ? 110.061 166.498 160.034 1.00 87.28  ? 2811 ARG A O     1 
ATOM   10711 C  CB    . ARG A 1 2811 ? 113.343 167.100 160.522 1.00 77.88  ? 2811 ARG A CB    1 
ATOM   10712 C  CG    . ARG A 1 2811 ? 112.925 168.490 160.077 1.00 84.07  ? 2811 ARG A CG    1 
ATOM   10713 C  CD    . ARG A 1 2811 ? 113.718 168.949 158.865 1.00 86.14  ? 2811 ARG A CD    1 
ATOM   10714 N  NE    . ARG A 1 2811 ? 115.131 168.609 158.970 1.00 89.40  ? 2811 ARG A NE    1 
ATOM   10715 C  CZ    . ARG A 1 2811 ? 116.082 169.468 159.314 1.00 88.39  ? 2811 ARG A CZ    1 
ATOM   10716 N  NH1   . ARG A 1 2811 ? 115.803 170.729 159.600 1.00 82.29  ? 2811 ARG A NH1   1 
ATOM   10717 N  NH2   . ARG A 1 2811 ? 117.343 169.050 159.371 1.00 86.17  ? 2811 ARG A NH2   1 
ATOM   10718 N  N     . PRO A 1 2812 ? 111.446 165.066 159.011 1.00 84.99  ? 2812 PRO A N     1 
ATOM   10719 C  CA    . PRO A 1 2812 ? 110.448 164.839 157.954 1.00 84.92  ? 2812 PRO A CA    1 
ATOM   10720 C  C     . PRO A 1 2812 ? 109.270 163.999 158.402 1.00 85.09  ? 2812 PRO A C     1 
ATOM   10721 O  O     . PRO A 1 2812 ? 108.216 164.046 157.757 1.00 89.34  ? 2812 PRO A O     1 
ATOM   10722 C  CB    . PRO A 1 2812 ? 111.251 164.126 156.861 1.00 86.68  ? 2812 PRO A CB    1 
ATOM   10723 C  CG    . PRO A 1 2812 ? 112.291 163.389 157.610 1.00 86.70  ? 2812 PRO A CG    1 
ATOM   10724 C  CD    . PRO A 1 2812 ? 112.665 164.266 158.776 1.00 87.59  ? 2812 PRO A CD    1 
ATOM   10725 N  N     . LEU A 1 2813 ? 109.413 163.232 159.477 1.00 89.67  ? 2813 LEU A N     1 
ATOM   10726 C  CA    . LEU A 1 2813 ? 108.370 162.300 159.877 1.00 96.39  ? 2813 LEU A CA    1 
ATOM   10727 C  C     . LEU A 1 2813 ? 107.203 163.033 160.527 1.00 96.71  ? 2813 LEU A C     1 
ATOM   10728 O  O     . LEU A 1 2813 ? 107.391 163.953 161.329 1.00 98.21  ? 2813 LEU A O     1 
ATOM   10729 C  CB    . LEU A 1 2813 ? 108.952 161.253 160.823 1.00 93.16  ? 2813 LEU A CB    1 
ATOM   10730 C  CG    . LEU A 1 2813 ? 110.205 160.595 160.237 1.00 96.92  ? 2813 LEU A CG    1 
ATOM   10731 C  CD1   . LEU A 1 2813 ? 110.727 159.492 161.136 1.00 93.62  ? 2813 LEU A CD1   1 
ATOM   10732 C  CD2   . LEU A 1 2813 ? 109.925 160.060 158.836 1.00 97.49  ? 2813 LEU A CD2   1 
ATOM   10733 N  N     . GLU A 1 2814 ? 105.987 162.618 160.172 1.00 113.28 ? 2814 GLU A N     1 
ATOM   10734 C  CA    . GLU A 1 2814 ? 104.777 163.264 160.665 1.00 114.66 ? 2814 GLU A CA    1 
ATOM   10735 C  C     . GLU A 1 2814 ? 104.277 162.671 161.975 1.00 112.22 ? 2814 GLU A C     1 
ATOM   10736 O  O     . GLU A 1 2814 ? 103.749 163.407 162.816 1.00 113.04 ? 2814 GLU A O     1 
ATOM   10737 C  CB    . GLU A 1 2814 ? 103.669 163.181 159.612 1.00 114.49 ? 2814 GLU A CB    1 
ATOM   10738 C  CG    . GLU A 1 2814 ? 104.145 163.399 158.183 1.00 115.36 ? 2814 GLU A CG    1 
ATOM   10739 C  CD    . GLU A 1 2814 ? 104.395 162.097 157.445 1.00 118.79 ? 2814 GLU A CD    1 
ATOM   10740 O  OE1   . GLU A 1 2814 ? 105.136 161.242 157.974 1.00 117.01 ? 2814 GLU A OE1   1 
ATOM   10741 O  OE2   . GLU A 1 2814 ? 103.846 161.926 156.335 1.00 119.41 ? 2814 GLU A OE2   1 
ATOM   10742 N  N     . THR A 1 2815 ? 104.426 161.362 162.171 1.00 110.52 ? 2815 THR A N     1 
ATOM   10743 C  CA    . THR A 1 2815 ? 104.013 160.724 163.412 1.00 113.31 ? 2815 THR A CA    1 
ATOM   10744 C  C     . THR A 1 2815 ? 104.941 159.551 163.689 1.00 116.21 ? 2815 THR A C     1 
ATOM   10745 O  O     . THR A 1 2815 ? 105.490 158.939 162.769 1.00 119.46 ? 2815 THR A O     1 
ATOM   10746 C  CB    . THR A 1 2815 ? 102.552 160.261 163.354 1.00 115.11 ? 2815 THR A CB    1 
ATOM   10747 O  OG1   . THR A 1 2815 ? 102.186 159.673 164.608 1.00 114.70 ? 2815 THR A OG1   1 
ATOM   10748 C  CG2   . THR A 1 2815 ? 102.352 159.242 162.236 1.00 112.08 ? 2815 THR A CG2   1 
ATOM   10749 N  N     . LEU A 1 2816 ? 105.115 159.243 164.973 1.00 96.47  ? 2816 LEU A N     1 
ATOM   10750 C  CA    . LEU A 1 2816 ? 106.095 158.238 165.366 1.00 92.85  ? 2816 LEU A CA    1 
ATOM   10751 C  C     . LEU A 1 2816 ? 105.902 157.829 166.821 1.00 93.52  ? 2816 LEU A C     1 
ATOM   10752 O  O     . LEU A 1 2816 ? 105.891 158.692 167.707 1.00 97.63  ? 2816 LEU A O     1 
ATOM   10753 C  CB    . LEU A 1 2816 ? 107.506 158.784 165.121 1.00 92.28  ? 2816 LEU A CB    1 
ATOM   10754 C  CG    . LEU A 1 2816 ? 108.736 157.899 165.290 1.00 94.55  ? 2816 LEU A CG    1 
ATOM   10755 C  CD1   . LEU A 1 2816 ? 109.794 158.364 164.338 1.00 94.44  ? 2816 LEU A CD1   1 
ATOM   10756 C  CD2   . LEU A 1 2816 ? 109.271 158.045 166.691 1.00 93.38  ? 2816 LEU A CD2   1 
ATOM   10757 N  N     . PRO A 1 2817 ? 105.757 156.536 167.110 1.00 87.01  ? 2817 PRO A N     1 
ATOM   10758 C  CA    . PRO A 1 2817 ? 105.559 156.099 168.499 1.00 86.68  ? 2817 PRO A CA    1 
ATOM   10759 C  C     . PRO A 1 2817 ? 106.855 156.143 169.295 1.00 88.63  ? 2817 PRO A C     1 
ATOM   10760 O  O     . PRO A 1 2817 ? 107.951 156.294 168.759 1.00 94.60  ? 2817 PRO A O     1 
ATOM   10761 C  CB    . PRO A 1 2817 ? 105.052 154.664 168.353 1.00 86.07  ? 2817 PRO A CB    1 
ATOM   10762 C  CG    . PRO A 1 2817 ? 105.618 154.203 167.050 1.00 86.50  ? 2817 PRO A CG    1 
ATOM   10763 C  CD    . PRO A 1 2817 ? 105.662 155.415 166.157 1.00 84.88  ? 2817 PRO A CD    1 
ATOM   10764 N  N     . VAL A 1 2818 ? 106.715 155.963 170.610 1.00 83.78  ? 2818 VAL A N     1 
ATOM   10765 C  CA    . VAL A 1 2818 ? 107.866 156.079 171.503 1.00 81.60  ? 2818 VAL A CA    1 
ATOM   10766 C  C     . VAL A 1 2818 ? 108.944 155.053 171.164 1.00 83.70  ? 2818 VAL A C     1 
ATOM   10767 O  O     . VAL A 1 2818 ? 110.140 155.321 171.336 1.00 86.13  ? 2818 VAL A O     1 
ATOM   10768 C  CB    . VAL A 1 2818 ? 107.400 155.966 172.967 1.00 82.40  ? 2818 VAL A CB    1 
ATOM   10769 C  CG1   . VAL A 1 2818 ? 106.735 154.628 173.203 1.00 85.99  ? 2818 VAL A CG1   1 
ATOM   10770 C  CG2   . VAL A 1 2818 ? 108.568 156.170 173.924 1.00 81.58  ? 2818 VAL A CG2   1 
ATOM   10771 N  N     . GLU A 1 2819 ? 108.553 153.879 170.658 1.00 87.00  ? 2819 GLU A N     1 
ATOM   10772 C  CA    . GLU A 1 2819 ? 109.535 152.858 170.299 1.00 83.16  ? 2819 GLU A CA    1 
ATOM   10773 C  C     . GLU A 1 2819 ? 110.457 153.341 169.185 1.00 86.14  ? 2819 GLU A C     1 
ATOM   10774 O  O     . GLU A 1 2819 ? 111.667 153.089 169.215 1.00 90.08  ? 2819 GLU A O     1 
ATOM   10775 C  CB    . GLU A 1 2819 ? 108.819 151.575 169.885 1.00 87.00  ? 2819 GLU A CB    1 
ATOM   10776 C  CG    . GLU A 1 2819 ? 108.335 150.739 171.054 1.00 92.55  ? 2819 GLU A CG    1 
ATOM   10777 C  CD    . GLU A 1 2819 ? 106.919 151.095 171.470 1.00 97.07  ? 2819 GLU A CD    1 
ATOM   10778 O  OE1   . GLU A 1 2819 ? 106.294 151.942 170.798 1.00 93.36  ? 2819 GLU A OE1   1 
ATOM   10779 O  OE2   . GLU A 1 2819 ? 106.429 150.527 172.468 1.00 101.43 ? 2819 GLU A OE2   1 
ATOM   10780 N  N     . GLY A 1 2820 ? 109.901 154.032 168.188 1.00 82.31  ? 2820 GLY A N     1 
ATOM   10781 C  CA    . GLY A 1 2820 ? 110.735 154.594 167.139 1.00 81.24  ? 2820 GLY A CA    1 
ATOM   10782 C  C     . GLY A 1 2820 ? 111.703 155.638 167.663 1.00 81.46  ? 2820 GLY A C     1 
ATOM   10783 O  O     . GLY A 1 2820 ? 112.853 155.711 167.221 1.00 87.15  ? 2820 GLY A O     1 
ATOM   10784 N  N     . LEU A 1 2821 ? 111.250 156.462 168.610 1.00 68.61  ? 2821 LEU A N     1 
ATOM   10785 C  CA    . LEU A 1 2821 ? 112.137 157.450 169.212 1.00 66.79  ? 2821 LEU A CA    1 
ATOM   10786 C  C     . LEU A 1 2821 ? 113.281 156.776 169.955 1.00 69.09  ? 2821 LEU A C     1 
ATOM   10787 O  O     . LEU A 1 2821 ? 114.436 157.204 169.853 1.00 71.31  ? 2821 LEU A O     1 
ATOM   10788 C  CB    . LEU A 1 2821 ? 111.347 158.363 170.149 1.00 64.86  ? 2821 LEU A CB    1 
ATOM   10789 C  CG    . LEU A 1 2821 ? 112.164 159.338 170.997 1.00 62.16  ? 2821 LEU A CG    1 
ATOM   10790 C  CD1   . LEU A 1 2821 ? 112.717 160.463 170.139 1.00 64.74  ? 2821 LEU A CD1   1 
ATOM   10791 C  CD2   . LEU A 1 2821 ? 111.322 159.889 172.133 1.00 64.33  ? 2821 LEU A CD2   1 
ATOM   10792 N  N     . ILE A 1 2822 ? 112.982 155.708 170.699 1.00 69.69  ? 2822 ILE A N     1 
ATOM   10793 C  CA    . ILE A 1 2822 ? 114.038 154.991 171.406 1.00 61.83  ? 2822 ILE A CA    1 
ATOM   10794 C  C     . ILE A 1 2822 ? 114.994 154.335 170.418 1.00 67.26  ? 2822 ILE A C     1 
ATOM   10795 O  O     . ILE A 1 2822 ? 116.207 154.284 170.652 1.00 74.84  ? 2822 ILE A O     1 
ATOM   10796 C  CB    . ILE A 1 2822 ? 113.437 153.963 172.381 1.00 65.98  ? 2822 ILE A CB    1 
ATOM   10797 C  CG1   . ILE A 1 2822 ? 112.422 154.636 173.300 1.00 70.02  ? 2822 ILE A CG1   1 
ATOM   10798 C  CG2   . ILE A 1 2822 ? 114.530 153.306 173.204 1.00 66.70  ? 2822 ILE A CG2   1 
ATOM   10799 C  CD1   . ILE A 1 2822 ? 112.976 155.822 174.043 1.00 72.84  ? 2822 ILE A CD1   1 
ATOM   10800 N  N     . ARG A 1 2823 ? 114.471 153.817 169.305 1.00 72.45  ? 2823 ARG A N     1 
ATOM   10801 C  CA    . ARG A 1 2823 ? 115.340 153.222 168.296 1.00 73.45  ? 2823 ARG A CA    1 
ATOM   10802 C  C     . ARG A 1 2823 ? 116.281 154.257 167.693 1.00 82.47  ? 2823 ARG A C     1 
ATOM   10803 O  O     . ARG A 1 2823 ? 117.474 153.989 167.510 1.00 89.80  ? 2823 ARG A O     1 
ATOM   10804 C  CB    . ARG A 1 2823 ? 114.506 152.558 167.201 1.00 74.05  ? 2823 ARG A CB    1 
ATOM   10805 C  CG    . ARG A 1 2823 ? 115.311 151.642 166.296 1.00 73.15  ? 2823 ARG A CG    1 
ATOM   10806 C  CD    . ARG A 1 2823 ? 114.425 150.630 165.592 1.00 78.68  ? 2823 ARG A CD    1 
ATOM   10807 N  NE    . ARG A 1 2823 ? 115.198 149.727 164.748 1.00 87.23  ? 2823 ARG A NE    1 
ATOM   10808 C  CZ    . ARG A 1 2823 ? 115.872 148.676 165.194 1.00 84.16  ? 2823 ARG A CZ    1 
ATOM   10809 N  NH1   . ARG A 1 2823 ? 115.888 148.359 166.478 1.00 79.46  ? 2823 ARG A NH1   1 
ATOM   10810 N  NH2   . ARG A 1 2823 ? 116.548 147.924 164.330 1.00 82.38  ? 2823 ARG A NH2   1 
ATOM   10811 N  N     . ILE A 1 2824 ? 115.764 155.448 167.379 1.00 71.23  ? 2824 ILE A N     1 
ATOM   10812 C  CA    . ILE A 1 2824 ? 116.615 156.509 166.843 1.00 63.31  ? 2824 ILE A CA    1 
ATOM   10813 C  C     . ILE A 1 2824 ? 117.658 156.925 167.872 1.00 61.22  ? 2824 ILE A C     1 
ATOM   10814 O  O     . ILE A 1 2824 ? 118.830 157.149 167.541 1.00 67.04  ? 2824 ILE A O     1 
ATOM   10815 C  CB    . ILE A 1 2824 ? 115.763 157.706 166.384 1.00 53.57  ? 2824 ILE A CB    1 
ATOM   10816 C  CG1   . ILE A 1 2824 ? 114.834 157.293 165.243 1.00 65.68  ? 2824 ILE A CG1   1 
ATOM   10817 C  CG2   . ILE A 1 2824 ? 116.650 158.854 165.944 1.00 51.98  ? 2824 ILE A CG2   1 
ATOM   10818 C  CD1   . ILE A 1 2824 ? 113.962 158.415 164.733 1.00 68.56  ? 2824 ILE A CD1   1 
ATOM   10819 N  N     . TRP A 1 2825 ? 117.244 157.043 169.135 1.00 59.39  ? 2825 TRP A N     1 
ATOM   10820 C  CA    . TRP A 1 2825 ? 118.168 157.400 170.207 1.00 57.27  ? 2825 TRP A CA    1 
ATOM   10821 C  C     . TRP A 1 2825 ? 119.293 156.378 170.324 1.00 64.89  ? 2825 TRP A C     1 
ATOM   10822 O  O     . TRP A 1 2825 ? 120.472 156.739 170.419 1.00 71.91  ? 2825 TRP A O     1 
ATOM   10823 C  CB    . TRP A 1 2825 ? 117.386 157.517 171.518 1.00 56.25  ? 2825 TRP A CB    1 
ATOM   10824 C  CG    . TRP A 1 2825 ? 118.213 157.661 172.751 1.00 57.48  ? 2825 TRP A CG    1 
ATOM   10825 C  CD1   . TRP A 1 2825 ? 118.620 158.823 173.330 1.00 65.54  ? 2825 TRP A CD1   1 
ATOM   10826 C  CD2   . TRP A 1 2825 ? 118.710 156.604 173.578 1.00 60.37  ? 2825 TRP A CD2   1 
ATOM   10827 N  NE1   . TRP A 1 2825 ? 119.348 158.558 174.462 1.00 65.78  ? 2825 TRP A NE1   1 
ATOM   10828 C  CE2   . TRP A 1 2825 ? 119.422 157.202 174.635 1.00 58.93  ? 2825 TRP A CE2   1 
ATOM   10829 C  CE3   . TRP A 1 2825 ? 118.630 155.210 173.524 1.00 66.07  ? 2825 TRP A CE3   1 
ATOM   10830 C  CZ2   . TRP A 1 2825 ? 120.049 156.457 175.628 1.00 63.71  ? 2825 TRP A CZ2   1 
ATOM   10831 C  CZ3   . TRP A 1 2825 ? 119.254 154.472 174.510 1.00 67.67  ? 2825 TRP A CZ3   1 
ATOM   10832 C  CH2   . TRP A 1 2825 ? 119.954 155.096 175.548 1.00 70.58  ? 2825 TRP A CH2   1 
ATOM   10833 N  N     . ALA A 1 2826 ? 118.944 155.090 170.296 1.00 64.36  ? 2826 ALA A N     1 
ATOM   10834 C  CA    . ALA A 1 2826 ? 119.950 154.038 170.393 1.00 61.42  ? 2826 ALA A CA    1 
ATOM   10835 C  C     . ALA A 1 2826 ? 120.872 154.037 169.181 1.00 63.15  ? 2826 ALA A C     1 
ATOM   10836 O  O     . ALA A 1 2826 ? 122.081 153.821 169.318 1.00 76.32  ? 2826 ALA A O     1 
ATOM   10837 C  CB    . ALA A 1 2826 ? 119.274 152.678 170.554 1.00 60.08  ? 2826 ALA A CB    1 
ATOM   10838 N  N     . HIS A 1 2827 ? 120.323 154.266 167.986 1.00 54.67  ? 2827 HIS A N     1 
ATOM   10839 C  CA    . HIS A 1 2827 ? 121.161 154.295 166.791 1.00 60.08  ? 2827 HIS A CA    1 
ATOM   10840 C  C     . HIS A 1 2827 ? 122.151 155.450 166.843 1.00 64.73  ? 2827 HIS A C     1 
ATOM   10841 O  O     . HIS A 1 2827 ? 123.324 155.289 166.485 1.00 74.05  ? 2827 HIS A O     1 
ATOM   10842 C  CB    . HIS A 1 2827 ? 120.295 154.393 165.538 1.00 55.18  ? 2827 HIS A CB    1 
ATOM   10843 C  CG    . HIS A 1 2827 ? 121.081 154.603 164.282 1.00 57.20  ? 2827 HIS A CG    1 
ATOM   10844 N  ND1   . HIS A 1 2827 ? 121.082 155.797 163.595 1.00 63.80  ? 2827 HIS A ND1   1 
ATOM   10845 C  CD2   . HIS A 1 2827 ? 121.899 153.772 163.594 1.00 64.47  ? 2827 HIS A CD2   1 
ATOM   10846 C  CE1   . HIS A 1 2827 ? 121.863 155.692 162.534 1.00 71.06  ? 2827 HIS A CE1   1 
ATOM   10847 N  NE2   . HIS A 1 2827 ? 122.371 154.473 162.511 1.00 71.34  ? 2827 HIS A NE2   1 
ATOM   10848 N  N     . GLU A 1 2828 ? 121.698 156.624 167.286 1.00 65.02  ? 2828 GLU A N     1 
ATOM   10849 C  CA    . GLU A 1 2828 ? 122.610 157.755 167.418 1.00 59.12  ? 2828 GLU A CA    1 
ATOM   10850 C  C     . GLU A 1 2828 ? 123.669 157.486 168.479 1.00 61.32  ? 2828 GLU A C     1 
ATOM   10851 O  O     . GLU A 1 2828 ? 124.841 157.843 168.299 1.00 70.33  ? 2828 GLU A O     1 
ATOM   10852 C  CB    . GLU A 1 2828 ? 121.829 159.026 167.741 1.00 59.44  ? 2828 GLU A CB    1 
ATOM   10853 C  CG    . GLU A 1 2828 ? 120.933 159.504 166.614 1.00 67.19  ? 2828 GLU A CG    1 
ATOM   10854 C  CD    . GLU A 1 2828 ? 121.705 159.843 165.355 1.00 70.96  ? 2828 GLU A CD    1 
ATOM   10855 O  OE1   . GLU A 1 2828 ? 122.869 160.280 165.466 1.00 69.37  ? 2828 GLU A OE1   1 
ATOM   10856 O  OE2   . GLU A 1 2828 ? 121.145 159.671 164.252 1.00 77.78  ? 2828 GLU A OE2   1 
ATOM   10857 N  N     . ALA A 1 2829 ? 123.279 156.855 169.590 1.00 47.55  ? 2829 ALA A N     1 
ATOM   10858 C  CA    . ALA A 1 2829 ? 124.256 156.501 170.614 1.00 46.54  ? 2829 ALA A CA    1 
ATOM   10859 C  C     . ALA A 1 2829 ? 125.307 155.548 170.063 1.00 57.93  ? 2829 ALA A C     1 
ATOM   10860 O  O     . ALA A 1 2829 ? 126.501 155.695 170.349 1.00 68.01  ? 2829 ALA A O     1 
ATOM   10861 C  CB    . ALA A 1 2829 ? 123.553 155.880 171.819 1.00 52.21  ? 2829 ALA A CB    1 
ATOM   10862 N  N     . LEU A 1 2830 ? 124.880 154.559 169.276 1.00 60.31  ? 2830 LEU A N     1 
ATOM   10863 C  CA    . LEU A 1 2830 ? 125.829 153.640 168.658 1.00 56.46  ? 2830 LEU A CA    1 
ATOM   10864 C  C     . LEU A 1 2830 ? 126.758 154.370 167.697 1.00 59.81  ? 2830 LEU A C     1 
ATOM   10865 O  O     . LEU A 1 2830 ? 127.970 154.125 167.688 1.00 70.19  ? 2830 LEU A O     1 
ATOM   10866 C  CB    . LEU A 1 2830 ? 125.081 152.524 167.930 1.00 55.30  ? 2830 LEU A CB    1 
ATOM   10867 C  CG    . LEU A 1 2830 ? 124.392 151.477 168.802 1.00 53.21  ? 2830 LEU A CG    1 
ATOM   10868 C  CD1   . LEU A 1 2830 ? 123.464 150.618 167.964 1.00 54.65  ? 2830 LEU A CD1   1 
ATOM   10869 C  CD2   . LEU A 1 2830 ? 125.427 150.620 169.502 1.00 61.36  ? 2830 LEU A CD2   1 
ATOM   10870 N  N     . ARG A 1 2831 ? 126.211 155.272 166.882 1.00 56.65  ? 2831 ARG A N     1 
ATOM   10871 C  CA    . ARG A 1 2831 ? 127.039 155.969 165.903 1.00 58.19  ? 2831 ARG A CA    1 
ATOM   10872 C  C     . ARG A 1 2831 ? 128.017 156.931 166.565 1.00 57.10  ? 2831 ARG A C     1 
ATOM   10873 O  O     . ARG A 1 2831 ? 129.077 157.217 165.998 1.00 62.02  ? 2831 ARG A O     1 
ATOM   10874 C  CB    . ARG A 1 2831 ? 126.160 156.713 164.900 1.00 58.00  ? 2831 ARG A CB    1 
ATOM   10875 C  CG    . ARG A 1 2831 ? 125.376 155.806 163.964 1.00 60.10  ? 2831 ARG A CG    1 
ATOM   10876 C  CD    . ARG A 1 2831 ? 126.276 155.168 162.916 1.00 58.54  ? 2831 ARG A CD    1 
ATOM   10877 N  NE    . ARG A 1 2831 ? 126.874 153.923 163.383 1.00 58.81  ? 2831 ARG A NE    1 
ATOM   10878 C  CZ    . ARG A 1 2831 ? 126.234 152.765 163.460 1.00 66.14  ? 2831 ARG A CZ    1 
ATOM   10879 N  NH1   . ARG A 1 2831 ? 124.968 152.648 163.093 1.00 62.27  ? 2831 ARG A NH1   1 
ATOM   10880 N  NH2   . ARG A 1 2831 ? 126.880 151.695 163.914 1.00 67.65  ? 2831 ARG A NH2   1 
ATOM   10881 N  N     . LEU A 1 2832 ? 127.688 157.441 167.750 1.00 57.93  ? 2832 LEU A N     1 
ATOM   10882 C  CA    . LEU A 1 2832 ? 128.574 158.400 168.400 1.00 57.58  ? 2832 LEU A CA    1 
ATOM   10883 C  C     . LEU A 1 2832 ? 129.594 157.744 169.324 1.00 61.08  ? 2832 LEU A C     1 
ATOM   10884 O  O     . LEU A 1 2832 ? 130.783 158.072 169.259 1.00 63.31  ? 2832 LEU A O     1 
ATOM   10885 C  CB    . LEU A 1 2832 ? 127.756 159.424 169.189 1.00 51.36  ? 2832 LEU A CB    1 
ATOM   10886 C  CG    . LEU A 1 2832 ? 126.889 160.361 168.353 1.00 56.74  ? 2832 LEU A CG    1 
ATOM   10887 C  CD1   . LEU A 1 2832 ? 126.050 161.232 169.260 1.00 56.49  ? 2832 LEU A CD1   1 
ATOM   10888 C  CD2   . LEU A 1 2832 ? 127.751 161.210 167.437 1.00 62.73  ? 2832 LEU A CD2   1 
ATOM   10889 N  N     . PHE A 1 2833 ? 129.159 156.825 170.186 1.00 68.02  ? 2833 PHE A N     1 
ATOM   10890 C  CA    . PHE A 1 2833 ? 130.014 156.292 171.238 1.00 67.05  ? 2833 PHE A CA    1 
ATOM   10891 C  C     . PHE A 1 2833 ? 130.637 154.945 170.900 1.00 67.38  ? 2833 PHE A C     1 
ATOM   10892 O  O     . PHE A 1 2833 ? 131.531 154.500 171.627 1.00 80.96  ? 2833 PHE A O     1 
ATOM   10893 C  CB    . PHE A 1 2833 ? 129.221 156.167 172.544 1.00 60.66  ? 2833 PHE A CB    1 
ATOM   10894 C  CG    . PHE A 1 2833 ? 128.701 157.475 173.064 1.00 62.71  ? 2833 PHE A CG    1 
ATOM   10895 C  CD1   . PHE A 1 2833 ? 127.469 157.955 172.659 1.00 59.70  ? 2833 PHE A CD1   1 
ATOM   10896 C  CD2   . PHE A 1 2833 ? 129.446 158.226 173.953 1.00 66.83  ? 2833 PHE A CD2   1 
ATOM   10897 C  CE1   . PHE A 1 2833 ? 126.990 159.159 173.134 1.00 60.28  ? 2833 PHE A CE1   1 
ATOM   10898 C  CE2   . PHE A 1 2833 ? 128.973 159.430 174.432 1.00 68.57  ? 2833 PHE A CE2   1 
ATOM   10899 C  CZ    . PHE A 1 2833 ? 127.743 159.897 174.021 1.00 65.88  ? 2833 PHE A CZ    1 
ATOM   10900 N  N     . GLN A 1 2834 ? 130.199 154.286 169.827 1.00 61.00  ? 2834 GLN A N     1 
ATOM   10901 C  CA    . GLN A 1 2834 ? 130.724 152.977 169.469 1.00 54.78  ? 2834 GLN A CA    1 
ATOM   10902 C  C     . GLN A 1 2834 ? 131.536 152.974 168.184 1.00 61.87  ? 2834 GLN A C     1 
ATOM   10903 O  O     . GLN A 1 2834 ? 132.290 152.024 167.953 1.00 71.99  ? 2834 GLN A O     1 
ATOM   10904 C  CB    . GLN A 1 2834 ? 129.579 151.962 169.335 1.00 52.22  ? 2834 GLN A CB    1 
ATOM   10905 C  CG    . GLN A 1 2834 ? 130.008 150.514 169.471 1.00 60.11  ? 2834 GLN A CG    1 
ATOM   10906 C  CD    . GLN A 1 2834 ? 128.901 149.545 169.120 1.00 69.11  ? 2834 GLN A CD    1 
ATOM   10907 O  OE1   . GLN A 1 2834 ? 128.310 149.625 168.043 1.00 71.03  ? 2834 GLN A OE1   1 
ATOM   10908 N  NE2   . GLN A 1 2834 ? 128.612 148.621 170.028 1.00 69.78  ? 2834 GLN A NE2   1 
ATOM   10909 N  N     . ASP A 1 2835 ? 131.409 154.007 167.350 1.00 69.67  ? 2835 ASP A N     1 
ATOM   10910 C  CA    . ASP A 1 2835 ? 132.128 154.028 166.082 1.00 64.95  ? 2835 ASP A CA    1 
ATOM   10911 C  C     . ASP A 1 2835 ? 133.631 154.161 166.286 1.00 68.18  ? 2835 ASP A C     1 
ATOM   10912 O  O     . ASP A 1 2835 ? 134.414 153.602 165.510 1.00 71.39  ? 2835 ASP A O     1 
ATOM   10913 C  CB    . ASP A 1 2835 ? 131.610 155.171 165.210 1.00 69.75  ? 2835 ASP A CB    1 
ATOM   10914 C  CG    . ASP A 1 2835 ? 130.596 154.707 164.188 1.00 75.75  ? 2835 ASP A CG    1 
ATOM   10915 O  OD1   . ASP A 1 2835 ? 130.238 153.511 164.207 1.00 71.83  ? 2835 ASP A OD1   1 
ATOM   10916 O  OD2   . ASP A 1 2835 ? 130.151 155.538 163.369 1.00 73.64  ? 2835 ASP A OD2   1 
ATOM   10917 N  N     . ARG A 1 2836 ? 134.053 154.891 167.316 1.00 59.52  ? 2836 ARG A N     1 
ATOM   10918 C  CA    . ARG A 1 2836 ? 135.464 155.152 167.558 1.00 52.36  ? 2836 ARG A CA    1 
ATOM   10919 C  C     . ARG A 1 2836 ? 136.135 154.105 168.436 1.00 56.56  ? 2836 ARG A C     1 
ATOM   10920 O  O     . ARG A 1 2836 ? 137.357 154.160 168.609 1.00 62.07  ? 2836 ARG A O     1 
ATOM   10921 C  CB    . ARG A 1 2836 ? 135.635 156.529 168.204 1.00 63.95  ? 2836 ARG A CB    1 
ATOM   10922 C  CG    . ARG A 1 2836 ? 135.355 156.544 169.695 1.00 62.99  ? 2836 ARG A CG    1 
ATOM   10923 C  CD    . ARG A 1 2836 ? 135.480 157.943 170.263 1.00 62.04  ? 2836 ARG A CD    1 
ATOM   10924 N  NE    . ARG A 1 2836 ? 134.370 158.792 169.850 1.00 59.37  ? 2836 ARG A NE    1 
ATOM   10925 C  CZ    . ARG A 1 2836 ? 134.389 160.117 169.884 1.00 64.81  ? 2836 ARG A CZ    1 
ATOM   10926 N  NH1   . ARG A 1 2836 ? 135.450 160.783 170.310 1.00 68.74  ? 2836 ARG A NH1   1 
ATOM   10927 N  NH2   . ARG A 1 2836 ? 133.316 160.792 169.481 1.00 68.28  ? 2836 ARG A NH2   1 
ATOM   10928 N  N     . LEU A 1 2837 ? 135.379 153.162 168.991 1.00 66.29  ? 2837 LEU A N     1 
ATOM   10929 C  CA    . LEU A 1 2837 ? 135.952 152.188 169.909 1.00 64.16  ? 2837 LEU A CA    1 
ATOM   10930 C  C     . LEU A 1 2837 ? 136.849 151.204 169.169 1.00 68.16  ? 2837 LEU A C     1 
ATOM   10931 O  O     . LEU A 1 2837 ? 136.624 150.890 167.998 1.00 68.84  ? 2837 LEU A O     1 
ATOM   10932 C  CB    . LEU A 1 2837 ? 134.845 151.438 170.645 1.00 60.98  ? 2837 LEU A CB    1 
ATOM   10933 C  CG    . LEU A 1 2837 ? 134.059 152.272 171.655 1.00 59.53  ? 2837 LEU A CG    1 
ATOM   10934 C  CD1   . LEU A 1 2837 ? 133.041 151.408 172.368 1.00 71.18  ? 2837 LEU A CD1   1 
ATOM   10935 C  CD2   . LEU A 1 2837 ? 134.999 152.928 172.648 1.00 57.22  ? 2837 LEU A CD2   1 
ATOM   10936 N  N     . VAL A 1 2838 ? 137.872 150.716 169.865 1.00 69.56  ? 2838 VAL A N     1 
ATOM   10937 C  CA    . VAL A 1 2838 ? 138.854 149.822 169.260 1.00 67.21  ? 2838 VAL A CA    1 
ATOM   10938 C  C     . VAL A 1 2838 ? 138.551 148.364 169.575 1.00 74.18  ? 2838 VAL A C     1 
ATOM   10939 O  O     . VAL A 1 2838 ? 138.325 147.557 168.670 1.00 78.67  ? 2838 VAL A O     1 
ATOM   10940 C  CB    . VAL A 1 2838 ? 140.273 150.212 169.725 1.00 67.64  ? 2838 VAL A CB    1 
ATOM   10941 C  CG1   . VAL A 1 2838 ? 141.291 149.207 169.218 1.00 71.23  ? 2838 VAL A CG1   1 
ATOM   10942 C  CG2   . VAL A 1 2838 ? 140.617 151.614 169.256 1.00 69.79  ? 2838 VAL A CG2   1 
ATOM   10943 N  N     . GLU A 1 2839 ? 138.541 148.003 170.853 1.00 83.78  ? 2839 GLU A N     1 
ATOM   10944 C  CA    . GLU A 1 2839 ? 138.376 146.617 171.262 1.00 84.80  ? 2839 GLU A CA    1 
ATOM   10945 C  C     . GLU A 1 2839 ? 136.919 146.179 171.140 1.00 85.18  ? 2839 GLU A C     1 
ATOM   10946 O  O     . GLU A 1 2839 ? 135.999 146.996 171.070 1.00 91.47  ? 2839 GLU A O     1 
ATOM   10947 C  CB    . GLU A 1 2839 ? 138.864 146.418 172.698 1.00 89.08  ? 2839 GLU A CB    1 
ATOM   10948 C  CG    . GLU A 1 2839 ? 140.102 147.230 173.061 1.00 89.92  ? 2839 GLU A CG    1 
ATOM   10949 C  CD    . GLU A 1 2839 ? 141.387 146.659 172.483 1.00 91.86  ? 2839 GLU A CD    1 
ATOM   10950 O  OE1   . GLU A 1 2839 ? 141.323 145.671 171.721 1.00 92.35  ? 2839 GLU A OE1   1 
ATOM   10951 O  OE2   . GLU A 1 2839 ? 142.467 147.204 172.792 1.00 92.15  ? 2839 GLU A OE2   1 
ATOM   10952 N  N     . ASP A 1 2840 ? 136.724 144.859 171.113 1.00 98.34  ? 2840 ASP A N     1 
ATOM   10953 C  CA    . ASP A 1 2840 ? 135.377 144.307 171.006 1.00 103.99 ? 2840 ASP A CA    1 
ATOM   10954 C  C     . ASP A 1 2840 ? 134.622 144.405 172.325 1.00 105.92 ? 2840 ASP A C     1 
ATOM   10955 O  O     . ASP A 1 2840 ? 133.410 144.660 172.329 1.00 107.75 ? 2840 ASP A O     1 
ATOM   10956 C  CB    . ASP A 1 2840 ? 135.447 142.854 170.538 1.00 104.99 ? 2840 ASP A CB    1 
ATOM   10957 C  CG    . ASP A 1 2840 ? 134.080 142.210 170.414 1.00 106.09 ? 2840 ASP A CG    1 
ATOM   10958 O  OD1   . ASP A 1 2840 ? 133.996 140.969 170.534 1.00 106.38 ? 2840 ASP A OD1   1 
ATOM   10959 O  OD2   . ASP A 1 2840 ? 133.091 142.936 170.180 1.00 105.49 ? 2840 ASP A OD2   1 
ATOM   10960 N  N     . GLU A 1 2841 ? 135.313 144.202 173.450 1.00 105.27 ? 2841 GLU A N     1 
ATOM   10961 C  CA    . GLU A 1 2841 ? 134.649 144.272 174.746 1.00 104.75 ? 2841 GLU A CA    1 
ATOM   10962 C  C     . GLU A 1 2841 ? 134.080 145.658 175.011 1.00 108.78 ? 2841 GLU A C     1 
ATOM   10963 O  O     . GLU A 1 2841 ? 133.027 145.781 175.642 1.00 112.69 ? 2841 GLU A O     1 
ATOM   10964 C  CB    . GLU A 1 2841 ? 135.615 143.874 175.860 1.00 105.00 ? 2841 GLU A CB    1 
ATOM   10965 C  CG    . GLU A 1 2841 ? 136.168 142.466 175.724 1.00 110.29 ? 2841 GLU A CG    1 
ATOM   10966 C  CD    . GLU A 1 2841 ? 137.682 142.436 175.699 1.00 116.00 ? 2841 GLU A CD    1 
ATOM   10967 O  OE1   . GLU A 1 2841 ? 138.299 143.522 175.708 1.00 114.98 ? 2841 GLU A OE1   1 
ATOM   10968 O  OE2   . GLU A 1 2841 ? 138.255 141.327 175.670 1.00 113.86 ? 2841 GLU A OE2   1 
ATOM   10969 N  N     . GLU A 1 2842 ? 134.751 146.708 174.534 1.00 90.27  ? 2842 GLU A N     1 
ATOM   10970 C  CA    . GLU A 1 2842 ? 134.221 148.056 174.704 1.00 86.21  ? 2842 GLU A CA    1 
ATOM   10971 C  C     . GLU A 1 2842 ? 132.929 148.247 173.915 1.00 88.07  ? 2842 GLU A C     1 
ATOM   10972 O  O     . GLU A 1 2842 ? 131.983 148.873 174.405 1.00 92.98  ? 2842 GLU A O     1 
ATOM   10973 C  CB    . GLU A 1 2842 ? 135.273 149.084 174.295 1.00 83.54  ? 2842 GLU A CB    1 
ATOM   10974 C  CG    . GLU A 1 2842 ? 136.487 149.096 175.210 1.00 84.88  ? 2842 GLU A CG    1 
ATOM   10975 C  CD    . GLU A 1 2842 ? 137.711 149.702 174.557 1.00 92.03  ? 2842 GLU A CD    1 
ATOM   10976 O  OE1   . GLU A 1 2842 ? 137.645 150.035 173.356 1.00 92.63  ? 2842 GLU A OE1   1 
ATOM   10977 O  OE2   . GLU A 1 2842 ? 138.742 149.844 175.247 1.00 93.09  ? 2842 GLU A OE2   1 
ATOM   10978 N  N     . ARG A 1 2843 ? 132.868 147.712 172.693 1.00 79.75  ? 2843 ARG A N     1 
ATOM   10979 C  CA    . ARG A 1 2843 ? 131.633 147.787 171.918 1.00 82.62  ? 2843 ARG A CA    1 
ATOM   10980 C  C     . ARG A 1 2843 ? 130.512 146.996 172.584 1.00 86.53  ? 2843 ARG A C     1 
ATOM   10981 O  O     . ARG A 1 2843 ? 129.356 147.443 172.609 1.00 91.48  ? 2843 ARG A O     1 
ATOM   10982 C  CB    . ARG A 1 2843 ? 131.876 147.288 170.495 1.00 80.00  ? 2843 ARG A CB    1 
ATOM   10983 C  CG    . ARG A 1 2843 ? 132.853 148.142 169.706 1.00 79.73  ? 2843 ARG A CG    1 
ATOM   10984 C  CD    . ARG A 1 2843 ? 132.855 147.771 168.233 1.00 83.77  ? 2843 ARG A CD    1 
ATOM   10985 N  NE    . ARG A 1 2843 ? 134.014 146.962 167.877 1.00 91.17  ? 2843 ARG A NE    1 
ATOM   10986 C  CZ    . ARG A 1 2843 ? 135.056 147.411 167.192 1.00 89.04  ? 2843 ARG A CZ    1 
ATOM   10987 N  NH1   . ARG A 1 2843 ? 135.118 148.664 166.770 1.00 80.62  ? 2843 ARG A NH1   1 
ATOM   10988 N  NH2   . ARG A 1 2843 ? 136.062 146.583 166.922 1.00 88.88  ? 2843 ARG A NH2   1 
ATOM   10989 N  N     . ARG A 1 2844 ? 130.832 145.817 173.122 1.00 89.40  ? 2844 ARG A N     1 
ATOM   10990 C  CA    . ARG A 1 2844 ? 129.832 145.043 173.852 1.00 90.03  ? 2844 ARG A CA    1 
ATOM   10991 C  C     . ARG A 1 2844 ? 129.326 145.809 175.068 1.00 92.95  ? 2844 ARG A C     1 
ATOM   10992 O  O     . ARG A 1 2844 ? 128.120 145.824 175.350 1.00 98.96  ? 2844 ARG A O     1 
ATOM   10993 C  CB    . ARG A 1 2844 ? 130.419 143.696 174.272 1.00 92.83  ? 2844 ARG A CB    1 
ATOM   10994 C  CG    . ARG A 1 2844 ? 129.510 142.870 175.163 1.00 93.88  ? 2844 ARG A CG    1 
ATOM   10995 C  CD    . ARG A 1 2844 ? 130.257 141.684 175.765 1.00 95.35  ? 2844 ARG A CD    1 
ATOM   10996 N  NE    . ARG A 1 2844 ? 131.387 142.083 176.599 1.00 100.64 ? 2844 ARG A NE    1 
ATOM   10997 C  CZ    . ARG A 1 2844 ? 131.301 142.811 177.706 1.00 102.32 ? 2844 ARG A CZ    1 
ATOM   10998 N  NH1   . ARG A 1 2844 ? 130.135 143.211 178.187 1.00 100.23 ? 2844 ARG A NH1   1 
ATOM   10999 N  NH2   . ARG A 1 2844 ? 132.415 143.133 178.357 1.00 99.90  ? 2844 ARG A NH2   1 
ATOM   11000 N  N     . TRP A 1 2845 ? 130.239 146.452 175.800 1.00 79.81  ? 2845 TRP A N     1 
ATOM   11001 C  CA    . TRP A 1 2845 ? 129.848 147.270 176.942 1.00 79.21  ? 2845 TRP A CA    1 
ATOM   11002 C  C     . TRP A 1 2845 ? 128.942 148.413 176.514 1.00 82.89  ? 2845 TRP A C     1 
ATOM   11003 O  O     . TRP A 1 2845 ? 127.949 148.710 177.185 1.00 87.95  ? 2845 TRP A O     1 
ATOM   11004 C  CB    . TRP A 1 2845 ? 131.095 147.806 177.647 1.00 79.65  ? 2845 TRP A CB    1 
ATOM   11005 C  CG    . TRP A 1 2845 ? 130.807 148.649 178.854 1.00 86.80  ? 2845 TRP A CG    1 
ATOM   11006 C  CD1   . TRP A 1 2845 ? 130.785 148.238 180.154 1.00 88.38  ? 2845 TRP A CD1   1 
ATOM   11007 C  CD2   . TRP A 1 2845 ? 130.522 150.054 178.874 1.00 84.02  ? 2845 TRP A CD2   1 
ATOM   11008 N  NE1   . TRP A 1 2845 ? 130.493 149.295 180.981 1.00 87.09  ? 2845 TRP A NE1   1 
ATOM   11009 C  CE2   . TRP A 1 2845 ? 130.329 150.422 180.219 1.00 84.63  ? 2845 TRP A CE2   1 
ATOM   11010 C  CE3   . TRP A 1 2845 ? 130.406 151.035 177.884 1.00 77.30  ? 2845 TRP A CE3   1 
ATOM   11011 C  CZ2   . TRP A 1 2845 ? 130.024 151.726 180.599 1.00 83.36  ? 2845 TRP A CZ2   1 
ATOM   11012 C  CZ3   . TRP A 1 2845 ? 130.105 152.328 178.264 1.00 79.29  ? 2845 TRP A CZ3   1 
ATOM   11013 C  CH2   . TRP A 1 2845 ? 129.917 152.662 179.609 1.00 82.68  ? 2845 TRP A CH2   1 
ATOM   11014 N  N     . THR A 1 2846 ? 129.272 149.071 175.401 1.00 77.26  ? 2846 THR A N     1 
ATOM   11015 C  CA    . THR A 1 2846 ? 128.445 150.173 174.922 1.00 76.60  ? 2846 THR A CA    1 
ATOM   11016 C  C     . THR A 1 2846 ? 127.044 149.697 174.561 1.00 76.52  ? 2846 THR A C     1 
ATOM   11017 O  O     . THR A 1 2846 ? 126.052 150.343 174.916 1.00 88.00  ? 2846 THR A O     1 
ATOM   11018 C  CB    . THR A 1 2846 ? 129.109 150.848 173.723 1.00 73.49  ? 2846 THR A CB    1 
ATOM   11019 O  OG1   . THR A 1 2846 ? 130.365 151.405 174.126 1.00 74.08  ? 2846 THR A OG1   1 
ATOM   11020 C  CG2   . THR A 1 2846 ? 128.225 151.957 173.176 1.00 75.80  ? 2846 THR A CG2   1 
ATOM   11021 N  N     . ASP A 1 2847 ? 126.941 148.559 173.870 1.00 76.52  ? 2847 ASP A N     1 
ATOM   11022 C  CA    . ASP A 1 2847 ? 125.627 148.031 173.512 1.00 78.34  ? 2847 ASP A CA    1 
ATOM   11023 C  C     . ASP A 1 2847 ? 124.815 147.680 174.755 1.00 84.28  ? 2847 ASP A C     1 
ATOM   11024 O  O     . ASP A 1 2847 ? 123.639 148.057 174.879 1.00 89.25  ? 2847 ASP A O     1 
ATOM   11025 C  CB    . ASP A 1 2847 ? 125.785 146.808 172.609 1.00 82.02  ? 2847 ASP A CB    1 
ATOM   11026 C  CG    . ASP A 1 2847 ? 125.777 147.165 171.137 1.00 89.48  ? 2847 ASP A CG    1 
ATOM   11027 O  OD1   . ASP A 1 2847 ? 124.735 147.648 170.649 1.00 92.45  ? 2847 ASP A OD1   1 
ATOM   11028 O  OD2   . ASP A 1 2847 ? 126.812 146.964 170.468 1.00 89.39  ? 2847 ASP A OD2   1 
ATOM   11029 N  N     . GLU A 1 2848 ? 125.435 146.963 175.697 1.00 84.56  ? 2848 GLU A N     1 
ATOM   11030 C  CA    . GLU A 1 2848 ? 124.723 146.560 176.904 1.00 83.57  ? 2848 GLU A CA    1 
ATOM   11031 C  C     . GLU A 1 2848 ? 124.289 147.771 177.719 1.00 88.86  ? 2848 GLU A C     1 
ATOM   11032 O  O     . GLU A 1 2848 ? 123.180 147.796 178.265 1.00 93.31  ? 2848 GLU A O     1 
ATOM   11033 C  CB    . GLU A 1 2848 ? 125.597 145.631 177.745 1.00 87.32  ? 2848 GLU A CB    1 
ATOM   11034 C  CG    . GLU A 1 2848 ? 125.823 144.263 177.124 1.00 89.50  ? 2848 GLU A CG    1 
ATOM   11035 C  CD    . GLU A 1 2848 ? 126.935 143.492 177.806 1.00 94.66  ? 2848 GLU A CD    1 
ATOM   11036 O  OE1   . GLU A 1 2848 ? 127.572 144.052 178.723 1.00 98.01  ? 2848 GLU A OE1   1 
ATOM   11037 O  OE2   . GLU A 1 2848 ? 127.173 142.327 177.426 1.00 92.20  ? 2848 GLU A OE2   1 
ATOM   11038 N  N     . ASN A 1 2849 ? 125.145 148.791 177.807 1.00 72.55  ? 2849 ASN A N     1 
ATOM   11039 C  CA    . ASN A 1 2849 ? 124.803 149.982 178.571 1.00 69.09  ? 2849 ASN A CA    1 
ATOM   11040 C  C     . ASN A 1 2849 ? 123.723 150.808 177.891 1.00 73.38  ? 2849 ASN A C     1 
ATOM   11041 O  O     . ASN A 1 2849 ? 122.871 151.377 178.578 1.00 85.38  ? 2849 ASN A O     1 
ATOM   11042 C  CB    . ASN A 1 2849 ? 126.055 150.823 178.812 1.00 74.32  ? 2849 ASN A CB    1 
ATOM   11043 C  CG    . ASN A 1 2849 ? 126.938 150.241 179.895 1.00 78.60  ? 2849 ASN A CG    1 
ATOM   11044 O  OD1   . ASN A 1 2849 ? 126.977 150.743 181.017 1.00 80.72  ? 2849 ASN A OD1   1 
ATOM   11045 N  ND2   . ASN A 1 2849 ? 127.632 149.157 179.571 1.00 77.38  ? 2849 ASN A ND2   1 
ATOM   11046 N  N     . ILE A 1 2850 ? 123.726 150.878 176.557 1.00 67.10  ? 2850 ILE A N     1 
ATOM   11047 C  CA    . ILE A 1 2850 ? 122.617 151.513 175.851 1.00 69.67  ? 2850 ILE A CA    1 
ATOM   11048 C  C     . ILE A 1 2850 ? 121.313 150.810 176.194 1.00 75.03  ? 2850 ILE A C     1 
ATOM   11049 O  O     . ILE A 1 2850 ? 120.300 151.451 176.508 1.00 82.34  ? 2850 ILE A O     1 
ATOM   11050 C  CB    . ILE A 1 2850 ? 122.869 151.509 174.332 1.00 70.05  ? 2850 ILE A CB    1 
ATOM   11051 C  CG1   . ILE A 1 2850 ? 123.950 152.522 173.964 1.00 75.45  ? 2850 ILE A CG1   1 
ATOM   11052 C  CG2   . ILE A 1 2850 ? 121.588 151.816 173.577 1.00 68.60  ? 2850 ILE A CG2   1 
ATOM   11053 C  CD1   . ILE A 1 2850 ? 124.416 152.414 172.535 1.00 68.53  ? 2850 ILE A CD1   1 
ATOM   11054 N  N     . ASP A 1 2851 ? 121.324 149.475 176.150 1.00 85.46  ? 2851 ASP A N     1 
ATOM   11055 C  CA    . ASP A 1 2851 ? 120.111 148.722 176.452 1.00 85.52  ? 2851 ASP A CA    1 
ATOM   11056 C  C     . ASP A 1 2851 ? 119.642 148.979 177.879 1.00 85.98  ? 2851 ASP A C     1 
ATOM   11057 O  O     . ASP A 1 2851 ? 118.457 149.247 178.119 1.00 89.28  ? 2851 ASP A O     1 
ATOM   11058 C  CB    . ASP A 1 2851 ? 120.349 147.231 176.216 1.00 88.02  ? 2851 ASP A CB    1 
ATOM   11059 C  CG    . ASP A 1 2851 ? 120.030 146.809 174.795 1.00 93.53  ? 2851 ASP A CG    1 
ATOM   11060 O  OD1   . ASP A 1 2851 ? 118.877 146.406 174.537 1.00 95.60  ? 2851 ASP A OD1   1 
ATOM   11061 O  OD2   . ASP A 1 2851 ? 120.932 146.887 173.935 1.00 94.01  ? 2851 ASP A OD2   1 
ATOM   11062 N  N     . THR A 1 2852 ? 120.566 148.919 178.841 1.00 77.14  ? 2852 THR A N     1 
ATOM   11063 C  CA    . THR A 1 2852 ? 120.192 149.115 180.238 1.00 75.11  ? 2852 THR A CA    1 
ATOM   11064 C  C     . THR A 1 2852 ? 119.670 150.525 180.483 1.00 79.63  ? 2852 THR A C     1 
ATOM   11065 O  O     . THR A 1 2852 ? 118.683 150.707 181.202 1.00 87.48  ? 2852 THR A O     1 
ATOM   11066 C  CB    . THR A 1 2852 ? 121.376 148.818 181.160 1.00 72.92  ? 2852 THR A CB    1 
ATOM   11067 O  OG1   . THR A 1 2852 ? 122.482 149.659 180.810 1.00 78.85  ? 2852 THR A OG1   1 
ATOM   11068 C  CG2   . THR A 1 2852 ? 121.789 147.356 181.056 1.00 75.18  ? 2852 THR A CG2   1 
ATOM   11069 N  N     . VAL A 1 2853 ? 120.313 151.536 179.893 1.00 68.77  ? 2853 VAL A N     1 
ATOM   11070 C  CA    . VAL A 1 2853 ? 119.865 152.913 180.085 1.00 69.02  ? 2853 VAL A CA    1 
ATOM   11071 C  C     . VAL A 1 2853 ? 118.474 153.111 179.499 1.00 69.22  ? 2853 VAL A C     1 
ATOM   11072 O  O     . VAL A 1 2853 ? 117.599 153.720 180.130 1.00 77.59  ? 2853 VAL A O     1 
ATOM   11073 C  CB    . VAL A 1 2853 ? 120.882 153.895 179.475 1.00 68.03  ? 2853 VAL A CB    1 
ATOM   11074 C  CG1   . VAL A 1 2853 ? 120.262 155.277 179.310 1.00 70.69  ? 2853 VAL A CG1   1 
ATOM   11075 C  CG2   . VAL A 1 2853 ? 122.126 153.967 180.343 1.00 69.71  ? 2853 VAL A CG2   1 
ATOM   11076 N  N     . ALA A 1 2854 ? 118.246 152.604 178.285 1.00 67.28  ? 2854 ALA A N     1 
ATOM   11077 C  CA    . ALA A 1 2854 ? 116.941 152.782 177.659 1.00 72.72  ? 2854 ALA A CA    1 
ATOM   11078 C  C     . ALA A 1 2854 ? 115.848 152.071 178.445 1.00 81.27  ? 2854 ALA A C     1 
ATOM   11079 O  O     . ALA A 1 2854 ? 114.743 152.602 178.600 1.00 83.71  ? 2854 ALA A O     1 
ATOM   11080 C  CB    . ALA A 1 2854 ? 116.979 152.290 176.215 1.00 77.54  ? 2854 ALA A CB    1 
ATOM   11081 N  N     . LEU A 1 2855 ? 116.132 150.867 178.951 1.00 85.18  ? 2855 LEU A N     1 
ATOM   11082 C  CA    . LEU A 1 2855 ? 115.131 150.176 179.758 1.00 78.84  ? 2855 LEU A CA    1 
ATOM   11083 C  C     . LEU A 1 2855 ? 114.913 150.863 181.100 1.00 80.22  ? 2855 LEU A C     1 
ATOM   11084 O  O     . LEU A 1 2855 ? 113.795 150.848 181.626 1.00 89.26  ? 2855 LEU A O     1 
ATOM   11085 C  CB    . LEU A 1 2855 ? 115.525 148.714 179.962 1.00 81.70  ? 2855 LEU A CB    1 
ATOM   11086 C  CG    . LEU A 1 2855 ? 115.685 147.878 178.691 1.00 89.79  ? 2855 LEU A CG    1 
ATOM   11087 C  CD1   . LEU A 1 2855 ? 115.761 146.398 179.024 1.00 85.94  ? 2855 LEU A CD1   1 
ATOM   11088 C  CD2   . LEU A 1 2855 ? 114.543 148.156 177.728 1.00 86.85  ? 2855 LEU A CD2   1 
ATOM   11089 N  N     . LYS A 1 2856 ? 115.959 151.466 181.668 1.00 72.85  ? 2856 LYS A N     1 
ATOM   11090 C  CA    . LYS A 1 2856 ? 115.821 152.132 182.958 1.00 76.51  ? 2856 LYS A CA    1 
ATOM   11091 C  C     . LYS A 1 2856 ? 114.990 153.403 182.843 1.00 78.07  ? 2856 LYS A C     1 
ATOM   11092 O  O     . LYS A 1 2856 ? 114.104 153.648 183.670 1.00 81.70  ? 2856 LYS A O     1 
ATOM   11093 C  CB    . LYS A 1 2856 ? 117.202 152.443 183.531 1.00 75.49  ? 2856 LYS A CB    1 
ATOM   11094 C  CG    . LYS A 1 2856 ? 117.181 153.266 184.806 1.00 79.23  ? 2856 LYS A CG    1 
ATOM   11095 C  CD    . LYS A 1 2856 ? 118.577 153.740 185.170 1.00 75.07  ? 2856 LYS A CD    1 
ATOM   11096 C  CE    . LYS A 1 2856 ? 118.561 154.583 186.434 1.00 78.34  ? 2856 LYS A CE    1 
ATOM   11097 N  NZ    . LYS A 1 2856 ? 119.936 154.895 186.912 1.00 81.69  ? 2856 LYS A NZ    1 
ATOM   11098 N  N     . HIS A 1 2857 ? 115.256 154.225 181.828 1.00 75.04  ? 2857 HIS A N     1 
ATOM   11099 C  CA    . HIS A 1 2857 ? 114.563 155.498 181.687 1.00 76.19  ? 2857 HIS A CA    1 
ATOM   11100 C  C     . HIS A 1 2857 ? 113.273 155.408 180.885 1.00 76.61  ? 2857 HIS A C     1 
ATOM   11101 O  O     . HIS A 1 2857 ? 112.470 156.346 180.935 1.00 76.54  ? 2857 HIS A O     1 
ATOM   11102 C  CB    . HIS A 1 2857 ? 115.486 156.539 181.044 1.00 76.19  ? 2857 HIS A CB    1 
ATOM   11103 C  CG    . HIS A 1 2857 ? 116.551 157.048 181.963 1.00 76.91  ? 2857 HIS A CG    1 
ATOM   11104 N  ND1   . HIS A 1 2857 ? 116.308 158.011 182.918 1.00 82.29  ? 2857 HIS A ND1   1 
ATOM   11105 C  CD2   . HIS A 1 2857 ? 117.861 156.728 182.075 1.00 76.92  ? 2857 HIS A CD2   1 
ATOM   11106 C  CE1   . HIS A 1 2857 ? 117.424 158.263 183.579 1.00 82.08  ? 2857 HIS A CE1   1 
ATOM   11107 N  NE2   . HIS A 1 2857 ? 118.381 157.499 183.087 1.00 82.40  ? 2857 HIS A NE2   1 
ATOM   11108 N  N     . PHE A 1 2858 ? 113.046 154.319 180.155 1.00 80.60  ? 2858 PHE A N     1 
ATOM   11109 C  CA    . PHE A 1 2858 ? 111.831 154.138 179.362 1.00 80.64  ? 2858 PHE A CA    1 
ATOM   11110 C  C     . PHE A 1 2858 ? 111.232 152.766 179.640 1.00 83.73  ? 2858 PHE A C     1 
ATOM   11111 O  O     . PHE A 1 2858 ? 111.321 151.853 178.810 1.00 84.86  ? 2858 PHE A O     1 
ATOM   11112 C  CB    . PHE A 1 2858 ? 112.119 154.315 177.871 1.00 79.68  ? 2858 PHE A CB    1 
ATOM   11113 C  CG    . PHE A 1 2858 ? 112.447 155.725 177.482 1.00 75.66  ? 2858 PHE A CG    1 
ATOM   11114 C  CD1   . PHE A 1 2858 ? 113.758 156.167 177.468 1.00 77.06  ? 2858 PHE A CD1   1 
ATOM   11115 C  CD2   . PHE A 1 2858 ? 111.442 156.608 177.130 1.00 78.12  ? 2858 PHE A CD2   1 
ATOM   11116 C  CE1   . PHE A 1 2858 ? 114.061 157.464 177.109 1.00 80.63  ? 2858 PHE A CE1   1 
ATOM   11117 C  CE2   . PHE A 1 2858 ? 111.739 157.906 176.770 1.00 84.01  ? 2858 PHE A CE2   1 
ATOM   11118 C  CZ    . PHE A 1 2858 ? 113.050 158.334 176.760 1.00 82.79  ? 2858 PHE A CZ    1 
ATOM   11119 N  N     . PRO A 1 2859 ? 110.616 152.582 180.805 1.00 92.31  ? 2859 PRO A N     1 
ATOM   11120 C  CA    . PRO A 1 2859 ? 109.926 151.319 181.081 1.00 92.03  ? 2859 PRO A CA    1 
ATOM   11121 C  C     . PRO A 1 2859 ? 108.597 151.253 180.342 1.00 95.29  ? 2859 PRO A C     1 
ATOM   11122 O  O     . PRO A 1 2859 ? 108.121 152.230 179.760 1.00 94.63  ? 2859 PRO A O     1 
ATOM   11123 C  CB    . PRO A 1 2859 ? 109.723 151.337 182.602 1.00 91.50  ? 2859 PRO A CB    1 
ATOM   11124 C  CG    . PRO A 1 2859 ? 110.509 152.523 183.109 1.00 89.55  ? 2859 PRO A CG    1 
ATOM   11125 C  CD    . PRO A 1 2859 ? 110.585 153.481 181.968 1.00 92.22  ? 2859 PRO A CD    1 
ATOM   11126 N  N     . ASN A 1 2860 ? 107.997 150.061 180.379 1.00 102.61 ? 2860 ASN A N     1 
ATOM   11127 C  CA    . ASN A 1 2860 ? 106.712 149.789 179.731 1.00 104.16 ? 2860 ASN A CA    1 
ATOM   11128 C  C     . ASN A 1 2860 ? 106.753 150.115 178.237 1.00 107.64 ? 2860 ASN A C     1 
ATOM   11129 O  O     . ASN A 1 2860 ? 105.824 150.701 177.677 1.00 110.82 ? 2860 ASN A O     1 
ATOM   11130 C  CB    . ASN A 1 2860 ? 105.569 150.537 180.423 1.00 104.30 ? 2860 ASN A CB    1 
ATOM   11131 C  CG    . ASN A 1 2860 ? 105.662 150.480 181.936 1.00 107.08 ? 2860 ASN A CG    1 
ATOM   11132 O  OD1   . ASN A 1 2860 ? 106.571 151.047 182.537 1.00 108.10 ? 2860 ASN A OD1   1 
ATOM   11133 N  ND2   . ASN A 1 2860 ? 104.716 149.787 182.558 1.00 107.92 ? 2860 ASN A ND2   1 
ATOM   11134 N  N     . ILE A 1 2861 ? 107.852 149.729 177.588 1.00 103.19 ? 2861 ILE A N     1 
ATOM   11135 C  CA    . ILE A 1 2861 ? 107.968 149.789 176.138 1.00 99.52  ? 2861 ILE A CA    1 
ATOM   11136 C  C     . ILE A 1 2861 ? 108.402 148.416 175.646 1.00 103.28 ? 2861 ILE A C     1 
ATOM   11137 O  O     . ILE A 1 2861 ? 109.043 147.645 176.365 1.00 106.20 ? 2861 ILE A O     1 
ATOM   11138 C  CB    . ILE A 1 2861 ? 108.955 150.875 175.656 1.00 96.40  ? 2861 ILE A CB    1 
ATOM   11139 C  CG1   . ILE A 1 2861 ? 110.393 150.499 176.016 1.00 98.48  ? 2861 ILE A CG1   1 
ATOM   11140 C  CG2   . ILE A 1 2861 ? 108.590 152.232 176.237 1.00 99.86  ? 2861 ILE A CG2   1 
ATOM   11141 C  CD1   . ILE A 1 2861 ? 111.433 151.388 175.373 1.00 96.92  ? 2861 ILE A CD1   1 
ATOM   11142 N  N     . ASP A 1 2862 ? 108.035 148.109 174.406 1.00 114.49 ? 2862 ASP A N     1 
ATOM   11143 C  CA    . ASP A 1 2862 ? 108.349 146.807 173.824 1.00 114.48 ? 2862 ASP A CA    1 
ATOM   11144 C  C     . ASP A 1 2862 ? 109.784 146.843 173.315 1.00 114.61 ? 2862 ASP A C     1 
ATOM   11145 O  O     . ASP A 1 2862 ? 110.105 147.560 172.365 1.00 113.72 ? 2862 ASP A O     1 
ATOM   11146 C  CB    . ASP A 1 2862 ? 107.364 146.466 172.712 1.00 113.94 ? 2862 ASP A CB    1 
ATOM   11147 C  CG    . ASP A 1 2862 ? 107.857 145.347 171.818 1.00 117.26 ? 2862 ASP A CG    1 
ATOM   11148 O  OD1   . ASP A 1 2862 ? 108.436 144.371 172.342 1.00 115.90 ? 2862 ASP A OD1   1 
ATOM   11149 O  OD2   . ASP A 1 2862 ? 107.656 145.436 170.591 1.00 120.37 ? 2862 ASP A OD2   1 
ATOM   11150 N  N     . ARG A 1 2863 ? 110.656 146.061 173.955 1.00 108.66 ? 2863 ARG A N     1 
ATOM   11151 C  CA    . ARG A 1 2863 ? 112.086 146.149 173.679 1.00 107.51 ? 2863 ARG A CA    1 
ATOM   11152 C  C     . ARG A 1 2863 ? 112.421 145.628 172.285 1.00 110.60 ? 2863 ARG A C     1 
ATOM   11153 O  O     . ARG A 1 2863 ? 113.265 146.198 171.585 1.00 113.67 ? 2863 ARG A O     1 
ATOM   11154 C  CB    . ARG A 1 2863 ? 112.863 145.392 174.763 1.00 105.33 ? 2863 ARG A CB    1 
ATOM   11155 C  CG    . ARG A 1 2863 ? 114.318 145.052 174.440 1.00 108.36 ? 2863 ARG A CG    1 
ATOM   11156 C  CD    . ARG A 1 2863 ? 114.467 143.671 173.808 1.00 111.21 ? 2863 ARG A CD    1 
ATOM   11157 N  NE    . ARG A 1 2863 ? 115.862 143.330 173.557 1.00 111.33 ? 2863 ARG A NE    1 
ATOM   11158 C  CZ    . ARG A 1 2863 ? 116.261 142.264 172.877 1.00 108.52 ? 2863 ARG A CZ    1 
ATOM   11159 N  NH1   . ARG A 1 2863 ? 115.393 141.410 172.361 1.00 107.57 ? 2863 ARG A NH1   1 
ATOM   11160 N  NH2   . ARG A 1 2863 ? 117.563 142.050 172.712 1.00 107.66 ? 2863 ARG A NH2   1 
ATOM   11161 N  N     . GLU A 1 2864 ? 111.770 144.539 171.866 1.00 115.42 ? 2864 GLU A N     1 
ATOM   11162 C  CA    . GLU A 1 2864 ? 112.168 143.867 170.631 1.00 116.39 ? 2864 GLU A CA    1 
ATOM   11163 C  C     . GLU A 1 2864 ? 111.976 144.758 169.409 1.00 116.05 ? 2864 GLU A C     1 
ATOM   11164 O  O     . GLU A 1 2864 ? 112.851 144.817 168.538 1.00 118.22 ? 2864 GLU A O     1 
ATOM   11165 C  CB    . GLU A 1 2864 ? 111.390 142.559 170.468 1.00 116.47 ? 2864 GLU A CB    1 
ATOM   11166 C  CG    . GLU A 1 2864 ? 111.810 141.422 171.407 1.00 119.05 ? 2864 GLU A CG    1 
ATOM   11167 C  CD    . GLU A 1 2864 ? 111.479 141.664 172.875 1.00 120.90 ? 2864 GLU A CD    1 
ATOM   11168 O  OE1   . GLU A 1 2864 ? 111.625 140.712 173.670 1.00 121.31 ? 2864 GLU A OE1   1 
ATOM   11169 O  OE2   . GLU A 1 2864 ? 111.060 142.783 173.239 1.00 118.84 ? 2864 GLU A OE2   1 
ATOM   11170 N  N     . LYS A 1 2865 ? 110.839 145.453 169.319 1.00 112.52 ? 2865 LYS A N     1 
ATOM   11171 C  CA    . LYS A 1 2865 ? 110.607 146.324 168.170 1.00 115.05 ? 2865 LYS A CA    1 
ATOM   11172 C  C     . LYS A 1 2865 ? 111.590 147.487 168.148 1.00 113.99 ? 2865 LYS A C     1 
ATOM   11173 O  O     . LYS A 1 2865 ? 112.106 147.853 167.086 1.00 113.83 ? 2865 LYS A O     1 
ATOM   11174 C  CB    . LYS A 1 2865 ? 109.171 146.848 168.179 1.00 115.38 ? 2865 LYS A CB    1 
ATOM   11175 C  CG    . LYS A 1 2865 ? 108.164 145.929 167.510 1.00 116.11 ? 2865 LYS A CG    1 
ATOM   11176 C  CD    . LYS A 1 2865 ? 106.927 146.702 167.083 1.00 116.00 ? 2865 LYS A CD    1 
ATOM   11177 C  CE    . LYS A 1 2865 ? 106.021 146.999 168.268 1.00 117.23 ? 2865 LYS A CE    1 
ATOM   11178 N  NZ    . LYS A 1 2865 ? 104.717 147.578 167.843 1.00 116.75 ? 2865 LYS A NZ    1 
ATOM   11179 N  N     . ALA A 1 2866 ? 111.863 148.078 169.308 1.00 103.54 ? 2866 ALA A N     1 
ATOM   11180 C  CA    . ALA A 1 2866 ? 112.688 149.272 169.388 1.00 103.50 ? 2866 ALA A CA    1 
ATOM   11181 C  C     . ALA A 1 2866 ? 114.178 148.981 169.491 1.00 104.98 ? 2866 ALA A C     1 
ATOM   11182 O  O     . ALA A 1 2866 ? 114.984 149.873 169.209 1.00 108.06 ? 2866 ALA A O     1 
ATOM   11183 C  CB    . ALA A 1 2866 ? 112.260 150.129 170.586 1.00 101.10 ? 2866 ALA A CB    1 
ATOM   11184 N  N     . MET A 1 2867 ? 114.570 147.769 169.884 1.00 100.64 ? 2867 MET A N     1 
ATOM   11185 C  CA    . MET A 1 2867 ? 115.975 147.483 170.160 1.00 97.51  ? 2867 MET A CA    1 
ATOM   11186 C  C     . MET A 1 2867 ? 116.405 146.164 169.536 1.00 99.80  ? 2867 MET A C     1 
ATOM   11187 O  O     . MET A 1 2867 ? 117.132 145.377 170.151 1.00 100.49 ? 2867 MET A O     1 
ATOM   11188 C  CB    . MET A 1 2867 ? 116.251 147.473 171.662 1.00 95.20  ? 2867 MET A CB    1 
ATOM   11189 C  CG    . MET A 1 2867 ? 115.697 148.673 172.398 1.00 97.12  ? 2867 MET A CG    1 
ATOM   11190 S  SD    . MET A 1 2867 ? 116.937 149.959 172.572 1.00 99.69  ? 2867 MET A SD    1 
ATOM   11191 C  CE    . MET A 1 2867 ? 117.609 149.511 174.160 1.00 98.77  ? 2867 MET A CE    1 
ATOM   11192 N  N     . SER A 1 2868 ? 115.967 145.899 168.309 1.00 100.69 ? 2868 SER A N     1 
ATOM   11193 C  CA    . SER A 1 2868 ? 116.538 144.792 167.554 1.00 97.76  ? 2868 SER A CA    1 
ATOM   11194 C  C     . SER A 1 2868 ? 117.987 145.116 167.217 1.00 100.02 ? 2868 SER A C     1 
ATOM   11195 O  O     . SER A 1 2868 ? 118.285 146.198 166.705 1.00 107.63 ? 2868 SER A O     1 
ATOM   11196 C  CB    . SER A 1 2868 ? 115.732 144.542 166.280 1.00 100.13 ? 2868 SER A CB    1 
ATOM   11197 O  OG    . SER A 1 2868 ? 114.379 144.254 166.584 1.00 105.62 ? 2868 SER A OG    1 
ATOM   11198 N  N     . ARG A 1 2869 ? 118.885 144.176 167.504 1.00 94.18  ? 2869 ARG A N     1 
ATOM   11199 C  CA    . ARG A 1 2869 ? 120.317 144.470 167.465 1.00 97.23  ? 2869 ARG A CA    1 
ATOM   11200 C  C     . ARG A 1 2869 ? 120.817 145.040 166.141 1.00 101.43 ? 2869 ARG A C     1 
ATOM   11201 O  O     . ARG A 1 2869 ? 121.597 146.007 166.180 1.00 104.24 ? 2869 ARG A O     1 
ATOM   11202 C  CB    . ARG A 1 2869 ? 121.112 143.214 167.847 1.00 102.26 ? 2869 ARG A CB    1 
ATOM   11203 C  CG    . ARG A 1 2869 ? 121.243 143.006 169.348 1.00 102.03 ? 2869 ARG A CG    1 
ATOM   11204 C  CD    . ARG A 1 2869 ? 121.968 144.176 170.002 1.00 100.79 ? 2869 ARG A CD    1 
ATOM   11205 N  NE    . ARG A 1 2869 ? 121.042 145.141 170.584 1.00 103.68 ? 2869 ARG A NE    1 
ATOM   11206 C  CZ    . ARG A 1 2869 ? 121.343 146.406 170.848 1.00 99.62  ? 2869 ARG A CZ    1 
ATOM   11207 N  NH1   . ARG A 1 2869 ? 122.540 146.901 170.583 1.00 96.64  ? 2869 ARG A NH1   1 
ATOM   11208 N  NH2   . ARG A 1 2869 ? 120.418 147.193 171.389 1.00 96.54  ? 2869 ARG A NH2   1 
ATOM   11209 N  N     . PRO A 1 2870 ? 120.440 144.524 164.960 1.00 96.86  ? 2870 PRO A N     1 
ATOM   11210 C  CA    . PRO A 1 2870 ? 120.889 145.178 163.723 1.00 94.42  ? 2870 PRO A CA    1 
ATOM   11211 C  C     . PRO A 1 2870 ? 120.184 146.505 163.491 1.00 98.08  ? 2870 PRO A C     1 
ATOM   11212 O  O     . PRO A 1 2870 ? 119.295 146.601 162.639 1.00 98.02  ? 2870 PRO A O     1 
ATOM   11213 C  CB    . PRO A 1 2870 ? 120.539 144.159 162.628 1.00 91.03  ? 2870 PRO A CB    1 
ATOM   11214 C  CG    . PRO A 1 2870 ? 120.264 142.878 163.344 1.00 92.41  ? 2870 PRO A CG    1 
ATOM   11215 C  CD    . PRO A 1 2870 ? 119.725 143.268 164.676 1.00 93.28  ? 2870 PRO A CD    1 
ATOM   11216 N  N     . ILE A 1 2871 ? 120.570 147.536 164.243 1.00 87.75  ? 2871 ILE A N     1 
ATOM   11217 C  CA    . ILE A 1 2871 ? 119.959 148.859 164.127 1.00 79.24  ? 2871 ILE A CA    1 
ATOM   11218 C  C     . ILE A 1 2871 ? 120.572 149.536 162.905 1.00 81.54  ? 2871 ILE A C     1 
ATOM   11219 O  O     . ILE A 1 2871 ? 121.740 149.926 162.920 1.00 82.86  ? 2871 ILE A O     1 
ATOM   11220 C  CB    . ILE A 1 2871 ? 120.155 149.698 165.391 1.00 75.31  ? 2871 ILE A CB    1 
ATOM   11221 C  CG1   . ILE A 1 2871 ? 119.797 148.890 166.637 1.00 75.10  ? 2871 ILE A CG1   1 
ATOM   11222 C  CG2   . ILE A 1 2871 ? 119.306 150.951 165.324 1.00 83.03  ? 2871 ILE A CG2   1 
ATOM   11223 C  CD1   . ILE A 1 2871 ? 119.798 149.701 167.912 1.00 78.22  ? 2871 ILE A CD1   1 
ATOM   11224 N  N     . LEU A 1 2872 ? 119.786 149.682 161.843 1.00 77.66  ? 2872 LEU A N     1 
ATOM   11225 C  CA    . LEU A 1 2872 ? 120.240 150.303 160.607 1.00 74.07  ? 2872 LEU A CA    1 
ATOM   11226 C  C     . LEU A 1 2872 ? 119.248 151.374 160.183 1.00 75.02  ? 2872 LEU A C     1 
ATOM   11227 O  O     . LEU A 1 2872 ? 118.039 151.124 160.137 1.00 80.16  ? 2872 LEU A O     1 
ATOM   11228 C  CB    . LEU A 1 2872 ? 120.404 149.264 159.496 1.00 74.29  ? 2872 LEU A CB    1 
ATOM   11229 C  CG    . LEU A 1 2872 ? 121.398 148.138 159.777 1.00 78.33  ? 2872 LEU A CG    1 
ATOM   11230 C  CD1   . LEU A 1 2872 ? 121.443 147.160 158.618 1.00 82.09  ? 2872 LEU A CD1   1 
ATOM   11231 C  CD2   . LEU A 1 2872 ? 122.778 148.703 160.058 1.00 78.62  ? 2872 LEU A CD2   1 
ATOM   11232 N  N     . TYR A 1 2873 ? 119.761 152.563 159.878 1.00 66.86  ? 2873 TYR A N     1 
ATOM   11233 C  CA    . TYR A 1 2873 ? 118.960 153.663 159.364 1.00 64.03  ? 2873 TYR A CA    1 
ATOM   11234 C  C     . TYR A 1 2873 ? 119.569 154.151 158.061 1.00 67.66  ? 2873 TYR A C     1 
ATOM   11235 O  O     . TYR A 1 2873 ? 120.776 154.400 157.986 1.00 76.17  ? 2873 TYR A O     1 
ATOM   11236 C  CB    . TYR A 1 2873 ? 118.879 154.817 160.369 1.00 66.83  ? 2873 TYR A CB    1 
ATOM   11237 C  CG    . TYR A 1 2873 ? 117.818 154.642 161.429 1.00 63.66  ? 2873 TYR A CG    1 
ATOM   11238 C  CD1   . TYR A 1 2873 ? 117.960 153.697 162.434 1.00 64.78  ? 2873 TYR A CD1   1 
ATOM   11239 C  CD2   . TYR A 1 2873 ? 116.674 155.426 161.425 1.00 69.48  ? 2873 TYR A CD2   1 
ATOM   11240 C  CE1   . TYR A 1 2873 ? 116.992 153.537 163.404 1.00 67.37  ? 2873 TYR A CE1   1 
ATOM   11241 C  CE2   . TYR A 1 2873 ? 115.702 155.274 162.390 1.00 71.90  ? 2873 TYR A CE2   1 
ATOM   11242 C  CZ    . TYR A 1 2873 ? 115.865 154.328 163.377 1.00 71.69  ? 2873 TYR A CZ    1 
ATOM   11243 O  OH    . TYR A 1 2873 ? 114.895 154.174 164.339 1.00 66.73  ? 2873 TYR A OH    1 
ATOM   11244 N  N     . SER A 1 2874 ? 118.733 154.290 157.035 1.00 71.90  ? 2874 SER A N     1 
ATOM   11245 C  CA    . SER A 1 2874 ? 119.217 154.720 155.732 1.00 71.78  ? 2874 SER A CA    1 
ATOM   11246 C  C     . SER A 1 2874 ? 118.083 155.379 154.965 1.00 74.42  ? 2874 SER A C     1 
ATOM   11247 O  O     . SER A 1 2874 ? 116.913 155.026 155.134 1.00 80.86  ? 2874 SER A O     1 
ATOM   11248 C  CB    . SER A 1 2874 ? 119.784 153.544 154.931 1.00 72.93  ? 2874 SER A CB    1 
ATOM   11249 O  OG    . SER A 1 2874 ? 120.312 153.981 153.692 1.00 76.66  ? 2874 SER A OG    1 
ATOM   11250 N  N     . ASN A 1 2875 ? 118.448 156.342 154.119 1.00 74.65  ? 2875 ASN A N     1 
ATOM   11251 C  CA    . ASN A 1 2875 ? 117.505 157.012 153.233 1.00 74.48  ? 2875 ASN A CA    1 
ATOM   11252 C  C     . ASN A 1 2875 ? 117.690 156.595 151.779 1.00 76.24  ? 2875 ASN A C     1 
ATOM   11253 O  O     . ASN A 1 2875 ? 117.307 157.337 150.870 1.00 80.36  ? 2875 ASN A O     1 
ATOM   11254 C  CB    . ASN A 1 2875 ? 117.624 158.530 153.374 1.00 74.24  ? 2875 ASN A CB    1 
ATOM   11255 C  CG    . ASN A 1 2875 ? 118.974 159.057 152.926 1.00 81.89  ? 2875 ASN A CG    1 
ATOM   11256 O  OD1   . ASN A 1 2875 ? 119.910 158.292 152.693 1.00 86.29  ? 2875 ASN A OD1   1 
ATOM   11257 N  ND2   . ASN A 1 2875 ? 119.080 160.374 152.801 1.00 80.23  ? 2875 ASN A ND2   1 
ATOM   11258 N  N     . TRP A 1 2876 ? 118.300 155.436 151.541 1.00 74.82  ? 2876 TRP A N     1 
ATOM   11259 C  CA    . TRP A 1 2876 ? 118.463 154.927 150.187 1.00 77.79  ? 2876 TRP A CA    1 
ATOM   11260 C  C     . TRP A 1 2876 ? 117.201 154.268 149.651 1.00 83.43  ? 2876 TRP A C     1 
ATOM   11261 O  O     . TRP A 1 2876 ? 116.936 154.345 148.446 1.00 85.27  ? 2876 TRP A O     1 
ATOM   11262 C  CB    . TRP A 1 2876 ? 119.624 153.931 150.136 1.00 75.93  ? 2876 TRP A CB    1 
ATOM   11263 C  CG    . TRP A 1 2876 ? 120.970 154.584 150.203 1.00 76.12  ? 2876 TRP A CG    1 
ATOM   11264 C  CD1   . TRP A 1 2876 ? 121.259 155.891 149.944 1.00 72.54  ? 2876 TRP A CD1   1 
ATOM   11265 C  CD2   . TRP A 1 2876 ? 122.209 153.961 150.560 1.00 78.38  ? 2876 TRP A CD2   1 
ATOM   11266 N  NE1   . TRP A 1 2876 ? 122.602 156.121 150.115 1.00 68.76  ? 2876 TRP A NE1   1 
ATOM   11267 C  CE2   . TRP A 1 2876 ? 123.208 154.952 150.492 1.00 71.95  ? 2876 TRP A CE2   1 
ATOM   11268 C  CE3   . TRP A 1 2876 ? 122.571 152.662 150.927 1.00 75.96  ? 2876 TRP A CE3   1 
ATOM   11269 C  CZ2   . TRP A 1 2876 ? 124.543 154.685 150.781 1.00 72.47  ? 2876 TRP A CZ2   1 
ATOM   11270 C  CZ3   . TRP A 1 2876 ? 123.898 152.399 151.211 1.00 73.03  ? 2876 TRP A CZ3   1 
ATOM   11271 C  CH2   . TRP A 1 2876 ? 124.868 153.405 151.135 1.00 74.74  ? 2876 TRP A CH2   1 
ATOM   11272 N  N     . LEU A 1 2877 ? 116.418 153.625 150.514 1.00 87.90  ? 2877 LEU A N     1 
ATOM   11273 C  CA    . LEU A 1 2877 ? 115.212 152.923 150.099 1.00 86.11  ? 2877 LEU A CA    1 
ATOM   11274 C  C     . LEU A 1 2877 ? 113.955 153.777 150.197 1.00 89.03  ? 2877 LEU A C     1 
ATOM   11275 O  O     . LEU A 1 2877 ? 112.868 153.289 149.871 1.00 92.95  ? 2877 LEU A O     1 
ATOM   11276 C  CB    . LEU A 1 2877 ? 115.030 151.651 150.934 1.00 86.58  ? 2877 LEU A CB    1 
ATOM   11277 C  CG    . LEU A 1 2877 ? 116.104 150.573 150.786 1.00 85.51  ? 2877 LEU A CG    1 
ATOM   11278 C  CD1   . LEU A 1 2877 ? 115.576 149.231 151.263 1.00 88.24  ? 2877 LEU A CD1   1 
ATOM   11279 C  CD2   . LEU A 1 2877 ? 116.583 150.480 149.348 1.00 86.89  ? 2877 LEU A CD2   1 
ATOM   11280 N  N     . SER A 1 2878 ? 114.071 155.028 150.632 1.00 95.14  ? 2878 SER A N     1 
ATOM   11281 C  CA    . SER A 1 2878 ? 112.920 155.912 150.759 1.00 97.54  ? 2878 SER A CA    1 
ATOM   11282 C  C     . SER A 1 2878 ? 113.420 157.350 150.758 1.00 97.14  ? 2878 SER A C     1 
ATOM   11283 O  O     . SER A 1 2878 ? 114.622 157.610 150.850 1.00 98.02  ? 2878 SER A O     1 
ATOM   11284 C  CB    . SER A 1 2878 ? 112.117 155.599 152.024 1.00 97.64  ? 2878 SER A CB    1 
ATOM   11285 O  OG    . SER A 1 2878 ? 112.912 155.769 153.183 1.00 99.96  ? 2878 SER A OG    1 
ATOM   11286 N  N     . LYS A 1 2879 ? 112.482 158.291 150.651 1.00 98.71  ? 2879 LYS A N     1 
ATOM   11287 C  CA    . LYS A 1 2879 ? 112.851 159.701 150.653 1.00 99.46  ? 2879 LYS A CA    1 
ATOM   11288 C  C     . LYS A 1 2879 ? 113.239 160.190 152.042 1.00 101.72 ? 2879 LYS A C     1 
ATOM   11289 O  O     . LYS A 1 2879 ? 113.906 161.223 152.166 1.00 101.10 ? 2879 LYS A O     1 
ATOM   11290 C  CB    . LYS A 1 2879 ? 111.701 160.548 150.105 1.00 98.64  ? 2879 LYS A CB    1 
ATOM   11291 C  CG    . LYS A 1 2879 ? 110.323 159.968 150.371 1.00 100.79 ? 2879 LYS A CG    1 
ATOM   11292 C  CD    . LYS A 1 2879 ? 109.243 160.769 149.666 1.00 102.75 ? 2879 LYS A CD    1 
ATOM   11293 C  CE    . LYS A 1 2879 ? 109.283 160.542 148.164 1.00 101.85 ? 2879 LYS A CE    1 
ATOM   11294 N  NZ    . LYS A 1 2879 ? 109.458 159.103 147.827 1.00 100.75 ? 2879 LYS A NZ    1 
ATOM   11295 N  N     . ASP A 1 2880 ? 112.839 159.473 153.087 1.00 99.30  ? 2880 ASP A N     1 
ATOM   11296 C  CA    . ASP A 1 2880 ? 113.087 159.881 154.460 1.00 95.19  ? 2880 ASP A CA    1 
ATOM   11297 C  C     . ASP A 1 2880 ? 114.074 158.940 155.140 1.00 95.47  ? 2880 ASP A C     1 
ATOM   11298 O  O     . ASP A 1 2880 ? 114.327 157.822 154.684 1.00 98.25  ? 2880 ASP A O     1 
ATOM   11299 C  CB    . ASP A 1 2880 ? 111.779 159.927 155.253 1.00 98.34  ? 2880 ASP A CB    1 
ATOM   11300 C  CG    . ASP A 1 2880 ? 110.793 160.928 154.689 1.00 104.57 ? 2880 ASP A CG    1 
ATOM   11301 O  OD1   . ASP A 1 2880 ? 111.240 161.931 154.094 1.00 103.07 ? 2880 ASP A OD1   1 
ATOM   11302 O  OD2   . ASP A 1 2880 ? 109.572 160.713 154.841 1.00 106.30 ? 2880 ASP A OD2   1 
ATOM   11303 N  N     . TYR A 1 2881 ? 114.631 159.414 156.252 1.00 77.58  ? 2881 TYR A N     1 
ATOM   11304 C  CA    . TYR A 1 2881 ? 115.598 158.656 157.043 1.00 72.88  ? 2881 TYR A CA    1 
ATOM   11305 C  C     . TYR A 1 2881 ? 114.831 157.717 157.967 1.00 72.19  ? 2881 TYR A C     1 
ATOM   11306 O  O     . TYR A 1 2881 ? 114.499 158.057 159.103 1.00 76.45  ? 2881 TYR A O     1 
ATOM   11307 C  CB    . TYR A 1 2881 ? 116.503 159.601 157.823 1.00 70.57  ? 2881 TYR A CB    1 
ATOM   11308 C  CG    . TYR A 1 2881 ? 117.813 158.989 158.253 1.00 70.25  ? 2881 TYR A CG    1 
ATOM   11309 C  CD1   . TYR A 1 2881 ? 118.752 158.585 157.317 1.00 74.58  ? 2881 TYR A CD1   1 
ATOM   11310 C  CD2   . TYR A 1 2881 ? 118.115 158.827 159.596 1.00 71.96  ? 2881 TYR A CD2   1 
ATOM   11311 C  CE1   . TYR A 1 2881 ? 119.951 158.028 157.706 1.00 73.50  ? 2881 TYR A CE1   1 
ATOM   11312 C  CE2   . TYR A 1 2881 ? 119.311 158.273 159.995 1.00 70.45  ? 2881 TYR A CE2   1 
ATOM   11313 C  CZ    . TYR A 1 2881 ? 120.225 157.874 159.047 1.00 73.34  ? 2881 TYR A CZ    1 
ATOM   11314 O  OH    . TYR A 1 2881 ? 121.417 157.319 159.442 1.00 76.23  ? 2881 TYR A OH    1 
ATOM   11315 N  N     . ILE A 1 2882 ? 114.552 156.516 157.472 1.00 69.58  ? 2882 ILE A N     1 
ATOM   11316 C  CA    . ILE A 1 2882 ? 113.745 155.542 158.205 1.00 72.96  ? 2882 ILE A CA    1 
ATOM   11317 C  C     . ILE A 1 2882 ? 114.572 154.279 158.401 1.00 74.90  ? 2882 ILE A C     1 
ATOM   11318 O  O     . ILE A 1 2882 ? 115.543 154.035 157.667 1.00 79.85  ? 2882 ILE A O     1 
ATOM   11319 C  CB    . ILE A 1 2882 ? 112.422 155.228 157.468 1.00 78.72  ? 2882 ILE A CB    1 
ATOM   11320 C  CG1   . ILE A 1 2882 ? 112.703 154.498 156.155 1.00 79.80  ? 2882 ILE A CG1   1 
ATOM   11321 C  CG2   . ILE A 1 2882 ? 111.636 156.503 157.217 1.00 81.72  ? 2882 ILE A CG2   1 
ATOM   11322 C  CD1   . ILE A 1 2882 ? 111.470 153.905 155.511 1.00 77.03  ? 2882 ILE A CD1   1 
ATOM   11323 N  N     . PRO A 1 2883 ? 114.226 153.462 159.397 1.00 70.86  ? 2883 PRO A N     1 
ATOM   11324 C  CA    . PRO A 1 2883 ? 114.943 152.195 159.587 1.00 71.96  ? 2883 PRO A CA    1 
ATOM   11325 C  C     . PRO A 1 2883 ? 114.809 151.293 158.369 1.00 77.24  ? 2883 PRO A C     1 
ATOM   11326 O  O     . PRO A 1 2883 ? 113.771 151.264 157.704 1.00 76.54  ? 2883 PRO A O     1 
ATOM   11327 C  CB    . PRO A 1 2883 ? 114.267 151.582 160.820 1.00 66.15  ? 2883 PRO A CB    1 
ATOM   11328 C  CG    . PRO A 1 2883 ? 112.964 152.302 160.950 1.00 72.22  ? 2883 PRO A CG    1 
ATOM   11329 C  CD    . PRO A 1 2883 ? 113.225 153.683 160.453 1.00 71.95  ? 2883 PRO A CD    1 
ATOM   11330 N  N     . VAL A 1 2884 ? 115.876 150.552 158.082 1.00 83.26  ? 2884 VAL A N     1 
ATOM   11331 C  CA    . VAL A 1 2884 ? 115.962 149.704 156.901 1.00 76.54  ? 2884 VAL A CA    1 
ATOM   11332 C  C     . VAL A 1 2884 ? 116.338 148.292 157.328 1.00 84.66  ? 2884 VAL A C     1 
ATOM   11333 O  O     . VAL A 1 2884 ? 117.180 148.102 158.213 1.00 87.93  ? 2884 VAL A O     1 
ATOM   11334 C  CB    . VAL A 1 2884 ? 116.973 150.266 155.877 1.00 69.17  ? 2884 VAL A CB    1 
ATOM   11335 C  CG1   . VAL A 1 2884 ? 118.367 150.349 156.477 1.00 74.07  ? 2884 VAL A CG1   1 
ATOM   11336 C  CG2   . VAL A 1 2884 ? 116.984 149.421 154.618 1.00 79.65  ? 2884 VAL A CG2   1 
ATOM   11337 N  N     . ASP A 1 2885 ? 115.689 147.304 156.719 1.00 100.82 ? 2885 ASP A N     1 
ATOM   11338 C  CA    . ASP A 1 2885 ? 116.020 145.913 156.990 1.00 101.05 ? 2885 ASP A CA    1 
ATOM   11339 C  C     . ASP A 1 2885 ? 117.364 145.553 156.367 1.00 103.85 ? 2885 ASP A C     1 
ATOM   11340 O  O     . ASP A 1 2885 ? 117.780 146.126 155.356 1.00 105.02 ? 2885 ASP A O     1 
ATOM   11341 C  CB    . ASP A 1 2885 ? 114.929 144.987 156.454 1.00 99.33  ? 2885 ASP A CB    1 
ATOM   11342 C  CG    . ASP A 1 2885 ? 114.935 143.630 157.129 1.00 103.70 ? 2885 ASP A CG    1 
ATOM   11343 O  OD1   . ASP A 1 2885 ? 115.707 143.449 158.093 1.00 104.29 ? 2885 ASP A OD1   1 
ATOM   11344 O  OD2   . ASP A 1 2885 ? 114.169 142.744 156.695 1.00 105.42 ? 2885 ASP A OD2   1 
ATOM   11345 N  N     . GLN A 1 2886 ? 118.048 144.591 156.990 1.00 97.25  ? 2886 GLN A N     1 
ATOM   11346 C  CA    . GLN A 1 2886 ? 119.387 144.223 156.537 1.00 94.38  ? 2886 GLN A CA    1 
ATOM   11347 C  C     . GLN A 1 2886 ? 119.363 143.615 155.139 1.00 99.94  ? 2886 GLN A C     1 
ATOM   11348 O  O     . GLN A 1 2886 ? 120.220 143.932 154.308 1.00 102.73 ? 2886 GLN A O     1 
ATOM   11349 C  CB    . GLN A 1 2886 ? 120.027 143.255 157.531 1.00 95.38  ? 2886 GLN A CB    1 
ATOM   11350 C  CG    . GLN A 1 2886 ? 121.537 143.147 157.401 1.00 96.25  ? 2886 GLN A CG    1 
ATOM   11351 C  CD    . GLN A 1 2886 ? 122.184 142.531 158.625 1.00 102.41 ? 2886 GLN A CD    1 
ATOM   11352 O  OE1   . GLN A 1 2886 ? 121.924 141.376 158.963 1.00 104.63 ? 2886 GLN A OE1   1 
ATOM   11353 N  NE2   . GLN A 1 2886 ? 123.031 143.300 159.298 1.00 101.75 ? 2886 GLN A NE2   1 
ATOM   11354 N  N     . GLU A 1 2887 ? 118.391 142.743 154.859 1.00 101.35 ? 2887 GLU A N     1 
ATOM   11355 C  CA    . GLU A 1 2887 ? 118.388 142.027 153.585 1.00 100.96 ? 2887 GLU A CA    1 
ATOM   11356 C  C     . GLU A 1 2887 ? 118.030 142.945 152.421 1.00 101.01 ? 2887 GLU A C     1 
ATOM   11357 O  O     . GLU A 1 2887 ? 118.649 142.870 151.352 1.00 100.19 ? 2887 GLU A O     1 
ATOM   11358 C  CB    . GLU A 1 2887 ? 117.425 140.844 153.654 1.00 100.37 ? 2887 GLU A CB    1 
ATOM   11359 C  CG    . GLU A 1 2887 ? 117.917 139.703 154.527 1.00 101.66 ? 2887 GLU A CG    1 
ATOM   11360 C  CD    . GLU A 1 2887 ? 119.400 139.438 154.359 1.00 103.51 ? 2887 GLU A CD    1 
ATOM   11361 O  OE1   . GLU A 1 2887 ? 119.817 139.065 153.242 1.00 101.06 ? 2887 GLU A OE1   1 
ATOM   11362 O  OE2   . GLU A 1 2887 ? 120.150 139.603 155.344 1.00 102.10 ? 2887 GLU A OE2   1 
ATOM   11363 N  N     . GLU A 1 2888 ? 117.026 143.807 152.601 1.00 99.11  ? 2888 GLU A N     1 
ATOM   11364 C  CA    . GLU A 1 2888 ? 116.673 144.753 151.547 1.00 99.03  ? 2888 GLU A CA    1 
ATOM   11365 C  C     . GLU A 1 2888 ? 117.820 145.714 151.272 1.00 98.83  ? 2888 GLU A C     1 
ATOM   11366 O  O     . GLU A 1 2888 ? 118.118 146.029 150.111 1.00 98.76  ? 2888 GLU A O     1 
ATOM   11367 C  CB    . GLU A 1 2888 ? 115.409 145.519 151.933 1.00 96.67  ? 2888 GLU A CB    1 
ATOM   11368 C  CG    . GLU A 1 2888 ? 114.125 144.901 151.408 1.00 99.05  ? 2888 GLU A CG    1 
ATOM   11369 C  CD    . GLU A 1 2888 ? 113.578 143.829 152.329 1.00 103.07 ? 2888 GLU A CD    1 
ATOM   11370 O  OE1   . GLU A 1 2888 ? 113.115 142.785 151.821 1.00 104.60 ? 2888 GLU A OE1   1 
ATOM   11371 O  OE2   . GLU A 1 2888 ? 113.610 144.029 153.561 1.00 102.45 ? 2888 GLU A OE2   1 
ATOM   11372 N  N     . LEU A 1 2889 ? 118.479 146.188 152.332 1.00 84.06  ? 2889 LEU A N     1 
ATOM   11373 C  CA    . LEU A 1 2889 ? 119.646 147.043 152.157 1.00 84.52  ? 2889 LEU A CA    1 
ATOM   11374 C  C     . LEU A 1 2889 ? 120.754 146.309 151.416 1.00 88.74  ? 2889 LEU A C     1 
ATOM   11375 O  O     . LEU A 1 2889 ? 121.412 146.885 150.544 1.00 92.06  ? 2889 LEU A O     1 
ATOM   11376 C  CB    . LEU A 1 2889 ? 120.141 147.537 153.515 1.00 79.45  ? 2889 LEU A CB    1 
ATOM   11377 C  CG    . LEU A 1 2889 ? 121.477 148.280 153.519 1.00 80.63  ? 2889 LEU A CG    1 
ATOM   11378 C  CD1   . LEU A 1 2889 ? 121.336 149.636 152.851 1.00 84.49  ? 2889 LEU A CD1   1 
ATOM   11379 C  CD2   . LEU A 1 2889 ? 121.999 148.429 154.937 1.00 82.75  ? 2889 LEU A CD2   1 
ATOM   11380 N  N     . ARG A 1 2890 ? 120.971 145.033 151.746 1.00 89.00  ? 2890 ARG A N     1 
ATOM   11381 C  CA    . ARG A 1 2890 ? 121.998 144.258 151.059 1.00 84.61  ? 2890 ARG A CA    1 
ATOM   11382 C  C     . ARG A 1 2890 ? 121.683 144.114 149.576 1.00 87.08  ? 2890 ARG A C     1 
ATOM   11383 O  O     . ARG A 1 2890 ? 122.573 144.248 148.732 1.00 92.19  ? 2890 ARG A O     1 
ATOM   11384 C  CB    . ARG A 1 2890 ? 122.145 142.883 151.710 1.00 86.79  ? 2890 ARG A CB    1 
ATOM   11385 C  CG    . ARG A 1 2890 ? 123.376 142.117 151.257 1.00 89.87  ? 2890 ARG A CG    1 
ATOM   11386 C  CD    . ARG A 1 2890 ? 123.276 140.645 151.616 1.00 89.73  ? 2890 ARG A CD    1 
ATOM   11387 N  NE    . ARG A 1 2890 ? 123.046 140.439 153.040 1.00 94.41  ? 2890 ARG A NE    1 
ATOM   11388 C  CZ    . ARG A 1 2890 ? 124.003 140.410 153.957 1.00 92.97  ? 2890 ARG A CZ    1 
ATOM   11389 N  NH1   . ARG A 1 2890 ? 125.276 140.571 153.633 1.00 85.78  ? 2890 ARG A NH1   1 
ATOM   11390 N  NH2   . ARG A 1 2890 ? 123.677 140.211 155.230 1.00 92.14  ? 2890 ARG A NH2   1 
ATOM   11391 N  N     . ASP A 1 2891 ? 120.421 143.841 149.240 1.00 92.07  ? 2891 ASP A N     1 
ATOM   11392 C  CA    . ASP A 1 2891 ? 120.046 143.713 147.832 1.00 91.99  ? 2891 ASP A CA    1 
ATOM   11393 C  C     . ASP A 1 2891 ? 120.226 145.032 147.088 1.00 92.37  ? 2891 ASP A C     1 
ATOM   11394 O  O     . ASP A 1 2891 ? 120.729 145.057 145.953 1.00 92.75  ? 2891 ASP A O     1 
ATOM   11395 C  CB    . ASP A 1 2891 ? 118.604 143.221 147.715 1.00 90.54  ? 2891 ASP A CB    1 
ATOM   11396 C  CG    . ASP A 1 2891 ? 118.371 141.922 148.460 1.00 93.85  ? 2891 ASP A CG    1 
ATOM   11397 O  OD1   . ASP A 1 2891 ? 119.358 141.319 148.929 1.00 95.39  ? 2891 ASP A OD1   1 
ATOM   11398 O  OD2   . ASP A 1 2891 ? 117.200 141.504 148.579 1.00 94.74  ? 2891 ASP A OD2   1 
ATOM   11399 N  N     . TYR A 1 2892 ? 119.820 146.142 147.711 1.00 82.96  ? 2892 TYR A N     1 
ATOM   11400 C  CA    . TYR A 1 2892 ? 120.007 147.445 147.081 1.00 79.85  ? 2892 TYR A CA    1 
ATOM   11401 C  C     . TYR A 1 2892 ? 121.486 147.742 146.867 1.00 82.60  ? 2892 TYR A C     1 
ATOM   11402 O  O     . TYR A 1 2892 ? 121.879 148.257 145.813 1.00 86.24  ? 2892 TYR A O     1 
ATOM   11403 C  CB    . TYR A 1 2892 ? 119.357 148.539 147.927 1.00 77.63  ? 2892 TYR A CB    1 
ATOM   11404 C  CG    . TYR A 1 2892 ? 119.502 149.924 147.342 1.00 79.55  ? 2892 TYR A CG    1 
ATOM   11405 C  CD1   . TYR A 1 2892 ? 118.682 150.349 146.306 1.00 79.40  ? 2892 TYR A CD1   1 
ATOM   11406 C  CD2   . TYR A 1 2892 ? 120.457 150.808 147.824 1.00 83.04  ? 2892 TYR A CD2   1 
ATOM   11407 C  CE1   . TYR A 1 2892 ? 118.809 151.613 145.767 1.00 80.54  ? 2892 TYR A CE1   1 
ATOM   11408 C  CE2   . TYR A 1 2892 ? 120.592 152.074 147.291 1.00 83.75  ? 2892 TYR A CE2   1 
ATOM   11409 C  CZ    . TYR A 1 2892 ? 119.765 152.471 146.263 1.00 85.51  ? 2892 TYR A CZ    1 
ATOM   11410 O  OH    . TYR A 1 2892 ? 119.896 153.733 145.730 1.00 90.20  ? 2892 TYR A OH    1 
ATOM   11411 N  N     . VAL A 1 2893 ? 122.321 147.425 147.860 1.00 74.90  ? 2893 VAL A N     1 
ATOM   11412 C  CA    . VAL A 1 2893 ? 123.754 147.650 147.722 1.00 72.43  ? 2893 VAL A CA    1 
ATOM   11413 C  C     . VAL A 1 2893 ? 124.338 146.757 146.636 1.00 76.54  ? 2893 VAL A C     1 
ATOM   11414 O  O     . VAL A 1 2893 ? 125.248 147.171 145.918 1.00 83.83  ? 2893 VAL A O     1 
ATOM   11415 C  CB    . VAL A 1 2893 ? 124.465 147.451 149.073 1.00 74.48  ? 2893 VAL A CB    1 
ATOM   11416 C  CG1   . VAL A 1 2893 ? 125.972 147.515 148.902 1.00 68.54  ? 2893 VAL A CG1   1 
ATOM   11417 C  CG2   . VAL A 1 2893 ? 124.020 148.513 150.060 1.00 80.00  ? 2893 VAL A CG2   1 
ATOM   11418 N  N     . LYS A 1 2894 ? 123.831 145.531 146.485 1.00 77.38  ? 2894 LYS A N     1 
ATOM   11419 C  CA    . LYS A 1 2894 ? 124.301 144.670 145.402 1.00 76.11  ? 2894 LYS A CA    1 
ATOM   11420 C  C     . LYS A 1 2894 ? 123.975 145.271 144.039 1.00 77.13  ? 2894 LYS A C     1 
ATOM   11421 O  O     . LYS A 1 2894 ? 124.815 145.275 143.130 1.00 77.43  ? 2894 LYS A O     1 
ATOM   11422 C  CB    . LYS A 1 2894 ? 123.694 143.271 145.528 1.00 77.00  ? 2894 LYS A CB    1 
ATOM   11423 C  CG    . LYS A 1 2894 ? 124.160 142.490 146.742 1.00 79.19  ? 2894 LYS A CG    1 
ATOM   11424 C  CD    . LYS A 1 2894 ? 123.523 141.113 146.797 1.00 79.33  ? 2894 LYS A CD    1 
ATOM   11425 C  CE    . LYS A 1 2894 ? 123.763 140.342 145.511 1.00 81.56  ? 2894 LYS A CE    1 
ATOM   11426 N  NZ    . LYS A 1 2894 ? 125.207 140.043 145.309 1.00 76.94  ? 2894 LYS A NZ    1 
ATOM   11427 N  N     . ALA A 1 2895 ? 122.753 145.781 143.876 1.00 74.41  ? 2895 ALA A N     1 
ATOM   11428 C  CA    . ALA A 1 2895 ? 122.386 146.402 142.604 1.00 74.81  ? 2895 ALA A CA    1 
ATOM   11429 C  C     . ALA A 1 2895 ? 123.247 147.632 142.325 1.00 80.53  ? 2895 ALA A C     1 
ATOM   11430 O  O     . ALA A 1 2895 ? 123.757 147.819 141.208 1.00 83.49  ? 2895 ALA A O     1 
ATOM   11431 C  CB    . ALA A 1 2895 ? 120.903 146.769 142.608 1.00 74.82  ? 2895 ALA A CB    1 
ATOM   11432 N  N     . ARG A 1 2896 ? 123.430 148.480 143.340 1.00 72.84  ? 2896 ARG A N     1 
ATOM   11433 C  CA    . ARG A 1 2896 ? 124.258 149.666 143.164 1.00 67.05  ? 2896 ARG A CA    1 
ATOM   11434 C  C     . ARG A 1 2896 ? 125.709 149.295 142.900 1.00 71.80  ? 2896 ARG A C     1 
ATOM   11435 O  O     . ARG A 1 2896 ? 126.402 150.001 142.164 1.00 76.36  ? 2896 ARG A O     1 
ATOM   11436 C  CB    . ARG A 1 2896 ? 124.151 150.576 144.386 1.00 71.84  ? 2896 ARG A CB    1 
ATOM   11437 C  CG    . ARG A 1 2896 ? 122.750 151.106 144.645 1.00 78.34  ? 2896 ARG A CG    1 
ATOM   11438 C  CD    . ARG A 1 2896 ? 122.052 151.510 143.355 1.00 73.72  ? 2896 ARG A CD    1 
ATOM   11439 N  NE    . ARG A 1 2896 ? 122.598 152.739 142.792 1.00 76.72  ? 2896 ARG A NE    1 
ATOM   11440 C  CZ    . ARG A 1 2896 ? 122.383 153.151 141.551 1.00 78.96  ? 2896 ARG A CZ    1 
ATOM   11441 N  NH1   . ARG A 1 2896 ? 121.634 152.456 140.712 1.00 75.95  ? 2896 ARG A NH1   1 
ATOM   11442 N  NH2   . ARG A 1 2896 ? 122.933 154.291 141.142 1.00 75.89  ? 2896 ARG A NH2   1 
ATOM   11443 N  N     . LEU A 1 2897 ? 126.183 148.190 143.477 1.00 69.79  ? 2897 LEU A N     1 
ATOM   11444 C  CA    . LEU A 1 2897 ? 127.539 147.727 143.209 1.00 65.80  ? 2897 LEU A CA    1 
ATOM   11445 C  C     . LEU A 1 2897 ? 127.677 147.231 141.780 1.00 71.70  ? 2897 LEU A C     1 
ATOM   11446 O  O     . LEU A 1 2897 ? 128.720 147.426 141.153 1.00 77.97  ? 2897 LEU A O     1 
ATOM   11447 C  CB    . LEU A 1 2897 ? 127.923 146.624 144.193 1.00 69.76  ? 2897 LEU A CB    1 
ATOM   11448 C  CG    . LEU A 1 2897 ? 128.799 147.027 145.378 1.00 65.37  ? 2897 LEU A CG    1 
ATOM   11449 C  CD1   . LEU A 1 2897 ? 129.068 145.824 146.258 1.00 72.48  ? 2897 LEU A CD1   1 
ATOM   11450 C  CD2   . LEU A 1 2897 ? 130.100 147.640 144.896 1.00 63.74  ? 2897 LEU A CD2   1 
ATOM   11451 N  N     . LYS A 1 2898 ? 126.646 146.571 141.253 1.00 76.23  ? 2898 LYS A N     1 
ATOM   11452 C  CA    . LYS A 1 2898 ? 126.678 146.169 139.849 1.00 78.72  ? 2898 LYS A CA    1 
ATOM   11453 C  C     . LYS A 1 2898 ? 126.772 147.391 138.941 1.00 78.74  ? 2898 LYS A C     1 
ATOM   11454 O  O     . LYS A 1 2898 ? 127.575 147.425 137.997 1.00 78.03  ? 2898 LYS A O     1 
ATOM   11455 C  CB    . LYS A 1 2898 ? 125.443 145.335 139.512 1.00 79.99  ? 2898 LYS A CB    1 
ATOM   11456 C  CG    . LYS A 1 2898 ? 125.729 143.854 139.327 1.00 79.95  ? 2898 LYS A CG    1 
ATOM   11457 C  CD    . LYS A 1 2898 ? 124.446 143.040 139.316 1.00 79.39  ? 2898 LYS A CD    1 
ATOM   11458 C  CE    . LYS A 1 2898 ? 124.552 141.856 138.370 1.00 76.83  ? 2898 LYS A CE    1 
ATOM   11459 N  NZ    . LYS A 1 2898 ? 123.216 141.304 138.015 1.00 79.80  ? 2898 LYS A NZ    1 
ATOM   11460 N  N     . VAL A 1 2899 ? 125.968 148.417 139.230 1.00 75.01  ? 2899 VAL A N     1 
ATOM   11461 C  CA    . VAL A 1 2899 ? 126.032 149.646 138.436 1.00 71.26  ? 2899 VAL A CA    1 
ATOM   11462 C  C     . VAL A 1 2899 ? 127.403 150.304 138.574 1.00 70.69  ? 2899 VAL A C     1 
ATOM   11463 O  O     . VAL A 1 2899 ? 127.989 150.773 137.589 1.00 70.92  ? 2899 VAL A O     1 
ATOM   11464 C  CB    . VAL A 1 2899 ? 124.898 150.605 138.839 1.00 74.52  ? 2899 VAL A CB    1 
ATOM   11465 C  CG1   . VAL A 1 2899 ? 124.945 151.862 137.989 1.00 74.48  ? 2899 VAL A CG1   1 
ATOM   11466 C  CG2   . VAL A 1 2899 ? 123.552 149.917 138.696 1.00 74.83  ? 2899 VAL A CG2   1 
ATOM   11467 N  N     . PHE A 1 2900 ? 127.932 150.346 139.799 1.00 72.21  ? 2900 PHE A N     1 
ATOM   11468 C  CA    . PHE A 1 2900 ? 129.247 150.924 140.054 1.00 72.01  ? 2900 PHE A CA    1 
ATOM   11469 C  C     . PHE A 1 2900 ? 130.332 150.185 139.281 1.00 72.48  ? 2900 PHE A C     1 
ATOM   11470 O  O     . PHE A 1 2900 ? 131.246 150.807 138.727 1.00 68.35  ? 2900 PHE A O     1 
ATOM   11471 C  CB    . PHE A 1 2900 ? 129.521 150.882 141.559 1.00 69.32  ? 2900 PHE A CB    1 
ATOM   11472 C  CG    . PHE A 1 2900 ? 130.861 151.422 141.962 1.00 63.11  ? 2900 PHE A CG    1 
ATOM   11473 C  CD1   . PHE A 1 2900 ? 131.152 152.767 141.834 1.00 68.18  ? 2900 PHE A CD1   1 
ATOM   11474 C  CD2   . PHE A 1 2900 ? 131.823 150.582 142.495 1.00 69.71  ? 2900 PHE A CD2   1 
ATOM   11475 C  CE1   . PHE A 1 2900 ? 132.382 153.261 142.220 1.00 70.03  ? 2900 PHE A CE1   1 
ATOM   11476 C  CE2   . PHE A 1 2900 ? 133.054 151.070 142.879 1.00 70.45  ? 2900 PHE A CE2   1 
ATOM   11477 C  CZ    . PHE A 1 2900 ? 133.334 152.411 142.741 1.00 65.87  ? 2900 PHE A CZ    1 
ATOM   11478 N  N     . TYR A 1 2901 ? 130.246 148.855 139.239 1.00 80.21  ? 2901 TYR A N     1 
ATOM   11479 C  CA    . TYR A 1 2901 ? 131.205 148.061 138.482 1.00 77.26  ? 2901 TYR A CA    1 
ATOM   11480 C  C     . TYR A 1 2901 ? 131.118 148.383 136.999 1.00 77.60  ? 2901 TYR A C     1 
ATOM   11481 O  O     . TYR A 1 2901 ? 132.144 148.535 136.325 1.00 76.15  ? 2901 TYR A O     1 
ATOM   11482 C  CB    . TYR A 1 2901 ? 130.943 146.573 138.707 1.00 74.15  ? 2901 TYR A CB    1 
ATOM   11483 C  CG    . TYR A 1 2901 ? 131.235 146.090 140.106 1.00 70.38  ? 2901 TYR A CG    1 
ATOM   11484 C  CD1   . TYR A 1 2901 ? 132.007 146.844 140.977 1.00 72.98  ? 2901 TYR A CD1   1 
ATOM   11485 C  CD2   . TYR A 1 2901 ? 130.721 144.885 140.561 1.00 72.28  ? 2901 TYR A CD2   1 
ATOM   11486 C  CE1   . TYR A 1 2901 ? 132.266 146.407 142.257 1.00 76.62  ? 2901 TYR A CE1   1 
ATOM   11487 C  CE2   . TYR A 1 2901 ? 130.975 144.439 141.838 1.00 74.76  ? 2901 TYR A CE2   1 
ATOM   11488 C  CZ    . TYR A 1 2901 ? 131.747 145.203 142.682 1.00 81.05  ? 2901 TYR A CZ    1 
ATOM   11489 O  OH    . TYR A 1 2901 ? 132.000 144.758 143.957 1.00 86.24  ? 2901 TYR A OH    1 
ATOM   11490 N  N     . GLU A 1 2902 ? 129.897 148.491 136.473 1.00 91.90  ? 2902 GLU A N     1 
ATOM   11491 C  CA    . GLU A 1 2902 ? 129.735 148.797 135.058 1.00 91.88  ? 2902 GLU A CA    1 
ATOM   11492 C  C     . GLU A 1 2902 ? 130.099 150.235 134.711 1.00 91.02  ? 2902 GLU A C     1 
ATOM   11493 O  O     . GLU A 1 2902 ? 130.307 150.530 133.530 1.00 90.84  ? 2902 GLU A O     1 
ATOM   11494 C  CB    . GLU A 1 2902 ? 128.298 148.517 134.615 1.00 93.76  ? 2902 GLU A CB    1 
ATOM   11495 C  CG    . GLU A 1 2902 ? 127.868 147.071 134.772 1.00 95.26  ? 2902 GLU A CG    1 
ATOM   11496 C  CD    . GLU A 1 2902 ? 126.403 146.865 134.444 1.00 96.68  ? 2902 GLU A CD    1 
ATOM   11497 O  OE1   . GLU A 1 2902 ? 125.924 145.717 134.550 1.00 99.00  ? 2902 GLU A OE1   1 
ATOM   11498 O  OE2   . GLU A 1 2902 ? 125.731 147.852 134.080 1.00 93.52  ? 2902 GLU A OE2   1 
ATOM   11499 N  N     . GLU A 1 2903 ? 130.187 151.130 135.692 1.00 94.33  ? 2903 GLU A N     1 
ATOM   11500 C  CA    . GLU A 1 2903 ? 130.415 152.539 135.390 1.00 95.33  ? 2903 GLU A CA    1 
ATOM   11501 C  C     . GLU A 1 2903 ? 131.764 153.071 135.846 1.00 97.76  ? 2903 GLU A C     1 
ATOM   11502 O  O     . GLU A 1 2903 ? 132.457 153.719 135.057 1.00 97.67  ? 2903 GLU A O     1 
ATOM   11503 C  CB    . GLU A 1 2903 ? 129.302 153.399 136.007 1.00 95.67  ? 2903 GLU A CB    1 
ATOM   11504 C  CG    . GLU A 1 2903 ? 127.949 153.233 135.335 1.00 96.44  ? 2903 GLU A CG    1 
ATOM   11505 C  CD    . GLU A 1 2903 ? 126.904 154.183 135.886 1.00 100.81 ? 2903 GLU A CD    1 
ATOM   11506 O  OE1   . GLU A 1 2903 ? 127.239 154.978 136.789 1.00 99.73  ? 2903 GLU A OE1   1 
ATOM   11507 O  OE2   . GLU A 1 2903 ? 125.748 154.137 135.414 1.00 97.03  ? 2903 GLU A OE2   1 
ATOM   11508 N  N     . GLU A 1 2904 ? 132.167 152.826 137.093 1.00 89.80  ? 2904 GLU A N     1 
ATOM   11509 C  CA    . GLU A 1 2904 ? 133.311 153.520 137.675 1.00 84.84  ? 2904 GLU A CA    1 
ATOM   11510 C  C     . GLU A 1 2904 ? 134.504 152.607 137.930 1.00 87.69  ? 2904 GLU A C     1 
ATOM   11511 O  O     . GLU A 1 2904 ? 135.599 152.870 137.424 1.00 90.28  ? 2904 GLU A O     1 
ATOM   11512 C  CB    . GLU A 1 2904 ? 132.887 154.209 138.977 1.00 85.79  ? 2904 GLU A CB    1 
ATOM   11513 C  CG    . GLU A 1 2904 ? 132.150 155.519 138.777 1.00 87.93  ? 2904 GLU A CG    1 
ATOM   11514 C  CD    . GLU A 1 2904 ? 133.088 156.685 138.555 1.00 93.33  ? 2904 GLU A CD    1 
ATOM   11515 O  OE1   . GLU A 1 2904 ? 134.252 156.605 139.000 1.00 96.07  ? 2904 GLU A OE1   1 
ATOM   11516 O  OE2   . GLU A 1 2904 ? 132.663 157.683 137.935 1.00 95.91  ? 2904 GLU A OE2   1 
ATOM   11517 N  N     . LEU A 1 2905 ? 134.331 151.540 138.706 1.00 84.45  ? 2905 LEU A N     1 
ATOM   11518 C  CA    . LEU A 1 2905 ? 135.453 150.712 139.137 1.00 83.06  ? 2905 LEU A CA    1 
ATOM   11519 C  C     . LEU A 1 2905 ? 135.032 149.253 139.114 1.00 83.48  ? 2905 LEU A C     1 
ATOM   11520 O  O     . LEU A 1 2905 ? 134.113 148.861 139.839 1.00 90.71  ? 2905 LEU A O     1 
ATOM   11521 C  CB    . LEU A 1 2905 ? 135.923 151.116 140.537 1.00 82.43  ? 2905 LEU A CB    1 
ATOM   11522 C  CG    . LEU A 1 2905 ? 137.292 150.606 140.984 1.00 81.23  ? 2905 LEU A CG    1 
ATOM   11523 C  CD1   . LEU A 1 2905 ? 138.382 151.191 140.106 1.00 84.76  ? 2905 LEU A CD1   1 
ATOM   11524 C  CD2   . LEU A 1 2905 ? 137.536 150.951 142.444 1.00 82.41  ? 2905 LEU A CD2   1 
ATOM   11525 N  N     . ASP A 1 2906 ? 135.705 148.453 138.291 1.00 87.51  ? 2906 ASP A N     1 
ATOM   11526 C  CA    . ASP A 1 2906 ? 135.363 147.039 138.133 1.00 90.27  ? 2906 ASP A CA    1 
ATOM   11527 C  C     . ASP A 1 2906 ? 136.251 146.162 139.017 1.00 90.97  ? 2906 ASP A C     1 
ATOM   11528 O  O     . ASP A 1 2906 ? 137.043 145.345 138.549 1.00 97.00  ? 2906 ASP A O     1 
ATOM   11529 C  CB    . ASP A 1 2906 ? 135.466 146.634 136.668 1.00 95.98  ? 2906 ASP A CB    1 
ATOM   11530 C  CG    . ASP A 1 2906 ? 134.573 145.459 136.326 1.00 101.30 ? 2906 ASP A CG    1 
ATOM   11531 O  OD1   . ASP A 1 2906 ? 134.730 144.390 136.951 1.00 97.22  ? 2906 ASP A OD1   1 
ATOM   11532 O  OD2   . ASP A 1 2906 ? 133.713 145.606 135.432 1.00 103.06 ? 2906 ASP A OD2   1 
ATOM   11533 N  N     . VAL A 1 2907 ? 136.104 146.349 140.322 1.00 87.08  ? 2907 VAL A N     1 
ATOM   11534 C  CA    . VAL A 1 2907 ? 136.786 145.545 141.325 1.00 88.10  ? 2907 VAL A CA    1 
ATOM   11535 C  C     . VAL A 1 2907 ? 135.730 144.882 142.200 1.00 89.95  ? 2907 VAL A C     1 
ATOM   11536 O  O     . VAL A 1 2907 ? 135.117 145.531 143.049 1.00 90.08  ? 2907 VAL A O     1 
ATOM   11537 C  CB    . VAL A 1 2907 ? 137.755 146.393 142.168 1.00 83.06  ? 2907 VAL A CB    1 
ATOM   11538 C  CG1   . VAL A 1 2907 ? 138.472 145.519 143.176 1.00 82.67  ? 2907 VAL A CG1   1 
ATOM   11539 C  CG2   . VAL A 1 2907 ? 138.754 147.105 141.273 1.00 85.69  ? 2907 VAL A CG2   1 
ATOM   11540 N  N     . PRO A 1 2908 ? 135.488 143.584 142.019 1.00 82.78  ? 2908 PRO A N     1 
ATOM   11541 C  CA    . PRO A 1 2908 ? 134.408 142.921 142.763 1.00 80.76  ? 2908 PRO A CA    1 
ATOM   11542 C  C     . PRO A 1 2908 ? 134.635 142.975 144.266 1.00 83.24  ? 2908 PRO A C     1 
ATOM   11543 O  O     . PRO A 1 2908 ? 135.765 142.877 144.749 1.00 84.38  ? 2908 PRO A O     1 
ATOM   11544 C  CB    . PRO A 1 2908 ? 134.449 141.480 142.239 1.00 77.13  ? 2908 PRO A CB    1 
ATOM   11545 C  CG    . PRO A 1 2908 ? 135.219 141.551 140.954 1.00 77.85  ? 2908 PRO A CG    1 
ATOM   11546 C  CD    . PRO A 1 2908 ? 136.212 142.647 141.148 1.00 79.50  ? 2908 PRO A CD    1 
ATOM   11547 N  N     . LEU A 1 2909 ? 133.539 143.132 145.006 1.00 77.31  ? 2909 LEU A N     1 
ATOM   11548 C  CA    . LEU A 1 2909 ? 133.565 143.203 146.460 1.00 75.12  ? 2909 LEU A CA    1 
ATOM   11549 C  C     . LEU A 1 2909 ? 132.625 142.154 147.035 1.00 73.49  ? 2909 LEU A C     1 
ATOM   11550 O  O     . LEU A 1 2909 ? 131.540 141.923 146.493 1.00 77.29  ? 2909 LEU A O     1 
ATOM   11551 C  CB    . LEU A 1 2909 ? 133.161 144.594 146.959 1.00 71.19  ? 2909 LEU A CB    1 
ATOM   11552 C  CG    . LEU A 1 2909 ? 133.916 145.798 146.395 1.00 76.27  ? 2909 LEU A CG    1 
ATOM   11553 C  CD1   . LEU A 1 2909 ? 133.428 147.080 147.051 1.00 73.56  ? 2909 LEU A CD1   1 
ATOM   11554 C  CD2   . LEU A 1 2909 ? 135.413 145.633 146.584 1.00 78.92  ? 2909 LEU A CD2   1 
ATOM   11555 N  N     . VAL A 1 2910 ? 133.045 141.524 148.127 1.00 71.83  ? 2910 VAL A N     1 
ATOM   11556 C  CA    . VAL A 1 2910 ? 132.193 140.583 148.844 1.00 75.48  ? 2910 VAL A CA    1 
ATOM   11557 C  C     . VAL A 1 2910 ? 131.470 141.331 149.954 1.00 77.54  ? 2910 VAL A C     1 
ATOM   11558 O  O     . VAL A 1 2910 ? 132.101 141.996 150.785 1.00 84.51  ? 2910 VAL A O     1 
ATOM   11559 C  CB    . VAL A 1 2910 ? 133.019 139.414 149.403 1.00 73.26  ? 2910 VAL A CB    1 
ATOM   11560 C  CG1   . VAL A 1 2910 ? 132.175 138.571 150.343 1.00 74.40  ? 2910 VAL A CG1   1 
ATOM   11561 C  CG2   . VAL A 1 2910 ? 133.567 138.563 148.270 1.00 74.13  ? 2910 VAL A CG2   1 
ATOM   11562 N  N     . LEU A 1 2911 ? 130.145 141.225 149.974 1.00 68.43  ? 2911 LEU A N     1 
ATOM   11563 C  CA    . LEU A 1 2911 ? 129.320 142.004 150.888 1.00 72.59  ? 2911 LEU A CA    1 
ATOM   11564 C  C     . LEU A 1 2911 ? 129.063 141.216 152.165 1.00 71.94  ? 2911 LEU A C     1 
ATOM   11565 O  O     . LEU A 1 2911 ? 128.684 140.041 152.113 1.00 78.64  ? 2911 LEU A O     1 
ATOM   11566 C  CB    . LEU A 1 2911 ? 127.999 142.387 150.225 1.00 70.23  ? 2911 LEU A CB    1 
ATOM   11567 C  CG    . LEU A 1 2911 ? 128.080 143.483 149.165 1.00 66.41  ? 2911 LEU A CG    1 
ATOM   11568 C  CD1   . LEU A 1 2911 ? 126.692 143.954 148.789 1.00 68.53  ? 2911 LEU A CD1   1 
ATOM   11569 C  CD2   . LEU A 1 2911 ? 128.917 144.640 149.669 1.00 68.96  ? 2911 LEU A CD2   1 
ATOM   11570 N  N     . PHE A 1 2912 ? 129.272 141.865 153.307 1.00 64.40  ? 2912 PHE A N     1 
ATOM   11571 C  CA    . PHE A 1 2912 ? 128.920 141.320 154.608 1.00 68.43  ? 2912 PHE A CA    1 
ATOM   11572 C  C     . PHE A 1 2912 ? 128.386 142.444 155.487 1.00 77.45  ? 2912 PHE A C     1 
ATOM   11573 O  O     . PHE A 1 2912 ? 128.359 143.612 155.091 1.00 83.66  ? 2912 PHE A O     1 
ATOM   11574 C  CB    . PHE A 1 2912 ? 130.109 140.601 155.269 1.00 66.07  ? 2912 PHE A CB    1 
ATOM   11575 C  CG    . PHE A 1 2912 ? 131.401 141.369 155.229 1.00 67.05  ? 2912 PHE A CG    1 
ATOM   11576 C  CD1   . PHE A 1 2912 ? 131.822 142.101 156.325 1.00 76.75  ? 2912 PHE A CD1   1 
ATOM   11577 C  CD2   . PHE A 1 2912 ? 132.214 141.328 154.109 1.00 63.73  ? 2912 PHE A CD2   1 
ATOM   11578 C  CE1   . PHE A 1 2912 ? 133.016 142.797 156.294 1.00 74.11  ? 2912 PHE A CE1   1 
ATOM   11579 C  CE2   . PHE A 1 2912 ? 133.407 142.020 154.073 1.00 65.97  ? 2912 PHE A CE2   1 
ATOM   11580 C  CZ    . PHE A 1 2912 ? 133.810 142.754 155.168 1.00 66.50  ? 2912 PHE A CZ    1 
ATOM   11581 N  N     . ASN A 1 2913 ? 127.947 142.073 156.693 1.00 79.91  ? 2913 ASN A N     1 
ATOM   11582 C  CA    . ASN A 1 2913 ? 127.226 143.013 157.548 1.00 80.64  ? 2913 ASN A CA    1 
ATOM   11583 C  C     . ASN A 1 2913 ? 128.078 144.228 157.895 1.00 78.79  ? 2913 ASN A C     1 
ATOM   11584 O  O     . ASN A 1 2913 ? 127.579 145.362 157.911 1.00 86.10  ? 2913 ASN A O     1 
ATOM   11585 C  CB    . ASN A 1 2913 ? 126.762 142.304 158.820 1.00 84.57  ? 2913 ASN A CB    1 
ATOM   11586 C  CG    . ASN A 1 2913 ? 126.055 140.996 158.531 1.00 82.55  ? 2913 ASN A CG    1 
ATOM   11587 O  OD1   . ASN A 1 2913 ? 125.823 140.645 157.374 1.00 83.05  ? 2913 ASN A OD1   1 
ATOM   11588 N  ND2   . ASN A 1 2913 ? 125.713 140.263 159.583 1.00 82.38  ? 2913 ASN A ND2   1 
ATOM   11589 N  N     . GLU A 1 2914 ? 129.362 144.013 158.186 1.00 66.91  ? 2914 GLU A N     1 
ATOM   11590 C  CA    . GLU A 1 2914 ? 130.234 145.133 158.516 1.00 74.33  ? 2914 GLU A CA    1 
ATOM   11591 C  C     . GLU A 1 2914 ? 130.379 146.096 157.346 1.00 80.87  ? 2914 GLU A C     1 
ATOM   11592 O  O     . GLU A 1 2914 ? 130.494 147.307 157.556 1.00 87.35  ? 2914 GLU A O     1 
ATOM   11593 C  CB    . GLU A 1 2914 ? 131.602 144.623 158.968 1.00 77.33  ? 2914 GLU A CB    1 
ATOM   11594 C  CG    . GLU A 1 2914 ? 131.644 144.166 160.419 1.00 80.48  ? 2914 GLU A CG    1 
ATOM   11595 C  CD    . GLU A 1 2914 ? 131.244 142.714 160.592 1.00 86.72  ? 2914 GLU A CD    1 
ATOM   11596 O  OE1   . GLU A 1 2914 ? 130.163 142.327 160.101 1.00 89.61  ? 2914 GLU A OE1   1 
ATOM   11597 O  OE2   . GLU A 1 2914 ? 132.011 141.959 161.225 1.00 89.00  ? 2914 GLU A OE2   1 
ATOM   11598 N  N     . VAL A 1 2915 ? 130.364 145.588 156.112 1.00 68.06  ? 2915 VAL A N     1 
ATOM   11599 C  CA    . VAL A 1 2915 ? 130.411 146.475 154.952 1.00 63.02  ? 2915 VAL A CA    1 
ATOM   11600 C  C     . VAL A 1 2915 ? 129.161 147.343 154.896 1.00 74.92  ? 2915 VAL A C     1 
ATOM   11601 O  O     . VAL A 1 2915 ? 129.234 148.542 154.602 1.00 87.88  ? 2915 VAL A O     1 
ATOM   11602 C  CB    . VAL A 1 2915 ? 130.597 145.665 153.656 1.00 62.99  ? 2915 VAL A CB    1 
ATOM   11603 C  CG1   . VAL A 1 2915 ? 130.200 146.496 152.453 1.00 59.88  ? 2915 VAL A CG1   1 
ATOM   11604 C  CG2   . VAL A 1 2915 ? 132.036 145.224 153.521 1.00 75.36  ? 2915 VAL A CG2   1 
ATOM   11605 N  N     . LEU A 1 2916 ? 127.995 146.753 155.170 1.00 68.54  ? 2916 LEU A N     1 
ATOM   11606 C  CA    . LEU A 1 2916 ? 126.764 147.536 155.199 1.00 62.33  ? 2916 LEU A CA    1 
ATOM   11607 C  C     . LEU A 1 2916 ? 126.828 148.616 156.271 1.00 65.38  ? 2916 LEU A C     1 
ATOM   11608 O  O     . LEU A 1 2916 ? 126.463 149.773 156.023 1.00 75.68  ? 2916 LEU A O     1 
ATOM   11609 C  CB    . LEU A 1 2916 ? 125.564 146.620 155.434 1.00 62.70  ? 2916 LEU A CB    1 
ATOM   11610 C  CG    . LEU A 1 2916 ? 125.420 145.426 154.491 1.00 65.17  ? 2916 LEU A CG    1 
ATOM   11611 C  CD1   . LEU A 1 2916 ? 124.119 144.689 154.761 1.00 75.42  ? 2916 LEU A CD1   1 
ATOM   11612 C  CD2   . LEU A 1 2916 ? 125.495 145.874 153.041 1.00 61.43  ? 2916 LEU A CD2   1 
ATOM   11613 N  N     . ASP A 1 2917 ? 127.307 148.262 157.465 1.00 71.36  ? 2917 ASP A N     1 
ATOM   11614 C  CA    . ASP A 1 2917 ? 127.423 149.252 158.532 1.00 75.68  ? 2917 ASP A CA    1 
ATOM   11615 C  C     . ASP A 1 2917 ? 128.378 150.372 158.136 1.00 79.90  ? 2917 ASP A C     1 
ATOM   11616 O  O     . ASP A 1 2917 ? 128.099 151.555 158.364 1.00 89.05  ? 2917 ASP A O     1 
ATOM   11617 C  CB    . ASP A 1 2917 ? 127.887 148.578 159.823 1.00 76.85  ? 2917 ASP A CB    1 
ATOM   11618 C  CG    . ASP A 1 2917 ? 126.938 147.493 160.287 1.00 89.03  ? 2917 ASP A CG    1 
ATOM   11619 O  OD1   . ASP A 1 2917 ? 125.767 147.503 159.858 1.00 88.87  ? 2917 ASP A OD1   1 
ATOM   11620 O  OD2   . ASP A 1 2917 ? 127.364 146.630 161.084 1.00 87.65  ? 2917 ASP A OD2   1 
ATOM   11621 N  N     . HIS A 1 2918 ? 129.512 150.014 157.530 1.00 65.10  ? 2918 HIS A N     1 
ATOM   11622 C  CA    . HIS A 1 2918 ? 130.506 151.015 157.159 1.00 64.70  ? 2918 HIS A CA    1 
ATOM   11623 C  C     . HIS A 1 2918 ? 129.985 151.947 156.073 1.00 69.54  ? 2918 HIS A C     1 
ATOM   11624 O  O     . HIS A 1 2918 ? 130.198 153.163 156.140 1.00 82.28  ? 2918 HIS A O     1 
ATOM   11625 C  CB    . HIS A 1 2918 ? 131.792 150.327 156.708 1.00 62.43  ? 2918 HIS A CB    1 
ATOM   11626 C  CG    . HIS A 1 2918 ? 132.469 149.551 157.793 1.00 71.06  ? 2918 HIS A CG    1 
ATOM   11627 N  ND1   . HIS A 1 2918 ? 133.307 148.487 157.536 1.00 77.26  ? 2918 HIS A ND1   1 
ATOM   11628 C  CD2   . HIS A 1 2918 ? 132.426 149.679 159.140 1.00 70.55  ? 2918 HIS A CD2   1 
ATOM   11629 C  CE1   . HIS A 1 2918 ? 133.754 147.996 158.678 1.00 81.06  ? 2918 HIS A CE1   1 
ATOM   11630 N  NE2   . HIS A 1 2918 ? 133.234 148.701 159.666 1.00 79.17  ? 2918 HIS A NE2   1 
ATOM   11631 N  N     . VAL A 1 2919 ? 129.307 151.402 155.059 1.00 57.83  ? 2919 VAL A N     1 
ATOM   11632 C  CA    . VAL A 1 2919 ? 128.778 152.267 154.011 1.00 61.48  ? 2919 VAL A CA    1 
ATOM   11633 C  C     . VAL A 1 2919 ? 127.667 153.150 154.562 1.00 63.29  ? 2919 VAL A C     1 
ATOM   11634 O  O     . VAL A 1 2919 ? 127.530 154.306 154.148 1.00 64.63  ? 2919 VAL A O     1 
ATOM   11635 C  CB    . VAL A 1 2919 ? 128.314 151.457 152.782 1.00 53.82  ? 2919 VAL A CB    1 
ATOM   11636 C  CG1   . VAL A 1 2919 ? 129.473 150.665 152.200 1.00 57.08  ? 2919 VAL A CG1   1 
ATOM   11637 C  CG2   . VAL A 1 2919 ? 127.150 150.548 153.118 1.00 58.03  ? 2919 VAL A CG2   1 
ATOM   11638 N  N     . LEU A 1 2920 ? 126.871 152.646 155.511 1.00 63.37  ? 2920 LEU A N     1 
ATOM   11639 C  CA    . LEU A 1 2920 ? 125.867 153.497 156.141 1.00 56.39  ? 2920 LEU A CA    1 
ATOM   11640 C  C     . LEU A 1 2920 ? 126.516 154.638 156.916 1.00 62.83  ? 2920 LEU A C     1 
ATOM   11641 O  O     . LEU A 1 2920 ? 126.051 155.782 156.855 1.00 73.74  ? 2920 LEU A O     1 
ATOM   11642 C  CB    . LEU A 1 2920 ? 124.967 152.666 157.054 1.00 54.42  ? 2920 LEU A CB    1 
ATOM   11643 C  CG    . LEU A 1 2920 ? 123.947 151.778 156.339 1.00 58.74  ? 2920 LEU A CG    1 
ATOM   11644 C  CD1   . LEU A 1 2920 ? 122.934 151.222 157.323 1.00 64.66  ? 2920 LEU A CD1   1 
ATOM   11645 C  CD2   . LEU A 1 2920 ? 123.257 152.544 155.226 1.00 56.86  ? 2920 LEU A CD2   1 
ATOM   11646 N  N     . ARG A 1 2921 ? 127.597 154.349 157.645 1.00 57.51  ? 2921 ARG A N     1 
ATOM   11647 C  CA    . ARG A 1 2921 ? 128.297 155.402 158.378 1.00 57.18  ? 2921 ARG A CA    1 
ATOM   11648 C  C     . ARG A 1 2921 ? 128.883 156.444 157.431 1.00 61.32  ? 2921 ARG A C     1 
ATOM   11649 O  O     . ARG A 1 2921 ? 128.781 157.655 157.678 1.00 69.73  ? 2921 ARG A O     1 
ATOM   11650 C  CB    . ARG A 1 2921 ? 129.399 154.794 159.244 1.00 54.77  ? 2921 ARG A CB    1 
ATOM   11651 C  CG    . ARG A 1 2921 ? 128.898 153.876 160.342 1.00 66.07  ? 2921 ARG A CG    1 
ATOM   11652 C  CD    . ARG A 1 2921 ? 130.044 153.108 160.977 1.00 67.22  ? 2921 ARG A CD    1 
ATOM   11653 N  NE    . ARG A 1 2921 ? 129.579 151.925 161.690 1.00 67.83  ? 2921 ARG A NE    1 
ATOM   11654 C  CZ    . ARG A 1 2921 ? 130.371 151.079 162.335 1.00 71.08  ? 2921 ARG A CZ    1 
ATOM   11655 N  NH1   . ARG A 1 2921 ? 131.682 151.253 162.374 1.00 73.08  ? 2921 ARG A NH1   1 
ATOM   11656 N  NH2   . ARG A 1 2921 ? 129.835 150.034 162.957 1.00 73.05  ? 2921 ARG A NH2   1 
ATOM   11657 N  N     . ILE A 1 2922 ? 129.507 155.992 156.342 1.00 60.97  ? 2922 ILE A N     1 
ATOM   11658 C  CA    . ILE A 1 2922 ? 130.109 156.925 155.396 1.00 61.12  ? 2922 ILE A CA    1 
ATOM   11659 C  C     . ILE A 1 2922 ? 129.033 157.765 154.717 1.00 62.26  ? 2922 ILE A C     1 
ATOM   11660 O  O     . ILE A 1 2922 ? 129.221 158.964 154.483 1.00 70.68  ? 2922 ILE A O     1 
ATOM   11661 C  CB    . ILE A 1 2922 ? 130.977 156.167 154.376 1.00 58.65  ? 2922 ILE A CB    1 
ATOM   11662 C  CG1   . ILE A 1 2922 ? 132.130 155.460 155.088 1.00 56.13  ? 2922 ILE A CG1   1 
ATOM   11663 C  CG2   . ILE A 1 2922 ? 131.537 157.118 153.339 1.00 56.16  ? 2922 ILE A CG2   1 
ATOM   11664 C  CD1   . ILE A 1 2922 ? 132.925 154.541 154.194 1.00 58.83  ? 2922 ILE A CD1   1 
ATOM   11665 N  N     . ASP A 1 2923 ? 127.890 157.156 154.393 1.00 61.72  ? 2923 ASP A N     1 
ATOM   11666 C  CA    . ASP A 1 2923 ? 126.782 157.915 153.824 1.00 62.66  ? 2923 ASP A CA    1 
ATOM   11667 C  C     . ASP A 1 2923 ? 126.252 158.942 154.816 1.00 66.21  ? 2923 ASP A C     1 
ATOM   11668 O  O     . ASP A 1 2923 ? 125.888 160.058 154.430 1.00 70.59  ? 2923 ASP A O     1 
ATOM   11669 C  CB    . ASP A 1 2923 ? 125.668 156.967 153.385 1.00 70.84  ? 2923 ASP A CB    1 
ATOM   11670 C  CG    . ASP A 1 2923 ? 124.507 157.692 152.737 1.00 79.26  ? 2923 ASP A CG    1 
ATOM   11671 O  OD1   . ASP A 1 2923 ? 124.704 158.285 151.656 1.00 84.36  ? 2923 ASP A OD1   1 
ATOM   11672 O  OD2   . ASP A 1 2923 ? 123.397 157.670 153.310 1.00 75.07  ? 2923 ASP A OD2   1 
ATOM   11673 N  N     . ARG A 1 2924 ? 126.190 158.577 156.098 1.00 65.15  ? 2924 ARG A N     1 
ATOM   11674 C  CA    . ARG A 1 2924 ? 125.780 159.531 157.123 1.00 63.53  ? 2924 ARG A CA    1 
ATOM   11675 C  C     . ARG A 1 2924 ? 126.719 160.727 157.159 1.00 64.44  ? 2924 ARG A C     1 
ATOM   11676 O  O     . ARG A 1 2924 ? 126.277 161.879 157.235 1.00 66.40  ? 2924 ARG A O     1 
ATOM   11677 C  CB    . ARG A 1 2924 ? 125.746 158.851 158.491 1.00 61.96  ? 2924 ARG A CB    1 
ATOM   11678 C  CG    . ARG A 1 2924 ? 124.425 158.211 158.852 1.00 65.57  ? 2924 ARG A CG    1 
ATOM   11679 C  CD    . ARG A 1 2924 ? 124.476 157.653 160.263 1.00 65.35  ? 2924 ARG A CD    1 
ATOM   11680 N  NE    . ARG A 1 2924 ? 125.347 158.446 161.124 1.00 65.60  ? 2924 ARG A NE    1 
ATOM   11681 C  CZ    . ARG A 1 2924 ? 124.919 159.234 162.100 1.00 69.27  ? 2924 ARG A CZ    1 
ATOM   11682 N  NH1   . ARG A 1 2924 ? 123.631 159.361 162.371 1.00 64.92  ? 2924 ARG A NH1   1 
ATOM   11683 N  NH2   . ARG A 1 2924 ? 125.806 159.914 162.820 1.00 70.55  ? 2924 ARG A NH2   1 
ATOM   11684 N  N     . ILE A 1 2925 ? 128.025 160.469 157.109 1.00 67.79  ? 2925 ILE A N     1 
ATOM   11685 C  CA    . ILE A 1 2925 ? 128.989 161.562 157.199 1.00 65.29  ? 2925 ILE A CA    1 
ATOM   11686 C  C     . ILE A 1 2925 ? 128.945 162.428 155.944 1.00 67.55  ? 2925 ILE A C     1 
ATOM   11687 O  O     . ILE A 1 2925 ? 129.047 163.658 156.021 1.00 65.91  ? 2925 ILE A O     1 
ATOM   11688 C  CB    . ILE A 1 2925 ? 130.402 161.015 157.462 1.00 58.35  ? 2925 ILE A CB    1 
ATOM   11689 C  CG1   . ILE A 1 2925 ? 130.435 160.253 158.786 1.00 68.09  ? 2925 ILE A CG1   1 
ATOM   11690 C  CG2   . ILE A 1 2925 ? 131.407 162.149 157.497 1.00 60.63  ? 2925 ILE A CG2   1 
ATOM   11691 C  CD1   . ILE A 1 2925 ? 129.818 161.010 159.938 1.00 66.82  ? 2925 ILE A CD1   1 
ATOM   11692 N  N     . PHE A 1 2926 ? 128.785 161.808 154.773 1.00 69.70  ? 2926 PHE A N     1 
ATOM   11693 C  CA    . PHE A 1 2926 ? 128.857 162.548 153.517 1.00 67.02  ? 2926 PHE A CA    1 
ATOM   11694 C  C     . PHE A 1 2926 ? 127.695 163.514 153.327 1.00 70.46  ? 2926 PHE A C     1 
ATOM   11695 O  O     . PHE A 1 2926 ? 127.838 164.490 152.584 1.00 72.34  ? 2926 PHE A O     1 
ATOM   11696 C  CB    . PHE A 1 2926 ? 128.913 161.577 152.337 1.00 60.18  ? 2926 PHE A CB    1 
ATOM   11697 C  CG    . PHE A 1 2926 ? 130.296 161.096 152.014 1.00 60.66  ? 2926 PHE A CG    1 
ATOM   11698 C  CD1   . PHE A 1 2926 ? 131.400 161.649 152.637 1.00 66.77  ? 2926 PHE A CD1   1 
ATOM   11699 C  CD2   . PHE A 1 2926 ? 130.493 160.091 151.084 1.00 63.59  ? 2926 PHE A CD2   1 
ATOM   11700 C  CE1   . PHE A 1 2926 ? 132.673 161.209 152.340 1.00 66.30  ? 2926 PHE A CE1   1 
ATOM   11701 C  CE2   . PHE A 1 2926 ? 131.764 159.647 150.783 1.00 63.33  ? 2926 PHE A CE2   1 
ATOM   11702 C  CZ    . PHE A 1 2926 ? 132.855 160.206 151.412 1.00 61.91  ? 2926 PHE A CZ    1 
ATOM   11703 N  N     . ARG A 1 2927 ? 126.558 163.273 153.972 1.00 73.01  ? 2927 ARG A N     1 
ATOM   11704 C  CA    . ARG A 1 2927 ? 125.392 164.132 153.813 1.00 68.41  ? 2927 ARG A CA    1 
ATOM   11705 C  C     . ARG A 1 2927 ? 125.433 165.363 154.707 1.00 74.08  ? 2927 ARG A C     1 
ATOM   11706 O  O     . ARG A 1 2927 ? 124.585 166.247 154.558 1.00 75.93  ? 2927 ARG A O     1 
ATOM   11707 C  CB    . ARG A 1 2927 ? 124.111 163.341 154.093 1.00 67.44  ? 2927 ARG A CB    1 
ATOM   11708 C  CG    . ARG A 1 2927 ? 123.696 162.405 152.971 1.00 69.16  ? 2927 ARG A CG    1 
ATOM   11709 C  CD    . ARG A 1 2927 ? 122.386 161.707 153.296 1.00 76.26  ? 2927 ARG A CD    1 
ATOM   11710 N  NE    . ARG A 1 2927 ? 122.510 160.817 154.443 1.00 82.10  ? 2927 ARG A NE    1 
ATOM   11711 C  CZ    . ARG A 1 2927 ? 121.992 161.059 155.639 1.00 77.99  ? 2927 ARG A CZ    1 
ATOM   11712 N  NH1   . ARG A 1 2927 ? 121.303 162.162 155.884 1.00 75.19  ? 2927 ARG A NH1   1 
ATOM   11713 N  NH2   . ARG A 1 2927 ? 122.170 160.174 156.615 1.00 71.03  ? 2927 ARG A NH2   1 
ATOM   11714 N  N     . GLN A 1 2928 ? 126.394 165.446 155.622 1.00 77.01  ? 2928 GLN A N     1 
ATOM   11715 C  CA    . GLN A 1 2928 ? 126.493 166.555 156.556 1.00 76.19  ? 2928 GLN A CA    1 
ATOM   11716 C  C     . GLN A 1 2928 ? 127.373 167.662 155.991 1.00 73.87  ? 2928 GLN A C     1 
ATOM   11717 O  O     . GLN A 1 2928 ? 128.309 167.395 155.232 1.00 76.33  ? 2928 GLN A O     1 
ATOM   11718 C  CB    . GLN A 1 2928 ? 127.078 166.084 157.890 1.00 69.76  ? 2928 GLN A CB    1 
ATOM   11719 C  CG    . GLN A 1 2928 ? 126.097 165.351 158.782 1.00 74.14  ? 2928 GLN A CG    1 
ATOM   11720 C  CD    . GLN A 1 2928 ? 126.717 164.935 160.099 1.00 81.23  ? 2928 GLN A CD    1 
ATOM   11721 O  OE1   . GLN A 1 2928 ? 127.837 165.331 160.423 1.00 76.21  ? 2928 GLN A OE1   1 
ATOM   11722 N  NE2   . GLN A 1 2928 ? 125.993 164.130 160.867 1.00 82.03  ? 2928 GLN A NE2   1 
ATOM   11723 N  N     . PRO A 1 2929 ? 127.096 168.917 156.340 1.00 73.57  ? 2929 PRO A N     1 
ATOM   11724 C  CA    . PRO A 1 2929 ? 127.995 170.002 155.935 1.00 72.27  ? 2929 PRO A CA    1 
ATOM   11725 C  C     . PRO A 1 2929 ? 129.292 169.949 156.725 1.00 73.31  ? 2929 PRO A C     1 
ATOM   11726 O  O     . PRO A 1 2929 ? 129.292 169.725 157.938 1.00 75.79  ? 2929 PRO A O     1 
ATOM   11727 C  CB    . PRO A 1 2929 ? 127.192 171.267 156.253 1.00 75.99  ? 2929 PRO A CB    1 
ATOM   11728 C  CG    . PRO A 1 2929 ? 126.276 170.853 157.353 1.00 82.29  ? 2929 PRO A CG    1 
ATOM   11729 C  CD    . PRO A 1 2929 ? 125.929 169.413 157.090 1.00 80.87  ? 2929 PRO A CD    1 
ATOM   11730 N  N     . GLN A 1 2930 ? 130.404 170.162 156.020 1.00 69.26  ? 2930 GLN A N     1 
ATOM   11731 C  CA    . GLN A 1 2930 ? 131.741 170.049 156.602 1.00 68.64  ? 2930 GLN A CA    1 
ATOM   11732 C  C     . GLN A 1 2930 ? 131.938 168.683 157.256 1.00 73.76  ? 2930 GLN A C     1 
ATOM   11733 O  O     . GLN A 1 2930 ? 132.521 168.561 158.335 1.00 68.99  ? 2930 GLN A O     1 
ATOM   11734 C  CB    . GLN A 1 2930 ? 132.007 171.177 157.601 1.00 67.57  ? 2930 GLN A CB    1 
ATOM   11735 C  CG    . GLN A 1 2930 ? 133.469 171.575 157.708 1.00 68.99  ? 2930 GLN A CG    1 
ATOM   11736 C  CD    . GLN A 1 2930 ? 133.684 172.760 158.625 1.00 72.69  ? 2930 GLN A CD    1 
ATOM   11737 O  OE1   . GLN A 1 2930 ? 132.742 173.268 159.232 1.00 73.92  ? 2930 GLN A OE1   1 
ATOM   11738 N  NE2   . GLN A 1 2930 ? 134.929 173.207 158.732 1.00 71.57  ? 2930 GLN A NE2   1 
ATOM   11739 N  N     . GLY A 1 2931 ? 131.441 167.643 156.592 1.00 76.08  ? 2931 GLY A N     1 
ATOM   11740 C  CA    . GLY A 1 2931 ? 131.551 166.293 157.106 1.00 73.53  ? 2931 GLY A CA    1 
ATOM   11741 C  C     . GLY A 1 2931 ? 132.803 165.587 156.634 1.00 69.37  ? 2931 GLY A C     1 
ATOM   11742 O  O     . GLY A 1 2931 ? 132.872 165.126 155.491 1.00 66.04  ? 2931 GLY A O     1 
ATOM   11743 N  N     . HIS A 1 2932 ? 133.799 165.493 157.507 1.00 60.59  ? 2932 HIS A N     1 
ATOM   11744 C  CA    . HIS A 1 2932 ? 135.077 164.881 157.185 1.00 56.16  ? 2932 HIS A CA    1 
ATOM   11745 C  C     . HIS A 1 2932 ? 135.222 163.559 157.924 1.00 58.59  ? 2932 HIS A C     1 
ATOM   11746 O  O     . HIS A 1 2932 ? 134.725 163.394 159.041 1.00 68.26  ? 2932 HIS A O     1 
ATOM   11747 C  CB    . HIS A 1 2932 ? 136.234 165.814 157.545 1.00 58.99  ? 2932 HIS A CB    1 
ATOM   11748 C  CG    . HIS A 1 2932 ? 136.074 167.204 157.014 1.00 56.87  ? 2932 HIS A CG    1 
ATOM   11749 N  ND1   . HIS A 1 2932 ? 136.076 167.490 155.666 1.00 64.35  ? 2932 HIS A ND1   1 
ATOM   11750 C  CD2   . HIS A 1 2932 ? 135.909 168.387 157.649 1.00 61.94  ? 2932 HIS A CD2   1 
ATOM   11751 C  CE1   . HIS A 1 2932 ? 135.918 168.790 155.493 1.00 64.12  ? 2932 HIS A CE1   1 
ATOM   11752 N  NE2   . HIS A 1 2932 ? 135.815 169.357 156.681 1.00 66.24  ? 2932 HIS A NE2   1 
ATOM   11753 N  N     . LEU A 1 2933 ? 135.914 162.616 157.291 1.00 46.11  ? 2933 LEU A N     1 
ATOM   11754 C  CA    . LEU A 1 2933 ? 136.046 161.263 157.804 1.00 42.32  ? 2933 LEU A CA    1 
ATOM   11755 C  C     . LEU A 1 2933 ? 137.496 160.962 158.157 1.00 51.06  ? 2933 LEU A C     1 
ATOM   11756 O  O     . LEU A 1 2933 ? 138.427 161.479 157.533 1.00 66.27  ? 2933 LEU A O     1 
ATOM   11757 C  CB    . LEU A 1 2933 ? 135.548 160.235 156.787 1.00 40.02  ? 2933 LEU A CB    1 
ATOM   11758 C  CG    . LEU A 1 2933 ? 134.085 159.820 156.912 1.00 52.75  ? 2933 LEU A CG    1 
ATOM   11759 C  CD1   . LEU A 1 2933 ? 133.627 159.107 155.654 1.00 61.11  ? 2933 LEU A CD1   1 
ATOM   11760 C  CD2   . LEU A 1 2933 ? 133.887 158.946 158.132 1.00 53.82  ? 2933 LEU A CD2   1 
ATOM   11761 N  N     . LEU A 1 2934 ? 137.674 160.116 159.170 1.00 48.57  ? 2934 LEU A N     1 
ATOM   11762 C  CA    . LEU A 1 2934 ? 138.982 159.601 159.573 1.00 44.79  ? 2934 LEU A CA    1 
ATOM   11763 C  C     . LEU A 1 2934 ? 138.827 158.090 159.712 1.00 54.10  ? 2934 LEU A C     1 
ATOM   11764 O  O     . LEU A 1 2934 ? 138.485 157.587 160.785 1.00 62.83  ? 2934 LEU A O     1 
ATOM   11765 C  CB    . LEU A 1 2934 ? 139.465 160.247 160.866 1.00 51.22  ? 2934 LEU A CB    1 
ATOM   11766 C  CG    . LEU A 1 2934 ? 140.805 159.749 161.408 1.00 44.58  ? 2934 LEU A CG    1 
ATOM   11767 C  CD1   . LEU A 1 2934 ? 141.905 159.960 160.384 1.00 48.72  ? 2934 LEU A CD1   1 
ATOM   11768 C  CD2   . LEU A 1 2934 ? 141.146 160.442 162.713 1.00 56.18  ? 2934 LEU A CD2   1 
ATOM   11769 N  N     . LEU A 1 2935 ? 139.072 157.369 158.622 1.00 59.79  ? 2935 LEU A N     1 
ATOM   11770 C  CA    . LEU A 1 2935 ? 138.900 155.921 158.590 1.00 53.98  ? 2935 LEU A CA    1 
ATOM   11771 C  C     . LEU A 1 2935 ? 140.193 155.265 159.055 1.00 60.80  ? 2935 LEU A C     1 
ATOM   11772 O  O     . LEU A 1 2935 ? 141.216 155.336 158.367 1.00 71.14  ? 2935 LEU A O     1 
ATOM   11773 C  CB    . LEU A 1 2935 ? 138.521 155.455 157.187 1.00 49.25  ? 2935 LEU A CB    1 
ATOM   11774 C  CG    . LEU A 1 2935 ? 137.328 156.158 156.541 1.00 51.95  ? 2935 LEU A CG    1 
ATOM   11775 C  CD1   . LEU A 1 2935 ? 137.015 155.539 155.193 1.00 51.92  ? 2935 LEU A CD1   1 
ATOM   11776 C  CD2   . LEU A 1 2935 ? 136.120 156.090 157.455 1.00 56.72  ? 2935 LEU A CD2   1 
ATOM   11777 N  N     . ILE A 1 2936 ? 140.149 154.624 160.218 1.00 59.16  ? 2936 ILE A N     1 
ATOM   11778 C  CA    . ILE A 1 2936 ? 141.308 153.958 160.799 1.00 53.47  ? 2936 ILE A CA    1 
ATOM   11779 C  C     . ILE A 1 2936 ? 141.081 152.457 160.708 1.00 64.04  ? 2936 ILE A C     1 
ATOM   11780 O  O     . ILE A 1 2936 ? 140.059 151.945 161.181 1.00 75.05  ? 2936 ILE A O     1 
ATOM   11781 C  CB    . ILE A 1 2936 ? 141.547 154.395 162.250 1.00 55.38  ? 2936 ILE A CB    1 
ATOM   11782 C  CG1   . ILE A 1 2936 ? 141.656 155.917 162.334 1.00 55.89  ? 2936 ILE A CG1   1 
ATOM   11783 C  CG2   . ILE A 1 2936 ? 142.801 153.744 162.801 1.00 55.65  ? 2936 ILE A CG2   1 
ATOM   11784 C  CD1   . ILE A 1 2936 ? 141.879 156.429 163.734 1.00 64.49  ? 2936 ILE A CD1   1 
ATOM   11785 N  N     . GLY A 1 2937 ? 142.028 151.758 160.101 1.00 61.58  ? 2937 GLY A N     1 
ATOM   11786 C  CA    . GLY A 1 2937 ? 141.929 150.318 159.960 1.00 57.37  ? 2937 GLY A CA    1 
ATOM   11787 C  C     . GLY A 1 2937 ? 143.111 149.804 159.173 1.00 62.53  ? 2937 GLY A C     1 
ATOM   11788 O  O     . GLY A 1 2937 ? 143.858 150.570 158.554 1.00 63.02  ? 2937 GLY A O     1 
ATOM   11789 N  N     . VAL A 1 2938 ? 143.274 148.481 159.209 1.00 67.22  ? 2938 VAL A N     1 
ATOM   11790 C  CA    . VAL A 1 2938 ? 144.385 147.850 158.510 1.00 63.46  ? 2938 VAL A CA    1 
ATOM   11791 C  C     . VAL A 1 2938 ? 144.220 148.046 157.010 1.00 64.42  ? 2938 VAL A C     1 
ATOM   11792 O  O     . VAL A 1 2938 ? 143.099 148.173 156.498 1.00 69.63  ? 2938 VAL A O     1 
ATOM   11793 C  CB    . VAL A 1 2938 ? 144.481 146.361 158.884 1.00 58.64  ? 2938 VAL A CB    1 
ATOM   11794 C  CG1   . VAL A 1 2938 ? 143.468 145.541 158.104 1.00 55.38  ? 2938 VAL A CG1   1 
ATOM   11795 C  CG2   . VAL A 1 2938 ? 145.892 145.842 158.650 1.00 64.57  ? 2938 VAL A CG2   1 
ATOM   11796 N  N     . SER A 1 2939 ? 145.344 148.103 156.300 1.00 63.46  ? 2939 SER A N     1 
ATOM   11797 C  CA    . SER A 1 2939 ? 145.304 148.307 154.859 1.00 62.46  ? 2939 SER A CA    1 
ATOM   11798 C  C     . SER A 1 2939 ? 144.676 147.104 154.170 1.00 67.26  ? 2939 SER A C     1 
ATOM   11799 O  O     . SER A 1 2939 ? 144.761 145.974 154.657 1.00 68.26  ? 2939 SER A O     1 
ATOM   11800 C  CB    . SER A 1 2939 ? 146.713 148.552 154.322 1.00 62.58  ? 2939 SER A CB    1 
ATOM   11801 O  OG    . SER A 1 2939 ? 147.294 149.690 154.935 1.00 67.07  ? 2939 SER A OG    1 
ATOM   11802 N  N     . GLY A 1 2940 ? 144.027 147.353 153.037 1.00 70.60  ? 2940 GLY A N     1 
ATOM   11803 C  CA    . GLY A 1 2940 ? 143.346 146.295 152.322 1.00 65.95  ? 2940 GLY A CA    1 
ATOM   11804 C  C     . GLY A 1 2940 ? 141.968 145.958 152.840 1.00 65.44  ? 2940 GLY A C     1 
ATOM   11805 O  O     . GLY A 1 2940 ? 141.360 144.997 152.354 1.00 67.73  ? 2940 GLY A O     1 
ATOM   11806 N  N     . ALA A 1 2941 ? 141.453 146.714 153.808 1.00 59.82  ? 2941 ALA A N     1 
ATOM   11807 C  CA    . ALA A 1 2941 ? 140.135 146.452 154.368 1.00 64.45  ? 2941 ALA A CA    1 
ATOM   11808 C  C     . ALA A 1 2941 ? 139.006 147.053 153.543 1.00 68.65  ? 2941 ALA A C     1 
ATOM   11809 O  O     . ALA A 1 2941 ? 137.837 146.860 153.892 1.00 67.46  ? 2941 ALA A O     1 
ATOM   11810 C  CB    . ALA A 1 2941 ? 140.056 146.982 155.802 1.00 66.01  ? 2941 ALA A CB    1 
ATOM   11811 N  N     . GLY A 1 2942 ? 139.320 147.771 152.470 1.00 65.75  ? 2942 GLY A N     1 
ATOM   11812 C  CA    . GLY A 1 2942 ? 138.308 148.364 151.625 1.00 61.96  ? 2942 GLY A CA    1 
ATOM   11813 C  C     . GLY A 1 2942 ? 137.910 149.780 151.970 1.00 67.24  ? 2942 GLY A C     1 
ATOM   11814 O  O     . GLY A 1 2942 ? 136.867 150.239 151.495 1.00 74.44  ? 2942 GLY A O     1 
ATOM   11815 N  N     . LYS A 1 2943 ? 138.701 150.485 152.782 1.00 61.73  ? 2943 LYS A N     1 
ATOM   11816 C  CA    . LYS A 1 2943 ? 138.333 151.838 153.187 1.00 56.59  ? 2943 LYS A CA    1 
ATOM   11817 C  C     . LYS A 1 2943 ? 138.236 152.768 151.984 1.00 62.27  ? 2943 LYS A C     1 
ATOM   11818 O  O     . LYS A 1 2943 ? 137.231 153.465 151.803 1.00 72.35  ? 2943 LYS A O     1 
ATOM   11819 C  CB    . LYS A 1 2943 ? 139.347 152.368 154.201 1.00 60.37  ? 2943 LYS A CB    1 
ATOM   11820 C  CG    . LYS A 1 2943 ? 139.705 151.373 155.292 1.00 63.10  ? 2943 LYS A CG    1 
ATOM   11821 C  CD    . LYS A 1 2943 ? 140.571 152.013 156.359 1.00 63.43  ? 2943 LYS A CD    1 
ATOM   11822 C  CE    . LYS A 1 2943 ? 141.954 152.331 155.822 1.00 64.53  ? 2943 LYS A CE    1 
ATOM   11823 N  NZ    . LYS A 1 2943 ? 142.698 151.094 155.467 1.00 61.40  ? 2943 LYS A NZ    1 
ATOM   11824 N  N     . THR A 1 2944 ? 139.273 152.788 151.145 1.00 56.87  ? 2944 THR A N     1 
ATOM   11825 C  CA    . THR A 1 2944 ? 139.256 153.652 149.969 1.00 49.27  ? 2944 THR A CA    1 
ATOM   11826 C  C     . THR A 1 2944 ? 138.163 153.237 148.991 1.00 61.34  ? 2944 THR A C     1 
ATOM   11827 O  O     . THR A 1 2944 ? 137.459 154.091 148.438 1.00 72.32  ? 2944 THR A O     1 
ATOM   11828 C  CB    . THR A 1 2944 ? 140.622 153.637 149.283 1.00 49.99  ? 2944 THR A CB    1 
ATOM   11829 O  OG1   . THR A 1 2944 ? 141.624 154.082 150.205 1.00 61.10  ? 2944 THR A OG1   1 
ATOM   11830 C  CG2   . THR A 1 2944 ? 140.620 154.550 148.069 1.00 52.23  ? 2944 THR A CG2   1 
ATOM   11831 N  N     . THR A 1 2945 ? 138.007 151.931 148.764 1.00 65.92  ? 2945 THR A N     1 
ATOM   11832 C  CA    . THR A 1 2945 ? 136.983 151.460 147.837 1.00 57.52  ? 2945 THR A CA    1 
ATOM   11833 C  C     . THR A 1 2945 ? 135.584 151.792 148.340 1.00 63.43  ? 2945 THR A C     1 
ATOM   11834 O  O     . THR A 1 2945 ? 134.731 152.236 147.564 1.00 76.73  ? 2945 THR A O     1 
ATOM   11835 C  CB    . THR A 1 2945 ? 137.126 149.957 147.611 1.00 57.38  ? 2945 THR A CB    1 
ATOM   11836 O  OG1   . THR A 1 2945 ? 138.508 149.635 147.412 1.00 68.19  ? 2945 THR A OG1   1 
ATOM   11837 C  CG2   . THR A 1 2945 ? 136.332 149.529 146.390 1.00 59.93  ? 2945 THR A CG2   1 
ATOM   11838 N  N     . LEU A 1 2946 ? 135.329 151.589 149.635 1.00 50.40  ? 2946 LEU A N     1 
ATOM   11839 C  CA    . LEU A 1 2946 ? 134.023 151.931 150.189 1.00 54.13  ? 2946 LEU A CA    1 
ATOM   11840 C  C     . LEU A 1 2946 ? 133.771 153.431 150.127 1.00 59.43  ? 2946 LEU A C     1 
ATOM   11841 O  O     . LEU A 1 2946 ? 132.646 153.867 149.854 1.00 65.69  ? 2946 LEU A O     1 
ATOM   11842 C  CB    . LEU A 1 2946 ? 133.908 151.427 151.627 1.00 52.33  ? 2946 LEU A CB    1 
ATOM   11843 C  CG    . LEU A 1 2946 ? 133.652 149.930 151.801 1.00 54.07  ? 2946 LEU A CG    1 
ATOM   11844 C  CD1   . LEU A 1 2946 ? 133.142 149.638 153.201 1.00 63.70  ? 2946 LEU A CD1   1 
ATOM   11845 C  CD2   . LEU A 1 2946 ? 132.676 149.425 150.753 1.00 52.60  ? 2946 LEU A CD2   1 
ATOM   11846 N  N     . SER A 1 2947 ? 134.803 154.238 150.392 1.00 51.36  ? 2947 SER A N     1 
ATOM   11847 C  CA    . SER A 1 2947 ? 134.649 155.684 150.286 1.00 50.06  ? 2947 SER A CA    1 
ATOM   11848 C  C     . SER A 1 2947 ? 134.292 156.094 148.865 1.00 61.94  ? 2947 SER A C     1 
ATOM   11849 O  O     . SER A 1 2947 ? 133.385 156.908 148.656 1.00 75.02  ? 2947 SER A O     1 
ATOM   11850 C  CB    . SER A 1 2947 ? 135.928 156.383 150.741 1.00 47.76  ? 2947 SER A CB    1 
ATOM   11851 O  OG    . SER A 1 2947 ? 136.298 155.969 152.043 1.00 56.90  ? 2947 SER A OG    1 
ATOM   11852 N  N     . ARG A 1 2948 ? 134.985 155.529 147.873 1.00 60.37  ? 2948 ARG A N     1 
ATOM   11853 C  CA    . ARG A 1 2948 ? 134.667 155.832 146.480 1.00 57.63  ? 2948 ARG A CA    1 
ATOM   11854 C  C     . ARG A 1 2948 ? 133.254 155.386 146.130 1.00 61.00  ? 2948 ARG A C     1 
ATOM   11855 O  O     . ARG A 1 2948 ? 132.532 156.087 145.417 1.00 67.46  ? 2948 ARG A O     1 
ATOM   11856 C  CB    . ARG A 1 2948 ? 135.680 155.164 145.552 1.00 50.72  ? 2948 ARG A CB    1 
ATOM   11857 C  CG    . ARG A 1 2948 ? 137.089 155.707 145.674 1.00 56.18  ? 2948 ARG A CG    1 
ATOM   11858 C  CD    . ARG A 1 2948 ? 138.056 154.930 144.800 1.00 63.49  ? 2948 ARG A CD    1 
ATOM   11859 N  NE    . ARG A 1 2948 ? 137.876 155.227 143.384 1.00 73.22  ? 2948 ARG A NE    1 
ATOM   11860 C  CZ    . ARG A 1 2948 ? 138.825 155.095 142.467 1.00 73.04  ? 2948 ARG A CZ    1 
ATOM   11861 N  NH1   . ARG A 1 2948 ? 140.038 154.675 142.784 1.00 66.95  ? 2948 ARG A NH1   1 
ATOM   11862 N  NH2   . ARG A 1 2948 ? 138.549 155.392 141.201 1.00 70.52  ? 2948 ARG A NH2   1 
ATOM   11863 N  N     . PHE A 1 2949 ? 132.846 154.221 146.632 1.00 55.42  ? 2949 PHE A N     1 
ATOM   11864 C  CA    . PHE A 1 2949 ? 131.522 153.683 146.337 1.00 62.69  ? 2949 PHE A CA    1 
ATOM   11865 C  C     . PHE A 1 2949 ? 130.426 154.592 146.887 1.00 74.42  ? 2949 PHE A C     1 
ATOM   11866 O  O     . PHE A 1 2949 ? 129.489 154.971 146.165 1.00 84.89  ? 2949 PHE A O     1 
ATOM   11867 C  CB    . PHE A 1 2949 ? 131.450 152.274 146.931 1.00 62.21  ? 2949 PHE A CB    1 
ATOM   11868 C  CG    . PHE A 1 2949 ? 130.133 151.582 146.770 1.00 64.82  ? 2949 PHE A CG    1 
ATOM   11869 C  CD1   . PHE A 1 2949 ? 129.566 151.416 145.521 1.00 74.44  ? 2949 PHE A CD1   1 
ATOM   11870 C  CD2   . PHE A 1 2949 ? 129.500 151.025 147.868 1.00 62.62  ? 2949 PHE A CD2   1 
ATOM   11871 C  CE1   . PHE A 1 2949 ? 128.369 150.747 145.375 1.00 76.28  ? 2949 PHE A CE1   1 
ATOM   11872 C  CE2   . PHE A 1 2949 ? 128.307 150.353 147.729 1.00 66.78  ? 2949 PHE A CE2   1 
ATOM   11873 C  CZ    . PHE A 1 2949 ? 127.743 150.207 146.480 1.00 73.27  ? 2949 PHE A CZ    1 
ATOM   11874 N  N     . VAL A 1 2950 ? 130.551 154.989 148.154 1.00 65.72  ? 2950 VAL A N     1 
ATOM   11875 C  CA    . VAL A 1 2950 ? 129.558 155.866 148.765 1.00 59.48  ? 2950 VAL A CA    1 
ATOM   11876 C  C     . VAL A 1 2950 ? 129.568 157.238 148.101 1.00 63.55  ? 2950 VAL A C     1 
ATOM   11877 O  O     . VAL A 1 2950 ? 128.509 157.836 147.871 1.00 73.06  ? 2950 VAL A O     1 
ATOM   11878 C  CB    . VAL A 1 2950 ? 129.796 155.964 150.282 1.00 56.76  ? 2950 VAL A CB    1 
ATOM   11879 C  CG1   . VAL A 1 2950 ? 128.835 156.957 150.902 1.00 64.60  ? 2950 VAL A CG1   1 
ATOM   11880 C  CG2   . VAL A 1 2950 ? 129.643 154.600 150.927 1.00 63.93  ? 2950 VAL A CG2   1 
ATOM   11881 N  N     . ALA A 1 2951 ? 130.756 157.763 147.786 1.00 58.96  ? 2951 ALA A N     1 
ATOM   11882 C  CA    . ALA A 1 2951 ? 130.839 159.059 147.123 1.00 51.55  ? 2951 ALA A CA    1 
ATOM   11883 C  C     . ALA A 1 2951 ? 130.187 159.017 145.749 1.00 60.41  ? 2951 ALA A C     1 
ATOM   11884 O  O     . ALA A 1 2951 ? 129.531 159.980 145.336 1.00 66.39  ? 2951 ALA A O     1 
ATOM   11885 C  CB    . ALA A 1 2951 ? 132.298 159.499 147.014 1.00 53.57  ? 2951 ALA A CB    1 
ATOM   11886 N  N     . TRP A 1 2952 ? 130.363 157.912 145.020 1.00 68.60  ? 2952 TRP A N     1 
ATOM   11887 C  CA    . TRP A 1 2952 ? 129.704 157.768 143.728 1.00 71.47  ? 2952 TRP A CA    1 
ATOM   11888 C  C     . TRP A 1 2952 ? 128.192 157.725 143.892 1.00 72.24  ? 2952 TRP A C     1 
ATOM   11889 O  O     . TRP A 1 2952 ? 127.458 158.281 143.067 1.00 72.05  ? 2952 TRP A O     1 
ATOM   11890 C  CB    . TRP A 1 2952 ? 130.200 156.514 143.011 1.00 70.88  ? 2952 TRP A CB    1 
ATOM   11891 C  CG    . TRP A 1 2952 ? 129.343 156.129 141.845 1.00 72.49  ? 2952 TRP A CG    1 
ATOM   11892 C  CD1   . TRP A 1 2952 ? 129.422 156.621 140.576 1.00 72.09  ? 2952 TRP A CD1   1 
ATOM   11893 C  CD2   . TRP A 1 2952 ? 128.274 155.176 141.839 1.00 73.36  ? 2952 TRP A CD2   1 
ATOM   11894 N  NE1   . TRP A 1 2952 ? 128.471 156.034 139.780 1.00 69.01  ? 2952 TRP A NE1   1 
ATOM   11895 C  CE2   . TRP A 1 2952 ? 127.752 155.143 140.531 1.00 69.66  ? 2952 TRP A CE2   1 
ATOM   11896 C  CE3   . TRP A 1 2952 ? 127.707 154.348 142.812 1.00 70.84  ? 2952 TRP A CE3   1 
ATOM   11897 C  CZ2   . TRP A 1 2952 ? 126.693 154.315 140.172 1.00 66.96  ? 2952 TRP A CZ2   1 
ATOM   11898 C  CZ3   . TRP A 1 2952 ? 126.656 153.527 142.453 1.00 73.84  ? 2952 TRP A CZ3   1 
ATOM   11899 C  CH2   . TRP A 1 2952 ? 126.160 153.517 141.144 1.00 71.77  ? 2952 TRP A CH2   1 
ATOM   11900 N  N     . MET A 1 2953 ? 127.704 157.056 144.941 1.00 67.50  ? 2953 MET A N     1 
ATOM   11901 C  CA    . MET A 1 2953 ? 126.270 157.121 145.217 1.00 70.76  ? 2953 MET A CA    1 
ATOM   11902 C  C     . MET A 1 2953 ? 125.812 158.554 145.448 1.00 75.79  ? 2953 MET A C     1 
ATOM   11903 O  O     . MET A 1 2953 ? 124.864 159.023 144.808 1.00 77.32  ? 2953 MET A O     1 
ATOM   11904 C  CB    . MET A 1 2953 ? 125.892 156.276 146.429 1.00 66.91  ? 2953 MET A CB    1 
ATOM   11905 C  CG    . MET A 1 2953 ? 124.891 155.189 146.117 1.00 75.29  ? 2953 MET A CG    1 
ATOM   11906 S  SD    . MET A 1 2953 ? 124.784 153.994 147.448 1.00 101.45 ? 2953 MET A SD    1 
ATOM   11907 C  CE    . MET A 1 2953 ? 126.185 152.990 147.045 1.00 76.37  ? 2953 MET A CE    1 
ATOM   11908 N  N     . ASN A 1 2954 ? 126.477 159.267 146.352 1.00 72.18  ? 2954 ASN A N     1 
ATOM   11909 C  CA    . ASN A 1 2954 ? 126.028 160.583 146.784 1.00 69.99  ? 2954 ASN A CA    1 
ATOM   11910 C  C     . ASN A 1 2954 ? 126.369 161.689 145.795 1.00 71.29  ? 2954 ASN A C     1 
ATOM   11911 O  O     . ASN A 1 2954 ? 126.135 162.863 146.100 1.00 75.51  ? 2954 ASN A O     1 
ATOM   11912 C  CB    . ASN A 1 2954 ? 126.622 160.915 148.155 1.00 71.20  ? 2954 ASN A CB    1 
ATOM   11913 C  CG    . ASN A 1 2954 ? 125.920 160.189 149.283 1.00 72.29  ? 2954 ASN A CG    1 
ATOM   11914 O  OD1   . ASN A 1 2954 ? 124.850 160.599 149.730 1.00 79.44  ? 2954 ASN A OD1   1 
ATOM   11915 N  ND2   . ASN A 1 2954 ? 126.518 159.100 149.748 1.00 68.57  ? 2954 ASN A ND2   1 
ATOM   11916 N  N     . GLY A 1 2955 ? 126.915 161.351 144.630 1.00 65.69  ? 2955 GLY A N     1 
ATOM   11917 C  CA    . GLY A 1 2955 ? 127.226 162.339 143.620 1.00 62.61  ? 2955 GLY A CA    1 
ATOM   11918 C  C     . GLY A 1 2955 ? 128.556 163.037 143.785 1.00 64.40  ? 2955 GLY A C     1 
ATOM   11919 O  O     . GLY A 1 2955 ? 128.914 163.856 142.929 1.00 72.20  ? 2955 GLY A O     1 
ATOM   11920 N  N     . LEU A 1 2956 ? 129.296 162.750 144.851 1.00 62.97  ? 2956 LEU A N     1 
ATOM   11921 C  CA    . LEU A 1 2956 ? 130.584 163.389 145.073 1.00 63.52  ? 2956 LEU A CA    1 
ATOM   11922 C  C     . LEU A 1 2956 ? 131.600 162.914 144.044 1.00 65.26  ? 2956 LEU A C     1 
ATOM   11923 O  O     . LEU A 1 2956 ? 131.586 161.754 143.623 1.00 67.82  ? 2956 LEU A O     1 
ATOM   11924 C  CB    . LEU A 1 2956 ? 131.096 163.095 146.483 1.00 60.11  ? 2956 LEU A CB    1 
ATOM   11925 C  CG    . LEU A 1 2956 ? 130.093 163.105 147.638 1.00 63.38  ? 2956 LEU A CG    1 
ATOM   11926 C  CD1   . LEU A 1 2956 ? 130.816 162.917 148.958 1.00 66.79  ? 2956 LEU A CD1   1 
ATOM   11927 C  CD2   . LEU A 1 2956 ? 129.289 164.393 147.658 1.00 66.07  ? 2956 LEU A CD2   1 
ATOM   11928 N  N     . SER A 1 2957 ? 132.483 163.820 143.638 1.00 71.16  ? 2957 SER A N     1 
ATOM   11929 C  CA    . SER A 1 2957 ? 133.567 163.488 142.726 1.00 69.04  ? 2957 SER A CA    1 
ATOM   11930 C  C     . SER A 1 2957 ? 134.812 163.141 143.532 1.00 68.83  ? 2957 SER A C     1 
ATOM   11931 O  O     . SER A 1 2957 ? 135.314 163.969 144.297 1.00 80.24  ? 2957 SER A O     1 
ATOM   11932 C  CB    . SER A 1 2957 ? 133.852 164.651 141.777 1.00 74.65  ? 2957 SER A CB    1 
ATOM   11933 O  OG    . SER A 1 2957 ? 132.660 165.113 141.166 1.00 75.21  ? 2957 SER A OG    1 
ATOM   11934 N  N     . VAL A 1 2958 ? 135.306 161.922 143.355 1.00 59.67  ? 2958 VAL A N     1 
ATOM   11935 C  CA    . VAL A 1 2958 ? 136.442 161.441 144.133 1.00 63.75  ? 2958 VAL A CA    1 
ATOM   11936 C  C     . VAL A 1 2958 ? 137.718 162.075 143.601 1.00 64.77  ? 2958 VAL A C     1 
ATOM   11937 O  O     . VAL A 1 2958 ? 137.997 162.027 142.398 1.00 69.70  ? 2958 VAL A O     1 
ATOM   11938 C  CB    . VAL A 1 2958 ? 136.522 159.907 144.086 1.00 63.08  ? 2958 VAL A CB    1 
ATOM   11939 C  CG1   . VAL A 1 2958 ? 137.884 159.433 144.565 1.00 60.95  ? 2958 VAL A CG1   1 
ATOM   11940 C  CG2   . VAL A 1 2958 ? 135.415 159.296 144.925 1.00 68.86  ? 2958 VAL A CG2   1 
ATOM   11941 N  N     . TYR A 1 2959 ? 138.496 162.675 144.498 1.00 65.09  ? 2959 TYR A N     1 
ATOM   11942 C  CA    . TYR A 1 2959 ? 139.776 163.278 144.157 1.00 66.99  ? 2959 TYR A CA    1 
ATOM   11943 C  C     . TYR A 1 2959 ? 140.867 162.651 145.010 1.00 70.30  ? 2959 TYR A C     1 
ATOM   11944 O  O     . TYR A 1 2959 ? 140.766 162.634 146.241 1.00 75.73  ? 2959 TYR A O     1 
ATOM   11945 C  CB    . TYR A 1 2959 ? 139.743 164.795 144.361 1.00 70.70  ? 2959 TYR A CB    1 
ATOM   11946 C  CG    . TYR A 1 2959 ? 140.953 165.517 143.807 1.00 72.88  ? 2959 TYR A CG    1 
ATOM   11947 C  CD1   . TYR A 1 2959 ? 142.123 165.622 144.547 1.00 72.57  ? 2959 TYR A CD1   1 
ATOM   11948 C  CD2   . TYR A 1 2959 ? 140.926 166.086 142.543 1.00 70.77  ? 2959 TYR A CD2   1 
ATOM   11949 C  CE1   . TYR A 1 2959 ? 143.228 166.277 144.045 1.00 71.89  ? 2959 TYR A CE1   1 
ATOM   11950 C  CE2   . TYR A 1 2959 ? 142.028 166.742 142.032 1.00 71.95  ? 2959 TYR A CE2   1 
ATOM   11951 C  CZ    . TYR A 1 2959 ? 143.176 166.835 142.788 1.00 76.53  ? 2959 TYR A CZ    1 
ATOM   11952 O  OH    . TYR A 1 2959 ? 144.276 167.488 142.285 1.00 80.01  ? 2959 TYR A OH    1 
ATOM   11953 N  N     . GLN A 1 2960 ? 141.905 162.139 144.354 1.00 78.03  ? 2960 GLN A N     1 
ATOM   11954 C  CA    . GLN A 1 2960 ? 143.068 161.579 145.025 1.00 81.49  ? 2960 GLN A CA    1 
ATOM   11955 C  C     . GLN A 1 2960 ? 144.325 162.194 144.433 1.00 83.28  ? 2960 GLN A C     1 
ATOM   11956 O  O     . GLN A 1 2960 ? 144.422 162.376 143.216 1.00 82.58  ? 2960 GLN A O     1 
ATOM   11957 C  CB    . GLN A 1 2960 ? 143.117 160.052 144.890 1.00 79.09  ? 2960 GLN A CB    1 
ATOM   11958 C  CG    . GLN A 1 2960 ? 141.804 159.357 145.193 1.00 78.66  ? 2960 GLN A CG    1 
ATOM   11959 C  CD    . GLN A 1 2960 ? 141.918 157.849 145.134 1.00 82.21  ? 2960 GLN A CD    1 
ATOM   11960 O  OE1   . GLN A 1 2960 ? 141.394 157.211 144.221 1.00 82.66  ? 2960 GLN A OE1   1 
ATOM   11961 N  NE2   . GLN A 1 2960 ? 142.606 157.269 146.109 1.00 82.39  ? 2960 GLN A NE2   1 
ATOM   11962 N  N     . ILE A 1 2961 ? 145.283 162.514 145.294 1.00 85.48  ? 2961 ILE A N     1 
ATOM   11963 C  CA    . ILE A 1 2961 ? 146.532 163.119 144.848 1.00 83.95  ? 2961 ILE A CA    1 
ATOM   11964 C  C     . ILE A 1 2961 ? 147.497 162.019 144.428 1.00 89.55  ? 2961 ILE A C     1 
ATOM   11965 O  O     . ILE A 1 2961 ? 147.730 161.059 145.172 1.00 90.20  ? 2961 ILE A O     1 
ATOM   11966 C  CB    . ILE A 1 2961 ? 147.131 164.010 145.948 1.00 84.09  ? 2961 ILE A CB    1 
ATOM   11967 C  CG1   . ILE A 1 2961 ? 147.122 163.290 147.296 1.00 83.92  ? 2961 ILE A CG1   1 
ATOM   11968 C  CG2   . ILE A 1 2961 ? 146.364 165.316 146.047 1.00 90.93  ? 2961 ILE A CG2   1 
ATOM   11969 C  CD1   . ILE A 1 2961 ? 148.204 163.761 148.236 1.00 87.71  ? 2961 ILE A CD1   1 
ATOM   11970 N  N     . LYS A 1 2962 ? 148.054 162.152 143.226 1.00 106.59 ? 2962 LYS A N     1 
ATOM   11971 C  CA    . LYS A 1 2962 ? 148.964 161.153 142.667 1.00 104.73 ? 2962 LYS A CA    1 
ATOM   11972 C  C     . LYS A 1 2962 ? 150.366 161.439 143.187 1.00 105.10 ? 2962 LYS A C     1 
ATOM   11973 O  O     . LYS A 1 2962 ? 151.127 162.210 142.601 1.00 105.97 ? 2962 LYS A O     1 
ATOM   11974 C  CB    . LYS A 1 2962 ? 148.911 161.170 141.145 1.00 100.53 ? 2962 LYS A CB    1 
ATOM   11975 C  CG    . LYS A 1 2962 ? 147.507 161.056 140.575 1.00 103.18 ? 2962 LYS A CG    1 
ATOM   11976 C  CD    . LYS A 1 2962 ? 146.830 159.774 141.030 1.00 106.56 ? 2962 LYS A CD    1 
ATOM   11977 C  CE    . LYS A 1 2962 ? 145.342 159.797 140.723 1.00 107.70 ? 2962 LYS A CE    1 
ATOM   11978 N  NZ    . LYS A 1 2962 ? 145.073 160.142 139.301 1.00 109.94 ? 2962 LYS A NZ    1 
ATOM   11979 N  N     . VAL A 1 2963 ? 150.711 160.808 144.303 1.00 98.05  ? 2963 VAL A N     1 
ATOM   11980 C  CA    . VAL A 1 2963 ? 152.006 161.023 144.937 1.00 97.99  ? 2963 VAL A CA    1 
ATOM   11981 C  C     . VAL A 1 2963 ? 153.062 160.195 144.218 1.00 99.15  ? 2963 VAL A C     1 
ATOM   11982 O  O     . VAL A 1 2963 ? 152.872 158.997 143.975 1.00 106.64 ? 2963 VAL A O     1 
ATOM   11983 C  CB    . VAL A 1 2963 ? 151.947 160.664 146.429 1.00 97.96  ? 2963 VAL A CB    1 
ATOM   11984 C  CG1   . VAL A 1 2963 ? 153.297 160.906 147.087 1.00 97.08  ? 2963 VAL A CG1   1 
ATOM   11985 C  CG2   . VAL A 1 2963 ? 150.858 161.461 147.123 1.00 103.31 ? 2963 VAL A CG2   1 
ATOM   11986 N  N     . HIS A 1 2964 ? 154.178 160.833 143.869 1.00 99.31  ? 2964 HIS A N     1 
ATOM   11987 C  CA    . HIS A 1 2964 ? 155.333 160.112 143.349 1.00 100.92 ? 2964 HIS A CA    1 
ATOM   11988 C  C     . HIS A 1 2964 ? 156.570 160.472 144.160 1.00 104.37 ? 2964 HIS A C     1 
ATOM   11989 O  O     . HIS A 1 2964 ? 156.465 161.137 145.196 1.00 104.81 ? 2964 HIS A O     1 
ATOM   11990 C  CB    . HIS A 1 2964 ? 155.546 160.410 141.863 1.00 98.70  ? 2964 HIS A CB    1 
ATOM   11991 C  CG    . HIS A 1 2964 ? 155.464 161.864 141.515 1.00 99.87  ? 2964 HIS A CG    1 
ATOM   11992 N  ND1   . HIS A 1 2964 ? 156.457 162.763 141.837 1.00 99.92  ? 2964 HIS A ND1   1 
ATOM   11993 C  CD2   . HIS A 1 2964 ? 154.512 162.571 140.862 1.00 102.62 ? 2964 HIS A CD2   1 
ATOM   11994 C  CE1   . HIS A 1 2964 ? 156.118 163.964 141.403 1.00 102.41 ? 2964 HIS A CE1   1 
ATOM   11995 N  NE2   . HIS A 1 2964 ? 154.942 163.875 140.808 1.00 106.27 ? 2964 HIS A NE2   1 
ATOM   11996 N  N     . ARG A 1 2965 ? 157.747 160.034 143.706 1.00 117.18 ? 2965 ARG A N     1 
ATOM   11997 C  CA    . ARG A 1 2965 ? 158.966 160.280 144.469 1.00 117.00 ? 2965 ARG A CA    1 
ATOM   11998 C  C     . ARG A 1 2965 ? 159.347 161.755 144.482 1.00 114.59 ? 2965 ARG A C     1 
ATOM   11999 O  O     . ARG A 1 2965 ? 159.927 162.233 145.463 1.00 114.11 ? 2965 ARG A O     1 
ATOM   12000 C  CB    . ARG A 1 2965 ? 160.115 159.441 143.912 1.00 117.23 ? 2965 ARG A CB    1 
ATOM   12001 C  CG    . ARG A 1 2965 ? 160.357 159.616 142.421 1.00 117.42 ? 2965 ARG A CG    1 
ATOM   12002 C  CD    . ARG A 1 2965 ? 161.350 158.588 141.908 1.00 116.75 ? 2965 ARG A CD    1 
ATOM   12003 N  NE    . ARG A 1 2965 ? 162.655 158.742 142.539 1.00 118.93 ? 2965 ARG A NE    1 
ATOM   12004 C  CZ    . ARG A 1 2965 ? 163.142 157.925 143.463 1.00 120.21 ? 2965 ARG A CZ    1 
ATOM   12005 N  NH1   . ARG A 1 2965 ? 162.458 156.876 143.888 1.00 119.90 ? 2965 ARG A NH1   1 
ATOM   12006 N  NH2   . ARG A 1 2965 ? 164.344 158.171 143.978 1.00 118.64 ? 2965 ARG A NH2   1 
ATOM   12007 N  N     . LYS A 1 2966 ? 159.035 162.489 143.416 1.00 110.18 ? 2966 LYS A N     1 
ATOM   12008 C  CA    . LYS A 1 2966 ? 159.389 163.897 143.306 1.00 112.24 ? 2966 LYS A CA    1 
ATOM   12009 C  C     . LYS A 1 2966 ? 158.290 164.820 143.815 1.00 113.36 ? 2966 LYS A C     1 
ATOM   12010 O  O     . LYS A 1 2966 ? 158.405 166.042 143.675 1.00 112.61 ? 2966 LYS A O     1 
ATOM   12011 C  CB    . LYS A 1 2966 ? 159.735 164.241 141.855 1.00 113.89 ? 2966 LYS A CB    1 
ATOM   12012 C  CG    . LYS A 1 2966 ? 160.818 165.300 141.711 1.00 112.44 ? 2966 LYS A CG    1 
ATOM   12013 C  CD    . LYS A 1 2966 ? 161.595 165.129 140.415 1.00 110.85 ? 2966 LYS A CD    1 
ATOM   12014 C  CE    . LYS A 1 2966 ? 162.654 164.047 140.546 1.00 112.37 ? 2966 LYS A CE    1 
ATOM   12015 N  NZ    . LYS A 1 2966 ? 163.618 164.073 139.411 1.00 112.92 ? 2966 LYS A NZ    1 
ATOM   12016 N  N     . TYR A 1 2967 ? 157.231 164.267 144.399 1.00 110.61 ? 2967 TYR A N     1 
ATOM   12017 C  CA    . TYR A 1 2967 ? 156.138 165.079 144.920 1.00 104.49 ? 2967 TYR A CA    1 
ATOM   12018 C  C     . TYR A 1 2967 ? 156.617 165.880 146.125 1.00 108.97 ? 2967 TYR A C     1 
ATOM   12019 O  O     . TYR A 1 2967 ? 157.082 165.306 147.116 1.00 107.80 ? 2967 TYR A O     1 
ATOM   12020 C  CB    . TYR A 1 2967 ? 154.962 164.186 145.302 1.00 104.16 ? 2967 TYR A CB    1 
ATOM   12021 C  CG    . TYR A 1 2967 ? 153.623 164.884 145.298 1.00 104.24 ? 2967 TYR A CG    1 
ATOM   12022 C  CD1   . TYR A 1 2967 ? 152.869 164.974 144.136 1.00 104.80 ? 2967 TYR A CD1   1 
ATOM   12023 C  CD2   . TYR A 1 2967 ? 153.110 165.448 146.456 1.00 105.26 ? 2967 TYR A CD2   1 
ATOM   12024 C  CE1   . TYR A 1 2967 ? 151.644 165.607 144.129 1.00 104.46 ? 2967 TYR A CE1   1 
ATOM   12025 C  CE2   . TYR A 1 2967 ? 151.886 166.084 146.458 1.00 105.57 ? 2967 TYR A CE2   1 
ATOM   12026 C  CZ    . TYR A 1 2967 ? 151.157 166.161 145.292 1.00 105.20 ? 2967 TYR A CZ    1 
ATOM   12027 O  OH    . TYR A 1 2967 ? 149.937 166.795 145.290 1.00 104.42 ? 2967 TYR A OH    1 
ATOM   12028 N  N     . THR A 1 2968 ? 156.506 167.200 146.043 1.00 118.08 ? 2968 THR A N     1 
ATOM   12029 C  CA    . THR A 1 2968 ? 156.922 168.100 147.110 1.00 114.87 ? 2968 THR A CA    1 
ATOM   12030 C  C     . THR A 1 2968 ? 155.727 168.919 147.590 1.00 113.44 ? 2968 THR A C     1 
ATOM   12031 O  O     . THR A 1 2968 ? 154.583 168.689 147.190 1.00 114.66 ? 2968 THR A O     1 
ATOM   12032 C  CB    . THR A 1 2968 ? 158.058 169.017 146.647 1.00 112.04 ? 2968 THR A CB    1 
ATOM   12033 O  OG1   . THR A 1 2968 ? 158.241 170.072 147.600 1.00 113.88 ? 2968 THR A OG1   1 
ATOM   12034 C  CG2   . THR A 1 2968 ? 157.736 169.623 145.293 1.00 111.14 ? 2968 THR A CG2   1 
ATOM   12035 N  N     . GLY A 1 2969 ? 156.008 169.886 148.466 1.00 107.74 ? 2969 GLY A N     1 
ATOM   12036 C  CA    . GLY A 1 2969 ? 154.948 170.708 149.021 1.00 107.58 ? 2969 GLY A CA    1 
ATOM   12037 C  C     . GLY A 1 2969 ? 154.243 171.570 147.994 1.00 108.94 ? 2969 GLY A C     1 
ATOM   12038 O  O     . GLY A 1 2969 ? 153.043 171.829 148.118 1.00 105.26 ? 2969 GLY A O     1 
ATOM   12039 N  N     . GLU A 1 2970 ? 154.971 172.036 146.977 1.00 119.02 ? 2970 GLU A N     1 
ATOM   12040 C  CA    . GLU A 1 2970 ? 154.364 172.892 145.961 1.00 116.37 ? 2970 GLU A CA    1 
ATOM   12041 C  C     . GLU A 1 2970 ? 153.329 172.135 145.138 1.00 116.18 ? 2970 GLU A C     1 
ATOM   12042 O  O     . GLU A 1 2970 ? 152.281 172.690 144.785 1.00 120.08 ? 2970 GLU A O     1 
ATOM   12043 C  CB    . GLU A 1 2970 ? 155.448 173.484 145.060 1.00 115.91 ? 2970 GLU A CB    1 
ATOM   12044 C  CG    . GLU A 1 2970 ? 156.305 174.554 145.731 1.00 117.26 ? 2970 GLU A CG    1 
ATOM   12045 C  CD    . GLU A 1 2970 ? 157.335 173.984 146.693 1.00 117.42 ? 2970 GLU A CD    1 
ATOM   12046 O  OE1   . GLU A 1 2970 ? 157.376 172.749 146.874 1.00 116.97 ? 2970 GLU A OE1   1 
ATOM   12047 O  OE2   . GLU A 1 2970 ? 158.105 174.778 147.274 1.00 117.69 ? 2970 GLU A OE2   1 
ATOM   12048 N  N     . ASP A 1 2971 ? 153.604 170.869 144.814 1.00 105.61 ? 2971 ASP A N     1 
ATOM   12049 C  CA    . ASP A 1 2971 ? 152.614 170.066 144.103 1.00 106.51 ? 2971 ASP A CA    1 
ATOM   12050 C  C     . ASP A 1 2971 ? 151.365 169.858 144.949 1.00 112.41 ? 2971 ASP A C     1 
ATOM   12051 O  O     . ASP A 1 2971 ? 150.242 169.893 144.432 1.00 115.47 ? 2971 ASP A O     1 
ATOM   12052 C  CB    . ASP A 1 2971 ? 153.219 168.724 143.694 1.00 107.09 ? 2971 ASP A CB    1 
ATOM   12053 C  CG    . ASP A 1 2971 ? 154.415 168.879 142.778 1.00 112.87 ? 2971 ASP A CG    1 
ATOM   12054 O  OD1   . ASP A 1 2971 ? 154.225 169.307 141.620 1.00 115.43 ? 2971 ASP A OD1   1 
ATOM   12055 O  OD2   . ASP A 1 2971 ? 155.543 168.570 143.211 1.00 114.20 ? 2971 ASP A OD2   1 
ATOM   12056 N  N     . PHE A 1 2972 ? 151.539 169.638 146.254 1.00 99.17  ? 2972 PHE A N     1 
ATOM   12057 C  CA    . PHE A 1 2972 ? 150.384 169.519 147.137 1.00 94.57  ? 2972 PHE A CA    1 
ATOM   12058 C  C     . PHE A 1 2972 ? 149.603 170.823 147.201 1.00 94.98  ? 2972 PHE A C     1 
ATOM   12059 O  O     . PHE A 1 2972 ? 148.370 170.810 147.251 1.00 98.03  ? 2972 PHE A O     1 
ATOM   12060 C  CB    . PHE A 1 2972 ? 150.822 169.098 148.535 1.00 95.59  ? 2972 PHE A CB    1 
ATOM   12061 C  CG    . PHE A 1 2972 ? 149.680 168.761 149.449 1.00 95.23  ? 2972 PHE A CG    1 
ATOM   12062 C  CD1   . PHE A 1 2972 ? 148.775 167.771 149.108 1.00 98.70  ? 2972 PHE A CD1   1 
ATOM   12063 C  CD2   . PHE A 1 2972 ? 149.510 169.433 150.646 1.00 96.89  ? 2972 PHE A CD2   1 
ATOM   12064 C  CE1   . PHE A 1 2972 ? 147.722 167.457 149.944 1.00 94.48  ? 2972 PHE A CE1   1 
ATOM   12065 C  CE2   . PHE A 1 2972 ? 148.459 169.123 151.487 1.00 96.86  ? 2972 PHE A CE2   1 
ATOM   12066 C  CZ    . PHE A 1 2972 ? 147.565 168.134 151.135 1.00 93.67  ? 2972 PHE A CZ    1 
ATOM   12067 N  N     . ASP A 1 2973 ? 150.305 171.957 147.218 1.00 97.85  ? 2973 ASP A N     1 
ATOM   12068 C  CA    . ASP A 1 2973 ? 149.622 173.245 147.205 1.00 96.97  ? 2973 ASP A CA    1 
ATOM   12069 C  C     . ASP A 1 2973 ? 148.823 173.426 145.922 1.00 95.76  ? 2973 ASP A C     1 
ATOM   12070 O  O     . ASP A 1 2973 ? 147.697 173.931 145.949 1.00 101.43 ? 2973 ASP A O     1 
ATOM   12071 C  CB    . ASP A 1 2973 ? 150.631 174.380 147.374 1.00 98.75  ? 2973 ASP A CB    1 
ATOM   12072 C  CG    . ASP A 1 2973 ? 151.194 174.454 148.778 1.00 103.86 ? 2973 ASP A CG    1 
ATOM   12073 O  OD1   . ASP A 1 2973 ? 151.040 173.472 149.532 1.00 107.75 ? 2973 ASP A OD1   1 
ATOM   12074 O  OD2   . ASP A 1 2973 ? 151.789 175.495 149.127 1.00 103.59 ? 2973 ASP A OD2   1 
ATOM   12075 N  N     . GLU A 1 2974 ? 149.393 173.018 144.786 1.00 90.29  ? 2974 GLU A N     1 
ATOM   12076 C  CA    . GLU A 1 2974 ? 148.666 173.105 143.522 1.00 89.13  ? 2974 GLU A CA    1 
ATOM   12077 C  C     . GLU A 1 2974 ? 147.437 172.204 143.525 1.00 90.28  ? 2974 GLU A C     1 
ATOM   12078 O  O     . GLU A 1 2974 ? 146.367 172.597 143.044 1.00 94.00  ? 2974 GLU A O     1 
ATOM   12079 C  CB    . GLU A 1 2974 ? 149.591 172.748 142.359 1.00 87.88  ? 2974 GLU A CB    1 
ATOM   12080 C  CG    . GLU A 1 2974 ? 149.139 173.298 141.017 1.00 93.34  ? 2974 GLU A CG    1 
ATOM   12081 C  CD    . GLU A 1 2974 ? 148.659 174.733 141.105 1.00 96.59  ? 2974 GLU A CD    1 
ATOM   12082 O  OE1   . GLU A 1 2974 ? 149.465 175.608 141.484 1.00 95.16  ? 2974 GLU A OE1   1 
ATOM   12083 O  OE2   . GLU A 1 2974 ? 147.476 174.985 140.794 1.00 97.72  ? 2974 GLU A OE2   1 
ATOM   12084 N  N     . ASP A 1 2975 ? 147.572 170.988 144.058 1.00 88.13  ? 2975 ASP A N     1 
ATOM   12085 C  CA    . ASP A 1 2975 ? 146.428 170.083 144.131 1.00 90.27  ? 2975 ASP A CA    1 
ATOM   12086 C  C     . ASP A 1 2975 ? 145.342 170.642 145.042 1.00 90.12  ? 2975 ASP A C     1 
ATOM   12087 O  O     . ASP A 1 2975 ? 144.148 170.556 144.726 1.00 92.91  ? 2975 ASP A O     1 
ATOM   12088 C  CB    . ASP A 1 2975 ? 146.879 168.705 144.613 1.00 90.85  ? 2975 ASP A CB    1 
ATOM   12089 C  CG    . ASP A 1 2975 ? 147.519 167.885 143.513 1.00 96.92  ? 2975 ASP A CG    1 
ATOM   12090 O  OD1   . ASP A 1 2975 ? 147.337 168.234 142.328 1.00 99.47  ? 2975 ASP A OD1   1 
ATOM   12091 O  OD2   . ASP A 1 2975 ? 148.206 166.892 143.831 1.00 96.76  ? 2975 ASP A OD2   1 
ATOM   12092 N  N     . LEU A 1 2976 ? 145.738 171.217 146.179 1.00 79.76  ? 2976 LEU A N     1 
ATOM   12093 C  CA    . LEU A 1 2976 ? 144.771 171.842 147.074 1.00 75.24  ? 2976 LEU A CA    1 
ATOM   12094 C  C     . LEU A 1 2976 ? 144.087 173.023 146.402 1.00 80.50  ? 2976 LEU A C     1 
ATOM   12095 O  O     . LEU A 1 2976 ? 142.879 173.219 146.561 1.00 85.38  ? 2976 LEU A O     1 
ATOM   12096 C  CB    . LEU A 1 2976 ? 145.457 172.285 148.366 1.00 71.45  ? 2976 LEU A CB    1 
ATOM   12097 C  CG    . LEU A 1 2976 ? 145.538 171.252 149.489 1.00 69.71  ? 2976 LEU A CG    1 
ATOM   12098 C  CD1   . LEU A 1 2976 ? 146.123 171.875 150.744 1.00 73.50  ? 2976 LEU A CD1   1 
ATOM   12099 C  CD2   . LEU A 1 2976 ? 144.167 170.662 149.771 1.00 78.10  ? 2976 LEU A CD2   1 
ATOM   12100 N  N     . ARG A 1 2977 ? 144.844 173.826 145.651 1.00 84.37  ? 2977 ARG A N     1 
ATOM   12101 C  CA    . ARG A 1 2977 ? 144.245 174.939 144.924 1.00 79.80  ? 2977 ARG A CA    1 
ATOM   12102 C  C     . ARG A 1 2977 ? 143.225 174.442 143.911 1.00 81.40  ? 2977 ARG A C     1 
ATOM   12103 O  O     . ARG A 1 2977 ? 142.134 175.009 143.791 1.00 83.67  ? 2977 ARG A O     1 
ATOM   12104 C  CB    . ARG A 1 2977 ? 145.330 175.758 144.226 1.00 80.45  ? 2977 ARG A CB    1 
ATOM   12105 C  CG    . ARG A 1 2977 ? 146.065 176.728 145.131 1.00 76.23  ? 2977 ARG A CG    1 
ATOM   12106 C  CD    . ARG A 1 2977 ? 147.166 177.448 144.375 1.00 80.27  ? 2977 ARG A CD    1 
ATOM   12107 N  NE    . ARG A 1 2977 ? 148.366 177.613 145.187 1.00 86.08  ? 2977 ARG A NE    1 
ATOM   12108 C  CZ    . ARG A 1 2977 ? 149.552 177.110 144.877 1.00 88.32  ? 2977 ARG A CZ    1 
ATOM   12109 N  NH1   . ARG A 1 2977 ? 149.736 176.401 143.776 1.00 86.35  ? 2977 ARG A NH1   1 
ATOM   12110 N  NH2   . ARG A 1 2977 ? 150.581 177.323 145.693 1.00 88.13  ? 2977 ARG A NH2   1 
ATOM   12111 N  N     . THR A 1 2978 ? 143.560 173.379 143.179 1.00 79.18  ? 2978 THR A N     1 
ATOM   12112 C  CA    . THR A 1 2978 ? 142.626 172.830 142.200 1.00 83.16  ? 2978 THR A CA    1 
ATOM   12113 C  C     . THR A 1 2978 ? 141.361 172.315 142.877 1.00 82.60  ? 2978 THR A C     1 
ATOM   12114 O  O     . THR A 1 2978 ? 140.242 172.574 142.413 1.00 86.14  ? 2978 THR A O     1 
ATOM   12115 C  CB    . THR A 1 2978 ? 143.298 171.713 141.401 1.00 81.74  ? 2978 THR A CB    1 
ATOM   12116 O  OG1   . THR A 1 2978 ? 144.449 172.232 140.724 1.00 87.02  ? 2978 THR A OG1   1 
ATOM   12117 C  CG2   . THR A 1 2978 ? 142.333 171.137 140.377 1.00 78.73  ? 2978 THR A CG2   1 
ATOM   12118 N  N     . VAL A 1 2979 ? 141.519 171.589 143.987 1.00 78.26  ? 2979 VAL A N     1 
ATOM   12119 C  CA    . VAL A 1 2979 ? 140.356 171.009 144.654 1.00 68.89  ? 2979 VAL A CA    1 
ATOM   12120 C  C     . VAL A 1 2979 ? 139.485 172.103 145.263 1.00 73.74  ? 2979 VAL A C     1 
ATOM   12121 O  O     . VAL A 1 2979 ? 138.252 172.034 145.205 1.00 76.62  ? 2979 VAL A O     1 
ATOM   12122 C  CB    . VAL A 1 2979 ? 140.795 169.953 145.691 1.00 70.38  ? 2979 VAL A CB    1 
ATOM   12123 C  CG1   . VAL A 1 2979 ? 141.124 170.573 147.041 1.00 77.45  ? 2979 VAL A CG1   1 
ATOM   12124 C  CG2   . VAL A 1 2979 ? 139.721 168.895 145.846 1.00 75.09  ? 2979 VAL A CG2   1 
ATOM   12125 N  N     . LEU A 1 2980 ? 140.104 173.148 145.823 1.00 76.90  ? 2980 LEU A N     1 
ATOM   12126 C  CA    . LEU A 1 2980 ? 139.330 174.251 146.380 1.00 73.95  ? 2980 LEU A CA    1 
ATOM   12127 C  C     . LEU A 1 2980 ? 138.620 175.031 145.284 1.00 79.33  ? 2980 LEU A C     1 
ATOM   12128 O  O     . LEU A 1 2980 ? 137.469 175.444 145.460 1.00 82.87  ? 2980 LEU A O     1 
ATOM   12129 C  CB    . LEU A 1 2980 ? 140.231 175.173 147.201 1.00 75.06  ? 2980 LEU A CB    1 
ATOM   12130 C  CG    . LEU A 1 2980 ? 140.800 174.599 148.500 1.00 70.05  ? 2980 LEU A CG    1 
ATOM   12131 C  CD1   . LEU A 1 2980 ? 141.378 175.705 149.365 1.00 73.51  ? 2980 LEU A CD1   1 
ATOM   12132 C  CD2   . LEU A 1 2980 ? 139.735 173.830 149.256 1.00 72.03  ? 2980 LEU A CD2   1 
ATOM   12133 N  N     . ARG A 1 2981 ? 139.283 175.238 144.145 1.00 86.02  ? 2981 ARG A N     1 
ATOM   12134 C  CA    . ARG A 1 2981 ? 138.630 175.904 143.026 1.00 88.61  ? 2981 ARG A CA    1 
ATOM   12135 C  C     . ARG A 1 2981 ? 137.415 175.118 142.559 1.00 88.04  ? 2981 ARG A C     1 
ATOM   12136 O  O     . ARG A 1 2981 ? 136.333 175.685 142.375 1.00 88.20  ? 2981 ARG A O     1 
ATOM   12137 C  CB    . ARG A 1 2981 ? 139.620 176.088 141.877 1.00 85.93  ? 2981 ARG A CB    1 
ATOM   12138 C  CG    . ARG A 1 2981 ? 140.277 177.453 141.826 1.00 88.68  ? 2981 ARG A CG    1 
ATOM   12139 C  CD    . ARG A 1 2981 ? 141.553 177.405 141.004 1.00 89.39  ? 2981 ARG A CD    1 
ATOM   12140 N  NE    . ARG A 1 2981 ? 142.212 178.703 140.930 1.00 91.79  ? 2981 ARG A NE    1 
ATOM   12141 C  CZ    . ARG A 1 2981 ? 143.520 178.870 140.793 1.00 97.21  ? 2981 ARG A CZ    1 
ATOM   12142 N  NH1   . ARG A 1 2981 ? 144.343 177.837 140.712 1.00 93.75  ? 2981 ARG A NH1   1 
ATOM   12143 N  NH2   . ARG A 1 2981 ? 144.014 180.103 140.734 1.00 97.34  ? 2981 ARG A NH2   1 
ATOM   12144 N  N     . ARG A 1 2982 ? 137.567 173.802 142.393 1.00 82.64  ? 2982 ARG A N     1 
ATOM   12145 C  CA    . ARG A 1 2982 ? 136.443 172.989 141.938 1.00 80.44  ? 2982 ARG A CA    1 
ATOM   12146 C  C     . ARG A 1 2982 ? 135.317 172.964 142.965 1.00 85.16  ? 2982 ARG A C     1 
ATOM   12147 O  O     . ARG A 1 2982 ? 134.137 173.004 142.598 1.00 88.21  ? 2982 ARG A O     1 
ATOM   12148 C  CB    . ARG A 1 2982 ? 136.909 171.569 141.619 1.00 78.59  ? 2982 ARG A CB    1 
ATOM   12149 C  CG    . ARG A 1 2982 ? 137.731 171.464 140.348 1.00 83.87  ? 2982 ARG A CG    1 
ATOM   12150 C  CD    . ARG A 1 2982 ? 138.336 170.080 140.188 1.00 85.71  ? 2982 ARG A CD    1 
ATOM   12151 N  NE    . ARG A 1 2982 ? 137.326 169.032 140.280 1.00 83.80  ? 2982 ARG A NE    1 
ATOM   12152 C  CZ    . ARG A 1 2982 ? 137.597 167.738 140.378 1.00 84.38  ? 2982 ARG A CZ    1 
ATOM   12153 N  NH1   . ARG A 1 2982 ? 138.842 167.293 140.397 1.00 85.56  ? 2982 ARG A NH1   1 
ATOM   12154 N  NH2   . ARG A 1 2982 ? 136.593 166.869 140.457 1.00 81.90  ? 2982 ARG A NH2   1 
ATOM   12155 N  N     . SER A 1 2983 ? 135.654 172.902 144.253 1.00 82.67  ? 2983 SER A N     1 
ATOM   12156 C  CA    . SER A 1 2983 ? 134.648 172.754 145.294 1.00 78.47  ? 2983 SER A CA    1 
ATOM   12157 C  C     . SER A 1 2983 ? 134.005 174.068 145.720 1.00 83.25  ? 2983 SER A C     1 
ATOM   12158 O  O     . SER A 1 2983 ? 132.949 174.037 146.359 1.00 90.06  ? 2983 SER A O     1 
ATOM   12159 C  CB    . SER A 1 2983 ? 135.266 172.073 146.520 1.00 79.48  ? 2983 SER A CB    1 
ATOM   12160 O  OG    . SER A 1 2983 ? 134.339 172.004 147.587 1.00 89.51  ? 2983 SER A OG    1 
ATOM   12161 N  N     . GLY A 1 2984 ? 134.598 175.213 145.388 1.00 82.77  ? 2984 GLY A N     1 
ATOM   12162 C  CA    . GLY A 1 2984 ? 134.025 176.474 145.811 1.00 82.50  ? 2984 GLY A CA    1 
ATOM   12163 C  C     . GLY A 1 2984 ? 133.571 177.383 144.688 1.00 85.25  ? 2984 GLY A C     1 
ATOM   12164 O  O     . GLY A 1 2984 ? 132.599 178.127 144.849 1.00 87.24  ? 2984 GLY A O     1 
ATOM   12165 N  N     . CYS A 1 2985 ? 134.254 177.338 143.546 1.00 94.78  ? 2985 CYS A N     1 
ATOM   12166 C  CA    . CYS A 1 2985 ? 133.917 178.192 142.415 1.00 93.09  ? 2985 CYS A CA    1 
ATOM   12167 C  C     . CYS A 1 2985 ? 132.938 177.539 141.451 1.00 92.69  ? 2985 CYS A C     1 
ATOM   12168 O  O     . CYS A 1 2985 ? 132.081 178.225 140.886 1.00 95.26  ? 2985 CYS A O     1 
ATOM   12169 C  CB    . CYS A 1 2985 ? 135.188 178.589 141.658 1.00 94.62  ? 2985 CYS A CB    1 
ATOM   12170 S  SG    . CYS A 1 2985 ? 136.486 179.287 142.702 1.00 103.43 ? 2985 CYS A SG    1 
ATOM   12171 N  N     . LYS A 1 2986 ? 133.047 176.229 141.247 1.00 91.21  ? 2986 LYS A N     1 
ATOM   12172 C  CA    . LYS A 1 2986 ? 132.159 175.503 140.351 1.00 91.95  ? 2986 LYS A CA    1 
ATOM   12173 C  C     . LYS A 1 2986 ? 130.993 174.845 141.075 1.00 95.59  ? 2986 LYS A C     1 
ATOM   12174 O  O     . LYS A 1 2986 ? 130.147 174.229 140.418 1.00 95.95  ? 2986 LYS A O     1 
ATOM   12175 C  CB    . LYS A 1 2986 ? 132.947 174.441 139.579 1.00 90.51  ? 2986 LYS A CB    1 
ATOM   12176 C  CG    . LYS A 1 2986 ? 134.302 174.914 139.080 1.00 92.36  ? 2986 LYS A CG    1 
ATOM   12177 C  CD    . LYS A 1 2986 ? 134.159 175.884 137.921 1.00 93.52  ? 2986 LYS A CD    1 
ATOM   12178 C  CE    . LYS A 1 2986 ? 135.516 176.248 137.340 1.00 92.92  ? 2986 LYS A CE    1 
ATOM   12179 N  NZ    . LYS A 1 2986 ? 135.490 177.569 136.653 1.00 92.30  ? 2986 LYS A NZ    1 
ATOM   12180 N  N     . ASN A 1 2987 ? 130.926 174.969 142.403 1.00 93.52  ? 2987 ASN A N     1 
ATOM   12181 C  CA    . ASN A 1 2987 ? 129.882 174.333 143.209 1.00 92.25  ? 2987 ASN A CA    1 
ATOM   12182 C  C     . ASN A 1 2987 ? 129.809 172.833 142.931 1.00 93.04  ? 2987 ASN A C     1 
ATOM   12183 O  O     . ASN A 1 2987 ? 128.731 172.257 142.771 1.00 93.04  ? 2987 ASN A O     1 
ATOM   12184 C  CB    . ASN A 1 2987 ? 128.524 174.999 142.979 1.00 91.92  ? 2987 ASN A CB    1 
ATOM   12185 C  CG    . ASN A 1 2987 ? 127.524 174.674 144.071 1.00 93.04  ? 2987 ASN A CG    1 
ATOM   12186 O  OD1   . ASN A 1 2987 ? 127.843 174.732 145.258 1.00 88.33  ? 2987 ASN A OD1   1 
ATOM   12187 N  ND2   . ASN A 1 2987 ? 126.306 174.326 143.673 1.00 92.33  ? 2987 ASN A ND2   1 
ATOM   12188 N  N     . GLU A 1 2988 ? 130.974 172.196 142.869 1.00 87.89  ? 2988 GLU A N     1 
ATOM   12189 C  CA    . GLU A 1 2988 ? 131.082 170.772 142.588 1.00 87.23  ? 2988 GLU A CA    1 
ATOM   12190 C  C     . GLU A 1 2988 ? 131.449 170.033 143.867 1.00 85.36  ? 2988 GLU A C     1 
ATOM   12191 O  O     . GLU A 1 2988 ? 132.493 170.305 144.469 1.00 84.84  ? 2988 GLU A O     1 
ATOM   12192 C  CB    . GLU A 1 2988 ? 132.128 170.511 141.502 1.00 87.07  ? 2988 GLU A CB    1 
ATOM   12193 C  CG    . GLU A 1 2988 ? 132.586 169.066 141.409 1.00 92.06  ? 2988 GLU A CG    1 
ATOM   12194 C  CD    . GLU A 1 2988 ? 133.634 168.858 140.334 1.00 95.06  ? 2988 GLU A CD    1 
ATOM   12195 O  OE1   . GLU A 1 2988 ? 133.866 169.793 139.540 1.00 93.65  ? 2988 GLU A OE1   1 
ATOM   12196 O  OE2   . GLU A 1 2988 ? 134.229 167.761 140.285 1.00 95.45  ? 2988 GLU A OE2   1 
ATOM   12197 N  N     . LYS A 1 2989 ? 130.591 169.101 144.276 1.00 76.09  ? 2989 LYS A N     1 
ATOM   12198 C  CA    . LYS A 1 2989 ? 130.828 168.318 145.481 1.00 77.20  ? 2989 LYS A CA    1 
ATOM   12199 C  C     . LYS A 1 2989 ? 132.002 167.376 145.247 1.00 75.90  ? 2989 LYS A C     1 
ATOM   12200 O  O     . LYS A 1 2989 ? 132.022 166.635 144.259 1.00 81.12  ? 2989 LYS A O     1 
ATOM   12201 C  CB    . LYS A 1 2989 ? 129.571 167.540 145.862 1.00 76.13  ? 2989 LYS A CB    1 
ATOM   12202 C  CG    . LYS A 1 2989 ? 128.466 168.405 146.443 1.00 76.52  ? 2989 LYS A CG    1 
ATOM   12203 C  CD    . LYS A 1 2989 ? 127.325 167.562 146.981 1.00 75.26  ? 2989 LYS A CD    1 
ATOM   12204 C  CE    . LYS A 1 2989 ? 126.547 166.907 145.852 1.00 78.94  ? 2989 LYS A CE    1 
ATOM   12205 N  NZ    . LYS A 1 2989 ? 125.349 166.179 146.351 1.00 81.71  ? 2989 LYS A NZ    1 
ATOM   12206 N  N     . ILE A 1 2990 ? 132.978 167.406 146.151 1.00 62.97  ? 2990 ILE A N     1 
ATOM   12207 C  CA    . ILE A 1 2990 ? 134.213 166.647 146.002 1.00 66.26  ? 2990 ILE A CA    1 
ATOM   12208 C  C     . ILE A 1 2990 ? 134.481 165.884 147.290 1.00 68.95  ? 2990 ILE A C     1 
ATOM   12209 O  O     . ILE A 1 2990 ? 134.415 166.459 148.382 1.00 74.18  ? 2990 ILE A O     1 
ATOM   12210 C  CB    . ILE A 1 2990 ? 135.403 167.563 145.660 1.00 60.28  ? 2990 ILE A CB    1 
ATOM   12211 C  CG1   . ILE A 1 2990 ? 135.351 167.972 144.187 1.00 65.34  ? 2990 ILE A CG1   1 
ATOM   12212 C  CG2   . ILE A 1 2990 ? 136.719 166.876 145.986 1.00 60.38  ? 2990 ILE A CG2   1 
ATOM   12213 C  CD1   . ILE A 1 2990 ? 136.672 168.455 143.639 1.00 74.62  ? 2990 ILE A CD1   1 
ATOM   12214 N  N     . ALA A 1 2991 ? 134.780 164.593 147.163 1.00 67.62  ? 2991 ALA A N     1 
ATOM   12215 C  CA    . ALA A 1 2991 ? 135.221 163.769 148.282 1.00 63.37  ? 2991 ALA A CA    1 
ATOM   12216 C  C     . ALA A 1 2991 ? 136.728 163.580 148.160 1.00 61.50  ? 2991 ALA A C     1 
ATOM   12217 O  O     . ALA A 1 2991 ? 137.193 162.692 147.439 1.00 69.52  ? 2991 ALA A O     1 
ATOM   12218 C  CB    . ALA A 1 2991 ? 134.495 162.427 148.297 1.00 60.21  ? 2991 ALA A CB    1 
ATOM   12219 N  N     . PHE A 1 2992 ? 137.488 164.412 148.867 1.00 55.99  ? 2992 PHE A N     1 
ATOM   12220 C  CA    . PHE A 1 2992 ? 138.946 164.410 148.777 1.00 54.05  ? 2992 PHE A CA    1 
ATOM   12221 C  C     . PHE A 1 2992 ? 139.476 163.265 149.630 1.00 55.05  ? 2992 PHE A C     1 
ATOM   12222 O  O     . PHE A 1 2992 ? 139.655 163.408 150.842 1.00 69.93  ? 2992 PHE A O     1 
ATOM   12223 C  CB    . PHE A 1 2992 ? 139.507 165.755 149.226 1.00 58.59  ? 2992 PHE A CB    1 
ATOM   12224 C  CG    . PHE A 1 2992 ? 140.997 165.875 149.083 1.00 61.54  ? 2992 PHE A CG    1 
ATOM   12225 C  CD1   . PHE A 1 2992 ? 141.667 165.218 148.066 1.00 68.80  ? 2992 PHE A CD1   1 
ATOM   12226 C  CD2   . PHE A 1 2992 ? 141.728 166.654 149.963 1.00 59.62  ? 2992 PHE A CD2   1 
ATOM   12227 C  CE1   . PHE A 1 2992 ? 143.037 165.331 147.934 1.00 68.52  ? 2992 PHE A CE1   1 
ATOM   12228 C  CE2   . PHE A 1 2992 ? 143.097 166.770 149.835 1.00 64.36  ? 2992 PHE A CE2   1 
ATOM   12229 C  CZ    . PHE A 1 2992 ? 143.752 166.108 148.820 1.00 66.26  ? 2992 PHE A CZ    1 
ATOM   12230 N  N     . ILE A 1 2993 ? 139.733 162.126 148.996 1.00 50.13  ? 2993 ILE A N     1 
ATOM   12231 C  CA    . ILE A 1 2993 ? 140.258 160.953 149.684 1.00 57.49  ? 2993 ILE A CA    1 
ATOM   12232 C  C     . ILE A 1 2993 ? 141.770 161.095 149.787 1.00 63.12  ? 2993 ILE A C     1 
ATOM   12233 O  O     . ILE A 1 2993 ? 142.456 161.285 148.778 1.00 67.17  ? 2993 ILE A O     1 
ATOM   12234 C  CB    . ILE A 1 2993 ? 139.875 159.659 148.953 1.00 56.01  ? 2993 ILE A CB    1 
ATOM   12235 C  CG1   . ILE A 1 2993 ? 138.362 159.595 148.747 1.00 58.52  ? 2993 ILE A CG1   1 
ATOM   12236 C  CG2   . ILE A 1 2993 ? 140.360 158.450 149.732 1.00 55.42  ? 2993 ILE A CG2   1 
ATOM   12237 C  CD1   . ILE A 1 2993 ? 137.885 158.299 148.144 1.00 59.26  ? 2993 ILE A CD1   1 
ATOM   12238 N  N     . MET A 1 2994 ? 142.290 161.002 151.007 1.00 73.14  ? 2994 MET A N     1 
ATOM   12239 C  CA    . MET A 1 2994 ? 143.703 161.215 151.272 1.00 68.72  ? 2994 MET A CA    1 
ATOM   12240 C  C     . MET A 1 2994 ? 144.194 160.177 152.269 1.00 67.60  ? 2994 MET A C     1 
ATOM   12241 O  O     . MET A 1 2994 ? 143.571 159.963 153.312 1.00 80.12  ? 2994 MET A O     1 
ATOM   12242 C  CB    . MET A 1 2994 ? 143.943 162.632 151.802 1.00 65.42  ? 2994 MET A CB    1 
ATOM   12243 C  CG    . MET A 1 2994 ? 145.392 163.061 151.845 1.00 72.15  ? 2994 MET A CG    1 
ATOM   12244 S  SD    . MET A 1 2994 ? 145.656 164.350 153.073 1.00 92.51  ? 2994 MET A SD    1 
ATOM   12245 C  CE    . MET A 1 2994 ? 147.409 164.178 153.370 1.00 71.08  ? 2994 MET A CE    1 
ATOM   12246 N  N     . ASP A 1 2995 ? 145.312 159.537 151.943 1.00 72.31  ? 2995 ASP A N     1 
ATOM   12247 C  CA    . ASP A 1 2995 ? 145.878 158.466 152.746 1.00 71.65  ? 2995 ASP A CA    1 
ATOM   12248 C  C     . ASP A 1 2995 ? 147.060 158.994 153.549 1.00 76.69  ? 2995 ASP A C     1 
ATOM   12249 O  O     . ASP A 1 2995 ? 147.700 159.981 153.177 1.00 87.27  ? 2995 ASP A O     1 
ATOM   12250 C  CB    . ASP A 1 2995 ? 146.314 157.296 151.852 1.00 74.33  ? 2995 ASP A CB    1 
ATOM   12251 C  CG    . ASP A 1 2995 ? 146.778 156.081 152.642 1.00 79.90  ? 2995 ASP A CG    1 
ATOM   12252 O  OD1   . ASP A 1 2995 ? 146.871 156.155 153.885 1.00 81.70  ? 2995 ASP A OD1   1 
ATOM   12253 O  OD2   . ASP A 1 2995 ? 147.053 155.040 152.010 1.00 82.97  ? 2995 ASP A OD2   1 
ATOM   12254 N  N     . GLU A 1 2996 ? 147.340 158.324 154.670 1.00 80.28  ? 2996 GLU A N     1 
ATOM   12255 C  CA    . GLU A 1 2996 ? 148.472 158.722 155.500 1.00 83.22  ? 2996 GLU A CA    1 
ATOM   12256 C  C     . GLU A 1 2996 ? 149.795 158.549 154.766 1.00 87.10  ? 2996 GLU A C     1 
ATOM   12257 O  O     . GLU A 1 2996 ? 150.762 159.262 155.055 1.00 90.88  ? 2996 GLU A O     1 
ATOM   12258 C  CB    . GLU A 1 2996 ? 148.484 157.921 156.803 1.00 91.00  ? 2996 GLU A CB    1 
ATOM   12259 C  CG    . GLU A 1 2996 ? 148.663 156.424 156.616 1.00 91.21  ? 2996 GLU A CG    1 
ATOM   12260 C  CD    . GLU A 1 2996 ? 149.442 155.785 157.748 1.00 94.05  ? 2996 GLU A CD    1 
ATOM   12261 O  OE1   . GLU A 1 2996 ? 149.748 156.490 158.733 1.00 91.57  ? 2996 GLU A OE1   1 
ATOM   12262 O  OE2   . GLU A 1 2996 ? 149.749 154.578 157.653 1.00 91.74  ? 2996 GLU A OE2   1 
ATOM   12263 N  N     . SER A 1 2997 ? 149.860 157.611 153.817 1.00 85.84  ? 2997 SER A N     1 
ATOM   12264 C  CA    . SER A 1 2997 ? 151.078 157.443 153.032 1.00 86.25  ? 2997 SER A CA    1 
ATOM   12265 C  C     . SER A 1 2997 ? 151.308 158.625 152.100 1.00 91.78  ? 2997 SER A C     1 
ATOM   12266 O  O     . SER A 1 2997 ? 152.430 158.828 151.623 1.00 89.66  ? 2997 SER A O     1 
ATOM   12267 C  CB    . SER A 1 2997 ? 151.017 156.142 152.233 1.00 83.87  ? 2997 SER A CB    1 
ATOM   12268 O  OG    . SER A 1 2997 ? 149.896 156.126 151.367 1.00 85.94  ? 2997 SER A OG    1 
ATOM   12269 N  N     . ASN A 1 2998 ? 150.263 159.410 151.829 1.00 89.69  ? 2998 ASN A N     1 
ATOM   12270 C  CA    . ASN A 1 2998 ? 150.417 160.601 151.005 1.00 81.82  ? 2998 ASN A CA    1 
ATOM   12271 C  C     . ASN A 1 2998 ? 151.054 161.751 151.772 1.00 84.57  ? 2998 ASN A C     1 
ATOM   12272 O  O     . ASN A 1 2998 ? 151.398 162.769 151.163 1.00 91.80  ? 2998 ASN A O     1 
ATOM   12273 C  CB    . ASN A 1 2998 ? 149.062 161.032 150.446 1.00 76.83  ? 2998 ASN A CB    1 
ATOM   12274 C  CG    . ASN A 1 2998 ? 148.505 160.041 149.446 1.00 80.99  ? 2998 ASN A CG    1 
ATOM   12275 O  OD1   . ASN A 1 2998 ? 149.171 159.073 149.078 1.00 82.29  ? 2998 ASN A OD1   1 
ATOM   12276 N  ND2   . ASN A 1 2998 ? 147.278 160.277 148.999 1.00 86.42  ? 2998 ASN A ND2   1 
ATOM   12277 N  N     . VAL A 1 2999 ? 151.214 161.616 153.086 1.00 88.15  ? 2999 VAL A N     1 
ATOM   12278 C  CA    . VAL A 1 2999 ? 151.882 162.633 153.890 1.00 89.20  ? 2999 VAL A CA    1 
ATOM   12279 C  C     . VAL A 1 2999 ? 153.385 162.405 153.778 1.00 90.15  ? 2999 VAL A C     1 
ATOM   12280 O  O     . VAL A 1 2999 ? 153.910 161.406 154.274 1.00 92.43  ? 2999 VAL A O     1 
ATOM   12281 C  CB    . VAL A 1 2999 ? 151.427 162.588 155.353 1.00 92.90  ? 2999 VAL A CB    1 
ATOM   12282 C  CG1   . VAL A 1 2999 ? 152.173 163.631 156.170 1.00 88.67  ? 2999 VAL A CG1   1 
ATOM   12283 C  CG2   . VAL A 1 2999 ? 149.929 162.798 155.453 1.00 93.00  ? 2999 VAL A CG2   1 
ATOM   12284 N  N     . LEU A 1 3000 ? 154.081 163.333 153.123 1.00 96.28  ? 3000 LEU A N     1 
ATOM   12285 C  CA    . LEU A 1 3000 ? 155.530 163.256 153.001 1.00 97.53  ? 3000 LEU A CA    1 
ATOM   12286 C  C     . LEU A 1 3000 ? 156.255 164.242 153.904 1.00 98.23  ? 3000 LEU A C     1 
ATOM   12287 O  O     . LEU A 1 3000 ? 157.315 163.902 154.441 1.00 97.31  ? 3000 LEU A O     1 
ATOM   12288 C  CB    . LEU A 1 3000 ? 155.952 163.497 151.548 1.00 98.60  ? 3000 LEU A CB    1 
ATOM   12289 C  CG    . LEU A 1 3000 ? 155.344 162.550 150.512 1.00 99.13  ? 3000 LEU A CG    1 
ATOM   12290 C  CD1   . LEU A 1 3000 ? 155.747 162.961 149.105 1.00 99.84  ? 3000 LEU A CD1   1 
ATOM   12291 C  CD2   . LEU A 1 3000 ? 155.746 161.111 150.792 1.00 98.71  ? 3000 LEU A CD2   1 
ATOM   12292 N  N     . ASP A 1 3001 ? 155.713 165.444 154.082 1.00 110.38 ? 3001 ASP A N     1 
ATOM   12293 C  CA    . ASP A 1 3001 ? 156.281 166.430 154.988 1.00 113.55 ? 3001 ASP A CA    1 
ATOM   12294 C  C     . ASP A 1 3001 ? 155.204 166.851 155.978 1.00 113.65 ? 3001 ASP A C     1 
ATOM   12295 O  O     . ASP A 1 3001 ? 154.045 166.440 155.880 1.00 111.17 ? 3001 ASP A O     1 
ATOM   12296 C  CB    . ASP A 1 3001 ? 156.824 167.653 154.237 1.00 112.43 ? 3001 ASP A CB    1 
ATOM   12297 C  CG    . ASP A 1 3001 ? 157.495 167.290 152.925 1.00 114.49 ? 3001 ASP A CG    1 
ATOM   12298 O  OD1   . ASP A 1 3001 ? 158.147 166.227 152.856 1.00 115.54 ? 3001 ASP A OD1   1 
ATOM   12299 O  OD2   . ASP A 1 3001 ? 157.372 168.073 151.960 1.00 114.02 ? 3001 ASP A OD2   1 
ATOM   12300 N  N     . SER A 1 3002 ? 155.604 167.678 156.946 1.00 114.89 ? 3002 SER A N     1 
ATOM   12301 C  CA    . SER A 1 3002 ? 154.646 168.205 157.909 1.00 117.54 ? 3002 SER A CA    1 
ATOM   12302 C  C     . SER A 1 3002 ? 153.783 169.311 157.316 1.00 118.61 ? 3002 SER A C     1 
ATOM   12303 O  O     . SER A 1 3002 ? 152.719 169.615 157.869 1.00 121.72 ? 3002 SER A O     1 
ATOM   12304 C  CB    . SER A 1 3002 ? 155.374 168.721 159.150 1.00 114.74 ? 3002 SER A CB    1 
ATOM   12305 O  OG    . SER A 1 3002 ? 154.453 169.154 160.134 1.00 115.64 ? 3002 SER A OG    1 
ATOM   12306 N  N     . GLY A 1 3003 ? 154.218 169.921 156.212 1.00 100.67 ? 3003 GLY A N     1 
ATOM   12307 C  CA    . GLY A 1 3003 ? 153.401 170.936 155.569 1.00 100.60 ? 3003 GLY A CA    1 
ATOM   12308 C  C     . GLY A 1 3003 ? 152.083 170.382 155.064 1.00 101.13 ? 3003 GLY A C     1 
ATOM   12309 O  O     . GLY A 1 3003 ? 151.054 171.060 155.112 1.00 107.48 ? 3003 GLY A O     1 
ATOM   12310 N  N     . PHE A 1 3004 ? 152.101 169.142 154.568 1.00 88.28  ? 3004 PHE A N     1 
ATOM   12311 C  CA    . PHE A 1 3004 ? 150.867 168.474 154.169 1.00 92.73  ? 3004 PHE A CA    1 
ATOM   12312 C  C     . PHE A 1 3004 ? 149.866 168.469 155.315 1.00 94.34  ? 3004 PHE A C     1 
ATOM   12313 O  O     . PHE A 1 3004 ? 148.711 168.884 155.158 1.00 95.60  ? 3004 PHE A O     1 
ATOM   12314 C  CB    . PHE A 1 3004 ? 151.166 167.038 153.734 1.00 95.53  ? 3004 PHE A CB    1 
ATOM   12315 C  CG    . PHE A 1 3004 ? 152.049 166.929 152.524 1.00 94.94  ? 3004 PHE A CG    1 
ATOM   12316 C  CD1   . PHE A 1 3004 ? 151.511 166.653 151.280 1.00 91.45  ? 3004 PHE A CD1   1 
ATOM   12317 C  CD2   . PHE A 1 3004 ? 153.419 167.090 152.633 1.00 94.09  ? 3004 PHE A CD2   1 
ATOM   12318 C  CE1   . PHE A 1 3004 ? 152.322 166.541 150.170 1.00 88.68  ? 3004 PHE A CE1   1 
ATOM   12319 C  CE2   . PHE A 1 3004 ? 154.233 166.985 151.525 1.00 92.64  ? 3004 PHE A CE2   1 
ATOM   12320 C  CZ    . PHE A 1 3004 ? 153.684 166.711 150.292 1.00 89.81  ? 3004 PHE A CZ    1 
ATOM   12321 N  N     . LEU A 1 3005 ? 150.309 168.015 156.489 1.00 98.64  ? 3005 LEU A N     1 
ATOM   12322 C  CA    . LEU A 1 3005 ? 149.425 167.938 157.643 1.00 96.68  ? 3005 LEU A CA    1 
ATOM   12323 C  C     . LEU A 1 3005 ? 148.996 169.317 158.120 1.00 95.52  ? 3005 LEU A C     1 
ATOM   12324 O  O     . LEU A 1 3005 ? 147.851 169.487 158.544 1.00 100.96 ? 3005 LEU A O     1 
ATOM   12325 C  CB    . LEU A 1 3005 ? 150.106 167.169 158.775 1.00 98.14  ? 3005 LEU A CB    1 
ATOM   12326 C  CG    . LEU A 1 3005 ? 149.925 165.651 158.730 1.00 99.84  ? 3005 LEU A CG    1 
ATOM   12327 C  CD1   . LEU A 1 3005 ? 150.784 164.973 159.784 1.00 99.68  ? 3005 LEU A CD1   1 
ATOM   12328 C  CD2   . LEU A 1 3005 ? 148.460 165.282 158.905 1.00 97.28  ? 3005 LEU A CD2   1 
ATOM   12329 N  N     . GLU A 1 3006 ? 149.886 170.309 158.062 1.00 87.76  ? 3006 GLU A N     1 
ATOM   12330 C  CA    . GLU A 1 3006 ? 149.514 171.656 158.490 1.00 87.94  ? 3006 GLU A CA    1 
ATOM   12331 C  C     . GLU A 1 3006 ? 148.420 172.238 157.599 1.00 92.41  ? 3006 GLU A C     1 
ATOM   12332 O  O     . GLU A 1 3006 ? 147.419 172.779 158.094 1.00 97.30  ? 3006 GLU A O     1 
ATOM   12333 C  CB    . GLU A 1 3006 ? 150.745 172.562 158.496 1.00 90.50  ? 3006 GLU A CB    1 
ATOM   12334 C  CG    . GLU A 1 3006 ? 150.432 174.035 158.700 1.00 98.16  ? 3006 GLU A CG    1 
ATOM   12335 C  CD    . GLU A 1 3006 ? 150.439 174.437 160.162 1.00 103.08 ? 3006 GLU A CD    1 
ATOM   12336 O  OE1   . GLU A 1 3006 ? 150.179 173.570 161.022 1.00 102.35 ? 3006 GLU A OE1   1 
ATOM   12337 O  OE2   . GLU A 1 3006 ? 150.710 175.621 160.451 1.00 102.42 ? 3006 GLU A OE2   1 
ATOM   12338 N  N     . ARG A 1 3007 ? 148.593 172.140 156.278 1.00 83.31  ? 3007 ARG A N     1 
ATOM   12339 C  CA    . ARG A 1 3007 ? 147.576 172.658 155.370 1.00 80.96  ? 3007 ARG A CA    1 
ATOM   12340 C  C     . ARG A 1 3007 ? 146.275 171.876 155.499 1.00 82.98  ? 3007 ARG A C     1 
ATOM   12341 O  O     . ARG A 1 3007 ? 145.186 172.457 155.429 1.00 82.69  ? 3007 ARG A O     1 
ATOM   12342 C  CB    . ARG A 1 3007 ? 148.079 172.638 153.926 1.00 76.46  ? 3007 ARG A CB    1 
ATOM   12343 C  CG    . ARG A 1 3007 ? 149.445 173.279 153.738 1.00 79.29  ? 3007 ARG A CG    1 
ATOM   12344 C  CD    . ARG A 1 3007 ? 149.569 173.976 152.393 1.00 81.26  ? 3007 ARG A CD    1 
ATOM   12345 N  NE    . ARG A 1 3007 ? 149.212 175.388 152.466 1.00 87.43  ? 3007 ARG A NE    1 
ATOM   12346 C  CZ    . ARG A 1 3007 ? 150.028 176.345 152.888 1.00 90.61  ? 3007 ARG A CZ    1 
ATOM   12347 N  NH1   . ARG A 1 3007 ? 151.263 176.079 153.280 1.00 89.83  ? 3007 ARG A NH1   1 
ATOM   12348 N  NH2   . ARG A 1 3007 ? 149.595 177.603 152.912 1.00 88.00  ? 3007 ARG A NH2   1 
ATOM   12349 N  N     . MET A 1 3008 ? 146.364 170.556 155.692 1.00 85.42  ? 3008 MET A N     1 
ATOM   12350 C  CA    . MET A 1 3008 ? 145.152 169.767 155.886 1.00 79.71  ? 3008 MET A CA    1 
ATOM   12351 C  C     . MET A 1 3008 ? 144.435 170.173 157.165 1.00 79.78  ? 3008 MET A C     1 
ATOM   12352 O  O     . MET A 1 3008 ? 143.204 170.251 157.196 1.00 88.98  ? 3008 MET A O     1 
ATOM   12353 C  CB    . MET A 1 3008 ? 145.490 168.276 155.912 1.00 80.49  ? 3008 MET A CB    1 
ATOM   12354 C  CG    . MET A 1 3008 ? 145.727 167.625 154.543 1.00 85.83  ? 3008 MET A CG    1 
ATOM   12355 S  SD    . MET A 1 3008 ? 144.613 167.944 153.145 1.00 96.85  ? 3008 MET A SD    1 
ATOM   12356 C  CE    . MET A 1 3008 ? 143.002 168.167 153.903 1.00 80.65  ? 3008 MET A CE    1 
ATOM   12357 N  N     . ASN A 1 3009 ? 145.192 170.432 158.232 1.00 66.87  ? 3009 ASN A N     1 
ATOM   12358 C  CA    . ASN A 1 3009 ? 144.617 170.907 159.484 1.00 68.92  ? 3009 ASN A CA    1 
ATOM   12359 C  C     . ASN A 1 3009 ? 143.863 172.212 159.269 1.00 69.00  ? 3009 ASN A C     1 
ATOM   12360 O  O     . ASN A 1 3009 ? 142.704 172.352 159.682 1.00 70.95  ? 3009 ASN A O     1 
ATOM   12361 C  CB    . ASN A 1 3009 ? 145.743 171.077 160.512 1.00 73.73  ? 3009 ASN A CB    1 
ATOM   12362 C  CG    . ASN A 1 3009 ? 145.290 171.732 161.809 1.00 74.51  ? 3009 ASN A CG    1 
ATOM   12363 O  OD1   . ASN A 1 3009 ? 144.105 171.947 162.046 1.00 82.05  ? 3009 ASN A OD1   1 
ATOM   12364 N  ND2   . ASN A 1 3009 ? 146.255 172.055 162.661 1.00 75.89  ? 3009 ASN A ND2   1 
ATOM   12365 N  N     . THR A 1 3010 ? 144.511 173.180 158.617 1.00 71.39  ? 3010 THR A N     1 
ATOM   12366 C  CA    . THR A 1 3010 ? 143.857 174.466 158.389 1.00 74.48  ? 3010 THR A CA    1 
ATOM   12367 C  C     . THR A 1 3010 ? 142.601 174.304 157.541 1.00 73.66  ? 3010 THR A C     1 
ATOM   12368 O  O     . THR A 1 3010 ? 141.553 174.882 157.855 1.00 74.64  ? 3010 THR A O     1 
ATOM   12369 C  CB    . THR A 1 3010 ? 144.826 175.446 157.727 1.00 76.90  ? 3010 THR A CB    1 
ATOM   12370 O  OG1   . THR A 1 3010 ? 146.004 175.576 158.532 1.00 75.54  ? 3010 THR A OG1   1 
ATOM   12371 C  CG2   . THR A 1 3010 ? 144.172 176.809 157.575 1.00 73.51  ? 3010 THR A CG2   1 
ATOM   12372 N  N     . LEU A 1 3011 ? 142.682 173.507 156.472 1.00 71.38  ? 3011 LEU A N     1 
ATOM   12373 C  CA    . LEU A 1 3011 ? 141.535 173.327 155.588 1.00 61.61  ? 3011 LEU A CA    1 
ATOM   12374 C  C     . LEU A 1 3011 ? 140.383 172.628 156.299 1.00 60.25  ? 3011 LEU A C     1 
ATOM   12375 O  O     . LEU A 1 3011 ? 139.219 173.004 156.121 1.00 61.38  ? 3011 LEU A O     1 
ATOM   12376 C  CB    . LEU A 1 3011 ? 141.952 172.545 154.344 1.00 63.21  ? 3011 LEU A CB    1 
ATOM   12377 C  CG    . LEU A 1 3011 ? 140.819 172.035 153.455 1.00 58.15  ? 3011 LEU A CG    1 
ATOM   12378 C  CD1   . LEU A 1 3011 ? 140.025 173.199 152.894 1.00 65.97  ? 3011 LEU A CD1   1 
ATOM   12379 C  CD2   . LEU A 1 3011 ? 141.369 171.172 152.334 1.00 62.64  ? 3011 LEU A CD2   1 
ATOM   12380 N  N     . LEU A 1 3012 ? 140.682 171.601 157.096 1.00 70.32  ? 3012 LEU A N     1 
ATOM   12381 C  CA    . LEU A 1 3012 ? 139.631 170.892 157.817 1.00 66.43  ? 3012 LEU A CA    1 
ATOM   12382 C  C     . LEU A 1 3012 ? 138.964 171.790 158.847 1.00 69.77  ? 3012 LEU A C     1 
ATOM   12383 O  O     . LEU A 1 3012 ? 137.732 171.819 158.948 1.00 67.85  ? 3012 LEU A O     1 
ATOM   12384 C  CB    . LEU A 1 3012 ? 140.207 169.650 158.497 1.00 57.89  ? 3012 LEU A CB    1 
ATOM   12385 C  CG    . LEU A 1 3012 ? 140.614 168.477 157.608 1.00 58.96  ? 3012 LEU A CG    1 
ATOM   12386 C  CD1   . LEU A 1 3012 ? 141.449 167.490 158.398 1.00 59.39  ? 3012 LEU A CD1   1 
ATOM   12387 C  CD2   . LEU A 1 3012 ? 139.392 167.802 157.033 1.00 63.87  ? 3012 LEU A CD2   1 
ATOM   12388 N  N     . ALA A 1 3013 ? 139.758 172.529 159.622 1.00 67.10  ? 3013 ALA A N     1 
ATOM   12389 C  CA    . ALA A 1 3013 ? 139.189 173.306 160.715 1.00 64.40  ? 3013 ALA A CA    1 
ATOM   12390 C  C     . ALA A 1 3013 ? 138.441 174.538 160.215 1.00 66.54  ? 3013 ALA A C     1 
ATOM   12391 O  O     . ALA A 1 3013 ? 137.329 174.821 160.672 1.00 64.14  ? 3013 ALA A O     1 
ATOM   12392 C  CB    . ALA A 1 3013 ? 140.289 173.699 161.697 1.00 64.95  ? 3013 ALA A CB    1 
ATOM   12393 N  N     . ASN A 1 3014 ? 139.027 175.283 159.276 1.00 77.23  ? 3014 ASN A N     1 
ATOM   12394 C  CA    . ASN A 1 3014 ? 138.436 176.541 158.833 1.00 75.41  ? 3014 ASN A CA    1 
ATOM   12395 C  C     . ASN A 1 3014 ? 137.683 176.438 157.516 1.00 75.79  ? 3014 ASN A C     1 
ATOM   12396 O  O     . ASN A 1 3014 ? 136.712 177.174 157.315 1.00 74.11  ? 3014 ASN A O     1 
ATOM   12397 C  CB    . ASN A 1 3014 ? 139.514 177.620 158.691 1.00 69.68  ? 3014 ASN A CB    1 
ATOM   12398 C  CG    . ASN A 1 3014 ? 140.136 178.002 160.016 1.00 72.44  ? 3014 ASN A CG    1 
ATOM   12399 O  OD1   . ASN A 1 3014 ? 141.351 177.921 160.189 1.00 74.85  ? 3014 ASN A OD1   1 
ATOM   12400 N  ND2   . ASN A 1 3014 ? 139.305 178.420 160.961 1.00 73.63  ? 3014 ASN A ND2   1 
ATOM   12401 N  N     . GLY A 1 3015 ? 138.098 175.552 156.619 1.00 72.84  ? 3015 GLY A N     1 
ATOM   12402 C  CA    . GLY A 1 3015 ? 137.547 175.523 155.283 1.00 68.12  ? 3015 GLY A CA    1 
ATOM   12403 C  C     . GLY A 1 3015 ? 138.276 176.385 154.280 1.00 71.43  ? 3015 GLY A C     1 
ATOM   12404 O  O     . GLY A 1 3015 ? 137.834 176.476 153.129 1.00 71.08  ? 3015 GLY A O     1 
ATOM   12405 N  N     . GLU A 1 3016 ? 139.374 177.023 154.677 1.00 85.47  ? 3016 GLU A N     1 
ATOM   12406 C  CA    . GLU A 1 3016 ? 140.165 177.833 153.761 1.00 81.77  ? 3016 GLU A CA    1 
ATOM   12407 C  C     . GLU A 1 3016 ? 141.584 177.927 154.299 1.00 84.46  ? 3016 GLU A C     1 
ATOM   12408 O  O     . GLU A 1 3016 ? 141.782 178.070 155.509 1.00 87.22  ? 3016 GLU A O     1 
ATOM   12409 C  CB    . GLU A 1 3016 ? 139.531 179.225 153.569 1.00 84.84  ? 3016 GLU A CB    1 
ATOM   12410 C  CG    . GLU A 1 3016 ? 139.388 180.098 154.825 1.00 90.17  ? 3016 GLU A CG    1 
ATOM   12411 C  CD    . GLU A 1 3016 ? 140.673 180.788 155.261 1.00 93.66  ? 3016 GLU A CD    1 
ATOM   12412 O  OE1   . GLU A 1 3016 ? 141.659 180.780 154.494 1.00 95.31  ? 3016 GLU A OE1   1 
ATOM   12413 O  OE2   . GLU A 1 3016 ? 140.694 181.340 156.381 1.00 90.17  ? 3016 GLU A OE2   1 
ATOM   12414 N  N     . VAL A 1 3017 ? 142.561 177.818 153.406 1.00 80.37  ? 3017 VAL A N     1 
ATOM   12415 C  CA    . VAL A 1 3017 ? 143.964 177.995 153.765 1.00 86.18  ? 3017 VAL A CA    1 
ATOM   12416 C  C     . VAL A 1 3017 ? 144.334 179.446 153.480 1.00 90.53  ? 3017 VAL A C     1 
ATOM   12417 O  O     . VAL A 1 3017 ? 144.154 179.917 152.348 1.00 86.96  ? 3017 VAL A O     1 
ATOM   12418 C  CB    . VAL A 1 3017 ? 144.867 177.014 153.003 1.00 87.66  ? 3017 VAL A CB    1 
ATOM   12419 C  CG1   . VAL A 1 3017 ? 146.279 177.047 153.564 1.00 87.73  ? 3017 VAL A CG1   1 
ATOM   12420 C  CG2   . VAL A 1 3017 ? 144.293 175.609 153.071 1.00 83.19  ? 3017 VAL A CG2   1 
ATOM   12421 N  N     . PRO A 1 3018 ? 144.843 180.191 154.465 1.00 91.03  ? 3018 PRO A N     1 
ATOM   12422 C  CA    . PRO A 1 3018 ? 145.028 181.636 154.250 1.00 86.17  ? 3018 PRO A CA    1 
ATOM   12423 C  C     . PRO A 1 3018 ? 146.113 181.970 153.242 1.00 89.67  ? 3018 PRO A C     1 
ATOM   12424 O  O     . PRO A 1 3018 ? 145.908 182.846 152.392 1.00 91.73  ? 3018 PRO A O     1 
ATOM   12425 C  CB    . PRO A 1 3018 ? 145.373 182.150 155.654 1.00 89.00  ? 3018 PRO A CB    1 
ATOM   12426 C  CG    . PRO A 1 3018 ? 146.007 180.981 156.328 1.00 86.93  ? 3018 PRO A CG    1 
ATOM   12427 C  CD    . PRO A 1 3018 ? 145.298 179.764 155.800 1.00 86.96  ? 3018 PRO A CD    1 
ATOM   12428 N  N     . GLY A 1 3019 ? 147.260 181.302 153.305 1.00 89.92  ? 3019 GLY A N     1 
ATOM   12429 C  CA    . GLY A 1 3019 ? 148.365 181.637 152.428 1.00 91.23  ? 3019 GLY A CA    1 
ATOM   12430 C  C     . GLY A 1 3019 ? 148.419 180.818 151.155 1.00 93.67  ? 3019 GLY A C     1 
ATOM   12431 O  O     . GLY A 1 3019 ? 149.400 180.889 150.409 1.00 98.39  ? 3019 GLY A O     1 
ATOM   12432 N  N     . LEU A 1 3020 ? 147.370 180.037 150.893 1.00 86.82  ? 3020 LEU A N     1 
ATOM   12433 C  CA    . LEU A 1 3020 ? 147.381 179.168 149.721 1.00 89.54  ? 3020 LEU A CA    1 
ATOM   12434 C  C     . LEU A 1 3020 ? 147.256 179.971 148.432 1.00 93.15  ? 3020 LEU A C     1 
ATOM   12435 O  O     . LEU A 1 3020 ? 147.982 179.715 147.464 1.00 94.36  ? 3020 LEU A O     1 
ATOM   12436 C  CB    . LEU A 1 3020 ? 146.261 178.135 149.825 1.00 85.59  ? 3020 LEU A CB    1 
ATOM   12437 C  CG    . LEU A 1 3020 ? 146.269 177.051 148.749 1.00 82.25  ? 3020 LEU A CG    1 
ATOM   12438 C  CD1   . LEU A 1 3020 ? 147.336 176.016 149.052 1.00 84.18  ? 3020 LEU A CD1   1 
ATOM   12439 C  CD2   . LEU A 1 3020 ? 144.907 176.395 148.646 1.00 88.35  ? 3020 LEU A CD2   1 
ATOM   12440 N  N     . PHE A 1 3021 ? 146.348 180.944 148.399 1.00 92.91  ? 3021 PHE A N     1 
ATOM   12441 C  CA    . PHE A 1 3021 ? 146.137 181.788 147.228 1.00 89.17  ? 3021 PHE A CA    1 
ATOM   12442 C  C     . PHE A 1 3021 ? 146.831 183.124 147.460 1.00 94.08  ? 3021 PHE A C     1 
ATOM   12443 O  O     . PHE A 1 3021 ? 146.467 183.870 148.375 1.00 97.20  ? 3021 PHE A O     1 
ATOM   12444 C  CB    . PHE A 1 3021 ? 144.649 181.989 146.956 1.00 88.80  ? 3021 PHE A CB    1 
ATOM   12445 C  CG    . PHE A 1 3021 ? 143.929 180.735 146.561 1.00 91.50  ? 3021 PHE A CG    1 
ATOM   12446 C  CD1   . PHE A 1 3021 ? 143.370 179.909 147.520 1.00 92.64  ? 3021 PHE A CD1   1 
ATOM   12447 C  CD2   . PHE A 1 3021 ? 143.813 180.381 145.229 1.00 92.27  ? 3021 PHE A CD2   1 
ATOM   12448 C  CE1   . PHE A 1 3021 ? 142.705 178.756 147.157 1.00 92.19  ? 3021 PHE A CE1   1 
ATOM   12449 C  CE2   . PHE A 1 3021 ? 143.151 179.229 144.860 1.00 92.76  ? 3021 PHE A CE2   1 
ATOM   12450 C  CZ    . PHE A 1 3021 ? 142.597 178.415 145.825 1.00 92.65  ? 3021 PHE A CZ    1 
ATOM   12451 N  N     . GLU A 1 3022 ? 147.827 183.424 146.630 1.00 106.70 ? 3022 GLU A N     1 
ATOM   12452 C  CA    . GLU A 1 3022 ? 148.571 184.669 146.725 1.00 106.13 ? 3022 GLU A CA    1 
ATOM   12453 C  C     . GLU A 1 3022 ? 149.051 185.081 145.342 1.00 109.89 ? 3022 GLU A C     1 
ATOM   12454 O  O     . GLU A 1 3022 ? 149.195 184.248 144.443 1.00 110.78 ? 3022 GLU A O     1 
ATOM   12455 C  CB    . GLU A 1 3022 ? 149.761 184.538 147.683 1.00 104.24 ? 3022 GLU A CB    1 
ATOM   12456 C  CG    . GLU A 1 3022 ? 150.510 183.221 147.561 1.00 108.20 ? 3022 GLU A CG    1 
ATOM   12457 C  CD    . GLU A 1 3022 ? 151.419 182.959 148.745 1.00 108.83 ? 3022 GLU A CD    1 
ATOM   12458 O  OE1   . GLU A 1 3022 ? 151.329 183.711 149.737 1.00 105.79 ? 3022 GLU A OE1   1 
ATOM   12459 O  OE2   . GLU A 1 3022 ? 152.223 182.005 148.685 1.00 108.68 ? 3022 GLU A OE2   1 
ATOM   12460 N  N     . GLY A 1 3023 ? 149.300 186.380 145.187 1.00 117.85 ? 3023 GLY A N     1 
ATOM   12461 C  CA    . GLY A 1 3023 ? 149.770 186.895 143.911 1.00 117.23 ? 3023 GLY A CA    1 
ATOM   12462 C  C     . GLY A 1 3023 ? 148.745 186.705 142.810 1.00 116.03 ? 3023 GLY A C     1 
ATOM   12463 O  O     . GLY A 1 3023 ? 147.560 187.022 142.961 1.00 114.54 ? 3023 GLY A O     1 
ATOM   12464 N  N     . ASP A 1 3024 ? 149.214 186.188 141.672 1.00 118.16 ? 3024 ASP A N     1 
ATOM   12465 C  CA    . ASP A 1 3024 ? 148.339 185.959 140.529 1.00 118.34 ? 3024 ASP A CA    1 
ATOM   12466 C  C     . ASP A 1 3024 ? 147.266 184.929 140.859 1.00 119.21 ? 3024 ASP A C     1 
ATOM   12467 O  O     . ASP A 1 3024 ? 146.100 185.131 140.501 1.00 118.99 ? 3024 ASP A O     1 
ATOM   12468 C  CB    . ASP A 1 3024 ? 149.200 185.534 139.326 1.00 117.95 ? 3024 ASP A CB    1 
ATOM   12469 C  CG    . ASP A 1 3024 ? 148.405 184.903 138.166 1.00 120.57 ? 3024 ASP A CG    1 
ATOM   12470 O  OD1   . ASP A 1 3024 ? 147.158 184.875 138.152 1.00 121.85 ? 3024 ASP A OD1   1 
ATOM   12471 O  OD2   . ASP A 1 3024 ? 149.069 184.413 137.228 1.00 120.78 ? 3024 ASP A OD2   1 
ATOM   12472 N  N     . GLU A 1 3025 ? 147.630 183.851 141.561 1.00 112.40 ? 3025 GLU A N     1 
ATOM   12473 C  CA    . GLU A 1 3025 ? 146.663 182.810 141.895 1.00 110.05 ? 3025 GLU A CA    1 
ATOM   12474 C  C     . GLU A 1 3025 ? 145.493 183.372 142.693 1.00 111.13 ? 3025 GLU A C     1 
ATOM   12475 O  O     . GLU A 1 3025 ? 144.374 182.851 142.621 1.00 110.42 ? 3025 GLU A O     1 
ATOM   12476 C  CB    . GLU A 1 3025 ? 147.348 181.687 142.675 1.00 110.63 ? 3025 GLU A CB    1 
ATOM   12477 C  CG    . GLU A 1 3025 ? 148.151 180.730 141.810 1.00 111.42 ? 3025 GLU A CG    1 
ATOM   12478 C  CD    . GLU A 1 3025 ? 149.639 180.798 142.092 1.00 113.62 ? 3025 GLU A CD    1 
ATOM   12479 O  OE1   . GLU A 1 3025 ? 150.014 181.101 143.245 1.00 113.23 ? 3025 GLU A OE1   1 
ATOM   12480 O  OE2   . GLU A 1 3025 ? 150.433 180.556 141.159 1.00 113.01 ? 3025 GLU A OE2   1 
ATOM   12481 N  N     . TYR A 1 3026 ? 145.733 184.433 143.468 1.00 105.33 ? 3026 TYR A N     1 
ATOM   12482 C  CA    . TYR A 1 3026 ? 144.644 185.052 144.216 1.00 104.72 ? 3026 TYR A CA    1 
ATOM   12483 C  C     . TYR A 1 3026 ? 143.675 185.774 143.289 1.00 107.75 ? 3026 TYR A C     1 
ATOM   12484 O  O     . TYR A 1 3026 ? 142.457 185.658 143.449 1.00 108.52 ? 3026 TYR A O     1 
ATOM   12485 C  CB    . TYR A 1 3026 ? 145.201 186.012 145.266 1.00 102.72 ? 3026 TYR A CB    1 
ATOM   12486 C  CG    . TYR A 1 3026 ? 144.153 186.534 146.224 1.00 103.13 ? 3026 TYR A CG    1 
ATOM   12487 C  CD1   . TYR A 1 3026 ? 143.599 185.708 147.193 1.00 105.03 ? 3026 TYR A CD1   1 
ATOM   12488 C  CD2   . TYR A 1 3026 ? 143.716 187.850 146.159 1.00 104.95 ? 3026 TYR A CD2   1 
ATOM   12489 C  CE1   . TYR A 1 3026 ? 142.641 186.178 148.070 1.00 105.40 ? 3026 TYR A CE1   1 
ATOM   12490 C  CE2   . TYR A 1 3026 ? 142.758 188.328 147.032 1.00 107.46 ? 3026 TYR A CE2   1 
ATOM   12491 C  CZ    . TYR A 1 3026 ? 142.224 187.488 147.985 1.00 108.07 ? 3026 TYR A CZ    1 
ATOM   12492 O  OH    . TYR A 1 3026 ? 141.269 187.962 148.855 1.00 108.63 ? 3026 TYR A OH    1 
ATOM   12493 N  N     . ALA A 1 3027 ? 144.194 186.527 142.315 1.00 110.26 ? 3027 ALA A N     1 
ATOM   12494 C  CA    . ALA A 1 3027 ? 143.325 187.299 141.428 1.00 109.31 ? 3027 ALA A CA    1 
ATOM   12495 C  C     . ALA A 1 3027 ? 142.476 186.393 140.544 1.00 109.46 ? 3027 ALA A C     1 
ATOM   12496 O  O     . ALA A 1 3027 ? 141.290 186.667 140.313 1.00 110.18 ? 3027 ALA A O     1 
ATOM   12497 C  CB    . ALA A 1 3027 ? 144.162 188.251 140.574 1.00 108.11 ? 3027 ALA A CB    1 
ATOM   12498 N  N     . THR A 1 3028 ? 143.069 185.315 140.026 1.00 108.59 ? 3028 THR A N     1 
ATOM   12499 C  CA    . THR A 1 3028 ? 142.299 184.364 139.232 1.00 108.33 ? 3028 THR A CA    1 
ATOM   12500 C  C     . THR A 1 3028 ? 141.206 183.716 140.071 1.00 110.70 ? 3028 THR A C     1 
ATOM   12501 O  O     . THR A 1 3028 ? 140.076 183.533 139.601 1.00 110.45 ? 3028 THR A O     1 
ATOM   12502 C  CB    . THR A 1 3028 ? 143.225 183.303 138.639 1.00 109.63 ? 3028 THR A CB    1 
ATOM   12503 O  OG1   . THR A 1 3028 ? 144.290 183.943 137.926 1.00 109.74 ? 3028 THR A OG1   1 
ATOM   12504 C  CG2   . THR A 1 3028 ? 142.458 182.400 137.685 1.00 108.63 ? 3028 THR A CG2   1 
ATOM   12505 N  N     . LEU A 1 3029 ? 141.525 183.367 141.320 1.00 105.15 ? 3029 LEU A N     1 
ATOM   12506 C  CA    . LEU A 1 3029 ? 140.510 182.837 142.223 1.00 105.46 ? 3029 LEU A CA    1 
ATOM   12507 C  C     . LEU A 1 3029 ? 139.408 183.859 142.463 1.00 104.31 ? 3029 LEU A C     1 
ATOM   12508 O  O     . LEU A 1 3029 ? 138.229 183.503 142.540 1.00 102.01 ? 3029 LEU A O     1 
ATOM   12509 C  CB    . LEU A 1 3029 ? 141.145 182.418 143.548 1.00 101.06 ? 3029 LEU A CB    1 
ATOM   12510 C  CG    . LEU A 1 3029 ? 140.165 182.192 144.702 1.00 98.29  ? 3029 LEU A CG    1 
ATOM   12511 C  CD1   . LEU A 1 3029 ? 139.443 180.864 144.540 1.00 99.80  ? 3029 LEU A CD1   1 
ATOM   12512 C  CD2   . LEU A 1 3029 ? 140.866 182.268 146.047 1.00 100.48 ? 3029 LEU A CD2   1 
ATOM   12513 N  N     . MET A 1 3030 ? 139.775 185.136 142.586 1.00 111.46 ? 3030 MET A N     1 
ATOM   12514 C  CA    . MET A 1 3030 ? 138.778 186.181 142.787 1.00 109.05 ? 3030 MET A CA    1 
ATOM   12515 C  C     . MET A 1 3030 ? 137.832 186.264 141.598 1.00 110.41 ? 3030 MET A C     1 
ATOM   12516 O  O     . MET A 1 3030 ? 136.609 186.349 141.768 1.00 111.93 ? 3030 MET A O     1 
ATOM   12517 C  CB    . MET A 1 3030 ? 139.469 187.529 143.006 1.00 108.83 ? 3030 MET A CB    1 
ATOM   12518 C  CG    . MET A 1 3030 ? 140.255 187.684 144.315 1.00 112.60 ? 3030 MET A CG    1 
ATOM   12519 S  SD    . MET A 1 3030 ? 139.487 187.401 145.932 1.00 125.20 ? 3030 MET A SD    1 
ATOM   12520 C  CE    . MET A 1 3030 ? 137.744 187.636 145.618 1.00 114.45 ? 3030 MET A CE    1 
ATOM   12521 N  N     . THR A 1 3031 ? 138.385 186.236 140.384 1.00 109.30 ? 3031 THR A N     1 
ATOM   12522 C  CA    . THR A 1 3031 ? 137.554 186.298 139.185 1.00 108.67 ? 3031 THR A CA    1 
ATOM   12523 C  C     . THR A 1 3031 ? 136.645 185.078 139.077 1.00 109.33 ? 3031 THR A C     1 
ATOM   12524 O  O     . THR A 1 3031 ? 135.456 185.203 138.753 1.00 108.32 ? 3031 THR A O     1 
ATOM   12525 C  CB    . THR A 1 3031 ? 138.435 186.421 137.942 1.00 107.42 ? 3031 THR A CB    1 
ATOM   12526 O  OG1   . THR A 1 3031 ? 139.265 187.583 138.056 1.00 108.44 ? 3031 THR A OG1   1 
ATOM   12527 C  CG2   . THR A 1 3031 ? 137.578 186.541 136.691 1.00 105.50 ? 3031 THR A CG2   1 
ATOM   12528 N  N     . GLN A 1 3032 ? 137.187 183.888 139.349 1.00 106.38 ? 3032 GLN A N     1 
ATOM   12529 C  CA    . GLN A 1 3032 ? 136.375 182.677 139.281 1.00 103.47 ? 3032 GLN A CA    1 
ATOM   12530 C  C     . GLN A 1 3032 ? 135.273 182.689 140.334 1.00 104.83 ? 3032 GLN A C     1 
ATOM   12531 O  O     . GLN A 1 3032 ? 134.151 182.246 140.069 1.00 103.74 ? 3032 GLN A O     1 
ATOM   12532 C  CB    . GLN A 1 3032 ? 137.258 181.439 139.433 1.00 101.05 ? 3032 GLN A CB    1 
ATOM   12533 C  CG    . GLN A 1 3032 ? 138.296 181.286 138.334 1.00 102.19 ? 3032 GLN A CG    1 
ATOM   12534 C  CD    . GLN A 1 3032 ? 138.704 179.845 138.112 1.00 107.19 ? 3032 GLN A CD    1 
ATOM   12535 O  OE1   . GLN A 1 3032 ? 137.858 178.968 137.940 1.00 108.92 ? 3032 GLN A OE1   1 
ATOM   12536 N  NE2   . GLN A 1 3032 ? 140.007 179.592 138.113 1.00 106.38 ? 3032 GLN A NE2   1 
ATOM   12537 N  N     . CYS A 1 3033 ? 135.572 183.193 141.533 1.00 110.00 ? 3033 CYS A N     1 
ATOM   12538 C  CA    . CYS A 1 3033 ? 134.552 183.293 142.571 1.00 110.34 ? 3033 CYS A CA    1 
ATOM   12539 C  C     . CYS A 1 3033 ? 133.478 184.302 142.192 1.00 112.44 ? 3033 CYS A C     1 
ATOM   12540 O  O     . CYS A 1 3033 ? 132.296 184.095 142.486 1.00 113.95 ? 3033 CYS A O     1 
ATOM   12541 C  CB    . CYS A 1 3033 ? 135.195 183.664 143.905 1.00 110.99 ? 3033 CYS A CB    1 
ATOM   12542 S  SG    . CYS A 1 3033 ? 136.135 182.327 144.667 1.00 121.39 ? 3033 CYS A SG    1 
ATOM   12543 N  N     . LYS A 1 3034 ? 133.867 185.407 141.551 1.00 110.23 ? 3034 LYS A N     1 
ATOM   12544 C  CA    . LYS A 1 3034 ? 132.874 186.362 141.072 1.00 106.20 ? 3034 LYS A CA    1 
ATOM   12545 C  C     . LYS A 1 3034 ? 131.965 185.727 140.028 1.00 108.36 ? 3034 LYS A C     1 
ATOM   12546 O  O     . LYS A 1 3034 ? 130.742 185.914 140.059 1.00 109.48 ? 3034 LYS A O     1 
ATOM   12547 C  CB    . LYS A 1 3034 ? 133.564 187.600 140.501 1.00 106.47 ? 3034 LYS A CB    1 
ATOM   12548 C  CG    . LYS A 1 3034 ? 132.640 188.795 140.327 1.00 109.91 ? 3034 LYS A CG    1 
ATOM   12549 C  CD    . LYS A 1 3034 ? 133.358 189.966 139.675 1.00 109.50 ? 3034 LYS A CD    1 
ATOM   12550 C  CE    . LYS A 1 3034 ? 132.435 191.165 139.530 1.00 109.20 ? 3034 LYS A CE    1 
ATOM   12551 N  NZ    . LYS A 1 3034 ? 131.835 191.567 140.832 1.00 107.95 ? 3034 LYS A NZ    1 
ATOM   12552 N  N     . GLU A 1 3035 ? 132.546 184.961 139.101 1.00 115.46 ? 3035 GLU A N     1 
ATOM   12553 C  CA    . GLU A 1 3035 ? 131.736 184.266 138.103 1.00 114.59 ? 3035 GLU A CA    1 
ATOM   12554 C  C     . GLU A 1 3035 ? 130.803 183.254 138.759 1.00 117.56 ? 3035 GLU A C     1 
ATOM   12555 O  O     . GLU A 1 3035 ? 129.632 183.134 138.376 1.00 121.49 ? 3035 GLU A O     1 
ATOM   12556 C  CB    . GLU A 1 3035 ? 132.642 183.580 137.078 1.00 114.18 ? 3035 GLU A CB    1 
ATOM   12557 C  CG    . GLU A 1 3035 ? 132.012 182.392 136.350 1.00 116.03 ? 3035 GLU A CG    1 
ATOM   12558 C  CD    . GLU A 1 3035 ? 130.902 182.782 135.383 1.00 117.80 ? 3035 GLU A CD    1 
ATOM   12559 O  OE1   . GLU A 1 3035 ? 130.552 183.979 135.299 1.00 118.50 ? 3035 GLU A OE1   1 
ATOM   12560 O  OE2   . GLU A 1 3035 ? 130.373 181.880 134.700 1.00 116.87 ? 3035 GLU A OE2   1 
ATOM   12561 N  N     . GLY A 1 3036 ? 131.302 182.521 139.755 1.00 110.58 ? 3036 GLY A N     1 
ATOM   12562 C  CA    . GLY A 1 3036 ? 130.455 181.571 140.458 1.00 109.41 ? 3036 GLY A CA    1 
ATOM   12563 C  C     . GLY A 1 3036 ? 129.310 182.239 141.194 1.00 108.32 ? 3036 GLY A C     1 
ATOM   12564 O  O     . GLY A 1 3036 ? 128.174 181.762 141.153 1.00 110.40 ? 3036 GLY A O     1 
ATOM   12565 N  N     . ALA A 1 3037 ? 129.591 183.354 141.872 1.00 109.28 ? 3037 ALA A N     1 
ATOM   12566 C  CA    . ALA A 1 3037 ? 128.539 184.091 142.562 1.00 110.03 ? 3037 ALA A CA    1 
ATOM   12567 C  C     . ALA A 1 3037 ? 127.513 184.634 141.577 1.00 114.20 ? 3037 ALA A C     1 
ATOM   12568 O  O     . ALA A 1 3037 ? 126.314 184.666 141.875 1.00 113.11 ? 3037 ALA A O     1 
ATOM   12569 C  CB    . ALA A 1 3037 ? 129.145 185.225 143.388 1.00 112.15 ? 3037 ALA A CB    1 
ATOM   12570 N  N     . GLN A 1 3038 ? 127.968 185.075 140.401 1.00 125.81 ? 3038 GLN A N     1 
ATOM   12571 C  CA    . GLN A 1 3038 ? 127.034 185.474 139.354 1.00 122.54 ? 3038 GLN A CA    1 
ATOM   12572 C  C     . GLN A 1 3038 ? 126.160 184.302 138.929 1.00 121.43 ? 3038 GLN A C     1 
ATOM   12573 O  O     . GLN A 1 3038 ? 124.957 184.466 138.691 1.00 122.33 ? 3038 GLN A O     1 
ATOM   12574 C  CB    . GLN A 1 3038 ? 127.798 186.037 138.156 1.00 121.72 ? 3038 GLN A CB    1 
ATOM   12575 C  CG    . GLN A 1 3038 ? 126.996 187.006 137.304 1.00 123.35 ? 3038 GLN A CG    1 
ATOM   12576 C  CD    . GLN A 1 3038 ? 126.174 187.971 138.135 1.00 125.65 ? 3038 GLN A CD    1 
ATOM   12577 O  OE1   . GLN A 1 3038 ? 126.717 188.848 138.806 1.00 124.49 ? 3038 GLN A OE1   1 
ATOM   12578 N  NE2   . GLN A 1 3038 ? 124.856 187.814 138.092 1.00 126.17 ? 3038 GLN A NE2   1 
ATOM   12579 N  N     . LYS A 1 3039 ? 126.752 183.110 138.820 1.00 119.13 ? 3039 LYS A N     1 
ATOM   12580 C  CA    . LYS A 1 3039 ? 125.974 181.927 138.462 1.00 118.40 ? 3039 LYS A CA    1 
ATOM   12581 C  C     . LYS A 1 3039 ? 124.927 181.607 139.525 1.00 121.04 ? 3039 LYS A C     1 
ATOM   12582 O  O     . LYS A 1 3039 ? 123.786 181.262 139.197 1.00 122.84 ? 3039 LYS A O     1 
ATOM   12583 C  CB    . LYS A 1 3039 ? 126.901 180.732 138.243 1.00 117.96 ? 3039 LYS A CB    1 
ATOM   12584 C  CG    . LYS A 1 3039 ? 127.672 180.783 136.933 1.00 119.69 ? 3039 LYS A CG    1 
ATOM   12585 C  CD    . LYS A 1 3039 ? 128.544 179.551 136.745 1.00 119.06 ? 3039 LYS A CD    1 
ATOM   12586 C  CE    . LYS A 1 3039 ? 127.803 178.280 137.129 1.00 121.81 ? 3039 LYS A CE    1 
ATOM   12587 N  NZ    . LYS A 1 3039 ? 126.939 177.786 136.022 1.00 122.01 ? 3039 LYS A NZ    1 
ATOM   12588 N  N     . GLU A 1 3040 ? 125.295 181.714 140.804 1.00 124.25 ? 3040 GLU A N     1 
ATOM   12589 C  CA    . GLU A 1 3040 ? 124.329 181.497 141.876 1.00 121.95 ? 3040 GLU A CA    1 
ATOM   12590 C  C     . GLU A 1 3040 ? 123.356 182.656 142.033 1.00 123.95 ? 3040 GLU A C     1 
ATOM   12591 O  O     . GLU A 1 3040 ? 122.336 182.503 142.714 1.00 124.20 ? 3040 GLU A O     1 
ATOM   12592 C  CB    . GLU A 1 3040 ? 125.040 181.252 143.211 1.00 122.57 ? 3040 GLU A CB    1 
ATOM   12593 C  CG    . GLU A 1 3040 ? 126.279 180.378 143.129 1.00 125.85 ? 3040 GLU A CG    1 
ATOM   12594 C  CD    . GLU A 1 3040 ? 125.953 178.916 142.900 1.00 126.63 ? 3040 GLU A CD    1 
ATOM   12595 O  OE1   . GLU A 1 3040 ? 124.888 178.462 143.369 1.00 126.80 ? 3040 GLU A OE1   1 
ATOM   12596 O  OE2   . GLU A 1 3040 ? 126.763 178.220 142.253 1.00 125.41 ? 3040 GLU A OE2   1 
ATOM   12597 N  N     . GLY A 1 3041 ? 123.642 183.805 141.427 1.00 125.44 ? 3041 GLY A N     1 
ATOM   12598 C  CA    . GLY A 1 3041 ? 122.752 184.944 141.506 1.00 122.82 ? 3041 GLY A CA    1 
ATOM   12599 C  C     . GLY A 1 3041 ? 123.040 185.922 142.620 1.00 124.51 ? 3041 GLY A C     1 
ATOM   12600 O  O     . GLY A 1 3041 ? 122.186 186.764 142.918 1.00 123.90 ? 3041 GLY A O     1 
ATOM   12601 N  N     . LEU A 1 3042 ? 124.209 185.841 143.246 1.00 122.56 ? 3042 LEU A N     1 
ATOM   12602 C  CA    . LEU A 1 3042 ? 124.578 186.766 144.307 1.00 121.77 ? 3042 LEU A CA    1 
ATOM   12603 C  C     . LEU A 1 3042 ? 125.264 187.997 143.727 1.00 123.24 ? 3042 LEU A C     1 
ATOM   12604 O  O     . LEU A 1 3042 ? 125.894 187.942 142.667 1.00 120.14 ? 3042 LEU A O     1 
ATOM   12605 C  CB    . LEU A 1 3042 ? 125.498 186.087 145.323 1.00 119.88 ? 3042 LEU A CB    1 
ATOM   12606 C  CG    . LEU A 1 3042 ? 124.816 185.397 146.506 1.00 119.18 ? 3042 LEU A CG    1 
ATOM   12607 C  CD1   . LEU A 1 3042 ? 125.820 185.108 147.611 1.00 119.61 ? 3042 LEU A CD1   1 
ATOM   12608 C  CD2   . LEU A 1 3042 ? 123.664 186.238 147.033 1.00 119.40 ? 3042 LEU A CD2   1 
ATOM   12609 N  N     . MET A 1 3043 ? 125.130 189.116 144.436 1.00 131.25 ? 3043 MET A N     1 
ATOM   12610 C  CA    . MET A 1 3043 ? 125.723 190.388 144.026 1.00 130.22 ? 3043 MET A CA    1 
ATOM   12611 C  C     . MET A 1 3043 ? 126.874 190.698 144.977 1.00 130.13 ? 3043 MET A C     1 
ATOM   12612 O  O     . MET A 1 3043 ? 126.692 191.323 146.022 1.00 130.85 ? 3043 MET A O     1 
ATOM   12613 C  CB    . MET A 1 3043 ? 124.679 191.499 144.023 1.00 130.61 ? 3043 MET A CB    1 
ATOM   12614 C  CG    . MET A 1 3043 ? 124.781 192.443 142.836 1.00 130.40 ? 3043 MET A CG    1 
ATOM   12615 S  SD    . MET A 1 3043 ? 123.554 193.764 142.890 1.00 135.90 ? 3043 MET A SD    1 
ATOM   12616 C  CE    . MET A 1 3043 ? 124.594 195.180 143.237 1.00 130.24 ? 3043 MET A CE    1 
ATOM   12617 N  N     . LEU A 1 3044 ? 128.072 190.253 144.607 1.00 116.99 ? 3044 LEU A N     1 
ATOM   12618 C  CA    . LEU A 1 3044 ? 129.277 190.482 145.392 1.00 116.62 ? 3044 LEU A CA    1 
ATOM   12619 C  C     . LEU A 1 3044 ? 130.370 191.026 144.486 1.00 118.52 ? 3044 LEU A C     1 
ATOM   12620 O  O     . LEU A 1 3044 ? 130.589 190.504 143.388 1.00 119.67 ? 3044 LEU A O     1 
ATOM   12621 C  CB    . LEU A 1 3044 ? 129.750 189.194 146.071 1.00 118.24 ? 3044 LEU A CB    1 
ATOM   12622 C  CG    . LEU A 1 3044 ? 128.682 188.288 146.685 1.00 118.66 ? 3044 LEU A CG    1 
ATOM   12623 C  CD1   . LEU A 1 3044 ? 129.274 186.938 147.055 1.00 117.90 ? 3044 LEU A CD1   1 
ATOM   12624 C  CD2   . LEU A 1 3044 ? 128.055 188.951 147.900 1.00 118.88 ? 3044 LEU A CD2   1 
ATOM   12625 N  N     . ASP A 1 3045 ? 131.051 192.066 144.943 1.00 120.55 ? 3045 ASP A N     1 
ATOM   12626 C  CA    . ASP A 1 3045 ? 132.166 192.634 144.194 1.00 120.85 ? 3045 ASP A CA    1 
ATOM   12627 C  C     . ASP A 1 3045 ? 133.436 192.788 145.018 1.00 120.23 ? 3045 ASP A C     1 
ATOM   12628 O  O     . ASP A 1 3045 ? 134.534 192.703 144.463 1.00 118.19 ? 3045 ASP A O     1 
ATOM   12629 C  CB    . ASP A 1 3045 ? 131.723 193.984 143.545 1.00 122.57 ? 3045 ASP A CB    1 
ATOM   12630 C  CG    . ASP A 1 3045 ? 131.911 195.212 144.452 1.00 122.51 ? 3045 ASP A CG    1 
ATOM   12631 O  OD1   . ASP A 1 3045 ? 132.347 195.114 145.618 1.00 120.96 ? 3045 ASP A OD1   1 
ATOM   12632 O  OD2   . ASP A 1 3045 ? 131.610 196.322 143.965 1.00 121.95 ? 3045 ASP A OD2   1 
ATOM   12633 N  N     . SER A 1 3046 ? 133.315 193.014 146.323 1.00 114.35 ? 3046 SER A N     1 
ATOM   12634 C  CA    . SER A 1 3046 ? 134.488 193.145 147.173 1.00 111.09 ? 3046 SER A CA    1 
ATOM   12635 C  C     . SER A 1 3046 ? 135.190 191.802 147.328 1.00 111.49 ? 3046 SER A C     1 
ATOM   12636 O  O     . SER A 1 3046 ? 134.574 190.737 147.240 1.00 116.87 ? 3046 SER A O     1 
ATOM   12637 C  CB    . SER A 1 3046 ? 134.097 193.693 148.545 1.00 109.48 ? 3046 SER A CB    1 
ATOM   12638 O  OG    . SER A 1 3046 ? 135.205 193.693 149.426 1.00 110.86 ? 3046 SER A OG    1 
ATOM   12639 N  N     . HIS A 1 3047 ? 136.503 191.862 147.554 1.00 103.89 ? 3047 HIS A N     1 
ATOM   12640 C  CA    . HIS A 1 3047 ? 137.272 190.634 147.717 1.00 106.03 ? 3047 HIS A CA    1 
ATOM   12641 C  C     . HIS A 1 3047 ? 136.924 189.931 149.023 1.00 106.68 ? 3047 HIS A C     1 
ATOM   12642 O  O     . HIS A 1 3047 ? 136.958 188.698 149.096 1.00 110.25 ? 3047 HIS A O     1 
ATOM   12643 C  CB    . HIS A 1 3047 ? 138.767 190.939 147.646 1.00 106.19 ? 3047 HIS A CB    1 
ATOM   12644 C  CG    . HIS A 1 3047 ? 139.218 191.433 146.307 1.00 108.15 ? 3047 HIS A CG    1 
ATOM   12645 N  ND1   . HIS A 1 3047 ? 139.014 190.722 145.145 1.00 108.07 ? 3047 HIS A ND1   1 
ATOM   12646 C  CD2   . HIS A 1 3047 ? 139.864 192.567 145.946 1.00 110.48 ? 3047 HIS A CD2   1 
ATOM   12647 C  CE1   . HIS A 1 3047 ? 139.513 191.397 144.125 1.00 108.72 ? 3047 HIS A CE1   1 
ATOM   12648 N  NE2   . HIS A 1 3047 ? 140.035 192.520 144.584 1.00 112.47 ? 3047 HIS A NE2   1 
ATOM   12649 N  N     . GLU A 1 3048 ? 136.581 190.694 150.063 1.00 107.09 ? 3048 GLU A N     1 
ATOM   12650 C  CA    . GLU A 1 3048 ? 136.274 190.090 151.356 1.00 105.62 ? 3048 GLU A CA    1 
ATOM   12651 C  C     . GLU A 1 3048 ? 134.997 189.258 151.294 1.00 109.95 ? 3048 GLU A C     1 
ATOM   12652 O  O     . GLU A 1 3048 ? 134.976 188.100 151.729 1.00 112.15 ? 3048 GLU A O     1 
ATOM   12653 C  CB    . GLU A 1 3048 ? 136.160 191.176 152.425 1.00 106.28 ? 3048 GLU A CB    1 
ATOM   12654 C  CG    . GLU A 1 3048 ? 137.223 192.256 152.318 1.00 113.68 ? 3048 GLU A CG    1 
ATOM   12655 C  CD    . GLU A 1 3048 ? 137.332 193.095 153.574 1.00 115.20 ? 3048 GLU A CD    1 
ATOM   12656 O  OE1   . GLU A 1 3048 ? 136.521 194.031 153.738 1.00 113.54 ? 3048 GLU A OE1   1 
ATOM   12657 O  OE2   . GLU A 1 3048 ? 138.228 192.817 154.399 1.00 114.10 ? 3048 GLU A OE2   1 
ATOM   12658 N  N     . GLU A 1 3049 ? 133.918 189.834 150.756 1.00 110.43 ? 3049 GLU A N     1 
ATOM   12659 C  CA    . GLU A 1 3049 ? 132.661 189.098 150.666 1.00 107.85 ? 3049 GLU A CA    1 
ATOM   12660 C  C     . GLU A 1 3049 ? 132.786 187.903 149.728 1.00 105.56 ? 3049 GLU A C     1 
ATOM   12661 O  O     . GLU A 1 3049 ? 132.239 186.829 150.005 1.00 107.24 ? 3049 GLU A O     1 
ATOM   12662 C  CB    . GLU A 1 3049 ? 131.535 190.027 150.210 1.00 106.65 ? 3049 GLU A CB    1 
ATOM   12663 C  CG    . GLU A 1 3049 ? 131.836 190.803 148.939 1.00 110.83 ? 3049 GLU A CG    1 
ATOM   12664 C  CD    . GLU A 1 3049 ? 131.038 192.087 148.834 1.00 113.18 ? 3049 GLU A CD    1 
ATOM   12665 O  OE1   . GLU A 1 3049 ? 131.059 192.713 147.754 1.00 111.16 ? 3049 GLU A OE1   1 
ATOM   12666 O  OE2   . GLU A 1 3049 ? 130.391 192.469 149.831 1.00 114.17 ? 3049 GLU A OE2   1 
ATOM   12667 N  N     . LEU A 1 3050 ? 133.502 188.071 148.615 1.00 96.51  ? 3050 LEU A N     1 
ATOM   12668 C  CA    . LEU A 1 3050 ? 133.698 186.960 147.691 1.00 100.51 ? 3050 LEU A CA    1 
ATOM   12669 C  C     . LEU A 1 3050 ? 134.502 185.839 148.336 1.00 102.18 ? 3050 LEU A C     1 
ATOM   12670 O  O     . LEU A 1 3050 ? 134.194 184.658 148.144 1.00 108.92 ? 3050 LEU A O     1 
ATOM   12671 C  CB    . LEU A 1 3050 ? 134.383 187.451 146.418 1.00 95.88  ? 3050 LEU A CB    1 
ATOM   12672 C  CG    . LEU A 1 3050 ? 133.484 187.967 145.297 1.00 96.79  ? 3050 LEU A CG    1 
ATOM   12673 C  CD1   . LEU A 1 3050 ? 134.307 188.262 144.057 1.00 100.73 ? 3050 LEU A CD1   1 
ATOM   12674 C  CD2   . LEU A 1 3050 ? 132.400 186.950 144.986 1.00 99.44  ? 3050 LEU A CD2   1 
ATOM   12675 N  N     . TYR A 1 3051 ? 135.536 186.184 149.106 1.00 85.65  ? 3051 TYR A N     1 
ATOM   12676 C  CA    . TYR A 1 3051 ? 136.313 185.154 149.786 1.00 84.81  ? 3051 TYR A CA    1 
ATOM   12677 C  C     . TYR A 1 3051 ? 135.487 184.457 150.860 1.00 90.35  ? 3051 TYR A C     1 
ATOM   12678 O  O     . TYR A 1 3051 ? 135.624 183.246 151.063 1.00 94.97  ? 3051 TYR A O     1 
ATOM   12679 C  CB    . TYR A 1 3051 ? 137.580 185.752 150.392 1.00 86.26  ? 3051 TYR A CB    1 
ATOM   12680 C  CG    . TYR A 1 3051 ? 138.636 184.718 150.702 1.00 84.26  ? 3051 TYR A CG    1 
ATOM   12681 C  CD1   . TYR A 1 3051 ? 139.331 184.081 149.682 1.00 87.01  ? 3051 TYR A CD1   1 
ATOM   12682 C  CD2   . TYR A 1 3051 ? 138.931 184.368 152.012 1.00 83.52  ? 3051 TYR A CD2   1 
ATOM   12683 C  CE1   . TYR A 1 3051 ? 140.295 183.132 149.959 1.00 87.17  ? 3051 TYR A CE1   1 
ATOM   12684 C  CE2   . TYR A 1 3051 ? 139.893 183.419 152.299 1.00 83.19  ? 3051 TYR A CE2   1 
ATOM   12685 C  CZ    . TYR A 1 3051 ? 140.571 182.805 151.269 1.00 85.56  ? 3051 TYR A CZ    1 
ATOM   12686 O  OH    . TYR A 1 3051 ? 141.531 181.859 151.548 1.00 84.82  ? 3051 TYR A OH    1 
ATOM   12687 N  N     . LYS A 1 3052 ? 134.632 185.202 151.564 1.00 86.05  ? 3052 LYS A N     1 
ATOM   12688 C  CA    . LYS A 1 3052 ? 133.747 184.571 152.539 1.00 84.12  ? 3052 LYS A CA    1 
ATOM   12689 C  C     . LYS A 1 3052 ? 132.781 183.607 151.860 1.00 87.32  ? 3052 LYS A C     1 
ATOM   12690 O  O     . LYS A 1 3052 ? 132.530 182.505 152.365 1.00 93.84  ? 3052 LYS A O     1 
ATOM   12691 C  CB    . LYS A 1 3052 ? 132.981 185.635 153.324 1.00 88.15  ? 3052 LYS A CB    1 
ATOM   12692 C  CG    . LYS A 1 3052 ? 133.840 186.428 154.293 1.00 90.29  ? 3052 LYS A CG    1 
ATOM   12693 C  CD    . LYS A 1 3052 ? 133.030 187.515 154.979 1.00 89.92  ? 3052 LYS A CD    1 
ATOM   12694 C  CE    . LYS A 1 3052 ? 133.905 188.372 155.877 1.00 91.29  ? 3052 LYS A CE    1 
ATOM   12695 N  NZ    . LYS A 1 3052 ? 133.133 189.477 156.509 1.00 93.08  ? 3052 LYS A NZ    1 
ATOM   12696 N  N     . TRP A 1 3053 ? 132.232 184.005 150.711 1.00 76.90  ? 3053 TRP A N     1 
ATOM   12697 C  CA    . TRP A 1 3053 ? 131.356 183.111 149.960 1.00 77.76  ? 3053 TRP A CA    1 
ATOM   12698 C  C     . TRP A 1 3053 ? 132.108 181.873 149.489 1.00 81.66  ? 3053 TRP A C     1 
ATOM   12699 O  O     . TRP A 1 3053 ? 131.572 180.760 149.522 1.00 91.25  ? 3053 TRP A O     1 
ATOM   12700 C  CB    . TRP A 1 3053 ? 130.742 183.853 148.773 1.00 78.57  ? 3053 TRP A CB    1 
ATOM   12701 C  CG    . TRP A 1 3053 ? 130.016 182.961 147.817 1.00 76.12  ? 3053 TRP A CG    1 
ATOM   12702 C  CD1   . TRP A 1 3053 ? 128.712 182.571 147.891 1.00 76.49  ? 3053 TRP A CD1   1 
ATOM   12703 C  CD2   . TRP A 1 3053 ? 130.553 182.347 146.640 1.00 76.53  ? 3053 TRP A CD2   1 
ATOM   12704 N  NE1   . TRP A 1 3053 ? 128.402 181.752 146.833 1.00 77.66  ? 3053 TRP A NE1   1 
ATOM   12705 C  CE2   . TRP A 1 3053 ? 129.516 181.599 146.050 1.00 79.34  ? 3053 TRP A CE2   1 
ATOM   12706 C  CE3   . TRP A 1 3053 ? 131.809 182.357 146.027 1.00 80.66  ? 3053 TRP A CE3   1 
ATOM   12707 C  CZ2   . TRP A 1 3053 ? 129.696 180.868 144.879 1.00 82.62  ? 3053 TRP A CZ2   1 
ATOM   12708 C  CZ3   . TRP A 1 3053 ? 131.986 181.631 144.865 1.00 85.19  ? 3053 TRP A CZ3   1 
ATOM   12709 C  CH2   . TRP A 1 3053 ? 130.936 180.897 144.303 1.00 83.94  ? 3053 TRP A CH2   1 
ATOM   12710 N  N     . PHE A 1 3054 ? 133.351 182.052 149.036 1.00 70.55  ? 3054 PHE A N     1 
ATOM   12711 C  CA    . PHE A 1 3054 ? 134.167 180.916 148.622 1.00 70.46  ? 3054 PHE A CA    1 
ATOM   12712 C  C     . PHE A 1 3054 ? 134.419 179.966 149.785 1.00 75.64  ? 3054 PHE A C     1 
ATOM   12713 O  O     . PHE A 1 3054 ? 134.353 178.742 149.622 1.00 84.59  ? 3054 PHE A O     1 
ATOM   12714 C  CB    . PHE A 1 3054 ? 135.489 181.412 148.038 1.00 67.90  ? 3054 PHE A CB    1 
ATOM   12715 C  CG    . PHE A 1 3054 ? 136.494 180.325 147.796 1.00 73.30  ? 3054 PHE A CG    1 
ATOM   12716 C  CD1   . PHE A 1 3054 ? 136.341 179.443 146.741 1.00 73.75  ? 3054 PHE A CD1   1 
ATOM   12717 C  CD2   . PHE A 1 3054 ? 137.597 180.189 148.621 1.00 75.27  ? 3054 PHE A CD2   1 
ATOM   12718 C  CE1   . PHE A 1 3054 ? 137.266 178.444 146.517 1.00 73.91  ? 3054 PHE A CE1   1 
ATOM   12719 C  CE2   . PHE A 1 3054 ? 138.526 179.193 148.401 1.00 75.50  ? 3054 PHE A CE2   1 
ATOM   12720 C  CZ    . PHE A 1 3054 ? 138.360 178.320 147.348 1.00 76.35  ? 3054 PHE A CZ    1 
ATOM   12721 N  N     . THR A 1 3055 ? 134.718 180.512 150.965 1.00 68.55  ? 3055 THR A N     1 
ATOM   12722 C  CA    . THR A 1 3055 ? 134.926 179.675 152.141 1.00 65.13  ? 3055 THR A CA    1 
ATOM   12723 C  C     . THR A 1 3055 ? 133.659 178.909 152.499 1.00 64.52  ? 3055 THR A C     1 
ATOM   12724 O  O     . THR A 1 3055 ? 133.714 177.718 152.827 1.00 76.02  ? 3055 THR A O     1 
ATOM   12725 C  CB    . THR A 1 3055 ? 135.389 180.532 153.319 1.00 69.21  ? 3055 THR A CB    1 
ATOM   12726 O  OG1   . THR A 1 3055 ? 136.694 181.055 153.047 1.00 76.15  ? 3055 THR A OG1   1 
ATOM   12727 C  CG2   . THR A 1 3055 ? 135.438 179.710 154.595 1.00 71.33  ? 3055 THR A CG2   1 
ATOM   12728 N  N     . SER A 1 3056 ? 132.504 179.576 152.433 1.00 73.62  ? 3056 SER A N     1 
ATOM   12729 C  CA    . SER A 1 3056 ? 131.244 178.895 152.717 1.00 77.88  ? 3056 SER A CA    1 
ATOM   12730 C  C     . SER A 1 3056 ? 130.984 177.778 151.714 1.00 81.53  ? 3056 SER A C     1 
ATOM   12731 O  O     . SER A 1 3056 ? 130.535 176.688 152.090 1.00 84.37  ? 3056 SER A O     1 
ATOM   12732 C  CB    . SER A 1 3056 ? 130.091 179.897 152.713 1.00 77.29  ? 3056 SER A CB    1 
ATOM   12733 O  OG    . SER A 1 3056 ? 129.805 180.335 151.397 1.00 85.92  ? 3056 SER A OG    1 
ATOM   12734 N  N     . GLN A 1 3057 ? 131.261 178.028 150.433 1.00 69.26  ? 3057 GLN A N     1 
ATOM   12735 C  CA    . GLN A 1 3057 ? 131.065 176.998 149.418 1.00 68.88  ? 3057 GLN A CA    1 
ATOM   12736 C  C     . GLN A 1 3057 ? 131.997 175.814 149.641 1.00 77.58  ? 3057 GLN A C     1 
ATOM   12737 O  O     . GLN A 1 3057 ? 131.589 174.656 149.489 1.00 81.54  ? 3057 GLN A O     1 
ATOM   12738 C  CB    . GLN A 1 3057 ? 131.271 177.587 148.024 1.00 63.43  ? 3057 GLN A CB    1 
ATOM   12739 C  CG    . GLN A 1 3057 ? 130.148 178.497 147.570 1.00 72.61  ? 3057 GLN A CG    1 
ATOM   12740 C  CD    . GLN A 1 3057 ? 128.843 177.755 147.381 1.00 77.67  ? 3057 GLN A CD    1 
ATOM   12741 O  OE1   . GLN A 1 3057 ? 127.918 177.890 148.181 1.00 80.92  ? 3057 GLN A OE1   1 
ATOM   12742 N  NE2   . GLN A 1 3057 ? 128.760 176.966 146.316 1.00 77.71  ? 3057 GLN A NE2   1 
ATOM   12743 N  N     . VAL A 1 3058 ? 133.256 176.082 149.994 1.00 64.99  ? 3058 VAL A N     1 
ATOM   12744 C  CA    . VAL A 1 3058 ? 134.196 174.998 150.267 1.00 52.70  ? 3058 VAL A CA    1 
ATOM   12745 C  C     . VAL A 1 3058 ? 133.733 174.186 151.468 1.00 60.29  ? 3058 VAL A C     1 
ATOM   12746 O  O     . VAL A 1 3058 ? 133.808 172.951 151.468 1.00 73.35  ? 3058 VAL A O     1 
ATOM   12747 C  CB    . VAL A 1 3058 ? 135.616 175.555 150.471 1.00 52.49  ? 3058 VAL A CB    1 
ATOM   12748 C  CG1   . VAL A 1 3058 ? 136.535 174.474 151.009 1.00 56.83  ? 3058 VAL A CG1   1 
ATOM   12749 C  CG2   . VAL A 1 3058 ? 136.158 176.104 149.166 1.00 65.27  ? 3058 VAL A CG2   1 
ATOM   12750 N  N     . ILE A 1 3059 ? 133.244 174.862 152.508 1.00 61.25  ? 3059 ILE A N     1 
ATOM   12751 C  CA    . ILE A 1 3059 ? 132.726 174.156 153.675 1.00 58.23  ? 3059 ILE A CA    1 
ATOM   12752 C  C     . ILE A 1 3059 ? 131.544 173.278 153.284 1.00 65.44  ? 3059 ILE A C     1 
ATOM   12753 O  O     . ILE A 1 3059 ? 131.440 172.121 153.709 1.00 70.43  ? 3059 ILE A O     1 
ATOM   12754 C  CB    . ILE A 1 3059 ? 132.348 175.161 154.779 1.00 59.13  ? 3059 ILE A CB    1 
ATOM   12755 C  CG1   . ILE A 1 3059 ? 133.601 175.646 155.510 1.00 62.36  ? 3059 ILE A CG1   1 
ATOM   12756 C  CG2   . ILE A 1 3059 ? 131.364 174.544 155.759 1.00 66.31  ? 3059 ILE A CG2   1 
ATOM   12757 C  CD1   . ILE A 1 3059 ? 133.333 176.740 156.519 1.00 65.90  ? 3059 ILE A CD1   1 
ATOM   12758 N  N     . ARG A 1 3060 ? 130.644 173.806 152.454 1.00 62.72  ? 3060 ARG A N     1 
ATOM   12759 C  CA    . ARG A 1 3060 ? 129.435 173.080 152.088 1.00 65.76  ? 3060 ARG A CA    1 
ATOM   12760 C  C     . ARG A 1 3060 ? 129.684 171.942 151.106 1.00 71.64  ? 3060 ARG A C     1 
ATOM   12761 O  O     . ARG A 1 3060 ? 128.886 171.000 151.064 1.00 73.65  ? 3060 ARG A O     1 
ATOM   12762 C  CB    . ARG A 1 3060 ? 128.408 174.043 151.490 1.00 65.63  ? 3060 ARG A CB    1 
ATOM   12763 C  CG    . ARG A 1 3060 ? 126.972 173.733 151.869 1.00 73.49  ? 3060 ARG A CG    1 
ATOM   12764 C  CD    . ARG A 1 3060 ? 126.016 174.768 151.300 1.00 76.01  ? 3060 ARG A CD    1 
ATOM   12765 N  NE    . ARG A 1 3060 ? 126.378 175.158 149.943 1.00 71.68  ? 3060 ARG A NE    1 
ATOM   12766 C  CZ    . ARG A 1 3060 ? 126.026 174.490 148.853 1.00 76.41  ? 3060 ARG A CZ    1 
ATOM   12767 N  NH1   . ARG A 1 3060 ? 125.298 173.388 148.923 1.00 77.54  ? 3060 ARG A NH1   1 
ATOM   12768 N  NH2   . ARG A 1 3060 ? 126.413 174.941 147.663 1.00 74.75  ? 3060 ARG A NH2   1 
ATOM   12769 N  N     . ASN A 1 3061 ? 130.759 171.997 150.320 1.00 70.75  ? 3061 ASN A N     1 
ATOM   12770 C  CA    . ASN A 1 3061 ? 130.950 171.046 149.231 1.00 65.80  ? 3061 ASN A CA    1 
ATOM   12771 C  C     . ASN A 1 3061 ? 132.111 170.083 149.423 1.00 62.76  ? 3061 ASN A C     1 
ATOM   12772 O  O     . ASN A 1 3061 ? 132.064 168.976 148.885 1.00 67.95  ? 3061 ASN A O     1 
ATOM   12773 C  CB    . ASN A 1 3061 ? 131.155 171.792 147.906 1.00 61.74  ? 3061 ASN A CB    1 
ATOM   12774 C  CG    . ASN A 1 3061 ? 129.886 172.446 147.404 1.00 69.96  ? 3061 ASN A CG    1 
ATOM   12775 O  OD1   . ASN A 1 3061 ? 128.799 171.881 147.511 1.00 75.01  ? 3061 ASN A OD1   1 
ATOM   12776 N  ND2   . ASN A 1 3061 ? 130.019 173.643 146.848 1.00 70.84  ? 3061 ASN A ND2   1 
ATOM   12777 N  N     . LEU A 1 3062 ? 133.147 170.462 150.164 1.00 53.71  ? 3062 LEU A N     1 
ATOM   12778 C  CA    . LEU A 1 3062 ? 134.351 169.648 150.264 1.00 53.78  ? 3062 LEU A CA    1 
ATOM   12779 C  C     . LEU A 1 3062 ? 134.276 168.715 151.465 1.00 62.88  ? 3062 LEU A C     1 
ATOM   12780 O  O     . LEU A 1 3062 ? 134.063 169.161 152.596 1.00 67.59  ? 3062 LEU A O     1 
ATOM   12781 C  CB    . LEU A 1 3062 ? 135.593 170.534 150.368 1.00 53.51  ? 3062 LEU A CB    1 
ATOM   12782 C  CG    . LEU A 1 3062 ? 136.925 169.792 150.474 1.00 52.91  ? 3062 LEU A CG    1 
ATOM   12783 C  CD1   . LEU A 1 3062 ? 137.087 168.818 149.321 1.00 59.15  ? 3062 LEU A CD1   1 
ATOM   12784 C  CD2   . LEU A 1 3062 ? 138.084 170.770 150.518 1.00 55.94  ? 3062 LEU A CD2   1 
ATOM   12785 N  N     . HIS A 1 3063 ? 134.456 167.419 151.211 1.00 56.72  ? 3063 HIS A N     1 
ATOM   12786 C  CA    . HIS A 1 3063 ? 134.569 166.403 152.253 1.00 50.75  ? 3063 HIS A CA    1 
ATOM   12787 C  C     . HIS A 1 3063 ? 135.932 165.739 152.113 1.00 50.46  ? 3063 HIS A C     1 
ATOM   12788 O  O     . HIS A 1 3063 ? 136.329 165.357 151.007 1.00 59.77  ? 3063 HIS A O     1 
ATOM   12789 C  CB    . HIS A 1 3063 ? 133.448 165.371 152.151 1.00 42.81  ? 3063 HIS A CB    1 
ATOM   12790 C  CG    . HIS A 1 3063 ? 132.075 165.964 152.155 1.00 51.24  ? 3063 HIS A CG    1 
ATOM   12791 N  ND1   . HIS A 1 3063 ? 131.334 166.129 151.006 1.00 59.46  ? 3063 HIS A ND1   1 
ATOM   12792 C  CD2   . HIS A 1 3063 ? 131.307 166.428 153.168 1.00 56.98  ? 3063 HIS A CD2   1 
ATOM   12793 C  CE1   . HIS A 1 3063 ? 130.168 166.669 151.310 1.00 59.38  ? 3063 HIS A CE1   1 
ATOM   12794 N  NE2   . HIS A 1 3063 ? 130.126 166.860 152.616 1.00 63.40  ? 3063 HIS A NE2   1 
ATOM   12795 N  N     . VAL A 1 3064 ? 136.646 165.604 153.224 1.00 50.29  ? 3064 VAL A N     1 
ATOM   12796 C  CA    . VAL A 1 3064 ? 137.969 164.992 153.241 1.00 46.23  ? 3064 VAL A CA    1 
ATOM   12797 C  C     . VAL A 1 3064 ? 137.868 163.657 153.965 1.00 52.48  ? 3064 VAL A C     1 
ATOM   12798 O  O     . VAL A 1 3064 ? 137.416 163.599 155.115 1.00 68.55  ? 3064 VAL A O     1 
ATOM   12799 C  CB    . VAL A 1 3064 ? 139.002 165.908 153.912 1.00 48.51  ? 3064 VAL A CB    1 
ATOM   12800 C  CG1   . VAL A 1 3064 ? 140.323 165.180 154.083 1.00 52.96  ? 3064 VAL A CG1   1 
ATOM   12801 C  CG2   . VAL A 1 3064 ? 139.190 167.178 153.101 1.00 57.51  ? 3064 VAL A CG2   1 
ATOM   12802 N  N     . VAL A 1 3065 ? 138.290 162.588 153.298 1.00 43.53  ? 3065 VAL A N     1 
ATOM   12803 C  CA    . VAL A 1 3065 ? 138.279 161.243 153.861 1.00 37.48  ? 3065 VAL A CA    1 
ATOM   12804 C  C     . VAL A 1 3065 ? 139.726 160.840 154.101 1.00 44.63  ? 3065 VAL A C     1 
ATOM   12805 O  O     . VAL A 1 3065 ? 140.480 160.600 153.150 1.00 57.55  ? 3065 VAL A O     1 
ATOM   12806 C  CB    . VAL A 1 3065 ? 137.570 160.244 152.939 1.00 40.92  ? 3065 VAL A CB    1 
ATOM   12807 C  CG1   . VAL A 1 3065 ? 137.404 158.908 153.637 1.00 55.47  ? 3065 VAL A CG1   1 
ATOM   12808 C  CG2   . VAL A 1 3065 ? 136.223 160.792 152.505 1.00 41.14  ? 3065 VAL A CG2   1 
ATOM   12809 N  N     . PHE A 1 3066 ? 140.116 160.758 155.368 1.00 54.83  ? 3066 PHE A N     1 
ATOM   12810 C  CA    . PHE A 1 3066 ? 141.484 160.437 155.747 1.00 51.30  ? 3066 PHE A CA    1 
ATOM   12811 C  C     . PHE A 1 3066 ? 141.558 158.987 156.207 1.00 59.23  ? 3066 PHE A C     1 
ATOM   12812 O  O     . PHE A 1 3066 ? 140.822 158.580 157.112 1.00 66.10  ? 3066 PHE A O     1 
ATOM   12813 C  CB    . PHE A 1 3066 ? 141.973 161.371 156.854 1.00 52.17  ? 3066 PHE A CB    1 
ATOM   12814 C  CG    . PHE A 1 3066 ? 143.463 161.547 156.882 1.00 61.93  ? 3066 PHE A CG    1 
ATOM   12815 C  CD1   . PHE A 1 3066 ? 144.057 162.619 156.240 1.00 65.70  ? 3066 PHE A CD1   1 
ATOM   12816 C  CD2   . PHE A 1 3066 ? 144.270 160.638 157.543 1.00 68.80  ? 3066 PHE A CD2   1 
ATOM   12817 C  CE1   . PHE A 1 3066 ? 145.428 162.784 156.261 1.00 71.15  ? 3066 PHE A CE1   1 
ATOM   12818 C  CE2   . PHE A 1 3066 ? 145.642 160.797 157.567 1.00 69.30  ? 3066 PHE A CE2   1 
ATOM   12819 C  CZ    . PHE A 1 3066 ? 146.221 161.871 156.925 1.00 69.28  ? 3066 PHE A CZ    1 
ATOM   12820 N  N     . THR A 1 3067 ? 142.443 158.215 155.584 1.00 65.32  ? 3067 THR A N     1 
ATOM   12821 C  CA    . THR A 1 3067 ? 142.632 156.809 155.910 1.00 58.22  ? 3067 THR A CA    1 
ATOM   12822 C  C     . THR A 1 3067 ? 144.042 156.593 156.440 1.00 68.74  ? 3067 THR A C     1 
ATOM   12823 O  O     . THR A 1 3067 ? 145.010 157.123 155.887 1.00 80.92  ? 3067 THR A O     1 
ATOM   12824 C  CB    . THR A 1 3067 ? 142.396 155.915 154.689 1.00 57.36  ? 3067 THR A CB    1 
ATOM   12825 O  OG1   . THR A 1 3067 ? 143.479 156.071 153.765 1.00 71.03  ? 3067 THR A OG1   1 
ATOM   12826 C  CG2   . THR A 1 3067 ? 141.095 156.287 153.999 1.00 60.61  ? 3067 THR A CG2   1 
ATOM   12827 N  N     . MET A 1 3068 ? 144.153 155.812 157.512 1.00 71.33  ? 3068 MET A N     1 
ATOM   12828 C  CA    . MET A 1 3068 ? 145.445 155.550 158.126 1.00 68.60  ? 3068 MET A CA    1 
ATOM   12829 C  C     . MET A 1 3068 ? 145.411 154.196 158.819 1.00 74.04  ? 3068 MET A C     1 
ATOM   12830 O  O     . MET A 1 3068 ? 144.344 153.649 159.106 1.00 80.36  ? 3068 MET A O     1 
ATOM   12831 C  CB    . MET A 1 3068 ? 145.827 156.650 159.122 1.00 59.61  ? 3068 MET A CB    1 
ATOM   12832 C  CG    . MET A 1 3068 ? 145.175 156.503 160.484 1.00 70.52  ? 3068 MET A CG    1 
ATOM   12833 S  SD    . MET A 1 3068 ? 145.831 157.663 161.696 1.00 93.01  ? 3068 MET A SD    1 
ATOM   12834 C  CE    . MET A 1 3068 ? 145.824 159.181 160.748 1.00 74.55  ? 3068 MET A CE    1 
ATOM   12835 N  N     . ASN A 1 3069 ? 146.602 153.661 159.080 1.00 77.88  ? 3069 ASN A N     1 
ATOM   12836 C  CA    . ASN A 1 3069 ? 146.742 152.385 159.761 1.00 73.82  ? 3069 ASN A CA    1 
ATOM   12837 C  C     . ASN A 1 3069 ? 146.559 152.557 161.268 1.00 76.06  ? 3069 ASN A C     1 
ATOM   12838 O  O     . ASN A 1 3069 ? 146.879 153.612 161.823 1.00 78.35  ? 3069 ASN A O     1 
ATOM   12839 C  CB    . ASN A 1 3069 ? 148.110 151.779 159.472 1.00 74.86  ? 3069 ASN A CB    1 
ATOM   12840 C  CG    . ASN A 1 3069 ? 148.118 150.935 158.215 1.00 77.89  ? 3069 ASN A CG    1 
ATOM   12841 O  OD1   . ASN A 1 3069 ? 147.361 149.973 158.095 1.00 76.34  ? 3069 ASN A OD1   1 
ATOM   12842 N  ND2   . ASN A 1 3069 ? 148.973 151.295 157.266 1.00 79.34  ? 3069 ASN A ND2   1 
ATOM   12843 N  N     . PRO A 1 3070 ? 146.051 151.531 161.956 1.00 85.78  ? 3070 PRO A N     1 
ATOM   12844 C  CA    . PRO A 1 3070 ? 145.796 151.640 163.404 1.00 89.29  ? 3070 PRO A CA    1 
ATOM   12845 C  C     . PRO A 1 3070 ? 147.067 151.509 164.238 1.00 95.98  ? 3070 PRO A C     1 
ATOM   12846 O  O     . PRO A 1 3070 ? 147.201 150.624 165.087 1.00 96.04  ? 3070 PRO A O     1 
ATOM   12847 C  CB    . PRO A 1 3070 ? 144.812 150.489 163.646 1.00 85.55  ? 3070 PRO A CB    1 
ATOM   12848 C  CG    . PRO A 1 3070 ? 145.190 149.469 162.641 1.00 89.72  ? 3070 PRO A CG    1 
ATOM   12849 C  CD    . PRO A 1 3070 ? 145.628 150.227 161.417 1.00 88.88  ? 3070 PRO A CD    1 
ATOM   12850 N  N     . SER A 1 3071 ? 148.019 152.404 163.995 1.00 111.55 ? 3071 SER A N     1 
ATOM   12851 C  CA    . SER A 1 3071 ? 149.251 152.421 164.767 1.00 112.66 ? 3071 SER A CA    1 
ATOM   12852 C  C     . SER A 1 3071 ? 149.000 152.993 166.157 1.00 114.09 ? 3071 SER A C     1 
ATOM   12853 O  O     . SER A 1 3071 ? 148.139 153.855 166.353 1.00 110.44 ? 3071 SER A O     1 
ATOM   12854 C  CB    . SER A 1 3071 ? 150.325 153.239 164.049 1.00 112.21 ? 3071 SER A CB    1 
ATOM   12855 O  OG    . SER A 1 3071 ? 151.514 153.305 164.817 1.00 115.44 ? 3071 SER A OG    1 
ATOM   12856 N  N     . SER A 1 3072 ? 149.766 152.499 167.131 1.00 119.00 ? 3072 SER A N     1 
ATOM   12857 C  CA    . SER A 1 3072 ? 149.599 152.947 168.510 1.00 116.64 ? 3072 SER A CA    1 
ATOM   12858 C  C     . SER A 1 3072 ? 150.215 154.326 168.722 1.00 114.54 ? 3072 SER A C     1 
ATOM   12859 O  O     . SER A 1 3072 ? 149.520 155.280 169.088 1.00 113.52 ? 3072 SER A O     1 
ATOM   12860 C  CB    . SER A 1 3072 ? 150.214 151.927 169.471 1.00 117.26 ? 3072 SER A CB    1 
ATOM   12861 O  OG    . SER A 1 3072 ? 149.679 150.633 169.255 1.00 114.57 ? 3072 SER A OG    1 
ATOM   12862 N  N     . GLU A 1 3073 ? 151.525 154.448 168.497 1.00 116.10 ? 3073 GLU A N     1 
ATOM   12863 C  CA    . GLU A 1 3073 ? 152.187 155.735 168.678 1.00 117.75 ? 3073 GLU A CA    1 
ATOM   12864 C  C     . GLU A 1 3073 ? 151.858 156.701 167.548 1.00 119.55 ? 3073 GLU A C     1 
ATOM   12865 O  O     . GLU A 1 3073 ? 151.914 157.921 167.741 1.00 122.18 ? 3073 GLU A O     1 
ATOM   12866 C  CB    . GLU A 1 3073 ? 153.700 155.525 168.818 1.00 117.23 ? 3073 GLU A CB    1 
ATOM   12867 C  CG    . GLU A 1 3073 ? 154.404 154.870 167.623 1.00 118.15 ? 3073 GLU A CG    1 
ATOM   12868 C  CD    . GLU A 1 3073 ? 154.669 155.814 166.461 1.00 119.43 ? 3073 GLU A CD    1 
ATOM   12869 O  OE1   . GLU A 1 3073 ? 155.049 155.323 165.377 1.00 120.40 ? 3073 GLU A OE1   1 
ATOM   12870 O  OE2   . GLU A 1 3073 ? 154.543 157.044 166.636 1.00 118.42 ? 3073 GLU A OE2   1 
ATOM   12871 N  N     . GLY A 1 3074 ? 151.521 156.179 166.366 1.00 108.70 ? 3074 GLY A N     1 
ATOM   12872 C  CA    . GLY A 1 3074 ? 151.160 157.052 165.261 1.00 107.40 ? 3074 GLY A CA    1 
ATOM   12873 C  C     . GLY A 1 3074 ? 149.910 157.861 165.544 1.00 109.41 ? 3074 GLY A C     1 
ATOM   12874 O  O     . GLY A 1 3074 ? 149.842 159.050 165.224 1.00 108.68 ? 3074 GLY A O     1 
ATOM   12875 N  N     . LEU A 1 3075 ? 148.904 157.229 166.152 1.00 103.68 ? 3075 LEU A N     1 
ATOM   12876 C  CA    . LEU A 1 3075 ? 147.688 157.951 166.512 1.00 102.09 ? 3075 LEU A CA    1 
ATOM   12877 C  C     . LEU A 1 3075 ? 147.972 159.023 167.557 1.00 100.12 ? 3075 LEU A C     1 
ATOM   12878 O  O     . LEU A 1 3075 ? 147.443 160.138 167.473 1.00 99.85  ? 3075 LEU A O     1 
ATOM   12879 C  CB    . LEU A 1 3075 ? 146.630 156.971 167.017 1.00 99.93  ? 3075 LEU A CB    1 
ATOM   12880 C  CG    . LEU A 1 3075 ? 145.178 157.369 166.760 1.00 97.40  ? 3075 LEU A CG    1 
ATOM   12881 C  CD1   . LEU A 1 3075 ? 144.957 157.618 165.281 1.00 91.95  ? 3075 LEU A CD1   1 
ATOM   12882 C  CD2   . LEU A 1 3075 ? 144.240 156.291 167.268 1.00 98.60  ? 3075 LEU A CD2   1 
ATOM   12883 N  N     . LYS A 1 3076 ? 148.808 158.706 168.548 1.00 96.99  ? 3076 LYS A N     1 
ATOM   12884 C  CA    . LYS A 1 3076 ? 149.158 159.698 169.559 1.00 97.29  ? 3076 LYS A CA    1 
ATOM   12885 C  C     . LYS A 1 3076 ? 149.897 160.877 168.941 1.00 98.03  ? 3076 LYS A C     1 
ATOM   12886 O  O     . LYS A 1 3076 ? 149.644 162.034 169.298 1.00 103.20 ? 3076 LYS A O     1 
ATOM   12887 C  CB    . LYS A 1 3076 ? 150.000 159.055 170.660 1.00 97.39  ? 3076 LYS A CB    1 
ATOM   12888 C  CG    . LYS A 1 3076 ? 149.323 157.893 171.365 1.00 98.98  ? 3076 LYS A CG    1 
ATOM   12889 C  CD    . LYS A 1 3076 ? 149.827 157.749 172.791 1.00 101.54 ? 3076 LYS A CD    1 
ATOM   12890 C  CE    . LYS A 1 3076 ? 151.247 157.209 172.824 1.00 104.16 ? 3076 LYS A CE    1 
ATOM   12891 N  NZ    . LYS A 1 3076 ? 151.391 156.083 173.787 1.00 101.23 ? 3076 LYS A NZ    1 
ATOM   12892 N  N     . ASP A 1 3077 ? 150.819 160.605 168.015 1.00 91.91  ? 3077 ASP A N     1 
ATOM   12893 C  CA    . ASP A 1 3077 ? 151.535 161.687 167.347 1.00 95.56  ? 3077 ASP A CA    1 
ATOM   12894 C  C     . ASP A 1 3077 ? 150.595 162.532 166.497 1.00 96.87  ? 3077 ASP A C     1 
ATOM   12895 O  O     . ASP A 1 3077 ? 150.699 163.765 166.481 1.00 98.97  ? 3077 ASP A O     1 
ATOM   12896 C  CB    . ASP A 1 3077 ? 152.667 161.118 166.492 1.00 99.52  ? 3077 ASP A CB    1 
ATOM   12897 C  CG    . ASP A 1 3077 ? 153.235 162.138 165.527 1.00 101.84 ? 3077 ASP A CG    1 
ATOM   12898 O  OD1   . ASP A 1 3077 ? 153.876 163.105 165.992 1.00 101.88 ? 3077 ASP A OD1   1 
ATOM   12899 O  OD2   . ASP A 1 3077 ? 153.042 161.975 164.305 1.00 101.61 ? 3077 ASP A OD2   1 
ATOM   12900 N  N     . ARG A 1 3078 ? 149.670 161.886 165.781 1.00 90.47  ? 3078 ARG A N     1 
ATOM   12901 C  CA    . ARG A 1 3078 ? 148.731 162.624 164.943 1.00 88.42  ? 3078 ARG A CA    1 
ATOM   12902 C  C     . ARG A 1 3078 ? 147.739 163.420 165.779 1.00 89.80  ? 3078 ARG A C     1 
ATOM   12903 O  O     . ARG A 1 3078 ? 147.180 164.412 165.297 1.00 84.32  ? 3078 ARG A O     1 
ATOM   12904 C  CB    . ARG A 1 3078 ? 147.995 161.664 164.011 1.00 90.51  ? 3078 ARG A CB    1 
ATOM   12905 C  CG    . ARG A 1 3078 ? 147.478 162.316 162.743 1.00 91.67  ? 3078 ARG A CG    1 
ATOM   12906 C  CD    . ARG A 1 3078 ? 148.537 162.306 161.657 1.00 88.60  ? 3078 ARG A CD    1 
ATOM   12907 N  NE    . ARG A 1 3078 ? 148.763 160.966 161.129 1.00 90.67  ? 3078 ARG A NE    1 
ATOM   12908 C  CZ    . ARG A 1 3078 ? 149.848 160.597 160.464 1.00 93.55  ? 3078 ARG A CZ    1 
ATOM   12909 N  NH1   . ARG A 1 3078 ? 150.836 161.445 160.227 1.00 94.09  ? 3078 ARG A NH1   1 
ATOM   12910 N  NH2   . ARG A 1 3078 ? 149.947 159.345 160.026 1.00 91.48  ? 3078 ARG A NH2   1 
ATOM   12911 N  N     . ALA A 1 3079 ? 147.507 163.005 167.025 1.00 91.20  ? 3079 ALA A N     1 
ATOM   12912 C  CA    . ALA A 1 3079 ? 146.676 163.795 167.923 1.00 89.09  ? 3079 ALA A CA    1 
ATOM   12913 C  C     . ALA A 1 3079 ? 147.334 165.116 168.294 1.00 91.21  ? 3079 ALA A C     1 
ATOM   12914 O  O     . ALA A 1 3079 ? 146.668 165.993 168.854 1.00 97.60  ? 3079 ALA A O     1 
ATOM   12915 C  CB    . ALA A 1 3079 ? 146.356 162.998 169.188 1.00 90.60  ? 3079 ALA A CB    1 
ATOM   12916 N  N     . ALA A 1 3080 ? 148.623 165.275 168.001 1.00 86.17  ? 3080 ALA A N     1 
ATOM   12917 C  CA    . ALA A 1 3080 ? 149.357 166.500 168.289 1.00 85.83  ? 3080 ALA A CA    1 
ATOM   12918 C  C     . ALA A 1 3080 ? 149.749 167.281 167.046 1.00 81.95  ? 3080 ALA A C     1 
ATOM   12919 O  O     . ALA A 1 3080 ? 149.646 168.509 167.043 1.00 86.58  ? 3080 ALA A O     1 
ATOM   12920 C  CB    . ALA A 1 3080 ? 150.618 166.182 169.099 1.00 85.49  ? 3080 ALA A CB    1 
ATOM   12921 N  N     . THR A 1 3081 ? 150.201 166.609 165.984 1.00 80.58  ? 3081 THR A N     1 
ATOM   12922 C  CA    . THR A 1 3081 ? 150.633 167.343 164.797 1.00 81.74  ? 3081 THR A CA    1 
ATOM   12923 C  C     . THR A 1 3081 ? 149.443 167.844 163.988 1.00 82.27  ? 3081 THR A C     1 
ATOM   12924 O  O     . THR A 1 3081 ? 149.552 168.847 163.273 1.00 81.13  ? 3081 THR A O     1 
ATOM   12925 C  CB    . THR A 1 3081 ? 151.542 166.478 163.923 1.00 86.14  ? 3081 THR A CB    1 
ATOM   12926 O  OG1   . THR A 1 3081 ? 151.771 167.142 162.674 1.00 81.82  ? 3081 THR A OG1   1 
ATOM   12927 C  CG2   . THR A 1 3081 ? 150.901 165.137 163.644 1.00 87.87  ? 3081 THR A CG2   1 
ATOM   12928 N  N     . SER A 1 3082 ? 148.306 167.156 164.072 1.00 81.76  ? 3082 SER A N     1 
ATOM   12929 C  CA    . SER A 1 3082 ? 147.087 167.539 163.359 1.00 77.28  ? 3082 SER A CA    1 
ATOM   12930 C  C     . SER A 1 3082 ? 145.900 167.370 164.298 1.00 85.29  ? 3082 SER A C     1 
ATOM   12931 O  O     . SER A 1 3082 ? 145.156 166.384 164.205 1.00 91.88  ? 3082 SER A O     1 
ATOM   12932 C  CB    . SER A 1 3082 ? 146.909 166.716 162.084 1.00 75.17  ? 3082 SER A CB    1 
ATOM   12933 O  OG    . SER A 1 3082 ? 145.910 167.279 161.253 1.00 77.70  ? 3082 SER A OG    1 
ATOM   12934 N  N     . PRO A 1 3083 ? 145.700 168.309 165.225 1.00 71.24  ? 3083 PRO A N     1 
ATOM   12935 C  CA    . PRO A 1 3083 ? 144.577 168.177 166.167 1.00 58.84  ? 3083 PRO A CA    1 
ATOM   12936 C  C     . PRO A 1 3083 ? 143.213 168.192 165.500 1.00 64.19  ? 3083 PRO A C     1 
ATOM   12937 O  O     . PRO A 1 3083 ? 142.268 167.601 166.037 1.00 72.29  ? 3083 PRO A O     1 
ATOM   12938 C  CB    . PRO A 1 3083 ? 144.762 169.382 167.099 1.00 54.88  ? 3083 PRO A CB    1 
ATOM   12939 C  CG    . PRO A 1 3083 ? 145.522 170.370 166.284 1.00 59.31  ? 3083 PRO A CG    1 
ATOM   12940 C  CD    . PRO A 1 3083 ? 146.442 169.565 165.419 1.00 68.41  ? 3083 PRO A CD    1 
ATOM   12941 N  N     . ALA A 1 3084 ? 143.076 168.853 164.348 1.00 61.54  ? 3084 ALA A N     1 
ATOM   12942 C  CA    . ALA A 1 3084 ? 141.781 168.920 163.681 1.00 61.30  ? 3084 ALA A CA    1 
ATOM   12943 C  C     . ALA A 1 3084 ? 141.321 167.567 163.160 1.00 65.15  ? 3084 ALA A C     1 
ATOM   12944 O  O     . ALA A 1 3084 ? 140.128 167.395 162.891 1.00 74.26  ? 3084 ALA A O     1 
ATOM   12945 C  CB    . ALA A 1 3084 ? 141.823 169.922 162.531 1.00 64.45  ? 3084 ALA A CB    1 
ATOM   12946 N  N     . LEU A 1 3085 ? 142.236 166.608 163.004 1.00 63.23  ? 3085 LEU A N     1 
ATOM   12947 C  CA    . LEU A 1 3085 ? 141.841 165.263 162.604 1.00 62.23  ? 3085 LEU A CA    1 
ATOM   12948 C  C     . LEU A 1 3085 ? 140.956 164.590 163.642 1.00 66.27  ? 3085 LEU A C     1 
ATOM   12949 O  O     . LEU A 1 3085 ? 140.251 163.633 163.310 1.00 73.50  ? 3085 LEU A O     1 
ATOM   12950 C  CB    . LEU A 1 3085 ? 143.079 164.403 162.347 1.00 61.78  ? 3085 LEU A CB    1 
ATOM   12951 C  CG    . LEU A 1 3085 ? 143.341 163.989 160.899 1.00 64.44  ? 3085 LEU A CG    1 
ATOM   12952 C  CD1   . LEU A 1 3085 ? 143.726 165.190 160.056 1.00 64.54  ? 3085 LEU A CD1   1 
ATOM   12953 C  CD2   . LEU A 1 3085 ? 144.418 162.919 160.837 1.00 62.62  ? 3085 LEU A CD2   1 
ATOM   12954 N  N     . PHE A 1 3086 ? 140.978 165.065 164.887 1.00 67.36  ? 3086 PHE A N     1 
ATOM   12955 C  CA    . PHE A 1 3086 ? 140.199 164.469 165.960 1.00 69.34  ? 3086 PHE A CA    1 
ATOM   12956 C  C     . PHE A 1 3086 ? 139.113 165.392 166.493 1.00 72.20  ? 3086 PHE A C     1 
ATOM   12957 O  O     . PHE A 1 3086 ? 138.392 165.004 167.419 1.00 77.76  ? 3086 PHE A O     1 
ATOM   12958 C  CB    . PHE A 1 3086 ? 141.123 164.041 167.108 1.00 64.74  ? 3086 PHE A CB    1 
ATOM   12959 C  CG    . PHE A 1 3086 ? 142.106 162.970 166.726 1.00 70.39  ? 3086 PHE A CG    1 
ATOM   12960 C  CD1   . PHE A 1 3086 ? 143.264 163.288 166.036 1.00 69.28  ? 3086 PHE A CD1   1 
ATOM   12961 C  CD2   . PHE A 1 3086 ? 141.869 161.647 167.049 1.00 77.15  ? 3086 PHE A CD2   1 
ATOM   12962 C  CE1   . PHE A 1 3086 ? 144.167 162.307 165.680 1.00 69.91  ? 3086 PHE A CE1   1 
ATOM   12963 C  CE2   . PHE A 1 3086 ? 142.770 160.661 166.696 1.00 78.28  ? 3086 PHE A CE2   1 
ATOM   12964 C  CZ    . PHE A 1 3086 ? 143.920 160.993 166.011 1.00 75.15  ? 3086 PHE A CZ    1 
ATOM   12965 N  N     . ASN A 1 3087 ? 138.974 166.595 165.942 1.00 68.85  ? 3087 ASN A N     1 
ATOM   12966 C  CA    . ASN A 1 3087 ? 137.933 167.527 166.350 1.00 66.02  ? 3087 ASN A CA    1 
ATOM   12967 C  C     . ASN A 1 3087 ? 136.909 167.813 165.265 1.00 72.56  ? 3087 ASN A C     1 
ATOM   12968 O  O     . ASN A 1 3087 ? 135.730 167.983 165.583 1.00 75.82  ? 3087 ASN A O     1 
ATOM   12969 C  CB    . ASN A 1 3087 ? 138.551 168.858 166.805 1.00 65.53  ? 3087 ASN A CB    1 
ATOM   12970 C  CG    . ASN A 1 3087 ? 139.553 168.682 167.927 1.00 75.31  ? 3087 ASN A CG    1 
ATOM   12971 O  OD1   . ASN A 1 3087 ? 139.605 167.633 168.568 1.00 79.01  ? 3087 ASN A OD1   1 
ATOM   12972 N  ND2   . ASN A 1 3087 ? 140.354 169.712 168.172 1.00 75.83  ? 3087 ASN A ND2   1 
ATOM   12973 N  N     . ARG A 1 3088 ? 137.321 167.872 163.999 1.00 76.17  ? 3088 ARG A N     1 
ATOM   12974 C  CA    . ARG A 1 3088 ? 136.406 168.121 162.896 1.00 74.04  ? 3088 ARG A CA    1 
ATOM   12975 C  C     . ARG A 1 3088 ? 136.129 166.887 162.051 1.00 76.79  ? 3088 ARG A C     1 
ATOM   12976 O  O     . ARG A 1 3088 ? 135.221 166.925 161.214 1.00 84.10  ? 3088 ARG A O     1 
ATOM   12977 C  CB    . ARG A 1 3088 ? 136.953 169.237 161.993 1.00 71.27  ? 3088 ARG A CB    1 
ATOM   12978 C  CG    . ARG A 1 3088 ? 137.217 170.547 162.716 1.00 80.60  ? 3088 ARG A CG    1 
ATOM   12979 C  CD    . ARG A 1 3088 ? 136.010 170.986 163.530 1.00 80.73  ? 3088 ARG A CD    1 
ATOM   12980 N  NE    . ARG A 1 3088 ? 135.918 172.437 163.636 1.00 79.10  ? 3088 ARG A NE    1 
ATOM   12981 C  CZ    . ARG A 1 3088 ? 136.647 173.177 164.460 1.00 78.20  ? 3088 ARG A CZ    1 
ATOM   12982 N  NH1   . ARG A 1 3088 ? 137.533 172.632 165.279 1.00 77.85  ? 3088 ARG A NH1   1 
ATOM   12983 N  NH2   . ARG A 1 3088 ? 136.481 174.496 164.466 1.00 76.45  ? 3088 ARG A NH2   1 
ATOM   12984 N  N     . CYS A 1 3089 ? 136.875 165.805 162.244 1.00 67.73  ? 3089 CYS A N     1 
ATOM   12985 C  CA    . CYS A 1 3089 ? 136.710 164.580 161.475 1.00 66.13  ? 3089 CYS A CA    1 
ATOM   12986 C  C     . CYS A 1 3089 ? 136.059 163.518 162.348 1.00 72.18  ? 3089 CYS A C     1 
ATOM   12987 O  O     . CYS A 1 3089 ? 136.513 163.266 163.468 1.00 77.96  ? 3089 CYS A O     1 
ATOM   12988 C  CB    . CYS A 1 3089 ? 138.056 164.076 160.950 1.00 65.61  ? 3089 CYS A CB    1 
ATOM   12989 S  SG    . CYS A 1 3089 ? 138.912 165.219 159.845 1.00 87.96  ? 3089 CYS A SG    1 
ATOM   12990 N  N     . VAL A 1 3090 ? 134.999 162.899 161.834 1.00 61.51  ? 3090 VAL A N     1 
ATOM   12991 C  CA    . VAL A 1 3090 ? 134.340 161.816 162.555 1.00 56.31  ? 3090 VAL A CA    1 
ATOM   12992 C  C     . VAL A 1 3090 ? 135.199 160.565 162.443 1.00 54.66  ? 3090 VAL A C     1 
ATOM   12993 O  O     . VAL A 1 3090 ? 135.521 160.112 161.339 1.00 61.69  ? 3090 VAL A O     1 
ATOM   12994 C  CB    . VAL A 1 3090 ? 132.927 161.574 162.013 1.00 57.23  ? 3090 VAL A CB    1 
ATOM   12995 C  CG1   . VAL A 1 3090 ? 132.337 160.314 162.621 1.00 61.75  ? 3090 VAL A CG1   1 
ATOM   12996 C  CG2   . VAL A 1 3090 ? 132.042 162.775 162.299 1.00 58.85  ? 3090 VAL A CG2   1 
ATOM   12997 N  N     . LEU A 1 3091 ? 135.572 159.999 163.587 1.00 51.50  ? 3091 LEU A N     1 
ATOM   12998 C  CA    . LEU A 1 3091 ? 136.492 158.872 163.626 1.00 50.94  ? 3091 LEU A CA    1 
ATOM   12999 C  C     . LEU A 1 3091 ? 135.725 157.560 163.537 1.00 62.15  ? 3091 LEU A C     1 
ATOM   13000 O  O     . LEU A 1 3091 ? 134.896 157.258 164.401 1.00 69.67  ? 3091 LEU A O     1 
ATOM   13001 C  CB    . LEU A 1 3091 ? 137.330 158.910 164.904 1.00 46.07  ? 3091 LEU A CB    1 
ATOM   13002 C  CG    . LEU A 1 3091 ? 138.666 158.166 164.877 1.00 55.39  ? 3091 LEU A CG    1 
ATOM   13003 C  CD1   . LEU A 1 3091 ? 139.685 158.893 165.733 1.00 60.41  ? 3091 LEU A CD1   1 
ATOM   13004 C  CD2   . LEU A 1 3091 ? 138.502 156.732 165.350 1.00 57.53  ? 3091 LEU A CD2   1 
ATOM   13005 N  N     . ASN A 1 3092 ? 136.006 156.787 162.492 1.00 59.53  ? 3092 ASN A N     1 
ATOM   13006 C  CA    . ASN A 1 3092 ? 135.463 155.444 162.327 1.00 54.94  ? 3092 ASN A CA    1 
ATOM   13007 C  C     . ASN A 1 3092 ? 136.613 154.452 162.396 1.00 65.04  ? 3092 ASN A C     1 
ATOM   13008 O  O     . ASN A 1 3092 ? 137.587 154.574 161.646 1.00 67.53  ? 3092 ASN A O     1 
ATOM   13009 C  CB    . ASN A 1 3092 ? 134.711 155.303 161.003 1.00 54.70  ? 3092 ASN A CB    1 
ATOM   13010 C  CG    . ASN A 1 3092 ? 133.316 155.883 161.063 1.00 65.16  ? 3092 ASN A CG    1 
ATOM   13011 O  OD1   . ASN A 1 3092 ? 132.650 155.818 162.094 1.00 73.96  ? 3092 ASN A OD1   1 
ATOM   13012 N  ND2   . ASN A 1 3092 ? 132.860 156.444 159.951 1.00 68.26  ? 3092 ASN A ND2   1 
ATOM   13013 N  N     . TRP A 1 3093 ? 136.501 153.476 163.293 1.00 65.44  ? 3093 TRP A N     1 
ATOM   13014 C  CA    . TRP A 1 3093 ? 137.535 152.458 163.468 1.00 56.28  ? 3093 TRP A CA    1 
ATOM   13015 C  C     . TRP A 1 3093 ? 137.108 151.201 162.725 1.00 61.12  ? 3093 TRP A C     1 
ATOM   13016 O  O     . TRP A 1 3093 ? 136.457 150.315 163.279 1.00 62.78  ? 3093 TRP A O     1 
ATOM   13017 C  CB    . TRP A 1 3093 ? 137.777 152.181 164.945 1.00 62.53  ? 3093 TRP A CB    1 
ATOM   13018 C  CG    . TRP A 1 3093 ? 139.083 151.507 165.214 1.00 61.82  ? 3093 TRP A CG    1 
ATOM   13019 C  CD1   . TRP A 1 3093 ? 139.358 150.178 165.084 1.00 62.07  ? 3093 TRP A CD1   1 
ATOM   13020 C  CD2   . TRP A 1 3093 ? 140.295 152.126 165.655 1.00 61.71  ? 3093 TRP A CD2   1 
ATOM   13021 N  NE1   . TRP A 1 3093 ? 140.665 149.930 165.419 1.00 59.57  ? 3093 TRP A NE1   1 
ATOM   13022 C  CE2   . TRP A 1 3093 ? 141.263 151.111 165.774 1.00 59.82  ? 3093 TRP A CE2   1 
ATOM   13023 C  CE3   . TRP A 1 3093 ? 140.656 153.440 165.963 1.00 64.79  ? 3093 TRP A CE3   1 
ATOM   13024 C  CZ2   . TRP A 1 3093 ? 142.566 151.368 166.187 1.00 61.87  ? 3093 TRP A CZ2   1 
ATOM   13025 C  CZ3   . TRP A 1 3093 ? 141.950 153.693 166.372 1.00 63.44  ? 3093 TRP A CZ3   1 
ATOM   13026 C  CH2   . TRP A 1 3093 ? 142.890 152.663 166.480 1.00 63.88  ? 3093 TRP A CH2   1 
ATOM   13027 N  N     . PHE A 1 3094 ? 137.476 151.127 161.444 1.00 66.69  ? 3094 PHE A N     1 
ATOM   13028 C  CA    . PHE A 1 3094 ? 137.214 149.915 160.676 1.00 66.89  ? 3094 PHE A CA    1 
ATOM   13029 C  C     . PHE A 1 3094 ? 138.001 148.737 161.232 1.00 67.76  ? 3094 PHE A C     1 
ATOM   13030 O  O     . PHE A 1 3094 ? 137.452 147.643 161.410 1.00 69.88  ? 3094 PHE A O     1 
ATOM   13031 C  CB    . PHE A 1 3094 ? 137.560 150.136 159.204 1.00 68.21  ? 3094 PHE A CB    1 
ATOM   13032 C  CG    . PHE A 1 3094 ? 136.534 150.929 158.445 1.00 67.62  ? 3094 PHE A CG    1 
ATOM   13033 C  CD1   . PHE A 1 3094 ? 135.487 151.553 159.102 1.00 71.13  ? 3094 PHE A CD1   1 
ATOM   13034 C  CD2   . PHE A 1 3094 ? 136.617 151.045 157.069 1.00 68.76  ? 3094 PHE A CD2   1 
ATOM   13035 C  CE1   . PHE A 1 3094 ? 134.547 152.281 158.401 1.00 72.00  ? 3094 PHE A CE1   1 
ATOM   13036 C  CE2   . PHE A 1 3094 ? 135.679 151.771 156.363 1.00 75.52  ? 3094 PHE A CE2   1 
ATOM   13037 C  CZ    . PHE A 1 3094 ? 134.644 152.390 157.030 1.00 74.51  ? 3094 PHE A CZ    1 
ATOM   13038 N  N     . GLY A 1 3095 ? 139.285 148.944 161.518 1.00 66.29  ? 3095 GLY A N     1 
ATOM   13039 C  CA    . GLY A 1 3095 ? 140.124 147.892 162.045 1.00 68.55  ? 3095 GLY A CA    1 
ATOM   13040 C  C     . GLY A 1 3095 ? 140.317 146.767 161.040 1.00 69.68  ? 3095 GLY A C     1 
ATOM   13041 O  O     . GLY A 1 3095 ? 140.056 146.900 159.841 1.00 73.95  ? 3095 GLY A O     1 
ATOM   13042 N  N     . ASP A 1 3096 ? 140.783 145.638 161.556 1.00 75.82  ? 3096 ASP A N     1 
ATOM   13043 C  CA    . ASP A 1 3096 ? 140.908 144.428 160.762 1.00 75.20  ? 3096 ASP A CA    1 
ATOM   13044 C  C     . ASP A 1 3096 ? 139.561 143.718 160.691 1.00 75.64  ? 3096 ASP A C     1 
ATOM   13045 O  O     . ASP A 1 3096 ? 138.679 143.922 161.529 1.00 80.43  ? 3096 ASP A O     1 
ATOM   13046 C  CB    . ASP A 1 3096 ? 141.969 143.502 161.359 1.00 76.10  ? 3096 ASP A CB    1 
ATOM   13047 C  CG    . ASP A 1 3096 ? 142.401 142.409 160.398 1.00 82.37  ? 3096 ASP A CG    1 
ATOM   13048 O  OD1   . ASP A 1 3096 ? 143.592 142.384 160.025 1.00 83.33  ? 3096 ASP A OD1   1 
ATOM   13049 O  OD2   . ASP A 1 3096 ? 141.554 141.572 160.021 1.00 80.61  ? 3096 ASP A OD2   1 
ATOM   13050 N  N     . TRP A 1 3097 ? 139.405 142.883 159.666 1.00 55.45  ? 3097 TRP A N     1 
ATOM   13051 C  CA    . TRP A 1 3097 ? 138.193 142.088 159.542 1.00 60.32  ? 3097 TRP A CA    1 
ATOM   13052 C  C     . TRP A 1 3097 ? 138.054 141.156 160.737 1.00 65.38  ? 3097 TRP A C     1 
ATOM   13053 O  O     . TRP A 1 3097 ? 138.973 140.397 161.059 1.00 67.70  ? 3097 TRP A O     1 
ATOM   13054 C  CB    . TRP A 1 3097 ? 138.213 141.280 158.246 1.00 60.28  ? 3097 TRP A CB    1 
ATOM   13055 C  CG    . TRP A 1 3097 ? 138.016 142.101 157.016 1.00 62.52  ? 3097 TRP A CG    1 
ATOM   13056 C  CD1   . TRP A 1 3097 ? 137.873 143.454 156.947 1.00 63.04  ? 3097 TRP A CD1   1 
ATOM   13057 C  CD2   . TRP A 1 3097 ? 137.934 141.619 155.671 1.00 61.93  ? 3097 TRP A CD2   1 
ATOM   13058 N  NE1   . TRP A 1 3097 ? 137.710 143.846 155.641 1.00 59.48  ? 3097 TRP A NE1   1 
ATOM   13059 C  CE2   . TRP A 1 3097 ? 137.744 142.737 154.838 1.00 55.75  ? 3097 TRP A CE2   1 
ATOM   13060 C  CE3   . TRP A 1 3097 ? 138.006 140.350 155.090 1.00 63.01  ? 3097 TRP A CE3   1 
ATOM   13061 C  CZ2   . TRP A 1 3097 ? 137.624 142.625 153.457 1.00 62.68  ? 3097 TRP A CZ2   1 
ATOM   13062 C  CZ3   . TRP A 1 3097 ? 137.887 140.241 153.719 1.00 59.62  ? 3097 TRP A CZ3   1 
ATOM   13063 C  CH2   . TRP A 1 3097 ? 137.698 141.371 152.917 1.00 63.91  ? 3097 TRP A CH2   1 
ATOM   13064 N  N     . SER A 1 3098 ? 136.902 141.217 161.396 1.00 70.76  ? 3098 SER A N     1 
ATOM   13065 C  CA    . SER A 1 3098 ? 136.655 140.359 162.540 1.00 67.85  ? 3098 SER A CA    1 
ATOM   13066 C  C     . SER A 1 3098 ? 136.456 138.915 162.084 1.00 70.68  ? 3098 SER A C     1 
ATOM   13067 O  O     . SER A 1 3098 ? 136.441 138.604 160.890 1.00 79.13  ? 3098 SER A O     1 
ATOM   13068 C  CB    . SER A 1 3098 ? 135.437 140.846 163.322 1.00 73.93  ? 3098 SER A CB    1 
ATOM   13069 O  OG    . SER A 1 3098 ? 134.279 140.857 162.507 1.00 77.78  ? 3098 SER A OG    1 
ATOM   13070 N  N     . THR A 1 3099 ? 136.305 138.022 163.064 1.00 72.24  ? 3099 THR A N     1 
ATOM   13071 C  CA    . THR A 1 3099 ? 136.081 136.615 162.748 1.00 70.58  ? 3099 THR A CA    1 
ATOM   13072 C  C     . THR A 1 3099 ? 134.792 136.430 161.957 1.00 72.24  ? 3099 THR A C     1 
ATOM   13073 O  O     . THR A 1 3099 ? 134.745 135.638 161.008 1.00 79.59  ? 3099 THR A O     1 
ATOM   13074 C  CB    . THR A 1 3099 ? 136.049 135.787 164.032 1.00 72.66  ? 3099 THR A CB    1 
ATOM   13075 O  OG1   . THR A 1 3099 ? 137.264 135.990 164.763 1.00 75.97  ? 3099 THR A OG1   1 
ATOM   13076 C  CG2   . THR A 1 3099 ? 135.902 134.310 163.710 1.00 75.00  ? 3099 THR A CG2   1 
ATOM   13077 N  N     . GLU A 1 3100 ? 133.738 137.159 162.330 1.00 70.90  ? 3100 GLU A N     1 
ATOM   13078 C  CA    . GLU A 1 3100 ? 132.480 137.071 161.597 1.00 71.55  ? 3100 GLU A CA    1 
ATOM   13079 C  C     . GLU A 1 3100 ? 132.648 137.536 160.157 1.00 75.81  ? 3100 GLU A C     1 
ATOM   13080 O  O     . GLU A 1 3100 ? 132.097 136.927 159.233 1.00 84.22  ? 3100 GLU A O     1 
ATOM   13081 C  CB    . GLU A 1 3100 ? 131.404 137.894 162.304 1.00 75.49  ? 3100 GLU A CB    1 
ATOM   13082 C  CG    . GLU A 1 3100 ? 131.527 137.900 163.818 1.00 82.59  ? 3100 GLU A CG    1 
ATOM   13083 C  CD    . GLU A 1 3100 ? 130.201 138.141 164.511 1.00 86.15  ? 3100 GLU A CD    1 
ATOM   13084 O  OE1   . GLU A 1 3100 ? 130.181 138.175 165.759 1.00 84.43  ? 3100 GLU A OE1   1 
ATOM   13085 O  OE2   . GLU A 1 3100 ? 129.181 138.297 163.808 1.00 86.60  ? 3100 GLU A OE2   1 
ATOM   13086 N  N     . ALA A 1 3101 ? 133.399 138.620 159.947 1.00 71.59  ? 3101 ALA A N     1 
ATOM   13087 C  CA    . ALA A 1 3101 ? 133.623 139.114 158.593 1.00 72.27  ? 3101 ALA A CA    1 
ATOM   13088 C  C     . ALA A 1 3101 ? 134.384 138.097 157.751 1.00 74.30  ? 3101 ALA A C     1 
ATOM   13089 O  O     . ALA A 1 3101 ? 134.026 137.846 156.594 1.00 68.73  ? 3101 ALA A O     1 
ATOM   13090 C  CB    . ALA A 1 3101 ? 134.374 140.444 158.638 1.00 65.26  ? 3101 ALA A CB    1 
ATOM   13091 N  N     . LEU A 1 3102 ? 135.437 137.501 158.316 1.00 74.17  ? 3102 LEU A N     1 
ATOM   13092 C  CA    . LEU A 1 3102 ? 136.190 136.483 157.590 1.00 62.95  ? 3102 LEU A CA    1 
ATOM   13093 C  C     . LEU A 1 3102 ? 135.315 135.282 157.263 1.00 70.17  ? 3102 LEU A C     1 
ATOM   13094 O  O     . LEU A 1 3102 ? 135.371 134.748 156.149 1.00 81.85  ? 3102 LEU A O     1 
ATOM   13095 C  CB    . LEU A 1 3102 ? 137.409 136.049 158.403 1.00 54.43  ? 3102 LEU A CB    1 
ATOM   13096 C  CG    . LEU A 1 3102 ? 138.465 137.115 158.689 1.00 62.70  ? 3102 LEU A CG    1 
ATOM   13097 C  CD1   . LEU A 1 3102 ? 139.533 136.572 159.623 1.00 67.75  ? 3102 LEU A CD1   1 
ATOM   13098 C  CD2   . LEU A 1 3102 ? 139.085 137.610 157.394 1.00 65.59  ? 3102 LEU A CD2   1 
ATOM   13099 N  N     . TYR A 1 3103 ? 134.497 134.844 158.223 1.00 70.25  ? 3103 TYR A N     1 
ATOM   13100 C  CA    . TYR A 1 3103 ? 133.623 133.701 157.984 1.00 72.13  ? 3103 TYR A CA    1 
ATOM   13101 C  C     . TYR A 1 3103 ? 132.606 134.000 156.891 1.00 73.98  ? 3103 TYR A C     1 
ATOM   13102 O  O     . TYR A 1 3103 ? 132.351 133.156 156.024 1.00 83.09  ? 3103 TYR A O     1 
ATOM   13103 C  CB    . TYR A 1 3103 ? 132.915 133.305 159.278 1.00 73.38  ? 3103 TYR A CB    1 
ATOM   13104 C  CG    . TYR A 1 3103 ? 132.034 132.088 159.140 1.00 74.56  ? 3103 TYR A CG    1 
ATOM   13105 C  CD1   . TYR A 1 3103 ? 132.561 130.811 159.254 1.00 76.39  ? 3103 TYR A CD1   1 
ATOM   13106 C  CD2   . TYR A 1 3103 ? 130.675 132.216 158.891 1.00 75.70  ? 3103 TYR A CD2   1 
ATOM   13107 C  CE1   . TYR A 1 3103 ? 131.761 129.696 159.126 1.00 76.37  ? 3103 TYR A CE1   1 
ATOM   13108 C  CE2   . TYR A 1 3103 ? 129.867 131.108 158.762 1.00 75.28  ? 3103 TYR A CE2   1 
ATOM   13109 C  CZ    . TYR A 1 3103 ? 130.415 129.851 158.880 1.00 76.60  ? 3103 TYR A CZ    1 
ATOM   13110 O  OH    . TYR A 1 3103 ? 129.613 128.745 158.753 1.00 82.65  ? 3103 TYR A OH    1 
ATOM   13111 N  N     . GLN A 1 3104 ? 132.008 135.192 156.918 1.00 62.28  ? 3104 GLN A N     1 
ATOM   13112 C  CA    . GLN A 1 3104 ? 131.028 135.549 155.899 1.00 64.87  ? 3104 GLN A CA    1 
ATOM   13113 C  C     . GLN A 1 3104 ? 131.674 135.657 154.524 1.00 71.84  ? 3104 GLN A C     1 
ATOM   13114 O  O     . GLN A 1 3104 ? 131.093 135.220 153.523 1.00 77.24  ? 3104 GLN A O     1 
ATOM   13115 C  CB    . GLN A 1 3104 ? 130.329 136.854 156.277 1.00 68.66  ? 3104 GLN A CB    1 
ATOM   13116 C  CG    . GLN A 1 3104 ? 129.118 136.659 157.175 1.00 68.96  ? 3104 GLN A CG    1 
ATOM   13117 C  CD    . GLN A 1 3104 ? 128.850 137.856 158.065 1.00 76.07  ? 3104 GLN A CD    1 
ATOM   13118 O  OE1   . GLN A 1 3104 ? 128.604 138.960 157.583 1.00 76.67  ? 3104 GLN A OE1   1 
ATOM   13119 N  NE2   . GLN A 1 3104 ? 128.898 137.641 159.374 1.00 76.46  ? 3104 GLN A NE2   1 
ATOM   13120 N  N     . VAL A 1 3105 ? 132.877 136.233 154.453 1.00 62.01  ? 3105 VAL A N     1 
ATOM   13121 C  CA    . VAL A 1 3105 ? 133.579 136.332 153.176 1.00 66.04  ? 3105 VAL A CA    1 
ATOM   13122 C  C     . VAL A 1 3105 ? 133.906 134.944 152.641 1.00 69.66  ? 3105 VAL A C     1 
ATOM   13123 O  O     . VAL A 1 3105 ? 133.740 134.668 151.447 1.00 70.64  ? 3105 VAL A O     1 
ATOM   13124 C  CB    . VAL A 1 3105 ? 134.844 137.197 153.327 1.00 64.21  ? 3105 VAL A CB    1 
ATOM   13125 C  CG1   . VAL A 1 3105 ? 135.777 136.992 152.145 1.00 65.20  ? 3105 VAL A CG1   1 
ATOM   13126 C  CG2   . VAL A 1 3105 ? 134.469 138.659 153.459 1.00 66.90  ? 3105 VAL A CG2   1 
ATOM   13127 N  N     . GLY A 1 3106 ? 134.370 134.048 153.514 1.00 67.42  ? 3106 GLY A N     1 
ATOM   13128 C  CA    . GLY A 1 3106 ? 134.673 132.697 153.075 1.00 66.91  ? 3106 GLY A CA    1 
ATOM   13129 C  C     . GLY A 1 3106 ? 133.444 131.944 152.602 1.00 74.99  ? 3106 GLY A C     1 
ATOM   13130 O  O     . GLY A 1 3106 ? 133.477 131.273 151.568 1.00 85.28  ? 3106 GLY A O     1 
ATOM   13131 N  N     . LYS A 1 3107 ? 132.344 132.045 153.350 1.00 76.49  ? 3107 LYS A N     1 
ATOM   13132 C  CA    . LYS A 1 3107 ? 131.125 131.338 152.971 1.00 72.74  ? 3107 LYS A CA    1 
ATOM   13133 C  C     . LYS A 1 3107 ? 130.550 131.874 151.666 1.00 70.40  ? 3107 LYS A C     1 
ATOM   13134 O  O     . LYS A 1 3107 ? 130.136 131.095 150.799 1.00 69.66  ? 3107 LYS A O     1 
ATOM   13135 C  CB    . LYS A 1 3107 ? 130.092 131.437 154.092 1.00 72.19  ? 3107 LYS A CB    1 
ATOM   13136 C  CG    . LYS A 1 3107 ? 128.755 130.802 153.758 1.00 75.62  ? 3107 LYS A CG    1 
ATOM   13137 C  CD    . LYS A 1 3107 ? 127.828 130.808 154.959 1.00 74.29  ? 3107 LYS A CD    1 
ATOM   13138 C  CE    . LYS A 1 3107 ? 128.195 129.710 155.940 1.00 71.86  ? 3107 LYS A CE    1 
ATOM   13139 N  NZ    . LYS A 1 3107 ? 127.962 128.357 155.366 1.00 78.22  ? 3107 LYS A NZ    1 
ATOM   13140 N  N     . GLU A 1 3108 ? 130.512 133.199 151.506 1.00 82.74  ? 3108 GLU A N     1 
ATOM   13141 C  CA    . GLU A 1 3108 ? 129.951 133.780 150.290 1.00 86.40  ? 3108 GLU A CA    1 
ATOM   13142 C  C     . GLU A 1 3108 ? 130.787 133.428 149.065 1.00 86.09  ? 3108 GLU A C     1 
ATOM   13143 O  O     . GLU A 1 3108 ? 130.239 133.108 148.004 1.00 86.11  ? 3108 GLU A O     1 
ATOM   13144 C  CB    . GLU A 1 3108 ? 129.833 135.296 150.440 1.00 85.21  ? 3108 GLU A CB    1 
ATOM   13145 C  CG    . GLU A 1 3108 ? 129.462 136.019 149.156 1.00 89.44  ? 3108 GLU A CG    1 
ATOM   13146 C  CD    . GLU A 1 3108 ? 128.099 135.616 148.632 1.00 91.78  ? 3108 GLU A CD    1 
ATOM   13147 O  OE1   . GLU A 1 3108 ? 127.193 135.367 149.455 1.00 91.46  ? 3108 GLU A OE1   1 
ATOM   13148 O  OE2   . GLU A 1 3108 ? 127.933 135.546 147.397 1.00 90.62  ? 3108 GLU A OE2   1 
ATOM   13149 N  N     . PHE A 1 3109 ? 132.113 133.481 149.192 1.00 80.92  ? 3109 PHE A N     1 
ATOM   13150 C  CA    . PHE A 1 3109 ? 132.975 133.225 148.043 1.00 80.26  ? 3109 PHE A CA    1 
ATOM   13151 C  C     . PHE A 1 3109 ? 132.988 131.744 147.679 1.00 83.02  ? 3109 PHE A C     1 
ATOM   13152 O  O     . PHE A 1 3109 ? 132.879 131.388 146.500 1.00 81.47  ? 3109 PHE A O     1 
ATOM   13153 C  CB    . PHE A 1 3109 ? 134.387 133.729 148.339 1.00 76.23  ? 3109 PHE A CB    1 
ATOM   13154 C  CG    . PHE A 1 3109 ? 135.165 134.133 147.117 1.00 78.83  ? 3109 PHE A CG    1 
ATOM   13155 C  CD1   . PHE A 1 3109 ? 135.938 135.281 147.129 1.00 78.59  ? 3109 PHE A CD1   1 
ATOM   13156 C  CD2   . PHE A 1 3109 ? 135.132 133.369 145.963 1.00 78.32  ? 3109 PHE A CD2   1 
ATOM   13157 C  CE1   . PHE A 1 3109 ? 136.656 135.661 146.015 1.00 79.68  ? 3109 PHE A CE1   1 
ATOM   13158 C  CE2   . PHE A 1 3109 ? 135.848 133.744 144.845 1.00 79.72  ? 3109 PHE A CE2   1 
ATOM   13159 C  CZ    . PHE A 1 3109 ? 136.611 134.891 144.871 1.00 81.39  ? 3109 PHE A CZ    1 
ATOM   13160 N  N     . THR A 1 3110 ? 133.107 130.867 148.674 1.00 86.46  ? 3110 THR A N     1 
ATOM   13161 C  CA    . THR A 1 3110 ? 133.171 129.431 148.434 1.00 81.16  ? 3110 THR A CA    1 
ATOM   13162 C  C     . THR A 1 3110 ? 131.802 128.801 148.217 1.00 82.17  ? 3110 THR A C     1 
ATOM   13163 O  O     . THR A 1 3110 ? 131.706 127.570 148.174 1.00 86.06  ? 3110 THR A O     1 
ATOM   13164 C  CB    . THR A 1 3110 ? 133.879 128.729 149.595 1.00 76.91  ? 3110 THR A CB    1 
ATOM   13165 O  OG1   . THR A 1 3110 ? 133.158 128.968 150.810 1.00 83.80  ? 3110 THR A OG1   1 
ATOM   13166 C  CG2   . THR A 1 3110 ? 135.300 129.247 149.744 1.00 78.06  ? 3110 THR A CG2   1 
ATOM   13167 N  N     . SER A 1 3111 ? 130.745 129.607 148.090 1.00 90.62  ? 3111 SER A N     1 
ATOM   13168 C  CA    . SER A 1 3111 ? 129.427 129.052 147.806 1.00 90.95  ? 3111 SER A CA    1 
ATOM   13169 C  C     . SER A 1 3111 ? 129.381 128.401 146.431 1.00 93.27  ? 3111 SER A C     1 
ATOM   13170 O  O     . SER A 1 3111 ? 128.632 127.439 146.224 1.00 91.81  ? 3111 SER A O     1 
ATOM   13171 C  CB    . SER A 1 3111 ? 128.363 130.144 147.913 1.00 89.77  ? 3111 SER A CB    1 
ATOM   13172 O  OG    . SER A 1 3111 ? 128.687 131.250 147.091 1.00 95.48  ? 3111 SER A OG    1 
ATOM   13173 N  N     . LYS A 1 3112 ? 130.166 128.911 145.479 1.00 101.44 ? 3112 LYS A N     1 
ATOM   13174 C  CA    . LYS A 1 3112 ? 130.217 128.304 144.153 1.00 99.34  ? 3112 LYS A CA    1 
ATOM   13175 C  C     . LYS A 1 3112 ? 130.812 126.903 144.200 1.00 100.08 ? 3112 LYS A C     1 
ATOM   13176 O  O     . LYS A 1 3112 ? 130.366 126.017 143.464 1.00 102.26 ? 3112 LYS A O     1 
ATOM   13177 C  CB    . LYS A 1 3112 ? 131.021 129.187 143.197 1.00 103.04 ? 3112 LYS A CB    1 
ATOM   13178 C  CG    . LYS A 1 3112 ? 130.526 130.626 143.077 1.00 105.25 ? 3112 LYS A CG    1 
ATOM   13179 C  CD    . LYS A 1 3112 ? 129.006 130.719 143.111 1.00 103.10 ? 3112 LYS A CD    1 
ATOM   13180 C  CE    . LYS A 1 3112 ? 128.544 132.164 143.210 1.00 102.38 ? 3112 LYS A CE    1 
ATOM   13181 N  NZ    . LYS A 1 3112 ? 128.910 132.778 144.516 1.00 101.14 ? 3112 LYS A NZ    1 
ATOM   13182 N  N     . MET A 1 3113 ? 131.814 126.688 145.048 1.00 97.64  ? 3113 MET A N     1 
ATOM   13183 C  CA    . MET A 1 3113 ? 132.448 125.383 145.159 1.00 97.21  ? 3113 MET A CA    1 
ATOM   13184 C  C     . MET A 1 3113 ? 131.476 124.362 145.739 1.00 96.29  ? 3113 MET A C     1 
ATOM   13185 O  O     . MET A 1 3113 ? 130.535 124.706 146.459 1.00 97.85  ? 3113 MET A O     1 
ATOM   13186 C  CB    . MET A 1 3113 ? 133.697 125.478 146.033 1.00 96.28  ? 3113 MET A CB    1 
ATOM   13187 C  CG    . MET A 1 3113 ? 134.828 126.267 145.396 1.00 93.75  ? 3113 MET A CG    1 
ATOM   13188 S  SD    . MET A 1 3113 ? 136.349 126.283 146.363 1.00 98.63  ? 3113 MET A SD    1 
ATOM   13189 C  CE    . MET A 1 3113 ? 135.951 125.156 147.689 1.00 93.36  ? 3113 MET A CE    1 
ATOM   13190 N  N     . ASP A 1 3114 ? 131.706 123.091 145.407 1.00 105.52 ? 3114 ASP A N     1 
ATOM   13191 C  CA    . ASP A 1 3114 ? 130.821 122.020 145.847 1.00 111.22 ? 3114 ASP A CA    1 
ATOM   13192 C  C     . ASP A 1 3114 ? 130.802 121.906 147.366 1.00 113.96 ? 3114 ASP A C     1 
ATOM   13193 O  O     . ASP A 1 3114 ? 129.785 122.206 148.000 1.00 116.79 ? 3114 ASP A O     1 
ATOM   13194 C  CB    . ASP A 1 3114 ? 131.248 120.689 145.224 1.00 109.86 ? 3114 ASP A CB    1 
ATOM   13195 C  CG    . ASP A 1 3114 ? 130.197 119.608 145.376 1.00 110.57 ? 3114 ASP A CG    1 
ATOM   13196 O  OD1   . ASP A 1 3114 ? 129.073 119.924 145.819 1.00 110.47 ? 3114 ASP A OD1   1 
ATOM   13197 O  OD2   . ASP A 1 3114 ? 130.495 118.439 145.052 1.00 108.90 ? 3114 ASP A OD2   1 
ATOM   13198 N  N     . LEU A 1 3115 ? 131.930 121.498 147.955 1.00 103.39 ? 3115 LEU A N     1 
ATOM   13199 C  CA    . LEU A 1 3115 ? 132.089 121.412 149.410 1.00 102.93 ? 3115 LEU A CA    1 
ATOM   13200 C  C     . LEU A 1 3115 ? 130.946 120.650 150.078 1.00 104.24 ? 3115 LEU A C     1 
ATOM   13201 O  O     . LEU A 1 3115 ? 130.584 120.928 151.223 1.00 103.30 ? 3115 LEU A O     1 
ATOM   13202 C  CB    . LEU A 1 3115 ? 132.231 122.804 150.027 1.00 102.05 ? 3115 LEU A CB    1 
ATOM   13203 C  CG    . LEU A 1 3115 ? 133.577 123.496 149.824 1.00 101.70 ? 3115 LEU A CG    1 
ATOM   13204 C  CD1   . LEU A 1 3115 ? 133.865 124.428 150.983 1.00 104.12 ? 3115 LEU A CD1   1 
ATOM   13205 C  CD2   . LEU A 1 3115 ? 134.687 122.465 149.683 1.00 102.85 ? 3115 LEU A CD2   1 
ATOM   13206 N  N     . GLU A 1 3116 ? 130.369 119.683 149.374 1.00 110.87 ? 3116 GLU A N     1 
ATOM   13207 C  CA    . GLU A 1 3116 ? 129.257 118.897 149.891 1.00 109.46 ? 3116 GLU A CA    1 
ATOM   13208 C  C     . GLU A 1 3116 ? 129.728 117.481 150.182 1.00 111.52 ? 3116 GLU A C     1 
ATOM   13209 O  O     . GLU A 1 3116 ? 130.194 116.778 149.278 1.00 113.42 ? 3116 GLU A O     1 
ATOM   13210 C  CB    . GLU A 1 3116 ? 128.089 118.877 148.903 1.00 109.12 ? 3116 GLU A CB    1 
ATOM   13211 C  CG    . GLU A 1 3116 ? 127.388 120.217 148.741 1.00 110.10 ? 3116 GLU A CG    1 
ATOM   13212 C  CD    . GLU A 1 3116 ? 126.612 120.633 149.977 1.00 114.02 ? 3116 GLU A CD    1 
ATOM   13213 O  OE1   . GLU A 1 3116 ? 126.340 119.767 150.835 1.00 113.45 ? 3116 GLU A OE1   1 
ATOM   13214 O  OE2   . GLU A 1 3116 ? 126.276 121.831 150.092 1.00 113.05 ? 3116 GLU A OE2   1 
ATOM   13215 N  N     . LYS A 1 3117 ? 129.605 117.067 151.442 1.00 112.64 ? 3117 LYS A N     1 
ATOM   13216 C  CA    . LYS A 1 3117 ? 129.971 115.718 151.864 1.00 112.63 ? 3117 LYS A CA    1 
ATOM   13217 C  C     . LYS A 1 3117 ? 128.919 115.232 152.848 1.00 115.79 ? 3117 LYS A C     1 
ATOM   13218 O  O     . LYS A 1 3117 ? 129.023 115.466 154.059 1.00 113.71 ? 3117 LYS A O     1 
ATOM   13219 C  CB    . LYS A 1 3117 ? 131.368 115.684 152.483 1.00 111.52 ? 3117 LYS A CB    1 
ATOM   13220 C  CG    . LYS A 1 3117 ? 132.132 114.398 152.210 1.00 112.62 ? 3117 LYS A CG    1 
ATOM   13221 C  CD    . LYS A 1 3117 ? 133.547 114.461 152.762 1.00 113.26 ? 3117 LYS A CD    1 
ATOM   13222 C  CE    . LYS A 1 3117 ? 133.559 114.339 154.276 1.00 112.53 ? 3117 LYS A CE    1 
ATOM   13223 N  NZ    . LYS A 1 3117 ? 134.844 113.773 154.771 1.00 111.34 ? 3117 LYS A NZ    1 
ATOM   13224 N  N     . PRO A 1 3118 ? 127.875 114.560 152.358 1.00 122.87 ? 3118 PRO A N     1 
ATOM   13225 C  CA    . PRO A 1 3118 ? 126.817 114.087 153.266 1.00 119.93 ? 3118 PRO A CA    1 
ATOM   13226 C  C     . PRO A 1 3118 ? 127.310 113.104 154.312 1.00 118.50 ? 3118 PRO A C     1 
ATOM   13227 O  O     . PRO A 1 3118 ? 126.707 113.003 155.387 1.00 115.17 ? 3118 PRO A O     1 
ATOM   13228 C  CB    . PRO A 1 3118 ? 125.802 113.441 152.313 1.00 119.40 ? 3118 PRO A CB    1 
ATOM   13229 C  CG    . PRO A 1 3118 ? 126.597 113.080 151.100 1.00 118.66 ? 3118 PRO A CG    1 
ATOM   13230 C  CD    . PRO A 1 3118 ? 127.638 114.150 150.964 1.00 118.24 ? 3118 PRO A CD    1 
ATOM   13231 N  N     . ASN A 1 3119 ? 128.392 112.375 154.031 1.00 120.43 ? 3119 ASN A N     1 
ATOM   13232 C  CA    . ASN A 1 3119 ? 128.959 111.416 154.970 1.00 119.78 ? 3119 ASN A CA    1 
ATOM   13233 C  C     . ASN A 1 3119 ? 129.990 112.045 155.900 1.00 120.44 ? 3119 ASN A C     1 
ATOM   13234 O  O     . ASN A 1 3119 ? 130.859 111.337 156.426 1.00 120.64 ? 3119 ASN A O     1 
ATOM   13235 C  CB    . ASN A 1 3119 ? 129.573 110.240 154.211 1.00 119.35 ? 3119 ASN A CB    1 
ATOM   13236 C  CG    . ASN A 1 3119 ? 130.675 110.669 153.262 1.00 118.97 ? 3119 ASN A CG    1 
ATOM   13237 O  OD1   . ASN A 1 3119 ? 130.424 111.356 152.272 1.00 117.92 ? 3119 ASN A OD1   1 
ATOM   13238 N  ND2   . ASN A 1 3119 ? 131.904 110.267 153.561 1.00 117.62 ? 3119 ASN A ND2   1 
ATOM   13239 N  N     . TYR A 1 3120 ? 129.922 113.357 156.111 1.00 112.74 ? 3120 TYR A N     1 
ATOM   13240 C  CA    . TYR A 1 3120 ? 130.838 114.035 157.017 1.00 111.67 ? 3120 TYR A CA    1 
ATOM   13241 C  C     . TYR A 1 3120 ? 130.469 113.722 158.462 1.00 113.10 ? 3120 TYR A C     1 
ATOM   13242 O  O     . TYR A 1 3120 ? 129.295 113.783 158.839 1.00 112.93 ? 3120 TYR A O     1 
ATOM   13243 C  CB    . TYR A 1 3120 ? 130.805 115.543 156.771 1.00 110.84 ? 3120 TYR A CB    1 
ATOM   13244 C  CG    . TYR A 1 3120 ? 131.544 116.358 157.807 1.00 110.99 ? 3120 TYR A CG    1 
ATOM   13245 C  CD1   . TYR A 1 3120 ? 132.928 116.309 157.901 1.00 110.33 ? 3120 TYR A CD1   1 
ATOM   13246 C  CD2   . TYR A 1 3120 ? 130.858 117.180 158.690 1.00 111.99 ? 3120 TYR A CD2   1 
ATOM   13247 C  CE1   . TYR A 1 3120 ? 133.607 117.054 158.846 1.00 109.88 ? 3120 TYR A CE1   1 
ATOM   13248 C  CE2   . TYR A 1 3120 ? 131.527 117.928 159.638 1.00 113.44 ? 3120 TYR A CE2   1 
ATOM   13249 C  CZ    . TYR A 1 3120 ? 132.901 117.861 159.712 1.00 112.24 ? 3120 TYR A CZ    1 
ATOM   13250 O  OH    . TYR A 1 3120 ? 133.572 118.605 160.655 1.00 113.43 ? 3120 TYR A OH    1 
ATOM   13251 N  N     . ILE A 1 3121 ? 131.472 113.386 159.267 1.00 113.76 ? 3121 ILE A N     1 
ATOM   13252 C  CA    . ILE A 1 3121 ? 131.279 113.067 160.677 1.00 112.28 ? 3121 ILE A CA    1 
ATOM   13253 C  C     . ILE A 1 3121 ? 131.778 114.244 161.503 1.00 112.34 ? 3121 ILE A C     1 
ATOM   13254 O  O     . ILE A 1 3121 ? 132.950 114.629 161.407 1.00 114.65 ? 3121 ILE A O     1 
ATOM   13255 C  CB    . ILE A 1 3121 ? 132.008 111.773 161.071 1.00 114.56 ? 3121 ILE A CB    1 
ATOM   13256 C  CG1   . ILE A 1 3121 ? 131.449 110.576 160.298 1.00 113.31 ? 3121 ILE A CG1   1 
ATOM   13257 C  CG2   . ILE A 1 3121 ? 131.902 111.538 162.570 1.00 112.40 ? 3121 ILE A CG2   1 
ATOM   13258 C  CD1   . ILE A 1 3121 ? 132.271 110.191 159.086 1.00 112.38 ? 3121 ILE A CD1   1 
ATOM   13259 N  N     . VAL A 1 3122 ? 130.895 114.815 162.310 1.00 107.75 ? 3122 VAL A N     1 
ATOM   13260 C  CA    . VAL A 1 3122 ? 131.281 115.947 163.160 1.00 109.80 ? 3122 VAL A CA    1 
ATOM   13261 C  C     . VAL A 1 3122 ? 132.165 115.441 164.295 1.00 110.29 ? 3122 VAL A C     1 
ATOM   13262 O  O     . VAL A 1 3122 ? 131.763 114.518 165.025 1.00 110.53 ? 3122 VAL A O     1 
ATOM   13263 C  CB    . VAL A 1 3122 ? 130.039 116.653 163.702 1.00 109.65 ? 3122 VAL A CB    1 
ATOM   13264 C  CG1   . VAL A 1 3122 ? 130.439 117.819 164.593 1.00 107.04 ? 3122 VAL A CG1   1 
ATOM   13265 C  CG2   . VAL A 1 3122 ? 129.156 117.127 162.558 1.00 107.43 ? 3122 VAL A CG2   1 
ATOM   13266 N  N     . PRO A 1 3123 ? 133.362 115.993 164.480 1.00 111.73 ? 3123 PRO A N     1 
ATOM   13267 C  CA    . PRO A 1 3123 ? 134.207 115.557 165.596 1.00 112.46 ? 3123 PRO A CA    1 
ATOM   13268 C  C     . PRO A 1 3123 ? 133.615 115.968 166.935 1.00 114.21 ? 3123 PRO A C     1 
ATOM   13269 O  O     . PRO A 1 3123 ? 132.875 116.949 167.040 1.00 115.37 ? 3123 PRO A O     1 
ATOM   13270 C  CB    . PRO A 1 3123 ? 135.537 116.270 165.333 1.00 111.59 ? 3123 PRO A CB    1 
ATOM   13271 C  CG    . PRO A 1 3123 ? 135.155 117.483 164.557 1.00 113.58 ? 3123 PRO A CG    1 
ATOM   13272 C  CD    . PRO A 1 3123 ? 133.987 117.074 163.701 1.00 113.18 ? 3123 PRO A CD    1 
ATOM   13273 N  N     . ASP A 1 3124 ? 133.949 115.190 167.968 1.00 128.75 ? 3124 ASP A N     1 
ATOM   13274 C  CA    . ASP A 1 3124 ? 133.418 115.464 169.300 1.00 130.16 ? 3124 ASP A CA    1 
ATOM   13275 C  C     . ASP A 1 3124 ? 133.882 116.821 169.814 1.00 129.69 ? 3124 ASP A C     1 
ATOM   13276 O  O     . ASP A 1 3124 ? 133.086 117.591 170.363 1.00 129.83 ? 3124 ASP A O     1 
ATOM   13277 C  CB    . ASP A 1 3124 ? 133.829 114.355 170.267 1.00 129.83 ? 3124 ASP A CB    1 
ATOM   13278 C  CG    . ASP A 1 3124 ? 133.120 113.047 169.985 1.00 131.77 ? 3124 ASP A CG    1 
ATOM   13279 O  OD1   . ASP A 1 3124 ? 131.995 113.085 169.443 1.00 131.08 ? 3124 ASP A OD1   1 
ATOM   13280 O  OD2   . ASP A 1 3124 ? 133.685 111.980 170.305 1.00 132.57 ? 3124 ASP A OD2   1 
ATOM   13281 N  N     . TYR A 1 3125 ? 135.162 117.133 169.644 1.00 132.25 ? 3125 TYR A N     1 
ATOM   13282 C  CA    . TYR A 1 3125 ? 135.724 118.420 170.046 1.00 133.19 ? 3125 TYR A CA    1 
ATOM   13283 C  C     . TYR A 1 3125 ? 135.997 119.216 168.773 1.00 134.49 ? 3125 TYR A C     1 
ATOM   13284 O  O     . TYR A 1 3125 ? 137.099 119.180 168.222 1.00 134.49 ? 3125 TYR A O     1 
ATOM   13285 C  CB    . TYR A 1 3125 ? 136.990 118.238 170.877 1.00 134.13 ? 3125 TYR A CB    1 
ATOM   13286 C  CG    . TYR A 1 3125 ? 137.613 119.542 171.321 1.00 134.70 ? 3125 TYR A CG    1 
ATOM   13287 C  CD1   . TYR A 1 3125 ? 136.982 120.351 172.257 1.00 134.27 ? 3125 TYR A CD1   1 
ATOM   13288 C  CD2   . TYR A 1 3125 ? 138.827 119.967 170.799 1.00 135.13 ? 3125 TYR A CD2   1 
ATOM   13289 C  CE1   . TYR A 1 3125 ? 137.546 121.544 172.664 1.00 135.38 ? 3125 TYR A CE1   1 
ATOM   13290 C  CE2   . TYR A 1 3125 ? 139.398 121.160 171.200 1.00 135.82 ? 3125 TYR A CE2   1 
ATOM   13291 C  CZ    . TYR A 1 3125 ? 138.753 121.944 172.132 1.00 136.20 ? 3125 TYR A CZ    1 
ATOM   13292 O  OH    . TYR A 1 3125 ? 139.318 123.132 172.535 1.00 135.76 ? 3125 TYR A OH    1 
ATOM   13293 N  N     . MET A 1 3126 ? 134.984 119.932 168.309 1.00 123.34 ? 3126 MET A N     1 
ATOM   13294 C  CA    . MET A 1 3126 ? 135.134 120.739 167.107 1.00 121.17 ? 3126 MET A CA    1 
ATOM   13295 C  C     . MET A 1 3126 ? 136.043 121.929 167.393 1.00 119.48 ? 3126 MET A C     1 
ATOM   13296 O  O     . MET A 1 3126 ? 135.800 122.671 168.352 1.00 120.04 ? 3126 MET A O     1 
ATOM   13297 C  CB    . MET A 1 3126 ? 133.772 121.220 166.612 1.00 119.07 ? 3126 MET A CB    1 
ATOM   13298 C  CG    . MET A 1 3126 ? 133.833 122.047 165.340 1.00 118.21 ? 3126 MET A CG    1 
ATOM   13299 S  SD    . MET A 1 3126 ? 134.127 121.050 163.868 1.00 120.95 ? 3126 MET A SD    1 
ATOM   13300 C  CE    . MET A 1 3126 ? 134.067 122.307 162.595 1.00 116.01 ? 3126 MET A CE    1 
ATOM   13301 N  N     . PRO A 1 3127 ? 137.092 122.144 166.599 1.00 109.95 ? 3127 PRO A N     1 
ATOM   13302 C  CA    . PRO A 1 3127 ? 137.940 123.325 166.807 1.00 109.05 ? 3127 PRO A CA    1 
ATOM   13303 C  C     . PRO A 1 3127 ? 137.219 124.595 166.391 1.00 111.02 ? 3127 PRO A C     1 
ATOM   13304 O  O     . PRO A 1 3127 ? 137.527 125.186 165.351 1.00 109.44 ? 3127 PRO A O     1 
ATOM   13305 C  CB    . PRO A 1 3127 ? 139.166 123.051 165.922 1.00 110.74 ? 3127 PRO A CB    1 
ATOM   13306 C  CG    . PRO A 1 3127 ? 139.000 121.641 165.402 1.00 109.76 ? 3127 PRO A CG    1 
ATOM   13307 C  CD    . PRO A 1 3127 ? 137.544 121.333 165.460 1.00 109.37 ? 3127 PRO A CD    1 
ATOM   13308 N  N     . VAL A 1 3128 ? 136.253 125.019 167.202 1.00 116.20 ? 3128 VAL A N     1 
ATOM   13309 C  CA    . VAL A 1 3128 ? 135.388 126.140 166.849 1.00 114.48 ? 3128 VAL A CA    1 
ATOM   13310 C  C     . VAL A 1 3128 ? 136.194 127.430 166.966 1.00 114.28 ? 3128 VAL A C     1 
ATOM   13311 O  O     . VAL A 1 3128 ? 136.671 127.782 168.049 1.00 110.32 ? 3128 VAL A O     1 
ATOM   13312 C  CB    . VAL A 1 3128 ? 134.136 126.181 167.731 1.00 112.85 ? 3128 VAL A CB    1 
ATOM   13313 C  CG1   . VAL A 1 3128 ? 133.477 127.547 167.658 1.00 111.95 ? 3128 VAL A CG1   1 
ATOM   13314 C  CG2   . VAL A 1 3128 ? 133.159 125.096 167.309 1.00 109.86 ? 3128 VAL A CG2   1 
ATOM   13315 N  N     . VAL A 1 3129 ? 136.355 128.128 165.848 1.00 101.57 ? 3129 VAL A N     1 
ATOM   13316 C  CA    . VAL A 1 3129 ? 136.984 129.442 165.820 1.00 98.01  ? 3129 VAL A CA    1 
ATOM   13317 C  C     . VAL A 1 3129 ? 135.942 130.548 165.755 1.00 96.68  ? 3129 VAL A C     1 
ATOM   13318 O  O     . VAL A 1 3129 ? 136.023 131.533 166.489 1.00 99.00  ? 3129 VAL A O     1 
ATOM   13319 C  CB    . VAL A 1 3129 ? 137.975 129.533 164.638 1.00 90.42  ? 3129 VAL A CB    1 
ATOM   13320 C  CG1   . VAL A 1 3129 ? 138.650 130.891 164.618 1.00 90.62  ? 3129 VAL A CG1   1 
ATOM   13321 C  CG2   . VAL A 1 3129 ? 139.003 128.422 164.728 1.00 94.92  ? 3129 VAL A CG2   1 
ATOM   13322 N  N     . TYR A 1 3130 ? 134.951 130.396 164.881 1.00 92.72  ? 3130 TYR A N     1 
ATOM   13323 C  CA    . TYR A 1 3130 ? 133.854 131.349 164.785 1.00 91.82  ? 3130 TYR A CA    1 
ATOM   13324 C  C     . TYR A 1 3130 ? 132.824 131.029 165.862 1.00 101.01 ? 3130 TYR A C     1 
ATOM   13325 O  O     . TYR A 1 3130 ? 132.283 129.919 165.900 1.00 102.72 ? 3130 TYR A O     1 
ATOM   13326 C  CB    . TYR A 1 3130 ? 133.229 131.292 163.394 1.00 88.75  ? 3130 TYR A CB    1 
ATOM   13327 C  CG    . TYR A 1 3130 ? 132.097 132.268 163.180 1.00 89.43  ? 3130 TYR A CG    1 
ATOM   13328 C  CD1   . TYR A 1 3130 ? 132.122 133.529 163.756 1.00 93.98  ? 3130 TYR A CD1   1 
ATOM   13329 C  CD2   . TYR A 1 3130 ? 131.004 131.929 162.395 1.00 92.34  ? 3130 TYR A CD2   1 
ATOM   13330 C  CE1   . TYR A 1 3130 ? 131.089 134.423 163.561 1.00 98.98  ? 3130 TYR A CE1   1 
ATOM   13331 C  CE2   . TYR A 1 3130 ? 129.967 132.817 162.194 1.00 94.12  ? 3130 TYR A CE2   1 
ATOM   13332 C  CZ    . TYR A 1 3130 ? 130.016 134.063 162.777 1.00 96.63  ? 3130 TYR A CZ    1 
ATOM   13333 O  OH    . TYR A 1 3130 ? 128.984 134.951 162.579 1.00 96.70  ? 3130 TYR A OH    1 
ATOM   13334 N  N     . ASP A 1 3131 ? 132.555 132.002 166.736 1.00 104.00 ? 3131 ASP A N     1 
ATOM   13335 C  CA    . ASP A 1 3131 ? 131.673 131.756 167.874 1.00 100.48 ? 3131 ASP A CA    1 
ATOM   13336 C  C     . ASP A 1 3131 ? 130.257 131.412 167.426 1.00 99.65  ? 3131 ASP A C     1 
ATOM   13337 O  O     . ASP A 1 3131 ? 129.624 130.511 167.987 1.00 97.53  ? 3131 ASP A O     1 
ATOM   13338 C  CB    . ASP A 1 3131 ? 131.669 132.971 168.803 1.00 102.82 ? 3131 ASP A CB    1 
ATOM   13339 C  CG    . ASP A 1 3131 ? 131.260 134.249 168.095 1.00 106.31 ? 3131 ASP A CG    1 
ATOM   13340 O  OD1   . ASP A 1 3131 ? 130.072 134.380 167.731 1.00 106.87 ? 3131 ASP A OD1   1 
ATOM   13341 O  OD2   . ASP A 1 3131 ? 132.129 135.125 167.903 1.00 108.27 ? 3131 ASP A OD2   1 
ATOM   13342 N  N     . LYS A 1 3132 ? 129.744 132.114 166.417 1.00 103.30 ? 3132 LYS A N     1 
ATOM   13343 C  CA    . LYS A 1 3132 ? 128.382 131.915 165.943 1.00 102.55 ? 3132 LYS A CA    1 
ATOM   13344 C  C     . LYS A 1 3132 ? 128.272 130.766 164.941 1.00 104.70 ? 3132 LYS A C     1 
ATOM   13345 O  O     . LYS A 1 3132 ? 127.281 130.684 164.206 1.00 106.53 ? 3132 LYS A O     1 
ATOM   13346 C  CB    . LYS A 1 3132 ? 127.847 133.216 165.336 1.00 100.52 ? 3132 LYS A CB    1 
ATOM   13347 C  CG    . LYS A 1 3132 ? 126.328 133.334 165.320 1.00 103.35 ? 3132 LYS A CG    1 
ATOM   13348 C  CD    . LYS A 1 3132 ? 125.823 134.142 166.504 1.00 105.63 ? 3132 LYS A CD    1 
ATOM   13349 C  CE    . LYS A 1 3132 ? 124.304 134.204 166.520 1.00 106.38 ? 3132 LYS A CE    1 
ATOM   13350 N  NZ    . LYS A 1 3132 ? 123.699 132.891 166.879 1.00 105.36 ? 3132 LYS A NZ    1 
ATOM   13351 N  N     . LEU A 1 3133 ? 129.265 129.886 164.894 1.00 105.87 ? 3133 LEU A N     1 
ATOM   13352 C  CA    . LEU A 1 3133 ? 129.175 128.717 164.034 1.00 105.51 ? 3133 LEU A CA    1 
ATOM   13353 C  C     . LEU A 1 3133 ? 128.051 127.805 164.521 1.00 109.48 ? 3133 LEU A C     1 
ATOM   13354 O  O     . LEU A 1 3133 ? 127.872 127.635 165.733 1.00 110.69 ? 3133 LEU A O     1 
ATOM   13355 C  CB    . LEU A 1 3133 ? 130.504 127.958 164.025 1.00 105.08 ? 3133 LEU A CB    1 
ATOM   13356 C  CG    . LEU A 1 3133 ? 130.641 126.781 163.058 1.00 104.64 ? 3133 LEU A CG    1 
ATOM   13357 C  CD1   . LEU A 1 3133 ? 130.870 127.274 161.641 1.00 104.12 ? 3133 LEU A CD1   1 
ATOM   13358 C  CD2   . LEU A 1 3133 ? 131.766 125.859 163.496 1.00 108.57 ? 3133 LEU A CD2   1 
ATOM   13359 N  N     . PRO A 1 3134 ? 127.267 127.222 163.614 1.00 109.83 ? 3134 PRO A N     1 
ATOM   13360 C  CA    . PRO A 1 3134 ? 126.201 126.307 164.044 1.00 108.31 ? 3134 PRO A CA    1 
ATOM   13361 C  C     . PRO A 1 3134 ? 126.761 125.131 164.830 1.00 110.38 ? 3134 PRO A C     1 
ATOM   13362 O  O     . PRO A 1 3134 ? 127.839 124.614 164.530 1.00 113.43 ? 3134 PRO A O     1 
ATOM   13363 C  CB    . PRO A 1 3134 ? 125.571 125.855 162.722 1.00 107.82 ? 3134 PRO A CB    1 
ATOM   13364 C  CG    . PRO A 1 3134 ? 125.865 126.964 161.771 1.00 107.65 ? 3134 PRO A CG    1 
ATOM   13365 C  CD    . PRO A 1 3134 ? 127.211 127.498 162.169 1.00 107.07 ? 3134 PRO A CD    1 
ATOM   13366 N  N     . GLN A 1 3135 ? 126.015 124.718 165.854 1.00 120.94 ? 3135 GLN A N     1 
ATOM   13367 C  CA    . GLN A 1 3135 ? 126.481 123.635 166.717 1.00 123.78 ? 3135 GLN A CA    1 
ATOM   13368 C  C     . GLN A 1 3135 ? 126.685 122.313 165.983 1.00 124.12 ? 3135 GLN A C     1 
ATOM   13369 O  O     . GLN A 1 3135 ? 127.694 121.644 166.263 1.00 121.57 ? 3135 GLN A O     1 
ATOM   13370 C  CB    . GLN A 1 3135 ? 125.522 123.468 167.904 1.00 123.76 ? 3135 GLN A CB    1 
ATOM   13371 C  CG    . GLN A 1 3135 ? 125.195 124.766 168.624 1.00 125.13 ? 3135 GLN A CG    1 
ATOM   13372 C  CD    . GLN A 1 3135 ? 126.431 125.588 168.938 1.00 124.07 ? 3135 GLN A CD    1 
ATOM   13373 O  OE1   . GLN A 1 3135 ? 127.402 125.082 169.499 1.00 121.02 ? 3135 GLN A OE1   1 
ATOM   13374 N  NE2   . GLN A 1 3135 ? 126.399 126.866 168.575 1.00 123.66 ? 3135 GLN A NE2   1 
ATOM   13375 N  N     . PRO A 1 3136 ? 125.779 121.843 165.124 1.00 115.98 ? 3136 PRO A N     1 
ATOM   13376 C  CA    . PRO A 1 3136 ? 126.104 120.713 164.245 1.00 112.67 ? 3136 PRO A CA    1 
ATOM   13377 C  C     . PRO A 1 3136 ? 126.632 121.192 162.903 1.00 112.84 ? 3136 PRO A C     1 
ATOM   13378 O  O     . PRO A 1 3136 ? 125.876 121.241 161.921 1.00 110.26 ? 3136 PRO A O     1 
ATOM   13379 C  CB    . PRO A 1 3136 ? 124.759 119.990 164.091 1.00 111.33 ? 3136 PRO A CB    1 
ATOM   13380 C  CG    . PRO A 1 3136 ? 123.721 121.057 164.308 1.00 111.88 ? 3136 PRO A CG    1 
ATOM   13381 C  CD    . PRO A 1 3136 ? 124.376 122.262 164.946 1.00 112.50 ? 3136 PRO A CD    1 
ATOM   13382 N  N     . PRO A 1 3137 ? 127.910 121.559 162.810 1.00 106.21 ? 3137 PRO A N     1 
ATOM   13383 C  CA    . PRO A 1 3137 ? 128.401 122.165 161.569 1.00 101.40 ? 3137 PRO A CA    1 
ATOM   13384 C  C     . PRO A 1 3137 ? 128.431 121.158 160.429 1.00 102.84 ? 3137 PRO A C     1 
ATOM   13385 O  O     . PRO A 1 3137 ? 128.645 119.962 160.636 1.00 107.45 ? 3137 PRO A O     1 
ATOM   13386 C  CB    . PRO A 1 3137 ? 129.811 122.630 161.940 1.00 100.26 ? 3137 PRO A CB    1 
ATOM   13387 C  CG    . PRO A 1 3137 ? 130.257 121.638 162.953 1.00 102.54 ? 3137 PRO A CG    1 
ATOM   13388 C  CD    . PRO A 1 3137 ? 129.024 121.137 163.678 1.00 105.46 ? 3137 PRO A CD    1 
ATOM   13389 N  N     . SER A 1 3138 ? 128.209 121.657 159.217 1.00 98.19  ? 3138 SER A N     1 
ATOM   13390 C  CA    . SER A 1 3138 ? 128.301 120.834 158.024 1.00 96.86  ? 3138 SER A CA    1 
ATOM   13391 C  C     . SER A 1 3138 ? 129.726 120.878 157.476 1.00 99.12  ? 3138 SER A C     1 
ATOM   13392 O  O     . SER A 1 3138 ? 130.635 121.455 158.078 1.00 102.67 ? 3138 SER A O     1 
ATOM   13393 C  CB    . SER A 1 3138 ? 127.288 121.292 156.977 1.00 93.33  ? 3138 SER A CB    1 
ATOM   13394 O  OG    . SER A 1 3138 ? 127.584 122.598 156.517 1.00 99.76  ? 3138 SER A OG    1 
ATOM   13395 N  N     . HIS A 1 3139 ? 129.929 120.250 156.316 1.00 93.74  ? 3139 HIS A N     1 
ATOM   13396 C  CA    . HIS A 1 3139 ? 131.254 120.243 155.706 1.00 94.12  ? 3139 HIS A CA    1 
ATOM   13397 C  C     . HIS A 1 3139 ? 131.681 121.646 155.292 1.00 96.88  ? 3139 HIS A C     1 
ATOM   13398 O  O     . HIS A 1 3139 ? 132.821 122.056 155.543 1.00 97.25  ? 3139 HIS A O     1 
ATOM   13399 C  CB    . HIS A 1 3139 ? 131.270 119.300 154.504 1.00 95.20  ? 3139 HIS A CB    1 
ATOM   13400 C  CG    . HIS A 1 3139 ? 132.639 119.039 153.959 1.00 94.56  ? 3139 HIS A CG    1 
ATOM   13401 N  ND1   . HIS A 1 3139 ? 133.666 118.544 154.734 1.00 94.42  ? 3139 HIS A ND1   1 
ATOM   13402 C  CD2   . HIS A 1 3139 ? 133.150 119.202 152.716 1.00 93.38  ? 3139 HIS A CD2   1 
ATOM   13403 C  CE1   . HIS A 1 3139 ? 134.751 118.415 153.992 1.00 94.17  ? 3139 HIS A CE1   1 
ATOM   13404 N  NE2   . HIS A 1 3139 ? 134.464 118.807 152.763 1.00 93.55  ? 3139 HIS A NE2   1 
ATOM   13405 N  N     . ARG A 1 3140 ? 130.776 122.399 154.661 1.00 94.08  ? 3140 ARG A N     1 
ATOM   13406 C  CA    . ARG A 1 3140 ? 131.114 123.743 154.202 1.00 93.36  ? 3140 ARG A CA    1 
ATOM   13407 C  C     . ARG A 1 3140 ? 131.449 124.659 155.371 1.00 95.29  ? 3140 ARG A C     1 
ATOM   13408 O  O     . ARG A 1 3140 ? 132.420 125.426 155.314 1.00 100.61 ? 3140 ARG A O     1 
ATOM   13409 C  CB    . ARG A 1 3140 ? 129.955 124.318 153.389 1.00 90.07  ? 3140 ARG A CB    1 
ATOM   13410 C  CG    . ARG A 1 3140 ? 130.305 125.553 152.582 1.00 93.14  ? 3140 ARG A CG    1 
ATOM   13411 C  CD    . ARG A 1 3140 ? 129.082 126.093 151.862 1.00 94.22  ? 3140 ARG A CD    1 
ATOM   13412 N  NE    . ARG A 1 3140 ? 128.563 125.146 150.882 1.00 97.25  ? 3140 ARG A NE    1 
ATOM   13413 C  CZ    . ARG A 1 3140 ? 129.041 125.001 149.655 1.00 95.58  ? 3140 ARG A CZ    1 
ATOM   13414 N  NH1   . ARG A 1 3140 ? 130.055 125.728 149.217 1.00 95.20  ? 3140 ARG A NH1   1 
ATOM   13415 N  NH2   . ARG A 1 3140 ? 128.486 124.104 148.845 1.00 93.10  ? 3140 ARG A NH2   1 
ATOM   13416 N  N     . GLU A 1 3141 ? 130.655 124.593 156.441 1.00 91.69  ? 3141 GLU A N     1 
ATOM   13417 C  CA    . GLU A 1 3141 ? 130.918 125.424 157.609 1.00 91.15  ? 3141 GLU A CA    1 
ATOM   13418 C  C     . GLU A 1 3141 ? 132.249 125.058 158.251 1.00 96.36  ? 3141 GLU A C     1 
ATOM   13419 O  O     . GLU A 1 3141 ? 133.001 125.939 158.682 1.00 98.46  ? 3141 GLU A O     1 
ATOM   13420 C  CB    . GLU A 1 3141 ? 129.772 125.292 158.611 1.00 89.46  ? 3141 GLU A CB    1 
ATOM   13421 C  CG    . GLU A 1 3141 ? 128.462 125.890 158.120 1.00 91.72  ? 3141 GLU A CG    1 
ATOM   13422 C  CD    . GLU A 1 3141 ? 127.267 125.004 158.401 1.00 100.09 ? 3141 GLU A CD    1 
ATOM   13423 O  OE1   . GLU A 1 3141 ? 126.306 125.028 157.604 1.00 100.04 ? 3141 GLU A OE1   1 
ATOM   13424 O  OE2   . GLU A 1 3141 ? 127.286 124.286 159.422 1.00 103.31 ? 3141 GLU A OE2   1 
ATOM   13425 N  N     . ALA A 1 3142 ? 132.563 123.762 158.310 1.00 89.65  ? 3142 ALA A N     1 
ATOM   13426 C  CA    . ALA A 1 3142 ? 133.852 123.338 158.845 1.00 89.10  ? 3142 ALA A CA    1 
ATOM   13427 C  C     . ALA A 1 3142 ? 135.002 123.859 157.993 1.00 91.29  ? 3142 ALA A C     1 
ATOM   13428 O  O     . ALA A 1 3142 ? 136.028 124.299 158.524 1.00 97.30  ? 3142 ALA A O     1 
ATOM   13429 C  CB    . ALA A 1 3142 ? 133.903 121.814 158.942 1.00 88.12  ? 3142 ALA A CB    1 
ATOM   13430 N  N     . ILE A 1 3143 ? 134.850 123.819 156.668 1.00 75.60  ? 3143 ILE A N     1 
ATOM   13431 C  CA    . ILE A 1 3143 ? 135.908 124.303 155.782 1.00 74.32  ? 3143 ILE A CA    1 
ATOM   13432 C  C     . ILE A 1 3143 ? 136.129 125.799 155.980 1.00 78.26  ? 3143 ILE A C     1 
ATOM   13433 O  O     . ILE A 1 3143 ? 137.270 126.274 156.061 1.00 80.33  ? 3143 ILE A O     1 
ATOM   13434 C  CB    . ILE A 1 3143 ? 135.574 123.971 154.317 1.00 72.36  ? 3143 ILE A CB    1 
ATOM   13435 C  CG1   . ILE A 1 3143 ? 135.608 122.459 154.090 1.00 74.65  ? 3143 ILE A CG1   1 
ATOM   13436 C  CG2   . ILE A 1 3143 ? 136.545 124.665 153.384 1.00 76.73  ? 3143 ILE A CG2   1 
ATOM   13437 C  CD1   . ILE A 1 3143 ? 136.999 121.874 154.082 1.00 77.43  ? 3143 ILE A CD1   1 
ATOM   13438 N  N     . VAL A 1 3144 ? 135.040 126.567 156.059 1.00 74.28  ? 3144 VAL A N     1 
ATOM   13439 C  CA    . VAL A 1 3144 ? 135.185 128.010 156.237 1.00 74.87  ? 3144 VAL A CA    1 
ATOM   13440 C  C     . VAL A 1 3144 ? 135.785 128.325 157.604 1.00 80.38  ? 3144 VAL A C     1 
ATOM   13441 O  O     . VAL A 1 3144 ? 136.606 129.242 157.742 1.00 80.75  ? 3144 VAL A O     1 
ATOM   13442 C  CB    . VAL A 1 3144 ? 133.837 128.720 156.025 1.00 70.25  ? 3144 VAL A CB    1 
ATOM   13443 C  CG1   . VAL A 1 3144 ? 134.016 130.222 156.122 1.00 75.73  ? 3144 VAL A CG1   1 
ATOM   13444 C  CG2   . VAL A 1 3144 ? 133.263 128.359 154.670 1.00 66.03  ? 3144 VAL A CG2   1 
ATOM   13445 N  N     . ASN A 1 3145 ? 135.395 127.568 158.634 1.00 78.46  ? 3145 ASN A N     1 
ATOM   13446 C  CA    . ASN A 1 3145 ? 136.002 127.741 159.949 1.00 77.36  ? 3145 ASN A CA    1 
ATOM   13447 C  C     . ASN A 1 3145 ? 137.496 127.454 159.901 1.00 83.08  ? 3145 ASN A C     1 
ATOM   13448 O  O     . ASN A 1 3145 ? 138.293 128.156 160.534 1.00 87.73  ? 3145 ASN A O     1 
ATOM   13449 C  CB    . ASN A 1 3145 ? 135.311 126.834 160.966 1.00 76.15  ? 3145 ASN A CB    1 
ATOM   13450 C  CG    . ASN A 1 3145 ? 135.710 127.149 162.392 1.00 83.97  ? 3145 ASN A CG    1 
ATOM   13451 O  OD1   . ASN A 1 3145 ? 135.466 128.248 162.888 1.00 90.59  ? 3145 ASN A OD1   1 
ATOM   13452 N  ND2   . ASN A 1 3145 ? 136.328 126.184 163.060 1.00 83.40  ? 3145 ASN A ND2   1 
ATOM   13453 N  N     . SER A 1 3146 ? 137.894 126.425 159.150 1.00 75.79  ? 3146 SER A N     1 
ATOM   13454 C  CA    . SER A 1 3146 ? 139.313 126.132 158.988 1.00 76.80  ? 3146 SER A CA    1 
ATOM   13455 C  C     . SER A 1 3146 ? 140.037 127.276 158.289 1.00 81.81  ? 3146 SER A C     1 
ATOM   13456 O  O     . SER A 1 3146 ? 141.175 127.604 158.638 1.00 82.99  ? 3146 SER A O     1 
ATOM   13457 C  CB    . SER A 1 3146 ? 139.492 124.828 158.214 1.00 77.75  ? 3146 SER A CB    1 
ATOM   13458 O  OG    . SER A 1 3146 ? 138.859 123.751 158.881 1.00 81.91  ? 3146 SER A OG    1 
ATOM   13459 N  N     . CYS A 1 3147 ? 139.399 127.887 157.288 1.00 67.84  ? 3147 CYS A N     1 
ATOM   13460 C  CA    . CYS A 1 3147 ? 140.016 129.028 156.610 1.00 63.06  ? 3147 CYS A CA    1 
ATOM   13461 C  C     . CYS A 1 3147 ? 140.222 130.201 157.567 1.00 72.11  ? 3147 CYS A C     1 
ATOM   13462 O  O     . CYS A 1 3147 ? 141.293 130.833 157.580 1.00 78.58  ? 3147 CYS A O     1 
ATOM   13463 C  CB    . CYS A 1 3147 ? 139.158 129.453 155.419 1.00 62.43  ? 3147 CYS A CB    1 
ATOM   13464 S  SG    . CYS A 1 3147 ? 139.006 128.208 154.121 1.00 69.92  ? 3147 CYS A SG    1 
ATOM   13465 N  N     . VAL A 1 3148 ? 139.204 130.508 158.374 1.00 67.18  ? 3148 VAL A N     1 
ATOM   13466 C  CA    . VAL A 1 3148 ? 139.349 131.571 159.366 1.00 60.37  ? 3148 VAL A CA    1 
ATOM   13467 C  C     . VAL A 1 3148 ? 140.458 131.227 160.352 1.00 70.71  ? 3148 VAL A C     1 
ATOM   13468 O  O     . VAL A 1 3148 ? 141.240 132.098 160.761 1.00 74.20  ? 3148 VAL A O     1 
ATOM   13469 C  CB    . VAL A 1 3148 ? 138.014 131.836 160.085 1.00 58.91  ? 3148 VAL A CB    1 
ATOM   13470 C  CG1   . VAL A 1 3148 ? 138.118 133.095 160.921 1.00 66.00  ? 3148 VAL A CG1   1 
ATOM   13471 C  CG2   . VAL A 1 3148 ? 136.897 131.990 159.077 1.00 64.06  ? 3148 VAL A CG2   1 
ATOM   13472 N  N     . PHE A 1 3149 ? 140.551 129.954 160.746 1.00 69.14  ? 3149 PHE A N     1 
ATOM   13473 C  CA    . PHE A 1 3149 ? 141.633 129.550 161.635 1.00 66.38  ? 3149 PHE A CA    1 
ATOM   13474 C  C     . PHE A 1 3149 ? 142.987 129.740 160.971 1.00 69.41  ? 3149 PHE A C     1 
ATOM   13475 O  O     . PHE A 1 3149 ? 143.967 130.067 161.642 1.00 80.31  ? 3149 PHE A O     1 
ATOM   13476 C  CB    . PHE A 1 3149 ? 141.480 128.095 162.071 1.00 67.81  ? 3149 PHE A CB    1 
ATOM   13477 C  CG    . PHE A 1 3149 ? 142.674 127.577 162.823 1.00 70.23  ? 3149 PHE A CG    1 
ATOM   13478 C  CD1   . PHE A 1 3149 ? 142.825 127.851 164.171 1.00 72.02  ? 3149 PHE A CD1   1 
ATOM   13479 C  CD2   . PHE A 1 3149 ? 143.666 126.858 162.177 1.00 68.75  ? 3149 PHE A CD2   1 
ATOM   13480 C  CE1   . PHE A 1 3149 ? 143.926 127.393 164.866 1.00 72.03  ? 3149 PHE A CE1   1 
ATOM   13481 C  CE2   . PHE A 1 3149 ? 144.772 126.403 162.867 1.00 71.04  ? 3149 PHE A CE2   1 
ATOM   13482 C  CZ    . PHE A 1 3149 ? 144.900 126.668 164.213 1.00 72.29  ? 3149 PHE A CZ    1 
ATOM   13483 N  N     . VAL A 1 3150 ? 143.073 129.490 159.664 1.00 56.29  ? 3150 VAL A N     1 
ATOM   13484 C  CA    . VAL A 1 3150 ? 144.334 129.681 158.951 1.00 62.46  ? 3150 VAL A CA    1 
ATOM   13485 C  C     . VAL A 1 3150 ? 144.753 131.144 159.010 1.00 62.94  ? 3150 VAL A C     1 
ATOM   13486 O  O     . VAL A 1 3150 ? 145.919 131.472 159.276 1.00 70.57  ? 3150 VAL A O     1 
ATOM   13487 C  CB    . VAL A 1 3150 ? 144.216 129.183 157.500 1.00 59.52  ? 3150 VAL A CB    1 
ATOM   13488 C  CG1   . VAL A 1 3150 ? 145.402 129.656 156.683 1.00 62.70  ? 3150 VAL A CG1   1 
ATOM   13489 C  CG2   . VAL A 1 3150 ? 144.127 127.667 157.466 1.00 60.18  ? 3150 VAL A CG2   1 
ATOM   13490 N  N     . HIS A 1 3151 ? 143.802 132.047 158.779 1.00 52.17  ? 3151 HIS A N     1 
ATOM   13491 C  CA    . HIS A 1 3151 ? 144.118 133.470 158.888 1.00 53.34  ? 3151 HIS A CA    1 
ATOM   13492 C  C     . HIS A 1 3151 ? 144.577 133.820 160.304 1.00 64.76  ? 3151 HIS A C     1 
ATOM   13493 O  O     . HIS A 1 3151 ? 145.569 134.541 160.499 1.00 74.87  ? 3151 HIS A O     1 
ATOM   13494 C  CB    . HIS A 1 3151 ? 142.907 134.309 158.482 1.00 59.95  ? 3151 HIS A CB    1 
ATOM   13495 C  CG    . HIS A 1 3151 ? 143.257 135.683 158.000 1.00 59.90  ? 3151 HIS A CG    1 
ATOM   13496 N  ND1   . HIS A 1 3151 ? 143.831 135.916 156.770 1.00 60.81  ? 3151 HIS A ND1   1 
ATOM   13497 C  CD2   . HIS A 1 3151 ? 143.112 136.896 158.583 1.00 61.86  ? 3151 HIS A CD2   1 
ATOM   13498 C  CE1   . HIS A 1 3151 ? 144.026 137.213 156.615 1.00 60.92  ? 3151 HIS A CE1   1 
ATOM   13499 N  NE2   . HIS A 1 3151 ? 143.598 137.831 157.701 1.00 61.14  ? 3151 HIS A NE2   1 
ATOM   13500 N  N     . GLN A 1 3152 ? 143.882 133.287 161.312 1.00 69.33  ? 3152 GLN A N     1 
ATOM   13501 C  CA    . GLN A 1 3152 ? 144.241 133.600 162.692 1.00 67.14  ? 3152 GLN A CA    1 
ATOM   13502 C  C     . GLN A 1 3152 ? 145.599 133.022 163.082 1.00 71.22  ? 3152 GLN A C     1 
ATOM   13503 O  O     . GLN A 1 3152 ? 146.338 133.651 163.846 1.00 74.51  ? 3152 GLN A O     1 
ATOM   13504 C  CB    . GLN A 1 3152 ? 143.155 133.110 163.648 1.00 63.50  ? 3152 GLN A CB    1 
ATOM   13505 C  CG    . GLN A 1 3152 ? 141.794 133.743 163.403 1.00 64.69  ? 3152 GLN A CG    1 
ATOM   13506 C  CD    . GLN A 1 3152 ? 140.994 133.919 164.677 1.00 72.74  ? 3152 GLN A CD    1 
ATOM   13507 O  OE1   . GLN A 1 3152 ? 140.916 133.013 165.505 1.00 74.74  ? 3152 GLN A OE1   1 
ATOM   13508 N  NE2   . GLN A 1 3152 ? 140.396 135.093 164.843 1.00 72.16  ? 3152 GLN A NE2   1 
ATOM   13509 N  N     . THR A 1 3153 ? 145.956 131.837 162.580 1.00 66.91  ? 3153 THR A N     1 
ATOM   13510 C  CA    . THR A 1 3153 ? 147.262 131.293 162.932 1.00 67.01  ? 3153 THR A CA    1 
ATOM   13511 C  C     . THR A 1 3153 ? 148.376 131.993 162.171 1.00 65.40  ? 3153 THR A C     1 
ATOM   13512 O  O     . THR A 1 3153 ? 149.508 132.028 162.653 1.00 76.26  ? 3153 THR A O     1 
ATOM   13513 C  CB    . THR A 1 3153 ? 147.347 129.782 162.691 1.00 79.48  ? 3153 THR A CB    1 
ATOM   13514 O  OG1   . THR A 1 3153 ? 148.709 129.364 162.837 1.00 87.12  ? 3153 THR A OG1   1 
ATOM   13515 C  CG2   . THR A 1 3153 ? 146.927 129.428 161.298 1.00 67.03  ? 3153 THR A CG2   1 
ATOM   13516 N  N     . LEU A 1 3154 ? 148.086 132.563 161.000 1.00 62.39  ? 3154 LEU A N     1 
ATOM   13517 C  CA    . LEU A 1 3154 ? 149.055 133.476 160.395 1.00 64.51  ? 3154 LEU A CA    1 
ATOM   13518 C  C     . LEU A 1 3154 ? 149.272 134.708 161.268 1.00 64.87  ? 3154 LEU A C     1 
ATOM   13519 O  O     . LEU A 1 3154 ? 150.412 135.164 161.446 1.00 69.53  ? 3154 LEU A O     1 
ATOM   13520 C  CB    . LEU A 1 3154 ? 148.614 133.882 158.990 1.00 56.58  ? 3154 LEU A CB    1 
ATOM   13521 C  CG    . LEU A 1 3154 ? 149.066 133.008 157.822 1.00 64.87  ? 3154 LEU A CG    1 
ATOM   13522 C  CD1   . LEU A 1 3154 ? 150.523 133.318 157.523 1.00 59.80  ? 3154 LEU A CD1   1 
ATOM   13523 C  CD2   . LEU A 1 3154 ? 148.884 131.532 158.093 1.00 78.61  ? 3154 LEU A CD2   1 
ATOM   13524 N  N     . HIS A 1 3155 ? 148.188 135.266 161.815 1.00 73.90  ? 3155 HIS A N     1 
ATOM   13525 C  CA    . HIS A 1 3155 ? 148.340 136.365 162.769 1.00 72.26  ? 3155 HIS A CA    1 
ATOM   13526 C  C     . HIS A 1 3155 ? 149.200 135.946 163.958 1.00 74.96  ? 3155 HIS A C     1 
ATOM   13527 O  O     . HIS A 1 3155 ? 150.101 136.683 164.380 1.00 76.08  ? 3155 HIS A O     1 
ATOM   13528 C  CB    . HIS A 1 3155 ? 146.971 136.845 163.250 1.00 75.18  ? 3155 HIS A CB    1 
ATOM   13529 C  CG    . HIS A 1 3155 ? 146.322 137.842 162.342 1.00 73.73  ? 3155 HIS A CG    1 
ATOM   13530 N  ND1   . HIS A 1 3155 ? 146.804 139.122 162.177 1.00 77.75  ? 3155 HIS A ND1   1 
ATOM   13531 C  CD2   . HIS A 1 3155 ? 145.223 137.750 161.557 1.00 74.03  ? 3155 HIS A CD2   1 
ATOM   13532 C  CE1   . HIS A 1 3155 ? 146.033 139.775 161.326 1.00 80.64  ? 3155 HIS A CE1   1 
ATOM   13533 N  NE2   . HIS A 1 3155 ? 145.066 138.964 160.935 1.00 78.40  ? 3155 HIS A NE2   1 
ATOM   13534 N  N     . GLN A 1 3156 ? 148.933 134.759 164.506 1.00 82.08  ? 3156 GLN A N     1 
ATOM   13535 C  CA    . GLN A 1 3156 ? 149.703 134.261 165.642 1.00 82.04  ? 3156 GLN A CA    1 
ATOM   13536 C  C     . GLN A 1 3156 ? 151.165 134.038 165.273 1.00 80.15  ? 3156 GLN A C     1 
ATOM   13537 O  O     . GLN A 1 3156 ? 152.058 134.277 166.091 1.00 80.38  ? 3156 GLN A O     1 
ATOM   13538 C  CB    . GLN A 1 3156 ? 149.084 132.967 166.170 1.00 82.06  ? 3156 GLN A CB    1 
ATOM   13539 C  CG    . GLN A 1 3156 ? 147.782 133.163 166.924 1.00 84.10  ? 3156 GLN A CG    1 
ATOM   13540 C  CD    . GLN A 1 3156 ? 146.879 131.947 166.851 1.00 88.23  ? 3156 GLN A CD    1 
ATOM   13541 O  OE1   . GLN A 1 3156 ? 147.345 130.824 166.656 1.00 87.95  ? 3156 GLN A OE1   1 
ATOM   13542 N  NE2   . GLN A 1 3156 ? 145.579 132.165 167.010 1.00 82.51  ? 3156 GLN A NE2   1 
ATOM   13543 N  N     . ALA A 1 3157 ? 151.426 133.558 164.056 1.00 88.05  ? 3157 ALA A N     1 
ATOM   13544 C  CA    . ALA A 1 3157 ? 152.799 133.338 163.618 1.00 87.04  ? 3157 ALA A CA    1 
ATOM   13545 C  C     . ALA A 1 3157 ? 153.560 134.650 163.506 1.00 86.43  ? 3157 ALA A C     1 
ATOM   13546 O  O     . ALA A 1 3157 ? 154.723 134.733 163.916 1.00 94.06  ? 3157 ALA A O     1 
ATOM   13547 C  CB    . ALA A 1 3157 ? 152.813 132.594 162.284 1.00 85.48  ? 3157 ALA A CB    1 
ATOM   13548 N  N     . ASN A 1 3158 ? 152.927 135.686 162.948 1.00 83.47  ? 3158 ASN A N     1 
ATOM   13549 C  CA    . ASN A 1 3158 ? 153.583 136.992 162.918 1.00 80.59  ? 3158 ASN A CA    1 
ATOM   13550 C  C     . ASN A 1 3158 ? 153.813 137.530 164.324 1.00 84.29  ? 3158 ASN A C     1 
ATOM   13551 O  O     . ASN A 1 3158 ? 154.858 138.130 164.599 1.00 85.75  ? 3158 ASN A O     1 
ATOM   13552 C  CB    . ASN A 1 3158 ? 152.780 137.990 162.086 1.00 82.26  ? 3158 ASN A CB    1 
ATOM   13553 C  CG    . ASN A 1 3158 ? 153.200 138.001 160.633 1.00 87.76  ? 3158 ASN A CG    1 
ATOM   13554 O  OD1   . ASN A 1 3158 ? 152.371 138.100 159.735 1.00 91.09  ? 3158 ASN A OD1   1 
ATOM   13555 N  ND2   . ASN A 1 3158 ? 154.501 137.896 160.396 1.00 87.89  ? 3158 ASN A ND2   1 
ATOM   13556 N  N     . ALA A 1 3159 ? 152.850 137.329 165.228 1.00 95.11  ? 3159 ALA A N     1 
ATOM   13557 C  CA    . ALA A 1 3159 ? 153.046 137.763 166.609 1.00 97.60  ? 3159 ALA A CA    1 
ATOM   13558 C  C     . ALA A 1 3159 ? 154.231 137.048 167.251 1.00 96.95  ? 3159 ALA A C     1 
ATOM   13559 O  O     . ALA A 1 3159 ? 155.058 137.677 167.923 1.00 99.07  ? 3159 ALA A O     1 
ATOM   13560 C  CB    . ALA A 1 3159 ? 151.772 137.526 167.419 1.00 97.75  ? 3159 ALA A CB    1 
ATOM   13561 N  N     . ARG A 1 3160 ? 154.329 135.733 167.049 1.00 104.42 ? 3160 ARG A N     1 
ATOM   13562 C  CA    . ARG A 1 3160 ? 155.436 134.963 167.606 1.00 102.75 ? 3160 ARG A CA    1 
ATOM   13563 C  C     . ARG A 1 3160 ? 156.770 135.403 167.016 1.00 101.78 ? 3160 ARG A C     1 
ATOM   13564 O  O     . ARG A 1 3160 ? 157.768 135.517 167.736 1.00 105.59 ? 3160 ARG A O     1 
ATOM   13565 C  CB    . ARG A 1 3160 ? 155.207 133.472 167.357 1.00 101.81 ? 3160 ARG A CB    1 
ATOM   13566 C  CG    . ARG A 1 3160 ? 156.250 132.560 167.978 1.00 103.75 ? 3160 ARG A CG    1 
ATOM   13567 C  CD    . ARG A 1 3160 ? 155.782 131.112 167.974 1.00 105.96 ? 3160 ARG A CD    1 
ATOM   13568 N  NE    . ARG A 1 3160 ? 156.899 130.175 167.978 1.00 110.70 ? 3160 ARG A NE    1 
ATOM   13569 C  CZ    . ARG A 1 3160 ? 156.769 128.855 167.988 1.00 109.96 ? 3160 ARG A CZ    1 
ATOM   13570 N  NH1   . ARG A 1 3160 ? 155.579 128.277 167.995 1.00 108.75 ? 3160 ARG A NH1   1 
ATOM   13571 N  NH2   . ARG A 1 3160 ? 157.861 128.096 167.990 1.00 102.15 ? 3160 ARG A NH2   1 
ATOM   13572 N  N     . LEU A 1 3161 ? 156.807 135.648 165.705 1.00 89.52  ? 3161 LEU A N     1 
ATOM   13573 C  CA    . LEU A 1 3161 ? 158.045 136.080 165.067 1.00 88.52  ? 3161 LEU A CA    1 
ATOM   13574 C  C     . LEU A 1 3161 ? 158.466 137.461 165.554 1.00 91.82  ? 3161 LEU A C     1 
ATOM   13575 O  O     . LEU A 1 3161 ? 159.660 137.720 165.746 1.00 93.93  ? 3161 LEU A O     1 
ATOM   13576 C  CB    . LEU A 1 3161 ? 157.881 136.068 163.548 1.00 91.19  ? 3161 LEU A CB    1 
ATOM   13577 C  CG    . LEU A 1 3161 ? 159.160 135.911 162.727 1.00 90.49  ? 3161 LEU A CG    1 
ATOM   13578 C  CD1   . LEU A 1 3161 ? 159.766 134.538 162.948 1.00 90.80  ? 3161 LEU A CD1   1 
ATOM   13579 C  CD2   . LEU A 1 3161 ? 158.876 136.139 161.253 1.00 93.81  ? 3161 LEU A CD2   1 
ATOM   13580 N  N     . ALA A 1 3162 ? 157.501 138.363 165.755 1.00 100.23 ? 3162 ALA A N     1 
ATOM   13581 C  CA    . ALA A 1 3162 ? 157.824 139.693 166.258 1.00 103.22 ? 3162 ALA A CA    1 
ATOM   13582 C  C     . ALA A 1 3162 ? 158.276 139.653 167.711 1.00 108.25 ? 3162 ALA A C     1 
ATOM   13583 O  O     . ALA A 1 3162 ? 159.137 140.444 168.111 1.00 104.48 ? 3162 ALA A O     1 
ATOM   13584 C  CB    . ALA A 1 3162 ? 156.619 140.621 166.104 1.00 100.83 ? 3162 ALA A CB    1 
ATOM   13585 N  N     . LYS A 1 3163 ? 157.706 138.750 168.514 1.00 119.19 ? 3163 LYS A N     1 
ATOM   13586 C  CA    . LYS A 1 3163 ? 158.123 138.635 169.908 1.00 115.50 ? 3163 LYS A CA    1 
ATOM   13587 C  C     . LYS A 1 3163 ? 159.585 138.226 170.024 1.00 115.10 ? 3163 LYS A C     1 
ATOM   13588 O  O     . LYS A 1 3163 ? 160.312 138.757 170.872 1.00 114.94 ? 3163 LYS A O     1 
ATOM   13589 C  CB    . LYS A 1 3163 ? 157.234 137.630 170.641 1.00 114.74 ? 3163 LYS A CB    1 
ATOM   13590 C  CG    . LYS A 1 3163 ? 157.406 137.632 172.151 1.00 115.82 ? 3163 LYS A CG    1 
ATOM   13591 C  CD    . LYS A 1 3163 ? 156.398 136.717 172.834 1.00 114.96 ? 3163 LYS A CD    1 
ATOM   13592 C  CE    . LYS A 1 3163 ? 156.257 135.384 172.110 1.00 113.78 ? 3163 LYS A CE    1 
ATOM   13593 N  NZ    . LYS A 1 3163 ? 157.562 134.679 171.958 1.00 114.46 ? 3163 LYS A NZ    1 
ATOM   13594 N  N     . ARG A 1 3164 ? 160.033 137.294 169.188 1.00 110.67 ? 3164 ARG A N     1 
ATOM   13595 C  CA    . ARG A 1 3164 ? 161.419 136.854 169.168 1.00 109.12 ? 3164 ARG A CA    1 
ATOM   13596 C  C     . ARG A 1 3164 ? 162.372 137.942 168.684 1.00 110.82 ? 3164 ARG A C     1 
ATOM   13597 O  O     . ARG A 1 3164 ? 163.523 137.987 169.130 1.00 113.39 ? 3164 ARG A O     1 
ATOM   13598 C  CB    . ARG A 1 3164 ? 161.549 135.598 168.298 1.00 106.98 ? 3164 ARG A CB    1 
ATOM   13599 C  CG    . ARG A 1 3164 ? 162.876 135.439 167.572 1.00 108.27 ? 3164 ARG A CG    1 
ATOM   13600 C  CD    . ARG A 1 3164 ? 163.166 133.983 167.228 1.00 111.87 ? 3164 ARG A CD    1 
ATOM   13601 N  NE    . ARG A 1 3164 ? 162.049 133.328 166.556 1.00 115.28 ? 3164 ARG A NE    1 
ATOM   13602 C  CZ    . ARG A 1 3164 ? 161.207 132.487 167.142 1.00 114.90 ? 3164 ARG A CZ    1 
ATOM   13603 N  NH1   . ARG A 1 3164 ? 161.326 132.169 168.420 1.00 113.83 ? 3164 ARG A NH1   1 
ATOM   13604 N  NH2   . ARG A 1 3164 ? 160.221 131.953 166.427 1.00 112.74 ? 3164 ARG A NH2   1 
ATOM   13605 N  N     . GLY A 1 3165 ? 161.909 138.836 167.814 1.00 108.53 ? 3165 GLY A N     1 
ATOM   13606 C  CA    . GLY A 1 3165 ? 162.743 139.908 167.312 1.00 109.43 ? 3165 GLY A CA    1 
ATOM   13607 C  C     . GLY A 1 3165 ? 163.039 139.861 165.831 1.00 108.80 ? 3165 GLY A C     1 
ATOM   13608 O  O     . GLY A 1 3165 ? 163.899 140.617 165.365 1.00 106.45 ? 3165 GLY A O     1 
ATOM   13609 N  N     . GLY A 1 3166 ? 162.359 139.001 165.076 1.00 108.44 ? 3166 GLY A N     1 
ATOM   13610 C  CA    . GLY A 1 3166 ? 162.566 138.918 163.648 1.00 106.46 ? 3166 GLY A CA    1 
ATOM   13611 C  C     . GLY A 1 3166 ? 161.801 139.984 162.887 1.00 105.95 ? 3166 GLY A C     1 
ATOM   13612 O  O     . GLY A 1 3166 ? 161.163 140.871 163.452 1.00 104.75 ? 3166 GLY A O     1 
ATOM   13613 N  N     . ARG A 1 3167 ? 161.875 139.884 161.564 1.00 101.38 ? 3167 ARG A N     1 
ATOM   13614 C  CA    . ARG A 1 3167 ? 161.204 140.812 160.666 1.00 100.18 ? 3167 ARG A CA    1 
ATOM   13615 C  C     . ARG A 1 3167 ? 159.881 140.211 160.212 1.00 99.98  ? 3167 ARG A C     1 
ATOM   13616 O  O     . ARG A 1 3167 ? 159.842 139.070 159.741 1.00 101.77 ? 3167 ARG A O     1 
ATOM   13617 C  CB    . ARG A 1 3167 ? 162.085 141.132 159.458 1.00 101.76 ? 3167 ARG A CB    1 
ATOM   13618 C  CG    . ARG A 1 3167 ? 161.605 142.309 158.628 1.00 98.77  ? 3167 ARG A CG    1 
ATOM   13619 C  CD    . ARG A 1 3167 ? 162.758 142.942 157.866 1.00 100.02 ? 3167 ARG A CD    1 
ATOM   13620 N  NE    . ARG A 1 3167 ? 163.662 143.666 158.753 1.00 106.24 ? 3167 ARG A NE    1 
ATOM   13621 C  CZ    . ARG A 1 3167 ? 164.824 143.197 159.187 1.00 104.70 ? 3167 ARG A CZ    1 
ATOM   13622 N  NH1   . ARG A 1 3167 ? 165.258 141.997 158.840 1.00 101.24 ? 3167 ARG A NH1   1 
ATOM   13623 N  NH2   . ARG A 1 3167 ? 165.566 143.950 159.993 1.00 102.19 ? 3167 ARG A NH2   1 
ATOM   13624 N  N     . THR A 1 3168 ? 158.803 140.980 160.355 1.00 95.82  ? 3168 THR A N     1 
ATOM   13625 C  CA    . THR A 1 3168 ? 157.463 140.517 160.033 1.00 96.03  ? 3168 THR A CA    1 
ATOM   13626 C  C     . THR A 1 3168 ? 156.811 141.462 159.036 1.00 97.86  ? 3168 THR A C     1 
ATOM   13627 O  O     . THR A 1 3168 ? 157.103 142.660 159.006 1.00 99.20  ? 3168 THR A O     1 
ATOM   13628 C  CB    . THR A 1 3168 ? 156.577 140.416 161.284 1.00 99.12  ? 3168 THR A CB    1 
ATOM   13629 O  OG1   . THR A 1 3168 ? 155.932 141.675 161.514 1.00 98.55  ? 3168 THR A OG1   1 
ATOM   13630 C  CG2   . THR A 1 3168 ? 157.404 140.047 162.504 1.00 100.71 ? 3168 THR A CG2   1 
ATOM   13631 N  N     . MET A 1 3169 ? 155.919 140.906 158.221 1.00 93.53  ? 3169 MET A N     1 
ATOM   13632 C  CA    . MET A 1 3169 ? 155.136 141.668 157.261 1.00 91.27  ? 3169 MET A CA    1 
ATOM   13633 C  C     . MET A 1 3169 ? 153.671 141.648 157.674 1.00 90.29  ? 3169 MET A C     1 
ATOM   13634 O  O     . MET A 1 3169 ? 153.148 140.609 158.089 1.00 94.34  ? 3169 MET A O     1 
ATOM   13635 C  CB    . MET A 1 3169 ? 155.293 141.105 155.847 1.00 84.88  ? 3169 MET A CB    1 
ATOM   13636 C  CG    . MET A 1 3169 ? 156.676 141.310 155.253 1.00 90.36  ? 3169 MET A CG    1 
ATOM   13637 S  SD    . MET A 1 3169 ? 157.066 143.053 155.006 1.00 106.37 ? 3169 MET A SD    1 
ATOM   13638 C  CE    . MET A 1 3169 ? 158.855 143.000 154.978 1.00 92.65  ? 3169 MET A CE    1 
ATOM   13639 N  N     . ALA A 1 3170 ? 153.018 142.801 157.563 1.00 82.66  ? 3170 ALA A N     1 
ATOM   13640 C  CA    . ALA A 1 3170 ? 151.640 142.932 158.013 1.00 84.89  ? 3170 ALA A CA    1 
ATOM   13641 C  C     . ALA A 1 3170 ? 150.716 142.022 157.215 1.00 88.50  ? 3170 ALA A C     1 
ATOM   13642 O  O     . ALA A 1 3170 ? 150.861 141.873 155.999 1.00 90.00  ? 3170 ALA A O     1 
ATOM   13643 C  CB    . ALA A 1 3170 ? 151.177 144.383 157.891 1.00 82.41  ? 3170 ALA A CB    1 
ATOM   13644 N  N     . ILE A 1 3171 ? 149.762 141.410 157.910 1.00 76.89  ? 3171 ILE A N     1 
ATOM   13645 C  CA    . ILE A 1 3171 ? 148.767 140.540 157.295 1.00 71.03  ? 3171 ILE A CA    1 
ATOM   13646 C  C     . ILE A 1 3171 ? 147.495 141.348 157.094 1.00 74.33  ? 3171 ILE A C     1 
ATOM   13647 O  O     . ILE A 1 3171 ? 146.991 141.977 158.033 1.00 75.28  ? 3171 ILE A O     1 
ATOM   13648 C  CB    . ILE A 1 3171 ? 148.504 139.290 158.146 1.00 64.07  ? 3171 ILE A CB    1 
ATOM   13649 C  CG1   . ILE A 1 3171 ? 149.488 138.189 157.771 1.00 67.77  ? 3171 ILE A CG1   1 
ATOM   13650 C  CG2   . ILE A 1 3171 ? 147.081 138.792 157.952 1.00 68.31  ? 3171 ILE A CG2   1 
ATOM   13651 C  CD1   . ILE A 1 3171 ? 149.624 137.148 158.826 1.00 75.91  ? 3171 ILE A CD1   1 
ATOM   13652 N  N     . THR A 1 3172 ? 146.984 141.337 155.871 1.00 63.27  ? 3172 THR A N     1 
ATOM   13653 C  CA    . THR A 1 3172 ? 145.841 142.154 155.494 1.00 64.60  ? 3172 THR A CA    1 
ATOM   13654 C  C     . THR A 1 3172 ? 144.724 141.270 154.955 1.00 67.29  ? 3172 THR A C     1 
ATOM   13655 O  O     . THR A 1 3172 ? 144.980 140.132 154.545 1.00 73.99  ? 3172 THR A O     1 
ATOM   13656 C  CB    . THR A 1 3172 ? 146.263 143.192 154.455 1.00 66.68  ? 3172 THR A CB    1 
ATOM   13657 O  OG1   . THR A 1 3172 ? 146.720 142.528 153.272 1.00 73.53  ? 3172 THR A OG1   1 
ATOM   13658 C  CG2   . THR A 1 3172 ? 147.382 144.062 155.006 1.00 69.46  ? 3172 THR A CG2   1 
ATOM   13659 N  N     . PRO A 1 3173 ? 143.476 141.746 154.949 1.00 49.56  ? 3173 PRO A N     1 
ATOM   13660 C  CA    . PRO A 1 3173 ? 142.386 140.934 154.385 1.00 46.42  ? 3173 PRO A CA    1 
ATOM   13661 C  C     . PRO A 1 3173 ? 142.594 140.564 152.928 1.00 56.37  ? 3173 PRO A C     1 
ATOM   13662 O  O     . PRO A 1 3173 ? 141.977 139.600 152.456 1.00 69.87  ? 3173 PRO A O     1 
ATOM   13663 C  CB    . PRO A 1 3173 ? 141.158 141.833 154.564 1.00 51.02  ? 3173 PRO A CB    1 
ATOM   13664 C  CG    . PRO A 1 3173 ? 141.492 142.677 155.740 1.00 52.90  ? 3173 PRO A CG    1 
ATOM   13665 C  CD    . PRO A 1 3173 ? 142.966 142.940 155.644 1.00 52.10  ? 3173 PRO A CD    1 
ATOM   13666 N  N     . ARG A 1 3174 ? 143.431 141.302 152.196 1.00 56.27  ? 3174 ARG A N     1 
ATOM   13667 C  CA    . ARG A 1 3174 ? 143.771 140.893 150.839 1.00 56.48  ? 3174 ARG A CA    1 
ATOM   13668 C  C     . ARG A 1 3174 ? 144.455 139.533 150.828 1.00 68.68  ? 3174 ARG A C     1 
ATOM   13669 O  O     . ARG A 1 3174 ? 144.294 138.767 149.872 1.00 75.17  ? 3174 ARG A O     1 
ATOM   13670 C  CB    . ARG A 1 3174 ? 144.657 141.946 150.178 1.00 60.33  ? 3174 ARG A CB    1 
ATOM   13671 C  CG    . ARG A 1 3174 ? 144.062 143.342 150.199 1.00 67.83  ? 3174 ARG A CG    1 
ATOM   13672 C  CD    . ARG A 1 3174 ? 144.527 144.161 149.010 1.00 67.10  ? 3174 ARG A CD    1 
ATOM   13673 N  NE    . ARG A 1 3174 ? 144.335 143.450 147.753 1.00 68.33  ? 3174 ARG A NE    1 
ATOM   13674 C  CZ    . ARG A 1 3174 ? 144.859 143.826 146.595 1.00 66.19  ? 3174 ARG A CZ    1 
ATOM   13675 N  NH1   . ARG A 1 3174 ? 145.615 144.907 146.497 1.00 68.50  ? 3174 ARG A NH1   1 
ATOM   13676 N  NH2   . ARG A 1 3174 ? 144.616 143.101 145.507 1.00 63.18  ? 3174 ARG A NH2   1 
ATOM   13677 N  N     . HIS A 1 3175 ? 145.208 139.208 151.883 1.00 64.11  ? 3175 HIS A N     1 
ATOM   13678 C  CA    . HIS A 1 3175 ? 145.763 137.864 152.001 1.00 56.74  ? 3175 HIS A CA    1 
ATOM   13679 C  C     . HIS A 1 3175 ? 144.657 136.820 152.083 1.00 55.89  ? 3175 HIS A C     1 
ATOM   13680 O  O     . HIS A 1 3175 ? 144.740 135.767 151.443 1.00 60.77  ? 3175 HIS A O     1 
ATOM   13681 C  CB    . HIS A 1 3175 ? 146.675 137.771 153.223 1.00 55.57  ? 3175 HIS A CB    1 
ATOM   13682 C  CG    . HIS A 1 3175 ? 147.944 138.554 153.097 1.00 64.92  ? 3175 HIS A CG    1 
ATOM   13683 N  ND1   . HIS A 1 3175 ? 147.972 139.932 153.097 1.00 68.80  ? 3175 HIS A ND1   1 
ATOM   13684 C  CD2   . HIS A 1 3175 ? 149.230 138.152 152.970 1.00 65.78  ? 3175 HIS A CD2   1 
ATOM   13685 C  CE1   . HIS A 1 3175 ? 149.221 140.344 152.974 1.00 67.05  ? 3175 HIS A CE1   1 
ATOM   13686 N  NE2   . HIS A 1 3175 ? 150.004 139.284 152.895 1.00 69.97  ? 3175 HIS A NE2   1 
ATOM   13687 N  N     . TYR A 1 3176 ? 143.610 137.097 152.863 1.00 48.56  ? 3176 TYR A N     1 
ATOM   13688 C  CA    . TYR A 1 3176 ? 142.489 136.166 152.955 1.00 43.54  ? 3176 TYR A CA    1 
ATOM   13689 C  C     . TYR A 1 3176 ? 141.767 136.036 151.621 1.00 51.61  ? 3176 TYR A C     1 
ATOM   13690 O  O     . TYR A 1 3176 ? 141.349 134.937 151.235 1.00 72.19  ? 3176 TYR A O     1 
ATOM   13691 C  CB    . TYR A 1 3176 ? 141.519 136.620 154.045 1.00 44.81  ? 3176 TYR A CB    1 
ATOM   13692 C  CG    . TYR A 1 3176 ? 140.416 135.628 154.326 1.00 45.87  ? 3176 TYR A CG    1 
ATOM   13693 C  CD1   . TYR A 1 3176 ? 140.692 134.396 154.899 1.00 53.50  ? 3176 TYR A CD1   1 
ATOM   13694 C  CD2   . TYR A 1 3176 ? 139.099 135.924 154.014 1.00 53.19  ? 3176 TYR A CD2   1 
ATOM   13695 C  CE1   . TYR A 1 3176 ? 139.686 133.488 155.156 1.00 56.53  ? 3176 TYR A CE1   1 
ATOM   13696 C  CE2   . TYR A 1 3176 ? 138.087 135.023 154.267 1.00 52.20  ? 3176 TYR A CE2   1 
ATOM   13697 C  CZ    . TYR A 1 3176 ? 138.385 133.807 154.838 1.00 55.42  ? 3176 TYR A CZ    1 
ATOM   13698 O  OH    . TYR A 1 3176 ? 137.377 132.907 155.091 1.00 65.66  ? 3176 TYR A OH    1 
ATOM   13699 N  N     . LEU A 1 3177 ? 141.595 137.151 150.910 1.00 59.83  ? 3177 LEU A N     1 
ATOM   13700 C  CA    . LEU A 1 3177 ? 140.946 137.105 149.604 1.00 57.43  ? 3177 LEU A CA    1 
ATOM   13701 C  C     . LEU A 1 3177 ? 141.761 136.275 148.619 1.00 66.52  ? 3177 LEU A C     1 
ATOM   13702 O  O     . LEU A 1 3177 ? 141.208 135.476 147.854 1.00 68.88  ? 3177 LEU A O     1 
ATOM   13703 C  CB    . LEU A 1 3177 ? 140.741 138.523 149.077 1.00 54.82  ? 3177 LEU A CB    1 
ATOM   13704 C  CG    . LEU A 1 3177 ? 139.753 139.365 149.881 1.00 56.05  ? 3177 LEU A CG    1 
ATOM   13705 C  CD1   . LEU A 1 3177 ? 139.784 140.801 149.406 1.00 62.90  ? 3177 LEU A CD1   1 
ATOM   13706 C  CD2   . LEU A 1 3177 ? 138.355 138.788 149.767 1.00 60.18  ? 3177 LEU A CD2   1 
ATOM   13707 N  N     . ASP A 1 3178 ? 143.085 136.451 148.630 1.00 72.45  ? 3178 ASP A N     1 
ATOM   13708 C  CA    . ASP A 1 3178 ? 143.950 135.633 147.788 1.00 64.96  ? 3178 ASP A CA    1 
ATOM   13709 C  C     . ASP A 1 3178 ? 143.861 134.165 148.176 1.00 68.56  ? 3178 ASP A C     1 
ATOM   13710 O  O     . ASP A 1 3178 ? 143.858 133.286 147.309 1.00 76.63  ? 3178 ASP A O     1 
ATOM   13711 C  CB    . ASP A 1 3178 ? 145.394 136.118 147.888 1.00 69.77  ? 3178 ASP A CB    1 
ATOM   13712 C  CG    . ASP A 1 3178 ? 145.634 137.390 147.112 1.00 84.16  ? 3178 ASP A CG    1 
ATOM   13713 O  OD1   . ASP A 1 3178 ? 144.670 137.915 146.516 1.00 83.02  ? 3178 ASP A OD1   1 
ATOM   13714 O  OD2   . ASP A 1 3178 ? 146.789 137.861 147.095 1.00 85.30  ? 3178 ASP A OD2   1 
ATOM   13715 N  N     . PHE A 1 3179 ? 143.799 133.883 149.478 1.00 51.76  ? 3179 PHE A N     1 
ATOM   13716 C  CA    . PHE A 1 3179 ? 143.673 132.506 149.938 1.00 47.80  ? 3179 PHE A CA    1 
ATOM   13717 C  C     . PHE A 1 3179 ? 142.394 131.871 149.410 1.00 55.26  ? 3179 PHE A C     1 
ATOM   13718 O  O     . PHE A 1 3179 ? 142.415 130.742 148.907 1.00 68.64  ? 3179 PHE A O     1 
ATOM   13719 C  CB    . PHE A 1 3179 ? 143.717 132.478 151.468 1.00 46.68  ? 3179 PHE A CB    1 
ATOM   13720 C  CG    . PHE A 1 3179 ? 143.314 131.164 152.078 1.00 45.39  ? 3179 PHE A CG    1 
ATOM   13721 C  CD1   . PHE A 1 3179 ? 143.742 129.962 151.542 1.00 58.35  ? 3179 PHE A CD1   1 
ATOM   13722 C  CD2   . PHE A 1 3179 ? 142.517 131.138 153.208 1.00 48.13  ? 3179 PHE A CD2   1 
ATOM   13723 C  CE1   . PHE A 1 3179 ? 143.370 128.764 152.112 1.00 57.82  ? 3179 PHE A CE1   1 
ATOM   13724 C  CE2   . PHE A 1 3179 ? 142.146 129.943 153.781 1.00 56.07  ? 3179 PHE A CE2   1 
ATOM   13725 C  CZ    . PHE A 1 3179 ? 142.572 128.755 153.233 1.00 60.41  ? 3179 PHE A CZ    1 
ATOM   13726 N  N     . ILE A 1 3180 ? 141.275 132.591 149.487 1.00 54.07  ? 3180 ILE A N     1 
ATOM   13727 C  CA    . ILE A 1 3180 ? 140.009 132.029 149.026 1.00 54.01  ? 3180 ILE A CA    1 
ATOM   13728 C  C     . ILE A 1 3180 ? 140.005 131.868 147.508 1.00 61.09  ? 3180 ILE A C     1 
ATOM   13729 O  O     . ILE A 1 3180 ? 139.498 130.869 146.977 1.00 65.41  ? 3180 ILE A O     1 
ATOM   13730 C  CB    . ILE A 1 3180 ? 138.832 132.890 149.513 1.00 46.04  ? 3180 ILE A CB    1 
ATOM   13731 C  CG1   . ILE A 1 3180 ? 138.838 132.975 151.037 1.00 47.97  ? 3180 ILE A CG1   1 
ATOM   13732 C  CG2   . ILE A 1 3180 ? 137.525 132.297 149.045 1.00 57.61  ? 3180 ILE A CG2   1 
ATOM   13733 C  CD1   . ILE A 1 3180 ? 138.718 131.631 151.716 1.00 51.22  ? 3180 ILE A CD1   1 
ATOM   13734 N  N     . ASN A 1 3181 ? 140.562 132.842 146.782 1.00 64.70  ? 3181 ASN A N     1 
ATOM   13735 C  CA    . ASN A 1 3181 ? 140.630 132.728 145.328 1.00 62.23  ? 3181 ASN A CA    1 
ATOM   13736 C  C     . ASN A 1 3181 ? 141.489 131.543 144.907 1.00 74.44  ? 3181 ASN A C     1 
ATOM   13737 O  O     . ASN A 1 3181 ? 141.129 130.798 143.986 1.00 80.61  ? 3181 ASN A O     1 
ATOM   13738 C  CB    . ASN A 1 3181 ? 141.174 134.021 144.724 1.00 67.77  ? 3181 ASN A CB    1 
ATOM   13739 C  CG    . ASN A 1 3181 ? 140.154 135.139 144.723 1.00 78.28  ? 3181 ASN A CG    1 
ATOM   13740 O  OD1   . ASN A 1 3181 ? 139.481 135.379 143.722 1.00 78.84  ? 3181 ASN A OD1   1 
ATOM   13741 N  ND2   . ASN A 1 3181 ? 140.035 135.833 145.849 1.00 80.96  ? 3181 ASN A ND2   1 
ATOM   13742 N  N     . HIS A 1 3182 ? 142.633 131.355 145.569 1.00 69.78  ? 3182 HIS A N     1 
ATOM   13743 C  CA    . HIS A 1 3182 ? 143.484 130.209 145.274 1.00 63.21  ? 3182 HIS A CA    1 
ATOM   13744 C  C     . HIS A 1 3182 ? 142.779 128.908 145.618 1.00 66.82  ? 3182 HIS A C     1 
ATOM   13745 O  O     . HIS A 1 3182 ? 142.907 127.917 144.893 1.00 73.04  ? 3182 HIS A O     1 
ATOM   13746 C  CB    . HIS A 1 3182 ? 144.804 130.323 146.033 1.00 60.21  ? 3182 HIS A CB    1 
ATOM   13747 C  CG    . HIS A 1 3182 ? 145.770 131.287 145.422 1.00 64.00  ? 3182 HIS A CG    1 
ATOM   13748 N  ND1   . HIS A 1 3182 ? 146.469 132.212 146.166 1.00 73.15  ? 3182 HIS A ND1   1 
ATOM   13749 C  CD2   . HIS A 1 3182 ? 146.149 131.475 144.136 1.00 65.58  ? 3182 HIS A CD2   1 
ATOM   13750 C  CE1   . HIS A 1 3182 ? 147.240 132.926 145.365 1.00 70.94  ? 3182 HIS A CE1   1 
ATOM   13751 N  NE2   . HIS A 1 3182 ? 147.065 132.499 144.128 1.00 73.02  ? 3182 HIS A NE2   1 
ATOM   13752 N  N     . TYR A 1 3183 ? 142.029 128.890 146.721 1.00 63.54  ? 3183 TYR A N     1 
ATOM   13753 C  CA    . TYR A 1 3183 ? 141.256 127.705 147.074 1.00 58.58  ? 3183 TYR A CA    1 
ATOM   13754 C  C     . TYR A 1 3183 ? 140.274 127.353 145.966 1.00 65.71  ? 3183 TYR A C     1 
ATOM   13755 O  O     . TYR A 1 3183 ? 140.197 126.198 145.534 1.00 75.11  ? 3183 TYR A O     1 
ATOM   13756 C  CB    . TYR A 1 3183 ? 140.524 127.943 148.395 1.00 56.36  ? 3183 TYR A CB    1 
ATOM   13757 C  CG    . TYR A 1 3183 ? 139.927 126.705 149.021 1.00 63.36  ? 3183 TYR A CG    1 
ATOM   13758 C  CD1   . TYR A 1 3183 ? 140.309 125.436 148.611 1.00 67.19  ? 3183 TYR A CD1   1 
ATOM   13759 C  CD2   . TYR A 1 3183 ? 138.977 126.808 150.026 1.00 68.02  ? 3183 TYR A CD2   1 
ATOM   13760 C  CE1   . TYR A 1 3183 ? 139.761 124.306 149.184 1.00 68.07  ? 3183 TYR A CE1   1 
ATOM   13761 C  CE2   . TYR A 1 3183 ? 138.425 125.685 150.603 1.00 67.45  ? 3183 TYR A CE2   1 
ATOM   13762 C  CZ    . TYR A 1 3183 ? 138.820 124.437 150.180 1.00 68.23  ? 3183 TYR A CZ    1 
ATOM   13763 O  OH    . TYR A 1 3183 ? 138.272 123.315 150.755 1.00 72.43  ? 3183 TYR A OH    1 
ATOM   13764 N  N     . ALA A 1 3184 ? 139.533 128.348 145.475 1.00 72.12  ? 3184 ALA A N     1 
ATOM   13765 C  CA    . ALA A 1 3184 ? 138.554 128.092 144.423 1.00 69.87  ? 3184 ALA A CA    1 
ATOM   13766 C  C     . ALA A 1 3184 ? 139.228 127.595 143.150 1.00 72.88  ? 3184 ALA A C     1 
ATOM   13767 O  O     . ALA A 1 3184 ? 138.804 126.593 142.555 1.00 80.54  ? 3184 ALA A O     1 
ATOM   13768 C  CB    . ALA A 1 3184 ? 137.740 129.356 144.147 1.00 67.70  ? 3184 ALA A CB    1 
ATOM   13769 N  N     . ASN A 1 3185 ? 140.287 128.284 142.718 1.00 70.47  ? 3185 ASN A N     1 
ATOM   13770 C  CA    . ASN A 1 3185 ? 140.955 127.912 141.475 1.00 70.74  ? 3185 ASN A CA    1 
ATOM   13771 C  C     . ASN A 1 3185 ? 141.564 126.519 141.571 1.00 77.03  ? 3185 ASN A C     1 
ATOM   13772 O  O     . ASN A 1 3185 ? 141.422 125.703 140.652 1.00 84.45  ? 3185 ASN A O     1 
ATOM   13773 C  CB    . ASN A 1 3185 ? 142.023 128.947 141.126 1.00 73.22  ? 3185 ASN A CB    1 
ATOM   13774 C  CG    . ASN A 1 3185 ? 141.439 130.319 140.863 1.00 77.99  ? 3185 ASN A CG    1 
ATOM   13775 O  OD1   . ASN A 1 3185 ? 140.222 130.501 140.883 1.00 80.75  ? 3185 ASN A OD1   1 
ATOM   13776 N  ND2   . ASN A 1 3185 ? 142.305 131.294 140.616 1.00 77.59  ? 3185 ASN A ND2   1 
ATOM   13777 N  N     . LEU A 1 3186 ? 142.245 126.226 142.682 1.00 75.03  ? 3186 LEU A N     1 
ATOM   13778 C  CA    . LEU A 1 3186 ? 142.861 124.916 142.851 1.00 71.22  ? 3186 LEU A CA    1 
ATOM   13779 C  C     . LEU A 1 3186 ? 141.811 123.819 142.932 1.00 75.57  ? 3186 LEU A C     1 
ATOM   13780 O  O     . LEU A 1 3186 ? 141.993 122.741 142.357 1.00 88.75  ? 3186 LEU A O     1 
ATOM   13781 C  CB    . LEU A 1 3186 ? 143.748 124.908 144.095 1.00 71.08  ? 3186 LEU A CB    1 
ATOM   13782 C  CG    . LEU A 1 3186 ? 145.092 125.621 143.954 1.00 72.73  ? 3186 LEU A CG    1 
ATOM   13783 C  CD1   . LEU A 1 3186 ? 145.819 125.671 145.286 1.00 77.78  ? 3186 LEU A CD1   1 
ATOM   13784 C  CD2   . LEU A 1 3186 ? 145.946 124.940 142.902 1.00 73.70  ? 3186 LEU A CD2   1 
ATOM   13785 N  N     . PHE A 1 3187 ? 140.706 124.068 143.640 1.00 77.91  ? 3187 PHE A N     1 
ATOM   13786 C  CA    . PHE A 1 3187 ? 139.643 123.073 143.715 1.00 74.28  ? 3187 PHE A CA    1 
ATOM   13787 C  C     . PHE A 1 3187 ? 139.103 122.755 142.329 1.00 78.77  ? 3187 PHE A C     1 
ATOM   13788 O  O     . PHE A 1 3187 ? 138.999 121.583 141.945 1.00 87.31  ? 3187 PHE A O     1 
ATOM   13789 C  CB    . PHE A 1 3187 ? 138.524 123.572 144.628 1.00 76.89  ? 3187 PHE A CB    1 
ATOM   13790 C  CG    . PHE A 1 3187 ? 137.566 122.499 145.054 1.00 80.90  ? 3187 PHE A CG    1 
ATOM   13791 C  CD1   . PHE A 1 3187 ? 137.794 121.766 146.205 1.00 83.91  ? 3187 PHE A CD1   1 
ATOM   13792 C  CD2   . PHE A 1 3187 ? 136.436 122.224 144.304 1.00 82.77  ? 3187 PHE A CD2   1 
ATOM   13793 C  CE1   . PHE A 1 3187 ? 136.913 120.780 146.600 1.00 85.06  ? 3187 PHE A CE1   1 
ATOM   13794 C  CE2   . PHE A 1 3187 ? 135.553 121.238 144.693 1.00 81.93  ? 3187 PHE A CE2   1 
ATOM   13795 C  CZ    . PHE A 1 3187 ? 135.792 120.515 145.843 1.00 84.95  ? 3187 PHE A CZ    1 
ATOM   13796 N  N     . HIS A 1 3188 ? 138.778 123.792 141.552 1.00 87.70  ? 3188 HIS A N     1 
ATOM   13797 C  CA    . HIS A 1 3188 ? 138.229 123.561 140.220 1.00 91.32  ? 3188 HIS A CA    1 
ATOM   13798 C  C     . HIS A 1 3188 ? 139.230 122.836 139.327 1.00 92.60  ? 3188 HIS A C     1 
ATOM   13799 O  O     . HIS A 1 3188 ? 138.873 121.875 138.632 1.00 96.52  ? 3188 HIS A O     1 
ATOM   13800 C  CB    . HIS A 1 3188 ? 137.806 124.889 139.593 1.00 91.93  ? 3188 HIS A CB    1 
ATOM   13801 C  CG    . HIS A 1 3188 ? 137.519 124.801 138.127 1.00 96.87  ? 3188 HIS A CG    1 
ATOM   13802 N  ND1   . HIS A 1 3188 ? 136.596 123.923 137.601 1.00 97.21  ? 3188 HIS A ND1   1 
ATOM   13803 C  CD2   . HIS A 1 3188 ? 138.030 125.485 137.076 1.00 98.01  ? 3188 HIS A CD2   1 
ATOM   13804 C  CE1   . HIS A 1 3188 ? 136.552 124.067 136.289 1.00 98.49  ? 3188 HIS A CE1   1 
ATOM   13805 N  NE2   . HIS A 1 3188 ? 137.412 125.009 135.944 1.00 99.36  ? 3188 HIS A NE2   1 
ATOM   13806 N  N     . GLU A 1 3189 ? 140.495 123.265 139.352 1.00 90.49  ? 3189 GLU A N     1 
ATOM   13807 C  CA    . GLU A 1 3189 ? 141.507 122.662 138.491 1.00 90.48  ? 3189 GLU A CA    1 
ATOM   13808 C  C     . GLU A 1 3189 ? 141.743 121.200 138.848 1.00 95.46  ? 3189 GLU A C     1 
ATOM   13809 O  O     . GLU A 1 3189 ? 141.774 120.331 137.968 1.00 103.27 ? 3189 GLU A O     1 
ATOM   13810 C  CB    . GLU A 1 3189 ? 142.809 123.458 138.588 1.00 88.38  ? 3189 GLU A CB    1 
ATOM   13811 C  CG    . GLU A 1 3189 ? 143.953 122.890 137.771 1.00 95.41  ? 3189 GLU A CG    1 
ATOM   13812 C  CD    . GLU A 1 3189 ? 145.305 123.382 138.250 1.00 100.77 ? 3189 GLU A CD    1 
ATOM   13813 O  OE1   . GLU A 1 3189 ? 145.445 124.600 138.488 1.00 99.26  ? 3189 GLU A OE1   1 
ATOM   13814 O  OE2   . GLU A 1 3189 ? 146.226 122.551 138.388 1.00 102.42 ? 3189 GLU A OE2   1 
ATOM   13815 N  N     . LYS A 1 3190 ? 141.919 120.909 140.140 1.00 88.65  ? 3190 LYS A N     1 
ATOM   13816 C  CA    . LYS A 1 3190 ? 142.160 119.535 140.563 1.00 87.03  ? 3190 LYS A CA    1 
ATOM   13817 C  C     . LYS A 1 3190 ? 140.963 118.647 140.258 1.00 91.74  ? 3190 LYS A C     1 
ATOM   13818 O  O     . LYS A 1 3190 ? 141.129 117.509 139.804 1.00 99.42  ? 3190 LYS A O     1 
ATOM   13819 C  CB    . LYS A 1 3190 ? 142.494 119.491 142.053 1.00 87.39  ? 3190 LYS A CB    1 
ATOM   13820 C  CG    . LYS A 1 3190 ? 143.822 120.136 142.414 1.00 88.33  ? 3190 LYS A CG    1 
ATOM   13821 C  CD    . LYS A 1 3190 ? 144.965 119.531 141.621 1.00 89.84  ? 3190 LYS A CD    1 
ATOM   13822 C  CE    . LYS A 1 3190 ? 146.272 120.249 141.909 1.00 93.17  ? 3190 LYS A CE    1 
ATOM   13823 N  NZ    . LYS A 1 3190 ? 147.375 119.755 141.041 1.00 94.18  ? 3190 LYS A NZ    1 
ATOM   13824 N  N     . ARG A 1 3191 ? 139.746 119.146 140.499 1.00 99.32  ? 3191 ARG A N     1 
ATOM   13825 C  CA    . ARG A 1 3191 ? 138.562 118.344 140.218 1.00 101.65 ? 3191 ARG A CA    1 
ATOM   13826 C  C     . ARG A 1 3191 ? 138.454 118.033 138.731 1.00 101.17 ? 3191 ARG A C     1 
ATOM   13827 O  O     . ARG A 1 3191 ? 138.183 116.890 138.345 1.00 102.86 ? 3191 ARG A O     1 
ATOM   13828 C  CB    . ARG A 1 3191 ? 137.310 119.067 140.715 1.00 104.71 ? 3191 ARG A CB    1 
ATOM   13829 C  CG    . ARG A 1 3191 ? 136.247 118.140 141.277 1.00 104.88 ? 3191 ARG A CG    1 
ATOM   13830 C  CD    . ARG A 1 3191 ? 135.110 118.923 141.919 1.00 103.79 ? 3191 ARG A CD    1 
ATOM   13831 N  NE    . ARG A 1 3191 ? 134.080 118.056 142.482 1.00 110.35 ? 3191 ARG A NE    1 
ATOM   13832 C  CZ    . ARG A 1 3191 ? 134.251 117.255 143.526 1.00 110.56 ? 3191 ARG A CZ    1 
ATOM   13833 N  NH1   . ARG A 1 3191 ? 135.401 117.201 144.179 1.00 107.53 ? 3191 ARG A NH1   1 
ATOM   13834 N  NH2   . ARG A 1 3191 ? 133.239 116.493 143.931 1.00 107.87 ? 3191 ARG A NH2   1 
ATOM   13835 N  N     . SER A 1 3192 ? 138.683 119.036 137.877 1.00 104.82 ? 3192 SER A N     1 
ATOM   13836 C  CA    . SER A 1 3192 ? 138.614 118.801 136.438 1.00 106.52 ? 3192 SER A CA    1 
ATOM   13837 C  C     . SER A 1 3192 ? 139.678 117.808 135.985 1.00 110.19 ? 3192 SER A C     1 
ATOM   13838 O  O     . SER A 1 3192 ? 139.391 116.895 135.199 1.00 110.85 ? 3192 SER A O     1 
ATOM   13839 C  CB    . SER A 1 3192 ? 138.756 120.122 135.683 1.00 104.95 ? 3192 SER A CB    1 
ATOM   13840 O  OG    . SER A 1 3192 ? 137.826 121.080 136.157 1.00 107.15 ? 3192 SER A OG    1 
ATOM   13841 N  N     . GLU A 1 3193 ? 140.912 117.967 136.474 1.00 111.19 ? 3193 GLU A N     1 
ATOM   13842 C  CA    . GLU A 1 3193 ? 141.982 117.060 136.072 1.00 107.91 ? 3193 GLU A CA    1 
ATOM   13843 C  C     . GLU A 1 3193 ? 141.690 115.633 136.510 1.00 109.62 ? 3193 GLU A C     1 
ATOM   13844 O  O     . GLU A 1 3193 ? 141.878 114.686 135.736 1.00 114.29 ? 3193 GLU A O     1 
ATOM   13845 C  CB    . GLU A 1 3193 ? 143.317 117.529 136.649 1.00 105.08 ? 3193 GLU A CB    1 
ATOM   13846 C  CG    . GLU A 1 3193 ? 143.890 118.765 135.979 1.00 110.52 ? 3193 GLU A CG    1 
ATOM   13847 C  CD    . GLU A 1 3193 ? 145.165 119.244 136.644 1.00 112.79 ? 3193 GLU A CD    1 
ATOM   13848 O  OE1   . GLU A 1 3193 ? 145.610 118.594 137.613 1.00 110.74 ? 3193 GLU A OE1   1 
ATOM   13849 O  OE2   . GLU A 1 3193 ? 145.720 120.271 136.200 1.00 112.56 ? 3193 GLU A OE2   1 
ATOM   13850 N  N     . LEU A 1 3194 ? 141.221 115.457 137.748 1.00 105.11 ? 3194 LEU A N     1 
ATOM   13851 C  CA    . LEU A 1 3194 ? 140.943 114.115 138.243 1.00 104.90 ? 3194 LEU A CA    1 
ATOM   13852 C  C     . LEU A 1 3194 ? 139.772 113.486 137.500 1.00 109.96 ? 3194 LEU A C     1 
ATOM   13853 O  O     . LEU A 1 3194 ? 139.802 112.290 137.190 1.00 112.09 ? 3194 LEU A O     1 
ATOM   13854 C  CB    . LEU A 1 3194 ? 140.682 114.160 139.748 1.00 103.75 ? 3194 LEU A CB    1 
ATOM   13855 C  CG    . LEU A 1 3194 ? 140.156 112.891 140.417 1.00 107.66 ? 3194 LEU A CG    1 
ATOM   13856 C  CD1   . LEU A 1 3194 ? 141.074 111.715 140.135 1.00 113.84 ? 3194 LEU A CD1   1 
ATOM   13857 C  CD2   . LEU A 1 3194 ? 140.032 113.115 141.908 1.00 108.54 ? 3194 LEU A CD2   1 
ATOM   13858 N  N     . GLU A 1 3195 ? 138.735 114.273 137.193 1.00 119.83 ? 3195 GLU A N     1 
ATOM   13859 C  CA    . GLU A 1 3195 ? 137.615 113.742 136.423 1.00 117.89 ? 3195 GLU A CA    1 
ATOM   13860 C  C     . GLU A 1 3195 ? 138.055 113.306 135.032 1.00 117.82 ? 3195 GLU A C     1 
ATOM   13861 O  O     . GLU A 1 3195 ? 137.664 112.232 134.559 1.00 120.19 ? 3195 GLU A O     1 
ATOM   13862 C  CB    . GLU A 1 3195 ? 136.497 114.781 136.326 1.00 120.82 ? 3195 GLU A CB    1 
ATOM   13863 C  CG    . GLU A 1 3195 ? 135.749 115.023 137.626 1.00 124.13 ? 3195 GLU A CG    1 
ATOM   13864 C  CD    . GLU A 1 3195 ? 134.403 114.327 137.659 1.00 123.76 ? 3195 GLU A CD    1 
ATOM   13865 O  OE1   . GLU A 1 3195 ? 133.871 114.009 136.574 1.00 122.58 ? 3195 GLU A OE1   1 
ATOM   13866 O  OE2   . GLU A 1 3195 ? 133.876 114.100 138.768 1.00 124.31 ? 3195 GLU A OE2   1 
ATOM   13867 N  N     . GLU A 1 3196 ? 138.869 114.125 134.359 1.00 115.53 ? 3196 GLU A N     1 
ATOM   13868 C  CA    . GLU A 1 3196 ? 139.343 113.751 133.029 1.00 116.00 ? 3196 GLU A CA    1 
ATOM   13869 C  C     . GLU A 1 3196 ? 140.208 112.498 133.082 1.00 116.20 ? 3196 GLU A C     1 
ATOM   13870 O  O     . GLU A 1 3196 ? 140.076 111.603 132.234 1.00 118.32 ? 3196 GLU A O     1 
ATOM   13871 C  CB    . GLU A 1 3196 ? 140.117 114.909 132.401 1.00 115.47 ? 3196 GLU A CB    1 
ATOM   13872 C  CG    . GLU A 1 3196 ? 140.448 114.700 130.934 1.00 116.15 ? 3196 GLU A CG    1 
ATOM   13873 C  CD    . GLU A 1 3196 ? 141.684 115.460 130.501 1.00 117.69 ? 3196 GLU A CD    1 
ATOM   13874 O  OE1   . GLU A 1 3196 ? 141.866 115.655 129.282 1.00 118.48 ? 3196 GLU A OE1   1 
ATOM   13875 O  OE2   . GLU A 1 3196 ? 142.472 115.865 131.381 1.00 119.23 ? 3196 GLU A OE2   1 
ATOM   13876 N  N     . GLN A 1 3197 ? 141.103 112.416 134.072 1.00 116.17 ? 3197 GLN A N     1 
ATOM   13877 C  CA    . GLN A 1 3197 ? 141.950 111.237 134.203 1.00 116.25 ? 3197 GLN A CA    1 
ATOM   13878 C  C     . GLN A 1 3197 ? 141.114 109.991 134.457 1.00 117.52 ? 3197 GLN A C     1 
ATOM   13879 O  O     . GLN A 1 3197 ? 141.356 108.940 133.853 1.00 121.98 ? 3197 GLN A O     1 
ATOM   13880 C  CB    . GLN A 1 3197 ? 142.971 111.449 135.323 1.00 116.64 ? 3197 GLN A CB    1 
ATOM   13881 C  CG    . GLN A 1 3197 ? 143.768 110.208 135.703 1.00 119.03 ? 3197 GLN A CG    1 
ATOM   13882 C  CD    . GLN A 1 3197 ? 144.278 110.257 137.133 1.00 120.65 ? 3197 GLN A CD    1 
ATOM   13883 O  OE1   . GLN A 1 3197 ? 143.935 109.410 137.958 1.00 118.47 ? 3197 GLN A OE1   1 
ATOM   13884 N  NE2   . GLN A 1 3197 ? 145.106 111.252 137.432 1.00 120.34 ? 3197 GLN A NE2   1 
ATOM   13885 N  N     . GLN A 1 3198 ? 140.108 110.095 135.328 1.00 120.77 ? 3198 GLN A N     1 
ATOM   13886 C  CA    . GLN A 1 3198 ? 139.260 108.946 135.623 1.00 122.14 ? 3198 GLN A CA    1 
ATOM   13887 C  C     . GLN A 1 3198 ? 138.444 108.529 134.405 1.00 123.79 ? 3198 GLN A C     1 
ATOM   13888 O  O     . GLN A 1 3198 ? 138.240 107.333 134.172 1.00 123.77 ? 3198 GLN A O     1 
ATOM   13889 C  CB    . GLN A 1 3198 ? 138.348 109.259 136.808 1.00 121.74 ? 3198 GLN A CB    1 
ATOM   13890 C  CG    . GLN A 1 3198 ? 137.273 108.217 137.067 1.00 121.82 ? 3198 GLN A CG    1 
ATOM   13891 C  CD    . GLN A 1 3198 ? 137.840 106.886 137.530 1.00 123.42 ? 3198 GLN A CD    1 
ATOM   13892 O  OE1   . GLN A 1 3198 ? 139.007 106.790 137.909 1.00 124.32 ? 3198 GLN A OE1   1 
ATOM   13893 N  NE2   . GLN A 1 3198 ? 137.011 105.851 137.500 1.00 124.72 ? 3198 GLN A NE2   1 
ATOM   13894 N  N     . MET A 1 3199 ? 137.962 109.495 133.618 1.00 123.38 ? 3199 MET A N     1 
ATOM   13895 C  CA    . MET A 1 3199 ? 137.212 109.151 132.412 1.00 120.13 ? 3199 MET A CA    1 
ATOM   13896 C  C     . MET A 1 3199 ? 138.093 108.435 131.396 1.00 120.84 ? 3199 MET A C     1 
ATOM   13897 O  O     . MET A 1 3199 ? 137.702 107.394 130.847 1.00 122.81 ? 3199 MET A O     1 
ATOM   13898 C  CB    . MET A 1 3199 ? 136.607 110.407 131.792 1.00 120.86 ? 3199 MET A CB    1 
ATOM   13899 C  CG    . MET A 1 3199 ? 135.781 110.137 130.548 1.00 121.86 ? 3199 MET A CG    1 
ATOM   13900 S  SD    . MET A 1 3199 ? 136.646 110.603 129.036 1.00 129.17 ? 3199 MET A SD    1 
ATOM   13901 C  CE    . MET A 1 3199 ? 136.578 112.388 129.142 1.00 121.94 ? 3199 MET A CE    1 
ATOM   13902 N  N     . HIS A 1 3200 ? 139.288 108.975 131.135 1.00 120.10 ? 3200 HIS A N     1 
ATOM   13903 C  CA    . HIS A 1 3200 ? 140.223 108.292 130.246 1.00 121.60 ? 3200 HIS A CA    1 
ATOM   13904 C  C     . HIS A 1 3200 ? 140.536 106.892 130.758 1.00 123.33 ? 3200 HIS A C     1 
ATOM   13905 O  O     . HIS A 1 3200 ? 140.617 105.934 129.978 1.00 123.83 ? 3200 HIS A O     1 
ATOM   13906 C  CB    . HIS A 1 3200 ? 141.515 109.101 130.115 1.00 118.92 ? 3200 HIS A CB    1 
ATOM   13907 C  CG    . HIS A 1 3200 ? 141.383 110.351 129.302 1.00 119.60 ? 3200 HIS A CG    1 
ATOM   13908 N  ND1   . HIS A 1 3200 ? 140.327 110.582 128.447 1.00 123.10 ? 3200 HIS A ND1   1 
ATOM   13909 C  CD2   . HIS A 1 3200 ? 142.184 111.439 129.212 1.00 121.13 ? 3200 HIS A CD2   1 
ATOM   13910 C  CE1   . HIS A 1 3200 ? 140.483 111.759 127.866 1.00 122.31 ? 3200 HIS A CE1   1 
ATOM   13911 N  NE2   . HIS A 1 3200 ? 141.601 112.300 128.314 1.00 122.56 ? 3200 HIS A NE2   1 
ATOM   13912 N  N     . LEU A 1 3201 ? 140.711 106.761 132.074 1.00 127.91 ? 3201 LEU A N     1 
ATOM   13913 C  CA    . LEU A 1 3201 ? 141.099 105.491 132.675 1.00 125.29 ? 3201 LEU A CA    1 
ATOM   13914 C  C     . LEU A 1 3201 ? 139.983 104.457 132.547 1.00 126.19 ? 3201 LEU A C     1 
ATOM   13915 O  O     . LEU A 1 3201 ? 140.239 103.284 132.249 1.00 128.86 ? 3201 LEU A O     1 
ATOM   13916 C  CB    . LEU A 1 3201 ? 141.458 105.741 134.138 1.00 126.29 ? 3201 LEU A CB    1 
ATOM   13917 C  CG    . LEU A 1 3201 ? 142.927 105.791 134.550 1.00 126.72 ? 3201 LEU A CG    1 
ATOM   13918 C  CD1   . LEU A 1 3201 ? 143.016 105.849 136.065 1.00 125.50 ? 3201 LEU A CD1   1 
ATOM   13919 C  CD2   . LEU A 1 3201 ? 143.682 104.622 133.993 1.00 128.44 ? 3201 LEU A CD2   1 
ATOM   13920 N  N     . ASN A 1 3202 ? 138.733 104.881 132.763 1.00 129.14 ? 3202 ASN A N     1 
ATOM   13921 C  CA    . ASN A 1 3202 ? 137.592 103.994 132.552 1.00 131.07 ? 3202 ASN A CA    1 
ATOM   13922 C  C     . ASN A 1 3202 ? 137.477 103.572 131.092 1.00 130.52 ? 3202 ASN A C     1 
ATOM   13923 O  O     . ASN A 1 3202 ? 137.173 102.410 130.799 1.00 129.84 ? 3202 ASN A O     1 
ATOM   13924 C  CB    . ASN A 1 3202 ? 136.298 104.671 133.010 1.00 131.60 ? 3202 ASN A CB    1 
ATOM   13925 C  CG    . ASN A 1 3202 ? 135.903 104.286 134.423 1.00 131.65 ? 3202 ASN A CG    1 
ATOM   13926 O  OD1   . ASN A 1 3202 ? 136.451 103.348 135.000 1.00 132.39 ? 3202 ASN A OD1   1 
ATOM   13927 N  ND2   . ASN A 1 3202 ? 134.920 104.990 134.975 1.00 131.03 ? 3202 ASN A ND2   1 
ATOM   13928 N  N     . VAL A 1 3203 ? 137.704 104.500 130.158 1.00 133.65 ? 3203 VAL A N     1 
ATOM   13929 C  CA    . VAL A 1 3203 ? 137.647 104.133 128.743 1.00 134.11 ? 3203 VAL A CA    1 
ATOM   13930 C  C     . VAL A 1 3203 ? 138.702 103.077 128.427 1.00 136.77 ? 3203 VAL A C     1 
ATOM   13931 O  O     . VAL A 1 3203 ? 138.428 102.077 127.748 1.00 137.97 ? 3203 VAL A O     1 
ATOM   13932 C  CB    . VAL A 1 3203 ? 137.807 105.378 127.854 1.00 132.13 ? 3203 VAL A CB    1 
ATOM   13933 C  CG1   . VAL A 1 3203 ? 137.963 104.965 126.407 1.00 132.82 ? 3203 VAL A CG1   1 
ATOM   13934 C  CG2   . VAL A 1 3203 ? 136.607 106.294 128.008 1.00 132.28 ? 3203 VAL A CG2   1 
ATOM   13935 N  N     . GLY A 1 3204 ? 139.923 103.280 128.926 1.00 138.80 ? 3204 GLY A N     1 
ATOM   13936 C  CA    . GLY A 1 3204 ? 140.977 102.305 128.690 1.00 136.33 ? 3204 GLY A CA    1 
ATOM   13937 C  C     . GLY A 1 3204 ? 140.666 100.946 129.289 1.00 137.02 ? 3204 GLY A C     1 
ATOM   13938 O  O     . GLY A 1 3204 ? 140.881 99.909  128.651 1.00 139.58 ? 3204 GLY A O     1 
ATOM   13939 N  N     . LEU A 1 3205 ? 140.152 100.931 130.521 1.00 136.83 ? 3205 LEU A N     1 
ATOM   13940 C  CA    . LEU A 1 3205 ? 139.804 99.665  131.159 1.00 137.43 ? 3205 LEU A CA    1 
ATOM   13941 C  C     . LEU A 1 3205 ? 138.697 98.949  130.397 1.00 139.41 ? 3205 LEU A C     1 
ATOM   13942 O  O     . LEU A 1 3205 ? 138.741 97.723  130.231 1.00 139.49 ? 3205 LEU A O     1 
ATOM   13943 C  CB    . LEU A 1 3205 ? 139.390 99.904  132.610 1.00 138.53 ? 3205 LEU A CB    1 
ATOM   13944 C  CG    . LEU A 1 3205 ? 139.971 98.928  133.632 1.00 139.50 ? 3205 LEU A CG    1 
ATOM   13945 C  CD1   . LEU A 1 3205 ? 141.480 99.083  133.709 1.00 139.09 ? 3205 LEU A CD1   1 
ATOM   13946 C  CD2   . LEU A 1 3205 ? 139.337 99.133  134.997 1.00 138.14 ? 3205 LEU A CD2   1 
ATOM   13947 N  N     . ARG A 1 3206 ? 137.691 99.695  129.930 1.00 150.53 ? 3206 ARG A N     1 
ATOM   13948 C  CA    . ARG A 1 3206 ? 136.617 99.082  129.156 1.00 150.67 ? 3206 ARG A CA    1 
ATOM   13949 C  C     . ARG A 1 3206 ? 137.149 98.481  127.863 1.00 148.97 ? 3206 ARG A C     1 
ATOM   13950 O  O     . ARG A 1 3206 ? 136.772 97.364  127.487 1.00 148.70 ? 3206 ARG A O     1 
ATOM   13951 C  CB    . ARG A 1 3206 ? 135.523 100.110 128.862 1.00 149.63 ? 3206 ARG A CB    1 
ATOM   13952 C  CG    . ARG A 1 3206 ? 134.680 99.783  127.638 1.00 148.63 ? 3206 ARG A CG    1 
ATOM   13953 C  CD    . ARG A 1 3206 ? 133.409 100.615 127.592 1.00 150.18 ? 3206 ARG A CD    1 
ATOM   13954 N  NE    . ARG A 1 3206 ? 133.676 102.005 127.242 1.00 151.30 ? 3206 ARG A NE    1 
ATOM   13955 C  CZ    . ARG A 1 3206 ? 133.482 103.033 128.056 1.00 149.69 ? 3206 ARG A CZ    1 
ATOM   13956 N  NH1   . ARG A 1 3206 ? 133.016 102.866 129.283 1.00 148.82 ? 3206 ARG A NH1   1 
ATOM   13957 N  NH2   . ARG A 1 3206 ? 133.763 104.261 127.629 1.00 148.80 ? 3206 ARG A NH2   1 
ATOM   13958 N  N     . LYS A 1 3207 ? 138.037 99.203  127.173 1.00 150.07 ? 3207 LYS A N     1 
ATOM   13959 C  CA    . LYS A 1 3207 ? 138.621 98.668  125.946 1.00 150.61 ? 3207 LYS A CA    1 
ATOM   13960 C  C     . LYS A 1 3207 ? 139.406 97.390  126.221 1.00 151.85 ? 3207 LYS A C     1 
ATOM   13961 O  O     . LYS A 1 3207 ? 139.299 96.412  125.470 1.00 153.16 ? 3207 LYS A O     1 
ATOM   13962 C  CB    . LYS A 1 3207 ? 139.518 99.715  125.287 1.00 152.32 ? 3207 LYS A CB    1 
ATOM   13963 C  CG    . LYS A 1 3207 ? 138.765 100.790 124.522 1.00 153.12 ? 3207 LYS A CG    1 
ATOM   13964 C  CD    . LYS A 1 3207 ? 137.824 100.180 123.497 1.00 152.70 ? 3207 LYS A CD    1 
ATOM   13965 C  CE    . LYS A 1 3207 ? 136.902 101.232 122.906 1.00 152.76 ? 3207 LYS A CE    1 
ATOM   13966 N  NZ    . LYS A 1 3207 ? 137.665 102.352 122.291 1.00 151.60 ? 3207 LYS A NZ    1 
ATOM   13967 N  N     . ILE A 1 3208 ? 140.191 97.375  127.300 1.00 156.20 ? 3208 ILE A N     1 
ATOM   13968 C  CA    . ILE A 1 3208 ? 140.997 96.196  127.607 1.00 156.10 ? 3208 ILE A CA    1 
ATOM   13969 C  C     . ILE A 1 3208 ? 140.108 95.004  127.948 1.00 157.61 ? 3208 ILE A C     1 
ATOM   13970 O  O     . ILE A 1 3208 ? 140.359 93.878  127.501 1.00 159.41 ? 3208 ILE A O     1 
ATOM   13971 C  CB    . ILE A 1 3208 ? 141.994 96.511  128.736 1.00 156.18 ? 3208 ILE A CB    1 
ATOM   13972 C  CG1   . ILE A 1 3208 ? 143.105 97.426  128.216 1.00 155.71 ? 3208 ILE A CG1   1 
ATOM   13973 C  CG2   . ILE A 1 3208 ? 142.586 95.231  129.301 1.00 154.90 ? 3208 ILE A CG2   1 
ATOM   13974 C  CD1   . ILE A 1 3208 ? 144.240 97.633  129.194 1.00 155.88 ? 3208 ILE A CD1   1 
ATOM   13975 N  N     . LYS A 1 3209 ? 139.055 95.226  128.742 1.00 162.36 ? 3209 LYS A N     1 
ATOM   13976 C  CA    . LYS A 1 3209 ? 138.155 94.129  129.092 1.00 161.95 ? 3209 LYS A CA    1 
ATOM   13977 C  C     . LYS A 1 3209 ? 137.418 93.601  127.865 1.00 162.88 ? 3209 LYS A C     1 
ATOM   13978 O  O     . LYS A 1 3209 ? 137.225 92.385  127.720 1.00 162.73 ? 3209 LYS A O     1 
ATOM   13979 C  CB    . LYS A 1 3209 ? 137.165 94.585  130.164 1.00 161.43 ? 3209 LYS A CB    1 
ATOM   13980 C  CG    . LYS A 1 3209 ? 136.116 93.545  130.532 1.00 162.23 ? 3209 LYS A CG    1 
ATOM   13981 C  CD    . LYS A 1 3209 ? 136.755 92.258  131.038 1.00 162.03 ? 3209 LYS A CD    1 
ATOM   13982 C  CE    . LYS A 1 3209 ? 137.623 92.505  132.264 1.00 161.40 ? 3209 LYS A CE    1 
ATOM   13983 N  NZ    . LYS A 1 3209 ? 136.807 92.725  133.490 1.00 161.64 ? 3209 LYS A NZ    1 
ATOM   13984 N  N     . GLU A 1 3210 ? 136.997 94.500  126.971 1.00 168.77 ? 3210 GLU A N     1 
ATOM   13985 C  CA    . GLU A 1 3210 ? 136.353 94.062  125.738 1.00 168.43 ? 3210 GLU A CA    1 
ATOM   13986 C  C     . GLU A 1 3210 ? 137.309 93.237  124.884 1.00 169.08 ? 3210 GLU A C     1 
ATOM   13987 O  O     . GLU A 1 3210 ? 136.910 92.230  124.289 1.00 168.85 ? 3210 GLU A O     1 
ATOM   13988 C  CB    . GLU A 1 3210 ? 135.823 95.274  124.967 1.00 167.95 ? 3210 GLU A CB    1 
ATOM   13989 C  CG    . GLU A 1 3210 ? 135.631 95.054  123.473 1.00 168.83 ? 3210 GLU A CG    1 
ATOM   13990 C  CD    . GLU A 1 3210 ? 136.895 95.314  122.677 1.00 170.07 ? 3210 GLU A CD    1 
ATOM   13991 O  OE1   . GLU A 1 3210 ? 137.486 96.402  122.835 1.00 170.36 ? 3210 GLU A OE1   1 
ATOM   13992 O  OE2   . GLU A 1 3210 ? 137.311 94.414  121.920 1.00 170.89 ? 3210 GLU A OE2   1 
ATOM   13993 N  N     . THR A 1 3211 ? 138.577 93.650  124.810 1.00 170.88 ? 3211 THR A N     1 
ATOM   13994 C  CA    . THR A 1 3211 ? 139.565 92.865  124.074 1.00 170.97 ? 3211 THR A CA    1 
ATOM   13995 C  C     . THR A 1 3211 ? 139.765 91.493  124.712 1.00 172.02 ? 3211 THR A C     1 
ATOM   13996 O  O     . THR A 1 3211 ? 139.939 90.491  124.008 1.00 172.34 ? 3211 THR A O     1 
ATOM   13997 C  CB    . THR A 1 3211 ? 140.889 93.626  124.001 1.00 168.53 ? 3211 THR A CB    1 
ATOM   13998 O  OG1   . THR A 1 3211 ? 140.676 94.891  123.363 1.00 167.70 ? 3211 THR A OG1   1 
ATOM   13999 C  CG2   . THR A 1 3211 ? 141.920 92.837  123.207 1.00 168.03 ? 3211 THR A CG2   1 
ATOM   14000 N  N     . VAL A 1 3212 ? 139.749 91.433  126.045 1.00 177.88 ? 3212 VAL A N     1 
ATOM   14001 C  CA    . VAL A 1 3212 ? 139.870 90.150  126.737 1.00 176.53 ? 3212 VAL A CA    1 
ATOM   14002 C  C     . VAL A 1 3212 ? 138.713 89.233  126.362 1.00 177.09 ? 3212 VAL A C     1 
ATOM   14003 O  O     . VAL A 1 3212 ? 138.908 88.046  126.064 1.00 177.80 ? 3212 VAL A O     1 
ATOM   14004 C  CB    . VAL A 1 3212 ? 139.948 90.371  128.260 1.00 175.26 ? 3212 VAL A CB    1 
ATOM   14005 C  CG1   . VAL A 1 3212 ? 139.407 89.159  129.013 1.00 174.37 ? 3212 VAL A CG1   1 
ATOM   14006 C  CG2   . VAL A 1 3212 ? 141.377 90.674  128.676 1.00 176.16 ? 3212 VAL A CG2   1 
ATOM   14007 N  N     . ASP A 1 3213 ? 137.491 89.768  126.362 1.00 181.77 ? 3213 ASP A N     1 
ATOM   14008 C  CA    . ASP A 1 3213 ? 136.341 88.969  125.947 1.00 181.78 ? 3213 ASP A CA    1 
ATOM   14009 C  C     . ASP A 1 3213 ? 136.465 88.540  124.487 1.00 180.80 ? 3213 ASP A C     1 
ATOM   14010 O  O     . ASP A 1 3213 ? 136.093 87.415  124.125 1.00 180.32 ? 3213 ASP A O     1 
ATOM   14011 C  CB    . ASP A 1 3213 ? 135.048 89.751  126.172 1.00 181.21 ? 3213 ASP A CB    1 
ATOM   14012 C  CG    . ASP A 1 3213 ? 134.664 89.830  127.636 1.00 180.02 ? 3213 ASP A CG    1 
ATOM   14013 O  OD1   . ASP A 1 3213 ? 135.043 88.919  128.402 1.00 181.02 ? 3213 ASP A OD1   1 
ATOM   14014 O  OD2   . ASP A 1 3213 ? 133.982 90.803  128.021 1.00 178.84 ? 3213 ASP A OD2   1 
ATOM   14015 N  N     . GLN A 1 3214 ? 136.984 89.427  123.636 1.00 181.01 ? 3214 GLN A N     1 
ATOM   14016 C  CA    . GLN A 1 3214 ? 137.148 89.099  122.224 1.00 180.91 ? 3214 GLN A CA    1 
ATOM   14017 C  C     . GLN A 1 3214 ? 138.113 87.936  122.035 1.00 183.09 ? 3214 GLN A C     1 
ATOM   14018 O  O     . GLN A 1 3214 ? 137.850 87.022  121.249 1.00 183.73 ? 3214 GLN A O     1 
ATOM   14019 C  CB    . GLN A 1 3214 ? 137.629 90.329  121.454 1.00 180.39 ? 3214 GLN A CB    1 
ATOM   14020 C  CG    . GLN A 1 3214 ? 136.531 91.330  121.142 1.00 181.46 ? 3214 GLN A CG    1 
ATOM   14021 C  CD    . GLN A 1 3214 ? 135.423 90.732  120.299 1.00 182.50 ? 3214 GLN A CD    1 
ATOM   14022 O  OE1   . GLN A 1 3214 ? 135.675 90.163  119.238 1.00 182.85 ? 3214 GLN A OE1   1 
ATOM   14023 N  NE2   . GLN A 1 3214 ? 134.187 90.861  120.768 1.00 182.40 ? 3214 GLN A NE2   1 
ATOM   14024 N  N     . VAL A 1 3215 ? 139.238 87.945  122.755 1.00 190.07 ? 3215 VAL A N     1 
ATOM   14025 C  CA    . VAL A 1 3215 ? 140.182 86.836  122.616 1.00 189.65 ? 3215 VAL A CA    1 
ATOM   14026 C  C     . VAL A 1 3215 ? 139.616 85.563  123.240 1.00 188.88 ? 3215 VAL A C     1 
ATOM   14027 O  O     . VAL A 1 3215 ? 139.878 84.451  122.752 1.00 188.24 ? 3215 VAL A O     1 
ATOM   14028 C  CB    . VAL A 1 3215 ? 141.564 87.199  123.198 1.00 187.82 ? 3215 VAL A CB    1 
ATOM   14029 C  CG1   . VAL A 1 3215 ? 141.993 88.573  122.722 1.00 187.62 ? 3215 VAL A CG1   1 
ATOM   14030 C  CG2   . VAL A 1 3215 ? 141.574 87.126  124.716 1.00 187.80 ? 3215 VAL A CG2   1 
ATOM   14031 N  N     . GLU A 1 3216 ? 138.820 85.692  124.307 1.00 193.34 ? 3216 GLU A N     1 
ATOM   14032 C  CA    . GLU A 1 3216 ? 138.186 84.515  124.890 1.00 193.56 ? 3216 GLU A CA    1 
ATOM   14033 C  C     . GLU A 1 3216 ? 137.237 83.857  123.896 1.00 194.03 ? 3216 GLU A C     1 
ATOM   14034 O  O     . GLU A 1 3216 ? 137.188 82.626  123.797 1.00 194.20 ? 3216 GLU A O     1 
ATOM   14035 C  CB    . GLU A 1 3216 ? 137.448 84.894  126.173 1.00 193.65 ? 3216 GLU A CB    1 
ATOM   14036 C  CG    . GLU A 1 3216 ? 137.282 83.745  127.156 1.00 193.83 ? 3216 GLU A CG    1 
ATOM   14037 C  CD    . GLU A 1 3216 ? 136.050 82.908  126.875 1.00 193.81 ? 3216 GLU A CD    1 
ATOM   14038 O  OE1   . GLU A 1 3216 ? 135.073 83.453  126.321 1.00 193.95 ? 3216 GLU A OE1   1 
ATOM   14039 O  OE2   . GLU A 1 3216 ? 136.060 81.704  127.209 1.00 192.94 ? 3216 GLU A OE2   1 
ATOM   14040 N  N     . GLU A 1 3217 ? 136.475 84.662  123.151 1.00 196.69 ? 3217 GLU A N     1 
ATOM   14041 C  CA    . GLU A 1 3217 ? 135.607 84.093  122.122 1.00 196.50 ? 3217 GLU A CA    1 
ATOM   14042 C  C     . GLU A 1 3217 ? 136.405 83.629  120.907 1.00 197.09 ? 3217 GLU A C     1 
ATOM   14043 O  O     . GLU A 1 3217 ? 135.984 82.703  120.203 1.00 197.74 ? 3217 GLU A O     1 
ATOM   14044 C  CB    . GLU A 1 3217 ? 134.535 85.107  121.715 1.00 196.93 ? 3217 GLU A CB    1 
ATOM   14045 C  CG    . GLU A 1 3217 ? 134.886 85.959  120.505 1.00 197.07 ? 3217 GLU A CG    1 
ATOM   14046 C  CD    . GLU A 1 3217 ? 133.786 86.936  120.142 1.00 196.64 ? 3217 GLU A CD    1 
ATOM   14047 O  OE1   . GLU A 1 3217 ? 132.834 87.083  120.938 1.00 196.77 ? 3217 GLU A OE1   1 
ATOM   14048 O  OE2   . GLU A 1 3217 ? 133.872 87.557  119.062 1.00 196.40 ? 3217 GLU A OE2   1 
ATOM   14049 N  N     . LEU A 1 3218 ? 137.562 84.248  120.653 1.00 198.20 ? 3218 LEU A N     1 
ATOM   14050 C  CA    . LEU A 1 3218 ? 138.400 83.824  119.538 1.00 198.17 ? 3218 LEU A CA    1 
ATOM   14051 C  C     . LEU A 1 3218 ? 139.003 82.452  119.786 1.00 198.84 ? 3218 LEU A C     1 
ATOM   14052 O  O     . LEU A 1 3218 ? 139.242 81.701  118.837 1.00 198.26 ? 3218 LEU A O     1 
ATOM   14053 C  CB    . LEU A 1 3218 ? 139.502 84.854  119.287 1.00 198.01 ? 3218 LEU A CB    1 
ATOM   14054 C  CG    . LEU A 1 3218 ? 139.392 85.651  117.986 1.00 197.53 ? 3218 LEU A CG    1 
ATOM   14055 C  CD1   . LEU A 1 3218 ? 138.167 86.550  118.007 1.00 197.17 ? 3218 LEU A CD1   1 
ATOM   14056 C  CD2   . LEU A 1 3218 ? 140.655 86.465  117.750 1.00 197.35 ? 3218 LEU A CD2   1 
ATOM   14057 N  N     . ARG A 1 3219 ? 139.265 82.107  121.048 1.00 203.43 ? 3219 ARG A N     1 
ATOM   14058 C  CA    . ARG A 1 3219 ? 139.717 80.749  121.348 1.00 203.18 ? 3219 ARG A CA    1 
ATOM   14059 C  C     . ARG A 1 3219 ? 138.660 79.716  120.962 1.00 203.48 ? 3219 ARG A C     1 
ATOM   14060 O  O     . ARG A 1 3219 ? 138.977 78.685  120.349 1.00 202.77 ? 3219 ARG A O     1 
ATOM   14061 C  CB    . ARG A 1 3219 ? 140.072 80.627  122.829 1.00 202.24 ? 3219 ARG A CB    1 
ATOM   14062 C  CG    . ARG A 1 3219 ? 141.514 80.982  123.151 1.00 201.66 ? 3219 ARG A CG    1 
ATOM   14063 C  CD    . ARG A 1 3219 ? 141.885 80.555  124.561 1.00 202.16 ? 3219 ARG A CD    1 
ATOM   14064 N  NE    . ARG A 1 3219 ? 141.011 81.157  125.561 1.00 203.19 ? 3219 ARG A NE    1 
ATOM   14065 C  CZ    . ARG A 1 3219 ? 141.391 82.089  126.424 1.00 202.77 ? 3219 ARG A CZ    1 
ATOM   14066 N  NH1   . ARG A 1 3219 ? 142.630 82.554  126.439 1.00 202.65 ? 3219 ARG A NH1   1 
ATOM   14067 N  NH2   . ARG A 1 3219 ? 140.506 82.568  127.293 1.00 202.34 ? 3219 ARG A NH2   1 
ATOM   14068 N  N     . ARG A 1 3220 ? 137.395 79.980  121.302 1.00 210.59 ? 3220 ARG A N     1 
ATOM   14069 C  CA    . ARG A 1 3220 ? 136.315 79.079  120.913 1.00 210.21 ? 3220 ARG A CA    1 
ATOM   14070 C  C     . ARG A 1 3220 ? 136.152 79.037  119.398 1.00 210.85 ? 3220 ARG A C     1 
ATOM   14071 O  O     . ARG A 1 3220 ? 135.888 77.974  118.821 1.00 211.26 ? 3220 ARG A O     1 
ATOM   14072 C  CB    . ARG A 1 3220 ? 135.011 79.509  121.587 1.00 210.08 ? 3220 ARG A CB    1 
ATOM   14073 C  CG    . ARG A 1 3220 ? 133.751 79.001  120.907 1.00 210.49 ? 3220 ARG A CG    1 
ATOM   14074 C  CD    . ARG A 1 3220 ? 132.647 80.045  120.947 1.00 210.73 ? 3220 ARG A CD    1 
ATOM   14075 N  NE    . ARG A 1 3220 ? 133.065 81.304  120.342 1.00 211.48 ? 3220 ARG A NE    1 
ATOM   14076 C  CZ    . ARG A 1 3220 ? 133.085 81.541  119.038 1.00 210.93 ? 3220 ARG A CZ    1 
ATOM   14077 N  NH1   . ARG A 1 3220 ? 132.713 80.621  118.162 1.00 210.48 ? 3220 ARG A NH1   1 
ATOM   14078 N  NH2   . ARG A 1 3220 ? 133.487 82.730  118.600 1.00 210.46 ? 3220 ARG A NH2   1 
ATOM   14079 N  N     . ASP A 1 3221 ? 136.298 80.189  118.737 1.00 210.68 ? 3221 ASP A N     1 
ATOM   14080 C  CA    . ASP A 1 3221 ? 136.244 80.216  117.278 1.00 209.99 ? 3221 ASP A CA    1 
ATOM   14081 C  C     . ASP A 1 3221 ? 137.358 79.369  116.672 1.00 210.55 ? 3221 ASP A C     1 
ATOM   14082 O  O     . ASP A 1 3221 ? 137.142 78.659  115.684 1.00 210.41 ? 3221 ASP A O     1 
ATOM   14083 C  CB    . ASP A 1 3221 ? 136.329 81.657  116.776 1.00 209.82 ? 3221 ASP A CB    1 
ATOM   14084 C  CG    . ASP A 1 3221 ? 136.214 81.758  115.267 1.00 209.72 ? 3221 ASP A CG    1 
ATOM   14085 O  OD1   . ASP A 1 3221 ? 137.240 81.582  114.576 1.00 209.54 ? 3221 ASP A OD1   1 
ATOM   14086 O  OD2   . ASP A 1 3221 ? 135.097 82.015  114.770 1.00 209.31 ? 3221 ASP A OD2   1 
ATOM   14087 N  N     . LEU A 1 3222 ? 138.558 79.439  117.252 1.00 212.65 ? 3222 LEU A N     1 
ATOM   14088 C  CA    . LEU A 1 3222 ? 139.669 78.615  116.789 1.00 212.47 ? 3222 LEU A CA    1 
ATOM   14089 C  C     . LEU A 1 3222 ? 139.367 77.134  116.964 1.00 213.09 ? 3222 LEU A C     1 
ATOM   14090 O  O     . LEU A 1 3222 ? 139.662 76.323  116.079 1.00 213.27 ? 3222 LEU A O     1 
ATOM   14091 C  CB    . LEU A 1 3222 ? 140.945 78.992  117.543 1.00 211.79 ? 3222 LEU A CB    1 
ATOM   14092 C  CG    . LEU A 1 3222 ? 142.184 78.131  117.291 1.00 211.48 ? 3222 LEU A CG    1 
ATOM   14093 C  CD1   . LEU A 1 3222 ? 142.909 78.592  116.041 1.00 211.74 ? 3222 LEU A CD1   1 
ATOM   14094 C  CD2   . LEU A 1 3222 ? 143.114 78.156  118.494 1.00 210.99 ? 3222 LEU A CD2   1 
ATOM   14095 N  N     . ARG A 1 3223 ? 138.786 76.759  118.107 1.00 215.73 ? 3223 ARG A N     1 
ATOM   14096 C  CA    . ARG A 1 3223 ? 138.430 75.357  118.320 1.00 215.68 ? 3223 ARG A CA    1 
ATOM   14097 C  C     . ARG A 1 3223 ? 137.389 74.889  117.307 1.00 215.76 ? 3223 ARG A C     1 
ATOM   14098 O  O     . ARG A 1 3223 ? 137.494 73.783  116.757 1.00 214.85 ? 3223 ARG A O     1 
ATOM   14099 C  CB    . ARG A 1 3223 ? 137.922 75.153  119.747 1.00 215.35 ? 3223 ARG A CB    1 
ATOM   14100 C  CG    . ARG A 1 3223 ? 137.657 73.698  120.103 1.00 215.11 ? 3223 ARG A CG    1 
ATOM   14101 C  CD    . ARG A 1 3223 ? 136.706 73.565  121.282 1.00 214.37 ? 3223 ARG A CD    1 
ATOM   14102 N  NE    . ARG A 1 3223 ? 135.584 74.492  121.204 1.00 214.23 ? 3223 ARG A NE    1 
ATOM   14103 C  CZ    . ARG A 1 3223 ? 134.516 74.314  120.438 1.00 214.50 ? 3223 ARG A CZ    1 
ATOM   14104 N  NH1   . ARG A 1 3223 ? 134.395 73.255  119.654 1.00 214.02 ? 3223 ARG A NH1   1 
ATOM   14105 N  NH2   . ARG A 1 3223 ? 133.542 75.220  120.463 1.00 214.72 ? 3223 ARG A NH2   1 
ATOM   14106 N  N     . ILE A 1 3224 ? 136.380 75.724  117.043 1.00 219.67 ? 3224 ILE A N     1 
ATOM   14107 C  CA    . ILE A 1 3224 ? 135.349 75.373  116.068 1.00 218.93 ? 3224 ILE A CA    1 
ATOM   14108 C  C     . ILE A 1 3224 ? 135.959 75.219  114.681 1.00 219.06 ? 3224 ILE A C     1 
ATOM   14109 O  O     . ILE A 1 3224 ? 135.628 74.284  113.939 1.00 219.56 ? 3224 ILE A O     1 
ATOM   14110 C  CB    . ILE A 1 3224 ? 134.226 76.427  116.078 1.00 218.47 ? 3224 ILE A CB    1 
ATOM   14111 C  CG1   . ILE A 1 3224 ? 133.406 76.323  117.365 1.00 218.96 ? 3224 ILE A CG1   1 
ATOM   14112 C  CG2   . ILE A 1 3224 ? 133.329 76.272  114.858 1.00 217.90 ? 3224 ILE A CG2   1 
ATOM   14113 C  CD1   . ILE A 1 3224 ? 132.256 77.303  117.437 1.00 218.21 ? 3224 ILE A CD1   1 
ATOM   14114 N  N     . LYS A 1 3225 ? 136.855 76.134  114.308 1.00 220.79 ? 3225 LYS A N     1 
ATOM   14115 C  CA    . LYS A 1 3225 ? 137.497 76.056  113.001 1.00 221.05 ? 3225 LYS A CA    1 
ATOM   14116 C  C     . LYS A 1 3225 ? 138.369 74.813  112.888 1.00 221.70 ? 3225 LYS A C     1 
ATOM   14117 O  O     . LYS A 1 3225 ? 138.428 74.183  111.826 1.00 221.86 ? 3225 LYS A O     1 
ATOM   14118 C  CB    . LYS A 1 3225 ? 138.320 77.319  112.751 1.00 220.36 ? 3225 LYS A CB    1 
ATOM   14119 C  CG    . LYS A 1 3225 ? 137.492 78.519  112.323 1.00 219.65 ? 3225 LYS A CG    1 
ATOM   14120 C  CD    . LYS A 1 3225 ? 136.937 78.337  110.919 1.00 219.28 ? 3225 LYS A CD    1 
ATOM   14121 C  CE    . LYS A 1 3225 ? 138.047 78.058  109.919 1.00 219.94 ? 3225 LYS A CE    1 
ATOM   14122 N  NZ    . LYS A 1 3225 ? 139.218 78.953  110.129 1.00 220.59 ? 3225 LYS A NZ    1 
ATOM   14123 N  N     . SER A 1 3226 ? 139.061 74.446  113.970 1.00 223.83 ? 3226 SER A N     1 
ATOM   14124 C  CA    . SER A 1 3226 ? 139.860 73.225  113.958 1.00 223.10 ? 3226 SER A CA    1 
ATOM   14125 C  C     . SER A 1 3226 ? 138.982 71.993  113.779 1.00 223.98 ? 3226 SER A C     1 
ATOM   14126 O  O     . SER A 1 3226 ? 139.328 71.077  113.022 1.00 224.60 ? 3226 SER A O     1 
ATOM   14127 C  CB    . SER A 1 3226 ? 140.677 73.120  115.245 1.00 222.63 ? 3226 SER A CB    1 
ATOM   14128 O  OG    . SER A 1 3226 ? 139.830 73.020  116.377 1.00 222.39 ? 3226 SER A OG    1 
ATOM   14129 N  N     . GLN A 1 3227 ? 137.841 71.950  114.473 1.00 226.11 ? 3227 GLN A N     1 
ATOM   14130 C  CA    . GLN A 1 3227 ? 136.921 70.828  114.305 1.00 225.87 ? 3227 GLN A CA    1 
ATOM   14131 C  C     . GLN A 1 3227 ? 136.389 70.762  112.877 1.00 225.99 ? 3227 GLN A C     1 
ATOM   14132 O  O     . GLN A 1 3227 ? 136.292 69.676  112.288 1.00 226.35 ? 3227 GLN A O     1 
ATOM   14133 C  CB    . GLN A 1 3227 ? 135.770 70.940  115.306 1.00 225.40 ? 3227 GLN A CB    1 
ATOM   14134 C  CG    . GLN A 1 3227 ? 134.716 69.850  115.175 1.00 225.29 ? 3227 GLN A CG    1 
ATOM   14135 C  CD    . GLN A 1 3227 ? 133.513 70.295  114.365 1.00 225.47 ? 3227 GLN A CD    1 
ATOM   14136 O  OE1   . GLN A 1 3227 ? 133.407 71.459  113.977 1.00 225.17 ? 3227 GLN A OE1   1 
ATOM   14137 N  NE2   . GLN A 1 3227 ? 132.599 69.368  114.106 1.00 225.18 ? 3227 GLN A NE2   1 
ATOM   14138 N  N     . GLU A 1 3228 ? 136.045 71.917  112.303 1.00 225.52 ? 3228 GLU A N     1 
ATOM   14139 C  CA    . GLU A 1 3228 ? 135.574 71.952  110.922 1.00 224.86 ? 3228 GLU A CA    1 
ATOM   14140 C  C     . GLU A 1 3228 ? 136.652 71.468  109.961 1.00 225.13 ? 3228 GLU A C     1 
ATOM   14141 O  O     . GLU A 1 3228 ? 136.364 70.729  109.013 1.00 225.91 ? 3228 GLU A O     1 
ATOM   14142 C  CB    . GLU A 1 3228 ? 135.126 73.368  110.558 1.00 225.48 ? 3228 GLU A CB    1 
ATOM   14143 C  CG    . GLU A 1 3228 ? 134.800 73.562  109.086 1.00 225.33 ? 3228 GLU A CG    1 
ATOM   14144 C  CD    . GLU A 1 3228 ? 134.701 75.025  108.700 1.00 225.40 ? 3228 GLU A CD    1 
ATOM   14145 O  OE1   . GLU A 1 3228 ? 134.966 75.888  109.563 1.00 225.49 ? 3228 GLU A OE1   1 
ATOM   14146 O  OE2   . GLU A 1 3228 ? 134.358 75.311  107.534 1.00 225.01 ? 3228 GLU A OE2   1 
ATOM   14147 N  N     . LEU A 1 3229 ? 137.901 71.881  110.190 1.00 226.84 ? 3229 LEU A N     1 
ATOM   14148 C  CA    . LEU A 1 3229 ? 139.001 71.433  109.344 1.00 226.67 ? 3229 LEU A CA    1 
ATOM   14149 C  C     . LEU A 1 3229 ? 139.191 69.927  109.440 1.00 227.14 ? 3229 LEU A C     1 
ATOM   14150 O  O     . LEU A 1 3229 ? 139.408 69.256  108.424 1.00 227.31 ? 3229 LEU A O     1 
ATOM   14151 C  CB    . LEU A 1 3229 ? 140.290 72.154  109.735 1.00 226.80 ? 3229 LEU A CB    1 
ATOM   14152 C  CG    . LEU A 1 3229 ? 141.530 71.711  108.961 1.00 226.52 ? 3229 LEU A CG    1 
ATOM   14153 C  CD1   . LEU A 1 3229 ? 141.269 71.799  107.466 1.00 226.49 ? 3229 LEU A CD1   1 
ATOM   14154 C  CD2   . LEU A 1 3229 ? 142.738 72.542  109.355 1.00 226.16 ? 3229 LEU A CD2   1 
ATOM   14155 N  N     . GLU A 1 3230 ? 139.125 69.380  110.655 1.00 227.30 ? 3230 GLU A N     1 
ATOM   14156 C  CA    . GLU A 1 3230 ? 139.251 67.936  110.818 1.00 226.70 ? 3230 GLU A CA    1 
ATOM   14157 C  C     . GLU A 1 3230 ? 138.139 67.204  110.078 1.00 227.56 ? 3230 GLU A C     1 
ATOM   14158 O  O     . GLU A 1 3230 ? 138.392 66.211  109.385 1.00 227.34 ? 3230 GLU A O     1 
ATOM   14159 C  CB    . GLU A 1 3230 ? 139.239 67.569  112.301 1.00 226.36 ? 3230 GLU A CB    1 
ATOM   14160 C  CG    . GLU A 1 3230 ? 140.440 68.076  113.079 1.00 226.26 ? 3230 GLU A CG    1 
ATOM   14161 C  CD    . GLU A 1 3230 ? 140.170 68.167  114.568 1.00 226.88 ? 3230 GLU A CD    1 
ATOM   14162 O  OE1   . GLU A 1 3230 ? 139.032 67.865  114.986 1.00 226.52 ? 3230 GLU A OE1   1 
ATOM   14163 O  OE2   . GLU A 1 3230 ? 141.094 68.542  115.320 1.00 226.93 ? 3230 GLU A OE2   1 
ATOM   14164 N  N     . VAL A 1 3231 ? 136.902 67.693  110.201 1.00 230.45 ? 3231 VAL A N     1 
ATOM   14165 C  CA    . VAL A 1 3231 ? 135.776 67.054  109.523 1.00 229.86 ? 3231 VAL A CA    1 
ATOM   14166 C  C     . VAL A 1 3231 ? 135.971 67.096  108.011 1.00 229.50 ? 3231 VAL A C     1 
ATOM   14167 O  O     . VAL A 1 3231 ? 135.793 66.089  107.315 1.00 228.95 ? 3231 VAL A O     1 
ATOM   14168 C  CB    . VAL A 1 3231 ? 134.451 67.718  109.940 1.00 229.01 ? 3231 VAL A CB    1 
ATOM   14169 C  CG1   . VAL A 1 3231 ? 133.329 67.312  108.996 1.00 228.22 ? 3231 VAL A CG1   1 
ATOM   14170 C  CG2   . VAL A 1 3231 ? 134.105 67.354  111.374 1.00 228.98 ? 3231 VAL A CG2   1 
ATOM   14171 N  N     . LYS A 1 3232 ? 136.349 68.264  107.483 1.00 230.64 ? 3232 LYS A N     1 
ATOM   14172 C  CA    . LYS A 1 3232 ? 136.520 68.409  106.040 1.00 229.73 ? 3232 LYS A CA    1 
ATOM   14173 C  C     . LYS A 1 3232 ? 137.634 67.509  105.522 1.00 230.38 ? 3232 LYS A C     1 
ATOM   14174 O  O     . LYS A 1 3232 ? 137.477 66.837  104.495 1.00 230.69 ? 3232 LYS A O     1 
ATOM   14175 C  CB    . LYS A 1 3232 ? 136.804 69.870  105.689 1.00 229.50 ? 3232 LYS A CB    1 
ATOM   14176 C  CG    . LYS A 1 3232 ? 135.619 70.803  105.878 1.00 229.60 ? 3232 LYS A CG    1 
ATOM   14177 C  CD    . LYS A 1 3232 ? 134.585 70.609  104.782 1.00 229.38 ? 3232 LYS A CD    1 
ATOM   14178 C  CE    . LYS A 1 3232 ? 133.546 71.718  104.803 1.00 229.23 ? 3232 LYS A CE    1 
ATOM   14179 N  NZ    . LYS A 1 3232 ? 132.650 71.662  103.615 1.00 228.87 ? 3232 LYS A NZ    1 
ATOM   14180 N  N     . ASN A 1 3233 ? 138.772 67.482  106.221 1.00 236.40 ? 3233 ASN A N     1 
ATOM   14181 C  CA    . ASN A 1 3233 ? 139.892 66.661  105.776 1.00 236.42 ? 3233 ASN A CA    1 
ATOM   14182 C  C     . ASN A 1 3233 ? 139.548 65.178  105.832 1.00 236.54 ? 3233 ASN A C     1 
ATOM   14183 O  O     . ASN A 1 3233 ? 139.867 64.428  104.900 1.00 236.81 ? 3233 ASN A O     1 
ATOM   14184 C  CB    . ASN A 1 3233 ? 141.131 66.959  106.621 1.00 235.64 ? 3233 ASN A CB    1 
ATOM   14185 C  CG    . ASN A 1 3233 ? 142.401 66.397  106.011 1.00 235.96 ? 3233 ASN A CG    1 
ATOM   14186 O  OD1   . ASN A 1 3233 ? 142.621 65.185  106.009 1.00 236.16 ? 3233 ASN A OD1   1 
ATOM   14187 N  ND2   . ASN A 1 3233 ? 143.245 67.278  105.486 1.00 235.68 ? 3233 ASN A ND2   1 
ATOM   14188 N  N     . ALA A 1 3234 ? 138.896 64.736  106.912 1.00 232.01 ? 3234 ALA A N     1 
ATOM   14189 C  CA    . ALA A 1 3234 ? 138.514 63.332  107.014 1.00 231.04 ? 3234 ALA A CA    1 
ATOM   14190 C  C     . ALA A 1 3234 ? 137.528 62.950  105.918 1.00 231.64 ? 3234 ALA A C     1 
ATOM   14191 O  O     . ALA A 1 3234 ? 137.661 61.887  105.299 1.00 231.66 ? 3234 ALA A O     1 
ATOM   14192 C  CB    . ALA A 1 3234 ? 137.923 63.047  108.394 1.00 230.86 ? 3234 ALA A CB    1 
ATOM   14193 N  N     . ALA A 1 3235 ? 136.537 63.808  105.658 1.00 234.66 ? 3235 ALA A N     1 
ATOM   14194 C  CA    . ALA A 1 3235 ? 135.566 63.515  104.609 1.00 234.41 ? 3235 ALA A CA    1 
ATOM   14195 C  C     . ALA A 1 3235 ? 136.232 63.452  103.241 1.00 234.83 ? 3235 ALA A C     1 
ATOM   14196 O  O     . ALA A 1 3235 ? 135.944 62.551  102.445 1.00 234.92 ? 3235 ALA A O     1 
ATOM   14197 C  CB    . ALA A 1 3235 ? 134.452 64.561  104.617 1.00 233.80 ? 3235 ALA A CB    1 
ATOM   14198 N  N     . ALA A 1 3236 ? 137.132 64.397  102.952 1.00 236.06 ? 3236 ALA A N     1 
ATOM   14199 C  CA    . ALA A 1 3236 ? 137.814 64.396  101.662 1.00 235.50 ? 3236 ALA A CA    1 
ATOM   14200 C  C     . ALA A 1 3236 ? 138.676 63.152  101.491 1.00 236.01 ? 3236 ALA A C     1 
ATOM   14201 O  O     . ALA A 1 3236 ? 138.664 62.521  100.427 1.00 236.09 ? 3236 ALA A O     1 
ATOM   14202 C  CB    . ALA A 1 3236 ? 138.660 65.660  101.516 1.00 234.50 ? 3236 ALA A CB    1 
ATOM   14203 N  N     . ASN A 1 3237 ? 139.426 62.777  102.531 1.00 236.71 ? 3237 ASN A N     1 
ATOM   14204 C  CA    . ASN A 1 3237 ? 140.281 61.598  102.434 1.00 236.33 ? 3237 ASN A CA    1 
ATOM   14205 C  C     . ASN A 1 3237 ? 139.459 60.323  102.287 1.00 236.01 ? 3237 ASN A C     1 
ATOM   14206 O  O     . ASN A 1 3237 ? 139.822 59.432  101.510 1.00 235.65 ? 3237 ASN A O     1 
ATOM   14207 C  CB    . ASN A 1 3237 ? 141.201 61.512  103.651 1.00 236.13 ? 3237 ASN A CB    1 
ATOM   14208 C  CG    . ASN A 1 3237 ? 142.185 62.665  103.718 1.00 235.80 ? 3237 ASN A CG    1 
ATOM   14209 O  OD1   . ASN A 1 3237 ? 142.166 63.563  102.876 1.00 235.90 ? 3237 ASN A OD1   1 
ATOM   14210 N  ND2   . ASN A 1 3237 ? 143.053 62.644  104.723 1.00 235.28 ? 3237 ASN A ND2   1 
ATOM   14211 N  N     . ASP A 1 3238 ? 138.349 60.213  103.023 1.00 232.37 ? 3238 ASP A N     1 
ATOM   14212 C  CA    . ASP A 1 3238 ? 137.516 59.020  102.918 1.00 231.93 ? 3238 ASP A CA    1 
ATOM   14213 C  C     . ASP A 1 3238 ? 136.815 58.937  101.568 1.00 231.57 ? 3238 ASP A C     1 
ATOM   14214 O  O     . ASP A 1 3238 ? 136.646 57.837  101.028 1.00 230.95 ? 3238 ASP A O     1 
ATOM   14215 C  CB    . ASP A 1 3238 ? 136.495 58.989  104.054 1.00 231.39 ? 3238 ASP A CB    1 
ATOM   14216 C  CG    . ASP A 1 3238 ? 137.135 58.719  105.403 1.00 230.75 ? 3238 ASP A CG    1 
ATOM   14217 O  OD1   . ASP A 1 3238 ? 138.369 58.524  105.448 1.00 230.64 ? 3238 ASP A OD1   1 
ATOM   14218 O  OD2   . ASP A 1 3238 ? 136.407 58.701  106.417 1.00 230.08 ? 3238 ASP A OD2   1 
ATOM   14219 N  N     . LYS A 1 3239 ? 136.397 60.076  101.009 1.00 230.90 ? 3239 LYS A N     1 
ATOM   14220 C  CA    . LYS A 1 3239 ? 135.777 60.062  99.690  1.00 230.84 ? 3239 LYS A CA    1 
ATOM   14221 C  C     . LYS A 1 3239 ? 136.793 59.763  98.596  1.00 231.09 ? 3239 LYS A C     1 
ATOM   14222 O  O     . LYS A 1 3239 ? 136.449 59.132  97.590  1.00 231.09 ? 3239 LYS A O     1 
ATOM   14223 C  CB    . LYS A 1 3239 ? 135.078 61.395  99.424  1.00 230.72 ? 3239 LYS A CB    1 
ATOM   14224 C  CG    . LYS A 1 3239 ? 133.728 61.533  100.109 1.00 230.27 ? 3239 LYS A CG    1 
ATOM   14225 C  CD    . LYS A 1 3239 ? 132.918 62.673  99.512  1.00 230.13 ? 3239 LYS A CD    1 
ATOM   14226 C  CE    . LYS A 1 3239 ? 131.585 62.835  100.225 1.00 230.30 ? 3239 LYS A CE    1 
ATOM   14227 N  NZ    . LYS A 1 3239 ? 130.791 63.968  99.672  1.00 229.78 ? 3239 LYS A NZ    1 
ATOM   14228 N  N     . LEU A 1 3240 ? 138.040 60.209  98.767  1.00 228.80 ? 3240 LEU A N     1 
ATOM   14229 C  CA    . LEU A 1 3240 ? 139.082 59.864  97.806  1.00 228.44 ? 3240 LEU A CA    1 
ATOM   14230 C  C     . LEU A 1 3240 ? 139.389 58.372  97.822  1.00 228.63 ? 3240 LEU A C     1 
ATOM   14231 O  O     . LEU A 1 3240 ? 139.901 57.835  96.833  1.00 227.65 ? 3240 LEU A O     1 
ATOM   14232 C  CB    . LEU A 1 3240 ? 140.350 60.670  98.090  1.00 228.03 ? 3240 LEU A CB    1 
ATOM   14233 C  CG    . LEU A 1 3240 ? 140.423 62.065  97.466  1.00 227.32 ? 3240 LEU A CG    1 
ATOM   14234 C  CD1   . LEU A 1 3240 ? 141.622 62.830  98.001  1.00 226.92 ? 3240 LEU A CD1   1 
ATOM   14235 C  CD2   . LEU A 1 3240 ? 140.482 61.966  95.950  1.00 227.31 ? 3240 LEU A CD2   1 
ATOM   14236 N  N     . LYS A 1 3241 ? 139.086 57.689  98.929  1.00 229.36 ? 3241 LYS A N     1 
ATOM   14237 C  CA    . LYS A 1 3241 ? 139.310 56.250  99.008  1.00 228.75 ? 3241 LYS A CA    1 
ATOM   14238 C  C     . LYS A 1 3241 ? 138.318 55.464  98.162  1.00 228.43 ? 3241 LYS A C     1 
ATOM   14239 O  O     . LYS A 1 3241 ? 138.537 54.272  97.917  1.00 227.64 ? 3241 LYS A O     1 
ATOM   14240 C  CB    . LYS A 1 3241 ? 139.233 55.786  100.463 1.00 227.57 ? 3241 LYS A CB    1 
ATOM   14241 C  CG    . LYS A 1 3241 ? 140.421 56.204  101.313 1.00 227.55 ? 3241 LYS A CG    1 
ATOM   14242 C  CD    . LYS A 1 3241 ? 140.070 56.195  102.791 1.00 227.39 ? 3241 LYS A CD    1 
ATOM   14243 C  CE    . LYS A 1 3241 ? 141.038 57.049  103.594 1.00 227.14 ? 3241 LYS A CE    1 
ATOM   14244 N  NZ    . LYS A 1 3241 ? 140.607 57.192  105.012 1.00 226.50 ? 3241 LYS A NZ    1 
ATOM   14245 N  N     . LYS A 1 3242 ? 137.237 56.096  97.716  1.00 224.57 ? 3242 LYS A N     1 
ATOM   14246 C  CA    . LYS A 1 3242 ? 136.220 55.422  96.917  1.00 223.19 ? 3242 LYS A CA    1 
ATOM   14247 C  C     . LYS A 1 3242 ? 136.759 55.036  95.543  1.00 222.48 ? 3242 LYS A C     1 
ATOM   14248 O  O     . LYS A 1 3242 ? 137.740 55.603  95.064  0.00 223.39 ? 3242 LYS A O     1 
ATOM   14249 C  CB    . LYS A 1 3242 ? 134.987 56.314  96.765  1.00 222.72 ? 3242 LYS A CB    1 
ATOM   14250 C  CG    . LYS A 1 3242 ? 134.163 56.451  98.034  1.00 223.02 ? 3242 LYS A CG    1 
ATOM   14251 C  CD    . LYS A 1 3242 ? 133.110 57.538  97.894  1.00 223.12 ? 3242 LYS A CD    1 
ATOM   14252 C  CE    . LYS A 1 3242 ? 132.339 57.729  99.189  1.00 223.18 ? 3242 LYS A CE    1 
ATOM   14253 N  NZ    . LYS A 1 3242 ? 131.529 58.978  99.175  1.00 222.65 ? 3242 LYS A NZ    1 
ATOM   14254 N  N     . GLU A 1 3449 ? 137.355 64.587  90.959  1.00 226.49 ? 3449 GLU A N     1 
ATOM   14255 C  CA    . GLU A 1 3449 ? 136.930 65.910  90.516  1.00 226.99 ? 3449 GLU A CA    1 
ATOM   14256 C  C     . GLU A 1 3449 ? 136.297 66.690  91.665  1.00 227.70 ? 3449 GLU A C     1 
ATOM   14257 O  O     . GLU A 1 3449 ? 136.810 67.729  92.078  1.00 227.59 ? 3449 GLU A O     1 
ATOM   14258 C  CB    . GLU A 1 3449 ? 135.949 65.793  89.348  1.00 226.74 ? 3449 GLU A CB    1 
ATOM   14259 C  CG    . GLU A 1 3449 ? 136.417 64.861  88.241  1.00 226.63 ? 3449 GLU A CG    1 
ATOM   14260 C  CD    . GLU A 1 3449 ? 135.429 64.771  87.095  1.00 226.77 ? 3449 GLU A CD    1 
ATOM   14261 O  OE1   . GLU A 1 3449 ? 134.392 65.466  87.147  1.00 226.69 ? 3449 GLU A OE1   1 
ATOM   14262 O  OE2   . GLU A 1 3449 ? 135.688 64.006  86.143  1.00 226.76 ? 3449 GLU A OE2   1 
ATOM   14263 N  N     . GLU A 1 3450 ? 135.172 66.181  92.173  1.00 234.62 ? 3450 GLU A N     1 
ATOM   14264 C  CA    . GLU A 1 3450 ? 134.528 66.811  93.322  1.00 234.41 ? 3450 GLU A CA    1 
ATOM   14265 C  C     . GLU A 1 3450 ? 135.381 66.666  94.577  1.00 235.12 ? 3450 GLU A C     1 
ATOM   14266 O  O     . GLU A 1 3450 ? 135.440 67.582  95.408  1.00 235.13 ? 3450 GLU A O     1 
ATOM   14267 C  CB    . GLU A 1 3450 ? 133.140 66.208  93.537  1.00 233.99 ? 3450 GLU A CB    1 
ATOM   14268 C  CG    . GLU A 1 3450 ? 132.381 66.785  94.719  1.00 234.20 ? 3450 GLU A CG    1 
ATOM   14269 C  CD    . GLU A 1 3450 ? 130.971 66.239  94.826  1.00 234.12 ? 3450 GLU A CD    1 
ATOM   14270 O  OE1   . GLU A 1 3450 ? 130.648 65.276  94.099  1.00 233.53 ? 3450 GLU A OE1   1 
ATOM   14271 O  OE2   . GLU A 1 3450 ? 130.185 66.771  95.638  1.00 234.21 ? 3450 GLU A OE2   1 
ATOM   14272 N  N     . TYR A 1 3451 ? 136.048 65.521  94.732  1.00 234.82 ? 3451 TYR A N     1 
ATOM   14273 C  CA    . TYR A 1 3451 ? 136.934 65.330  95.874  1.00 234.03 ? 3451 TYR A CA    1 
ATOM   14274 C  C     . TYR A 1 3451 ? 138.140 66.259  95.804  1.00 234.57 ? 3451 TYR A C     1 
ATOM   14275 O  O     . TYR A 1 3451 ? 138.696 66.634  96.843  1.00 234.26 ? 3451 TYR A O     1 
ATOM   14276 C  CB    . TYR A 1 3451 ? 137.372 63.869  95.948  1.00 233.16 ? 3451 TYR A CB    1 
ATOM   14277 C  CG    . TYR A 1 3451 ? 136.271 62.901  95.571  1.00 233.32 ? 3451 TYR A CG    1 
ATOM   14278 C  CD1   . TYR A 1 3451 ? 135.078 62.867  96.281  1.00 233.27 ? 3451 TYR A CD1   1 
ATOM   14279 C  CD2   . TYR A 1 3451 ? 136.421 62.029  94.502  1.00 233.23 ? 3451 TYR A CD2   1 
ATOM   14280 C  CE1   . TYR A 1 3451 ? 134.067 61.988  95.940  1.00 233.21 ? 3451 TYR A CE1   1 
ATOM   14281 C  CE2   . TYR A 1 3451 ? 135.416 61.146  94.153  1.00 233.26 ? 3451 TYR A CE2   1 
ATOM   14282 C  CZ    . TYR A 1 3451 ? 134.242 61.130  94.875  1.00 233.17 ? 3451 TYR A CZ    1 
ATOM   14283 O  OH    . TYR A 1 3451 ? 133.239 60.254  94.531  1.00 232.73 ? 3451 TYR A OH    1 
ATOM   14284 N  N     . ALA A 1 3452 ? 138.550 66.650  94.595  1.00 240.37 ? 3452 ALA A N     1 
ATOM   14285 C  CA    . ALA A 1 3452 ? 139.563 67.691  94.464  1.00 239.73 ? 3452 ALA A CA    1 
ATOM   14286 C  C     . ALA A 1 3452 ? 139.059 69.012  95.032  1.00 240.28 ? 3452 ALA A C     1 
ATOM   14287 O  O     . ALA A 1 3452 ? 139.804 69.734  95.704  1.00 240.41 ? 3452 ALA A O     1 
ATOM   14288 C  CB    . ALA A 1 3452 ? 139.969 67.851  92.999  1.00 239.22 ? 3452 ALA A CB    1 
ATOM   14289 N  N     . VAL A 1 3453 ? 137.792 69.343  94.777  1.00 240.70 ? 3453 VAL A N     1 
ATOM   14290 C  CA    . VAL A 1 3453 ? 137.200 70.534  95.381  1.00 240.10 ? 3453 VAL A CA    1 
ATOM   14291 C  C     . VAL A 1 3453 ? 137.154 70.391  96.897  1.00 240.38 ? 3453 VAL A C     1 
ATOM   14292 O  O     . VAL A 1 3453 ? 137.356 71.364  97.636  1.00 240.16 ? 3453 VAL A O     1 
ATOM   14293 C  CB    . VAL A 1 3453 ? 135.801 70.794  94.792  1.00 239.20 ? 3453 VAL A CB    1 
ATOM   14294 C  CG1   . VAL A 1 3453 ? 135.262 72.133  95.271  1.00 238.94 ? 3453 VAL A CG1   1 
ATOM   14295 C  CG2   . VAL A 1 3453 ? 135.848 70.742  93.272  1.00 239.06 ? 3453 VAL A CG2   1 
ATOM   14296 N  N     . LEU A 1 3454 ? 136.884 69.177  97.383  1.00 240.42 ? 3454 LEU A N     1 
ATOM   14297 C  CA    . LEU A 1 3454 ? 136.857 68.943  98.825  1.00 239.85 ? 3454 LEU A CA    1 
ATOM   14298 C  C     . LEU A 1 3454 ? 138.225 69.196  99.451  1.00 240.00 ? 3454 LEU A C     1 
ATOM   14299 O  O     . LEU A 1 3454 ? 138.334 69.864  100.486 1.00 239.99 ? 3454 LEU A O     1 
ATOM   14300 C  CB    . LEU A 1 3454 ? 136.387 67.517  99.115  1.00 238.90 ? 3454 LEU A CB    1 
ATOM   14301 C  CG    . LEU A 1 3454 ? 134.933 67.354  99.562  1.00 238.34 ? 3454 LEU A CG    1 
ATOM   14302 C  CD1   . LEU A 1 3454 ? 133.978 67.727  98.440  1.00 238.55 ? 3454 LEU A CD1   1 
ATOM   14303 C  CD2   . LEU A 1 3454 ? 134.676 65.934  100.041 1.00 237.97 ? 3454 LEU A CD2   1 
ATOM   14304 N  N     . ILE A 1 3455 ? 139.287 68.674  98.834  1.00 240.00 ? 3455 ILE A N     1 
ATOM   14305 C  CA    . ILE A 1 3455 ? 140.619 68.897  99.394  1.00 239.47 ? 3455 ILE A CA    1 
ATOM   14306 C  C     . ILE A 1 3455 ? 141.036 70.357  99.238  1.00 239.98 ? 3455 ILE A C     1 
ATOM   14307 O  O     . ILE A 1 3455 ? 141.761 70.894  100.085 1.00 239.59 ? 3455 ILE A O     1 
ATOM   14308 C  CB    . ILE A 1 3455 ? 141.653 67.931  98.779  1.00 238.81 ? 3455 ILE A CB    1 
ATOM   14309 C  CG1   . ILE A 1 3455 ? 141.981 68.304  97.333  1.00 238.75 ? 3455 ILE A CG1   1 
ATOM   14310 C  CG2   . ILE A 1 3455 ? 141.166 66.491  98.877  1.00 238.85 ? 3455 ILE A CG2   1 
ATOM   14311 C  CD1   . ILE A 1 3455 ? 143.139 67.525  96.749  1.00 238.10 ? 3455 ILE A CD1   1 
ATOM   14312 N  N     . SER A 1 3456 ? 140.580 71.033  98.178  1.00 241.42 ? 3456 SER A N     1 
ATOM   14313 C  CA    . SER A 1 3456 ? 140.882 72.454  98.029  1.00 240.43 ? 3456 SER A CA    1 
ATOM   14314 C  C     . SER A 1 3456 ? 140.225 73.281  99.129  1.00 240.47 ? 3456 SER A C     1 
ATOM   14315 O  O     . SER A 1 3456 ? 140.861 74.169  99.712  1.00 240.49 ? 3456 SER A O     1 
ATOM   14316 C  CB    . SER A 1 3456 ? 140.436 72.944  96.652  1.00 239.96 ? 3456 SER A CB    1 
ATOM   14317 O  OG    . SER A 1 3456 ? 139.023 72.960  96.549  1.00 239.85 ? 3456 SER A OG    1 
ATOM   14318 N  N     . GLU A 1 3457 ? 138.954 73.005  99.432  1.00 238.75 ? 3457 GLU A N     1 
ATOM   14319 C  CA    . GLU A 1 3457 ? 138.306 73.729  100.521 1.00 238.00 ? 3457 GLU A CA    1 
ATOM   14320 C  C     . GLU A 1 3457 ? 138.900 73.341  101.870 1.00 238.29 ? 3457 GLU A C     1 
ATOM   14321 O  O     . GLU A 1 3457 ? 138.938 74.168  102.787 1.00 238.33 ? 3457 GLU A O     1 
ATOM   14322 C  CB    . GLU A 1 3457 ? 136.792 73.500  100.500 1.00 237.72 ? 3457 GLU A CB    1 
ATOM   14323 C  CG    . GLU A 1 3457 ? 136.334 72.130  100.963 1.00 238.25 ? 3457 GLU A CG    1 
ATOM   14324 C  CD    . GLU A 1 3457 ? 134.844 71.921  100.776 1.00 238.26 ? 3457 GLU A CD    1 
ATOM   14325 O  OE1   . GLU A 1 3457 ? 134.176 72.834  100.248 1.00 237.71 ? 3457 GLU A OE1   1 
ATOM   14326 O  OE2   . GLU A 1 3457 ? 134.342 70.842  101.157 1.00 238.49 ? 3457 GLU A OE2   1 
ATOM   14327 N  N     . ALA A 1 3458 ? 139.393 72.107  102.003 1.00 237.55 ? 3458 ALA A N     1 
ATOM   14328 C  CA    . ALA A 1 3458 ? 140.118 71.732  103.212 1.00 237.17 ? 3458 ALA A CA    1 
ATOM   14329 C  C     . ALA A 1 3458 ? 141.391 72.556  103.366 1.00 237.35 ? 3458 ALA A C     1 
ATOM   14330 O  O     . ALA A 1 3458 ? 141.722 73.000  104.470 1.00 237.30 ? 3458 ALA A O     1 
ATOM   14331 C  CB    . ALA A 1 3458 ? 140.439 70.238  103.192 1.00 236.30 ? 3458 ALA A CB    1 
ATOM   14332 N  N     . GLN A 1 3459 ? 142.118 72.771  102.267 1.00 235.71 ? 3459 GLN A N     1 
ATOM   14333 C  CA    . GLN A 1 3459 ? 143.303 73.625  102.312 1.00 235.34 ? 3459 GLN A CA    1 
ATOM   14334 C  C     . GLN A 1 3459 ? 142.934 75.065  102.655 1.00 234.65 ? 3459 GLN A C     1 
ATOM   14335 O  O     . GLN A 1 3459 ? 143.661 75.748  103.390 1.00 234.84 ? 3459 GLN A O     1 
ATOM   14336 C  CB    . GLN A 1 3459 ? 144.041 73.565  100.975 1.00 235.70 ? 3459 GLN A CB    1 
ATOM   14337 C  CG    . GLN A 1 3459 ? 145.423 74.196  100.995 1.00 235.23 ? 3459 GLN A CG    1 
ATOM   14338 C  CD    . GLN A 1 3459 ? 146.169 74.003  99.689  1.00 234.79 ? 3459 GLN A CD    1 
ATOM   14339 O  OE1   . GLN A 1 3459 ? 146.362 72.877  99.232  1.00 235.25 ? 3459 GLN A OE1   1 
ATOM   14340 N  NE2   . GLN A 1 3459 ? 146.591 75.106  99.080  1.00 234.13 ? 3459 GLN A NE2   1 
ATOM   14341 N  N     . ALA A 1 3460 ? 141.814 75.549  102.115 1.00 229.91 ? 3460 ALA A N     1 
ATOM   14342 C  CA    . ALA A 1 3460 ? 141.350 76.891  102.457 1.00 229.36 ? 3460 ALA A CA    1 
ATOM   14343 C  C     . ALA A 1 3460 ? 141.045 77.004  103.947 1.00 230.29 ? 3460 ALA A C     1 
ATOM   14344 O  O     . ALA A 1 3460 ? 141.390 78.006  104.588 1.00 230.24 ? 3460 ALA A O     1 
ATOM   14345 C  CB    . ALA A 1 3460 ? 140.119 77.250  101.626 1.00 229.08 ? 3460 ALA A CB    1 
ATOM   14346 N  N     . ILE A 1 3461 ? 140.397 75.984  104.514 1.00 230.89 ? 3461 ILE A N     1 
ATOM   14347 C  CA    . ILE A 1 3461 ? 140.124 75.980  105.949 1.00 230.37 ? 3461 ILE A CA    1 
ATOM   14348 C  C     . ILE A 1 3461 ? 141.425 75.900  106.740 1.00 229.97 ? 3461 ILE A C     1 
ATOM   14349 O  O     . ILE A 1 3461 ? 141.547 76.490  107.818 1.00 229.74 ? 3461 ILE A O     1 
ATOM   14350 C  CB    . ILE A 1 3461 ? 139.159 74.836  106.313 1.00 229.90 ? 3461 ILE A CB    1 
ATOM   14351 C  CG1   . ILE A 1 3461 ? 137.834 74.996  105.566 1.00 229.30 ? 3461 ILE A CG1   1 
ATOM   14352 C  CG2   . ILE A 1 3461 ? 138.891 74.817  107.806 1.00 229.33 ? 3461 ILE A CG2   1 
ATOM   14353 C  CD1   . ILE A 1 3461 ? 137.154 76.326  105.807 1.00 228.92 ? 3461 ILE A CD1   1 
ATOM   14354 N  N     . LYS A 1 3462 ? 142.415 75.166  106.222 1.00 228.78 ? 3462 LYS A N     1 
ATOM   14355 C  CA    . LYS A 1 3462 ? 143.734 75.142  106.852 1.00 228.36 ? 3462 LYS A CA    1 
ATOM   14356 C  C     . LYS A 1 3462 ? 144.321 76.545  106.938 1.00 228.13 ? 3462 LYS A C     1 
ATOM   14357 O  O     . LYS A 1 3462 ? 144.810 76.966  107.994 1.00 227.35 ? 3462 LYS A O     1 
ATOM   14358 C  CB    . LYS A 1 3462 ? 144.683 74.230  106.070 1.00 228.47 ? 3462 LYS A CB    1 
ATOM   14359 C  CG    . LYS A 1 3462 ? 144.391 72.747  106.161 1.00 228.28 ? 3462 LYS A CG    1 
ATOM   14360 C  CD    . LYS A 1 3462 ? 145.177 71.971  105.116 1.00 228.11 ? 3462 LYS A CD    1 
ATOM   14361 C  CE    . LYS A 1 3462 ? 144.815 70.495  105.131 1.00 228.00 ? 3462 LYS A CE    1 
ATOM   14362 N  NZ    . LYS A 1 3462 ? 143.378 70.273  104.814 1.00 227.77 ? 3462 LYS A NZ    1 
ATOM   14363 N  N     . ALA A 1 3463 ? 144.287 77.278  105.824 1.00 227.48 ? 3463 ALA A N     1 
ATOM   14364 C  CA    . ALA A 1 3463 ? 144.833 78.633  105.810 1.00 226.85 ? 3463 ALA A CA    1 
ATOM   14365 C  C     . ALA A 1 3463 ? 144.063 79.550  106.754 1.00 226.96 ? 3463 ALA A C     1 
ATOM   14366 O  O     . ALA A 1 3463 ? 144.662 80.360  107.475 1.00 227.34 ? 3463 ALA A O     1 
ATOM   14367 C  CB    . ALA A 1 3463 ? 144.817 79.191  104.387 1.00 226.25 ? 3463 ALA A CB    1 
ATOM   14368 N  N     . ASP A 1 3464 ? 142.733 79.435  106.762 1.00 223.07 ? 3464 ASP A N     1 
ATOM   14369 C  CA    . ASP A 1 3464 ? 141.925 80.263  107.653 1.00 222.96 ? 3464 ASP A CA    1 
ATOM   14370 C  C     . ASP A 1 3464 ? 142.229 79.959  109.117 1.00 223.04 ? 3464 ASP A C     1 
ATOM   14371 O  O     . ASP A 1 3464 ? 142.339 80.876  109.940 1.00 222.79 ? 3464 ASP A O     1 
ATOM   14372 C  CB    . ASP A 1 3464 ? 140.440 80.056  107.352 1.00 222.49 ? 3464 ASP A CB    1 
ATOM   14373 C  CG    . ASP A 1 3464 ? 139.572 81.174  107.895 1.00 221.94 ? 3464 ASP A CG    1 
ATOM   14374 O  OD1   . ASP A 1 3464 ? 140.129 82.182  108.379 1.00 222.15 ? 3464 ASP A OD1   1 
ATOM   14375 O  OD2   . ASP A 1 3464 ? 138.331 81.046  107.837 1.00 221.62 ? 3464 ASP A OD2   1 
ATOM   14376 N  N     . LEU A 1 3465 ? 142.375 78.676  109.458 1.00 221.61 ? 3465 LEU A N     1 
ATOM   14377 C  CA    . LEU A 1 3465 ? 142.710 78.295  110.826 1.00 221.10 ? 3465 LEU A CA    1 
ATOM   14378 C  C     . LEU A 1 3465 ? 144.092 78.801  111.217 1.00 221.18 ? 3465 LEU A C     1 
ATOM   14379 O  O     . LEU A 1 3465 ? 144.303 79.233  112.356 1.00 220.37 ? 3465 LEU A O     1 
ATOM   14380 C  CB    . LEU A 1 3465 ? 142.633 76.775  110.977 1.00 221.09 ? 3465 LEU A CB    1 
ATOM   14381 C  CG    . LEU A 1 3465 ? 142.934 76.198  112.362 1.00 220.54 ? 3465 LEU A CG    1 
ATOM   14382 C  CD1   . LEU A 1 3465 ? 141.797 76.492  113.323 1.00 219.96 ? 3465 LEU A CD1   1 
ATOM   14383 C  CD2   . LEU A 1 3465 ? 143.195 74.702  112.281 1.00 220.21 ? 3465 LEU A CD2   1 
ATOM   14384 N  N     . ALA A 1 3466 ? 145.050 78.745  110.288 1.00 218.49 ? 3466 ALA A N     1 
ATOM   14385 C  CA    . ALA A 1 3466 ? 146.381 79.273  110.570 1.00 217.48 ? 3466 ALA A CA    1 
ATOM   14386 C  C     . ALA A 1 3466 ? 146.333 80.772  110.835 1.00 217.12 ? 3466 ALA A C     1 
ATOM   14387 O  O     . ALA A 1 3466 ? 146.979 81.268  111.767 1.00 217.39 ? 3466 ALA A O     1 
ATOM   14388 C  CB    . ALA A 1 3466 ? 147.327 78.961  109.411 1.00 216.84 ? 3466 ALA A CB    1 
ATOM   14389 N  N     . ALA A 1 3467 ? 145.565 81.510  110.029 1.00 210.29 ? 3467 ALA A N     1 
ATOM   14390 C  CA    . ALA A 1 3467 ? 145.423 82.945  110.260 1.00 209.57 ? 3467 ALA A CA    1 
ATOM   14391 C  C     . ALA A 1 3467 ? 144.763 83.224  111.605 1.00 210.21 ? 3467 ALA A C     1 
ATOM   14392 O  O     . ALA A 1 3467 ? 145.180 84.133  112.337 1.00 209.79 ? 3467 ALA A O     1 
ATOM   14393 C  CB    . ALA A 1 3467 ? 144.623 83.584  109.125 1.00 209.03 ? 3467 ALA A CB    1 
ATOM   14394 N  N     . VAL A 1 3468 ? 143.735 82.445  111.951 1.00 210.04 ? 3468 VAL A N     1 
ATOM   14395 C  CA    . VAL A 1 3468 ? 143.049 82.632  113.226 1.00 209.86 ? 3468 VAL A CA    1 
ATOM   14396 C  C     . VAL A 1 3468 ? 144.000 82.373  114.388 1.00 209.26 ? 3468 VAL A C     1 
ATOM   14397 O  O     . VAL A 1 3468 ? 144.021 83.124  115.370 1.00 209.27 ? 3468 VAL A O     1 
ATOM   14398 C  CB    . VAL A 1 3468 ? 141.802 81.731  113.299 1.00 208.90 ? 3468 VAL A CB    1 
ATOM   14399 C  CG1   . VAL A 1 3468 ? 141.289 81.639  114.728 1.00 208.80 ? 3468 VAL A CG1   1 
ATOM   14400 C  CG2   . VAL A 1 3468 ? 140.713 82.256  112.377 1.00 208.45 ? 3468 VAL A CG2   1 
ATOM   14401 N  N     . GLU A 1 3469 ? 144.806 81.313  114.296 1.00 202.73 ? 3469 GLU A N     1 
ATOM   14402 C  CA    . GLU A 1 3469 ? 145.727 80.997  115.384 1.00 201.93 ? 3469 GLU A CA    1 
ATOM   14403 C  C     . GLU A 1 3469 ? 146.837 82.037  115.493 1.00 201.94 ? 3469 GLU A C     1 
ATOM   14404 O  O     . GLU A 1 3469 ? 147.278 82.365  116.601 1.00 201.61 ? 3469 GLU A O     1 
ATOM   14405 C  CB    . GLU A 1 3469 ? 146.296 79.586  115.204 1.00 202.65 ? 3469 GLU A CB    1 
ATOM   14406 C  CG    . GLU A 1 3469 ? 147.554 79.483  114.358 1.00 203.17 ? 3469 GLU A CG    1 
ATOM   14407 C  CD    . GLU A 1 3469 ? 148.124 78.079  114.336 1.00 202.65 ? 3469 GLU A CD    1 
ATOM   14408 O  OE1   . GLU A 1 3469 ? 148.469 77.559  115.418 1.00 202.43 ? 3469 GLU A OE1   1 
ATOM   14409 O  OE2   . GLU A 1 3469 ? 148.224 77.495  113.237 1.00 202.32 ? 3469 GLU A OE2   1 
ATOM   14410 N  N     . ALA A 1 3470 ? 147.292 82.583  114.360 1.00 197.19 ? 3470 ALA A N     1 
ATOM   14411 C  CA    . ALA A 1 3470 ? 148.279 83.658  114.414 1.00 196.43 ? 3470 ALA A CA    1 
ATOM   14412 C  C     . ALA A 1 3470 ? 147.700 84.898  115.083 1.00 196.23 ? 3470 ALA A C     1 
ATOM   14413 O  O     . ALA A 1 3470 ? 148.362 85.537  115.913 1.00 195.73 ? 3470 ALA A O     1 
ATOM   14414 C  CB    . ALA A 1 3470 ? 148.778 83.987  113.007 1.00 195.61 ? 3470 ALA A CB    1 
ATOM   14415 N  N     . LYS A 1 3471 ? 146.456 85.247  114.742 1.00 186.79 ? 3471 LYS A N     1 
ATOM   14416 C  CA    . LYS A 1 3471 ? 145.806 86.381  115.390 1.00 185.37 ? 3471 LYS A CA    1 
ATOM   14417 C  C     . LYS A 1 3471 ? 145.624 86.130  116.881 1.00 186.03 ? 3471 LYS A C     1 
ATOM   14418 O  O     . LYS A 1 3471 ? 145.785 87.045  117.695 1.00 186.20 ? 3471 LYS A O     1 
ATOM   14419 C  CB    . LYS A 1 3471 ? 144.462 86.669  114.723 1.00 184.43 ? 3471 LYS A CB    1 
ATOM   14420 C  CG    . LYS A 1 3471 ? 143.984 88.103  114.887 1.00 183.87 ? 3471 LYS A CG    1 
ATOM   14421 C  CD    . LYS A 1 3471 ? 145.057 89.093  114.460 1.00 184.80 ? 3471 LYS A CD    1 
ATOM   14422 C  CE    . LYS A 1 3471 ? 144.454 90.275  113.720 1.00 185.07 ? 3471 LYS A CE    1 
ATOM   14423 N  NZ    . LYS A 1 3471 ? 145.500 91.217  113.231 1.00 184.37 ? 3471 LYS A NZ    1 
ATOM   14424 N  N     . VAL A 1 3472 ? 145.288 84.894  117.257 1.00 186.05 ? 3472 VAL A N     1 
ATOM   14425 C  CA    . VAL A 1 3472 ? 145.115 84.558  118.669 1.00 184.97 ? 3472 VAL A CA    1 
ATOM   14426 C  C     . VAL A 1 3472 ? 146.434 84.696  119.419 1.00 184.81 ? 3472 VAL A C     1 
ATOM   14427 O  O     . VAL A 1 3472 ? 146.477 85.219  120.540 1.00 185.42 ? 3472 VAL A O     1 
ATOM   14428 C  CB    . VAL A 1 3472 ? 144.524 83.142  118.809 1.00 184.75 ? 3472 VAL A CB    1 
ATOM   14429 C  CG1   . VAL A 1 3472 ? 144.771 82.590  120.206 1.00 183.75 ? 3472 VAL A CG1   1 
ATOM   14430 C  CG2   . VAL A 1 3472 ? 143.035 83.157  118.496 1.00 185.40 ? 3472 VAL A CG2   1 
ATOM   14431 N  N     . ASN A 1 3473 ? 147.529 84.221  118.821 1.00 179.34 ? 3473 ASN A N     1 
ATOM   14432 C  CA    . ASN A 1 3473 ? 148.837 84.358  119.457 1.00 178.77 ? 3473 ASN A CA    1 
ATOM   14433 C  C     . ASN A 1 3473 ? 149.224 85.824  119.613 1.00 177.86 ? 3473 ASN A C     1 
ATOM   14434 O  O     . ASN A 1 3473 ? 149.741 86.232  120.663 1.00 177.63 ? 3473 ASN A O     1 
ATOM   14435 C  CB    . ASN A 1 3473 ? 149.895 83.606  118.650 1.00 178.12 ? 3473 ASN A CB    1 
ATOM   14436 C  CG    . ASN A 1 3473 ? 150.840 82.810  119.527 1.00 177.52 ? 3473 ASN A CG    1 
ATOM   14437 O  OD1   . ASN A 1 3473 ? 151.156 83.215  120.646 1.00 177.78 ? 3473 ASN A OD1   1 
ATOM   14438 N  ND2   . ASN A 1 3473 ? 151.299 81.671  119.022 1.00 177.06 ? 3473 ASN A ND2   1 
ATOM   14439 N  N     . ARG A 1 3474 ? 148.977 86.633  118.579 1.00 169.44 ? 3474 ARG A N     1 
ATOM   14440 C  CA    . ARG A 1 3474 ? 149.267 88.060  118.678 1.00 168.98 ? 3474 ARG A CA    1 
ATOM   14441 C  C     . ARG A 1 3474 ? 148.422 88.718  119.762 1.00 170.01 ? 3474 ARG A C     1 
ATOM   14442 O  O     . ARG A 1 3474 ? 148.904 89.590  120.496 1.00 169.37 ? 3474 ARG A O     1 
ATOM   14443 C  CB    . ARG A 1 3474 ? 149.034 88.736  117.328 1.00 168.17 ? 3474 ARG A CB    1 
ATOM   14444 C  CG    . ARG A 1 3474 ? 149.647 90.120  117.212 1.00 167.75 ? 3474 ARG A CG    1 
ATOM   14445 C  CD    . ARG A 1 3474 ? 149.808 90.523  115.756 1.00 168.19 ? 3474 ARG A CD    1 
ATOM   14446 N  NE    . ARG A 1 3474 ? 150.620 91.724  115.605 1.00 168.87 ? 3474 ARG A NE    1 
ATOM   14447 C  CZ    . ARG A 1 3474 ? 150.199 92.844  115.034 1.00 167.97 ? 3474 ARG A CZ    1 
ATOM   14448 N  NH1   . ARG A 1 3474 ? 148.972 92.954  114.552 1.00 167.75 ? 3474 ARG A NH1   1 
ATOM   14449 N  NH2   . ARG A 1 3474 ? 151.029 93.879  114.946 1.00 167.25 ? 3474 ARG A NH2   1 
ATOM   14450 N  N     . SER A 1 3475 ? 147.157 88.310  119.878 1.00 176.90 ? 3475 SER A N     1 
ATOM   14451 C  CA    . SER A 1 3475 ? 146.285 88.849  120.916 1.00 175.75 ? 3475 SER A CA    1 
ATOM   14452 C  C     . SER A 1 3475 ? 146.780 88.475  122.307 1.00 175.10 ? 3475 SER A C     1 
ATOM   14453 O  O     . SER A 1 3475 ? 146.742 89.298  123.228 1.00 174.50 ? 3475 SER A O     1 
ATOM   14454 C  CB    . SER A 1 3475 ? 144.860 88.343  120.704 1.00 176.64 ? 3475 SER A CB    1 
ATOM   14455 O  OG    . SER A 1 3475 ? 144.415 88.605  119.386 1.00 177.64 ? 3475 SER A OG    1 
ATOM   14456 N  N     . THR A 1 3476 ? 147.229 87.230  122.481 1.00 172.51 ? 3476 THR A N     1 
ATOM   14457 C  CA    . THR A 1 3476 ? 147.771 86.816  123.771 1.00 171.40 ? 3476 THR A CA    1 
ATOM   14458 C  C     . THR A 1 3476 ? 149.022 87.611  124.117 1.00 172.59 ? 3476 THR A C     1 
ATOM   14459 O  O     . THR A 1 3476 ? 149.207 88.023  125.269 1.00 172.46 ? 3476 THR A O     1 
ATOM   14460 C  CB    . THR A 1 3476 ? 148.078 85.318  123.766 1.00 171.65 ? 3476 THR A CB    1 
ATOM   14461 O  OG1   . THR A 1 3476 ? 148.903 85.000  122.639 1.00 172.87 ? 3476 THR A OG1   1 
ATOM   14462 C  CG2   . THR A 1 3476 ? 146.791 84.508  123.696 1.00 171.29 ? 3476 THR A CG2   1 
ATOM   14463 N  N     . ALA A 1 3477 ? 149.894 87.836  123.131 1.00 171.70 ? 3477 ALA A N     1 
ATOM   14464 C  CA    . ALA A 1 3477 ? 151.082 88.650  123.371 1.00 170.42 ? 3477 ALA A CA    1 
ATOM   14465 C  C     . ALA A 1 3477 ? 150.703 90.074  123.762 1.00 170.26 ? 3477 ALA A C     1 
ATOM   14466 O  O     . ALA A 1 3477 ? 151.289 90.651  124.687 1.00 168.45 ? 3477 ALA A O     1 
ATOM   14467 C  CB    . ALA A 1 3477 ? 151.979 88.650  122.133 1.00 169.07 ? 3477 ALA A CB    1 
ATOM   14468 N  N     . LEU A 1 3478 ? 149.711 90.652  123.076 1.00 166.16 ? 3478 LEU A N     1 
ATOM   14469 C  CA    . LEU A 1 3478 ? 149.257 91.998  123.413 1.00 164.28 ? 3478 LEU A CA    1 
ATOM   14470 C  C     . LEU A 1 3478 ? 148.699 92.057  124.831 1.00 163.89 ? 3478 LEU A C     1 
ATOM   14471 O  O     . LEU A 1 3478 ? 148.999 92.991  125.584 1.00 163.98 ? 3478 LEU A O     1 
ATOM   14472 C  CB    . LEU A 1 3478 ? 148.204 92.463  122.406 1.00 164.25 ? 3478 LEU A CB    1 
ATOM   14473 C  CG    . LEU A 1 3478 ? 147.966 93.970  122.268 1.00 164.53 ? 3478 LEU A CG    1 
ATOM   14474 C  CD1   . LEU A 1 3478 ? 149.279 94.742  122.249 1.00 165.22 ? 3478 LEU A CD1   1 
ATOM   14475 C  CD2   . LEU A 1 3478 ? 147.133 94.278  121.030 1.00 164.44 ? 3478 LEU A CD2   1 
ATOM   14476 N  N     . LEU A 1 3479 ? 147.886 91.069  125.214 1.00 162.85 ? 3479 LEU A N     1 
ATOM   14477 C  CA    . LEU A 1 3479 ? 147.306 91.071  126.554 1.00 162.01 ? 3479 LEU A CA    1 
ATOM   14478 C  C     . LEU A 1 3479 ? 148.383 90.914  127.620 1.00 163.14 ? 3479 LEU A C     1 
ATOM   14479 O  O     . LEU A 1 3479 ? 148.362 91.604  128.647 1.00 163.00 ? 3479 LEU A O     1 
ATOM   14480 C  CB    . LEU A 1 3479 ? 146.263 89.961  126.684 1.00 162.18 ? 3479 LEU A CB    1 
ATOM   14481 C  CG    . LEU A 1 3479 ? 145.752 89.751  128.112 1.00 162.76 ? 3479 LEU A CG    1 
ATOM   14482 C  CD1   . LEU A 1 3479 ? 145.033 90.996  128.616 1.00 162.82 ? 3479 LEU A CD1   1 
ATOM   14483 C  CD2   . LEU A 1 3479 ? 144.861 88.521  128.218 1.00 161.61 ? 3479 LEU A CD2   1 
ATOM   14484 N  N     . LYS A 1 3480 ? 149.342 90.013  127.391 1.00 164.17 ? 3480 LYS A N     1 
ATOM   14485 C  CA    . LYS A 1 3480 ? 150.439 89.844  128.335 1.00 163.73 ? 3480 LYS A CA    1 
ATOM   14486 C  C     . LYS A 1 3480 ? 151.291 91.097  128.451 1.00 163.88 ? 3480 LYS A C     1 
ATOM   14487 O  O     . LYS A 1 3480 ? 151.793 91.392  129.541 1.00 162.70 ? 3480 LYS A O     1 
ATOM   14488 C  CB    . LYS A 1 3480 ? 151.314 88.658  127.925 1.00 162.72 ? 3480 LYS A CB    1 
ATOM   14489 C  CG    . LYS A 1 3480 ? 150.777 87.313  128.375 1.00 163.04 ? 3480 LYS A CG    1 
ATOM   14490 C  CD    . LYS A 1 3480 ? 150.640 87.261  129.887 1.00 162.75 ? 3480 LYS A CD    1 
ATOM   14491 C  CE    . LYS A 1 3480 ? 149.358 86.562  130.303 1.00 162.19 ? 3480 LYS A CE    1 
ATOM   14492 N  NZ    . LYS A 1 3480 ? 148.901 87.008  131.648 1.00 162.09 ? 3480 LYS A NZ    1 
ATOM   14493 N  N     . SER A 1 3481 ? 151.464 91.838  127.355 1.00 161.54 ? 3481 SER A N     1 
ATOM   14494 C  CA    . SER A 1 3481 ? 152.187 93.101  127.427 1.00 161.11 ? 3481 SER A CA    1 
ATOM   14495 C  C     . SER A 1 3481 ? 151.392 94.160  128.183 1.00 160.59 ? 3481 SER A C     1 
ATOM   14496 O  O     . SER A 1 3481 ? 151.970 94.957  128.930 1.00 158.28 ? 3481 SER A O     1 
ATOM   14497 C  CB    . SER A 1 3481 ? 152.525 93.592  126.019 1.00 159.44 ? 3481 SER A CB    1 
ATOM   14498 O  OG    . SER A 1 3481 ? 153.443 94.670  126.063 1.00 158.79 ? 3481 SER A OG    1 
ATOM   14499 N  N     . LEU A 1 3482 ? 150.072 94.179  128.010 1.00 159.29 ? 3482 LEU A N     1 
ATOM   14500 C  CA    . LEU A 1 3482 ? 149.224 95.194  128.625 1.00 156.83 ? 3482 LEU A CA    1 
ATOM   14501 C  C     . LEU A 1 3482 ? 148.715 94.801  130.005 1.00 156.48 ? 3482 LEU A C     1 
ATOM   14502 O  O     . LEU A 1 3482 ? 147.914 95.542  130.584 1.00 155.89 ? 3482 LEU A O     1 
ATOM   14503 C  CB    . LEU A 1 3482 ? 148.030 95.507  127.717 1.00 155.99 ? 3482 LEU A CB    1 
ATOM   14504 C  CG    . LEU A 1 3482 ? 148.339 96.132  126.357 1.00 155.89 ? 3482 LEU A CG    1 
ATOM   14505 C  CD1   . LEU A 1 3482 ? 147.063 96.648  125.714 1.00 155.82 ? 3482 LEU A CD1   1 
ATOM   14506 C  CD2   . LEU A 1 3482 ? 149.366 97.243  126.497 1.00 154.62 ? 3482 LEU A CD2   1 
ATOM   14507 N  N     . SER A 1 3483 ? 149.146 93.656  130.540 1.00 155.14 ? 3483 SER A N     1 
ATOM   14508 C  CA    . SER A 1 3483 ? 148.673 93.233  131.854 1.00 154.54 ? 3483 SER A CA    1 
ATOM   14509 C  C     . SER A 1 3483 ? 149.047 94.239  132.937 1.00 155.60 ? 3483 SER A C     1 
ATOM   14510 O  O     . SER A 1 3483 ? 148.219 94.575  133.792 1.00 155.79 ? 3483 SER A O     1 
ATOM   14511 C  CB    . SER A 1 3483 ? 149.237 91.854  132.193 1.00 154.08 ? 3483 SER A CB    1 
ATOM   14512 O  OG    . SER A 1 3483 ? 149.101 91.579  133.577 1.00 155.06 ? 3483 SER A OG    1 
ATOM   14513 N  N     . ALA A 1 3484 ? 150.289 94.730  132.918 1.00 150.14 ? 3484 ALA A N     1 
ATOM   14514 C  CA    . ALA A 1 3484 ? 150.730 95.678  133.939 1.00 149.44 ? 3484 ALA A CA    1 
ATOM   14515 C  C     . ALA A 1 3484 ? 149.959 96.989  133.856 1.00 150.40 ? 3484 ALA A C     1 
ATOM   14516 O  O     . ALA A 1 3484 ? 149.576 97.561  134.886 1.00 148.85 ? 3484 ALA A O     1 
ATOM   14517 C  CB    . ALA A 1 3484 ? 152.231 95.933  133.804 1.00 147.99 ? 3484 ALA A CB    1 
ATOM   14518 N  N     . GLU A 1 3485 ? 149.733 97.489  132.637 1.00 152.21 ? 3485 GLU A N     1 
ATOM   14519 C  CA    . GLU A 1 3485 ? 148.973 98.723  132.477 1.00 150.02 ? 3485 GLU A CA    1 
ATOM   14520 C  C     . GLU A 1 3485 ? 147.577 98.579  133.058 1.00 150.90 ? 3485 GLU A C     1 
ATOM   14521 O  O     . GLU A 1 3485 ? 147.117 99.447  133.808 1.00 152.01 ? 3485 GLU A O     1 
ATOM   14522 C  CB    . GLU A 1 3485 ? 148.888 99.100  130.999 1.00 149.68 ? 3485 GLU A CB    1 
ATOM   14523 C  CG    . GLU A 1 3485 ? 150.018 99.977  130.501 1.00 150.58 ? 3485 GLU A CG    1 
ATOM   14524 C  CD    . GLU A 1 3485 ? 151.319 99.223  130.359 1.00 152.31 ? 3485 GLU A CD    1 
ATOM   14525 O  OE1   . GLU A 1 3485 ? 151.289 97.976  130.386 1.00 154.09 ? 3485 GLU A OE1   1 
ATOM   14526 O  OE2   . GLU A 1 3485 ? 152.372 99.879  130.212 1.00 150.87 ? 3485 GLU A OE2   1 
ATOM   14527 N  N     . ARG A 1 3486 ? 146.905 97.470  132.746 1.00 150.89 ? 3486 ARG A N     1 
ATOM   14528 C  CA    . ARG A 1 3486 ? 145.575 97.223  133.287 1.00 150.49 ? 3486 ARG A CA    1 
ATOM   14529 C  C     . ARG A 1 3486 ? 145.599 97.173  134.808 1.00 150.16 ? 3486 ARG A C     1 
ATOM   14530 O  O     . ARG A 1 3486 ? 144.707 97.716  135.466 1.00 153.21 ? 3486 ARG A O     1 
ATOM   14531 C  CB    . ARG A 1 3486 ? 145.021 95.915  132.725 1.00 151.12 ? 3486 ARG A CB    1 
ATOM   14532 C  CG    . ARG A 1 3486 ? 143.639 95.564  133.243 1.00 150.72 ? 3486 ARG A CG    1 
ATOM   14533 C  CD    . ARG A 1 3486 ? 143.176 94.210  132.729 1.00 149.63 ? 3486 ARG A CD    1 
ATOM   14534 N  NE    . ARG A 1 3486 ? 144.208 93.189  132.870 1.00 151.83 ? 3486 ARG A NE    1 
ATOM   14535 C  CZ    . ARG A 1 3486 ? 144.490 92.560  134.004 1.00 150.73 ? 3486 ARG A CZ    1 
ATOM   14536 N  NH1   . ARG A 1 3486 ? 143.816 92.804  135.116 1.00 149.47 ? 3486 ARG A NH1   1 
ATOM   14537 N  NH2   . ARG A 1 3486 ? 145.474 91.666  134.023 1.00 150.51 ? 3486 ARG A NH2   1 
ATOM   14538 N  N     . GLU A 1 3487 ? 146.614 96.529  135.387 1.00 147.03 ? 3487 GLU A N     1 
ATOM   14539 C  CA    . GLU A 1 3487 ? 146.670 96.395  136.840 1.00 148.48 ? 3487 GLU A CA    1 
ATOM   14540 C  C     . GLU A 1 3487 ? 146.850 97.752  137.515 1.00 150.27 ? 3487 GLU A C     1 
ATOM   14541 O  O     . GLU A 1 3487 ? 146.111 98.100  138.448 1.00 150.86 ? 3487 GLU A O     1 
ATOM   14542 C  CB    . GLU A 1 3487 ? 147.800 95.441  137.231 1.00 149.18 ? 3487 GLU A CB    1 
ATOM   14543 C  CG    . GLU A 1 3487 ? 147.418 93.964  137.184 1.00 149.95 ? 3487 GLU A CG    1 
ATOM   14544 C  CD    . GLU A 1 3487 ? 147.037 93.400  138.540 1.00 151.02 ? 3487 GLU A CD    1 
ATOM   14545 O  OE1   . GLU A 1 3487 ? 147.022 92.159  138.688 1.00 150.55 ? 3487 GLU A OE1   1 
ATOM   14546 O  OE2   . GLU A 1 3487 ? 146.754 94.195  139.458 1.00 151.11 ? 3487 GLU A OE2   1 
ATOM   14547 N  N     . ARG A 1 3488 ? 147.831 98.536  137.058 1.00 149.58 ? 3488 ARG A N     1 
ATOM   14548 C  CA    . ARG A 1 3488 ? 148.050 99.839  137.680 1.00 149.78 ? 3488 ARG A CA    1 
ATOM   14549 C  C     . ARG A 1 3488 ? 146.858 100.761 137.450 1.00 149.61 ? 3488 ARG A C     1 
ATOM   14550 O  O     . ARG A 1 3488 ? 146.491 101.552 138.331 1.00 151.09 ? 3488 ARG A O     1 
ATOM   14551 C  CB    . ARG A 1 3488 ? 149.343 100.471 137.165 1.00 147.92 ? 3488 ARG A CB    1 
ATOM   14552 C  CG    . ARG A 1 3488 ? 149.296 101.984 137.082 1.00 147.33 ? 3488 ARG A CG    1 
ATOM   14553 C  CD    . ARG A 1 3488 ? 150.521 102.533 136.398 1.00 147.82 ? 3488 ARG A CD    1 
ATOM   14554 N  NE    . ARG A 1 3488 ? 150.949 101.755 135.243 1.00 150.25 ? 3488 ARG A NE    1 
ATOM   14555 C  CZ    . ARG A 1 3488 ? 151.582 102.282 134.205 1.00 150.58 ? 3488 ARG A CZ    1 
ATOM   14556 N  NH1   . ARG A 1 3488 ? 151.901 103.564 134.173 1.00 149.48 ? 3488 ARG A NH1   1 
ATOM   14557 N  NH2   . ARG A 1 3488 ? 151.912 101.503 133.179 1.00 149.14 ? 3488 ARG A NH2   1 
ATOM   14558 N  N     . TRP A 1 3489 ? 146.231 100.666 136.277 1.00 141.24 ? 3489 TRP A N     1 
ATOM   14559 C  CA    . TRP A 1 3489 ? 145.037 101.458 136.016 1.00 139.99 ? 3489 TRP A CA    1 
ATOM   14560 C  C     . TRP A 1 3489 ? 143.900 101.052 136.945 1.00 140.45 ? 3489 TRP A C     1 
ATOM   14561 O  O     . TRP A 1 3489 ? 143.120 101.902 137.387 1.00 140.82 ? 3489 TRP A O     1 
ATOM   14562 C  CB    . TRP A 1 3489 ? 144.632 101.303 134.554 1.00 138.77 ? 3489 TRP A CB    1 
ATOM   14563 C  CG    . TRP A 1 3489 ? 145.591 101.963 133.614 1.00 139.13 ? 3489 TRP A CG    1 
ATOM   14564 C  CD1   . TRP A 1 3489 ? 146.589 102.835 133.937 1.00 138.21 ? 3489 TRP A CD1   1 
ATOM   14565 C  CD2   . TRP A 1 3489 ? 145.653 101.792 132.195 1.00 142.53 ? 3489 TRP A CD2   1 
ATOM   14566 N  NE1   . TRP A 1 3489 ? 147.258 103.229 132.806 1.00 139.54 ? 3489 TRP A NE1   1 
ATOM   14567 C  CE2   . TRP A 1 3489 ? 146.707 102.598 131.722 1.00 142.10 ? 3489 TRP A CE2   1 
ATOM   14568 C  CE3   . TRP A 1 3489 ? 144.919 101.035 131.278 1.00 142.68 ? 3489 TRP A CE3   1 
ATOM   14569 C  CZ2   . TRP A 1 3489 ? 147.047 102.666 130.374 1.00 141.59 ? 3489 TRP A CZ2   1 
ATOM   14570 C  CZ3   . TRP A 1 3489 ? 145.257 101.106 129.941 1.00 142.78 ? 3489 TRP A CZ3   1 
ATOM   14571 C  CH2   . TRP A 1 3489 ? 146.310 101.915 129.501 1.00 141.23 ? 3489 TRP A CH2   1 
ATOM   14572 N  N     . GLU A 1 3490 ? 143.795 99.757  137.257 1.00 144.66 ? 3490 GLU A N     1 
ATOM   14573 C  CA    . GLU A 1 3490 ? 142.792 99.304  138.214 1.00 144.65 ? 3490 GLU A CA    1 
ATOM   14574 C  C     . GLU A 1 3490 ? 143.042 99.888  139.598 1.00 144.61 ? 3490 GLU A C     1 
ATOM   14575 O  O     . GLU A 1 3490 ? 142.104 100.348 140.260 1.00 147.22 ? 3490 GLU A O     1 
ATOM   14576 C  CB    . GLU A 1 3490 ? 142.766 97.776  138.270 1.00 146.06 ? 3490 GLU A CB    1 
ATOM   14577 C  CG    . GLU A 1 3490 ? 141.880 97.126  137.216 1.00 146.74 ? 3490 GLU A CG    1 
ATOM   14578 C  CD    . GLU A 1 3490 ? 142.410 95.784  136.751 1.00 147.72 ? 3490 GLU A CD    1 
ATOM   14579 O  OE1   . GLU A 1 3490 ? 143.532 95.415  137.157 1.00 148.06 ? 3490 GLU A OE1   1 
ATOM   14580 O  OE2   . GLU A 1 3490 ? 141.705 95.097  135.982 1.00 147.53 ? 3490 GLU A OE2   1 
ATOM   14581 N  N     . LYS A 1 3491 ? 144.301 99.886  140.054 1.00 138.42 ? 3491 LYS A N     1 
ATOM   14582 C  CA    . LYS A 1 3491 ? 144.580 100.509 141.351 1.00 138.70 ? 3491 LYS A CA    1 
ATOM   14583 C  C     . LYS A 1 3491 ? 144.227 101.993 141.348 1.00 139.60 ? 3491 LYS A C     1 
ATOM   14584 O  O     . LYS A 1 3491 ? 143.605 102.492 142.296 1.00 138.02 ? 3491 LYS A O     1 
ATOM   14585 C  CB    . LYS A 1 3491 ? 146.041 100.330 141.778 1.00 139.04 ? 3491 LYS A CB    1 
ATOM   14586 C  CG    . LYS A 1 3491 ? 146.834 99.239  141.111 1.00 140.96 ? 3491 LYS A CG    1 
ATOM   14587 C  CD    . LYS A 1 3491 ? 146.833 97.998  141.991 1.00 141.77 ? 3491 LYS A CD    1 
ATOM   14588 C  CE    . LYS A 1 3491 ? 147.692 96.894  141.410 1.00 140.13 ? 3491 LYS A CE    1 
ATOM   14589 N  NZ    . LYS A 1 3491 ? 147.045 96.256  140.241 1.00 140.39 ? 3491 LYS A NZ    1 
ATOM   14590 N  N     . THR A 1 3492 ? 144.617 102.716 140.297 1.00 139.19 ? 3492 THR A N     1 
ATOM   14591 C  CA    . THR A 1 3492 ? 144.342 104.150 140.261 1.00 136.64 ? 3492 THR A CA    1 
ATOM   14592 C  C     . THR A 1 3492 ? 142.842 104.431 140.225 1.00 136.15 ? 3492 THR A C     1 
ATOM   14593 O  O     . THR A 1 3492 ? 142.356 105.333 140.920 1.00 136.64 ? 3492 THR A O     1 
ATOM   14594 C  CB    . THR A 1 3492 ? 145.043 104.788 139.064 1.00 135.48 ? 3492 THR A CB    1 
ATOM   14595 O  OG1   . THR A 1 3492 ? 144.765 104.021 137.888 1.00 137.74 ? 3492 THR A OG1   1 
ATOM   14596 C  CG2   . THR A 1 3492 ? 146.548 104.837 139.292 1.00 133.04 ? 3492 THR A CG2   1 
ATOM   14597 N  N     . SER A 1 3493 ? 142.090 103.661 139.434 1.00 132.03 ? 3493 SER A N     1 
ATOM   14598 C  CA    . SER A 1 3493 ? 140.641 103.823 139.401 1.00 131.45 ? 3493 SER A CA    1 
ATOM   14599 C  C     . SER A 1 3493 ? 140.004 103.473 140.738 1.00 133.08 ? 3493 SER A C     1 
ATOM   14600 O  O     . SER A 1 3493 ? 138.978 104.057 141.104 1.00 132.18 ? 3493 SER A O     1 
ATOM   14601 C  CB    . SER A 1 3493 ? 140.043 102.965 138.286 1.00 131.64 ? 3493 SER A CB    1 
ATOM   14602 O  OG    . SER A 1 3493 ? 138.627 102.969 138.342 1.00 131.79 ? 3493 SER A OG    1 
ATOM   14603 N  N     . GLU A 1 3494 ? 140.584 102.521 141.475 1.00 140.74 ? 3494 GLU A N     1 
ATOM   14604 C  CA    . GLU A 1 3494 ? 140.060 102.209 142.801 1.00 140.61 ? 3494 GLU A CA    1 
ATOM   14605 C  C     . GLU A 1 3494 ? 140.292 103.365 143.766 1.00 142.03 ? 3494 GLU A C     1 
ATOM   14606 O  O     . GLU A 1 3494 ? 139.398 103.721 144.542 1.00 141.27 ? 3494 GLU A O     1 
ATOM   14607 C  CB    . GLU A 1 3494 ? 140.695 100.917 143.325 1.00 139.01 ? 3494 GLU A CB    1 
ATOM   14608 C  CG    . GLU A 1 3494 ? 139.966 100.271 144.505 1.00 138.99 ? 3494 GLU A CG    1 
ATOM   14609 C  CD    . GLU A 1 3494 ? 140.208 100.968 145.835 1.00 140.70 ? 3494 GLU A CD    1 
ATOM   14610 O  OE1   . GLU A 1 3494 ? 141.196 101.721 145.954 1.00 141.00 ? 3494 GLU A OE1   1 
ATOM   14611 O  OE2   . GLU A 1 3494 ? 139.399 100.762 146.765 1.00 142.12 ? 3494 GLU A OE2   1 
ATOM   14612 N  N     . THR A 1 3495 ? 141.484 103.964 143.735 1.00 137.69 ? 3495 THR A N     1 
ATOM   14613 C  CA    . THR A 1 3495 ? 141.754 105.101 144.611 1.00 136.23 ? 3495 THR A CA    1 
ATOM   14614 C  C     . THR A 1 3495 ? 141.192 106.414 144.081 1.00 135.72 ? 3495 THR A C     1 
ATOM   14615 O  O     . THR A 1 3495 ? 141.399 107.453 144.717 1.00 135.97 ? 3495 THR A O     1 
ATOM   14616 C  CB    . THR A 1 3495 ? 143.258 105.268 144.867 1.00 135.07 ? 3495 THR A CB    1 
ATOM   14617 O  OG1   . THR A 1 3495 ? 143.838 106.095 143.849 1.00 135.32 ? 3495 THR A OG1   1 
ATOM   14618 C  CG2   . THR A 1 3495 ? 143.963 103.925 144.931 1.00 134.14 ? 3495 THR A CG2   1 
ATOM   14619 N  N     . PHE A 1 3496 ? 140.502 106.394 142.936 1.00 129.46 ? 3496 PHE A N     1 
ATOM   14620 C  CA    . PHE A 1 3496 ? 139.863 107.605 142.426 1.00 127.99 ? 3496 PHE A CA    1 
ATOM   14621 C  C     . PHE A 1 3496 ? 138.924 108.229 143.454 1.00 128.51 ? 3496 PHE A C     1 
ATOM   14622 O  O     . PHE A 1 3496 ? 138.874 109.457 143.594 1.00 128.74 ? 3496 PHE A O     1 
ATOM   14623 C  CB    . PHE A 1 3496 ? 139.103 107.283 141.137 1.00 129.13 ? 3496 PHE A CB    1 
ATOM   14624 C  CG    . PHE A 1 3496 ? 137.943 108.199 140.867 1.00 129.31 ? 3496 PHE A CG    1 
ATOM   14625 C  CD1   . PHE A 1 3496 ? 138.151 109.495 140.427 1.00 128.60 ? 3496 PHE A CD1   1 
ATOM   14626 C  CD2   . PHE A 1 3496 ? 136.642 107.761 141.051 1.00 128.37 ? 3496 PHE A CD2   1 
ATOM   14627 C  CE1   . PHE A 1 3496 ? 137.084 110.336 140.176 1.00 126.39 ? 3496 PHE A CE1   1 
ATOM   14628 C  CE2   . PHE A 1 3496 ? 135.572 108.598 140.804 1.00 127.60 ? 3496 PHE A CE2   1 
ATOM   14629 C  CZ    . PHE A 1 3496 ? 135.793 109.887 140.366 1.00 127.48 ? 3496 PHE A CZ    1 
ATOM   14630 N  N     . LYS A 1 3497 ? 138.167 107.401 144.179 1.00 122.17 ? 3497 LYS A N     1 
ATOM   14631 C  CA    . LYS A 1 3497 ? 137.229 107.930 145.167 1.00 122.91 ? 3497 LYS A CA    1 
ATOM   14632 C  C     . LYS A 1 3497 ? 137.956 108.616 146.318 1.00 122.34 ? 3497 LYS A C     1 
ATOM   14633 O  O     . LYS A 1 3497 ? 137.497 109.648 146.825 1.00 119.67 ? 3497 LYS A O     1 
ATOM   14634 C  CB    . LYS A 1 3497 ? 136.333 106.809 145.693 1.00 120.83 ? 3497 LYS A CB    1 
ATOM   14635 C  CG    . LYS A 1 3497 ? 135.096 106.558 144.847 1.00 122.31 ? 3497 LYS A CG    1 
ATOM   14636 C  CD    . LYS A 1 3497 ? 134.379 107.859 144.524 1.00 122.18 ? 3497 LYS A CD    1 
ATOM   14637 C  CE    . LYS A 1 3497 ? 132.936 107.610 144.118 1.00 120.94 ? 3497 LYS A CE    1 
ATOM   14638 N  NZ    . LYS A 1 3497 ? 132.822 106.529 143.101 1.00 120.58 ? 3497 LYS A NZ    1 
ATOM   14639 N  N     . ASN A 1 3498 ? 139.085 108.050 146.752 1.00 120.77 ? 3498 ASN A N     1 
ATOM   14640 C  CA    . ASN A 1 3498 ? 139.841 108.650 147.846 1.00 118.57 ? 3498 ASN A CA    1 
ATOM   14641 C  C     . ASN A 1 3498 ? 140.316 110.050 147.483 1.00 119.47 ? 3498 ASN A C     1 
ATOM   14642 O  O     . ASN A 1 3498 ? 140.210 110.980 148.292 1.00 120.88 ? 3498 ASN A O     1 
ATOM   14643 C  CB    . ASN A 1 3498 ? 141.026 107.759 148.215 1.00 118.27 ? 3498 ASN A CB    1 
ATOM   14644 C  CG    . ASN A 1 3498 ? 141.632 108.122 149.555 1.00 121.09 ? 3498 ASN A CG    1 
ATOM   14645 O  OD1   . ASN A 1 3498 ? 142.640 108.825 149.624 1.00 122.04 ? 3498 ASN A OD1   1 
ATOM   14646 N  ND2   . ASN A 1 3498 ? 141.017 107.643 150.630 1.00 122.41 ? 3498 ASN A ND2   1 
ATOM   14647 N  N     . GLN A 1 3499 ? 140.833 110.223 146.264 1.00 119.53 ? 3499 GLN A N     1 
ATOM   14648 C  CA    . GLN A 1 3499 ? 141.261 111.547 145.827 1.00 118.10 ? 3499 GLN A CA    1 
ATOM   14649 C  C     . GLN A 1 3499 ? 140.091 112.521 145.798 1.00 118.49 ? 3499 GLN A C     1 
ATOM   14650 O  O     . GLN A 1 3499 ? 140.226 113.674 146.222 1.00 118.75 ? 3499 GLN A O     1 
ATOM   14651 C  CB    . GLN A 1 3499 ? 141.926 111.462 144.454 1.00 117.21 ? 3499 GLN A CB    1 
ATOM   14652 C  CG    . GLN A 1 3499 ? 143.326 110.871 144.471 1.00 120.38 ? 3499 GLN A CG    1 
ATOM   14653 C  CD    . GLN A 1 3499 ? 143.393 109.510 143.811 1.00 121.96 ? 3499 GLN A CD    1 
ATOM   14654 O  OE1   . GLN A 1 3499 ? 142.855 109.308 142.722 1.00 118.83 ? 3499 GLN A OE1   1 
ATOM   14655 N  NE2   . GLN A 1 3499 ? 144.055 108.565 144.468 1.00 121.43 ? 3499 GLN A NE2   1 
ATOM   14656 N  N     . MET A 1 3500 ? 138.931 112.076 145.306 1.00 115.24 ? 3500 MET A N     1 
ATOM   14657 C  CA    . MET A 1 3500 ? 137.757 112.944 145.286 1.00 114.67 ? 3500 MET A CA    1 
ATOM   14658 C  C     . MET A 1 3500 ? 137.354 113.381 146.686 1.00 113.87 ? 3500 MET A C     1 
ATOM   14659 O  O     . MET A 1 3500 ? 137.033 114.555 146.901 1.00 114.53 ? 3500 MET A O     1 
ATOM   14660 C  CB    . MET A 1 3500 ? 136.587 112.238 144.600 1.00 116.06 ? 3500 MET A CB    1 
ATOM   14661 C  CG    . MET A 1 3500 ? 136.655 112.241 143.086 1.00 120.13 ? 3500 MET A CG    1 
ATOM   14662 S  SD    . MET A 1 3500 ? 136.645 113.911 142.403 1.00 123.39 ? 3500 MET A SD    1 
ATOM   14663 C  CE    . MET A 1 3500 ? 134.918 114.089 141.961 1.00 115.19 ? 3500 MET A CE    1 
ATOM   14664 N  N     . SER A 1 3501 ? 137.361 112.459 147.650 1.00 111.94 ? 3501 SER A N     1 
ATOM   14665 C  CA    . SER A 1 3501 ? 136.993 112.827 149.013 1.00 112.74 ? 3501 SER A CA    1 
ATOM   14666 C  C     . SER A 1 3501 ? 138.055 113.709 149.658 1.00 111.70 ? 3501 SER A C     1 
ATOM   14667 O  O     . SER A 1 3501 ? 137.751 114.499 150.559 1.00 112.82 ? 3501 SER A O     1 
ATOM   14668 C  CB    . SER A 1 3501 ? 136.759 111.571 149.851 1.00 111.50 ? 3501 SER A CB    1 
ATOM   14669 O  OG    . SER A 1 3501 ? 137.981 110.912 150.133 1.00 114.25 ? 3501 SER A OG    1 
ATOM   14670 N  N     . THR A 1 3502 ? 139.303 113.591 149.211 1.00 103.88 ? 3502 THR A N     1 
ATOM   14671 C  CA    . THR A 1 3502 ? 140.429 114.263 149.845 1.00 104.87 ? 3502 THR A CA    1 
ATOM   14672 C  C     . THR A 1 3502 ? 140.739 115.631 149.230 1.00 103.42 ? 3502 THR A C     1 
ATOM   14673 O  O     . THR A 1 3502 ? 141.401 116.450 149.879 1.00 104.08 ? 3502 THR A O     1 
ATOM   14674 C  CB    . THR A 1 3502 ? 141.647 113.319 149.783 1.00 104.78 ? 3502 THR A CB    1 
ATOM   14675 O  OG1   . THR A 1 3502 ? 141.510 112.308 150.789 1.00 102.28 ? 3502 THR A OG1   1 
ATOM   14676 C  CG2   . THR A 1 3502 ? 142.956 114.036 150.020 1.00 102.77 ? 3502 THR A CG2   1 
ATOM   14677 N  N     . ILE A 1 3503 ? 140.200 115.929 148.042 1.00 94.69  ? 3503 ILE A N     1 
ATOM   14678 C  CA    . ILE A 1 3503 ? 140.596 117.125 147.295 1.00 93.14  ? 3503 ILE A CA    1 
ATOM   14679 C  C     . ILE A 1 3503 ? 140.440 118.389 148.136 1.00 92.70  ? 3503 ILE A C     1 
ATOM   14680 O  O     . ILE A 1 3503 ? 141.296 119.281 148.099 1.00 95.33  ? 3503 ILE A O     1 
ATOM   14681 C  CB    . ILE A 1 3503 ? 139.795 117.224 145.981 1.00 92.27  ? 3503 ILE A CB    1 
ATOM   14682 C  CG1   . ILE A 1 3503 ? 140.467 116.416 144.871 1.00 93.68  ? 3503 ILE A CG1   1 
ATOM   14683 C  CG2   . ILE A 1 3503 ? 139.628 118.669 145.545 1.00 90.20  ? 3503 ILE A CG2   1 
ATOM   14684 C  CD1   . ILE A 1 3503 ? 139.716 116.451 143.559 1.00 94.21  ? 3503 ILE A CD1   1 
ATOM   14685 N  N     . ALA A 1 3504 ? 139.354 118.487 148.907 1.00 82.28  ? 3504 ALA A N     1 
ATOM   14686 C  CA    . ALA A 1 3504 ? 139.073 119.721 149.638 1.00 77.44  ? 3504 ALA A CA    1 
ATOM   14687 C  C     . ALA A 1 3504 ? 140.207 120.076 150.594 1.00 80.14  ? 3504 ALA A C     1 
ATOM   14688 O  O     . ALA A 1 3504 ? 140.668 121.224 150.631 1.00 84.68  ? 3504 ALA A O     1 
ATOM   14689 C  CB    . ALA A 1 3504 ? 137.751 119.590 150.395 1.00 74.69  ? 3504 ALA A CB    1 
ATOM   14690 N  N     . GLY A 1 3505 ? 140.679 119.098 151.370 1.00 76.22  ? 3505 GLY A N     1 
ATOM   14691 C  CA    . GLY A 1 3505 ? 141.758 119.370 152.306 1.00 77.03  ? 3505 GLY A CA    1 
ATOM   14692 C  C     . GLY A 1 3505 ? 143.059 119.743 151.619 1.00 82.23  ? 3505 GLY A C     1 
ATOM   14693 O  O     . GLY A 1 3505 ? 143.730 120.700 152.020 1.00 85.77  ? 3505 GLY A O     1 
ATOM   14694 N  N     . ASP A 1 3506 ? 143.435 118.995 150.577 1.00 85.19  ? 3506 ASP A N     1 
ATOM   14695 C  CA    . ASP A 1 3506 ? 144.666 119.304 149.857 1.00 82.28  ? 3506 ASP A CA    1 
ATOM   14696 C  C     . ASP A 1 3506 ? 144.592 120.677 149.209 1.00 83.44  ? 3506 ASP A C     1 
ATOM   14697 O  O     . ASP A 1 3506 ? 145.563 121.441 149.245 1.00 90.63  ? 3506 ASP A O     1 
ATOM   14698 C  CB    . ASP A 1 3506 ? 144.952 118.243 148.795 1.00 87.47  ? 3506 ASP A CB    1 
ATOM   14699 C  CG    . ASP A 1 3506 ? 145.038 116.848 149.366 1.00 94.04  ? 3506 ASP A CG    1 
ATOM   14700 O  OD1   . ASP A 1 3506 ? 144.947 115.887 148.575 1.00 90.51  ? 3506 ASP A OD1   1 
ATOM   14701 O  OD2   . ASP A 1 3506 ? 145.193 116.710 150.597 1.00 95.69  ? 3506 ASP A OD2   1 
ATOM   14702 N  N     . CYS A 1 3507 ? 143.453 121.003 148.596 1.00 72.48  ? 3507 CYS A N     1 
ATOM   14703 C  CA    . CYS A 1 3507 ? 143.307 122.311 147.971 1.00 70.64  ? 3507 CYS A CA    1 
ATOM   14704 C  C     . CYS A 1 3507 ? 143.368 123.431 148.998 1.00 77.97  ? 3507 CYS A C     1 
ATOM   14705 O  O     . CYS A 1 3507 ? 144.008 124.457 148.749 1.00 82.45  ? 3507 CYS A O     1 
ATOM   14706 C  CB    . CYS A 1 3507 ? 142.003 122.374 147.181 1.00 71.76  ? 3507 CYS A CB    1 
ATOM   14707 S  SG    . CYS A 1 3507 ? 142.013 121.351 145.697 1.00 90.01  ? 3507 CYS A SG    1 
ATOM   14708 N  N     . LEU A 1 3508 ? 142.728 123.251 150.157 1.00 70.26  ? 3508 LEU A N     1 
ATOM   14709 C  CA    . LEU A 1 3508 ? 142.803 124.264 151.204 1.00 68.76  ? 3508 LEU A CA    1 
ATOM   14710 C  C     . LEU A 1 3508 ? 144.241 124.463 151.668 1.00 71.79  ? 3508 LEU A C     1 
ATOM   14711 O  O     . LEU A 1 3508 ? 144.715 125.600 151.795 1.00 74.97  ? 3508 LEU A O     1 
ATOM   14712 C  CB    . LEU A 1 3508 ? 141.903 123.870 152.376 1.00 66.84  ? 3508 LEU A CB    1 
ATOM   14713 C  CG    . LEU A 1 3508 ? 141.557 124.936 153.419 1.00 63.35  ? 3508 LEU A CG    1 
ATOM   14714 C  CD1   . LEU A 1 3508 ? 140.189 124.656 154.009 1.00 68.78  ? 3508 LEU A CD1   1 
ATOM   14715 C  CD2   . LEU A 1 3508 ? 142.598 124.993 154.525 1.00 64.61  ? 3508 LEU A CD2   1 
ATOM   14716 N  N     . LEU A 1 3509 ? 144.957 123.362 151.914 1.00 66.33  ? 3509 LEU A N     1 
ATOM   14717 C  CA    . LEU A 1 3509 ? 146.338 123.467 152.376 1.00 61.21  ? 3509 LEU A CA    1 
ATOM   14718 C  C     . LEU A 1 3509 ? 147.222 124.146 151.340 1.00 69.08  ? 3509 LEU A C     1 
ATOM   14719 O  O     . LEU A 1 3509 ? 148.019 125.030 151.676 1.00 78.32  ? 3509 LEU A O     1 
ATOM   14720 C  CB    . LEU A 1 3509 ? 146.885 122.081 152.713 1.00 66.25  ? 3509 LEU A CB    1 
ATOM   14721 C  CG    . LEU A 1 3509 ? 146.356 121.440 153.992 1.00 65.00  ? 3509 LEU A CG    1 
ATOM   14722 C  CD1   . LEU A 1 3509 ? 147.057 120.121 154.250 1.00 73.47  ? 3509 LEU A CD1   1 
ATOM   14723 C  CD2   . LEU A 1 3509 ? 146.547 122.383 155.157 1.00 62.38  ? 3509 LEU A CD2   1 
ATOM   14724 N  N     . SER A 1 3510 ? 147.096 123.746 150.073 1.00 56.97  ? 3510 SER A N     1 
ATOM   14725 C  CA    . SER A 1 3510 ? 147.933 124.323 149.027 1.00 54.17  ? 3510 SER A CA    1 
ATOM   14726 C  C     . SER A 1 3510 ? 147.624 125.799 148.819 1.00 67.46  ? 3510 SER A C     1 
ATOM   14727 O  O     . SER A 1 3510 ? 148.538 126.611 148.634 1.00 82.95  ? 3510 SER A O     1 
ATOM   14728 C  CB    . SER A 1 3510 ? 147.751 123.544 147.727 1.00 59.10  ? 3510 SER A CB    1 
ATOM   14729 O  OG    . SER A 1 3510 ? 148.008 122.166 147.924 1.00 68.67  ? 3510 SER A OG    1 
ATOM   14730 N  N     . ALA A 1 3511 ? 146.341 126.168 148.843 1.00 56.95  ? 3511 ALA A N     1 
ATOM   14731 C  CA    . ALA A 1 3511 ? 145.976 127.571 148.700 1.00 58.11  ? 3511 ALA A CA    1 
ATOM   14732 C  C     . ALA A 1 3511 ? 146.519 128.401 149.853 1.00 61.99  ? 3511 ALA A C     1 
ATOM   14733 O  O     . ALA A 1 3511 ? 147.040 129.504 149.642 1.00 71.64  ? 3511 ALA A O     1 
ATOM   14734 C  CB    . ALA A 1 3511 ? 144.460 127.709 148.611 1.00 59.42  ? 3511 ALA A CB    1 
ATOM   14735 N  N     . ALA A 1 3512 ? 146.407 127.890 151.082 1.00 51.60  ? 3512 ALA A N     1 
ATOM   14736 C  CA    . ALA A 1 3512 ? 146.948 128.613 152.226 1.00 54.06  ? 3512 ALA A CA    1 
ATOM   14737 C  C     . ALA A 1 3512 ? 148.457 128.768 152.110 1.00 58.95  ? 3512 ALA A C     1 
ATOM   14738 O  O     . ALA A 1 3512 ? 149.002 129.839 152.400 1.00 70.43  ? 3512 ALA A O     1 
ATOM   14739 C  CB    . ALA A 1 3512 ? 146.578 127.896 153.524 1.00 58.71  ? 3512 ALA A CB    1 
ATOM   14740 N  N     . PHE A 1 3513 ? 149.147 127.711 151.677 1.00 56.03  ? 3513 PHE A N     1 
ATOM   14741 C  CA    . PHE A 1 3513 ? 150.596 127.787 151.523 1.00 56.70  ? 3513 PHE A CA    1 
ATOM   14742 C  C     . PHE A 1 3513 ? 150.990 128.808 150.464 1.00 56.21  ? 3513 PHE A C     1 
ATOM   14743 O  O     . PHE A 1 3513 ? 151.940 129.576 150.656 1.00 62.46  ? 3513 PHE A O     1 
ATOM   14744 C  CB    . PHE A 1 3513 ? 151.156 126.410 151.174 1.00 62.10  ? 3513 PHE A CB    1 
ATOM   14745 C  CG    . PHE A 1 3513 ? 152.650 126.335 151.245 1.00 64.39  ? 3513 PHE A CG    1 
ATOM   14746 C  CD1   . PHE A 1 3513 ? 153.294 126.293 152.468 1.00 60.81  ? 3513 PHE A CD1   1 
ATOM   14747 C  CD2   . PHE A 1 3513 ? 153.410 126.310 150.090 1.00 63.27  ? 3513 PHE A CD2   1 
ATOM   14748 C  CE1   . PHE A 1 3513 ? 154.668 126.226 152.538 1.00 67.75  ? 3513 PHE A CE1   1 
ATOM   14749 C  CE2   . PHE A 1 3513 ? 154.785 126.244 150.154 1.00 61.44  ? 3513 PHE A CE2   1 
ATOM   14750 C  CZ    . PHE A 1 3513 ? 155.415 126.202 151.379 1.00 69.23  ? 3513 PHE A CZ    1 
ATOM   14751 N  N     . ILE A 1 3514 ? 150.277 128.830 149.338 1.00 51.79  ? 3514 ILE A N     1 
ATOM   14752 C  CA    . ILE A 1 3514 ? 150.609 129.764 148.266 1.00 54.84  ? 3514 ILE A CA    1 
ATOM   14753 C  C     . ILE A 1 3514 ? 150.350 131.200 148.704 1.00 63.47  ? 3514 ILE A C     1 
ATOM   14754 O  O     . ILE A 1 3514 ? 151.176 132.092 148.483 1.00 73.66  ? 3514 ILE A O     1 
ATOM   14755 C  CB    . ILE A 1 3514 ? 149.823 129.418 146.989 1.00 52.55  ? 3514 ILE A CB    1 
ATOM   14756 C  CG1   . ILE A 1 3514 ? 150.327 128.109 146.384 1.00 54.22  ? 3514 ILE A CG1   1 
ATOM   14757 C  CG2   . ILE A 1 3514 ? 149.922 130.544 145.975 1.00 58.06  ? 3514 ILE A CG2   1 
ATOM   14758 C  CD1   . ILE A 1 3514 ? 149.490 127.626 145.228 1.00 55.98  ? 3514 ILE A CD1   1 
ATOM   14759 N  N     . ALA A 1 3515 ? 149.202 131.445 149.337 1.00 48.80  ? 3515 ALA A N     1 
ATOM   14760 C  CA    . ALA A 1 3515 ? 148.812 132.815 149.644 1.00 39.84  ? 3515 ALA A CA    1 
ATOM   14761 C  C     . ALA A 1 3515 ? 149.526 133.377 150.866 1.00 47.43  ? 3515 ALA A C     1 
ATOM   14762 O  O     . ALA A 1 3515 ? 149.730 134.593 150.949 1.00 56.37  ? 3515 ALA A O     1 
ATOM   14763 C  CB    . ALA A 1 3515 ? 147.299 132.893 149.847 1.00 44.20  ? 3515 ALA A CB    1 
ATOM   14764 N  N     . TYR A 1 3516 ? 149.916 132.529 151.816 1.00 51.24  ? 3516 TYR A N     1 
ATOM   14765 C  CA    . TYR A 1 3516 ? 150.369 132.988 153.122 1.00 46.58  ? 3516 TYR A CA    1 
ATOM   14766 C  C     . TYR A 1 3516 ? 151.858 132.792 153.361 1.00 53.21  ? 3516 TYR A C     1 
ATOM   14767 O  O     . TYR A 1 3516 ? 152.539 133.720 153.807 1.00 66.68  ? 3516 TYR A O     1 
ATOM   14768 C  CB    . TYR A 1 3516 ? 149.574 132.267 154.218 1.00 52.37  ? 3516 TYR A CB    1 
ATOM   14769 C  CG    . TYR A 1 3516 ? 148.194 132.836 154.442 1.00 56.05  ? 3516 TYR A CG    1 
ATOM   14770 C  CD1   . TYR A 1 3516 ? 148.014 134.188 154.691 1.00 59.29  ? 3516 TYR A CD1   1 
ATOM   14771 C  CD2   . TYR A 1 3516 ? 147.072 132.023 154.401 1.00 55.66  ? 3516 TYR A CD2   1 
ATOM   14772 C  CE1   . TYR A 1 3516 ? 146.758 134.712 154.898 1.00 56.36  ? 3516 TYR A CE1   1 
ATOM   14773 C  CE2   . TYR A 1 3516 ? 145.811 132.540 154.605 1.00 52.66  ? 3516 TYR A CE2   1 
ATOM   14774 C  CZ    . TYR A 1 3516 ? 145.660 133.885 154.853 1.00 60.10  ? 3516 TYR A CZ    1 
ATOM   14775 O  OH    . TYR A 1 3516 ? 144.405 134.407 155.057 1.00 76.35  ? 3516 TYR A OH    1 
ATOM   14776 N  N     . ALA A 1 3517 ? 152.389 131.606 153.075 1.00 50.40  ? 3517 ALA A N     1 
ATOM   14777 C  CA    . ALA A 1 3517 ? 153.744 131.247 153.473 1.00 54.32  ? 3517 ALA A CA    1 
ATOM   14778 C  C     . ALA A 1 3517 ? 154.814 131.760 152.519 1.00 55.91  ? 3517 ALA A C     1 
ATOM   14779 O  O     . ALA A 1 3517 ? 155.925 131.222 152.519 1.00 72.34  ? 3517 ALA A O     1 
ATOM   14780 C  CB    . ALA A 1 3517 ? 153.862 129.728 153.609 1.00 65.78  ? 3517 ALA A CB    1 
ATOM   14781 N  N     . GLY A 1 3518 ? 154.512 132.771 151.704 1.00 54.32  ? 3518 GLY A N     1 
ATOM   14782 C  CA    . GLY A 1 3518 ? 155.498 133.259 150.754 1.00 59.07  ? 3518 GLY A CA    1 
ATOM   14783 C  C     . GLY A 1 3518 ? 156.694 133.925 151.407 1.00 53.94  ? 3518 GLY A C     1 
ATOM   14784 O  O     . GLY A 1 3518 ? 157.840 133.675 151.024 1.00 55.02  ? 3518 GLY A O     1 
ATOM   14785 N  N     . TYR A 1 3519 ? 156.449 134.782 152.399 1.00 57.65  ? 3519 TYR A N     1 
ATOM   14786 C  CA    . TYR A 1 3519 ? 157.525 135.582 152.974 1.00 62.89  ? 3519 TYR A CA    1 
ATOM   14787 C  C     . TYR A 1 3519 ? 158.408 134.787 153.928 1.00 63.48  ? 3519 TYR A C     1 
ATOM   14788 O  O     . TYR A 1 3519 ? 159.597 135.095 154.062 1.00 69.24  ? 3519 TYR A O     1 
ATOM   14789 C  CB    . TYR A 1 3519 ? 156.944 136.794 153.701 1.00 62.45  ? 3519 TYR A CB    1 
ATOM   14790 C  CG    . TYR A 1 3519 ? 157.989 137.703 154.305 1.00 62.65  ? 3519 TYR A CG    1 
ATOM   14791 C  CD1   . TYR A 1 3519 ? 158.789 138.502 153.501 1.00 64.58  ? 3519 TYR A CD1   1 
ATOM   14792 C  CD2   . TYR A 1 3519 ? 158.179 137.760 155.678 1.00 67.06  ? 3519 TYR A CD2   1 
ATOM   14793 C  CE1   . TYR A 1 3519 ? 159.745 139.334 154.046 1.00 66.43  ? 3519 TYR A CE1   1 
ATOM   14794 C  CE2   . TYR A 1 3519 ? 159.133 138.588 156.233 1.00 68.51  ? 3519 TYR A CE2   1 
ATOM   14795 C  CZ    . TYR A 1 3519 ? 159.913 139.373 155.412 1.00 70.57  ? 3519 TYR A CZ    1 
ATOM   14796 O  OH    . TYR A 1 3519 ? 160.866 140.202 155.958 1.00 73.37  ? 3519 TYR A OH    1 
ATOM   14797 N  N     . PHE A 1 3520 ? 157.858 133.777 154.591 1.00 59.49  ? 3520 PHE A N     1 
ATOM   14798 C  CA    . PHE A 1 3520 ? 158.567 133.105 155.667 1.00 65.40  ? 3520 PHE A CA    1 
ATOM   14799 C  C     . PHE A 1 3520 ? 159.649 132.174 155.125 1.00 70.91  ? 3520 PHE A C     1 
ATOM   14800 O  O     . PHE A 1 3520 ? 159.679 131.827 153.942 1.00 73.74  ? 3520 PHE A O     1 
ATOM   14801 C  CB    . PHE A 1 3520 ? 157.587 132.322 156.537 1.00 64.27  ? 3520 PHE A CB    1 
ATOM   14802 C  CG    . PHE A 1 3520 ? 156.461 133.154 157.071 1.00 62.49  ? 3520 PHE A CG    1 
ATOM   14803 C  CD1   . PHE A 1 3520 ? 156.670 134.037 158.116 1.00 64.19  ? 3520 PHE A CD1   1 
ATOM   14804 C  CD2   . PHE A 1 3520 ? 155.194 133.060 156.524 1.00 65.87  ? 3520 PHE A CD2   1 
ATOM   14805 C  CE1   . PHE A 1 3520 ? 155.637 134.806 158.607 1.00 64.13  ? 3520 PHE A CE1   1 
ATOM   14806 C  CE2   . PHE A 1 3520 ? 154.157 133.827 157.012 1.00 67.15  ? 3520 PHE A CE2   1 
ATOM   14807 C  CZ    . PHE A 1 3520 ? 154.378 134.701 158.054 1.00 68.12  ? 3520 PHE A CZ    1 
ATOM   14808 N  N     . ASP A 1 3521 ? 160.549 131.771 156.020 1.00 74.01  ? 3521 ASP A N     1 
ATOM   14809 C  CA    . ASP A 1 3521 ? 161.633 130.863 155.676 1.00 70.29  ? 3521 ASP A CA    1 
ATOM   14810 C  C     . ASP A 1 3521 ? 161.138 129.420 155.768 1.00 79.21  ? 3521 ASP A C     1 
ATOM   14811 O  O     . ASP A 1 3521 ? 159.957 129.157 156.005 1.00 87.86  ? 3521 ASP A O     1 
ATOM   14812 C  CB    . ASP A 1 3521 ? 162.840 131.115 156.574 1.00 71.69  ? 3521 ASP A CB    1 
ATOM   14813 C  CG    . ASP A 1 3521 ? 162.454 131.314 158.024 1.00 79.18  ? 3521 ASP A CG    1 
ATOM   14814 O  OD1   . ASP A 1 3521 ? 161.243 131.292 158.323 1.00 79.11  ? 3521 ASP A OD1   1 
ATOM   14815 O  OD2   . ASP A 1 3521 ? 163.360 131.494 158.864 1.00 84.28  ? 3521 ASP A OD2   1 
ATOM   14816 N  N     . GLN A 1 3522 ? 162.052 128.464 155.582 1.00 78.78  ? 3522 GLN A N     1 
ATOM   14817 C  CA    . GLN A 1 3522 ? 161.661 127.059 155.500 1.00 78.53  ? 3522 GLN A CA    1 
ATOM   14818 C  C     . GLN A 1 3522 ? 161.040 126.572 156.805 1.00 78.84  ? 3522 GLN A C     1 
ATOM   14819 O  O     . GLN A 1 3522 ? 160.005 125.894 156.799 1.00 85.25  ? 3522 GLN A O     1 
ATOM   14820 C  CB    . GLN A 1 3522 ? 162.874 126.206 155.130 1.00 73.58  ? 3522 GLN A CB    1 
ATOM   14821 C  CG    . GLN A 1 3522 ? 162.618 124.711 155.161 1.00 77.85  ? 3522 GLN A CG    1 
ATOM   14822 C  CD    . GLN A 1 3522 ? 163.856 123.904 154.825 1.00 84.19  ? 3522 GLN A CD    1 
ATOM   14823 O  OE1   . GLN A 1 3522 ? 164.970 124.272 155.198 1.00 82.71  ? 3522 GLN A OE1   1 
ATOM   14824 N  NE2   . GLN A 1 3522 ? 163.668 122.798 154.115 1.00 82.14  ? 3522 GLN A NE2   1 
ATOM   14825 N  N     . GLN A 1 3523 ? 161.660 126.910 157.938 1.00 78.91  ? 3523 GLN A N     1 
ATOM   14826 C  CA    . GLN A 1 3523 ? 161.159 126.433 159.223 1.00 80.52  ? 3523 GLN A CA    1 
ATOM   14827 C  C     . GLN A 1 3523 ? 159.776 126.996 159.525 1.00 78.47  ? 3523 GLN A C     1 
ATOM   14828 O  O     . GLN A 1 3523 ? 158.889 126.267 159.985 1.00 84.68  ? 3523 GLN A O     1 
ATOM   14829 C  CB    . GLN A 1 3523 ? 162.142 126.795 160.337 1.00 84.03  ? 3523 GLN A CB    1 
ATOM   14830 C  CG    . GLN A 1 3523 ? 161.672 126.445 161.746 1.00 87.04  ? 3523 GLN A CG    1 
ATOM   14831 C  CD    . GLN A 1 3523 ? 161.451 124.954 161.953 1.00 90.99  ? 3523 GLN A CD    1 
ATOM   14832 O  OE1   . GLN A 1 3523 ? 160.470 124.383 161.477 1.00 90.09  ? 3523 GLN A OE1   1 
ATOM   14833 N  NE2   . GLN A 1 3523 ? 162.370 124.318 162.670 1.00 86.06  ? 3523 GLN A NE2   1 
ATOM   14834 N  N     . MET A 1 3524 ? 159.567 128.289 159.266 1.00 75.78  ? 3524 MET A N     1 
ATOM   14835 C  CA    . MET A 1 3524 ? 158.260 128.884 159.520 1.00 80.00  ? 3524 MET A CA    1 
ATOM   14836 C  C     . MET A 1 3524 ? 157.202 128.344 158.566 1.00 80.58  ? 3524 MET A C     1 
ATOM   14837 O  O     . MET A 1 3524 ? 156.050 128.148 158.970 1.00 85.40  ? 3524 MET A O     1 
ATOM   14838 C  CB    . MET A 1 3524 ? 158.344 130.405 159.421 1.00 78.08  ? 3524 MET A CB    1 
ATOM   14839 C  CG    . MET A 1 3524 ? 157.511 131.139 160.457 1.00 79.61  ? 3524 MET A CG    1 
ATOM   14840 S  SD    . MET A 1 3524 ? 157.615 130.385 162.091 1.00 94.03  ? 3524 MET A SD    1 
ATOM   14841 C  CE    . MET A 1 3524 ? 155.880 130.239 162.506 1.00 81.76  ? 3524 MET A CE    1 
ATOM   14842 N  N     . ARG A 1 3525 ? 157.566 128.101 157.304 1.00 69.76  ? 3525 ARG A N     1 
ATOM   14843 C  CA    . ARG A 1 3525 ? 156.631 127.478 156.373 1.00 67.89  ? 3525 ARG A CA    1 
ATOM   14844 C  C     . ARG A 1 3525 ? 156.221 126.095 156.858 1.00 71.12  ? 3525 ARG A C     1 
ATOM   14845 O  O     . ARG A 1 3525 ? 155.036 125.735 156.818 1.00 78.61  ? 3525 ARG A O     1 
ATOM   14846 C  CB    . ARG A 1 3525 ? 157.258 127.384 154.983 1.00 63.26  ? 3525 ARG A CB    1 
ATOM   14847 C  CG    . ARG A 1 3525 ? 157.375 128.703 154.244 1.00 62.00  ? 3525 ARG A CG    1 
ATOM   14848 C  CD    . ARG A 1 3525 ? 157.976 128.484 152.867 1.00 58.00  ? 3525 ARG A CD    1 
ATOM   14849 N  NE    . ARG A 1 3525 ? 158.503 129.714 152.291 1.00 58.18  ? 3525 ARG A NE    1 
ATOM   14850 C  CZ    . ARG A 1 3525 ? 158.802 129.867 151.009 1.00 64.56  ? 3525 ARG A CZ    1 
ATOM   14851 N  NH1   . ARG A 1 3525 ? 158.643 128.883 150.140 1.00 66.93  ? 3525 ARG A NH1   1 
ATOM   14852 N  NH2   . ARG A 1 3525 ? 159.272 131.037 150.588 1.00 71.34  ? 3525 ARG A NH2   1 
ATOM   14853 N  N     . GLN A 1 3526 ? 157.192 125.303 157.321 1.00 70.26  ? 3526 GLN A N     1 
ATOM   14854 C  CA    . GLN A 1 3526 ? 156.879 123.978 157.842 1.00 70.01  ? 3526 GLN A CA    1 
ATOM   14855 C  C     . GLN A 1 3526 ? 155.990 124.069 159.074 1.00 75.53  ? 3526 GLN A C     1 
ATOM   14856 O  O     . GLN A 1 3526 ? 155.060 123.271 159.235 1.00 79.67  ? 3526 GLN A O     1 
ATOM   14857 C  CB    . GLN A 1 3526 ? 158.167 123.222 158.164 1.00 68.71  ? 3526 GLN A CB    1 
ATOM   14858 C  CG    . GLN A 1 3526 ? 157.953 121.756 158.494 1.00 72.65  ? 3526 GLN A CG    1 
ATOM   14859 C  CD    . GLN A 1 3526 ? 156.962 121.089 157.562 1.00 76.30  ? 3526 GLN A CD    1 
ATOM   14860 O  OE1   . GLN A 1 3526 ? 157.174 121.029 156.351 1.00 76.89  ? 3526 GLN A OE1   1 
ATOM   14861 N  NE2   . GLN A 1 3526 ? 155.871 120.583 158.123 1.00 72.42  ? 3526 GLN A NE2   1 
ATOM   14862 N  N     . ASN A 1 3527 ? 156.261 125.033 159.957 1.00 73.52  ? 3527 ASN A N     1 
ATOM   14863 C  CA    . ASN A 1 3527 ? 155.430 125.204 161.145 1.00 72.17  ? 3527 ASN A CA    1 
ATOM   14864 C  C     . ASN A 1 3527 ? 153.998 125.568 160.772 1.00 73.55  ? 3527 ASN A C     1 
ATOM   14865 O  O     . ASN A 1 3527 ? 153.042 125.032 161.346 1.00 81.50  ? 3527 ASN A O     1 
ATOM   14866 C  CB    . ASN A 1 3527 ? 156.032 126.272 162.057 1.00 65.78  ? 3527 ASN A CB    1 
ATOM   14867 C  CG    . ASN A 1 3527 ? 157.286 125.798 162.759 1.00 79.31  ? 3527 ASN A CG    1 
ATOM   14868 O  OD1   . ASN A 1 3527 ? 157.683 124.640 162.632 1.00 82.46  ? 3527 ASN A OD1   1 
ATOM   14869 N  ND2   . ASN A 1 3527 ? 157.921 126.694 163.506 1.00 78.25  ? 3527 ASN A ND2   1 
ATOM   14870 N  N     . LEU A 1 3528 ? 153.830 126.479 159.810 1.00 60.43  ? 3528 LEU A N     1 
ATOM   14871 C  CA    . LEU A 1 3528 ? 152.488 126.860 159.379 1.00 60.42  ? 3528 LEU A CA    1 
ATOM   14872 C  C     . LEU A 1 3528 ? 151.749 125.676 158.770 1.00 59.64  ? 3528 LEU A C     1 
ATOM   14873 O  O     . LEU A 1 3528 ? 150.569 125.450 159.069 1.00 74.04  ? 3528 LEU A O     1 
ATOM   14874 C  CB    . LEU A 1 3528 ? 152.562 128.011 158.377 1.00 56.56  ? 3528 LEU A CB    1 
ATOM   14875 C  CG    . LEU A 1 3528 ? 153.021 129.369 158.903 1.00 55.49  ? 3528 LEU A CG    1 
ATOM   14876 C  CD1   . LEU A 1 3528 ? 153.168 130.352 157.757 1.00 58.66  ? 3528 LEU A CD1   1 
ATOM   14877 C  CD2   . LEU A 1 3528 ? 152.047 129.895 159.938 1.00 60.69  ? 3528 LEU A CD2   1 
ATOM   14878 N  N     . PHE A 1 3529 ? 152.426 124.911 157.910 1.00 51.24  ? 3529 PHE A N     1 
ATOM   14879 C  CA    . PHE A 1 3529 ? 151.774 123.760 157.297 1.00 55.66  ? 3529 PHE A CA    1 
ATOM   14880 C  C     . PHE A 1 3529 ? 151.412 122.713 158.342 1.00 64.39  ? 3529 PHE A C     1 
ATOM   14881 O  O     . PHE A 1 3529 ? 150.342 122.098 158.268 1.00 76.13  ? 3529 PHE A O     1 
ATOM   14882 C  CB    . PHE A 1 3529 ? 152.667 123.155 156.215 1.00 61.28  ? 3529 PHE A CB    1 
ATOM   14883 C  CG    . PHE A 1 3529 ? 151.905 122.427 155.147 1.00 62.65  ? 3529 PHE A CG    1 
ATOM   14884 C  CD1   . PHE A 1 3529 ? 151.291 123.122 154.120 1.00 61.66  ? 3529 PHE A CD1   1 
ATOM   14885 C  CD2   . PHE A 1 3529 ? 151.794 121.048 155.176 1.00 63.39  ? 3529 PHE A CD2   1 
ATOM   14886 C  CE1   . PHE A 1 3529 ? 150.587 122.456 153.138 1.00 59.23  ? 3529 PHE A CE1   1 
ATOM   14887 C  CE2   . PHE A 1 3529 ? 151.090 120.376 154.196 1.00 68.80  ? 3529 PHE A CE2   1 
ATOM   14888 C  CZ    . PHE A 1 3529 ? 150.486 121.082 153.176 1.00 65.20  ? 3529 PHE A CZ    1 
ATOM   14889 N  N     . THR A 1 3530 ? 152.287 122.501 159.327 1.00 65.42  ? 3530 THR A N     1 
ATOM   14890 C  CA    . THR A 1 3530 ? 151.984 121.560 160.398 1.00 69.67  ? 3530 THR A CA    1 
ATOM   14891 C  C     . THR A 1 3530 ? 150.776 122.015 161.205 1.00 69.63  ? 3530 THR A C     1 
ATOM   14892 O  O     . THR A 1 3530 ? 149.912 121.202 161.552 1.00 69.39  ? 3530 THR A O     1 
ATOM   14893 C  CB    . THR A 1 3530 ? 153.203 121.390 161.305 1.00 69.60  ? 3530 THR A CB    1 
ATOM   14894 O  OG1   . THR A 1 3530 ? 154.297 120.865 160.543 1.00 71.28  ? 3530 THR A OG1   1 
ATOM   14895 C  CG2   . THR A 1 3530 ? 152.891 120.440 162.450 1.00 72.22  ? 3530 THR A CG2   1 
ATOM   14896 N  N     . THR A 1 3531 ? 150.695 123.312 161.512 1.00 62.86  ? 3531 THR A N     1 
ATOM   14897 C  CA    . THR A 1 3531 ? 149.553 123.825 162.263 1.00 59.91  ? 3531 THR A CA    1 
ATOM   14898 C  C     . THR A 1 3531 ? 148.256 123.638 161.484 1.00 67.51  ? 3531 THR A C     1 
ATOM   14899 O  O     . THR A 1 3531 ? 147.240 123.193 162.039 1.00 77.21  ? 3531 THR A O     1 
ATOM   14900 C  CB    . THR A 1 3531 ? 149.768 125.301 162.599 1.00 57.46  ? 3531 THR A CB    1 
ATOM   14901 O  OG1   . THR A 1 3531 ? 150.996 125.455 163.321 1.00 58.36  ? 3531 THR A OG1   1 
ATOM   14902 C  CG2   . THR A 1 3531 ? 148.621 125.826 163.443 1.00 60.45  ? 3531 THR A CG2   1 
ATOM   14903 N  N     . TRP A 1 3532 ? 148.273 123.965 160.189 1.00 66.92  ? 3532 TRP A N     1 
ATOM   14904 C  CA    . TRP A 1 3532 ? 147.069 123.802 159.379 1.00 55.54  ? 3532 TRP A CA    1 
ATOM   14905 C  C     . TRP A 1 3532 ? 146.669 122.336 159.275 1.00 60.86  ? 3532 TRP A C     1 
ATOM   14906 O  O     . TRP A 1 3532 ? 145.479 122.002 159.347 1.00 70.64  ? 3532 TRP A O     1 
ATOM   14907 C  CB    . TRP A 1 3532 ? 147.274 124.391 157.985 1.00 53.20  ? 3532 TRP A CB    1 
ATOM   14908 C  CG    . TRP A 1 3532 ? 147.806 125.785 157.962 1.00 57.04  ? 3532 TRP A CG    1 
ATOM   14909 C  CD1   . TRP A 1 3532 ? 147.685 126.729 158.937 1.00 61.83  ? 3532 TRP A CD1   1 
ATOM   14910 C  CD2   . TRP A 1 3532 ? 148.543 126.396 156.900 1.00 57.73  ? 3532 TRP A CD2   1 
ATOM   14911 N  NE1   . TRP A 1 3532 ? 148.306 127.891 158.548 1.00 64.35  ? 3532 TRP A NE1   1 
ATOM   14912 C  CE2   . TRP A 1 3532 ? 148.841 127.711 157.300 1.00 61.46  ? 3532 TRP A CE2   1 
ATOM   14913 C  CE3   . TRP A 1 3532 ? 148.984 125.956 155.649 1.00 61.32  ? 3532 TRP A CE3   1 
ATOM   14914 C  CZ2   . TRP A 1 3532 ? 149.559 128.590 156.495 1.00 61.36  ? 3532 TRP A CZ2   1 
ATOM   14915 C  CZ3   . TRP A 1 3532 ? 149.695 126.831 154.852 1.00 64.99  ? 3532 TRP A CZ3   1 
ATOM   14916 C  CH2   . TRP A 1 3532 ? 149.974 128.132 155.277 1.00 66.50  ? 3532 TRP A CH2   1 
ATOM   14917 N  N     . SER A 1 3533 ? 147.648 121.445 159.096 1.00 63.25  ? 3533 SER A N     1 
ATOM   14918 C  CA    . SER A 1 3533 ? 147.346 120.021 159.016 1.00 68.45  ? 3533 SER A CA    1 
ATOM   14919 C  C     . SER A 1 3533 ? 146.761 119.508 160.324 1.00 76.80  ? 3533 SER A C     1 
ATOM   14920 O  O     . SER A 1 3533 ? 145.817 118.711 160.318 1.00 83.08  ? 3533 SER A O     1 
ATOM   14921 C  CB    . SER A 1 3533 ? 148.605 119.239 158.647 1.00 73.15  ? 3533 SER A CB    1 
ATOM   14922 O  OG    . SER A 1 3533 ? 149.127 119.672 157.403 1.00 74.82  ? 3533 SER A OG    1 
ATOM   14923 N  N     . HIS A 1 3534 ? 147.309 119.954 161.457 1.00 84.48  ? 3534 HIS A N     1 
ATOM   14924 C  CA    . HIS A 1 3534 ? 146.768 119.545 162.748 1.00 82.39  ? 3534 HIS A CA    1 
ATOM   14925 C  C     . HIS A 1 3534 ? 145.332 120.021 162.915 1.00 80.35  ? 3534 HIS A C     1 
ATOM   14926 O  O     . HIS A 1 3534 ? 144.473 119.270 163.394 1.00 85.07  ? 3534 HIS A O     1 
ATOM   14927 C  CB    . HIS A 1 3534 ? 147.642 120.083 163.881 1.00 81.33  ? 3534 HIS A CB    1 
ATOM   14928 C  CG    . HIS A 1 3534 ? 148.883 119.282 164.120 1.00 88.77  ? 3534 HIS A CG    1 
ATOM   14929 N  ND1   . HIS A 1 3534 ? 149.918 119.732 164.912 1.00 88.48  ? 3534 HIS A ND1   1 
ATOM   14930 C  CD2   . HIS A 1 3534 ? 149.258 118.061 163.670 1.00 87.29  ? 3534 HIS A CD2   1 
ATOM   14931 C  CE1   . HIS A 1 3534 ? 150.875 118.823 164.940 1.00 86.75  ? 3534 HIS A CE1   1 
ATOM   14932 N  NE2   . HIS A 1 3534 ? 150.500 117.799 164.194 1.00 87.29  ? 3534 HIS A NE2   1 
ATOM   14933 N  N     . HIS A 1 3535 ? 145.051 121.266 162.523 1.00 73.88  ? 3535 HIS A N     1 
ATOM   14934 C  CA    . HIS A 1 3535 ? 143.688 121.771 162.644 1.00 75.88  ? 3535 HIS A CA    1 
ATOM   14935 C  C     . HIS A 1 3535 ? 142.727 121.001 161.748 1.00 75.72  ? 3535 HIS A C     1 
ATOM   14936 O  O     . HIS A 1 3535 ? 141.607 120.681 162.161 1.00 86.78  ? 3535 HIS A O     1 
ATOM   14937 C  CB    . HIS A 1 3535 ? 143.637 123.260 162.320 1.00 71.98  ? 3535 HIS A CB    1 
ATOM   14938 C  CG    . HIS A 1 3535 ? 142.302 123.884 162.578 1.00 72.41  ? 3535 HIS A CG    1 
ATOM   14939 N  ND1   . HIS A 1 3535 ? 141.276 123.853 161.658 1.00 76.19  ? 3535 HIS A ND1   1 
ATOM   14940 C  CD2   . HIS A 1 3535 ? 141.819 124.540 163.659 1.00 75.80  ? 3535 HIS A CD2   1 
ATOM   14941 C  CE1   . HIS A 1 3535 ? 140.222 124.473 162.157 1.00 74.62  ? 3535 HIS A CE1   1 
ATOM   14942 N  NE2   . HIS A 1 3535 ? 140.525 124.900 163.370 1.00 78.73  ? 3535 HIS A NE2   1 
ATOM   14943 N  N     . LEU A 1 3536 ? 143.140 120.702 160.515 1.00 67.36  ? 3536 LEU A N     1 
ATOM   14944 C  CA    . LEU A 1 3536 ? 142.273 119.938 159.624 1.00 73.11  ? 3536 LEU A CA    1 
ATOM   14945 C  C     . LEU A 1 3536 ? 142.044 118.527 160.152 1.00 76.52  ? 3536 LEU A C     1 
ATOM   14946 O  O     . LEU A 1 3536 ? 140.945 117.978 160.015 1.00 78.53  ? 3536 LEU A O     1 
ATOM   14947 C  CB    . LEU A 1 3536 ? 142.858 119.897 158.214 1.00 77.69  ? 3536 LEU A CB    1 
ATOM   14948 C  CG    . LEU A 1 3536 ? 142.838 121.217 157.444 1.00 73.11  ? 3536 LEU A CG    1 
ATOM   14949 C  CD1   . LEU A 1 3536 ? 143.316 121.005 156.021 1.00 74.28  ? 3536 LEU A CD1   1 
ATOM   14950 C  CD2   . LEU A 1 3536 ? 141.449 121.822 157.457 1.00 72.42  ? 3536 LEU A CD2   1 
ATOM   14951 N  N     . GLN A 1 3537 ? 143.072 117.921 160.749 1.00 91.72  ? 3537 GLN A N     1 
ATOM   14952 C  CA    . GLN A 1 3537 ? 142.907 116.601 161.347 1.00 96.39  ? 3537 GLN A CA    1 
ATOM   14953 C  C     . GLN A 1 3537 ? 141.937 116.647 162.521 1.00 96.92  ? 3537 GLN A C     1 
ATOM   14954 O  O     . GLN A 1 3537 ? 141.117 115.738 162.694 1.00 98.81  ? 3537 GLN A O     1 
ATOM   14955 C  CB    . GLN A 1 3537 ? 144.264 116.056 161.790 1.00 95.99  ? 3537 GLN A CB    1 
ATOM   14956 C  CG    . GLN A 1 3537 ? 144.417 114.555 161.623 1.00 93.68  ? 3537 GLN A CG    1 
ATOM   14957 C  CD    . GLN A 1 3537 ? 145.748 114.048 162.140 1.00 96.22  ? 3537 GLN A CD    1 
ATOM   14958 O  OE1   . GLN A 1 3537 ? 146.231 114.489 163.182 1.00 98.87  ? 3537 GLN A OE1   1 
ATOM   14959 N  NE2   . GLN A 1 3537 ? 146.348 113.115 161.410 1.00 93.84  ? 3537 GLN A NE2   1 
ATOM   14960 N  N     . GLN A 1 3538 ? 142.017 117.698 163.341 1.00 89.51  ? 3538 GLN A N     1 
ATOM   14961 C  CA    . GLN A 1 3538 ? 141.103 117.830 164.469 1.00 87.80  ? 3538 GLN A CA    1 
ATOM   14962 C  C     . GLN A 1 3538 ? 139.675 118.127 164.031 1.00 91.39  ? 3538 GLN A C     1 
ATOM   14963 O  O     . GLN A 1 3538 ? 138.742 117.894 164.806 1.00 96.90  ? 3538 GLN A O     1 
ATOM   14964 C  CB    . GLN A 1 3538 ? 141.589 118.924 165.419 1.00 87.07  ? 3538 GLN A CB    1 
ATOM   14965 C  CG    . GLN A 1 3538 ? 142.871 118.582 166.154 1.00 94.51  ? 3538 GLN A CG    1 
ATOM   14966 C  CD    . GLN A 1 3538 ? 143.559 119.807 166.718 1.00 98.06  ? 3538 GLN A CD    1 
ATOM   14967 O  OE1   . GLN A 1 3538 ? 142.939 120.857 166.888 1.00 91.77  ? 3538 GLN A OE1   1 
ATOM   14968 N  NE2   . GLN A 1 3538 ? 144.848 119.680 167.012 1.00 96.75  ? 3538 GLN A NE2   1 
ATOM   14969 N  N     . ALA A 1 3539 ? 139.483 118.634 162.814 1.00 89.49  ? 3539 ALA A N     1 
ATOM   14970 C  CA    . ALA A 1 3539 ? 138.160 118.950 162.296 1.00 88.52  ? 3539 ALA A CA    1 
ATOM   14971 C  C     . ALA A 1 3539 ? 137.587 117.835 161.432 1.00 88.96  ? 3539 ALA A C     1 
ATOM   14972 O  O     . ALA A 1 3539 ? 136.543 118.031 160.800 1.00 88.50  ? 3539 ALA A O     1 
ATOM   14973 C  CB    . ALA A 1 3539 ? 138.202 120.256 161.502 1.00 88.80  ? 3539 ALA A CB    1 
ATOM   14974 N  N     . ASN A 1 3540 ? 138.247 116.675 161.390 1.00 97.80  ? 3540 ASN A N     1 
ATOM   14975 C  CA    . ASN A 1 3540 ? 137.797 115.526 160.602 1.00 98.86  ? 3540 ASN A CA    1 
ATOM   14976 C  C     . ASN A 1 3540 ? 137.633 115.887 159.127 1.00 99.11  ? 3540 ASN A C     1 
ATOM   14977 O  O     . ASN A 1 3540 ? 136.660 115.501 158.478 1.00 99.60  ? 3540 ASN A O     1 
ATOM   14978 C  CB    . ASN A 1 3540 ? 136.500 114.941 161.166 1.00 98.65  ? 3540 ASN A CB    1 
ATOM   14979 C  CG    . ASN A 1 3540 ? 136.710 114.233 162.489 1.00 100.12 ? 3540 ASN A CG    1 
ATOM   14980 O  OD1   . ASN A 1 3540 ? 137.810 114.237 163.040 1.00 98.92  ? 3540 ASN A OD1   1 
ATOM   14981 N  ND2   . ASN A 1 3540 ? 135.652 113.622 163.007 1.00 102.02 ? 3540 ASN A ND2   1 
ATOM   14982 N  N     . ILE A 1 3541 ? 138.596 116.634 158.594 1.00 91.11  ? 3541 ILE A N     1 
ATOM   14983 C  CA    . ILE A 1 3541 ? 138.633 116.994 157.181 1.00 90.40  ? 3541 ILE A CA    1 
ATOM   14984 C  C     . ILE A 1 3541 ? 139.740 116.178 156.530 1.00 90.53  ? 3541 ILE A C     1 
ATOM   14985 O  O     . ILE A 1 3541 ? 140.903 116.252 156.946 1.00 88.93  ? 3541 ILE A O     1 
ATOM   14986 C  CB    . ILE A 1 3541 ? 138.862 118.500 156.984 1.00 87.60  ? 3541 ILE A CB    1 
ATOM   14987 C  CG1   . ILE A 1 3541 ? 137.730 119.296 157.634 1.00 89.35  ? 3541 ILE A CG1   1 
ATOM   14988 C  CG2   . ILE A 1 3541 ? 138.962 118.832 155.506 1.00 86.54  ? 3541 ILE A CG2   1 
ATOM   14989 C  CD1   . ILE A 1 3541 ? 137.890 120.793 157.514 1.00 90.69  ? 3541 ILE A CD1   1 
ATOM   14990 N  N     . GLN A 1 3542 ? 139.381 115.401 155.512 1.00 102.44 ? 3542 GLN A N     1 
ATOM   14991 C  CA    . GLN A 1 3542 ? 140.322 114.481 154.890 1.00 100.93 ? 3542 GLN A CA    1 
ATOM   14992 C  C     . GLN A 1 3542 ? 141.315 115.235 154.015 1.00 101.56 ? 3542 GLN A C     1 
ATOM   14993 O  O     . GLN A 1 3542 ? 140.931 116.108 153.232 1.00 100.33 ? 3542 GLN A O     1 
ATOM   14994 C  CB    . GLN A 1 3542 ? 139.574 113.437 154.062 1.00 101.37 ? 3542 GLN A CB    1 
ATOM   14995 C  CG    . GLN A 1 3542 ? 138.685 112.520 154.884 1.00 102.29 ? 3542 GLN A CG    1 
ATOM   14996 C  CD    . GLN A 1 3542 ? 139.408 111.928 156.078 1.00 103.99 ? 3542 GLN A CD    1 
ATOM   14997 O  OE1   . GLN A 1 3542 ? 139.025 112.154 157.225 1.00 103.24 ? 3542 GLN A OE1   1 
ATOM   14998 N  NE2   . GLN A 1 3542 ? 140.463 111.167 155.813 1.00 105.60 ? 3542 GLN A NE2   1 
ATOM   14999 N  N     . PHE A 1 3543 ? 142.594 114.891 154.151 1.00 94.11  ? 3543 PHE A N     1 
ATOM   15000 C  CA    . PHE A 1 3543 ? 143.649 115.467 153.332 1.00 90.20  ? 3543 PHE A CA    1 
ATOM   15001 C  C     . PHE A 1 3543 ? 144.831 114.510 153.320 1.00 93.67  ? 3543 PHE A C     1 
ATOM   15002 O  O     . PHE A 1 3543 ? 145.150 113.898 154.343 1.00 97.11  ? 3543 PHE A O     1 
ATOM   15003 C  CB    . PHE A 1 3543 ? 144.078 116.845 153.848 1.00 88.41  ? 3543 PHE A CB    1 
ATOM   15004 C  CG    . PHE A 1 3543 ? 144.768 116.809 155.182 1.00 88.50  ? 3543 PHE A CG    1 
ATOM   15005 C  CD1   . PHE A 1 3543 ? 144.036 116.728 156.353 1.00 92.15  ? 3543 PHE A CD1   1 
ATOM   15006 C  CD2   . PHE A 1 3543 ? 146.149 116.861 155.264 1.00 89.01  ? 3543 PHE A CD2   1 
ATOM   15007 C  CE1   . PHE A 1 3543 ? 144.668 116.695 157.581 1.00 89.34  ? 3543 PHE A CE1   1 
ATOM   15008 C  CE2   . PHE A 1 3543 ? 146.786 116.829 156.489 1.00 91.02  ? 3543 PHE A CE2   1 
ATOM   15009 C  CZ    . PHE A 1 3543 ? 146.044 116.746 157.648 1.00 86.79  ? 3543 PHE A CZ    1 
ATOM   15010 N  N     . ARG A 1 3544 ? 145.472 114.382 152.163 1.00 101.58 ? 3544 ARG A N     1 
ATOM   15011 C  CA    . ARG A 1 3544 ? 146.621 113.500 152.035 1.00 101.77 ? 3544 ARG A CA    1 
ATOM   15012 C  C     . ARG A 1 3544 ? 147.837 114.086 152.740 1.00 105.68 ? 3544 ARG A C     1 
ATOM   15013 O  O     . ARG A 1 3544 ? 148.031 115.304 152.789 1.00 108.99 ? 3544 ARG A O     1 
ATOM   15014 C  CB    . ARG A 1 3544 ? 146.953 113.247 150.564 1.00 99.45  ? 3544 ARG A CB    1 
ATOM   15015 C  CG    . ARG A 1 3544 ? 146.062 112.218 149.893 1.00 101.87 ? 3544 ARG A CG    1 
ATOM   15016 C  CD    . ARG A 1 3544 ? 146.464 112.003 148.444 1.00 103.65 ? 3544 ARG A CD    1 
ATOM   15017 N  NE    . ARG A 1 3544 ? 146.117 113.144 147.606 1.00 105.71 ? 3544 ARG A NE    1 
ATOM   15018 C  CZ    . ARG A 1 3544 ? 146.435 113.255 146.323 1.00 103.78 ? 3544 ARG A CZ    1 
ATOM   15019 N  NH1   . ARG A 1 3544 ? 147.114 112.309 145.695 1.00 105.66 ? 3544 ARG A NH1   1 
ATOM   15020 N  NH2   . ARG A 1 3544 ? 146.063 114.342 145.654 1.00 103.21 ? 3544 ARG A NH2   1 
ATOM   15021 N  N     . THR A 1 3545 ? 148.658 113.197 153.296 1.00 114.34 ? 3545 THR A N     1 
ATOM   15022 C  CA    . THR A 1 3545 ? 149.910 113.577 153.935 1.00 115.36 ? 3545 THR A CA    1 
ATOM   15023 C  C     . THR A 1 3545 ? 151.139 113.022 153.234 1.00 114.62 ? 3545 THR A C     1 
ATOM   15024 O  O     . THR A 1 3545 ? 152.244 113.511 153.474 1.00 112.27 ? 3545 THR A O     1 
ATOM   15025 C  CB    . THR A 1 3545 ? 149.926 113.112 155.398 1.00 114.47 ? 3545 THR A CB    1 
ATOM   15026 O  OG1   . THR A 1 3545 ? 150.056 111.686 155.447 1.00 116.04 ? 3545 THR A OG1   1 
ATOM   15027 C  CG2   . THR A 1 3545 ? 148.642 113.522 156.104 1.00 109.18 ? 3545 THR A CG2   1 
ATOM   15028 N  N     . ASP A 1 3546 ? 150.971 112.013 152.376 1.00 124.36 ? 3546 ASP A N     1 
ATOM   15029 C  CA    . ASP A 1 3546 ? 152.117 111.414 151.700 1.00 123.75 ? 3546 ASP A CA    1 
ATOM   15030 C  C     . ASP A 1 3546 ? 152.678 112.337 150.625 1.00 125.52 ? 3546 ASP A C     1 
ATOM   15031 O  O     . ASP A 1 3546 ? 153.899 112.452 150.471 1.00 127.28 ? 3546 ASP A O     1 
ATOM   15032 C  CB    . ASP A 1 3546 ? 151.719 110.069 151.093 1.00 121.89 ? 3546 ASP A CB    1 
ATOM   15033 C  CG    . ASP A 1 3546 ? 150.426 110.145 150.304 1.00 124.47 ? 3546 ASP A CG    1 
ATOM   15034 O  OD1   . ASP A 1 3546 ? 149.841 111.245 150.223 1.00 128.23 ? 3546 ASP A OD1   1 
ATOM   15035 O  OD2   . ASP A 1 3546 ? 149.995 109.106 149.762 1.00 123.27 ? 3546 ASP A OD2   1 
ATOM   15036 N  N     . ILE A 1 3547 ? 151.805 113.002 149.874 1.00 116.74 ? 3547 ILE A N     1 
ATOM   15037 C  CA    . ILE A 1 3547 ? 152.233 113.798 148.729 1.00 115.00 ? 3547 ILE A CA    1 
ATOM   15038 C  C     . ILE A 1 3547 ? 152.766 115.141 149.213 1.00 112.44 ? 3547 ILE A C     1 
ATOM   15039 O  O     . ILE A 1 3547 ? 152.136 115.819 150.033 1.00 107.75 ? 3547 ILE A O     1 
ATOM   15040 C  CB    . ILE A 1 3547 ? 151.079 113.977 147.728 1.00 114.93 ? 3547 ILE A CB    1 
ATOM   15041 C  CG1   . ILE A 1 3547 ? 151.507 114.880 146.570 1.00 111.99 ? 3547 ILE A CG1   1 
ATOM   15042 C  CG2   . ILE A 1 3547 ? 149.831 114.514 148.419 1.00 113.93 ? 3547 ILE A CG2   1 
ATOM   15043 C  CD1   . ILE A 1 3547 ? 150.609 114.782 145.358 1.00 110.35 ? 3547 ILE A CD1   1 
ATOM   15044 N  N     . ALA A 1 3548 ? 153.941 115.518 148.718 1.00 102.19 ? 3548 ALA A N     1 
ATOM   15045 C  CA    . ALA A 1 3548 ? 154.531 116.803 149.051 1.00 102.94 ? 3548 ALA A CA    1 
ATOM   15046 C  C     . ALA A 1 3548 ? 153.806 117.928 148.323 1.00 104.85 ? 3548 ALA A C     1 
ATOM   15047 O  O     . ALA A 1 3548 ? 153.235 117.733 147.246 1.00 104.84 ? 3548 ALA A O     1 
ATOM   15048 C  CB    . ALA A 1 3548 ? 156.017 116.823 148.694 1.00 101.38 ? 3548 ALA A CB    1 
ATOM   15049 N  N     . ARG A 1 3549 ? 153.833 119.118 148.927 1.00 87.82  ? 3549 ARG A N     1 
ATOM   15050 C  CA    . ARG A 1 3549 ? 153.139 120.258 148.340 1.00 81.58  ? 3549 ARG A CA    1 
ATOM   15051 C  C     . ARG A 1 3549 ? 153.754 120.676 147.011 1.00 82.45  ? 3549 ARG A C     1 
ATOM   15052 O  O     . ARG A 1 3549 ? 153.041 121.170 146.131 1.00 90.61  ? 3549 ARG A O     1 
ATOM   15053 C  CB    . ARG A 1 3549 ? 153.141 121.435 149.315 1.00 74.29  ? 3549 ARG A CB    1 
ATOM   15054 C  CG    . ARG A 1 3549 ? 154.475 121.678 149.993 1.00 77.29  ? 3549 ARG A CG    1 
ATOM   15055 C  CD    . ARG A 1 3549 ? 154.342 122.706 151.101 1.00 79.04  ? 3549 ARG A CD    1 
ATOM   15056 N  NE    . ARG A 1 3549 ? 155.611 122.954 151.773 1.00 76.96  ? 3549 ARG A NE    1 
ATOM   15057 C  CZ    . ARG A 1 3549 ? 155.981 122.381 152.909 1.00 79.51  ? 3549 ARG A CZ    1 
ATOM   15058 N  NH1   . ARG A 1 3549 ? 155.201 121.511 153.530 1.00 81.14  ? 3549 ARG A NH1   1 
ATOM   15059 N  NH2   . ARG A 1 3549 ? 157.163 122.688 153.435 1.00 83.10  ? 3549 ARG A NH2   1 
ATOM   15060 N  N     . THR A 1 3550 ? 155.067 120.497 146.848 1.00 85.30  ? 3550 THR A N     1 
ATOM   15061 C  CA    . THR A 1 3550 ? 155.715 120.884 145.599 1.00 85.96  ? 3550 THR A CA    1 
ATOM   15062 C  C     . THR A 1 3550 ? 155.196 120.063 144.425 1.00 91.41  ? 3550 THR A C     1 
ATOM   15063 O  O     . THR A 1 3550 ? 154.935 120.605 143.346 1.00 92.14  ? 3550 THR A O     1 
ATOM   15064 C  CB    . THR A 1 3550 ? 157.231 120.733 145.722 1.00 88.92  ? 3550 THR A CB    1 
ATOM   15065 O  OG1   . THR A 1 3550 ? 157.559 119.355 145.934 1.00 95.47  ? 3550 THR A OG1   1 
ATOM   15066 C  CG2   . THR A 1 3550 ? 157.752 121.554 146.887 1.00 88.54  ? 3550 THR A CG2   1 
ATOM   15067 N  N     . GLU A 1 3551 ? 155.041 118.752 144.615 1.00 97.27  ? 3551 GLU A N     1 
ATOM   15068 C  CA    . GLU A 1 3551 ? 154.549 117.891 143.548 1.00 95.71  ? 3551 GLU A CA    1 
ATOM   15069 C  C     . GLU A 1 3551 ? 153.048 118.016 143.332 1.00 98.05  ? 3551 GLU A C     1 
ATOM   15070 O  O     . GLU A 1 3551 ? 152.568 117.734 142.229 1.00 100.25 ? 3551 GLU A O     1 
ATOM   15071 C  CB    . GLU A 1 3551 ? 154.905 116.432 143.839 1.00 96.00  ? 3551 GLU A CB    1 
ATOM   15072 C  CG    . GLU A 1 3551 ? 156.388 116.125 143.734 1.00 99.98  ? 3551 GLU A CG    1 
ATOM   15073 C  CD    . GLU A 1 3551 ? 156.790 114.907 144.539 1.00 104.35 ? 3551 GLU A CD    1 
ATOM   15074 O  OE1   . GLU A 1 3551 ? 156.026 113.919 144.545 1.00 106.32 ? 3551 GLU A OE1   1 
ATOM   15075 O  OE2   . GLU A 1 3551 ? 157.869 114.937 145.166 1.00 103.18 ? 3551 GLU A OE2   1 
ATOM   15076 N  N     . TYR A 1 3552 ? 152.295 118.421 144.357 1.00 86.77  ? 3552 TYR A N     1 
ATOM   15077 C  CA    . TYR A 1 3552 ? 150.852 118.560 144.197 1.00 84.42  ? 3552 TYR A CA    1 
ATOM   15078 C  C     . TYR A 1 3552 ? 150.500 119.808 143.396 1.00 81.15  ? 3552 TYR A C     1 
ATOM   15079 O  O     . TYR A 1 3552 ? 149.487 119.831 142.688 1.00 86.15  ? 3552 TYR A O     1 
ATOM   15080 C  CB    . TYR A 1 3552 ? 150.174 118.592 145.565 1.00 84.96  ? 3552 TYR A CB    1 
ATOM   15081 C  CG    . TYR A 1 3552 ? 148.665 118.572 145.497 1.00 82.29  ? 3552 TYR A CG    1 
ATOM   15082 C  CD1   . TYR A 1 3552 ? 147.991 117.497 144.936 1.00 87.48  ? 3552 TYR A CD1   1 
ATOM   15083 C  CD2   . TYR A 1 3552 ? 147.915 119.629 145.991 1.00 82.81  ? 3552 TYR A CD2   1 
ATOM   15084 C  CE1   . TYR A 1 3552 ? 146.612 117.475 144.871 1.00 87.69  ? 3552 TYR A CE1   1 
ATOM   15085 C  CE2   . TYR A 1 3552 ? 146.536 119.616 145.930 1.00 85.49  ? 3552 TYR A CE2   1 
ATOM   15086 C  CZ    . TYR A 1 3552 ? 145.890 118.536 145.369 1.00 85.90  ? 3552 TYR A CZ    1 
ATOM   15087 O  OH    . TYR A 1 3552 ? 144.517 118.519 145.306 1.00 90.86  ? 3552 TYR A OH    1 
ATOM   15088 N  N     . LEU A 1 3553 ? 151.317 120.852 143.497 1.00 77.68  ? 3553 LEU A N     1 
ATOM   15089 C  CA    . LEU A 1 3553 ? 151.036 122.128 142.855 1.00 79.08  ? 3553 LEU A CA    1 
ATOM   15090 C  C     . LEU A 1 3553 ? 151.704 122.287 141.496 1.00 83.14  ? 3553 LEU A C     1 
ATOM   15091 O  O     . LEU A 1 3553 ? 151.463 123.293 140.821 1.00 88.49  ? 3553 LEU A O     1 
ATOM   15092 C  CB    . LEU A 1 3553 ? 151.465 123.277 143.770 1.00 74.86  ? 3553 LEU A CB    1 
ATOM   15093 C  CG    . LEU A 1 3553 ? 150.557 123.514 144.973 1.00 75.13  ? 3553 LEU A CG    1 
ATOM   15094 C  CD1   . LEU A 1 3553 ? 151.208 124.467 145.960 1.00 74.80  ? 3553 LEU A CD1   1 
ATOM   15095 C  CD2   . LEU A 1 3553 ? 149.217 124.046 144.503 1.00 78.39  ? 3553 LEU A CD2   1 
ATOM   15096 N  N     . SER A 1 3554 ? 152.533 121.335 141.076 1.00 78.37  ? 3554 SER A N     1 
ATOM   15097 C  CA    . SER A 1 3554 ? 153.217 121.447 139.797 1.00 79.42  ? 3554 SER A CA    1 
ATOM   15098 C  C     . SER A 1 3554 ? 153.471 120.056 139.240 1.00 84.17  ? 3554 SER A C     1 
ATOM   15099 O  O     . SER A 1 3554 ? 153.553 119.073 139.980 1.00 89.66  ? 3554 SER A O     1 
ATOM   15100 C  CB    . SER A 1 3554 ? 154.534 122.219 139.931 1.00 78.88  ? 3554 SER A CB    1 
ATOM   15101 O  OG    . SER A 1 3554 ? 155.458 121.510 140.737 1.00 85.01  ? 3554 SER A OG    1 
ATOM   15102 N  N     . ASN A 1 3555 ? 153.598 119.985 137.920 1.00 85.99  ? 3555 ASN A N     1 
ATOM   15103 C  CA    . ASN A 1 3555 ? 153.856 118.733 137.228 1.00 87.42  ? 3555 ASN A CA    1 
ATOM   15104 C  C     . ASN A 1 3555 ? 155.340 118.605 136.899 1.00 89.81  ? 3555 ASN A C     1 
ATOM   15105 O  O     . ASN A 1 3555 ? 156.122 119.547 137.044 1.00 93.19  ? 3555 ASN A O     1 
ATOM   15106 C  CB    . ASN A 1 3555 ? 153.008 118.634 135.957 1.00 86.74  ? 3555 ASN A CB    1 
ATOM   15107 C  CG    . ASN A 1 3555 ? 153.076 119.887 135.112 1.00 88.46  ? 3555 ASN A CG    1 
ATOM   15108 O  OD1   . ASN A 1 3555 ? 154.109 120.192 134.518 1.00 94.69  ? 3555 ASN A OD1   1 
ATOM   15109 N  ND2   . ASN A 1 3555 ? 151.973 120.624 135.054 1.00 87.44  ? 3555 ASN A ND2   1 
ATOM   15110 N  N     . ALA A 1 3556 ? 155.723 117.406 136.455 1.00 88.76  ? 3556 ALA A N     1 
ATOM   15111 C  CA    . ALA A 1 3556 ? 157.130 117.128 136.185 1.00 89.51  ? 3556 ALA A CA    1 
ATOM   15112 C  C     . ALA A 1 3556 ? 157.659 117.969 135.029 1.00 93.56  ? 3556 ALA A C     1 
ATOM   15113 O  O     . ALA A 1 3556 ? 158.800 118.444 135.072 1.00 94.73  ? 3556 ALA A O     1 
ATOM   15114 C  CB    . ALA A 1 3556 ? 157.322 115.640 135.898 1.00 91.63  ? 3556 ALA A CB    1 
ATOM   15115 N  N     . ASP A 1 3557 ? 156.852 118.152 133.980 1.00 93.82  ? 3557 ASP A N     1 
ATOM   15116 C  CA    . ASP A 1 3557 ? 157.301 118.928 132.827 1.00 91.19  ? 3557 ASP A CA    1 
ATOM   15117 C  C     . ASP A 1 3557 ? 157.594 120.372 133.212 1.00 93.93  ? 3557 ASP A C     1 
ATOM   15118 O  O     . ASP A 1 3557 ? 158.597 120.951 132.774 1.00 99.08  ? 3557 ASP A O     1 
ATOM   15119 C  CB    . ASP A 1 3557 ? 156.249 118.876 131.720 1.00 93.12  ? 3557 ASP A CB    1 
ATOM   15120 C  CG    . ASP A 1 3557 ? 155.742 117.472 131.464 1.00 98.80  ? 3557 ASP A CG    1 
ATOM   15121 O  OD1   . ASP A 1 3557 ? 154.510 117.268 131.491 1.00 100.77 ? 3557 ASP A OD1   1 
ATOM   15122 O  OD2   . ASP A 1 3557 ? 156.575 116.573 131.231 1.00 99.96  ? 3557 ASP A OD2   1 
ATOM   15123 N  N     . GLU A 1 3558 ? 156.726 120.972 134.027 1.00 88.96  ? 3558 GLU A N     1 
ATOM   15124 C  CA    . GLU A 1 3558 ? 156.947 122.344 134.466 1.00 84.82  ? 3558 GLU A CA    1 
ATOM   15125 C  C     . GLU A 1 3558 ? 158.200 122.455 135.325 1.00 87.71  ? 3558 GLU A C     1 
ATOM   15126 O  O     . GLU A 1 3558 ? 158.960 123.422 135.201 1.00 90.06  ? 3558 GLU A O     1 
ATOM   15127 C  CB    . GLU A 1 3558 ? 155.726 122.845 135.229 1.00 86.74  ? 3558 GLU A CB    1 
ATOM   15128 C  CG    . GLU A 1 3558 ? 155.473 124.329 135.101 1.00 91.18  ? 3558 GLU A CG    1 
ATOM   15129 C  CD    . GLU A 1 3558 ? 154.076 124.699 135.538 1.00 95.23  ? 3558 GLU A CD    1 
ATOM   15130 O  OE1   . GLU A 1 3558 ? 153.838 124.735 136.761 1.00 97.29  ? 3558 GLU A OE1   1 
ATOM   15131 O  OE2   . GLU A 1 3558 ? 153.220 124.954 134.666 1.00 91.32  ? 3558 GLU A OE2   1 
ATOM   15132 N  N     . ARG A 1 3559 ? 158.431 121.478 136.205 1.00 86.86  ? 3559 ARG A N     1 
ATOM   15133 C  CA    . ARG A 1 3559 ? 159.647 121.489 137.010 1.00 83.30  ? 3559 ARG A CA    1 
ATOM   15134 C  C     . ARG A 1 3559 ? 160.885 121.372 136.133 1.00 87.77  ? 3559 ARG A C     1 
ATOM   15135 O  O     . ARG A 1 3559 ? 161.888 122.056 136.368 1.00 88.60  ? 3559 ARG A O     1 
ATOM   15136 C  CB    . ARG A 1 3559 ? 159.608 120.362 138.041 1.00 83.07  ? 3559 ARG A CB    1 
ATOM   15137 C  CG    . ARG A 1 3559 ? 158.683 120.629 139.215 1.00 85.39  ? 3559 ARG A CG    1 
ATOM   15138 C  CD    . ARG A 1 3559 ? 158.906 119.626 140.334 1.00 87.91  ? 3559 ARG A CD    1 
ATOM   15139 N  NE    . ARG A 1 3559 ? 158.597 118.264 139.919 1.00 89.65  ? 3559 ARG A NE    1 
ATOM   15140 C  CZ    . ARG A 1 3559 ? 157.431 117.665 140.122 1.00 88.18  ? 3559 ARG A CZ    1 
ATOM   15141 N  NH1   . ARG A 1 3559 ? 156.434 118.284 140.732 1.00 88.85  ? 3559 ARG A NH1   1 
ATOM   15142 N  NH2   . ARG A 1 3559 ? 157.262 116.415 139.703 1.00 90.17  ? 3559 ARG A NH2   1 
ATOM   15143 N  N     . LEU A 1 3560 ? 160.834 120.510 135.115 1.00 92.25  ? 3560 LEU A N     1 
ATOM   15144 C  CA    . LEU A 1 3560 ? 161.958 120.383 134.195 1.00 88.99  ? 3560 LEU A CA    1 
ATOM   15145 C  C     . LEU A 1 3560 ? 162.215 121.690 133.456 1.00 89.62  ? 3560 LEU A C     1 
ATOM   15146 O  O     . LEU A 1 3560 ? 163.369 122.105 133.294 1.00 94.70  ? 3560 LEU A O     1 
ATOM   15147 C  CB    . LEU A 1 3560 ? 161.696 119.249 133.204 1.00 89.17  ? 3560 LEU A CB    1 
ATOM   15148 C  CG    . LEU A 1 3560 ? 162.886 118.784 132.364 1.00 93.45  ? 3560 LEU A CG    1 
ATOM   15149 C  CD1   . LEU A 1 3560 ? 164.122 118.616 133.232 1.00 94.20  ? 3560 LEU A CD1   1 
ATOM   15150 C  CD2   . LEU A 1 3560 ? 162.554 117.488 131.645 1.00 91.51  ? 3560 LEU A CD2   1 
ATOM   15151 N  N     . ARG A 1 3561 ? 161.149 122.353 133.002 1.00 85.89  ? 3561 ARG A N     1 
ATOM   15152 C  CA    . ARG A 1 3561 ? 161.318 123.632 132.319 1.00 84.99  ? 3561 ARG A CA    1 
ATOM   15153 C  C     . ARG A 1 3561 ? 161.905 124.681 133.255 1.00 86.79  ? 3561 ARG A C     1 
ATOM   15154 O  O     . ARG A 1 3561 ? 162.735 125.499 132.840 1.00 87.72  ? 3561 ARG A O     1 
ATOM   15155 C  CB    . ARG A 1 3561 ? 159.985 124.107 131.742 1.00 86.37  ? 3561 ARG A CB    1 
ATOM   15156 C  CG    . ARG A 1 3561 ? 160.125 125.272 130.773 1.00 89.73  ? 3561 ARG A CG    1 
ATOM   15157 C  CD    . ARG A 1 3561 ? 158.775 125.799 130.316 1.00 92.08  ? 3561 ARG A CD    1 
ATOM   15158 N  NE    . ARG A 1 3561 ? 158.154 126.661 131.314 1.00 90.33  ? 3561 ARG A NE    1 
ATOM   15159 C  CZ    . ARG A 1 3561 ? 157.103 126.321 132.048 1.00 91.25  ? 3561 ARG A CZ    1 
ATOM   15160 N  NH1   . ARG A 1 3561 ? 156.524 125.139 131.920 1.00 90.39  ? 3561 ARG A NH1   1 
ATOM   15161 N  NH2   . ARG A 1 3561 ? 156.619 127.191 132.930 1.00 89.90  ? 3561 ARG A NH2   1 
ATOM   15162 N  N     . TRP A 1 3562 ? 161.481 124.679 134.522 1.00 80.88  ? 3562 TRP A N     1 
ATOM   15163 C  CA    . TRP A 1 3562 ? 162.060 125.600 135.495 1.00 78.68  ? 3562 TRP A CA    1 
ATOM   15164 C  C     . TRP A 1 3562 ? 163.546 125.330 135.695 1.00 80.89  ? 3562 TRP A C     1 
ATOM   15165 O  O     . TRP A 1 3562 ? 164.350 126.266 135.762 1.00 82.46  ? 3562 TRP A O     1 
ATOM   15166 C  CB    . TRP A 1 3562 ? 161.318 125.501 136.828 1.00 79.60  ? 3562 TRP A CB    1 
ATOM   15167 C  CG    . TRP A 1 3562 ? 159.914 126.012 136.788 1.00 77.85  ? 3562 TRP A CG    1 
ATOM   15168 C  CD1   . TRP A 1 3562 ? 159.384 126.887 135.887 1.00 79.22  ? 3562 TRP A CD1   1 
ATOM   15169 C  CD2   . TRP A 1 3562 ? 158.859 125.687 137.700 1.00 77.66  ? 3562 TRP A CD2   1 
ATOM   15170 N  NE1   . TRP A 1 3562 ? 158.062 127.122 136.177 1.00 76.63  ? 3562 TRP A NE1   1 
ATOM   15171 C  CE2   . TRP A 1 3562 ? 157.716 126.397 137.286 1.00 78.83  ? 3562 TRP A CE2   1 
ATOM   15172 C  CE3   . TRP A 1 3562 ? 158.770 124.861 138.824 1.00 78.07  ? 3562 TRP A CE3   1 
ATOM   15173 C  CZ2   . TRP A 1 3562 ? 156.499 126.307 137.957 1.00 81.41  ? 3562 TRP A CZ2   1 
ATOM   15174 C  CZ3   . TRP A 1 3562 ? 157.562 124.773 139.487 1.00 73.97  ? 3562 TRP A CZ3   1 
ATOM   15175 C  CH2   . TRP A 1 3562 ? 156.443 125.492 139.053 1.00 77.71  ? 3562 TRP A CH2   1 
ATOM   15176 N  N     . GLN A 1 3563 ? 163.928 124.054 135.798 1.00 83.02  ? 3563 GLN A N     1 
ATOM   15177 C  CA    . GLN A 1 3563 ? 165.345 123.719 135.921 1.00 81.57  ? 3563 GLN A CA    1 
ATOM   15178 C  C     . GLN A 1 3563 ? 166.123 124.169 134.693 1.00 83.93  ? 3563 GLN A C     1 
ATOM   15179 O  O     . GLN A 1 3563 ? 167.281 124.590 134.801 1.00 82.20  ? 3563 GLN A O     1 
ATOM   15180 C  CB    . GLN A 1 3563 ? 165.528 122.217 136.148 1.00 81.79  ? 3563 GLN A CB    1 
ATOM   15181 C  CG    . GLN A 1 3563 ? 164.750 121.650 137.322 1.00 84.99  ? 3563 GLN A CG    1 
ATOM   15182 C  CD    . GLN A 1 3563 ? 165.125 122.291 138.643 1.00 88.06  ? 3563 GLN A CD    1 
ATOM   15183 O  OE1   . GLN A 1 3563 ? 166.250 122.757 138.825 1.00 90.02  ? 3563 GLN A OE1   1 
ATOM   15184 N  NE2   . GLN A 1 3563 ? 164.179 122.320 139.574 1.00 86.55  ? 3563 GLN A NE2   1 
ATOM   15185 N  N     . ALA A 1 3564 ? 165.505 124.084 133.513 1.00 90.44  ? 3564 ALA A N     1 
ATOM   15186 C  CA    . ALA A 1 3564 ? 166.148 124.579 132.302 1.00 86.86  ? 3564 ALA A CA    1 
ATOM   15187 C  C     . ALA A 1 3564 ? 166.352 126.088 132.328 1.00 87.22  ? 3564 ALA A C     1 
ATOM   15188 O  O     . ALA A 1 3564 ? 167.201 126.598 131.588 1.00 89.93  ? 3564 ALA A O     1 
ATOM   15189 C  CB    . ALA A 1 3564 ? 165.330 124.185 131.072 1.00 87.26  ? 3564 ALA A CB    1 
ATOM   15190 N  N     . SER A 1 3565 ? 165.600 126.813 133.158 1.00 87.65  ? 3565 SER A N     1 
ATOM   15191 C  CA    . SER A 1 3565 ? 165.712 128.262 133.271 1.00 82.62  ? 3565 SER A CA    1 
ATOM   15192 C  C     . SER A 1 3565 ? 166.596 128.686 134.441 1.00 80.80  ? 3565 SER A C     1 
ATOM   15193 O  O     . SER A 1 3565 ? 166.380 129.753 135.024 1.00 77.78  ? 3565 SER A O     1 
ATOM   15194 C  CB    . SER A 1 3565 ? 164.326 128.892 133.396 1.00 84.70  ? 3565 SER A CB    1 
ATOM   15195 O  OG    . SER A 1 3565 ? 163.589 128.739 132.197 1.00 87.30  ? 3565 SER A OG    1 
ATOM   15196 N  N     . SER A 1 3566 ? 167.583 127.860 134.794 1.00 91.88  ? 3566 SER A N     1 
ATOM   15197 C  CA    . SER A 1 3566 ? 168.558 128.176 135.840 1.00 93.16  ? 3566 SER A CA    1 
ATOM   15198 C  C     . SER A 1 3566 ? 167.889 128.411 137.193 1.00 89.03  ? 3566 SER A C     1 
ATOM   15199 O  O     . SER A 1 3566 ? 168.290 129.287 137.961 1.00 88.61  ? 3566 SER A O     1 
ATOM   15200 C  CB    . SER A 1 3566 ? 169.420 129.378 135.448 1.00 93.66  ? 3566 SER A CB    1 
ATOM   15201 O  OG    . SER A 1 3566 ? 168.717 130.592 135.644 1.00 96.59  ? 3566 SER A OG    1 
ATOM   15202 N  N     . LEU A 1 3567 ? 166.860 127.624 137.490 1.00 85.59  ? 3567 LEU A N     1 
ATOM   15203 C  CA    . LEU A 1 3567 ? 166.272 127.685 138.824 1.00 86.50  ? 3567 LEU A CA    1 
ATOM   15204 C  C     . LEU A 1 3567 ? 166.954 126.670 139.732 1.00 90.50  ? 3567 LEU A C     1 
ATOM   15205 O  O     . LEU A 1 3567 ? 167.030 125.488 139.377 1.00 95.39  ? 3567 LEU A O     1 
ATOM   15206 C  CB    . LEU A 1 3567 ? 164.776 127.410 138.778 1.00 86.71  ? 3567 LEU A CB    1 
ATOM   15207 C  CG    . LEU A 1 3567 ? 164.057 127.437 140.128 1.00 83.40  ? 3567 LEU A CG    1 
ATOM   15208 C  CD1   . LEU A 1 3567 ? 163.632 128.853 140.481 1.00 84.75  ? 3567 LEU A CD1   1 
ATOM   15209 C  CD2   . LEU A 1 3567 ? 162.860 126.501 140.125 1.00 83.45  ? 3567 LEU A CD2   1 
ATOM   15210 N  N     . PRO A 1 3568 ? 167.472 127.088 140.886 1.00 91.81  ? 3568 PRO A N     1 
ATOM   15211 C  CA    . PRO A 1 3568 ? 168.166 126.141 141.768 1.00 90.55  ? 3568 PRO A CA    1 
ATOM   15212 C  C     . PRO A 1 3568 ? 167.246 125.016 142.220 1.00 87.69  ? 3568 PRO A C     1 
ATOM   15213 O  O     . PRO A 1 3568 ? 166.055 125.219 142.462 1.00 91.41  ? 3568 PRO A O     1 
ATOM   15214 C  CB    . PRO A 1 3568 ? 168.615 127.012 142.947 1.00 88.55  ? 3568 PRO A CB    1 
ATOM   15215 C  CG    . PRO A 1 3568 ? 167.785 128.251 142.865 1.00 86.72  ? 3568 PRO A CG    1 
ATOM   15216 C  CD    . PRO A 1 3568 ? 167.481 128.459 141.420 1.00 89.48  ? 3568 PRO A CD    1 
ATOM   15217 N  N     . ALA A 1 3569 ? 167.816 123.818 142.330 1.00 84.49  ? 3569 ALA A N     1 
ATOM   15218 C  CA    . ALA A 1 3569 ? 167.062 122.617 142.684 1.00 88.73  ? 3569 ALA A CA    1 
ATOM   15219 C  C     . ALA A 1 3569 ? 166.888 122.573 144.196 1.00 92.10  ? 3569 ALA A C     1 
ATOM   15220 O  O     . ALA A 1 3569 ? 167.728 122.049 144.929 1.00 93.02  ? 3569 ALA A O     1 
ATOM   15221 C  CB    . ALA A 1 3569 ? 167.765 121.369 142.166 1.00 88.50  ? 3569 ALA A CB    1 
ATOM   15222 N  N     . ASP A 1 3570 ? 165.777 123.131 144.668 1.00 93.05  ? 3570 ASP A N     1 
ATOM   15223 C  CA    . ASP A 1 3570 ? 165.455 123.128 146.087 1.00 89.93  ? 3570 ASP A CA    1 
ATOM   15224 C  C     . ASP A 1 3570 ? 163.945 123.045 146.248 1.00 91.14  ? 3570 ASP A C     1 
ATOM   15225 O  O     . ASP A 1 3570 ? 163.189 123.495 145.384 1.00 95.45  ? 3570 ASP A O     1 
ATOM   15226 C  CB    . ASP A 1 3570 ? 165.993 124.378 146.793 1.00 89.40  ? 3570 ASP A CB    1 
ATOM   15227 C  CG    . ASP A 1 3570 ? 165.945 124.263 148.306 1.00 94.37  ? 3570 ASP A CG    1 
ATOM   15228 O  OD1   . ASP A 1 3570 ? 166.443 125.183 148.987 1.00 94.05  ? 3570 ASP A OD1   1 
ATOM   15229 O  OD2   . ASP A 1 3570 ? 165.418 123.253 148.816 1.00 98.50  ? 3570 ASP A OD2   1 
ATOM   15230 N  N     . ASP A 1 3571 ? 163.514 122.458 147.367 1.00 89.88  ? 3571 ASP A N     1 
ATOM   15231 C  CA    . ASP A 1 3571 ? 162.090 122.435 147.681 1.00 86.53  ? 3571 ASP A CA    1 
ATOM   15232 C  C     . ASP A 1 3571 ? 161.561 123.843 147.917 1.00 85.62  ? 3571 ASP A C     1 
ATOM   15233 O  O     . ASP A 1 3571 ? 160.474 124.195 147.443 1.00 92.00  ? 3571 ASP A O     1 
ATOM   15234 C  CB    . ASP A 1 3571 ? 161.835 121.552 148.901 1.00 89.59  ? 3571 ASP A CB    1 
ATOM   15235 C  CG    . ASP A 1 3571 ? 161.572 120.107 148.528 1.00 92.83  ? 3571 ASP A CG    1 
ATOM   15236 O  OD1   . ASP A 1 3571 ? 161.479 119.814 147.318 1.00 89.55  ? 3571 ASP A OD1   1 
ATOM   15237 O  OD2   . ASP A 1 3571 ? 161.459 119.266 149.444 1.00 94.36  ? 3571 ASP A OD2   1 
ATOM   15238 N  N     . LEU A 1 3572 ? 162.319 124.664 148.646 1.00 72.04  ? 3572 LEU A N     1 
ATOM   15239 C  CA    . LEU A 1 3572 ? 161.915 126.049 148.864 1.00 75.83  ? 3572 LEU A CA    1 
ATOM   15240 C  C     . LEU A 1 3572 ? 161.863 126.818 147.550 1.00 80.76  ? 3572 LEU A C     1 
ATOM   15241 O  O     . LEU A 1 3572 ? 160.929 127.592 147.311 1.00 86.12  ? 3572 LEU A O     1 
ATOM   15242 C  CB    . LEU A 1 3572 ? 162.872 126.723 149.846 1.00 74.63  ? 3572 LEU A CB    1 
ATOM   15243 C  CG    . LEU A 1 3572 ? 162.466 128.101 150.369 1.00 72.94  ? 3572 LEU A CG    1 
ATOM   15244 C  CD1   . LEU A 1 3572 ? 162.646 128.172 151.874 1.00 74.94  ? 3572 LEU A CD1   1 
ATOM   15245 C  CD2   . LEU A 1 3572 ? 163.271 129.191 149.684 1.00 75.27  ? 3572 LEU A CD2   1 
ATOM   15246 N  N     . CYS A 1 3573 ? 162.853 126.611 146.681 1.00 74.29  ? 3573 CYS A N     1 
ATOM   15247 C  CA    . CYS A 1 3573 ? 162.850 127.294 145.392 1.00 70.99  ? 3573 CYS A CA    1 
ATOM   15248 C  C     . CYS A 1 3573 ? 161.727 126.783 144.499 1.00 74.19  ? 3573 CYS A C     1 
ATOM   15249 O  O     . CYS A 1 3573 ? 161.147 127.552 143.725 1.00 86.15  ? 3573 CYS A O     1 
ATOM   15250 C  CB    . CYS A 1 3573 ? 164.207 127.130 144.712 1.00 75.98  ? 3573 CYS A CB    1 
ATOM   15251 S  SG    . CYS A 1 3573 ? 165.557 127.954 145.584 1.00 86.82  ? 3573 CYS A SG    1 
ATOM   15252 N  N     . THR A 1 3574 ? 161.400 125.492 144.592 1.00 63.98  ? 3574 THR A N     1 
ATOM   15253 C  CA    . THR A 1 3574 ? 160.262 124.969 143.842 1.00 65.97  ? 3574 THR A CA    1 
ATOM   15254 C  C     . THR A 1 3574 ? 158.958 125.602 144.313 1.00 74.84  ? 3574 THR A C     1 
ATOM   15255 O  O     . THR A 1 3574 ? 158.108 125.976 143.496 1.00 80.69  ? 3574 THR A O     1 
ATOM   15256 C  CB    . THR A 1 3574 ? 160.199 123.448 143.974 1.00 72.95  ? 3574 THR A CB    1 
ATOM   15257 O  OG1   . THR A 1 3574 ? 161.410 122.873 143.469 1.00 82.60  ? 3574 THR A OG1   1 
ATOM   15258 C  CG2   . THR A 1 3574 ? 159.023 122.894 143.189 1.00 72.80  ? 3574 THR A CG2   1 
ATOM   15259 N  N     . GLU A 1 3575 ? 158.788 125.738 145.631 1.00 75.44  ? 3575 GLU A N     1 
ATOM   15260 C  CA    . GLU A 1 3575 ? 157.606 126.414 146.156 1.00 70.16  ? 3575 GLU A CA    1 
ATOM   15261 C  C     . GLU A 1 3575 ? 157.559 127.865 145.697 1.00 77.49  ? 3575 GLU A C     1 
ATOM   15262 O  O     . GLU A 1 3575 ? 156.491 128.381 145.348 1.00 87.70  ? 3575 GLU A O     1 
ATOM   15263 C  CB    . GLU A 1 3575 ? 157.596 126.339 147.682 1.00 67.75  ? 3575 GLU A CB    1 
ATOM   15264 C  CG    . GLU A 1 3575 ? 157.466 124.937 148.236 1.00 73.63  ? 3575 GLU A CG    1 
ATOM   15265 C  CD    . GLU A 1 3575 ? 157.987 124.829 149.653 1.00 83.74  ? 3575 GLU A CD    1 
ATOM   15266 O  OE1   . GLU A 1 3575 ? 158.449 125.855 150.195 1.00 86.30  ? 3575 GLU A OE1   1 
ATOM   15267 O  OE2   . GLU A 1 3575 ? 157.936 123.721 150.227 1.00 85.39  ? 3575 GLU A OE2   1 
ATOM   15268 N  N     . ASN A 1 3576 ? 158.710 128.539 145.695 1.00 66.09  ? 3576 ASN A N     1 
ATOM   15269 C  CA    . ASN A 1 3576 ? 158.754 129.928 145.255 1.00 60.23  ? 3576 ASN A CA    1 
ATOM   15270 C  C     . ASN A 1 3576 ? 158.389 130.053 143.781 1.00 65.39  ? 3576 ASN A C     1 
ATOM   15271 O  O     . ASN A 1 3576 ? 157.689 130.991 143.386 1.00 81.43  ? 3576 ASN A O     1 
ATOM   15272 C  CB    . ASN A 1 3576 ? 160.136 130.517 145.526 1.00 61.93  ? 3576 ASN A CB    1 
ATOM   15273 C  CG    . ASN A 1 3576 ? 160.424 130.662 147.005 1.00 70.04  ? 3576 ASN A CG    1 
ATOM   15274 O  OD1   . ASN A 1 3576 ? 159.549 130.446 147.843 1.00 68.37  ? 3576 ASN A OD1   1 
ATOM   15275 N  ND2   . ASN A 1 3576 ? 161.655 131.032 147.336 1.00 72.98  ? 3576 ASN A ND2   1 
ATOM   15276 N  N     . ALA A 1 3577 ? 158.854 129.118 142.950 1.00 54.49  ? 3577 ALA A N     1 
ATOM   15277 C  CA    . ALA A 1 3577 ? 158.473 129.127 141.541 1.00 56.17  ? 3577 ALA A CA    1 
ATOM   15278 C  C     . ALA A 1 3577 ? 156.979 128.878 141.372 1.00 62.35  ? 3577 ALA A C     1 
ATOM   15279 O  O     . ALA A 1 3577 ? 156.327 129.511 140.531 1.00 66.28  ? 3577 ALA A O     1 
ATOM   15280 C  CB    . ALA A 1 3577 ? 159.282 128.085 140.771 1.00 67.23  ? 3577 ALA A CB    1 
ATOM   15281 N  N     . ILE A 1 3578 ? 156.422 127.956 142.161 1.00 67.93  ? 3578 ILE A N     1 
ATOM   15282 C  CA    . ILE A 1 3578 ? 154.983 127.708 142.119 1.00 63.43  ? 3578 ILE A CA    1 
ATOM   15283 C  C     . ILE A 1 3578 ? 154.217 128.979 142.461 1.00 64.95  ? 3578 ILE A C     1 
ATOM   15284 O  O     . ILE A 1 3578 ? 153.219 129.316 141.812 1.00 69.00  ? 3578 ILE A O     1 
ATOM   15285 C  CB    . ILE A 1 3578 ? 154.614 126.551 143.066 1.00 58.74  ? 3578 ILE A CB    1 
ATOM   15286 C  CG1   . ILE A 1 3578 ? 155.030 125.211 142.460 1.00 67.55  ? 3578 ILE A CG1   1 
ATOM   15287 C  CG2   . ILE A 1 3578 ? 153.128 126.557 143.369 1.00 64.85  ? 3578 ILE A CG2   1 
ATOM   15288 C  CD1   . ILE A 1 3578 ? 155.113 124.091 143.467 1.00 68.86  ? 3578 ILE A CD1   1 
ATOM   15289 N  N     . MET A 1 3579 ? 154.675 129.704 143.482 1.00 60.90  ? 3579 MET A N     1 
ATOM   15290 C  CA    . MET A 1 3579 ? 154.054 130.981 143.823 1.00 54.54  ? 3579 MET A CA    1 
ATOM   15291 C  C     . MET A 1 3579 ? 154.192 131.983 142.683 1.00 61.20  ? 3579 MET A C     1 
ATOM   15292 O  O     . MET A 1 3579 ? 153.245 132.712 142.368 1.00 71.15  ? 3579 MET A O     1 
ATOM   15293 C  CB    . MET A 1 3579 ? 154.676 131.541 145.101 1.00 49.17  ? 3579 MET A CB    1 
ATOM   15294 C  CG    . MET A 1 3579 ? 154.549 130.626 146.298 1.00 57.37  ? 3579 MET A CG    1 
ATOM   15295 S  SD    . MET A 1 3579 ? 154.915 131.464 147.843 1.00 75.29  ? 3579 MET A SD    1 
ATOM   15296 C  CE    . MET A 1 3579 ? 154.914 130.080 148.977 1.00 64.29  ? 3579 MET A CE    1 
ATOM   15297 N  N     . LEU A 1 3580 ? 155.369 132.034 142.055 1.00 56.57  ? 3580 LEU A N     1 
ATOM   15298 C  CA    . LEU A 1 3580 ? 155.596 132.950 140.944 1.00 51.24  ? 3580 LEU A CA    1 
ATOM   15299 C  C     . LEU A 1 3580 ? 154.761 132.599 139.722 1.00 55.87  ? 3580 LEU A C     1 
ATOM   15300 O  O     . LEU A 1 3580 ? 154.613 133.437 138.828 1.00 59.77  ? 3580 LEU A O     1 
ATOM   15301 C  CB    . LEU A 1 3580 ? 157.076 132.968 140.564 1.00 49.54  ? 3580 LEU A CB    1 
ATOM   15302 C  CG    . LEU A 1 3580 ? 158.028 133.719 141.494 1.00 50.02  ? 3580 LEU A CG    1 
ATOM   15303 C  CD1   . LEU A 1 3580 ? 159.469 133.501 141.066 1.00 54.66  ? 3580 LEU A CD1   1 
ATOM   15304 C  CD2   . LEU A 1 3580 ? 157.693 135.199 141.520 1.00 48.53  ? 3580 LEU A CD2   1 
ATOM   15305 N  N     . LYS A 1 3581 ? 154.234 131.378 139.650 1.00 63.29  ? 3581 LYS A N     1 
ATOM   15306 C  CA    . LYS A 1 3581 ? 153.328 131.033 138.561 1.00 66.54  ? 3581 LYS A CA    1 
ATOM   15307 C  C     . LYS A 1 3581 ? 151.867 131.281 138.920 1.00 70.69  ? 3581 LYS A C     1 
ATOM   15308 O  O     . LYS A 1 3581 ? 151.118 131.841 138.112 1.00 73.34  ? 3581 LYS A O     1 
ATOM   15309 C  CB    . LYS A 1 3581 ? 153.510 129.568 138.160 1.00 68.96  ? 3581 LYS A CB    1 
ATOM   15310 C  CG    . LYS A 1 3581 ? 152.352 129.019 137.348 1.00 66.62  ? 3581 LYS A CG    1 
ATOM   15311 C  CD    . LYS A 1 3581 ? 152.496 127.533 137.112 1.00 66.12  ? 3581 LYS A CD    1 
ATOM   15312 C  CE    . LYS A 1 3581 ? 152.073 126.747 138.342 1.00 67.67  ? 3581 LYS A CE    1 
ATOM   15313 N  NZ    . LYS A 1 3581 ? 151.606 125.378 137.992 1.00 71.18  ? 3581 LYS A NZ    1 
ATOM   15314 N  N     . ARG A 1 3582 ? 151.448 130.883 140.122 1.00 70.74  ? 3582 ARG A N     1 
ATOM   15315 C  CA    . ARG A 1 3582 ? 150.051 130.940 140.536 1.00 63.96  ? 3582 ARG A CA    1 
ATOM   15316 C  C     . ARG A 1 3582 ? 149.736 132.181 141.363 1.00 69.19  ? 3582 ARG A C     1 
ATOM   15317 O  O     . ARG A 1 3582 ? 148.823 132.150 142.193 1.00 74.95  ? 3582 ARG A O     1 
ATOM   15318 C  CB    . ARG A 1 3582 ? 149.684 129.682 141.322 1.00 61.79  ? 3582 ARG A CB    1 
ATOM   15319 C  CG    . ARG A 1 3582 ? 149.757 128.399 140.519 1.00 65.47  ? 3582 ARG A CG    1 
ATOM   15320 C  CD    . ARG A 1 3582 ? 149.553 127.184 141.405 1.00 67.43  ? 3582 ARG A CD    1 
ATOM   15321 N  NE    . ARG A 1 3582 ? 149.515 125.945 140.638 1.00 72.28  ? 3582 ARG A NE    1 
ATOM   15322 C  CZ    . ARG A 1 3582 ? 148.453 125.505 139.978 1.00 72.86  ? 3582 ARG A CZ    1 
ATOM   15323 N  NH1   . ARG A 1 3582 ? 147.315 126.180 139.968 1.00 68.17  ? 3582 ARG A NH1   1 
ATOM   15324 N  NH2   . ARG A 1 3582 ? 148.533 124.356 139.312 1.00 72.20  ? 3582 ARG A NH2   1 
ATOM   15325 N  N     . PHE A 1 3583 ? 150.475 133.267 141.162 1.00 69.57  ? 3583 PHE A N     1 
ATOM   15326 C  CA    . PHE A 1 3583 ? 150.256 134.470 141.953 1.00 67.17  ? 3583 PHE A CA    1 
ATOM   15327 C  C     . PHE A 1 3583 ? 148.927 135.121 141.590 1.00 72.95  ? 3583 PHE A C     1 
ATOM   15328 O  O     . PHE A 1 3583 ? 148.538 135.171 140.421 1.00 72.73  ? 3583 PHE A O     1 
ATOM   15329 C  CB    . PHE A 1 3583 ? 151.402 135.461 141.745 1.00 64.28  ? 3583 PHE A CB    1 
ATOM   15330 C  CG    . PHE A 1 3583 ? 151.523 135.968 140.334 1.00 67.50  ? 3583 PHE A CG    1 
ATOM   15331 C  CD1   . PHE A 1 3583 ? 152.269 135.275 139.399 1.00 72.85  ? 3583 PHE A CD1   1 
ATOM   15332 C  CD2   . PHE A 1 3583 ? 150.906 137.145 139.949 1.00 71.53  ? 3583 PHE A CD2   1 
ATOM   15333 C  CE1   . PHE A 1 3583 ? 152.387 135.738 138.104 1.00 73.54  ? 3583 PHE A CE1   1 
ATOM   15334 C  CE2   . PHE A 1 3583 ? 151.020 137.613 138.655 1.00 73.67  ? 3583 PHE A CE2   1 
ATOM   15335 C  CZ    . PHE A 1 3583 ? 151.762 136.909 137.733 1.00 74.40  ? 3583 PHE A CZ    1 
ATOM   15336 N  N     . ASN A 1 3584 ? 148.225 135.616 142.609 1.00 73.40  ? 3584 ASN A N     1 
ATOM   15337 C  CA    . ASN A 1 3584 ? 147.025 136.418 142.396 1.00 70.04  ? 3584 ASN A CA    1 
ATOM   15338 C  C     . ASN A 1 3584 ? 147.379 137.902 142.366 1.00 70.56  ? 3584 ASN A C     1 
ATOM   15339 O  O     . ASN A 1 3584 ? 147.118 138.591 141.375 1.00 78.47  ? 3584 ASN A O     1 
ATOM   15340 C  CB    . ASN A 1 3584 ? 145.990 136.120 143.486 1.00 68.33  ? 3584 ASN A CB    1 
ATOM   15341 C  CG    . ASN A 1 3584 ? 144.590 136.535 143.087 1.00 74.40  ? 3584 ASN A CG    1 
ATOM   15342 O  OD1   . ASN A 1 3584 ? 144.362 137.665 142.658 1.00 78.70  ? 3584 ASN A OD1   1 
ATOM   15343 N  ND2   . ASN A 1 3584 ? 143.642 135.616 143.220 1.00 75.58  ? 3584 ASN A ND2   1 
ATOM   15344 N  N     . ARG A 1 3585 ? 147.971 138.401 143.445 1.00 56.51  ? 3585 ARG A N     1 
ATOM   15345 C  CA    . ARG A 1 3585 ? 148.587 139.716 143.427 1.00 60.87  ? 3585 ARG A CA    1 
ATOM   15346 C  C     . ARG A 1 3585 ? 149.972 139.623 142.800 1.00 61.79  ? 3585 ARG A C     1 
ATOM   15347 O  O     . ARG A 1 3585 ? 150.583 138.552 142.753 1.00 68.35  ? 3585 ARG A O     1 
ATOM   15348 C  CB    . ARG A 1 3585 ? 148.684 140.291 144.840 1.00 61.10  ? 3585 ARG A CB    1 
ATOM   15349 C  CG    . ARG A 1 3585 ? 147.348 140.693 145.436 1.00 61.65  ? 3585 ARG A CG    1 
ATOM   15350 C  CD    . ARG A 1 3585 ? 147.463 140.957 146.928 1.00 65.20  ? 3585 ARG A CD    1 
ATOM   15351 N  NE    . ARG A 1 3585 ? 147.962 139.793 147.649 1.00 62.71  ? 3585 ARG A NE    1 
ATOM   15352 C  CZ    . ARG A 1 3585 ? 148.428 139.824 148.890 1.00 61.50  ? 3585 ARG A CZ    1 
ATOM   15353 N  NH1   . ARG A 1 3585 ? 148.472 140.949 149.584 1.00 57.33  ? 3585 ARG A NH1   1 
ATOM   15354 N  NH2   . ARG A 1 3585 ? 148.857 138.696 149.450 1.00 60.35  ? 3585 ARG A NH2   1 
ATOM   15355 N  N     . TYR A 1 3586 ? 150.459 140.752 142.303 1.00 66.60  ? 3586 TYR A N     1 
ATOM   15356 C  CA    . TYR A 1 3586 ? 151.752 140.759 141.637 1.00 65.24  ? 3586 TYR A CA    1 
ATOM   15357 C  C     . TYR A 1 3586 ? 152.862 140.463 142.643 1.00 74.56  ? 3586 TYR A C     1 
ATOM   15358 O  O     . TYR A 1 3586 ? 152.844 140.984 143.762 1.00 85.16  ? 3586 TYR A O     1 
ATOM   15359 C  CB    . TYR A 1 3586 ? 151.989 142.101 140.953 1.00 59.34  ? 3586 TYR A CB    1 
ATOM   15360 C  CG    . TYR A 1 3586 ? 151.059 142.327 139.786 1.00 69.07  ? 3586 TYR A CG    1 
ATOM   15361 C  CD1   . TYR A 1 3586 ? 150.999 141.418 138.739 1.00 69.32  ? 3586 TYR A CD1   1 
ATOM   15362 C  CD2   . TYR A 1 3586 ? 150.230 143.437 139.737 1.00 74.64  ? 3586 TYR A CD2   1 
ATOM   15363 C  CE1   . TYR A 1 3586 ? 150.146 141.615 137.672 1.00 71.75  ? 3586 TYR A CE1   1 
ATOM   15364 C  CE2   . TYR A 1 3586 ? 149.375 143.642 138.673 1.00 72.91  ? 3586 TYR A CE2   1 
ATOM   15365 C  CZ    . TYR A 1 3586 ? 149.337 142.728 137.644 1.00 73.86  ? 3586 TYR A CZ    1 
ATOM   15366 O  OH    . TYR A 1 3586 ? 148.486 142.929 136.582 1.00 76.95  ? 3586 TYR A OH    1 
ATOM   15367 N  N     . PRO A 1 3587 ? 153.835 139.633 142.280 1.00 62.67  ? 3587 PRO A N     1 
ATOM   15368 C  CA    . PRO A 1 3587 ? 154.801 139.146 143.267 1.00 56.86  ? 3587 PRO A CA    1 
ATOM   15369 C  C     . PRO A 1 3587 ? 155.899 140.151 143.569 1.00 55.03  ? 3587 PRO A C     1 
ATOM   15370 O  O     . PRO A 1 3587 ? 156.352 140.904 142.704 1.00 62.14  ? 3587 PRO A O     1 
ATOM   15371 C  CB    . PRO A 1 3587 ? 155.384 137.889 142.604 1.00 57.41  ? 3587 PRO A CB    1 
ATOM   15372 C  CG    . PRO A 1 3587 ? 154.609 137.690 141.322 1.00 58.42  ? 3587 PRO A CG    1 
ATOM   15373 C  CD    . PRO A 1 3587 ? 154.044 139.017 140.963 1.00 63.36  ? 3587 PRO A CD    1 
ATOM   15374 N  N     . LEU A 1 3588 ? 156.325 140.147 144.829 1.00 56.36  ? 3588 LEU A N     1 
ATOM   15375 C  CA    . LEU A 1 3588 ? 157.508 140.871 145.279 1.00 57.68  ? 3588 LEU A CA    1 
ATOM   15376 C  C     . LEU A 1 3588 ? 158.576 139.831 145.590 1.00 64.18  ? 3588 LEU A C     1 
ATOM   15377 O  O     . LEU A 1 3588 ? 158.412 139.021 146.508 1.00 71.97  ? 3588 LEU A O     1 
ATOM   15378 C  CB    . LEU A 1 3588 ? 157.201 141.737 146.499 1.00 61.30  ? 3588 LEU A CB    1 
ATOM   15379 C  CG    . LEU A 1 3588 ? 158.220 142.824 146.854 1.00 55.72  ? 3588 LEU A CG    1 
ATOM   15380 C  CD1   . LEU A 1 3588 ? 157.530 143.997 147.519 1.00 63.15  ? 3588 LEU A CD1   1 
ATOM   15381 C  CD2   . LEU A 1 3588 ? 159.314 142.281 147.757 1.00 56.06  ? 3588 LEU A CD2   1 
ATOM   15382 N  N     . ILE A 1 3589 ? 159.664 139.853 144.828 1.00 63.24  ? 3589 ILE A N     1 
ATOM   15383 C  CA    . ILE A 1 3589 ? 160.715 138.849 144.926 1.00 60.01  ? 3589 ILE A CA    1 
ATOM   15384 C  C     . ILE A 1 3589 ? 161.849 139.400 145.776 1.00 64.03  ? 3589 ILE A C     1 
ATOM   15385 O  O     . ILE A 1 3589 ? 162.339 140.509 145.531 1.00 73.33  ? 3589 ILE A O     1 
ATOM   15386 C  CB    . ILE A 1 3589 ? 161.223 138.441 143.533 1.00 56.71  ? 3589 ILE A CB    1 
ATOM   15387 C  CG1   . ILE A 1 3589 ? 160.054 138.012 142.648 1.00 59.71  ? 3589 ILE A CG1   1 
ATOM   15388 C  CG2   . ILE A 1 3589 ? 162.237 137.324 143.649 1.00 65.20  ? 3589 ILE A CG2   1 
ATOM   15389 C  CD1   . ILE A 1 3589 ? 160.425 137.833 141.198 1.00 62.11  ? 3589 ILE A CD1   1 
ATOM   15390 N  N     . ILE A 1 3590 ? 162.263 138.631 146.778 1.00 64.57  ? 3590 ILE A N     1 
ATOM   15391 C  CA    . ILE A 1 3590 ? 163.404 138.969 147.620 1.00 61.70  ? 3590 ILE A CA    1 
ATOM   15392 C  C     . ILE A 1 3590 ? 164.463 137.903 147.382 1.00 67.55  ? 3590 ILE A C     1 
ATOM   15393 O  O     . ILE A 1 3590 ? 164.267 136.735 147.739 1.00 73.01  ? 3590 ILE A O     1 
ATOM   15394 C  CB    . ILE A 1 3590 ? 163.025 139.049 149.104 1.00 60.14  ? 3590 ILE A CB    1 
ATOM   15395 C  CG1   . ILE A 1 3590 ? 161.794 139.935 149.295 1.00 63.74  ? 3590 ILE A CG1   1 
ATOM   15396 C  CG2   . ILE A 1 3590 ? 164.191 139.572 149.919 1.00 63.70  ? 3590 ILE A CG2   1 
ATOM   15397 C  CD1   . ILE A 1 3590 ? 161.218 139.882 150.691 1.00 62.47  ? 3590 ILE A CD1   1 
ATOM   15398 N  N     . ASP A 1 3591 ? 165.585 138.298 146.784 1.00 81.69  ? 3591 ASP A N     1 
ATOM   15399 C  CA    . ASP A 1 3591 ? 166.663 137.363 146.462 1.00 77.83  ? 3591 ASP A CA    1 
ATOM   15400 C  C     . ASP A 1 3591 ? 168.000 138.082 146.581 1.00 76.03  ? 3591 ASP A C     1 
ATOM   15401 O  O     . ASP A 1 3591 ? 168.420 138.799 145.659 1.00 80.41  ? 3591 ASP A O     1 
ATOM   15402 C  CB    . ASP A 1 3591 ? 166.484 136.756 145.072 1.00 75.61  ? 3591 ASP A CB    1 
ATOM   15403 C  CG    . ASP A 1 3591 ? 166.325 137.805 143.990 1.00 80.83  ? 3591 ASP A CG    1 
ATOM   15404 O  OD1   . ASP A 1 3591 ? 165.962 138.953 144.321 1.00 83.97  ? 3591 ASP A OD1   1 
ATOM   15405 O  OD2   . ASP A 1 3591 ? 166.573 137.486 142.809 1.00 88.09  ? 3591 ASP A OD2   1 
ATOM   15406 N  N     . PRO A 1 3592 ? 168.695 137.927 147.708 1.00 80.48  ? 3592 PRO A N     1 
ATOM   15407 C  CA    . PRO A 1 3592 ? 170.045 138.504 147.813 1.00 84.41  ? 3592 PRO A CA    1 
ATOM   15408 C  C     . PRO A 1 3592 ? 171.018 137.941 146.792 1.00 86.62  ? 3592 PRO A C     1 
ATOM   15409 O  O     . PRO A 1 3592 ? 171.905 138.668 146.329 1.00 82.06  ? 3592 PRO A O     1 
ATOM   15410 C  CB    . PRO A 1 3592 ? 170.465 138.159 149.249 1.00 85.66  ? 3592 PRO A CB    1 
ATOM   15411 C  CG    . PRO A 1 3592 ? 169.582 137.022 149.651 1.00 85.30  ? 3592 PRO A CG    1 
ATOM   15412 C  CD    . PRO A 1 3592 ? 168.286 137.231 148.939 1.00 82.39  ? 3592 PRO A CD    1 
ATOM   15413 N  N     . SER A 1 3593 ? 170.875 136.666 146.423 1.00 95.75  ? 3593 SER A N     1 
ATOM   15414 C  CA    . SER A 1 3593 ? 171.808 136.047 145.489 1.00 93.47  ? 3593 SER A CA    1 
ATOM   15415 C  C     . SER A 1 3593 ? 171.573 136.483 144.049 1.00 94.46  ? 3593 SER A C     1 
ATOM   15416 O  O     . SER A 1 3593 ? 172.479 136.349 143.221 1.00 98.58  ? 3593 SER A O     1 
ATOM   15417 C  CB    . SER A 1 3593 ? 171.717 134.524 145.587 1.00 90.99  ? 3593 SER A CB    1 
ATOM   15418 O  OG    . SER A 1 3593 ? 172.066 134.075 146.884 1.00 94.93  ? 3593 SER A OG    1 
ATOM   15419 N  N     . GLY A 1 3594 ? 170.386 136.995 143.730 1.00 90.49  ? 3594 GLY A N     1 
ATOM   15420 C  CA    . GLY A 1 3594 ? 170.081 137.422 142.382 1.00 87.07  ? 3594 GLY A CA    1 
ATOM   15421 C  C     . GLY A 1 3594 ? 169.697 136.316 141.424 1.00 91.19  ? 3594 GLY A C     1 
ATOM   15422 O  O     . GLY A 1 3594 ? 169.517 136.591 140.231 1.00 90.91  ? 3594 GLY A O     1 
ATOM   15423 N  N     . GLN A 1 3595 ? 169.565 135.076 141.900 1.00 95.32  ? 3595 GLN A N     1 
ATOM   15424 C  CA    . GLN A 1 3595 ? 169.212 133.976 141.009 1.00 92.55  ? 3595 GLN A CA    1 
ATOM   15425 C  C     . GLN A 1 3595 ? 167.750 134.036 140.586 1.00 92.18  ? 3595 GLN A C     1 
ATOM   15426 O  O     . GLN A 1 3595 ? 167.418 133.656 139.457 1.00 95.37  ? 3595 GLN A O     1 
ATOM   15427 C  CB    . GLN A 1 3595 ? 169.511 132.637 141.684 1.00 91.63  ? 3595 GLN A CB    1 
ATOM   15428 C  CG    . GLN A 1 3595 ? 170.850 132.029 141.300 1.00 97.55  ? 3595 GLN A CG    1 
ATOM   15429 C  CD    . GLN A 1 3595 ? 170.910 131.617 139.842 1.00 100.37 ? 3595 GLN A CD    1 
ATOM   15430 O  OE1   . GLN A 1 3595 ? 169.882 131.394 139.203 1.00 99.74  ? 3595 GLN A OE1   1 
ATOM   15431 N  NE2   . GLN A 1 3595 ? 172.121 131.513 139.308 1.00 97.44  ? 3595 GLN A NE2   1 
ATOM   15432 N  N     . ALA A 1 3596 ? 166.867 134.497 141.475 1.00 78.02  ? 3596 ALA A N     1 
ATOM   15433 C  CA    . ALA A 1 3596 ? 165.448 134.562 141.144 1.00 76.03  ? 3596 ALA A CA    1 
ATOM   15434 C  C     . ALA A 1 3596 ? 165.187 135.548 140.013 1.00 79.69  ? 3596 ALA A C     1 
ATOM   15435 O  O     . ALA A 1 3596 ? 164.336 135.303 139.151 1.00 85.87  ? 3596 ALA A O     1 
ATOM   15436 C  CB    . ALA A 1 3596 ? 164.637 134.938 142.381 1.00 77.27  ? 3596 ALA A CB    1 
ATOM   15437 N  N     . THR A 1 3597 ? 165.901 136.675 140.006 1.00 86.12  ? 3597 THR A N     1 
ATOM   15438 C  CA    . THR A 1 3597 ? 165.752 137.637 138.919 1.00 85.50  ? 3597 THR A CA    1 
ATOM   15439 C  C     . THR A 1 3597 ? 166.164 137.027 137.585 1.00 91.06  ? 3597 THR A C     1 
ATOM   15440 O  O     . THR A 1 3597 ? 165.480 137.211 136.570 1.00 93.79  ? 3597 THR A O     1 
ATOM   15441 C  CB    . THR A 1 3597 ? 166.577 138.890 139.216 1.00 86.36  ? 3597 THR A CB    1 
ATOM   15442 O  OG1   . THR A 1 3597 ? 166.034 139.560 140.361 1.00 88.06  ? 3597 THR A OG1   1 
ATOM   15443 C  CG2   . THR A 1 3597 ? 166.564 139.835 138.029 1.00 86.21  ? 3597 THR A CG2   1 
ATOM   15444 N  N     . GLU A 1 3598 ? 167.276 136.289 137.569 1.00 94.65  ? 3598 GLU A N     1 
ATOM   15445 C  CA    . GLU A 1 3598 ? 167.711 135.630 136.342 1.00 92.68  ? 3598 GLU A CA    1 
ATOM   15446 C  C     . GLU A 1 3598 ? 166.702 134.581 135.893 1.00 92.00  ? 3598 GLU A C     1 
ATOM   15447 O  O     . GLU A 1 3598 ? 166.419 134.453 134.696 1.00 96.62  ? 3598 GLU A O     1 
ATOM   15448 C  CB    . GLU A 1 3598 ? 169.089 135.000 136.546 1.00 91.35  ? 3598 GLU A CB    1 
ATOM   15449 C  CG    . GLU A 1 3598 ? 169.799 134.596 135.261 1.00 96.91  ? 3598 GLU A CG    1 
ATOM   15450 C  CD    . GLU A 1 3598 ? 169.676 135.632 134.157 1.00 101.68 ? 3598 GLU A CD    1 
ATOM   15451 O  OE1   . GLU A 1 3598 ? 169.852 136.837 134.437 1.00 101.78 ? 3598 GLU A OE1   1 
ATOM   15452 O  OE2   . GLU A 1 3598 ? 169.402 135.238 133.003 1.00 102.32 ? 3598 GLU A OE2   1 
ATOM   15453 N  N     . PHE A 1 3599 ? 166.151 133.818 136.841 1.00 75.20  ? 3599 PHE A N     1 
ATOM   15454 C  CA    . PHE A 1 3599 ? 165.141 132.824 136.493 1.00 70.91  ? 3599 PHE A CA    1 
ATOM   15455 C  C     . PHE A 1 3599 ? 163.900 133.483 135.905 1.00 74.92  ? 3599 PHE A C     1 
ATOM   15456 O  O     . PHE A 1 3599 ? 163.327 132.986 134.929 1.00 79.61  ? 3599 PHE A O     1 
ATOM   15457 C  CB    . PHE A 1 3599 ? 164.778 131.993 137.724 1.00 73.65  ? 3599 PHE A CB    1 
ATOM   15458 C  CG    . PHE A 1 3599 ? 163.403 131.390 137.667 1.00 72.52  ? 3599 PHE A CG    1 
ATOM   15459 C  CD1   . PHE A 1 3599 ? 163.104 130.394 136.753 1.00 79.69  ? 3599 PHE A CD1   1 
ATOM   15460 C  CD2   . PHE A 1 3599 ? 162.411 131.815 138.533 1.00 75.80  ? 3599 PHE A CD2   1 
ATOM   15461 C  CE1   . PHE A 1 3599 ? 161.842 129.838 136.701 1.00 79.35  ? 3599 PHE A CE1   1 
ATOM   15462 C  CE2   . PHE A 1 3599 ? 161.147 131.263 138.485 1.00 75.90  ? 3599 PHE A CE2   1 
ATOM   15463 C  CZ    . PHE A 1 3599 ? 160.863 130.273 137.569 1.00 75.95  ? 3599 PHE A CZ    1 
ATOM   15464 N  N     . ILE A 1 3600 ? 163.471 134.604 136.488 1.00 83.81  ? 3600 ILE A N     1 
ATOM   15465 C  CA    . ILE A 1 3600 ? 162.312 135.322 135.967 1.00 81.67  ? 3600 ILE A CA    1 
ATOM   15466 C  C     . ILE A 1 3600 ? 162.592 135.838 134.561 1.00 84.30  ? 3600 ILE A C     1 
ATOM   15467 O  O     . ILE A 1 3600 ? 161.747 135.725 133.664 1.00 83.34  ? 3600 ILE A O     1 
ATOM   15468 C  CB    . ILE A 1 3600 ? 161.919 136.461 136.924 1.00 74.47  ? 3600 ILE A CB    1 
ATOM   15469 C  CG1   . ILE A 1 3600 ? 161.135 135.907 138.112 1.00 74.54  ? 3600 ILE A CG1   1 
ATOM   15470 C  CG2   . ILE A 1 3600 ? 161.102 137.516 136.201 1.00 80.88  ? 3600 ILE A CG2   1 
ATOM   15471 C  CD1   . ILE A 1 3600 ? 159.805 135.307 137.730 1.00 76.32  ? 3600 ILE A CD1   1 
ATOM   15472 N  N     . MET A 1 3601 ? 163.780 136.405 134.343 1.00 86.77  ? 3601 MET A N     1 
ATOM   15473 C  CA    . MET A 1 3601 ? 164.118 136.930 133.024 1.00 83.93  ? 3601 MET A CA    1 
ATOM   15474 C  C     . MET A 1 3601 ? 164.173 135.818 131.983 1.00 87.00  ? 3601 MET A C     1 
ATOM   15475 O  O     . MET A 1 3601 ? 163.751 136.010 130.837 1.00 87.81  ? 3601 MET A O     1 
ATOM   15476 C  CB    . MET A 1 3601 ? 165.450 137.677 133.081 1.00 82.47  ? 3601 MET A CB    1 
ATOM   15477 C  CG    . MET A 1 3601 ? 165.367 139.043 133.739 1.00 87.35  ? 3601 MET A CG    1 
ATOM   15478 S  SD    . MET A 1 3601 ? 164.337 140.202 132.819 1.00 100.98 ? 3601 MET A SD    1 
ATOM   15479 C  CE    . MET A 1 3601 ? 165.409 140.586 131.438 1.00 84.94  ? 3601 MET A CE    1 
ATOM   15480 N  N     . ASN A 1 3602 ? 164.694 134.649 132.360 1.00 86.22  ? 3602 ASN A N     1 
ATOM   15481 C  CA    . ASN A 1 3602 ? 164.781 133.544 131.410 1.00 83.09  ? 3602 ASN A CA    1 
ATOM   15482 C  C     . ASN A 1 3602 ? 163.411 132.936 131.132 1.00 83.45  ? 3602 ASN A C     1 
ATOM   15483 O  O     . ASN A 1 3602 ? 163.136 132.506 130.006 1.00 86.68  ? 3602 ASN A O     1 
ATOM   15484 C  CB    . ASN A 1 3602 ? 165.746 132.479 131.929 1.00 83.26  ? 3602 ASN A CB    1 
ATOM   15485 C  CG    . ASN A 1 3602 ? 167.191 132.932 131.884 1.00 85.38  ? 3602 ASN A CG    1 
ATOM   15486 O  OD1   . ASN A 1 3602 ? 167.627 133.559 130.919 1.00 83.57  ? 3602 ASN A OD1   1 
ATOM   15487 N  ND2   . ASN A 1 3602 ? 167.944 132.613 132.929 1.00 88.89  ? 3602 ASN A ND2   1 
ATOM   15488 N  N     . GLU A 1 3603 ? 162.543 132.884 132.145 1.00 83.81  ? 3603 GLU A N     1 
ATOM   15489 C  CA    . GLU A 1 3603 ? 161.225 132.283 131.960 1.00 86.10  ? 3603 GLU A CA    1 
ATOM   15490 C  C     . GLU A 1 3603 ? 160.364 133.101 131.005 1.00 88.75  ? 3603 GLU A C     1 
ATOM   15491 O  O     . GLU A 1 3603 ? 159.709 132.542 130.118 1.00 85.85  ? 3603 GLU A O     1 
ATOM   15492 C  CB    . GLU A 1 3603 ? 160.526 132.129 133.309 1.00 83.54  ? 3603 GLU A CB    1 
ATOM   15493 C  CG    . GLU A 1 3603 ? 159.288 131.252 133.267 1.00 85.29  ? 3603 GLU A CG    1 
ATOM   15494 C  CD    . GLU A 1 3603 ? 159.619 129.775 133.325 1.00 89.70  ? 3603 GLU A CD    1 
ATOM   15495 O  OE1   . GLU A 1 3603 ? 160.792 129.438 133.588 1.00 90.46  ? 3603 GLU A OE1   1 
ATOM   15496 O  OE2   . GLU A 1 3603 ? 158.707 128.951 133.106 1.00 91.66  ? 3603 GLU A OE2   1 
ATOM   15497 N  N     . TYR A 1 3604 ? 160.352 134.424 131.168 1.00 93.48  ? 3604 TYR A N     1 
ATOM   15498 C  CA    . TYR A 1 3604 ? 159.542 135.308 130.343 1.00 91.45  ? 3604 TYR A CA    1 
ATOM   15499 C  C     . TYR A 1 3604 ? 160.339 135.928 129.201 1.00 93.47  ? 3604 TYR A C     1 
ATOM   15500 O  O     . TYR A 1 3604 ? 159.950 136.978 128.679 1.00 89.19  ? 3604 TYR A O     1 
ATOM   15501 C  CB    . TYR A 1 3604 ? 158.913 136.403 131.206 1.00 89.05  ? 3604 TYR A CB    1 
ATOM   15502 C  CG    . TYR A 1 3604 ? 157.815 135.907 132.120 1.00 90.27  ? 3604 TYR A CG    1 
ATOM   15503 C  CD1   . TYR A 1 3604 ? 158.114 135.247 133.304 1.00 92.34  ? 3604 TYR A CD1   1 
ATOM   15504 C  CD2   . TYR A 1 3604 ? 156.479 136.102 131.801 1.00 92.19  ? 3604 TYR A CD2   1 
ATOM   15505 C  CE1   . TYR A 1 3604 ? 157.113 134.793 134.141 1.00 93.96  ? 3604 TYR A CE1   1 
ATOM   15506 C  CE2   . TYR A 1 3604 ? 155.471 135.652 132.632 1.00 90.14  ? 3604 TYR A CE2   1 
ATOM   15507 C  CZ    . TYR A 1 3604 ? 155.795 134.998 133.801 1.00 92.26  ? 3604 TYR A CZ    1 
ATOM   15508 O  OH    . TYR A 1 3604 ? 154.795 134.548 134.631 1.00 92.28  ? 3604 TYR A OH    1 
ATOM   15509 N  N     . LYS A 1 3605 ? 161.450 135.300 128.808 1.00 102.73 ? 3605 LYS A N     1 
ATOM   15510 C  CA    . LYS A 1 3605 ? 162.257 135.829 127.713 1.00 99.40  ? 3605 LYS A CA    1 
ATOM   15511 C  C     . LYS A 1 3605 ? 161.491 135.807 126.396 1.00 103.92 ? 3605 LYS A C     1 
ATOM   15512 O  O     . LYS A 1 3605 ? 161.567 136.759 125.611 1.00 105.01 ? 3605 LYS A O     1 
ATOM   15513 C  CB    . LYS A 1 3605 ? 163.558 135.037 127.596 1.00 97.21  ? 3605 LYS A CB    1 
ATOM   15514 C  CG    . LYS A 1 3605 ? 164.172 135.042 126.207 1.00 102.15 ? 3605 LYS A CG    1 
ATOM   15515 C  CD    . LYS A 1 3605 ? 165.385 134.132 126.139 1.00 104.60 ? 3605 LYS A CD    1 
ATOM   15516 C  CE    . LYS A 1 3605 ? 166.605 134.798 126.750 1.00 105.54 ? 3605 LYS A CE    1 
ATOM   15517 N  NZ    . LYS A 1 3605 ? 167.014 136.008 125.984 1.00 106.39 ? 3605 LYS A NZ    1 
ATOM   15518 N  N     . ASP A 1 3606 ? 160.742 134.732 126.139 1.00 111.85 ? 3606 ASP A N     1 
ATOM   15519 C  CA    . ASP A 1 3606 ? 159.992 134.623 124.893 1.00 110.81 ? 3606 ASP A CA    1 
ATOM   15520 C  C     . ASP A 1 3606 ? 158.876 135.655 124.788 1.00 107.81 ? 3606 ASP A C     1 
ATOM   15521 O  O     . ASP A 1 3606 ? 158.379 135.900 123.684 1.00 107.49 ? 3606 ASP A O     1 
ATOM   15522 C  CB    . ASP A 1 3606 ? 159.434 133.203 124.741 1.00 111.75 ? 3606 ASP A CB    1 
ATOM   15523 C  CG    . ASP A 1 3606 ? 158.462 132.820 125.852 1.00 113.66 ? 3606 ASP A CG    1 
ATOM   15524 O  OD1   . ASP A 1 3606 ? 158.626 131.717 126.416 1.00 111.33 ? 3606 ASP A OD1   1 
ATOM   15525 O  OD2   . ASP A 1 3606 ? 157.528 133.592 126.153 1.00 113.12 ? 3606 ASP A OD2   1 
ATOM   15526 N  N     . ARG A 1 3607 ? 158.471 136.258 125.903 1.00 96.27  ? 3607 ARG A N     1 
ATOM   15527 C  CA    . ARG A 1 3607 ? 157.463 137.308 125.907 1.00 97.41  ? 3607 ARG A CA    1 
ATOM   15528 C  C     . ARG A 1 3607 ? 158.079 138.700 125.962 1.00 98.14  ? 3607 ARG A C     1 
ATOM   15529 O  O     . ARG A 1 3607 ? 157.352 139.683 126.138 1.00 103.11 ? 3607 ARG A O     1 
ATOM   15530 C  CB    . ARG A 1 3607 ? 156.499 137.105 127.078 1.00 100.21 ? 3607 ARG A CB    1 
ATOM   15531 C  CG    . ARG A 1 3607 ? 155.080 137.587 126.813 1.00 97.61  ? 3607 ARG A CG    1 
ATOM   15532 C  CD    . ARG A 1 3607 ? 154.045 136.718 127.513 1.00 98.38  ? 3607 ARG A CD    1 
ATOM   15533 N  NE    . ARG A 1 3607 ? 154.216 135.302 127.209 1.00 102.98 ? 3607 ARG A NE    1 
ATOM   15534 C  CZ    . ARG A 1 3607 ? 154.698 134.404 128.057 1.00 101.98 ? 3607 ARG A CZ    1 
ATOM   15535 N  NH1   . ARG A 1 3607 ? 155.063 134.738 129.283 1.00 97.97  ? 3607 ARG A NH1   1 
ATOM   15536 N  NH2   . ARG A 1 3607 ? 154.817 133.139 127.664 1.00 103.26 ? 3607 ARG A NH2   1 
ATOM   15537 N  N     . LYS A 1 3608 ? 159.402 138.800 125.819 1.00 92.68  ? 3608 LYS A N     1 
ATOM   15538 C  CA    . LYS A 1 3608 ? 160.122 140.073 125.799 1.00 97.98  ? 3608 LYS A CA    1 
ATOM   15539 C  C     . LYS A 1 3608 ? 159.932 140.840 127.110 1.00 95.40  ? 3608 LYS A C     1 
ATOM   15540 O  O     . LYS A 1 3608 ? 159.493 141.991 127.136 1.00 94.68  ? 3608 LYS A O     1 
ATOM   15541 C  CB    . LYS A 1 3608 ? 159.704 140.923 124.592 1.00 97.77  ? 3608 LYS A CB    1 
ATOM   15542 C  CG    . LYS A 1 3608 ? 160.341 140.502 123.273 1.00 100.24 ? 3608 LYS A CG    1 
ATOM   15543 C  CD    . LYS A 1 3608 ? 161.731 139.909 123.471 1.00 99.53  ? 3608 LYS A CD    1 
ATOM   15544 C  CE    . LYS A 1 3608 ? 162.790 140.997 123.581 1.00 96.36  ? 3608 LYS A CE    1 
ATOM   15545 N  NZ    . LYS A 1 3608 ? 164.168 140.441 123.489 1.00 96.87  ? 3608 LYS A NZ    1 
ATOM   15546 N  N     . ILE A 1 3609 ? 160.277 140.170 128.210 1.00 86.34  ? 3609 ILE A N     1 
ATOM   15547 C  CA    . ILE A 1 3609 ? 160.240 140.811 129.518 1.00 84.00  ? 3609 ILE A CA    1 
ATOM   15548 C  C     . ILE A 1 3609 ? 161.321 141.882 129.585 1.00 87.00  ? 3609 ILE A C     1 
ATOM   15549 O  O     . ILE A 1 3609 ? 162.417 141.724 129.029 1.00 88.70  ? 3609 ILE A O     1 
ATOM   15550 C  CB    . ILE A 1 3609 ? 160.402 139.762 130.633 1.00 85.24  ? 3609 ILE A CB    1 
ATOM   15551 C  CG1   . ILE A 1 3609 ? 160.248 140.406 132.012 1.00 84.98  ? 3609 ILE A CG1   1 
ATOM   15552 C  CG2   . ILE A 1 3609 ? 161.737 139.044 130.512 1.00 89.44  ? 3609 ILE A CG2   1 
ATOM   15553 C  CD1   . ILE A 1 3609 ? 160.151 139.405 133.141 1.00 85.57  ? 3609 ILE A CD1   1 
ATOM   15554 N  N     . THR A 1 3610 ? 161.011 142.990 130.253 1.00 90.56  ? 3610 THR A N     1 
ATOM   15555 C  CA    . THR A 1 3610 ? 161.893 144.148 130.312 1.00 88.46  ? 3610 THR A CA    1 
ATOM   15556 C  C     . THR A 1 3610 ? 162.318 144.399 131.751 1.00 85.75  ? 3610 THR A C     1 
ATOM   15557 O  O     . THR A 1 3610 ? 161.471 144.489 132.646 1.00 92.34  ? 3610 THR A O     1 
ATOM   15558 C  CB    . THR A 1 3610 ? 161.206 145.392 129.745 1.00 88.45  ? 3610 THR A CB    1 
ATOM   15559 O  OG1   . THR A 1 3610 ? 160.836 145.156 128.381 1.00 88.78  ? 3610 THR A OG1   1 
ATOM   15560 C  CG2   . THR A 1 3610 ? 162.137 146.592 129.811 1.00 88.56  ? 3610 THR A CG2   1 
ATOM   15561 N  N     . ARG A 1 3611 ? 163.625 144.513 131.967 1.00 82.15  ? 3611 ARG A N     1 
ATOM   15562 C  CA    . ARG A 1 3611 ? 164.157 144.843 133.281 1.00 81.10  ? 3611 ARG A CA    1 
ATOM   15563 C  C     . ARG A 1 3611 ? 164.184 146.355 133.462 1.00 84.96  ? 3611 ARG A C     1 
ATOM   15564 O  O     . ARG A 1 3611 ? 164.644 147.086 132.579 1.00 90.79  ? 3611 ARG A O     1 
ATOM   15565 C  CB    . ARG A 1 3611 ? 165.559 144.261 133.447 1.00 85.74  ? 3611 ARG A CB    1 
ATOM   15566 C  CG    . ARG A 1 3611 ? 166.178 144.501 134.810 1.00 82.94  ? 3611 ARG A CG    1 
ATOM   15567 C  CD    . ARG A 1 3611 ? 167.692 144.611 134.707 1.00 88.01  ? 3611 ARG A CD    1 
ATOM   15568 N  NE    . ARG A 1 3611 ? 168.320 143.335 134.380 1.00 93.88  ? 3611 ARG A NE    1 
ATOM   15569 C  CZ    . ARG A 1 3611 ? 168.418 142.308 135.214 1.00 94.96  ? 3611 ARG A CZ    1 
ATOM   15570 N  NH1   . ARG A 1 3611 ? 167.962 142.376 136.454 1.00 93.12  ? 3611 ARG A NH1   1 
ATOM   15571 N  NH2   . ARG A 1 3611 ? 168.996 141.186 134.795 1.00 91.62  ? 3611 ARG A NH2   1 
ATOM   15572 N  N     . THR A 1 3612 ? 163.692 146.823 134.606 1.00 85.36  ? 3612 THR A N     1 
ATOM   15573 C  CA    . THR A 1 3612 ? 163.597 148.250 134.875 1.00 86.72  ? 3612 THR A CA    1 
ATOM   15574 C  C     . THR A 1 3612 ? 163.869 148.482 136.354 1.00 87.42  ? 3612 THR A C     1 
ATOM   15575 O  O     . THR A 1 3612 ? 163.813 147.557 137.167 1.00 94.44  ? 3612 THR A O     1 
ATOM   15576 C  CB    . THR A 1 3612 ? 162.221 148.804 134.476 1.00 87.29  ? 3612 THR A CB    1 
ATOM   15577 O  OG1   . THR A 1 3612 ? 161.807 148.207 133.242 1.00 86.60  ? 3612 THR A OG1   1 
ATOM   15578 C  CG2   . THR A 1 3612 ? 162.277 150.312 134.284 1.00 86.92  ? 3612 THR A CG2   1 
ATOM   15579 N  N     . SER A 1 3613 ? 164.183 149.730 136.695 1.00 84.63  ? 3613 SER A N     1 
ATOM   15580 C  CA    . SER A 1 3613 ? 164.465 150.116 138.068 1.00 87.06  ? 3613 SER A CA    1 
ATOM   15581 C  C     . SER A 1 3613 ? 163.567 151.276 138.471 1.00 89.84  ? 3613 SER A C     1 
ATOM   15582 O  O     . SER A 1 3613 ? 163.221 152.128 137.648 1.00 92.58  ? 3613 SER A O     1 
ATOM   15583 C  CB    . SER A 1 3613 ? 165.936 150.508 138.247 1.00 90.24  ? 3613 SER A CB    1 
ATOM   15584 O  OG    . SER A 1 3613 ? 166.135 151.191 139.473 1.00 97.05  ? 3613 SER A OG    1 
ATOM   15585 N  N     . PHE A 1 3614 ? 163.186 151.297 139.751 1.00 88.96  ? 3614 PHE A N     1 
ATOM   15586 C  CA    . PHE A 1 3614 ? 162.380 152.401 140.261 1.00 87.47  ? 3614 PHE A CA    1 
ATOM   15587 C  C     . PHE A 1 3614 ? 163.151 153.714 140.245 1.00 91.70  ? 3614 PHE A C     1 
ATOM   15588 O  O     . PHE A 1 3614 ? 162.575 154.766 139.949 1.00 94.48  ? 3614 PHE A O     1 
ATOM   15589 C  CB    . PHE A 1 3614 ? 161.888 152.093 141.675 1.00 88.22  ? 3614 PHE A CB    1 
ATOM   15590 C  CG    . PHE A 1 3614 ? 160.640 151.259 141.715 1.00 88.37  ? 3614 PHE A CG    1 
ATOM   15591 C  CD1   . PHE A 1 3614 ? 159.466 151.723 141.149 1.00 88.14  ? 3614 PHE A CD1   1 
ATOM   15592 C  CD2   . PHE A 1 3614 ? 160.638 150.018 142.325 1.00 89.00  ? 3614 PHE A CD2   1 
ATOM   15593 C  CE1   . PHE A 1 3614 ? 158.317 150.961 141.187 1.00 90.64  ? 3614 PHE A CE1   1 
ATOM   15594 C  CE2   . PHE A 1 3614 ? 159.491 149.252 142.366 1.00 86.89  ? 3614 PHE A CE2   1 
ATOM   15595 C  CZ    . PHE A 1 3614 ? 158.329 149.724 141.796 1.00 89.55  ? 3614 PHE A CZ    1 
ATOM   15596 N  N     . LEU A 1 3615 ? 164.448 153.677 140.563 1.00 97.51  ? 3615 LEU A N     1 
ATOM   15597 C  CA    . LEU A 1 3615 ? 165.261 154.887 140.510 1.00 97.88  ? 3615 LEU A CA    1 
ATOM   15598 C  C     . LEU A 1 3615 ? 165.416 155.419 139.093 1.00 100.78 ? 3615 LEU A C     1 
ATOM   15599 O  O     . LEU A 1 3615 ? 165.655 156.619 138.919 1.00 103.45 ? 3615 LEU A O     1 
ATOM   15600 C  CB    . LEU A 1 3615 ? 166.645 154.632 141.111 1.00 98.29  ? 3615 LEU A CB    1 
ATOM   15601 C  CG    . LEU A 1 3615 ? 166.754 154.391 142.619 1.00 102.77 ? 3615 LEU A CG    1 
ATOM   15602 C  CD1   . LEU A 1 3615 ? 165.749 155.242 143.378 1.00 100.21 ? 3615 LEU A CD1   1 
ATOM   15603 C  CD2   . LEU A 1 3615 ? 166.590 152.921 142.958 1.00 99.39  ? 3615 LEU A CD2   1 
ATOM   15604 N  N     . ASP A 1 3616 ? 165.294 154.560 138.085 1.00 107.27 ? 3616 ASP A N     1 
ATOM   15605 C  CA    . ASP A 1 3616 ? 165.443 154.996 136.704 1.00 107.32 ? 3616 ASP A CA    1 
ATOM   15606 C  C     . ASP A 1 3616 ? 164.347 155.985 136.330 1.00 110.89 ? 3616 ASP A C     1 
ATOM   15607 O  O     . ASP A 1 3616 ? 163.170 155.782 136.641 1.00 113.96 ? 3616 ASP A O     1 
ATOM   15608 C  CB    . ASP A 1 3616 ? 165.408 153.793 135.763 1.00 109.28 ? 3616 ASP A CB    1 
ATOM   15609 C  CG    . ASP A 1 3616 ? 166.741 153.543 135.088 1.00 116.07 ? 3616 ASP A CG    1 
ATOM   15610 O  OD1   . ASP A 1 3616 ? 167.713 154.259 135.407 1.00 115.27 ? 3616 ASP A OD1   1 
ATOM   15611 O  OD2   . ASP A 1 3616 ? 166.818 152.632 134.237 1.00 117.19 ? 3616 ASP A OD2   1 
ATOM   15612 N  N     . ASP A 1 3617 ? 164.745 157.069 135.661 1.00 121.97 ? 3617 ASP A N     1 
ATOM   15613 C  CA    . ASP A 1 3617 ? 163.771 158.061 135.218 1.00 122.86 ? 3617 ASP A CA    1 
ATOM   15614 C  C     . ASP A 1 3617 ? 162.890 157.522 134.100 1.00 123.25 ? 3617 ASP A C     1 
ATOM   15615 O  O     . ASP A 1 3617 ? 161.773 158.012 133.901 1.00 123.38 ? 3617 ASP A O     1 
ATOM   15616 C  CB    . ASP A 1 3617 ? 164.488 159.333 134.766 1.00 122.40 ? 3617 ASP A CB    1 
ATOM   15617 C  CG    . ASP A 1 3617 ? 165.803 159.044 134.071 1.00 124.54 ? 3617 ASP A CG    1 
ATOM   15618 O  OD1   . ASP A 1 3617 ? 165.906 157.993 133.404 1.00 120.99 ? 3617 ASP A OD1   1 
ATOM   15619 O  OD2   . ASP A 1 3617 ? 166.735 159.867 134.192 1.00 126.92 ? 3617 ASP A OD2   1 
ATOM   15620 N  N     . ALA A 1 3618 ? 163.372 156.520 133.363 1.00 107.97 ? 3618 ALA A N     1 
ATOM   15621 C  CA    . ALA A 1 3618 ? 162.602 155.931 132.276 1.00 105.81 ? 3618 ALA A CA    1 
ATOM   15622 C  C     . ALA A 1 3618 ? 161.582 154.909 132.759 1.00 108.09 ? 3618 ALA A C     1 
ATOM   15623 O  O     . ALA A 1 3618 ? 160.935 154.269 131.923 1.00 109.40 ? 3618 ALA A O     1 
ATOM   15624 C  CB    . ALA A 1 3618 ? 163.541 155.279 131.260 1.00 101.60 ? 3618 ALA A CB    1 
ATOM   15625 N  N     . PHE A 1 3619 ? 161.428 154.738 134.073 1.00 103.29 ? 3619 PHE A N     1 
ATOM   15626 C  CA    . PHE A 1 3619 ? 160.502 153.741 134.601 1.00 102.00 ? 3619 PHE A CA    1 
ATOM   15627 C  C     . PHE A 1 3619 ? 159.071 154.032 134.166 1.00 102.73 ? 3619 PHE A C     1 
ATOM   15628 O  O     . PHE A 1 3619 ? 158.313 153.120 133.820 1.00 103.28 ? 3619 PHE A O     1 
ATOM   15629 C  CB    . PHE A 1 3619 ? 160.603 153.690 136.126 1.00 99.40  ? 3619 PHE A CB    1 
ATOM   15630 C  CG    . PHE A 1 3619 ? 159.432 153.021 136.787 1.00 100.30 ? 3619 PHE A CG    1 
ATOM   15631 C  CD1   . PHE A 1 3619 ? 159.179 151.676 136.582 1.00 100.41 ? 3619 PHE A CD1   1 
ATOM   15632 C  CD2   . PHE A 1 3619 ? 158.584 153.739 137.612 1.00 101.11 ? 3619 PHE A CD2   1 
ATOM   15633 C  CE1   . PHE A 1 3619 ? 158.103 151.060 137.188 1.00 101.07 ? 3619 PHE A CE1   1 
ATOM   15634 C  CE2   . PHE A 1 3619 ? 157.505 153.128 138.221 1.00 99.30  ? 3619 PHE A CE2   1 
ATOM   15635 C  CZ    . PHE A 1 3619 ? 157.265 151.787 138.008 1.00 101.80 ? 3619 PHE A CZ    1 
ATOM   15636 N  N     . ARG A 1 3620 ? 158.683 155.309 134.184 1.00 99.54  ? 3620 ARG A N     1 
ATOM   15637 C  CA    . ARG A 1 3620 ? 157.342 155.697 133.766 1.00 98.23  ? 3620 ARG A CA    1 
ATOM   15638 C  C     . ARG A 1 3620 ? 157.093 155.330 132.307 1.00 100.43 ? 3620 ARG A C     1 
ATOM   15639 O  O     . ARG A 1 3620 ? 156.034 154.798 131.955 1.00 101.75 ? 3620 ARG A O     1 
ATOM   15640 C  CB    . ARG A 1 3620 ? 157.148 157.201 133.989 1.00 97.69  ? 3620 ARG A CB    1 
ATOM   15641 C  CG    . ARG A 1 3620 ? 156.945 157.586 135.444 1.00 102.42 ? 3620 ARG A CG    1 
ATOM   15642 C  CD    . ARG A 1 3620 ? 155.525 157.308 135.906 1.00 101.54 ? 3620 ARG A CD    1 
ATOM   15643 N  NE    . ARG A 1 3620 ? 154.532 157.852 134.988 1.00 100.80 ? 3620 ARG A NE    1 
ATOM   15644 C  CZ    . ARG A 1 3620 ? 153.659 158.797 135.309 1.00 102.15 ? 3620 ARG A CZ    1 
ATOM   15645 N  NH1   . ARG A 1 3620 ? 153.633 159.332 136.518 1.00 99.08  ? 3620 ARG A NH1   1 
ATOM   15646 N  NH2   . ARG A 1 3620 ? 152.791 159.217 134.393 1.00 104.33 ? 3620 ARG A NH2   1 
ATOM   15647 N  N     . LYS A 1 3621 ? 158.076 155.606 131.446 1.00 105.35 ? 3621 LYS A N     1 
ATOM   15648 C  CA    . LYS A 1 3621 ? 157.955 155.253 130.035 1.00 102.23 ? 3621 LYS A CA    1 
ATOM   15649 C  C     . LYS A 1 3621 ? 157.843 153.745 129.852 1.00 103.49 ? 3621 LYS A C     1 
ATOM   15650 O  O     . LYS A 1 3621 ? 156.971 153.256 129.123 1.00 106.11 ? 3621 LYS A O     1 
ATOM   15651 C  CB    . LYS A 1 3621 ? 159.156 155.798 129.261 1.00 102.77 ? 3621 LYS A CB    1 
ATOM   15652 C  CG    . LYS A 1 3621 ? 159.513 157.240 129.596 1.00 104.86 ? 3621 LYS A CG    1 
ATOM   15653 C  CD    . LYS A 1 3621 ? 160.933 157.591 129.162 1.00 107.08 ? 3621 LYS A CD    1 
ATOM   15654 C  CE    . LYS A 1 3621 ? 161.285 157.022 127.793 1.00 108.08 ? 3621 LYS A CE    1 
ATOM   15655 N  NZ    . LYS A 1 3621 ? 160.297 157.398 126.741 1.00 106.62 ? 3621 LYS A NZ    1 
ATOM   15656 N  N     . ASN A 1 3622 ? 158.727 152.990 130.508 1.00 97.42  ? 3622 ASN A N     1 
ATOM   15657 C  CA    . ASN A 1 3622 ? 158.703 151.536 130.386 1.00 94.52  ? 3622 ASN A CA    1 
ATOM   15658 C  C     . ASN A 1 3622 ? 157.412 150.957 130.949 1.00 96.72  ? 3622 ASN A C     1 
ATOM   15659 O  O     . ASN A 1 3622 ? 156.832 150.030 130.375 1.00 97.55  ? 3622 ASN A O     1 
ATOM   15660 C  CB    . ASN A 1 3622 ? 159.917 150.927 131.089 1.00 96.04  ? 3622 ASN A CB    1 
ATOM   15661 C  CG    . ASN A 1 3622 ? 161.222 151.270 130.399 1.00 100.23 ? 3622 ASN A CG    1 
ATOM   15662 O  OD1   . ASN A 1 3622 ? 162.099 151.904 130.984 1.00 103.97 ? 3622 ASN A OD1   1 
ATOM   15663 N  ND2   . ASN A 1 3622 ? 161.357 150.850 129.147 1.00 97.10  ? 3622 ASN A ND2   1 
ATOM   15664 N  N     . LEU A 1 3623 ? 156.951 151.488 132.084 1.00 97.58  ? 3623 LEU A N     1 
ATOM   15665 C  CA    . LEU A 1 3623 ? 155.710 150.995 132.672 1.00 98.80  ? 3623 LEU A CA    1 
ATOM   15666 C  C     . LEU A 1 3623 ? 154.518 151.282 131.768 1.00 98.12  ? 3623 LEU A C     1 
ATOM   15667 O  O     . LEU A 1 3623 ? 153.636 150.433 131.605 1.00 98.65  ? 3623 LEU A O     1 
ATOM   15668 C  CB    . LEU A 1 3623 ? 155.503 151.609 134.055 1.00 96.58  ? 3623 LEU A CB    1 
ATOM   15669 C  CG    . LEU A 1 3623 ? 154.094 151.522 134.638 1.00 96.36  ? 3623 LEU A CG    1 
ATOM   15670 C  CD1   . LEU A 1 3623 ? 153.765 150.089 135.011 1.00 96.18  ? 3623 LEU A CD1   1 
ATOM   15671 C  CD2   . LEU A 1 3623 ? 153.975 152.429 135.847 1.00 96.08  ? 3623 LEU A CD2   1 
ATOM   15672 N  N     . GLU A 1 3624 ? 154.476 152.475 131.169 1.00 102.38 ? 3624 GLU A N     1 
ATOM   15673 C  CA    . GLU A 1 3624 ? 153.398 152.795 130.239 1.00 101.10 ? 3624 GLU A CA    1 
ATOM   15674 C  C     . GLU A 1 3624 ? 153.435 151.886 129.017 1.00 101.35 ? 3624 GLU A C     1 
ATOM   15675 O  O     . GLU A 1 3624 ? 152.390 151.414 128.550 1.00 101.02 ? 3624 GLU A O     1 
ATOM   15676 C  CB    . GLU A 1 3624 ? 153.485 154.264 129.824 1.00 101.92 ? 3624 GLU A CB    1 
ATOM   15677 C  CG    . GLU A 1 3624 ? 152.399 154.703 128.857 1.00 106.12 ? 3624 GLU A CG    1 
ATOM   15678 C  CD    . GLU A 1 3624 ? 152.795 155.924 128.050 1.00 108.67 ? 3624 GLU A CD    1 
ATOM   15679 O  OE1   . GLU A 1 3624 ? 153.900 156.458 128.280 1.00 108.33 ? 3624 GLU A OE1   1 
ATOM   15680 O  OE2   . GLU A 1 3624 ? 151.999 156.352 127.188 1.00 107.47 ? 3624 GLU A OE2   1 
ATOM   15681 N  N     . SER A 1 3625 ? 154.632 151.629 128.483 1.00 102.64 ? 3625 SER A N     1 
ATOM   15682 C  CA    . SER A 1 3625 ? 154.754 150.742 127.331 1.00 102.31 ? 3625 SER A CA    1 
ATOM   15683 C  C     . SER A 1 3625 ? 154.307 149.327 127.677 1.00 106.33 ? 3625 SER A C     1 
ATOM   15684 O  O     . SER A 1 3625 ? 153.631 148.664 126.882 1.00 106.33 ? 3625 SER A O     1 
ATOM   15685 C  CB    . SER A 1 3625 ? 156.194 150.744 126.819 1.00 103.90 ? 3625 SER A CB    1 
ATOM   15686 O  OG    . SER A 1 3625 ? 156.624 152.059 126.513 1.00 107.21 ? 3625 SER A OG    1 
ATOM   15687 N  N     . ALA A 1 3626 ? 154.684 148.843 128.864 1.00 105.47 ? 3626 ALA A N     1 
ATOM   15688 C  CA    . ALA A 1 3626 ? 154.257 147.517 129.295 1.00 101.03 ? 3626 ALA A CA    1 
ATOM   15689 C  C     . ALA A 1 3626 ? 152.748 147.449 129.483 1.00 102.43 ? 3626 ALA A C     1 
ATOM   15690 O  O     . ALA A 1 3626 ? 152.123 146.447 129.120 1.00 103.91 ? 3626 ALA A O     1 
ATOM   15691 C  CB    . ALA A 1 3626 ? 154.972 147.126 130.588 1.00 98.96  ? 3626 ALA A CB    1 
ATOM   15692 N  N     . LEU A 1 3627 ? 152.149 148.496 130.052 1.00 99.16  ? 3627 LEU A N     1 
ATOM   15693 C  CA    . LEU A 1 3627 ? 150.701 148.556 130.192 1.00 92.64  ? 3627 LEU A CA    1 
ATOM   15694 C  C     . LEU A 1 3627 ? 149.985 148.564 128.851 1.00 95.40  ? 3627 LEU A C     1 
ATOM   15695 O  O     . LEU A 1 3627 ? 148.938 147.922 128.718 1.00 98.37  ? 3627 LEU A O     1 
ATOM   15696 C  CB    . LEU A 1 3627 ? 150.298 149.800 130.987 1.00 96.41  ? 3627 LEU A CB    1 
ATOM   15697 C  CG    . LEU A 1 3627 ? 150.502 149.767 132.501 1.00 96.81  ? 3627 LEU A CG    1 
ATOM   15698 C  CD1   . LEU A 1 3627 ? 149.787 150.935 133.159 1.00 95.99  ? 3627 LEU A CD1   1 
ATOM   15699 C  CD2   . LEU A 1 3627 ? 150.007 148.455 133.068 1.00 97.77  ? 3627 LEU A CD2   1 
ATOM   15700 N  N     . ARG A 1 3628 ? 150.523 149.270 127.858 1.00 103.20 ? 3628 ARG A N     1 
ATOM   15701 C  CA    . ARG A 1 3628 ? 149.885 149.382 126.553 1.00 104.79 ? 3628 ARG A CA    1 
ATOM   15702 C  C     . ARG A 1 3628 ? 150.050 148.127 125.702 1.00 103.50 ? 3628 ARG A C     1 
ATOM   15703 O  O     . ARG A 1 3628 ? 149.059 147.586 125.204 1.00 103.70 ? 3628 ARG A O     1 
ATOM   15704 C  CB    . ARG A 1 3628 ? 150.439 150.599 125.803 1.00 103.31 ? 3628 ARG A CB    1 
ATOM   15705 C  CG    . ARG A 1 3628 ? 149.638 151.869 126.028 1.00 102.70 ? 3628 ARG A CG    1 
ATOM   15706 C  CD    . ARG A 1 3628 ? 150.249 153.054 125.299 1.00 102.87 ? 3628 ARG A CD    1 
ATOM   15707 N  NE    . ARG A 1 3628 ? 149.868 154.326 125.902 1.00 106.27 ? 3628 ARG A NE    1 
ATOM   15708 C  CZ    . ARG A 1 3628 ? 148.651 154.852 125.851 1.00 107.72 ? 3628 ARG A CZ    1 
ATOM   15709 N  NH1   . ARG A 1 3628 ? 147.662 154.249 125.212 1.00 104.19 ? 3628 ARG A NH1   1 
ATOM   15710 N  NH2   . ARG A 1 3628 ? 148.422 156.016 126.452 1.00 107.63 ? 3628 ARG A NH2   1 
ATOM   15711 N  N     . PHE A 1 3629 ? 151.281 147.652 125.522 1.00 96.96  ? 3629 PHE A N     1 
ATOM   15712 C  CA    . PHE A 1 3629 ? 151.540 146.499 124.669 1.00 96.50  ? 3629 PHE A CA    1 
ATOM   15713 C  C     . PHE A 1 3629 ? 151.407 145.164 125.392 1.00 98.68  ? 3629 PHE A C     1 
ATOM   15714 O  O     . PHE A 1 3629 ? 151.395 144.121 124.730 1.00 95.61  ? 3629 PHE A O     1 
ATOM   15715 C  CB    . PHE A 1 3629 ? 152.938 146.603 124.050 1.00 98.47  ? 3629 PHE A CB    1 
ATOM   15716 C  CG    . PHE A 1 3629 ? 153.212 147.923 123.389 1.00 100.82 ? 3629 PHE A CG    1 
ATOM   15717 C  CD1   . PHE A 1 3629 ? 152.263 148.512 122.570 1.00 100.56 ? 3629 PHE A CD1   1 
ATOM   15718 C  CD2   . PHE A 1 3629 ? 154.417 148.576 123.585 1.00 101.37 ? 3629 PHE A CD2   1 
ATOM   15719 C  CE1   . PHE A 1 3629 ? 152.511 149.727 121.959 1.00 100.90 ? 3629 PHE A CE1   1 
ATOM   15720 C  CE2   . PHE A 1 3629 ? 154.671 149.791 122.977 1.00 98.16  ? 3629 PHE A CE2   1 
ATOM   15721 C  CZ    . PHE A 1 3629 ? 153.716 150.367 122.163 1.00 97.41  ? 3629 PHE A CZ    1 
ATOM   15722 N  N     . GLY A 1 3630 ? 151.308 145.165 126.718 1.00 98.22  ? 3630 GLY A N     1 
ATOM   15723 C  CA    . GLY A 1 3630 ? 151.100 143.932 127.451 1.00 96.47  ? 3630 GLY A CA    1 
ATOM   15724 C  C     . GLY A 1 3630 ? 152.333 143.096 127.694 1.00 95.27  ? 3630 GLY A C     1 
ATOM   15725 O  O     . GLY A 1 3630 ? 152.208 141.942 128.116 1.00 94.62  ? 3630 GLY A O     1 
ATOM   15726 N  N     . ASN A 1 3631 ? 153.523 143.634 127.443 1.00 93.72  ? 3631 ASN A N     1 
ATOM   15727 C  CA    . ASN A 1 3631 ? 154.731 142.868 127.700 1.00 93.43  ? 3631 ASN A CA    1 
ATOM   15728 C  C     . ASN A 1 3631 ? 155.000 142.773 129.200 1.00 91.50  ? 3631 ASN A C     1 
ATOM   15729 O  O     . ASN A 1 3631 ? 154.699 143.703 129.953 1.00 93.16  ? 3631 ASN A O     1 
ATOM   15730 C  CB    . ASN A 1 3631 ? 155.927 143.508 127.005 1.00 91.30  ? 3631 ASN A CB    1 
ATOM   15731 C  CG    . ASN A 1 3631 ? 155.631 143.888 125.570 1.00 94.22  ? 3631 ASN A CG    1 
ATOM   15732 O  OD1   . ASN A 1 3631 ? 154.865 143.214 124.883 1.00 94.15  ? 3631 ASN A OD1   1 
ATOM   15733 N  ND2   . ASN A 1 3631 ? 156.240 144.974 125.108 1.00 93.47  ? 3631 ASN A ND2   1 
ATOM   15734 N  N     . PRO A 1 3632 ? 155.557 141.653 129.659 1.00 73.60  ? 3632 PRO A N     1 
ATOM   15735 C  CA    . PRO A 1 3632 ? 155.908 141.537 131.078 1.00 70.37  ? 3632 PRO A CA    1 
ATOM   15736 C  C     . PRO A 1 3632 ? 156.991 142.532 131.461 1.00 72.02  ? 3632 PRO A C     1 
ATOM   15737 O  O     . PRO A 1 3632 ? 157.837 142.910 130.648 1.00 79.59  ? 3632 PRO A O     1 
ATOM   15738 C  CB    . PRO A 1 3632 ? 156.402 140.091 131.209 1.00 71.79  ? 3632 PRO A CB    1 
ATOM   15739 C  CG    . PRO A 1 3632 ? 156.732 139.663 129.821 1.00 75.65  ? 3632 PRO A CG    1 
ATOM   15740 C  CD    . PRO A 1 3632 ? 155.795 140.402 128.925 1.00 76.85  ? 3632 PRO A CD    1 
ATOM   15741 N  N     . LEU A 1 3633 ? 156.954 142.958 132.720 1.00 65.79  ? 3633 LEU A N     1 
ATOM   15742 C  CA    . LEU A 1 3633 ? 157.881 143.950 133.237 1.00 63.39  ? 3633 LEU A CA    1 
ATOM   15743 C  C     . LEU A 1 3633 ? 158.449 143.472 134.565 1.00 70.23  ? 3633 LEU A C     1 
ATOM   15744 O  O     . LEU A 1 3633 ? 157.743 142.879 135.382 1.00 82.97  ? 3633 LEU A O     1 
ATOM   15745 C  CB    . LEU A 1 3633 ? 157.193 145.309 133.414 1.00 65.75  ? 3633 LEU A CB    1 
ATOM   15746 C  CG    . LEU A 1 3633 ? 158.069 146.510 133.762 1.00 68.44  ? 3633 LEU A CG    1 
ATOM   15747 C  CD1   . LEU A 1 3633 ? 158.892 146.925 132.558 1.00 72.94  ? 3633 LEU A CD1   1 
ATOM   15748 C  CD2   . LEU A 1 3633 ? 157.208 147.662 134.244 1.00 73.40  ? 3633 LEU A CD2   1 
ATOM   15749 N  N     . LEU A 1 3634 ? 159.738 143.731 134.770 1.00 66.90  ? 3634 LEU A N     1 
ATOM   15750 C  CA    . LEU A 1 3634 ? 160.430 143.363 136.001 1.00 65.03  ? 3634 LEU A CA    1 
ATOM   15751 C  C     . LEU A 1 3634 ? 161.108 144.609 136.552 1.00 70.82  ? 3634 LEU A C     1 
ATOM   15752 O  O     . LEU A 1 3634 ? 162.061 145.117 135.954 1.00 82.79  ? 3634 LEU A O     1 
ATOM   15753 C  CB    . LEU A 1 3634 ? 161.444 142.246 135.754 1.00 65.96  ? 3634 LEU A CB    1 
ATOM   15754 C  CG    . LEU A 1 3634 ? 162.462 141.977 136.862 1.00 65.42  ? 3634 LEU A CG    1 
ATOM   15755 C  CD1   . LEU A 1 3634 ? 161.776 141.435 138.101 1.00 68.78  ? 3634 LEU A CD1   1 
ATOM   15756 C  CD2   . LEU A 1 3634 ? 163.522 141.010 136.374 1.00 68.97  ? 3634 LEU A CD2   1 
ATOM   15757 N  N     . VAL A 1 3635 ? 160.618 145.099 137.688 1.00 69.39  ? 3635 VAL A N     1 
ATOM   15758 C  CA    . VAL A 1 3635 ? 161.101 146.331 138.297 1.00 65.18  ? 3635 VAL A CA    1 
ATOM   15759 C  C     . VAL A 1 3635 ? 161.864 145.976 139.564 1.00 70.90  ? 3635 VAL A C     1 
ATOM   15760 O  O     . VAL A 1 3635 ? 161.358 145.235 140.414 1.00 83.11  ? 3635 VAL A O     1 
ATOM   15761 C  CB    . VAL A 1 3635 ? 159.944 147.296 138.607 1.00 68.71  ? 3635 VAL A CB    1 
ATOM   15762 C  CG1   . VAL A 1 3635 ? 160.484 148.648 139.030 1.00 76.71  ? 3635 VAL A CG1   1 
ATOM   15763 C  CG2   . VAL A 1 3635 ? 159.033 147.433 137.401 1.00 67.12  ? 3635 VAL A CG2   1 
ATOM   15764 N  N     . GLN A 1 3636 ? 163.078 146.504 139.691 1.00 73.94  ? 3636 GLN A N     1 
ATOM   15765 C  CA    . GLN A 1 3636 ? 163.915 146.247 140.849 1.00 76.24  ? 3636 GLN A CA    1 
ATOM   15766 C  C     . GLN A 1 3636 ? 163.893 147.442 141.799 1.00 82.34  ? 3636 GLN A C     1 
ATOM   15767 O  O     . GLN A 1 3636 ? 163.248 148.462 141.549 1.00 85.70  ? 3636 GLN A O     1 
ATOM   15768 C  CB    . GLN A 1 3636 ? 165.346 145.922 140.419 1.00 75.59  ? 3636 GLN A CB    1 
ATOM   15769 C  CG    . GLN A 1 3636 ? 165.445 144.981 139.238 1.00 82.73  ? 3636 GLN A CG    1 
ATOM   15770 C  CD    . GLN A 1 3636 ? 166.851 144.901 138.686 1.00 87.04  ? 3636 GLN A CD    1 
ATOM   15771 O  OE1   . GLN A 1 3636 ? 167.156 144.050 137.853 1.00 91.75  ? 3636 GLN A OE1   1 
ATOM   15772 N  NE2   . GLN A 1 3636 ? 167.720 145.793 139.149 1.00 81.87  ? 3636 GLN A NE2   1 
ATOM   15773 N  N     . ASP A 1 3637 ? 164.619 147.300 142.910 1.00 94.82  ? 3637 ASP A N     1 
ATOM   15774 C  CA    . ASP A 1 3637 ? 164.745 148.344 143.929 1.00 94.70  ? 3637 ASP A CA    1 
ATOM   15775 C  C     . ASP A 1 3637 ? 163.382 148.749 144.488 1.00 96.70  ? 3637 ASP A C     1 
ATOM   15776 O  O     . ASP A 1 3637 ? 162.946 149.894 144.360 1.00 98.25  ? 3637 ASP A O     1 
ATOM   15777 C  CB    . ASP A 1 3637 ? 165.498 149.560 143.384 1.00 94.41  ? 3637 ASP A CB    1 
ATOM   15778 C  CG    . ASP A 1 3637 ? 166.593 149.179 142.409 1.00 101.57 ? 3637 ASP A CG    1 
ATOM   15779 O  OD1   . ASP A 1 3637 ? 167.451 148.348 142.772 1.00 105.15 ? 3637 ASP A OD1   1 
ATOM   15780 O  OD2   . ASP A 1 3637 ? 166.599 149.716 141.282 1.00 102.47 ? 3637 ASP A OD2   1 
ATOM   15781 N  N     . VAL A 1 3638 ? 162.710 147.791 145.131 1.00 82.66  ? 3638 VAL A N     1 
ATOM   15782 C  CA    . VAL A 1 3638 ? 161.400 148.064 145.710 1.00 77.01  ? 3638 VAL A CA    1 
ATOM   15783 C  C     . VAL A 1 3638 ? 161.504 148.937 146.955 1.00 81.96  ? 3638 VAL A C     1 
ATOM   15784 O  O     . VAL A 1 3638 ? 160.503 149.527 147.377 1.00 84.10  ? 3638 VAL A O     1 
ATOM   15785 C  CB    . VAL A 1 3638 ? 160.671 146.743 146.021 1.00 81.34  ? 3638 VAL A CB    1 
ATOM   15786 C  CG1   . VAL A 1 3638 ? 159.189 146.990 146.256 1.00 83.86  ? 3638 VAL A CG1   1 
ATOM   15787 C  CG2   . VAL A 1 3638 ? 160.866 145.755 144.888 1.00 82.44  ? 3638 VAL A CG2   1 
ATOM   15788 N  N     . GLU A 1 3639 ? 162.693 149.050 147.554 1.00 97.04  ? 3639 GLU A N     1 
ATOM   15789 C  CA    . GLU A 1 3639 ? 162.857 149.943 148.696 1.00 96.42  ? 3639 GLU A CA    1 
ATOM   15790 C  C     . GLU A 1 3639 ? 162.611 151.399 148.323 1.00 96.66  ? 3639 GLU A C     1 
ATOM   15791 O  O     . GLU A 1 3639 ? 162.353 152.221 149.209 1.00 97.46  ? 3639 GLU A O     1 
ATOM   15792 C  CB    . GLU A 1 3639 ? 164.254 149.790 149.300 1.00 96.35  ? 3639 GLU A CB    1 
ATOM   15793 C  CG    . GLU A 1 3639 ? 164.786 148.368 149.301 1.00 96.68  ? 3639 GLU A CG    1 
ATOM   15794 C  CD    . GLU A 1 3639 ? 165.747 148.105 148.163 1.00 97.35  ? 3639 GLU A CD    1 
ATOM   15795 O  OE1   . GLU A 1 3639 ? 166.848 147.574 148.422 1.00 99.68  ? 3639 GLU A OE1   1 
ATOM   15796 O  OE2   . GLU A 1 3639 ? 165.405 148.432 147.010 1.00 96.62  ? 3639 GLU A OE2   1 
ATOM   15797 N  N     . SER A 1 3640 ? 162.685 151.731 147.038 1.00 93.41  ? 3640 SER A N     1 
ATOM   15798 C  CA    . SER A 1 3640 ? 162.344 153.051 146.521 1.00 92.94  ? 3640 SER A CA    1 
ATOM   15799 C  C     . SER A 1 3640 ? 161.056 152.991 145.706 1.00 91.05  ? 3640 SER A C     1 
ATOM   15800 O  O     . SER A 1 3640 ? 160.952 153.586 144.632 1.00 91.35  ? 3640 SER A O     1 
ATOM   15801 C  CB    . SER A 1 3640 ? 163.486 153.618 145.683 1.00 91.61  ? 3640 SER A CB    1 
ATOM   15802 O  OG    . SER A 1 3640 ? 164.671 153.729 146.450 1.00 97.79  ? 3640 SER A OG    1 
ATOM   15803 N  N     . TYR A 1 3641 ? 160.073 152.246 146.211 1.00 88.00  ? 3641 TYR A N     1 
ATOM   15804 C  CA    . TYR A 1 3641 ? 158.841 151.995 145.475 1.00 87.42  ? 3641 TYR A CA    1 
ATOM   15805 C  C     . TYR A 1 3641 ? 158.144 153.299 145.106 1.00 88.68  ? 3641 TYR A C     1 
ATOM   15806 O  O     . TYR A 1 3641 ? 158.014 154.207 145.931 1.00 91.34  ? 3641 TYR A O     1 
ATOM   15807 C  CB    . TYR A 1 3641 ? 157.910 151.115 146.309 1.00 83.26  ? 3641 TYR A CB    1 
ATOM   15808 C  CG    . TYR A 1 3641 ? 156.482 151.074 145.817 1.00 83.46  ? 3641 TYR A CG    1 
ATOM   15809 C  CD1   . TYR A 1 3641 ? 156.143 150.367 144.672 1.00 85.41  ? 3641 TYR A CD1   1 
ATOM   15810 C  CD2   . TYR A 1 3641 ? 155.472 151.733 146.502 1.00 88.32  ? 3641 TYR A CD2   1 
ATOM   15811 C  CE1   . TYR A 1 3641 ? 154.839 150.324 144.220 1.00 86.89  ? 3641 TYR A CE1   1 
ATOM   15812 C  CE2   . TYR A 1 3641 ? 154.164 151.695 146.058 1.00 89.78  ? 3641 TYR A CE2   1 
ATOM   15813 C  CZ    . TYR A 1 3641 ? 153.854 150.989 144.917 1.00 88.96  ? 3641 TYR A CZ    1 
ATOM   15814 O  OH    . TYR A 1 3641 ? 152.555 150.948 144.470 1.00 88.65  ? 3641 TYR A OH    1 
ATOM   15815 N  N     . ASP A 1 3642 ? 157.699 153.384 143.852 1.00 95.17  ? 3642 ASP A N     1 
ATOM   15816 C  CA    . ASP A 1 3642 ? 157.012 154.564 143.352 1.00 93.55  ? 3642 ASP A CA    1 
ATOM   15817 C  C     . ASP A 1 3642 ? 155.518 154.380 143.545 1.00 91.72  ? 3642 ASP A C     1 
ATOM   15818 O  O     . ASP A 1 3642 ? 154.953 153.409 143.018 1.00 94.16  ? 3642 ASP A O     1 
ATOM   15819 C  CB    . ASP A 1 3642 ? 157.336 154.783 141.877 1.00 96.28  ? 3642 ASP A CB    1 
ATOM   15820 C  CG    . ASP A 1 3642 ? 156.864 156.134 141.360 1.00 100.76 ? 3642 ASP A CG    1 
ATOM   15821 O  OD1   . ASP A 1 3642 ? 155.781 156.602 141.766 1.00 101.66 ? 3642 ASP A OD1   1 
ATOM   15822 O  OD2   . ASP A 1 3642 ? 157.587 156.732 140.536 1.00 100.48 ? 3642 ASP A OD2   1 
ATOM   15823 N  N     . PRO A 1 3643 ? 154.839 155.266 144.280 1.00 85.71  ? 3643 PRO A N     1 
ATOM   15824 C  CA    . PRO A 1 3643 ? 153.396 155.085 144.506 1.00 85.47  ? 3643 PRO A CA    1 
ATOM   15825 C  C     . PRO A 1 3643 ? 152.548 155.225 143.251 1.00 87.01  ? 3643 PRO A C     1 
ATOM   15826 O  O     . PRO A 1 3643 ? 151.325 155.058 143.338 1.00 92.96  ? 3643 PRO A O     1 
ATOM   15827 C  CB    . PRO A 1 3643 ? 153.058 156.183 145.525 1.00 84.93  ? 3643 PRO A CB    1 
ATOM   15828 C  CG    . PRO A 1 3643 ? 154.366 156.532 146.163 1.00 86.79  ? 3643 PRO A CG    1 
ATOM   15829 C  CD    . PRO A 1 3643 ? 155.391 156.366 145.085 1.00 88.05  ? 3643 PRO A CD    1 
ATOM   15830 N  N     . VAL A 1 3644 ? 153.146 155.524 142.095 1.00 83.04  ? 3644 VAL A N     1 
ATOM   15831 C  CA    . VAL A 1 3644 ? 152.379 155.625 140.860 1.00 84.99  ? 3644 VAL A CA    1 
ATOM   15832 C  C     . VAL A 1 3644 ? 151.838 154.269 140.431 1.00 87.28  ? 3644 VAL A C     1 
ATOM   15833 O  O     . VAL A 1 3644 ? 150.922 154.199 139.606 1.00 84.24  ? 3644 VAL A O     1 
ATOM   15834 C  CB    . VAL A 1 3644 ? 153.242 156.256 139.746 1.00 83.54  ? 3644 VAL A CB    1 
ATOM   15835 C  CG1   . VAL A 1 3644 ? 154.152 155.212 139.114 1.00 86.48  ? 3644 VAL A CG1   1 
ATOM   15836 C  CG2   . VAL A 1 3644 ? 152.362 156.921 138.700 1.00 84.48  ? 3644 VAL A CG2   1 
ATOM   15837 N  N     . LEU A 1 3645 ? 152.380 153.183 140.979 1.00 86.72  ? 3645 LEU A N     1 
ATOM   15838 C  CA    . LEU A 1 3645 ? 151.941 151.834 140.652 1.00 86.06  ? 3645 LEU A CA    1 
ATOM   15839 C  C     . LEU A 1 3645 ? 150.746 151.380 141.479 1.00 86.71  ? 3645 LEU A C     1 
ATOM   15840 O  O     . LEU A 1 3645 ? 150.291 150.245 141.300 1.00 91.69  ? 3645 LEU A O     1 
ATOM   15841 C  CB    . LEU A 1 3645 ? 153.096 150.849 140.844 1.00 82.82  ? 3645 LEU A CB    1 
ATOM   15842 C  CG    . LEU A 1 3645 ? 153.931 150.497 139.614 1.00 79.09  ? 3645 LEU A CG    1 
ATOM   15843 C  CD1   . LEU A 1 3645 ? 155.142 149.683 140.024 1.00 82.11  ? 3645 LEU A CD1   1 
ATOM   15844 C  CD2   . LEU A 1 3645 ? 153.096 149.736 138.605 1.00 81.56  ? 3645 LEU A CD2   1 
ATOM   15845 N  N     . ASN A 1 3646 ? 150.240 152.224 142.379 1.00 78.94  ? 3646 ASN A N     1 
ATOM   15846 C  CA    . ASN A 1 3646 ? 149.143 151.813 143.254 1.00 78.25  ? 3646 ASN A CA    1 
ATOM   15847 C  C     . ASN A 1 3646 ? 147.904 151.357 142.492 1.00 83.35  ? 3646 ASN A C     1 
ATOM   15848 O  O     . ASN A 1 3646 ? 147.355 150.297 142.839 1.00 84.86  ? 3646 ASN A O     1 
ATOM   15849 C  CB    . ASN A 1 3646 ? 148.815 152.947 144.232 1.00 78.34  ? 3646 ASN A CB    1 
ATOM   15850 C  CG    . ASN A 1 3646 ? 149.837 153.070 145.344 1.00 84.45  ? 3646 ASN A CG    1 
ATOM   15851 O  OD1   . ASN A 1 3646 ? 150.804 152.311 145.400 1.00 85.48  ? 3646 ASN A OD1   1 
ATOM   15852 N  ND2   . ASN A 1 3646 ? 149.628 154.031 146.235 1.00 85.90  ? 3646 ASN A ND2   1 
ATOM   15853 N  N     . PRO A 1 3647 ? 147.401 152.079 141.482 1.00 87.33  ? 3647 PRO A N     1 
ATOM   15854 C  CA    . PRO A 1 3647 ? 146.263 151.537 140.720 1.00 86.69  ? 3647 PRO A CA    1 
ATOM   15855 C  C     . PRO A 1 3647 ? 146.579 150.237 140.005 1.00 91.97  ? 3647 PRO A C     1 
ATOM   15856 O  O     . PRO A 1 3647 ? 145.689 149.389 139.859 1.00 93.86  ? 3647 PRO A O     1 
ATOM   15857 C  CB    . PRO A 1 3647 ? 145.934 152.664 139.730 1.00 82.11  ? 3647 PRO A CB    1 
ATOM   15858 C  CG    . PRO A 1 3647 ? 147.189 153.449 139.623 1.00 87.92  ? 3647 PRO A CG    1 
ATOM   15859 C  CD    . PRO A 1 3647 ? 147.777 153.418 140.996 1.00 87.85  ? 3647 PRO A CD    1 
ATOM   15860 N  N     . VAL A 1 3648 ? 147.819 150.053 139.549 1.00 85.56  ? 3648 VAL A N     1 
ATOM   15861 C  CA    . VAL A 1 3648 ? 148.176 148.835 138.827 1.00 79.41  ? 3648 VAL A CA    1 
ATOM   15862 C  C     . VAL A 1 3648 ? 148.169 147.635 139.765 1.00 80.18  ? 3648 VAL A C     1 
ATOM   15863 O  O     . VAL A 1 3648 ? 147.615 146.578 139.442 1.00 81.42  ? 3648 VAL A O     1 
ATOM   15864 C  CB    . VAL A 1 3648 ? 149.539 149.002 138.135 1.00 78.22  ? 3648 VAL A CB    1 
ATOM   15865 C  CG1   . VAL A 1 3648 ? 149.877 147.763 137.330 1.00 79.50  ? 3648 VAL A CG1   1 
ATOM   15866 C  CG2   . VAL A 1 3648 ? 149.534 150.235 137.248 1.00 81.88  ? 3648 VAL A CG2   1 
ATOM   15867 N  N     . LEU A 1 3649 ? 148.788 147.778 140.939 1.00 76.40  ? 3649 LEU A N     1 
ATOM   15868 C  CA    . LEU A 1 3649 ? 148.854 146.666 141.882 1.00 77.37  ? 3649 LEU A CA    1 
ATOM   15869 C  C     . LEU A 1 3649 ? 147.469 146.291 142.396 1.00 79.60  ? 3649 LEU A C     1 
ATOM   15870 O  O     . LEU A 1 3649 ? 147.150 145.103 142.525 1.00 78.72  ? 3649 LEU A O     1 
ATOM   15871 C  CB    . LEU A 1 3649 ? 149.784 147.020 143.041 1.00 72.14  ? 3649 LEU A CB    1 
ATOM   15872 C  CG    . LEU A 1 3649 ? 151.249 147.229 142.660 1.00 65.11  ? 3649 LEU A CG    1 
ATOM   15873 C  CD1   . LEU A 1 3649 ? 152.096 147.495 143.892 1.00 72.95  ? 3649 LEU A CD1   1 
ATOM   15874 C  CD2   . LEU A 1 3649 ? 151.776 146.029 141.893 1.00 66.91  ? 3649 LEU A CD2   1 
ATOM   15875 N  N     . ASN A 1 3650 ? 146.633 147.287 142.693 1.00 78.15  ? 3650 ASN A N     1 
ATOM   15876 C  CA    . ASN A 1 3650 ? 145.278 147.023 143.157 1.00 72.93  ? 3650 ASN A CA    1 
ATOM   15877 C  C     . ASN A 1 3650 ? 144.356 146.543 142.045 1.00 80.33  ? 3650 ASN A C     1 
ATOM   15878 O  O     . ASN A 1 3650 ? 143.229 146.129 142.340 1.00 83.60  ? 3650 ASN A O     1 
ATOM   15879 C  CB    . ASN A 1 3650 ? 144.691 148.279 143.803 1.00 78.45  ? 3650 ASN A CB    1 
ATOM   15880 C  CG    . ASN A 1 3650 ? 145.090 148.428 145.255 1.00 86.87  ? 3650 ASN A CG    1 
ATOM   15881 O  OD1   . ASN A 1 3650 ? 145.191 147.444 145.987 1.00 92.12  ? 3650 ASN A OD1   1 
ATOM   15882 N  ND2   . ASN A 1 3650 ? 145.320 149.664 145.681 1.00 83.22  ? 3650 ASN A ND2   1 
ATOM   15883 N  N     . ARG A 1 3651 ? 144.805 146.589 140.789 1.00 88.87  ? 3651 ARG A N     1 
ATOM   15884 C  CA    . ARG A 1 3651 ? 143.985 146.217 139.634 1.00 89.69  ? 3651 ARG A CA    1 
ATOM   15885 C  C     . ARG A 1 3651 ? 142.698 147.035 139.583 1.00 89.33  ? 3651 ARG A C     1 
ATOM   15886 O  O     . ARG A 1 3651 ? 141.618 146.514 139.297 1.00 91.35  ? 3651 ARG A O     1 
ATOM   15887 C  CB    . ARG A 1 3651 ? 143.680 144.717 139.626 1.00 85.46  ? 3651 ARG A CB    1 
ATOM   15888 C  CG    . ARG A 1 3651 ? 144.694 143.884 138.860 1.00 84.94  ? 3651 ARG A CG    1 
ATOM   15889 C  CD    . ARG A 1 3651 ? 144.160 142.490 138.576 1.00 88.80  ? 3651 ARG A CD    1 
ATOM   15890 N  NE    . ARG A 1 3651 ? 145.231 141.519 138.389 1.00 95.32  ? 3651 ARG A NE    1 
ATOM   15891 C  CZ    . ARG A 1 3651 ? 145.908 140.949 139.376 1.00 93.71  ? 3651 ARG A CZ    1 
ATOM   15892 N  NH1   . ARG A 1 3651 ? 145.650 141.229 140.643 1.00 89.72  ? 3651 ARG A NH1   1 
ATOM   15893 N  NH2   . ARG A 1 3651 ? 146.867 140.075 139.085 1.00 87.75  ? 3651 ARG A NH2   1 
ATOM   15894 N  N     . GLU A 1 3652 ? 142.815 148.331 139.864 1.00 96.71  ? 3652 GLU A N     1 
ATOM   15895 C  CA    . GLU A 1 3652 ? 141.682 149.252 139.800 1.00 96.64  ? 3652 GLU A CA    1 
ATOM   15896 C  C     . GLU A 1 3652 ? 141.516 149.696 138.354 1.00 98.74  ? 3652 GLU A C     1 
ATOM   15897 O  O     . GLU A 1 3652 ? 142.130 150.662 137.899 1.00 101.18 ? 3652 GLU A O     1 
ATOM   15898 C  CB    . GLU A 1 3652 ? 141.898 150.440 140.730 1.00 95.88  ? 3652 GLU A CB    1 
ATOM   15899 C  CG    . GLU A 1 3652 ? 141.882 150.086 142.206 1.00 98.19  ? 3652 GLU A CG    1 
ATOM   15900 C  CD    . GLU A 1 3652 ? 142.332 151.236 143.084 1.00 103.16 ? 3652 GLU A CD    1 
ATOM   15901 O  OE1   . GLU A 1 3652 ? 142.711 152.292 142.536 1.00 101.10 ? 3652 GLU A OE1   1 
ATOM   15902 O  OE2   . GLU A 1 3652 ? 142.306 151.085 144.324 1.00 105.38 ? 3652 GLU A OE2   1 
ATOM   15903 N  N     . VAL A 1 3653 ? 140.669 148.980 137.618 1.00 98.35  ? 3653 VAL A N     1 
ATOM   15904 C  CA    . VAL A 1 3653 ? 140.449 149.243 136.204 1.00 98.90  ? 3653 VAL A CA    1 
ATOM   15905 C  C     . VAL A 1 3653 ? 138.957 149.413 135.955 1.00 103.00 ? 3653 VAL A C     1 
ATOM   15906 O  O     . VAL A 1 3653 ? 138.113 148.904 136.696 1.00 107.31 ? 3653 VAL A O     1 
ATOM   15907 C  CB    . VAL A 1 3653 ? 141.023 148.126 135.308 1.00 98.36  ? 3653 VAL A CB    1 
ATOM   15908 C  CG1   . VAL A 1 3653 ? 142.531 148.035 135.470 1.00 100.61 ? 3653 VAL A CG1   1 
ATOM   15909 C  CG2   . VAL A 1 3653 ? 140.366 146.795 135.635 1.00 93.91  ? 3653 VAL A CG2   1 
ATOM   15910 N  N     . ARG A 1 3654 ? 138.641 150.147 134.891 1.00 110.16 ? 3654 ARG A N     1 
ATOM   15911 C  CA    . ARG A 1 3654 ? 137.267 150.369 134.458 1.00 107.67 ? 3654 ARG A CA    1 
ATOM   15912 C  C     . ARG A 1 3654 ? 137.106 149.811 133.051 1.00 110.27 ? 3654 ARG A C     1 
ATOM   15913 O  O     . ARG A 1 3654 ? 137.912 150.112 132.164 1.00 113.98 ? 3654 ARG A O     1 
ATOM   15914 C  CB    . ARG A 1 3654 ? 136.908 151.857 134.503 1.00 104.49 ? 3654 ARG A CB    1 
ATOM   15915 C  CG    . ARG A 1 3654 ? 137.914 152.768 133.818 1.00 107.12 ? 3654 ARG A CG    1 
ATOM   15916 C  CD    . ARG A 1 3654 ? 137.793 154.203 134.309 1.00 110.18 ? 3654 ARG A CD    1 
ATOM   15917 N  NE    . ARG A 1 3654 ? 136.406 154.610 134.501 1.00 113.14 ? 3654 ARG A NE    1 
ATOM   15918 C  CZ    . ARG A 1 3654 ? 135.556 154.877 133.518 1.00 113.43 ? 3654 ARG A CZ    1 
ATOM   15919 N  NH1   . ARG A 1 3654 ? 135.921 154.802 132.248 1.00 113.73 ? 3654 ARG A NH1   1 
ATOM   15920 N  NH2   . ARG A 1 3654 ? 134.310 155.232 133.816 1.00 110.69 ? 3654 ARG A NH2   1 
ATOM   15921 N  N     . ARG A 1 3655 ? 136.076 148.994 132.853 1.00 117.18 ? 3655 ARG A N     1 
ATOM   15922 C  CA    . ARG A 1 3655 ? 135.815 148.350 131.568 1.00 118.87 ? 3655 ARG A CA    1 
ATOM   15923 C  C     . ARG A 1 3655 ? 134.649 149.075 130.904 1.00 121.60 ? 3655 ARG A C     1 
ATOM   15924 O  O     . ARG A 1 3655 ? 133.483 148.763 131.159 1.00 122.59 ? 3655 ARG A O     1 
ATOM   15925 C  CB    . ARG A 1 3655 ? 135.525 146.866 131.759 1.00 116.22 ? 3655 ARG A CB    1 
ATOM   15926 C  CG    . ARG A 1 3655 ? 136.732 146.066 132.222 1.00 119.29 ? 3655 ARG A CG    1 
ATOM   15927 C  CD    . ARG A 1 3655 ? 136.406 144.592 132.383 1.00 120.79 ? 3655 ARG A CD    1 
ATOM   15928 N  NE    . ARG A 1 3655 ? 137.581 143.817 132.762 1.00 121.79 ? 3655 ARG A NE    1 
ATOM   15929 C  CZ    . ARG A 1 3655 ? 137.942 143.566 134.013 1.00 121.54 ? 3655 ARG A CZ    1 
ATOM   15930 N  NH1   . ARG A 1 3655 ? 137.237 144.013 135.039 1.00 120.37 ? 3655 ARG A NH1   1 
ATOM   15931 N  NH2   . ARG A 1 3655 ? 139.039 142.849 134.240 1.00 121.26 ? 3655 ARG A NH2   1 
ATOM   15932 N  N     . THR A 1 3656 ? 134.968 150.043 130.048 1.00 129.73 ? 3656 THR A N     1 
ATOM   15933 C  CA    . THR A 1 3656 ? 133.967 150.864 129.380 1.00 130.62 ? 3656 THR A CA    1 
ATOM   15934 C  C     . THR A 1 3656 ? 134.171 150.788 127.875 1.00 128.56 ? 3656 THR A C     1 
ATOM   15935 O  O     . THR A 1 3656 ? 135.263 151.081 127.378 1.00 126.42 ? 3656 THR A O     1 
ATOM   15936 C  CB    . THR A 1 3656 ? 134.044 152.321 129.849 1.00 127.59 ? 3656 THR A CB    1 
ATOM   15937 O  OG1   . THR A 1 3656 ? 133.597 152.412 131.208 1.00 126.27 ? 3656 THR A OG1   1 
ATOM   15938 C  CG2   . THR A 1 3656 ? 133.175 153.212 128.973 1.00 126.92 ? 3656 THR A CG2   1 
ATOM   15939 N  N     . GLY A 1 3657 ? 133.119 150.405 127.157 1.00 128.10 ? 3657 GLY A N     1 
ATOM   15940 C  CA    . GLY A 1 3657 ? 133.181 150.337 125.705 1.00 127.19 ? 3657 GLY A CA    1 
ATOM   15941 C  C     . GLY A 1 3657 ? 134.206 149.358 125.175 1.00 128.02 ? 3657 GLY A C     1 
ATOM   15942 O  O     . GLY A 1 3657 ? 134.901 149.659 124.197 1.00 127.87 ? 3657 GLY A O     1 
ATOM   15943 N  N     . GLY A 1 3658 ? 134.318 148.189 125.802 1.00 127.72 ? 3658 GLY A N     1 
ATOM   15944 C  CA    . GLY A 1 3658 ? 135.302 147.210 125.388 1.00 127.52 ? 3658 GLY A CA    1 
ATOM   15945 C  C     . GLY A 1 3658 ? 136.738 147.606 125.637 1.00 128.52 ? 3658 GLY A C     1 
ATOM   15946 O  O     . GLY A 1 3658 ? 137.644 146.977 125.081 1.00 126.83 ? 3658 GLY A O     1 
ATOM   15947 N  N     . ARG A 1 3659 ? 136.976 148.629 126.453 1.00 123.77 ? 3659 ARG A N     1 
ATOM   15948 C  CA    . ARG A 1 3659 ? 138.315 149.108 126.759 1.00 121.61 ? 3659 ARG A CA    1 
ATOM   15949 C  C     . ARG A 1 3659 ? 138.562 148.980 128.254 1.00 119.64 ? 3659 ARG A C     1 
ATOM   15950 O  O     . ARG A 1 3659 ? 137.814 149.544 129.060 1.00 119.23 ? 3659 ARG A O     1 
ATOM   15951 C  CB    . ARG A 1 3659 ? 138.491 150.564 126.315 1.00 122.41 ? 3659 ARG A CB    1 
ATOM   15952 C  CG    . ARG A 1 3659 ? 138.501 150.755 124.808 1.00 121.61 ? 3659 ARG A CG    1 
ATOM   15953 C  CD    . ARG A 1 3659 ? 137.826 152.064 124.403 1.00 121.08 ? 3659 ARG A CD    1 
ATOM   15954 N  NE    . ARG A 1 3659 ? 138.318 153.236 125.122 1.00 122.09 ? 3659 ARG A NE    1 
ATOM   15955 C  CZ    . ARG A 1 3659 ? 139.571 153.674 125.109 1.00 122.33 ? 3659 ARG A CZ    1 
ATOM   15956 N  NH1   . ARG A 1 3659 ? 140.511 153.075 124.395 1.00 121.62 ? 3659 ARG A NH1   1 
ATOM   15957 N  NH2   . ARG A 1 3659 ? 139.886 154.755 125.817 1.00 122.32 ? 3659 ARG A NH2   1 
ATOM   15958 N  N     . VAL A 1 3660 ? 139.605 148.245 128.619 1.00 106.30 ? 3660 VAL A N     1 
ATOM   15959 C  CA    . VAL A 1 3660 ? 140.013 148.089 130.009 1.00 104.99 ? 3660 VAL A CA    1 
ATOM   15960 C  C     . VAL A 1 3660 ? 141.007 149.208 130.293 1.00 102.52 ? 3660 VAL A C     1 
ATOM   15961 O  O     . VAL A 1 3660 ? 142.195 149.098 129.981 1.00 108.81 ? 3660 VAL A O     1 
ATOM   15962 C  CB    . VAL A 1 3660 ? 140.616 146.708 130.276 1.00 103.71 ? 3660 VAL A CB    1 
ATOM   15963 C  CG1   . VAL A 1 3660 ? 141.048 146.591 131.729 1.00 105.99 ? 3660 VAL A CG1   1 
ATOM   15964 C  CG2   . VAL A 1 3660 ? 139.618 145.617 129.922 1.00 101.35 ? 3660 VAL A CG2   1 
ATOM   15965 N  N     . LEU A 1 3661 ? 140.520 150.294 130.881 1.00 104.39 ? 3661 LEU A N     1 
ATOM   15966 C  CA    . LEU A 1 3661 ? 141.327 151.481 131.118 1.00 108.18 ? 3661 LEU A CA    1 
ATOM   15967 C  C     . LEU A 1 3661 ? 141.778 151.537 132.569 1.00 108.76 ? 3661 LEU A C     1 
ATOM   15968 O  O     . LEU A 1 3661 ? 141.014 151.214 133.483 1.00 113.11 ? 3661 LEU A O     1 
ATOM   15969 C  CB    . LEU A 1 3661 ? 140.546 152.748 130.768 1.00 111.65 ? 3661 LEU A CB    1 
ATOM   15970 C  CG    . LEU A 1 3661 ? 139.937 152.777 129.367 1.00 110.70 ? 3661 LEU A CG    1 
ATOM   15971 C  CD1   . LEU A 1 3661 ? 138.869 153.854 129.266 1.00 109.87 ? 3661 LEU A CD1   1 
ATOM   15972 C  CD2   . LEU A 1 3661 ? 141.024 152.988 128.329 1.00 109.07 ? 3661 LEU A CD2   1 
ATOM   15973 N  N     . ILE A 1 3662 ? 143.026 151.948 132.771 1.00 100.10 ? 3662 ILE A N     1 
ATOM   15974 C  CA    . ILE A 1 3662 ? 143.595 152.127 134.099 1.00 101.34 ? 3662 ILE A CA    1 
ATOM   15975 C  C     . ILE A 1 3662 ? 144.209 153.517 134.174 1.00 103.47 ? 3662 ILE A C     1 
ATOM   15976 O  O     . ILE A 1 3662 ? 144.911 153.950 133.253 1.00 105.19 ? 3662 ILE A O     1 
ATOM   15977 C  CB    . ILE A 1 3662 ? 144.632 151.031 134.428 1.00 100.82 ? 3662 ILE A CB    1 
ATOM   15978 C  CG1   . ILE A 1 3662 ? 145.193 151.226 135.835 1.00 101.61 ? 3662 ILE A CG1   1 
ATOM   15979 C  CG2   . ILE A 1 3662 ? 145.744 150.989 133.388 1.00 104.01 ? 3662 ILE A CG2   1 
ATOM   15980 C  CD1   . ILE A 1 3662 ? 145.822 149.984 136.402 1.00 101.03 ? 3662 ILE A CD1   1 
ATOM   15981 N  N     . THR A 1 3663 ? 143.920 154.229 135.261 1.00 116.68 ? 3663 THR A N     1 
ATOM   15982 C  CA    . THR A 1 3663 ? 144.376 155.606 135.435 1.00 116.83 ? 3663 THR A CA    1 
ATOM   15983 C  C     . THR A 1 3663 ? 145.744 155.584 136.103 1.00 116.28 ? 3663 THR A C     1 
ATOM   15984 O  O     . THR A 1 3663 ? 145.848 155.522 137.330 1.00 117.48 ? 3663 THR A O     1 
ATOM   15985 C  CB    . THR A 1 3663 ? 143.371 156.407 136.255 1.00 116.99 ? 3663 THR A CB    1 
ATOM   15986 O  OG1   . THR A 1 3663 ? 143.497 156.058 137.640 1.00 119.40 ? 3663 THR A OG1   1 
ATOM   15987 C  CG2   . THR A 1 3663 ? 141.953 156.111 135.793 1.00 112.31 ? 3663 THR A CG2   1 
ATOM   15988 N  N     . LEU A 1 3664 ? 146.799 155.636 135.294 1.00 113.56 ? 3664 LEU A N     1 
ATOM   15989 C  CA    . LEU A 1 3664 ? 148.165 155.691 135.802 1.00 114.60 ? 3664 LEU A CA    1 
ATOM   15990 C  C     . LEU A 1 3664 ? 148.542 157.155 135.993 1.00 115.52 ? 3664 LEU A C     1 
ATOM   15991 O  O     . LEU A 1 3664 ? 148.714 157.892 135.016 1.00 116.27 ? 3664 LEU A O     1 
ATOM   15992 C  CB    . LEU A 1 3664 ? 149.130 154.993 134.849 1.00 111.87 ? 3664 LEU A CB    1 
ATOM   15993 C  CG    . LEU A 1 3664 ? 150.610 155.225 135.152 1.00 113.25 ? 3664 LEU A CG    1 
ATOM   15994 C  CD1   . LEU A 1 3664 ? 151.013 154.438 136.383 1.00 113.25 ? 3664 LEU A CD1   1 
ATOM   15995 C  CD2   . LEU A 1 3664 ? 151.482 154.849 133.967 1.00 114.28 ? 3664 LEU A CD2   1 
ATOM   15996 N  N     . GLY A 1 3665 ? 148.677 157.573 137.244 1.00 119.85 ? 3665 GLY A N     1 
ATOM   15997 C  CA    . GLY A 1 3665 ? 148.948 158.973 137.522 1.00 118.98 ? 3665 GLY A CA    1 
ATOM   15998 C  C     . GLY A 1 3665 ? 147.777 159.831 137.086 1.00 120.11 ? 3665 GLY A C     1 
ATOM   15999 O  O     . GLY A 1 3665 ? 146.637 159.639 137.526 1.00 120.16 ? 3665 GLY A O     1 
ATOM   16000 N  N     . ASP A 1 3666 ? 148.049 160.794 136.207 1.00 130.79 ? 3666 ASP A N     1 
ATOM   16001 C  CA    . ASP A 1 3666 ? 147.020 161.672 135.665 1.00 130.95 ? 3666 ASP A CA    1 
ATOM   16002 C  C     . ASP A 1 3666 ? 146.645 161.318 134.232 1.00 131.18 ? 3666 ASP A C     1 
ATOM   16003 O  O     . ASP A 1 3666 ? 145.912 162.075 133.587 1.00 131.01 ? 3666 ASP A O     1 
ATOM   16004 C  CB    . ASP A 1 3666 ? 147.478 163.130 135.739 1.00 130.95 ? 3666 ASP A CB    1 
ATOM   16005 C  CG    . ASP A 1 3666 ? 148.773 163.373 134.989 1.00 132.63 ? 3666 ASP A CG    1 
ATOM   16006 O  OD1   . ASP A 1 3666 ? 149.767 162.672 135.274 1.00 135.01 ? 3666 ASP A OD1   1 
ATOM   16007 O  OD2   . ASP A 1 3666 ? 148.797 164.264 134.115 1.00 132.70 ? 3666 ASP A OD2   1 
ATOM   16008 N  N     . GLN A 1 3667 ? 147.126 160.188 133.718 1.00 121.43 ? 3667 GLN A N     1 
ATOM   16009 C  CA    . GLN A 1 3667 ? 146.894 159.783 132.338 1.00 119.30 ? 3667 GLN A CA    1 
ATOM   16010 C  C     . GLN A 1 3667 ? 146.115 158.477 132.312 1.00 116.78 ? 3667 GLN A C     1 
ATOM   16011 O  O     . GLN A 1 3667 ? 146.459 157.530 133.027 1.00 115.57 ? 3667 GLN A O     1 
ATOM   16012 C  CB    . GLN A 1 3667 ? 148.219 159.629 131.585 1.00 118.25 ? 3667 GLN A CB    1 
ATOM   16013 C  CG    . GLN A 1 3667 ? 148.073 159.145 130.154 1.00 119.45 ? 3667 GLN A CG    1 
ATOM   16014 C  CD    . GLN A 1 3667 ? 149.390 158.688 129.559 1.00 120.24 ? 3667 GLN A CD    1 
ATOM   16015 O  OE1   . GLN A 1 3667 ? 150.416 158.668 130.239 1.00 120.14 ? 3667 GLN A OE1   1 
ATOM   16016 N  NE2   . GLN A 1 3667 ? 149.368 158.316 128.285 1.00 117.68 ? 3667 GLN A NE2   1 
ATOM   16017 N  N     . ASP A 1 3668 ? 145.070 158.430 131.489 1.00 116.11 ? 3668 ASP A N     1 
ATOM   16018 C  CA    . ASP A 1 3668 ? 144.260 157.231 131.320 1.00 118.04 ? 3668 ASP A CA    1 
ATOM   16019 C  C     . ASP A 1 3668 ? 144.891 156.357 130.243 1.00 118.38 ? 3668 ASP A C     1 
ATOM   16020 O  O     . ASP A 1 3668 ? 145.119 156.817 129.119 1.00 119.65 ? 3668 ASP A O     1 
ATOM   16021 C  CB    . ASP A 1 3668 ? 142.824 157.599 130.950 1.00 119.02 ? 3668 ASP A CB    1 
ATOM   16022 C  CG    . ASP A 1 3668 ? 141.850 156.464 131.191 1.00 121.45 ? 3668 ASP A CG    1 
ATOM   16023 O  OD1   . ASP A 1 3668 ? 141.516 156.205 132.367 1.00 123.50 ? 3668 ASP A OD1   1 
ATOM   16024 O  OD2   . ASP A 1 3668 ? 141.416 155.833 130.205 1.00 117.83 ? 3668 ASP A OD2   1 
ATOM   16025 N  N     . ILE A 1 3669 ? 145.173 155.101 130.585 1.00 110.97 ? 3669 ILE A N     1 
ATOM   16026 C  CA    . ILE A 1 3669 ? 145.903 154.190 129.712 1.00 110.27 ? 3669 ILE A CA    1 
ATOM   16027 C  C     . ILE A 1 3669 ? 145.112 152.897 129.571 1.00 109.96 ? 3669 ILE A C     1 
ATOM   16028 O  O     . ILE A 1 3669 ? 144.661 152.328 130.571 1.00 109.60 ? 3669 ILE A O     1 
ATOM   16029 C  CB    . ILE A 1 3669 ? 147.317 153.900 130.252 1.00 107.68 ? 3669 ILE A CB    1 
ATOM   16030 C  CG1   . ILE A 1 3669 ? 148.151 155.181 130.262 1.00 110.77 ? 3669 ILE A CG1   1 
ATOM   16031 C  CG2   . ILE A 1 3669 ? 148.001 152.828 129.423 1.00 106.75 ? 3669 ILE A CG2   1 
ATOM   16032 C  CD1   . ILE A 1 3669 ? 149.459 155.044 130.995 1.00 111.96 ? 3669 ILE A CD1   1 
ATOM   16033 N  N     . ASP A 1 3670 ? 144.941 152.441 128.333 1.00 107.32 ? 3670 ASP A N     1 
ATOM   16034 C  CA    . ASP A 1 3670 ? 144.334 151.141 128.086 1.00 107.40 ? 3670 ASP A CA    1 
ATOM   16035 C  C     . ASP A 1 3670 ? 145.234 150.033 128.618 1.00 107.16 ? 3670 ASP A C     1 
ATOM   16036 O  O     . ASP A 1 3670 ? 146.461 150.104 128.512 1.00 107.71 ? 3670 ASP A O     1 
ATOM   16037 C  CB    . ASP A 1 3670 ? 144.084 150.949 126.590 1.00 106.60 ? 3670 ASP A CB    1 
ATOM   16038 C  CG    . ASP A 1 3670 ? 143.087 149.845 126.300 1.00 108.33 ? 3670 ASP A CG    1 
ATOM   16039 O  OD1   . ASP A 1 3670 ? 143.355 148.683 126.669 1.00 106.76 ? 3670 ASP A OD1   1 
ATOM   16040 O  OD2   . ASP A 1 3670 ? 142.033 150.140 125.698 1.00 108.29 ? 3670 ASP A OD2   1 
ATOM   16041 N  N     . LEU A 1 3671 ? 144.620 149.003 129.191 1.00 104.37 ? 3671 LEU A N     1 
ATOM   16042 C  CA    . LEU A 1 3671 ? 145.343 147.903 129.814 1.00 102.12 ? 3671 LEU A CA    1 
ATOM   16043 C  C     . LEU A 1 3671 ? 145.227 146.654 128.952 1.00 101.05 ? 3671 LEU A C     1 
ATOM   16044 O  O     . LEU A 1 3671 ? 144.119 146.241 128.595 1.00 99.46  ? 3671 LEU A O     1 
ATOM   16045 C  CB    . LEU A 1 3671 ? 144.807 147.621 131.219 1.00 99.13  ? 3671 LEU A CB    1 
ATOM   16046 C  CG    . LEU A 1 3671 ? 145.460 146.459 131.969 1.00 96.08  ? 3671 LEU A CG    1 
ATOM   16047 C  CD1   . LEU A 1 3671 ? 146.707 146.927 132.697 1.00 98.27  ? 3671 LEU A CD1   1 
ATOM   16048 C  CD2   . LEU A 1 3671 ? 144.479 145.820 132.937 1.00 96.73  ? 3671 LEU A CD2   1 
ATOM   16049 N  N     . SER A 1 3672 ? 146.371 146.059 128.623 1.00 96.94  ? 3672 SER A N     1 
ATOM   16050 C  CA    . SER A 1 3672 ? 146.399 144.807 127.879 1.00 92.80  ? 3672 SER A CA    1 
ATOM   16051 C  C     . SER A 1 3672 ? 146.321 143.623 128.840 1.00 94.95  ? 3672 SER A C     1 
ATOM   16052 O  O     . SER A 1 3672 ? 146.935 143.652 129.910 1.00 102.40 ? 3672 SER A O     1 
ATOM   16053 C  CB    . SER A 1 3672 ? 147.669 144.706 127.042 1.00 92.63  ? 3672 SER A CB    1 
ATOM   16054 O  OG    . SER A 1 3672 ? 147.823 143.407 126.499 1.00 97.87  ? 3672 SER A OG    1 
ATOM   16055 N  N     . PRO A 1 3673 ? 145.570 142.577 128.482 1.00 90.30  ? 3673 PRO A N     1 
ATOM   16056 C  CA    . PRO A 1 3673 ? 145.383 141.453 129.415 1.00 92.97  ? 3673 PRO A CA    1 
ATOM   16057 C  C     . PRO A 1 3673 ? 146.655 140.681 129.726 1.00 94.93  ? 3673 PRO A C     1 
ATOM   16058 O  O     . PRO A 1 3673 ? 146.699 139.990 130.751 1.00 92.09  ? 3673 PRO A O     1 
ATOM   16059 C  CB    . PRO A 1 3673 ? 144.359 140.566 128.695 1.00 92.67  ? 3673 PRO A CB    1 
ATOM   16060 C  CG    . PRO A 1 3673 ? 144.515 140.910 127.251 1.00 92.05  ? 3673 PRO A CG    1 
ATOM   16061 C  CD    . PRO A 1 3673 ? 144.852 142.370 127.213 1.00 91.61  ? 3673 PRO A CD    1 
ATOM   16062 N  N     . SER A 1 3674 ? 147.685 140.772 128.889 1.00 96.10  ? 3674 SER A N     1 
ATOM   16063 C  CA    . SER A 1 3674 ? 148.895 139.980 129.063 1.00 92.28  ? 3674 SER A CA    1 
ATOM   16064 C  C     . SER A 1 3674 ? 149.942 140.663 129.933 1.00 93.59  ? 3674 SER A C     1 
ATOM   16065 O  O     . SER A 1 3674 ? 151.047 140.130 130.077 1.00 96.17  ? 3674 SER A O     1 
ATOM   16066 C  CB    . SER A 1 3674 ? 149.506 139.647 127.699 1.00 90.13  ? 3674 SER A CB    1 
ATOM   16067 O  OG    . SER A 1 3674 ? 149.522 140.785 126.855 1.00 92.44  ? 3674 SER A OG    1 
ATOM   16068 N  N     . PHE A 1 3675 ? 149.633 141.821 130.509 1.00 85.68  ? 3675 PHE A N     1 
ATOM   16069 C  CA    . PHE A 1 3675 ? 150.616 142.539 131.307 1.00 79.52  ? 3675 PHE A CA    1 
ATOM   16070 C  C     . PHE A 1 3675 ? 150.805 141.873 132.664 1.00 83.08  ? 3675 PHE A C     1 
ATOM   16071 O  O     . PHE A 1 3675 ? 149.840 141.608 133.386 1.00 89.94  ? 3675 PHE A O     1 
ATOM   16072 C  CB    . PHE A 1 3675 ? 150.186 143.992 131.499 1.00 77.94  ? 3675 PHE A CB    1 
ATOM   16073 C  CG    . PHE A 1 3675 ? 150.953 144.712 132.568 1.00 80.31  ? 3675 PHE A CG    1 
ATOM   16074 C  CD1   . PHE A 1 3675 ? 152.248 145.141 132.339 1.00 81.90  ? 3675 PHE A CD1   1 
ATOM   16075 C  CD2   . PHE A 1 3675 ? 150.382 144.953 133.806 1.00 84.86  ? 3675 PHE A CD2   1 
ATOM   16076 C  CE1   . PHE A 1 3675 ? 152.957 145.802 133.321 1.00 84.39  ? 3675 PHE A CE1   1 
ATOM   16077 C  CE2   . PHE A 1 3675 ? 151.087 145.611 134.792 1.00 83.90  ? 3675 PHE A CE2   1 
ATOM   16078 C  CZ    . PHE A 1 3675 ? 152.375 146.038 134.549 1.00 83.69  ? 3675 PHE A CZ    1 
ATOM   16079 N  N     . VAL A 1 3676 ? 152.062 141.607 133.010 1.00 67.92  ? 3676 VAL A N     1 
ATOM   16080 C  CA    . VAL A 1 3676 ? 152.418 141.089 134.326 1.00 66.98  ? 3676 VAL A CA    1 
ATOM   16081 C  C     . VAL A 1 3676 ? 153.675 141.813 134.784 1.00 68.72  ? 3676 VAL A C     1 
ATOM   16082 O  O     . VAL A 1 3676 ? 154.600 142.031 133.999 1.00 75.77  ? 3676 VAL A O     1 
ATOM   16083 C  CB    . VAL A 1 3676 ? 152.618 139.555 134.299 1.00 65.23  ? 3676 VAL A CB    1 
ATOM   16084 C  CG1   . VAL A 1 3676 ? 151.276 138.841 134.305 1.00 67.45  ? 3676 VAL A CG1   1 
ATOM   16085 C  CG2   . VAL A 1 3676 ? 153.434 139.148 133.088 1.00 72.89  ? 3676 VAL A CG2   1 
ATOM   16086 N  N     . ILE A 1 3677 ? 153.703 142.188 136.060 1.00 63.16  ? 3677 ILE A N     1 
ATOM   16087 C  CA    . ILE A 1 3677 ? 154.807 142.953 136.625 1.00 60.87  ? 3677 ILE A CA    1 
ATOM   16088 C  C     . ILE A 1 3677 ? 155.367 142.210 137.829 1.00 69.51  ? 3677 ILE A C     1 
ATOM   16089 O  O     . ILE A 1 3677 ? 154.614 141.716 138.676 1.00 74.06  ? 3677 ILE A O     1 
ATOM   16090 C  CB    . ILE A 1 3677 ? 154.371 144.384 137.010 1.00 57.04  ? 3677 ILE A CB    1 
ATOM   16091 C  CG1   . ILE A 1 3677 ? 155.523 145.143 137.668 1.00 61.32  ? 3677 ILE A CG1   1 
ATOM   16092 C  CG2   . ILE A 1 3677 ? 153.149 144.361 137.910 1.00 68.02  ? 3677 ILE A CG2   1 
ATOM   16093 C  CD1   . ILE A 1 3677 ? 155.208 146.591 137.952 1.00 67.47  ? 3677 ILE A CD1   1 
ATOM   16094 N  N     . PHE A 1 3678 ? 156.694 142.114 137.892 1.00 67.74  ? 3678 PHE A N     1 
ATOM   16095 C  CA    . PHE A 1 3678 ? 157.399 141.490 139.005 1.00 57.66  ? 3678 PHE A CA    1 
ATOM   16096 C  C     . PHE A 1 3678 ? 158.261 142.541 139.687 1.00 60.58  ? 3678 PHE A C     1 
ATOM   16097 O  O     . PHE A 1 3678 ? 159.063 143.212 139.030 1.00 70.64  ? 3678 PHE A O     1 
ATOM   16098 C  CB    . PHE A 1 3678 ? 158.267 140.324 138.529 1.00 55.07  ? 3678 PHE A CB    1 
ATOM   16099 C  CG    . PHE A 1 3678 ? 157.503 139.241 137.829 1.00 55.50  ? 3678 PHE A CG    1 
ATOM   16100 C  CD1   . PHE A 1 3678 ? 156.889 138.233 138.549 1.00 64.33  ? 3678 PHE A CD1   1 
ATOM   16101 C  CD2   . PHE A 1 3678 ? 157.408 139.226 136.449 1.00 55.00  ? 3678 PHE A CD2   1 
ATOM   16102 C  CE1   . PHE A 1 3678 ? 156.189 137.233 137.907 1.00 70.86  ? 3678 PHE A CE1   1 
ATOM   16103 C  CE2   . PHE A 1 3678 ? 156.709 138.229 135.802 1.00 60.20  ? 3678 PHE A CE2   1 
ATOM   16104 C  CZ    . PHE A 1 3678 ? 156.099 137.231 136.532 1.00 70.66  ? 3678 PHE A CZ    1 
ATOM   16105 N  N     . LEU A 1 3679 ? 158.098 142.681 140.999 1.00 65.18  ? 3679 LEU A N     1 
ATOM   16106 C  CA    . LEU A 1 3679 ? 158.935 143.570 141.791 1.00 65.51  ? 3679 LEU A CA    1 
ATOM   16107 C  C     . LEU A 1 3679 ? 159.996 142.746 142.508 1.00 67.90  ? 3679 LEU A C     1 
ATOM   16108 O  O     . LEU A 1 3679 ? 159.684 141.715 143.112 1.00 78.88  ? 3679 LEU A O     1 
ATOM   16109 C  CB    . LEU A 1 3679 ? 158.092 144.353 142.798 1.00 64.19  ? 3679 LEU A CB    1 
ATOM   16110 C  CG    . LEU A 1 3679 ? 156.829 145.016 142.248 1.00 61.64  ? 3679 LEU A CG    1 
ATOM   16111 C  CD1   . LEU A 1 3679 ? 156.136 145.827 143.327 1.00 65.84  ? 3679 LEU A CD1   1 
ATOM   16112 C  CD2   . LEU A 1 3679 ? 157.163 145.893 141.055 1.00 64.56  ? 3679 LEU A CD2   1 
ATOM   16113 N  N     . SER A 1 3680 ? 161.248 143.193 142.434 1.00 62.79  ? 3680 SER A N     1 
ATOM   16114 C  CA    . SER A 1 3680 ? 162.355 142.439 143.002 1.00 67.07  ? 3680 SER A CA    1 
ATOM   16115 C  C     . SER A 1 3680 ? 163.237 143.356 143.834 1.00 70.71  ? 3680 SER A C     1 
ATOM   16116 O  O     . SER A 1 3680 ? 163.477 144.510 143.474 1.00 76.08  ? 3680 SER A O     1 
ATOM   16117 C  CB    . SER A 1 3680 ? 163.193 141.762 141.912 1.00 70.37  ? 3680 SER A CB    1 
ATOM   16118 O  OG    . SER A 1 3680 ? 163.829 142.724 141.091 1.00 80.56  ? 3680 SER A OG    1 
ATOM   16119 N  N     . THR A 1 3681 ? 163.724 142.824 144.953 1.00 70.02  ? 3681 THR A N     1 
ATOM   16120 C  CA    . THR A 1 3681 ? 164.645 143.543 145.820 1.00 72.23  ? 3681 THR A CA    1 
ATOM   16121 C  C     . THR A 1 3681 ? 165.780 142.613 146.224 1.00 74.34  ? 3681 THR A C     1 
ATOM   16122 O  O     . THR A 1 3681 ? 165.603 141.396 146.317 1.00 74.98  ? 3681 THR A O     1 
ATOM   16123 C  CB    . THR A 1 3681 ? 163.946 144.094 147.071 1.00 69.66  ? 3681 THR A CB    1 
ATOM   16124 O  OG1   . THR A 1 3681 ? 164.898 144.788 147.886 1.00 75.15  ? 3681 THR A OG1   1 
ATOM   16125 C  CG2   . THR A 1 3681 ? 163.320 142.970 147.876 1.00 70.27  ? 3681 THR A CG2   1 
ATOM   16126 N  N     . ARG A 1 3682 ? 166.951 143.200 146.453 1.00 90.14  ? 3682 ARG A N     1 
ATOM   16127 C  CA    . ARG A 1 3682 ? 168.134 142.449 146.847 1.00 85.19  ? 3682 ARG A CA    1 
ATOM   16128 C  C     . ARG A 1 3682 ? 168.407 142.512 148.342 1.00 86.67  ? 3682 ARG A C     1 
ATOM   16129 O  O     . ARG A 1 3682 ? 169.393 141.928 148.802 1.00 91.62  ? 3682 ARG A O     1 
ATOM   16130 C  CB    . ARG A 1 3682 ? 169.361 142.957 146.084 1.00 84.62  ? 3682 ARG A CB    1 
ATOM   16131 C  CG    . ARG A 1 3682 ? 169.307 142.728 144.585 1.00 81.63  ? 3682 ARG A CG    1 
ATOM   16132 C  CD    . ARG A 1 3682 ? 170.584 143.205 143.912 1.00 83.40  ? 3682 ARG A CD    1 
ATOM   16133 N  NE    . ARG A 1 3682 ? 170.850 144.615 144.173 1.00 89.56  ? 3682 ARG A NE    1 
ATOM   16134 C  CZ    . ARG A 1 3682 ? 171.800 145.061 144.983 1.00 89.60  ? 3682 ARG A CZ    1 
ATOM   16135 N  NH1   . ARG A 1 3682 ? 172.600 144.232 145.632 1.00 88.85  ? 3682 ARG A NH1   1 
ATOM   16136 N  NH2   . ARG A 1 3682 ? 171.950 146.372 145.147 1.00 87.72  ? 3682 ARG A NH2   1 
ATOM   16137 N  N     . ASP A 1 3683 ? 167.566 143.199 149.109 1.00 86.02  ? 3683 ASP A N     1 
ATOM   16138 C  CA    . ASP A 1 3683 ? 167.794 143.370 150.538 1.00 86.93  ? 3683 ASP A CA    1 
ATOM   16139 C  C     . ASP A 1 3683 ? 166.818 142.505 151.321 1.00 85.70  ? 3683 ASP A C     1 
ATOM   16140 O  O     . ASP A 1 3683 ? 165.621 142.827 151.375 1.00 89.37  ? 3683 ASP A O     1 
ATOM   16141 C  CB    . ASP A 1 3683 ? 167.639 144.840 150.931 1.00 88.67  ? 3683 ASP A CB    1 
ATOM   16142 C  CG    . ASP A 1 3683 ? 168.384 145.185 152.203 1.00 92.54  ? 3683 ASP A CG    1 
ATOM   16143 O  OD1   . ASP A 1 3683 ? 169.154 144.333 152.693 1.00 95.84  ? 3683 ASP A OD1   1 
ATOM   16144 O  OD2   . ASP A 1 3683 ? 168.202 146.311 152.712 1.00 93.02  ? 3683 ASP A OD2   1 
ATOM   16145 N  N     . PRO A 1 3684 ? 167.266 141.407 151.934 1.00 80.73  ? 3684 PRO A N     1 
ATOM   16146 C  CA    . PRO A 1 3684 ? 166.337 140.575 152.714 1.00 79.67  ? 3684 PRO A CA    1 
ATOM   16147 C  C     . PRO A 1 3684 ? 165.848 141.234 153.990 1.00 85.14  ? 3684 PRO A C     1 
ATOM   16148 O  O     . PRO A 1 3684 ? 164.831 140.793 154.540 1.00 89.59  ? 3684 PRO A O     1 
ATOM   16149 C  CB    . PRO A 1 3684 ? 167.164 139.319 153.019 1.00 83.26  ? 3684 PRO A CB    1 
ATOM   16150 C  CG    . PRO A 1 3684 ? 168.578 139.788 152.976 1.00 87.51  ? 3684 PRO A CG    1 
ATOM   16151 C  CD    . PRO A 1 3684 ? 168.631 140.856 151.922 1.00 83.41  ? 3684 PRO A CD    1 
ATOM   16152 N  N     . THR A 1 3685 ? 166.528 142.269 154.478 1.00 95.22  ? 3685 THR A N     1 
ATOM   16153 C  CA    . THR A 1 3685 ? 166.196 142.900 155.748 1.00 93.41  ? 3685 THR A CA    1 
ATOM   16154 C  C     . THR A 1 3685 ? 165.374 144.172 155.583 1.00 93.79  ? 3685 THR A C     1 
ATOM   16155 O  O     . THR A 1 3685 ? 165.205 144.916 156.554 1.00 100.08 ? 3685 THR A O     1 
ATOM   16156 C  CB    . THR A 1 3685 ? 167.472 143.212 156.532 1.00 96.52  ? 3685 THR A CB    1 
ATOM   16157 O  OG1   . THR A 1 3685 ? 167.952 144.513 156.168 1.00 91.65  ? 3685 THR A OG1   1 
ATOM   16158 C  CG2   . THR A 1 3685 ? 168.547 142.179 156.234 1.00 97.61  ? 3685 THR A CG2   1 
ATOM   16159 N  N     . VAL A 1 3686 ? 164.864 144.442 154.381 1.00 98.31  ? 3686 VAL A N     1 
ATOM   16160 C  CA    . VAL A 1 3686 ? 164.108 145.666 154.149 1.00 98.57  ? 3686 VAL A CA    1 
ATOM   16161 C  C     . VAL A 1 3686 ? 162.753 145.578 154.838 1.00 101.34 ? 3686 VAL A C     1 
ATOM   16162 O  O     . VAL A 1 3686 ? 162.143 144.503 154.926 1.00 104.33 ? 3686 VAL A O     1 
ATOM   16163 C  CB    . VAL A 1 3686 ? 163.959 145.923 152.639 1.00 99.85  ? 3686 VAL A CB    1 
ATOM   16164 C  CG1   . VAL A 1 3686 ? 163.152 144.815 151.981 1.00 98.81  ? 3686 VAL A CG1   1 
ATOM   16165 C  CG2   . VAL A 1 3686 ? 163.320 147.281 152.387 1.00 97.06  ? 3686 VAL A CG2   1 
ATOM   16166 N  N     . GLU A 1 3687 ? 162.284 146.711 155.351 1.00 105.00 ? 3687 GLU A N     1 
ATOM   16167 C  CA    . GLU A 1 3687 ? 160.963 146.821 155.952 1.00 103.04 ? 3687 GLU A CA    1 
ATOM   16168 C  C     . GLU A 1 3687 ? 160.023 147.531 154.987 1.00 102.86 ? 3687 GLU A C     1 
ATOM   16169 O  O     . GLU A 1 3687 ? 160.390 148.539 154.376 1.00 105.55 ? 3687 GLU A O     1 
ATOM   16170 C  CB    . GLU A 1 3687 ? 161.025 147.580 157.279 1.00 105.16 ? 3687 GLU A CB    1 
ATOM   16171 C  CG    . GLU A 1 3687 ? 161.621 146.789 158.436 1.00 106.12 ? 3687 GLU A CG    1 
ATOM   16172 C  CD    . GLU A 1 3687 ? 160.612 145.885 159.124 1.00 111.52 ? 3687 GLU A CD    1 
ATOM   16173 O  OE1   . GLU A 1 3687 ? 159.793 145.251 158.426 1.00 114.94 ? 3687 GLU A OE1   1 
ATOM   16174 O  OE2   . GLU A 1 3687 ? 160.637 145.810 160.370 1.00 109.01 ? 3687 GLU A OE2   1 
ATOM   16175 N  N     . PHE A 1 3688 ? 158.810 147.002 154.854 1.00 90.30  ? 3688 PHE A N     1 
ATOM   16176 C  CA    . PHE A 1 3688 ? 157.850 147.549 153.912 1.00 95.81  ? 3688 PHE A CA    1 
ATOM   16177 C  C     . PHE A 1 3688 ? 156.647 148.128 154.646 1.00 98.25  ? 3688 PHE A C     1 
ATOM   16178 O  O     . PHE A 1 3688 ? 156.217 147.584 155.668 1.00 99.26  ? 3688 PHE A O     1 
ATOM   16179 C  CB    . PHE A 1 3688 ? 157.370 146.476 152.927 1.00 93.27  ? 3688 PHE A CB    1 
ATOM   16180 C  CG    . PHE A 1 3688 ? 158.375 146.132 151.867 1.00 97.12  ? 3688 PHE A CG    1 
ATOM   16181 C  CD1   . PHE A 1 3688 ? 158.784 147.080 150.946 1.00 94.51  ? 3688 PHE A CD1   1 
ATOM   16182 C  CD2   . PHE A 1 3688 ? 158.907 144.857 151.791 1.00 93.57  ? 3688 PHE A CD2   1 
ATOM   16183 C  CE1   . PHE A 1 3688 ? 159.707 146.763 149.969 1.00 92.24  ? 3688 PHE A CE1   1 
ATOM   16184 C  CE2   . PHE A 1 3688 ? 159.830 144.534 150.816 1.00 88.77  ? 3688 PHE A CE2   1 
ATOM   16185 C  CZ    . PHE A 1 3688 ? 160.230 145.488 149.905 1.00 91.12  ? 3688 PHE A CZ    1 
ATOM   16186 N  N     . PRO A 1 3689 ? 156.087 149.235 154.153 1.00 90.11  ? 3689 PRO A N     1 
ATOM   16187 C  CA    . PRO A 1 3689 ? 154.867 149.761 154.757 1.00 86.52  ? 3689 PRO A CA    1 
ATOM   16188 C  C     . PRO A 1 3689 ? 153.720 148.786 154.572 1.00 85.85  ? 3689 PRO A C     1 
ATOM   16189 O  O     . PRO A 1 3689 ? 153.650 148.074 153.556 1.00 86.08  ? 3689 PRO A O     1 
ATOM   16190 C  CB    . PRO A 1 3689 ? 154.625 151.070 153.984 1.00 88.83  ? 3689 PRO A CB    1 
ATOM   16191 C  CG    . PRO A 1 3689 ? 155.336 150.881 152.690 1.00 84.89  ? 3689 PRO A CG    1 
ATOM   16192 C  CD    . PRO A 1 3689 ? 156.537 150.043 153.006 1.00 84.13  ? 3689 PRO A CD    1 
ATOM   16193 N  N     . PRO A 1 3690 ? 152.787 148.723 155.527 1.00 83.71  ? 3690 PRO A N     1 
ATOM   16194 C  CA    . PRO A 1 3690 ? 151.743 147.684 155.470 1.00 85.10  ? 3690 PRO A CA    1 
ATOM   16195 C  C     . PRO A 1 3690 ? 150.908 147.711 154.201 1.00 86.70  ? 3690 PRO A C     1 
ATOM   16196 O  O     . PRO A 1 3690 ? 150.453 146.652 153.751 1.00 89.56  ? 3690 PRO A O     1 
ATOM   16197 C  CB    . PRO A 1 3690 ? 150.890 147.981 156.710 1.00 85.14  ? 3690 PRO A CB    1 
ATOM   16198 C  CG    . PRO A 1 3690 ? 151.807 148.711 157.634 1.00 86.30  ? 3690 PRO A CG    1 
ATOM   16199 C  CD    . PRO A 1 3690 ? 152.699 149.532 156.753 1.00 86.03  ? 3690 PRO A CD    1 
ATOM   16200 N  N     . ASP A 1 3691 ? 150.690 148.887 153.609 1.00 88.40  ? 3691 ASP A N     1 
ATOM   16201 C  CA    . ASP A 1 3691 ? 149.912 148.955 152.376 1.00 91.94  ? 3691 ASP A CA    1 
ATOM   16202 C  C     . ASP A 1 3691 ? 150.608 148.217 151.238 1.00 91.99  ? 3691 ASP A C     1 
ATOM   16203 O  O     . ASP A 1 3691 ? 149.958 147.504 150.463 1.00 93.27  ? 3691 ASP A O     1 
ATOM   16204 C  CB    . ASP A 1 3691 ? 149.651 150.413 152.000 1.00 87.43  ? 3691 ASP A CB    1 
ATOM   16205 C  CG    . ASP A 1 3691 ? 150.926 151.221 151.870 1.00 89.01  ? 3691 ASP A CG    1 
ATOM   16206 O  OD1   . ASP A 1 3691 ? 152.011 150.675 152.156 1.00 89.88  ? 3691 ASP A OD1   1 
ATOM   16207 O  OD2   . ASP A 1 3691 ? 150.842 152.404 151.480 1.00 91.35  ? 3691 ASP A OD2   1 
ATOM   16208 N  N     . LEU A 1 3692 ? 151.929 148.375 151.119 1.00 80.33  ? 3692 LEU A N     1 
ATOM   16209 C  CA    . LEU A 1 3692 ? 152.660 147.655 150.081 1.00 76.07  ? 3692 LEU A CA    1 
ATOM   16210 C  C     . LEU A 1 3692 ? 152.617 146.151 150.318 1.00 76.76  ? 3692 LEU A C     1 
ATOM   16211 O  O     . LEU A 1 3692 ? 152.455 145.376 149.369 1.00 79.18  ? 3692 LEU A O     1 
ATOM   16212 C  CB    . LEU A 1 3692 ? 154.103 148.150 150.008 1.00 77.34  ? 3692 LEU A CB    1 
ATOM   16213 C  CG    . LEU A 1 3692 ? 154.941 147.551 148.878 1.00 76.35  ? 3692 LEU A CG    1 
ATOM   16214 C  CD1   . LEU A 1 3692 ? 154.183 147.607 147.564 1.00 73.87  ? 3692 LEU A CD1   1 
ATOM   16215 C  CD2   . LEU A 1 3692 ? 156.268 148.276 148.755 1.00 80.89  ? 3692 LEU A CD2   1 
ATOM   16216 N  N     . CYS A 1 3693 ? 152.759 145.716 151.574 1.00 73.44  ? 3693 CYS A N     1 
ATOM   16217 C  CA    . CYS A 1 3693 ? 152.619 144.295 151.873 1.00 74.69  ? 3693 CYS A CA    1 
ATOM   16218 C  C     . CYS A 1 3693 ? 151.226 143.790 151.528 1.00 77.24  ? 3693 CYS A C     1 
ATOM   16219 O  O     . CYS A 1 3693 ? 151.063 142.624 151.150 1.00 83.66  ? 3693 CYS A O     1 
ATOM   16220 C  CB    . CYS A 1 3693 ? 152.931 144.020 153.344 1.00 77.57  ? 3693 CYS A CB    1 
ATOM   16221 S  SG    . CYS A 1 3693 ? 154.159 145.112 154.082 1.00 97.72  ? 3693 CYS A SG    1 
ATOM   16222 N  N     . SER A 1 3694 ? 150.211 144.645 151.659 1.00 69.94  ? 3694 SER A N     1 
ATOM   16223 C  CA    . SER A 1 3694 ? 148.872 144.268 151.224 1.00 72.44  ? 3694 SER A CA    1 
ATOM   16224 C  C     . SER A 1 3694 ? 148.784 144.154 149.710 1.00 71.88  ? 3694 SER A C     1 
ATOM   16225 O  O     . SER A 1 3694 ? 148.095 143.266 149.195 1.00 77.24  ? 3694 SER A O     1 
ATOM   16226 C  CB    . SER A 1 3694 ? 147.850 145.284 151.728 1.00 75.61  ? 3694 SER A CB    1 
ATOM   16227 O  OG    . SER A 1 3694 ? 147.978 146.514 151.038 1.00 80.00  ? 3694 SER A OG    1 
ATOM   16228 N  N     . ARG A 1 3695 ? 149.473 145.034 148.983 1.00 67.28  ? 3695 ARG A N     1 
ATOM   16229 C  CA    . ARG A 1 3695 ? 149.294 145.120 147.539 1.00 65.36  ? 3695 ARG A CA    1 
ATOM   16230 C  C     . ARG A 1 3695 ? 150.044 144.045 146.763 1.00 65.64  ? 3695 ARG A C     1 
ATOM   16231 O  O     . ARG A 1 3695 ? 149.721 143.815 145.593 1.00 68.45  ? 3695 ARG A O     1 
ATOM   16232 C  CB    . ARG A 1 3695 ? 149.727 146.500 147.042 1.00 62.91  ? 3695 ARG A CB    1 
ATOM   16233 C  CG    . ARG A 1 3695 ? 148.602 147.515 147.003 1.00 62.86  ? 3695 ARG A CG    1 
ATOM   16234 C  CD    . ARG A 1 3695 ? 149.061 148.825 146.394 1.00 68.74  ? 3695 ARG A CD    1 
ATOM   16235 N  NE    . ARG A 1 3695 ? 149.457 149.791 147.410 1.00 70.26  ? 3695 ARG A NE    1 
ATOM   16236 C  CZ    . ARG A 1 3695 ? 148.619 150.612 148.028 1.00 71.03  ? 3695 ARG A CZ    1 
ATOM   16237 N  NH1   . ARG A 1 3695 ? 147.322 150.599 147.768 1.00 71.91  ? 3695 ARG A NH1   1 
ATOM   16238 N  NH2   . ARG A 1 3695 ? 149.094 151.468 148.928 1.00 72.34  ? 3695 ARG A NH2   1 
ATOM   16239 N  N     . VAL A 1 3696 ? 151.030 143.384 147.370 1.00 63.38  ? 3696 VAL A N     1 
ATOM   16240 C  CA    . VAL A 1 3696 ? 151.842 142.398 146.670 1.00 59.45  ? 3696 VAL A CA    1 
ATOM   16241 C  C     . VAL A 1 3696 ? 151.956 141.139 147.517 1.00 63.16  ? 3696 VAL A C     1 
ATOM   16242 O  O     . VAL A 1 3696 ? 151.743 141.153 148.731 1.00 72.71  ? 3696 VAL A O     1 
ATOM   16243 C  CB    . VAL A 1 3696 ? 153.251 142.930 146.330 1.00 62.53  ? 3696 VAL A CB    1 
ATOM   16244 C  CG1   . VAL A 1 3696 ? 153.165 144.140 145.412 1.00 65.39  ? 3696 VAL A CG1   1 
ATOM   16245 C  CG2   . VAL A 1 3696 ? 154.009 143.260 147.599 1.00 69.04  ? 3696 VAL A CG2   1 
ATOM   16246 N  N     . THR A 1 3697 ? 152.299 140.038 146.854 1.00 56.72  ? 3697 THR A N     1 
ATOM   16247 C  CA    . THR A 1 3697 ? 152.584 138.775 147.520 1.00 67.11  ? 3697 THR A CA    1 
ATOM   16248 C  C     . THR A 1 3697 ? 154.092 138.564 147.558 1.00 69.15  ? 3697 THR A C     1 
ATOM   16249 O  O     . THR A 1 3697 ? 154.775 138.723 146.541 1.00 69.01  ? 3697 THR A O     1 
ATOM   16250 C  CB    . THR A 1 3697 ? 151.891 137.602 146.821 1.00 65.28  ? 3697 THR A CB    1 
ATOM   16251 O  OG1   . THR A 1 3697 ? 152.324 136.368 147.409 1.00 64.42  ? 3697 THR A OG1   1 
ATOM   16252 C  CG2   . THR A 1 3697 ? 152.197 137.588 145.333 1.00 57.91  ? 3697 THR A CG2   1 
ATOM   16253 N  N     . PHE A 1 3698 ? 154.609 138.232 148.736 1.00 65.66  ? 3698 PHE A N     1 
ATOM   16254 C  CA    . PHE A 1 3698 ? 156.046 138.117 148.921 1.00 55.53  ? 3698 PHE A CA    1 
ATOM   16255 C  C     . PHE A 1 3698 ? 156.536 136.737 148.510 1.00 65.47  ? 3698 PHE A C     1 
ATOM   16256 O  O     . PHE A 1 3698 ? 155.899 135.722 148.801 1.00 73.87  ? 3698 PHE A O     1 
ATOM   16257 C  CB    . PHE A 1 3698 ? 156.414 138.391 150.378 1.00 62.68  ? 3698 PHE A CB    1 
ATOM   16258 C  CG    . PHE A 1 3698 ? 156.288 139.831 150.766 1.00 60.18  ? 3698 PHE A CG    1 
ATOM   16259 C  CD1   . PHE A 1 3698 ? 157.322 140.718 150.530 1.00 64.22  ? 3698 PHE A CD1   1 
ATOM   16260 C  CD2   . PHE A 1 3698 ? 155.132 140.301 151.360 1.00 62.29  ? 3698 PHE A CD2   1 
ATOM   16261 C  CE1   . PHE A 1 3698 ? 157.207 142.044 150.883 1.00 62.91  ? 3698 PHE A CE1   1 
ATOM   16262 C  CE2   . PHE A 1 3698 ? 155.011 141.626 151.716 1.00 67.68  ? 3698 PHE A CE2   1 
ATOM   16263 C  CZ    . PHE A 1 3698 ? 156.050 142.499 151.477 1.00 64.07  ? 3698 PHE A CZ    1 
ATOM   16264 N  N     . VAL A 1 3699 ? 157.674 136.708 147.821 1.00 61.42  ? 3699 VAL A N     1 
ATOM   16265 C  CA    . VAL A 1 3699 ? 158.328 135.469 147.413 1.00 58.23  ? 3699 VAL A CA    1 
ATOM   16266 C  C     . VAL A 1 3699 ? 159.771 135.572 147.889 1.00 64.10  ? 3699 VAL A C     1 
ATOM   16267 O  O     . VAL A 1 3699 ? 160.623 136.131 147.190 1.00 69.24  ? 3699 VAL A O     1 
ATOM   16268 C  CB    . VAL A 1 3699 ? 158.257 135.237 145.901 1.00 53.95  ? 3699 VAL A CB    1 
ATOM   16269 C  CG1   . VAL A 1 3699 ? 158.844 133.887 145.552 1.00 59.65  ? 3699 VAL A CG1   1 
ATOM   16270 C  CG2   . VAL A 1 3699 ? 156.821 135.329 145.416 1.00 58.77  ? 3699 VAL A CG2   1 
ATOM   16271 N  N     . ASN A 1 3700 ? 160.050 135.040 149.075 1.00 60.97  ? 3700 ASN A N     1 
ATOM   16272 C  CA    . ASN A 1 3700 ? 161.365 135.139 149.694 1.00 52.76  ? 3700 ASN A CA    1 
ATOM   16273 C  C     . ASN A 1 3700 ? 162.235 133.981 149.222 1.00 59.33  ? 3700 ASN A C     1 
ATOM   16274 O  O     . ASN A 1 3700 ? 161.882 132.813 149.418 1.00 66.67  ? 3700 ASN A O     1 
ATOM   16275 C  CB    . ASN A 1 3700 ? 161.248 135.134 151.217 1.00 55.16  ? 3700 ASN A CB    1 
ATOM   16276 C  CG    . ASN A 1 3700 ? 162.407 135.835 151.892 1.00 62.86  ? 3700 ASN A CG    1 
ATOM   16277 O  OD1   . ASN A 1 3700 ? 163.391 136.193 151.246 1.00 72.57  ? 3700 ASN A OD1   1 
ATOM   16278 N  ND2   . ASN A 1 3700 ? 162.300 136.033 153.200 1.00 60.98  ? 3700 ASN A ND2   1 
ATOM   16279 N  N     . PHE A 1 3701 ? 163.369 134.307 148.601 1.00 62.48  ? 3701 PHE A N     1 
ATOM   16280 C  CA    . PHE A 1 3701 ? 164.331 133.305 148.148 1.00 63.88  ? 3701 PHE A CA    1 
ATOM   16281 C  C     . PHE A 1 3701 ? 165.446 133.203 149.185 1.00 68.35  ? 3701 PHE A C     1 
ATOM   16282 O  O     . PHE A 1 3701 ? 166.557 133.700 149.003 1.00 68.93  ? 3701 PHE A O     1 
ATOM   16283 C  CB    . PHE A 1 3701 ? 164.873 133.661 146.767 1.00 62.75  ? 3701 PHE A CB    1 
ATOM   16284 C  CG    . PHE A 1 3701 ? 164.010 133.187 145.636 1.00 58.84  ? 3701 PHE A CG    1 
ATOM   16285 C  CD1   . PHE A 1 3701 ? 162.861 133.873 145.287 1.00 60.07  ? 3701 PHE A CD1   1 
ATOM   16286 C  CD2   . PHE A 1 3701 ? 164.352 132.056 144.917 1.00 61.07  ? 3701 PHE A CD2   1 
ATOM   16287 C  CE1   . PHE A 1 3701 ? 162.069 133.436 144.245 1.00 60.41  ? 3701 PHE A CE1   1 
ATOM   16288 C  CE2   . PHE A 1 3701 ? 163.564 131.617 143.874 1.00 62.56  ? 3701 PHE A CE2   1 
ATOM   16289 C  CZ    . PHE A 1 3701 ? 162.422 132.308 143.537 1.00 61.43  ? 3701 PHE A CZ    1 
ATOM   16290 N  N     . THR A 1 3702 ? 165.133 132.543 150.293 1.00 73.32  ? 3702 THR A N     1 
ATOM   16291 C  CA    . THR A 1 3702 ? 166.098 132.292 151.351 1.00 73.68  ? 3702 THR A CA    1 
ATOM   16292 C  C     . THR A 1 3702 ? 166.971 131.097 150.992 1.00 74.63  ? 3702 THR A C     1 
ATOM   16293 O  O     . THR A 1 3702 ? 166.628 130.280 150.133 1.00 75.53  ? 3702 THR A O     1 
ATOM   16294 C  CB    . THR A 1 3702 ? 165.394 132.041 152.687 1.00 74.25  ? 3702 THR A CB    1 
ATOM   16295 O  OG1   . THR A 1 3702 ? 164.382 131.041 152.516 1.00 78.64  ? 3702 THR A OG1   1 
ATOM   16296 C  CG2   . THR A 1 3702 ? 164.754 133.320 153.201 1.00 74.86  ? 3702 THR A CG2   1 
ATOM   16297 N  N     . VAL A 1 3703 ? 168.115 131.006 151.659 1.00 73.81  ? 3703 VAL A N     1 
ATOM   16298 C  CA    . VAL A 1 3703 ? 169.044 129.901 151.457 1.00 75.67  ? 3703 VAL A CA    1 
ATOM   16299 C  C     . VAL A 1 3703 ? 168.822 128.882 152.567 1.00 74.29  ? 3703 VAL A C     1 
ATOM   16300 O  O     . VAL A 1 3703 ? 168.964 129.200 153.752 1.00 75.27  ? 3703 VAL A O     1 
ATOM   16301 C  CB    . VAL A 1 3703 ? 170.499 130.391 151.439 1.00 71.29  ? 3703 VAL A CB    1 
ATOM   16302 C  CG1   . VAL A 1 3703 ? 171.433 129.258 151.049 1.00 67.74  ? 3703 VAL A CG1   1 
ATOM   16303 C  CG2   . VAL A 1 3703 ? 170.650 131.565 150.487 1.00 75.37  ? 3703 VAL A CG2   1 
ATOM   16304 N  N     . THR A 1 3704 ? 168.471 127.660 152.185 1.00 76.11  ? 3704 THR A N     1 
ATOM   16305 C  CA    . THR A 1 3704 ? 168.229 126.584 153.131 1.00 74.75  ? 3704 THR A CA    1 
ATOM   16306 C  C     . THR A 1 3704 ? 169.504 125.782 153.361 1.00 79.03  ? 3704 THR A C     1 
ATOM   16307 O  O     . THR A 1 3704 ? 170.452 125.836 152.575 1.00 85.58  ? 3704 THR A O     1 
ATOM   16308 C  CB    . THR A 1 3704 ? 167.114 125.659 152.636 1.00 77.33  ? 3704 THR A CB    1 
ATOM   16309 O  OG1   . THR A 1 3704 ? 167.486 125.091 151.375 1.00 78.66  ? 3704 THR A OG1   1 
ATOM   16310 C  CG2   . THR A 1 3704 ? 165.820 126.431 152.472 1.00 82.45  ? 3704 THR A CG2   1 
ATOM   16311 N  N     . ARG A 1 3705 ? 169.515 125.036 154.467 1.00 79.86  ? 3705 ARG A N     1 
ATOM   16312 C  CA    . ARG A 1 3705 ? 170.683 124.227 154.798 1.00 76.91  ? 3705 ARG A CA    1 
ATOM   16313 C  C     . ARG A 1 3705 ? 170.908 123.131 153.765 1.00 78.43  ? 3705 ARG A C     1 
ATOM   16314 O  O     . ARG A 1 3705 ? 172.048 122.867 153.368 1.00 87.36  ? 3705 ARG A O     1 
ATOM   16315 C  CB    . ARG A 1 3705 ? 170.523 123.629 156.195 1.00 80.41  ? 3705 ARG A CB    1 
ATOM   16316 C  CG    . ARG A 1 3705 ? 170.658 124.648 157.314 1.00 79.26  ? 3705 ARG A CG    1 
ATOM   16317 C  CD    . ARG A 1 3705 ? 170.456 124.012 158.678 1.00 79.67  ? 3705 ARG A CD    1 
ATOM   16318 N  NE    . ARG A 1 3705 ? 170.991 124.843 159.749 1.00 81.27  ? 3705 ARG A NE    1 
ATOM   16319 C  CZ    . ARG A 1 3705 ? 172.253 124.821 160.156 1.00 83.41  ? 3705 ARG A CZ    1 
ATOM   16320 N  NH1   . ARG A 1 3705 ? 173.143 124.016 159.601 1.00 84.62  ? 3705 ARG A NH1   1 
ATOM   16321 N  NH2   . ARG A 1 3705 ? 172.630 125.627 161.144 1.00 81.89  ? 3705 ARG A NH2   1 
ATOM   16322 N  N     . SER A 1 3706 ? 169.831 122.482 153.315 1.00 70.33  ? 3706 SER A N     1 
ATOM   16323 C  CA    . SER A 1 3706 ? 169.969 121.402 152.342 1.00 74.04  ? 3706 SER A CA    1 
ATOM   16324 C  C     . SER A 1 3706 ? 170.480 121.918 151.002 1.00 77.82  ? 3706 SER A C     1 
ATOM   16325 O  O     . SER A 1 3706 ? 171.341 121.286 150.376 1.00 87.55  ? 3706 SER A O     1 
ATOM   16326 C  CB    . SER A 1 3706 ? 168.632 120.684 152.167 1.00 83.53  ? 3706 SER A CB    1 
ATOM   16327 O  OG    . SER A 1 3706 ? 168.059 120.365 153.423 1.00 89.17  ? 3706 SER A OG    1 
ATOM   16328 N  N     . SER A 1 3707 ? 169.960 123.058 150.541 1.00 73.57  ? 3707 SER A N     1 
ATOM   16329 C  CA    . SER A 1 3707 ? 170.413 123.610 149.268 1.00 75.78  ? 3707 SER A CA    1 
ATOM   16330 C  C     . SER A 1 3707 ? 171.880 124.004 149.330 1.00 75.91  ? 3707 SER A C     1 
ATOM   16331 O  O     . SER A 1 3707 ? 172.637 123.759 148.384 1.00 78.43  ? 3707 SER A O     1 
ATOM   16332 C  CB    . SER A 1 3707 ? 169.558 124.814 148.879 1.00 78.86  ? 3707 SER A CB    1 
ATOM   16333 O  OG    . SER A 1 3707 ? 169.806 125.911 149.739 1.00 78.11  ? 3707 SER A OG    1 
ATOM   16334 N  N     . LEU A 1 3708 ? 172.301 124.621 150.436 1.00 71.91  ? 3708 LEU A N     1 
ATOM   16335 C  CA    . LEU A 1 3708 ? 173.704 124.989 150.579 1.00 73.28  ? 3708 LEU A CA    1 
ATOM   16336 C  C     . LEU A 1 3708 ? 174.594 123.757 150.662 1.00 75.60  ? 3708 LEU A C     1 
ATOM   16337 O  O     . LEU A 1 3708 ? 175.695 123.742 150.099 1.00 85.73  ? 3708 LEU A O     1 
ATOM   16338 C  CB    . LEU A 1 3708 ? 173.896 125.869 151.809 1.00 68.67  ? 3708 LEU A CB    1 
ATOM   16339 C  CG    . LEU A 1 3708 ? 175.298 126.459 151.928 1.00 69.17  ? 3708 LEU A CG    1 
ATOM   16340 C  CD1   . LEU A 1 3708 ? 175.596 127.385 150.762 1.00 67.08  ? 3708 LEU A CD1   1 
ATOM   16341 C  CD2   . LEU A 1 3708 ? 175.437 127.185 153.237 1.00 72.97  ? 3708 LEU A CD2   1 
ATOM   16342 N  N     . GLN A 1 3709 ? 174.140 122.715 151.363 1.00 70.76  ? 3709 GLN A N     1 
ATOM   16343 C  CA    . GLN A 1 3709 ? 174.904 121.474 151.412 1.00 69.34  ? 3709 GLN A CA    1 
ATOM   16344 C  C     . GLN A 1 3709 ? 175.074 120.886 150.019 1.00 75.53  ? 3709 GLN A C     1 
ATOM   16345 O  O     . GLN A 1 3709 ? 176.175 120.465 149.645 1.00 84.44  ? 3709 GLN A O     1 
ATOM   16346 C  CB    . GLN A 1 3709 ? 174.216 120.466 152.331 1.00 64.12  ? 3709 GLN A CB    1 
ATOM   16347 C  CG    . GLN A 1 3709 ? 174.471 120.685 153.808 1.00 73.26  ? 3709 GLN A CG    1 
ATOM   16348 C  CD    . GLN A 1 3709 ? 173.605 119.802 154.681 1.00 80.83  ? 3709 GLN A CD    1 
ATOM   16349 O  OE1   . GLN A 1 3709 ? 173.194 118.717 154.271 1.00 80.89  ? 3709 GLN A OE1   1 
ATOM   16350 N  NE2   . GLN A 1 3709 ? 173.321 120.263 155.894 1.00 82.18  ? 3709 GLN A NE2   1 
ATOM   16351 N  N     . SER A 1 3710 ? 173.995 120.859 149.234 1.00 72.39  ? 3710 SER A N     1 
ATOM   16352 C  CA    . SER A 1 3710 ? 174.082 120.328 147.878 1.00 71.13  ? 3710 SER A CA    1 
ATOM   16353 C  C     . SER A 1 3710 ? 175.009 121.171 147.012 1.00 77.51  ? 3710 SER A C     1 
ATOM   16354 O  O     . SER A 1 3710 ? 175.806 120.632 146.237 1.00 82.07  ? 3710 SER A O     1 
ATOM   16355 C  CB    . SER A 1 3710 ? 172.688 120.250 147.257 1.00 71.88  ? 3710 SER A CB    1 
ATOM   16356 O  OG    . SER A 1 3710 ? 172.742 119.692 145.957 1.00 78.12  ? 3710 SER A OG    1 
ATOM   16357 N  N     . GLN A 1 3711 ? 174.920 122.498 147.133 1.00 75.92  ? 3711 GLN A N     1 
ATOM   16358 C  CA    . GLN A 1 3711 ? 175.782 123.378 146.349 1.00 77.43  ? 3711 GLN A CA    1 
ATOM   16359 C  C     . GLN A 1 3711 ? 177.249 123.150 146.685 1.00 78.54  ? 3711 GLN A C     1 
ATOM   16360 O  O     . GLN A 1 3711 ? 178.094 123.035 145.789 1.00 82.21  ? 3711 GLN A O     1 
ATOM   16361 C  CB    . GLN A 1 3711 ? 175.399 124.838 146.592 1.00 74.78  ? 3711 GLN A CB    1 
ATOM   16362 C  CG    . GLN A 1 3711 ? 174.144 125.288 145.868 1.00 78.62  ? 3711 GLN A CG    1 
ATOM   16363 C  CD    . GLN A 1 3711 ? 173.781 126.726 146.179 1.00 82.43  ? 3711 GLN A CD    1 
ATOM   16364 O  OE1   . GLN A 1 3711 ? 172.629 127.036 146.480 1.00 83.37  ? 3711 GLN A OE1   1 
ATOM   16365 N  NE2   . GLN A 1 3711 ? 174.766 127.613 146.109 1.00 78.16  ? 3711 GLN A NE2   1 
ATOM   16366 N  N     . CYS A 1 3712 ? 177.570 123.078 147.979 1.00 70.51  ? 3712 CYS A N     1 
ATOM   16367 C  CA    . CYS A 1 3712 ? 178.956 122.875 148.386 1.00 67.92  ? 3712 CYS A CA    1 
ATOM   16368 C  C     . CYS A 1 3712 ? 179.464 121.503 147.964 1.00 73.69  ? 3712 CYS A C     1 
ATOM   16369 O  O     . CYS A 1 3712 ? 180.617 121.367 147.538 1.00 82.94  ? 3712 CYS A O     1 
ATOM   16370 C  CB    . CYS A 1 3712 ? 179.091 123.063 149.896 1.00 66.08  ? 3712 CYS A CB    1 
ATOM   16371 S  SG    . CYS A 1 3712 ? 178.695 124.730 150.467 1.00 87.19  ? 3712 CYS A SG    1 
ATOM   16372 N  N     . LEU A 1 3713 ? 178.621 120.472 148.073 1.00 65.08  ? 3713 LEU A N     1 
ATOM   16373 C  CA    . LEU A 1 3713 ? 179.034 119.140 147.646 1.00 64.14  ? 3713 LEU A CA    1 
ATOM   16374 C  C     . LEU A 1 3713 ? 179.296 119.099 146.146 1.00 73.09  ? 3713 LEU A C     1 
ATOM   16375 O  O     . LEU A 1 3713 ? 180.288 118.512 145.698 1.00 79.49  ? 3713 LEU A O     1 
ATOM   16376 C  CB    . LEU A 1 3713 ? 177.973 118.113 148.038 1.00 59.58  ? 3713 LEU A CB    1 
ATOM   16377 C  CG    . LEU A 1 3713 ? 178.184 116.690 147.526 1.00 62.28  ? 3713 LEU A CG    1 
ATOM   16378 C  CD1   . LEU A 1 3713 ? 179.429 116.087 148.146 1.00 70.84  ? 3713 LEU A CD1   1 
ATOM   16379 C  CD2   . LEU A 1 3713 ? 176.967 115.837 147.831 1.00 69.90  ? 3713 LEU A CD2   1 
ATOM   16380 N  N     . ASN A 1 3714 ? 178.425 119.726 145.352 1.00 82.72  ? 3714 ASN A N     1 
ATOM   16381 C  CA    . ASN A 1 3714 ? 178.646 119.772 143.911 1.00 82.23  ? 3714 ASN A CA    1 
ATOM   16382 C  C     . ASN A 1 3714 ? 179.916 120.543 143.573 1.00 80.71  ? 3714 ASN A C     1 
ATOM   16383 O  O     . ASN A 1 3714 ? 180.680 120.140 142.688 1.00 84.85  ? 3714 ASN A O     1 
ATOM   16384 C  CB    . ASN A 1 3714 ? 177.436 120.392 143.215 1.00 81.26  ? 3714 ASN A CB    1 
ATOM   16385 C  CG    . ASN A 1 3714 ? 176.189 119.544 143.356 1.00 82.97  ? 3714 ASN A CG    1 
ATOM   16386 O  OD1   . ASN A 1 3714 ? 176.268 118.334 143.561 1.00 81.11  ? 3714 ASN A OD1   1 
ATOM   16387 N  ND2   . ASN A 1 3714 ? 175.028 120.178 143.249 1.00 83.28  ? 3714 ASN A ND2   1 
ATOM   16388 N  N     . GLU A 1 3715 ? 180.160 121.655 144.271 1.00 81.56  ? 3715 GLU A N     1 
ATOM   16389 C  CA    . GLU A 1 3715 ? 181.361 122.442 144.008 1.00 81.61  ? 3715 GLU A CA    1 
ATOM   16390 C  C     . GLU A 1 3715 ? 182.624 121.657 144.343 1.00 84.20  ? 3715 GLU A C     1 
ATOM   16391 O  O     . GLU A 1 3715 ? 183.594 121.671 143.575 1.00 88.56  ? 3715 GLU A O     1 
ATOM   16392 C  CB    . GLU A 1 3715 ? 181.311 123.747 144.801 1.00 80.95  ? 3715 GLU A CB    1 
ATOM   16393 C  CG    . GLU A 1 3715 ? 182.489 124.669 144.554 1.00 87.10  ? 3715 GLU A CG    1 
ATOM   16394 C  CD    . GLU A 1 3715 ? 182.087 126.130 144.539 1.00 97.16  ? 3715 GLU A CD    1 
ATOM   16395 O  OE1   . GLU A 1 3715 ? 182.983 126.996 144.453 1.00 99.62  ? 3715 GLU A OE1   1 
ATOM   16396 O  OE2   . GLU A 1 3715 ? 180.873 126.413 144.616 1.00 95.15  ? 3715 GLU A OE2   1 
ATOM   16397 N  N     . VAL A 1 3716 ? 182.631 120.956 145.480 1.00 79.70  ? 3716 VAL A N     1 
ATOM   16398 C  CA    . VAL A 1 3716 ? 183.821 120.194 145.847 1.00 78.75  ? 3716 VAL A CA    1 
ATOM   16399 C  C     . VAL A 1 3716 ? 183.998 118.992 144.927 1.00 78.18  ? 3716 VAL A C     1 
ATOM   16400 O  O     . VAL A 1 3716 ? 185.131 118.577 144.655 1.00 80.41  ? 3716 VAL A O     1 
ATOM   16401 C  CB    . VAL A 1 3716 ? 183.779 119.784 147.332 1.00 75.63  ? 3716 VAL A CB    1 
ATOM   16402 C  CG1   . VAL A 1 3716 ? 182.818 118.633 147.565 1.00 78.20  ? 3716 VAL A CG1   1 
ATOM   16403 C  CG2   . VAL A 1 3716 ? 185.173 119.417 147.811 1.00 77.01  ? 3716 VAL A CG2   1 
ATOM   16404 N  N     . LEU A 1 3717 ? 182.902 118.416 144.427 1.00 78.17  ? 3717 LEU A N     1 
ATOM   16405 C  CA    . LEU A 1 3717 ? 183.025 117.347 143.445 1.00 75.93  ? 3717 LEU A CA    1 
ATOM   16406 C  C     . LEU A 1 3717 ? 183.623 117.864 142.144 1.00 81.29  ? 3717 LEU A C     1 
ATOM   16407 O  O     . LEU A 1 3717 ? 184.482 117.208 141.546 1.00 88.89  ? 3717 LEU A O     1 
ATOM   16408 C  CB    . LEU A 1 3717 ? 181.662 116.707 143.192 1.00 80.01  ? 3717 LEU A CB    1 
ATOM   16409 C  CG    . LEU A 1 3717 ? 181.230 115.652 144.207 1.00 81.23  ? 3717 LEU A CG    1 
ATOM   16410 C  CD1   . LEU A 1 3717 ? 179.872 115.085 143.835 1.00 81.52  ? 3717 LEU A CD1   1 
ATOM   16411 C  CD2   . LEU A 1 3717 ? 182.271 114.550 144.297 1.00 78.00  ? 3717 LEU A CD2   1 
ATOM   16412 N  N     . LYS A 1 3718 ? 183.185 119.042 141.695 1.00 89.04  ? 3718 LYS A N     1 
ATOM   16413 C  CA    . LYS A 1 3718 ? 183.747 119.623 140.480 1.00 88.16  ? 3718 LYS A CA    1 
ATOM   16414 C  C     . LYS A 1 3718 ? 185.220 119.962 140.668 1.00 88.98  ? 3718 LYS A C     1 
ATOM   16415 O  O     . LYS A 1 3718 ? 186.022 119.826 139.737 1.00 91.05  ? 3718 LYS A O     1 
ATOM   16416 C  CB    . LYS A 1 3718 ? 182.953 120.867 140.077 1.00 88.66  ? 3718 LYS A CB    1 
ATOM   16417 C  CG    . LYS A 1 3718 ? 183.760 121.939 139.368 1.00 89.27  ? 3718 LYS A CG    1 
ATOM   16418 C  CD    . LYS A 1 3718 ? 183.047 123.278 139.414 1.00 92.20  ? 3718 LYS A CD    1 
ATOM   16419 C  CE    . LYS A 1 3718 ? 182.235 123.517 138.152 1.00 93.08  ? 3718 LYS A CE    1 
ATOM   16420 N  NZ    . LYS A 1 3718 ? 181.206 124.571 138.352 1.00 91.41  ? 3718 LYS A NZ    1 
ATOM   16421 N  N     . ALA A 1 3719 ? 185.595 120.396 141.872 1.00 85.71  ? 3719 ALA A N     1 
ATOM   16422 C  CA    . ALA A 1 3719 ? 186.981 120.771 142.126 1.00 85.90  ? 3719 ALA A CA    1 
ATOM   16423 C  C     . ALA A 1 3719 ? 187.882 119.545 142.206 1.00 91.39  ? 3719 ALA A C     1 
ATOM   16424 O  O     . ALA A 1 3719 ? 188.824 119.397 141.418 1.00 98.63  ? 3719 ALA A O     1 
ATOM   16425 C  CB    . ALA A 1 3719 ? 187.069 121.587 143.416 1.00 86.98  ? 3719 ALA A CB    1 
ATOM   16426 N  N     . GLU A 1 3720 ? 187.611 118.653 143.161 1.00 89.58  ? 3720 GLU A N     1 
ATOM   16427 C  CA    . GLU A 1 3720 ? 188.532 117.553 143.429 1.00 91.03  ? 3720 GLU A CA    1 
ATOM   16428 C  C     . GLU A 1 3720 ? 188.460 116.470 142.357 1.00 95.69  ? 3720 GLU A C     1 
ATOM   16429 O  O     . GLU A 1 3720 ? 189.497 115.982 141.894 1.00 100.84 ? 3720 GLU A O     1 
ATOM   16430 C  CB    . GLU A 1 3720 ? 188.245 116.961 144.808 1.00 90.42  ? 3720 GLU A CB    1 
ATOM   16431 C  CG    . GLU A 1 3720 ? 188.764 117.810 145.953 1.00 95.48  ? 3720 GLU A CG    1 
ATOM   16432 C  CD    . GLU A 1 3720 ? 190.190 118.267 145.731 1.00 98.23  ? 3720 GLU A CD    1 
ATOM   16433 O  OE1   . GLU A 1 3720 ? 191.101 117.415 145.778 1.00 99.64  ? 3720 GLU A OE1   1 
ATOM   16434 O  OE2   . GLU A 1 3720 ? 190.399 119.477 145.506 1.00 95.10  ? 3720 GLU A OE2   1 
ATOM   16435 N  N     . ARG A 1 3721 ? 187.254 116.079 141.951 1.00 97.50  ? 3721 ARG A N     1 
ATOM   16436 C  CA    . ARG A 1 3721 ? 187.047 114.931 141.067 1.00 94.06  ? 3721 ARG A CA    1 
ATOM   16437 C  C     . ARG A 1 3721 ? 186.166 115.340 139.893 1.00 97.18  ? 3721 ARG A C     1 
ATOM   16438 O  O     . ARG A 1 3721 ? 184.969 115.028 139.857 1.00 104.33 ? 3721 ARG A O     1 
ATOM   16439 C  CB    . ARG A 1 3721 ? 186.429 113.764 141.838 1.00 91.03  ? 3721 ARG A CB    1 
ATOM   16440 C  CG    . ARG A 1 3721 ? 187.292 113.257 142.984 1.00 90.22  ? 3721 ARG A CG    1 
ATOM   16441 C  CD    . ARG A 1 3721 ? 186.593 112.157 143.767 1.00 92.96  ? 3721 ARG A CD    1 
ATOM   16442 N  NE    . ARG A 1 3721 ? 186.344 110.975 142.953 1.00 103.10 ? 3721 ARG A NE    1 
ATOM   16443 C  CZ    . ARG A 1 3721 ? 187.208 109.983 142.788 1.00 101.27 ? 3721 ARG A CZ    1 
ATOM   16444 N  NH1   . ARG A 1 3721 ? 188.393 109.994 143.377 1.00 100.92 ? 3721 ARG A NH1   1 
ATOM   16445 N  NH2   . ARG A 1 3721 ? 186.875 108.953 142.016 1.00 97.11  ? 3721 ARG A NH2   1 
ATOM   16446 N  N     . PRO A 1 3722 ? 186.733 116.039 138.906 1.00 98.91  ? 3722 PRO A N     1 
ATOM   16447 C  CA    . PRO A 1 3722 ? 185.906 116.542 137.794 1.00 103.21 ? 3722 PRO A CA    1 
ATOM   16448 C  C     . PRO A 1 3722 ? 185.208 115.450 137.000 1.00 107.07 ? 3722 PRO A C     1 
ATOM   16449 O  O     . PRO A 1 3722 ? 184.085 115.668 136.522 1.00 105.76 ? 3722 PRO A O     1 
ATOM   16450 C  CB    . PRO A 1 3722 ? 186.916 117.310 136.931 1.00 100.28 ? 3722 PRO A CB    1 
ATOM   16451 C  CG    . PRO A 1 3722 ? 188.237 116.699 137.258 1.00 101.53 ? 3722 PRO A CG    1 
ATOM   16452 C  CD    . PRO A 1 3722 ? 188.166 116.312 138.705 1.00 99.18  ? 3722 PRO A CD    1 
ATOM   16453 N  N     . ASP A 1 3723 ? 185.836 114.282 136.845 1.00 111.76 ? 3723 ASP A N     1 
ATOM   16454 C  CA    . ASP A 1 3723 ? 185.205 113.196 136.101 1.00 109.16 ? 3723 ASP A CA    1 
ATOM   16455 C  C     . ASP A 1 3723 ? 183.926 112.736 136.786 1.00 110.94 ? 3723 ASP A C     1 
ATOM   16456 O  O     . ASP A 1 3723 ? 182.918 112.464 136.122 1.00 113.88 ? 3723 ASP A O     1 
ATOM   16457 C  CB    . ASP A 1 3723 ? 186.180 112.030 135.945 1.00 109.07 ? 3723 ASP A CB    1 
ATOM   16458 C  CG    . ASP A 1 3723 ? 186.774 111.589 137.266 1.00 111.84 ? 3723 ASP A CG    1 
ATOM   16459 O  OD1   . ASP A 1 3723 ? 187.648 112.305 137.796 1.00 113.20 ? 3723 ASP A OD1   1 
ATOM   16460 O  OD2   . ASP A 1 3723 ? 186.363 110.527 137.777 1.00 113.06 ? 3723 ASP A OD2   1 
ATOM   16461 N  N     . VAL A 1 3724 ? 183.944 112.651 138.117 1.00 106.53 ? 3724 VAL A N     1 
ATOM   16462 C  CA    . VAL A 1 3724 ? 182.755 112.228 138.847 1.00 107.17 ? 3724 VAL A CA    1 
ATOM   16463 C  C     . VAL A 1 3724 ? 181.621 113.221 138.640 1.00 109.93 ? 3724 VAL A C     1 
ATOM   16464 O  O     . VAL A 1 3724 ? 180.468 112.829 138.429 1.00 110.12 ? 3724 VAL A O     1 
ATOM   16465 C  CB    . VAL A 1 3724 ? 183.084 112.045 140.339 1.00 102.56 ? 3724 VAL A CB    1 
ATOM   16466 C  CG1   . VAL A 1 3724 ? 181.819 111.752 141.130 1.00 103.13 ? 3724 VAL A CG1   1 
ATOM   16467 C  CG2   . VAL A 1 3724 ? 184.100 110.937 140.516 1.00 103.47 ? 3724 VAL A CG2   1 
ATOM   16468 N  N     . ASP A 1 3725 ? 181.925 114.520 138.691 1.00 111.85 ? 3725 ASP A N     1 
ATOM   16469 C  CA    . ASP A 1 3725 ? 180.874 115.520 138.534 1.00 109.84 ? 3725 ASP A CA    1 
ATOM   16470 C  C     . ASP A 1 3725 ? 180.330 115.517 137.109 1.00 117.17 ? 3725 ASP A C     1 
ATOM   16471 O  O     . ASP A 1 3725 ? 179.117 115.648 136.908 1.00 121.46 ? 3725 ASP A O     1 
ATOM   16472 C  CB    . ASP A 1 3725 ? 181.402 116.901 138.942 1.00 110.72 ? 3725 ASP A CB    1 
ATOM   16473 C  CG    . ASP A 1 3725 ? 180.334 118.005 138.888 1.00 118.72 ? 3725 ASP A CG    1 
ATOM   16474 O  OD1   . ASP A 1 3725 ? 179.317 117.884 138.179 1.00 119.60 ? 3725 ASP A OD1   1 
ATOM   16475 O  OD2   . ASP A 1 3725 ? 180.504 119.011 139.605 1.00 119.54 ? 3725 ASP A OD2   1 
ATOM   16476 N  N     . GLU A 1 3726 ? 181.197 115.369 136.102 1.00 116.03 ? 3726 GLU A N     1 
ATOM   16477 C  CA    . GLU A 1 3726 ? 180.687 115.326 134.734 1.00 114.54 ? 3726 GLU A CA    1 
ATOM   16478 C  C     . GLU A 1 3726 ? 179.819 114.090 134.517 1.00 114.20 ? 3726 GLU A C     1 
ATOM   16479 O  O     . GLU A 1 3726 ? 178.770 114.164 133.862 1.00 115.68 ? 3726 GLU A O     1 
ATOM   16480 C  CB    . GLU A 1 3726 ? 181.833 115.393 133.715 1.00 112.16 ? 3726 GLU A CB    1 
ATOM   16481 C  CG    . GLU A 1 3726 ? 182.676 114.136 133.555 1.00 115.61 ? 3726 GLU A CG    1 
ATOM   16482 C  CD    . GLU A 1 3726 ? 184.068 114.427 133.019 1.00 120.02 ? 3726 GLU A CD    1 
ATOM   16483 O  OE1   . GLU A 1 3726 ? 184.591 115.527 133.290 1.00 120.64 ? 3726 GLU A OE1   1 
ATOM   16484 O  OE2   . GLU A 1 3726 ? 184.637 113.558 132.324 1.00 119.85 ? 3726 GLU A OE2   1 
ATOM   16485 N  N     . LYS A 1 3727 ? 180.218 112.951 135.095 1.00 110.86 ? 3727 LYS A N     1 
ATOM   16486 C  CA    . LYS A 1 3727 ? 179.388 111.755 135.015 1.00 113.43 ? 3727 LYS A CA    1 
ATOM   16487 C  C     . LYS A 1 3727 ? 178.051 111.967 135.713 1.00 115.57 ? 3727 LYS A C     1 
ATOM   16488 O  O     . LYS A 1 3727 ? 177.006 111.544 135.209 1.00 120.88 ? 3727 LYS A O     1 
ATOM   16489 C  CB    . LYS A 1 3727 ? 180.129 110.562 135.618 1.00 112.66 ? 3727 LYS A CB    1 
ATOM   16490 C  CG    . LYS A 1 3727 ? 179.343 109.262 135.594 1.00 114.03 ? 3727 LYS A CG    1 
ATOM   16491 C  CD    . LYS A 1 3727 ? 179.979 108.217 136.496 1.00 113.51 ? 3727 LYS A CD    1 
ATOM   16492 C  CE    . LYS A 1 3727 ? 181.466 108.081 136.218 1.00 113.85 ? 3727 LYS A CE    1 
ATOM   16493 N  NZ    . LYS A 1 3727 ? 181.729 107.712 134.800 1.00 113.64 ? 3727 LYS A NZ    1 
ATOM   16494 N  N     . ARG A 1 3728 ? 178.065 112.626 136.874 1.00 107.44 ? 3728 ARG A N     1 
ATOM   16495 C  CA    . ARG A 1 3728 ? 176.829 112.882 137.607 1.00 108.60 ? 3728 ARG A CA    1 
ATOM   16496 C  C     . ARG A 1 3728 ? 175.898 113.803 136.828 1.00 109.44 ? 3728 ARG A C     1 
ATOM   16497 O  O     . ARG A 1 3728 ? 174.682 113.587 136.796 1.00 112.02 ? 3728 ARG A O     1 
ATOM   16498 C  CB    . ARG A 1 3728 ? 177.156 113.478 138.976 1.00 107.34 ? 3728 ARG A CB    1 
ATOM   16499 C  CG    . ARG A 1 3728 ? 175.955 113.659 139.886 1.00 109.36 ? 3728 ARG A CG    1 
ATOM   16500 C  CD    . ARG A 1 3728 ? 176.311 114.484 141.114 1.00 110.38 ? 3728 ARG A CD    1 
ATOM   16501 N  NE    . ARG A 1 3728 ? 176.714 115.843 140.772 1.00 111.44 ? 3728 ARG A NE    1 
ATOM   16502 C  CZ    . ARG A 1 3728 ? 175.871 116.827 140.488 1.00 111.61 ? 3728 ARG A CZ    1 
ATOM   16503 N  NH1   . ARG A 1 3728 ? 174.561 116.640 140.500 1.00 110.46 ? 3728 ARG A NH1   1 
ATOM   16504 N  NH2   . ARG A 1 3728 ? 176.353 118.029 140.187 1.00 111.15 ? 3728 ARG A NH2   1 
ATOM   16505 N  N     . SER A 1 3729 ? 176.450 114.845 136.203 1.00 109.81 ? 3729 SER A N     1 
ATOM   16506 C  CA    . SER A 1 3729 ? 175.630 115.754 135.408 1.00 113.96 ? 3729 SER A CA    1 
ATOM   16507 C  C     . SER A 1 3729 ? 175.029 115.042 134.202 1.00 116.39 ? 3729 SER A C     1 
ATOM   16508 O  O     . SER A 1 3729 ? 173.841 115.216 133.891 1.00 116.28 ? 3729 SER A O     1 
ATOM   16509 C  CB    . SER A 1 3729 ? 176.462 116.956 134.962 1.00 113.20 ? 3729 SER A CB    1 
ATOM   16510 O  OG    . SER A 1 3729 ? 176.912 117.705 136.077 1.00 112.22 ? 3729 SER A OG    1 
ATOM   16511 N  N     . ASP A 1 3730 ? 175.836 114.230 133.512 1.00 119.48 ? 3730 ASP A N     1 
ATOM   16512 C  CA    . ASP A 1 3730 ? 175.313 113.463 132.388 1.00 117.63 ? 3730 ASP A CA    1 
ATOM   16513 C  C     . ASP A 1 3730 ? 174.222 112.505 132.846 1.00 116.46 ? 3730 ASP A C     1 
ATOM   16514 O  O     . ASP A 1 3730 ? 173.201 112.344 132.168 1.00 120.90 ? 3730 ASP A O     1 
ATOM   16515 C  CB    . ASP A 1 3730 ? 176.445 112.705 131.697 1.00 115.48 ? 3730 ASP A CB    1 
ATOM   16516 C  CG    . ASP A 1 3730 ? 177.473 113.632 131.077 1.00 119.06 ? 3730 ASP A CG    1 
ATOM   16517 O  OD1   . ASP A 1 3730 ? 177.272 114.863 131.127 1.00 119.77 ? 3730 ASP A OD1   1 
ATOM   16518 O  OD2   . ASP A 1 3730 ? 178.482 113.129 130.538 1.00 120.66 ? 3730 ASP A OD2   1 
ATOM   16519 N  N     . LEU A 1 3731 ? 174.417 111.870 134.003 1.00 110.49 ? 3731 LEU A N     1 
ATOM   16520 C  CA    . LEU A 1 3731 ? 173.412 110.958 134.536 1.00 110.61 ? 3731 LEU A CA    1 
ATOM   16521 C  C     . LEU A 1 3731 ? 172.124 111.691 134.885 1.00 112.48 ? 3731 LEU A C     1 
ATOM   16522 O  O     . LEU A 1 3731 ? 171.031 111.172 134.647 1.00 113.22 ? 3731 LEU A O     1 
ATOM   16523 C  CB    . LEU A 1 3731 ? 173.965 110.235 135.761 1.00 109.57 ? 3731 LEU A CB    1 
ATOM   16524 C  CG    . LEU A 1 3731 ? 174.576 108.851 135.545 1.00 110.29 ? 3731 LEU A CG    1 
ATOM   16525 C  CD1   . LEU A 1 3731 ? 175.436 108.807 134.293 1.00 112.60 ? 3731 LEU A CD1   1 
ATOM   16526 C  CD2   . LEU A 1 3731 ? 175.397 108.479 136.761 1.00 109.04 ? 3731 LEU A CD2   1 
ATOM   16527 N  N     . LEU A 1 3732 ? 172.231 112.888 135.464 1.00 114.43 ? 3732 LEU A N     1 
ATOM   16528 C  CA    . LEU A 1 3732 ? 171.038 113.674 135.769 1.00 115.46 ? 3732 LEU A CA    1 
ATOM   16529 C  C     . LEU A 1 3732 ? 170.278 114.026 134.498 1.00 116.21 ? 3732 LEU A C     1 
ATOM   16530 O  O     . LEU A 1 3732 ? 169.045 113.918 134.444 1.00 118.45 ? 3732 LEU A O     1 
ATOM   16531 C  CB    . LEU A 1 3732 ? 171.423 114.941 136.534 1.00 114.67 ? 3732 LEU A CB    1 
ATOM   16532 C  CG    . LEU A 1 3732 ? 171.833 114.790 138.000 1.00 112.79 ? 3732 LEU A CG    1 
ATOM   16533 C  CD1   . LEU A 1 3732 ? 171.451 116.034 138.784 1.00 114.00 ? 3732 LEU A CD1   1 
ATOM   16534 C  CD2   . LEU A 1 3732 ? 171.180 113.563 138.608 1.00 111.35 ? 3732 LEU A CD2   1 
ATOM   16535 N  N     . LYS A 1 3733 ? 171.003 114.448 133.459 1.00 113.61 ? 3733 LYS A N     1 
ATOM   16536 C  CA    . LYS A 1 3733 ? 170.349 114.769 132.194 1.00 112.71 ? 3733 LYS A CA    1 
ATOM   16537 C  C     . LYS A 1 3733 ? 169.669 113.540 131.600 1.00 114.37 ? 3733 LYS A C     1 
ATOM   16538 O  O     . LYS A 1 3733 ? 168.534 113.621 131.109 1.00 117.23 ? 3733 LYS A O     1 
ATOM   16539 C  CB    . LYS A 1 3733 ? 171.365 115.356 131.215 1.00 113.38 ? 3733 LYS A CB    1 
ATOM   16540 C  CG    . LYS A 1 3733 ? 170.824 115.582 129.814 1.00 115.19 ? 3733 LYS A CG    1 
ATOM   16541 C  CD    . LYS A 1 3733 ? 171.791 116.404 128.975 1.00 116.09 ? 3733 LYS A CD    1 
ATOM   16542 C  CE    . LYS A 1 3733 ? 171.953 117.810 129.531 1.00 116.70 ? 3733 LYS A CE    1 
ATOM   16543 N  NZ    . LYS A 1 3733 ? 170.652 118.401 129.949 1.00 115.94 ? 3733 LYS A NZ    1 
ATOM   16544 N  N     . LEU A 1 3734 ? 170.344 112.388 131.646 1.00 116.63 ? 3734 LEU A N     1 
ATOM   16545 C  CA    . LEU A 1 3734 ? 169.756 111.162 131.116 1.00 116.32 ? 3734 LEU A CA    1 
ATOM   16546 C  C     . LEU A 1 3734 ? 168.521 110.746 131.906 1.00 117.29 ? 3734 LEU A C     1 
ATOM   16547 O  O     . LEU A 1 3734 ? 167.527 110.308 131.321 1.00 121.91 ? 3734 LEU A O     1 
ATOM   16548 C  CB    . LEU A 1 3734 ? 170.790 110.036 131.108 1.00 116.80 ? 3734 LEU A CB    1 
ATOM   16549 C  CG    . LEU A 1 3734 ? 172.008 110.228 130.202 1.00 118.53 ? 3734 LEU A CG    1 
ATOM   16550 C  CD1   . LEU A 1 3734 ? 172.871 108.975 130.188 1.00 117.71 ? 3734 LEU A CD1   1 
ATOM   16551 C  CD2   . LEU A 1 3734 ? 171.578 110.607 128.793 1.00 117.07 ? 3734 LEU A CD2   1 
ATOM   16552 N  N     . GLN A 1 3735 ? 168.567 110.864 133.236 1.00 114.55 ? 3735 GLN A N     1 
ATOM   16553 C  CA    . GLN A 1 3735 ? 167.398 110.532 134.045 1.00 114.97 ? 3735 GLN A CA    1 
ATOM   16554 C  C     . GLN A 1 3735 ? 166.227 111.445 133.720 1.00 115.69 ? 3735 GLN A C     1 
ATOM   16555 O  O     . GLN A 1 3735 ? 165.087 110.982 133.606 1.00 118.06 ? 3735 GLN A O     1 
ATOM   16556 C  CB    . GLN A 1 3735 ? 167.731 110.615 135.535 1.00 115.99 ? 3735 GLN A CB    1 
ATOM   16557 C  CG    . GLN A 1 3735 ? 168.751 109.605 136.013 1.00 116.61 ? 3735 GLN A CG    1 
ATOM   16558 C  CD    . GLN A 1 3735 ? 168.112 108.365 136.602 1.00 118.92 ? 3735 GLN A CD    1 
ATOM   16559 O  OE1   . GLN A 1 3735 ? 168.002 108.228 137.820 1.00 117.95 ? 3735 GLN A OE1   1 
ATOM   16560 N  NE2   . GLN A 1 3735 ? 167.687 107.452 135.738 1.00 119.95 ? 3735 GLN A NE2   1 
ATOM   16561 N  N     . GLY A 1 3736 ? 166.487 112.746 133.571 1.00 116.26 ? 3736 GLY A N     1 
ATOM   16562 C  CA    . GLY A 1 3736 ? 165.415 113.656 133.202 1.00 117.08 ? 3736 GLY A CA    1 
ATOM   16563 C  C     . GLY A 1 3736 ? 164.801 113.302 131.862 1.00 117.83 ? 3736 GLY A C     1 
ATOM   16564 O  O     . GLY A 1 3736 ? 163.574 113.234 131.721 1.00 122.80 ? 3736 GLY A O     1 
ATOM   16565 N  N     . GLU A 1 3737 ? 165.650 113.045 130.863 1.00 116.32 ? 3737 GLU A N     1 
ATOM   16566 C  CA    . GLU A 1 3737 ? 165.148 112.694 129.538 1.00 117.05 ? 3737 GLU A CA    1 
ATOM   16567 C  C     . GLU A 1 3737 ? 164.357 111.391 129.570 1.00 119.71 ? 3737 GLU A C     1 
ATOM   16568 O  O     . GLU A 1 3737 ? 163.302 111.281 128.935 1.00 121.83 ? 3737 GLU A O     1 
ATOM   16569 C  CB    . GLU A 1 3737 ? 166.308 112.594 128.548 1.00 119.05 ? 3737 GLU A CB    1 
ATOM   16570 C  CG    . GLU A 1 3737 ? 166.951 113.929 128.212 1.00 120.66 ? 3737 GLU A CG    1 
ATOM   16571 C  CD    . GLU A 1 3737 ? 168.314 113.773 127.568 1.00 123.80 ? 3737 GLU A CD    1 
ATOM   16572 O  OE1   . GLU A 1 3737 ? 168.775 112.621 127.423 1.00 125.52 ? 3737 GLU A OE1   1 
ATOM   16573 O  OE2   . GLU A 1 3737 ? 168.924 114.801 127.208 1.00 120.74 ? 3737 GLU A OE2   1 
ATOM   16574 N  N     . PHE A 1 3738 ? 164.845 110.395 130.313 1.00 119.78 ? 3738 PHE A N     1 
ATOM   16575 C  CA    . PHE A 1 3738 ? 164.171 109.103 130.357 1.00 117.80 ? 3738 PHE A CA    1 
ATOM   16576 C  C     . PHE A 1 3738 ? 162.836 109.193 131.085 1.00 122.52 ? 3738 PHE A C     1 
ATOM   16577 O  O     . PHE A 1 3738 ? 161.856 108.568 130.668 1.00 127.29 ? 3738 PHE A O     1 
ATOM   16578 C  CB    . PHE A 1 3738 ? 165.075 108.063 131.015 1.00 118.50 ? 3738 PHE A CB    1 
ATOM   16579 C  CG    . PHE A 1 3738 ? 166.300 107.732 130.212 1.00 122.03 ? 3738 PHE A CG    1 
ATOM   16580 C  CD1   . PHE A 1 3738 ? 166.360 108.032 128.861 1.00 122.25 ? 3738 PHE A CD1   1 
ATOM   16581 C  CD2   . PHE A 1 3738 ? 167.392 107.127 130.808 1.00 122.07 ? 3738 PHE A CD2   1 
ATOM   16582 C  CE1   . PHE A 1 3738 ? 167.485 107.733 128.120 1.00 121.87 ? 3738 PHE A CE1   1 
ATOM   16583 C  CE2   . PHE A 1 3738 ? 168.521 106.827 130.072 1.00 120.67 ? 3738 PHE A CE2   1 
ATOM   16584 C  CZ    . PHE A 1 3738 ? 168.567 107.129 128.726 1.00 121.12 ? 3738 PHE A CZ    1 
ATOM   16585 N  N     . GLN A 1 3739 ? 162.775 109.959 132.177 1.00 120.47 ? 3739 GLN A N     1 
ATOM   16586 C  CA    . GLN A 1 3739 ? 161.501 110.141 132.864 1.00 117.56 ? 3739 GLN A CA    1 
ATOM   16587 C  C     . GLN A 1 3739 ? 160.507 110.884 131.982 1.00 119.36 ? 3739 GLN A C     1 
ATOM   16588 O  O     . GLN A 1 3739 ? 159.318 110.538 131.940 1.00 120.54 ? 3739 GLN A O     1 
ATOM   16589 C  CB    . GLN A 1 3739 ? 161.713 110.882 134.182 1.00 118.06 ? 3739 GLN A CB    1 
ATOM   16590 C  CG    . GLN A 1 3739 ? 162.442 110.065 135.232 1.00 121.25 ? 3739 GLN A CG    1 
ATOM   16591 C  CD    . GLN A 1 3739 ? 161.879 108.665 135.373 1.00 124.06 ? 3739 GLN A CD    1 
ATOM   16592 O  OE1   . GLN A 1 3739 ? 160.715 108.484 135.729 1.00 124.59 ? 3739 GLN A OE1   1 
ATOM   16593 N  NE2   . GLN A 1 3739 ? 162.705 107.664 135.091 1.00 122.28 ? 3739 GLN A NE2   1 
ATOM   16594 N  N     . LEU A 1 3740 ? 160.978 111.909 131.264 1.00 117.45 ? 3740 LEU A N     1 
ATOM   16595 C  CA    . LEU A 1 3740 ? 160.101 112.628 130.348 1.00 116.62 ? 3740 LEU A CA    1 
ATOM   16596 C  C     . LEU A 1 3740 ? 159.580 111.698 129.259 1.00 118.68 ? 3740 LEU A C     1 
ATOM   16597 O  O     . LEU A 1 3740 ? 158.396 111.744 128.905 1.00 119.84 ? 3740 LEU A O     1 
ATOM   16598 C  CB    . LEU A 1 3740 ? 160.849 113.831 129.762 1.00 116.89 ? 3740 LEU A CB    1 
ATOM   16599 C  CG    . LEU A 1 3740 ? 160.347 114.693 128.595 1.00 118.48 ? 3740 LEU A CG    1 
ATOM   16600 C  CD1   . LEU A 1 3740 ? 161.116 116.002 128.583 1.00 118.58 ? 3740 LEU A CD1   1 
ATOM   16601 C  CD2   . LEU A 1 3740 ? 160.512 114.020 127.244 1.00 116.44 ? 3740 LEU A CD2   1 
ATOM   16602 N  N     . ARG A 1 3741 ? 160.450 110.838 128.725 1.00 123.14 ? 3741 ARG A N     1 
ATOM   16603 C  CA    . ARG A 1 3741 ? 160.027 109.889 127.701 1.00 123.32 ? 3741 ARG A CA    1 
ATOM   16604 C  C     . ARG A 1 3741 ? 159.020 108.885 128.255 1.00 123.24 ? 3741 ARG A C     1 
ATOM   16605 O  O     . ARG A 1 3741 ? 158.053 108.533 127.573 1.00 124.67 ? 3741 ARG A O     1 
ATOM   16606 C  CB    . ARG A 1 3741 ? 161.247 109.176 127.117 1.00 119.82 ? 3741 ARG A CB    1 
ATOM   16607 C  CG    . ARG A 1 3741 ? 160.926 108.062 126.130 1.00 121.97 ? 3741 ARG A CG    1 
ATOM   16608 C  CD    . ARG A 1 3741 ? 159.925 108.510 125.074 1.00 125.74 ? 3741 ARG A CD    1 
ATOM   16609 N  NE    . ARG A 1 3741 ? 160.356 109.711 124.369 1.00 124.76 ? 3741 ARG A NE    1 
ATOM   16610 C  CZ    . ARG A 1 3741 ? 159.927 110.061 123.164 1.00 123.22 ? 3741 ARG A CZ    1 
ATOM   16611 N  NH1   . ARG A 1 3741 ? 159.054 109.322 122.500 1.00 121.44 ? 3741 ARG A NH1   1 
ATOM   16612 N  NH2   . ARG A 1 3741 ? 160.386 111.181 122.613 1.00 122.74 ? 3741 ARG A NH2   1 
ATOM   16613 N  N     . LEU A 1 3742 ? 159.230 108.406 129.483 1.00 115.62 ? 3742 LEU A N     1 
ATOM   16614 C  CA    . LEU A 1 3742 ? 158.278 107.474 130.081 1.00 113.87 ? 3742 LEU A CA    1 
ATOM   16615 C  C     . LEU A 1 3742 ? 156.911 108.123 130.261 1.00 119.02 ? 3742 LEU A C     1 
ATOM   16616 O  O     . LEU A 1 3742 ? 155.875 107.508 129.970 1.00 122.03 ? 3742 LEU A O     1 
ATOM   16617 C  CB    . LEU A 1 3742 ? 158.811 106.967 131.421 1.00 115.62 ? 3742 LEU A CB    1 
ATOM   16618 C  CG    . LEU A 1 3742 ? 159.520 105.611 131.421 1.00 117.96 ? 3742 LEU A CG    1 
ATOM   16619 C  CD1   . LEU A 1 3742 ? 159.687 105.095 132.842 1.00 118.26 ? 3742 LEU A CD1   1 
ATOM   16620 C  CD2   . LEU A 1 3742 ? 158.761 104.608 130.570 1.00 118.01 ? 3742 LEU A CD2   1 
ATOM   16621 N  N     . ARG A 1 3743 ? 156.888 109.371 130.738 1.00 119.54 ? 3743 ARG A N     1 
ATOM   16622 C  CA    . ARG A 1 3743 ? 155.619 110.074 130.893 1.00 119.08 ? 3743 ARG A CA    1 
ATOM   16623 C  C     . ARG A 1 3743 ? 154.940 110.290 129.545 1.00 119.28 ? 3743 ARG A C     1 
ATOM   16624 O  O     . ARG A 1 3743 ? 153.719 110.117 129.419 1.00 119.99 ? 3743 ARG A O     1 
ATOM   16625 C  CB    . ARG A 1 3743 ? 155.842 111.406 131.606 1.00 118.66 ? 3743 ARG A CB    1 
ATOM   16626 C  CG    . ARG A 1 3743 ? 156.093 111.268 133.098 1.00 117.78 ? 3743 ARG A CG    1 
ATOM   16627 C  CD    . ARG A 1 3743 ? 156.193 112.626 133.764 1.00 115.95 ? 3743 ARG A CD    1 
ATOM   16628 N  NE    . ARG A 1 3743 ? 157.549 113.159 133.723 1.00 118.94 ? 3743 ARG A NE    1 
ATOM   16629 C  CZ    . ARG A 1 3743 ? 157.977 114.045 132.834 1.00 119.45 ? 3743 ARG A CZ    1 
ATOM   16630 N  NH1   . ARG A 1 3743 ? 157.190 114.495 131.872 1.00 117.88 ? 3743 ARG A NH1   1 
ATOM   16631 N  NH2   . ARG A 1 3743 ? 159.228 114.492 132.915 1.00 118.41 ? 3743 ARG A NH2   1 
ATOM   16632 N  N     . GLN A 1 3744 ? 155.717 110.663 128.524 1.00 118.69 ? 3744 GLN A N     1 
ATOM   16633 C  CA    . GLN A 1 3744 ? 155.151 110.831 127.190 1.00 117.88 ? 3744 GLN A CA    1 
ATOM   16634 C  C     . GLN A 1 3744 ? 154.573 109.524 126.667 1.00 120.85 ? 3744 GLN A C     1 
ATOM   16635 O  O     . GLN A 1 3744 ? 153.502 109.515 126.052 1.00 124.09 ? 3744 GLN A O     1 
ATOM   16636 C  CB    . GLN A 1 3744 ? 156.209 111.363 126.224 1.00 115.96 ? 3744 GLN A CB    1 
ATOM   16637 C  CG    . GLN A 1 3744 ? 156.568 112.821 126.420 1.00 120.63 ? 3744 GLN A CG    1 
ATOM   16638 C  CD    . GLN A 1 3744 ? 157.484 113.337 125.329 1.00 121.01 ? 3744 GLN A CD    1 
ATOM   16639 O  OE1   . GLN A 1 3744 ? 158.528 112.748 125.051 1.00 119.85 ? 3744 GLN A OE1   1 
ATOM   16640 N  NE2   . GLN A 1 3744 ? 157.094 114.439 124.699 1.00 120.97 ? 3744 GLN A NE2   1 
ATOM   16641 N  N     . LEU A 1 3745 ? 155.273 108.410 126.889 1.00 122.25 ? 3745 LEU A N     1 
ATOM   16642 C  CA    . LEU A 1 3745 ? 154.779 107.123 126.413 1.00 121.95 ? 3745 LEU A CA    1 
ATOM   16643 C  C     . LEU A 1 3745 ? 153.491 106.729 127.123 1.00 123.29 ? 3745 LEU A C     1 
ATOM   16644 O  O     . LEU A 1 3745 ? 152.573 106.188 126.497 1.00 125.62 ? 3745 LEU A O     1 
ATOM   16645 C  CB    . LEU A 1 3745 ? 155.846 106.043 126.589 1.00 119.76 ? 3745 LEU A CB    1 
ATOM   16646 C  CG    . LEU A 1 3745 ? 157.033 106.129 125.627 1.00 123.50 ? 3745 LEU A CG    1 
ATOM   16647 C  CD1   . LEU A 1 3745 ? 157.873 104.861 125.678 1.00 125.17 ? 3745 LEU A CD1   1 
ATOM   16648 C  CD2   . LEU A 1 3745 ? 156.555 106.405 124.211 1.00 122.20 ? 3745 LEU A CD2   1 
ATOM   16649 N  N     . GLU A 1 3746 ? 153.403 106.986 128.430 1.00 125.13 ? 3746 GLU A N     1 
ATOM   16650 C  CA    . GLU A 1 3746 ? 152.162 106.696 129.146 1.00 125.61 ? 3746 GLU A CA    1 
ATOM   16651 C  C     . GLU A 1 3746 ? 151.008 107.546 128.625 1.00 126.95 ? 3746 GLU A C     1 
ATOM   16652 O  O     . GLU A 1 3746 ? 149.895 107.044 128.418 1.00 126.75 ? 3746 GLU A O     1 
ATOM   16653 C  CB    . GLU A 1 3746 ? 152.351 106.910 130.646 1.00 125.64 ? 3746 GLU A CB    1 
ATOM   16654 C  CG    . GLU A 1 3746 ? 151.099 106.625 131.461 1.00 126.48 ? 3746 GLU A CG    1 
ATOM   16655 C  CD    . GLU A 1 3746 ? 150.704 105.159 131.447 1.00 127.14 ? 3746 GLU A CD    1 
ATOM   16656 O  OE1   . GLU A 1 3746 ? 151.603 104.300 131.338 1.00 126.73 ? 3746 GLU A OE1   1 
ATOM   16657 O  OE2   . GLU A 1 3746 ? 149.495 104.867 131.556 1.00 129.54 ? 3746 GLU A OE2   1 
ATOM   16658 N  N     . LYS A 1 3747 ? 151.251 108.843 128.413 1.00 124.22 ? 3747 LYS A N     1 
ATOM   16659 C  CA    . LYS A 1 3747 ? 150.191 109.707 127.902 1.00 122.07 ? 3747 LYS A CA    1 
ATOM   16660 C  C     . LYS A 1 3747 ? 149.764 109.279 126.501 1.00 123.92 ? 3747 LYS A C     1 
ATOM   16661 O  O     . LYS A 1 3747 ? 148.569 109.281 126.178 1.00 128.95 ? 3747 LYS A O     1 
ATOM   16662 C  CB    . LYS A 1 3747 ? 150.646 111.168 127.924 1.00 121.54 ? 3747 LYS A CB    1 
ATOM   16663 C  CG    . LYS A 1 3747 ? 149.717 112.136 127.209 1.00 121.43 ? 3747 LYS A CG    1 
ATOM   16664 C  CD    . LYS A 1 3747 ? 150.196 113.570 127.363 1.00 121.58 ? 3747 LYS A CD    1 
ATOM   16665 C  CE    . LYS A 1 3747 ? 150.269 113.964 128.830 1.00 121.43 ? 3747 LYS A CE    1 
ATOM   16666 N  NZ    . LYS A 1 3747 ? 150.716 115.373 129.004 1.00 123.68 ? 3747 LYS A NZ    1 
ATOM   16667 N  N     . SER A 1 3748 ? 150.727 108.889 125.663 1.00 126.60 ? 3748 SER A N     1 
ATOM   16668 C  CA    . SER A 1 3748 ? 150.407 108.407 124.323 1.00 127.72 ? 3748 SER A CA    1 
ATOM   16669 C  C     . SER A 1 3748 ? 149.610 107.109 124.371 1.00 128.69 ? 3748 SER A C     1 
ATOM   16670 O  O     . SER A 1 3748 ? 148.693 106.914 123.568 1.00 130.85 ? 3748 SER A O     1 
ATOM   16671 C  CB    . SER A 1 3748 ? 151.689 108.217 123.515 1.00 127.47 ? 3748 SER A CB    1 
ATOM   16672 O  OG    . SER A 1 3748 ? 152.361 107.033 123.903 1.00 132.10 ? 3748 SER A OG    1 
ATOM   16673 N  N     . LEU A 1 3749 ? 149.955 106.200 125.286 1.00 126.26 ? 3749 LEU A N     1 
ATOM   16674 C  CA    . LEU A 1 3749 ? 149.188 104.965 125.419 1.00 127.40 ? 3749 LEU A CA    1 
ATOM   16675 C  C     . LEU A 1 3749 ? 147.758 105.262 125.853 1.00 130.16 ? 3749 LEU A C     1 
ATOM   16676 O  O     . LEU A 1 3749 ? 146.803 104.675 125.325 1.00 130.84 ? 3749 LEU A O     1 
ATOM   16677 C  CB    . LEU A 1 3749 ? 149.881 104.026 126.411 1.00 128.77 ? 3749 LEU A CB    1 
ATOM   16678 C  CG    . LEU A 1 3749 ? 149.714 102.504 126.292 1.00 129.45 ? 3749 LEU A CG    1 
ATOM   16679 C  CD1   . LEU A 1 3749 ? 150.597 101.796 127.311 1.00 130.59 ? 3749 LEU A CD1   1 
ATOM   16680 C  CD2   . LEU A 1 3749 ? 148.271 102.054 126.453 1.00 130.02 ? 3749 LEU A CD2   1 
ATOM   16681 N  N     . LEU A 1 3750 ? 147.593 106.179 126.811 1.00 132.13 ? 3750 LEU A N     1 
ATOM   16682 C  CA    . LEU A 1 3750 ? 146.253 106.584 127.227 1.00 130.63 ? 3750 LEU A CA    1 
ATOM   16683 C  C     . LEU A 1 3750 ? 145.465 107.154 126.055 1.00 130.97 ? 3750 LEU A C     1 
ATOM   16684 O  O     . LEU A 1 3750 ? 144.302 106.790 125.841 1.00 133.03 ? 3750 LEU A O     1 
ATOM   16685 C  CB    . LEU A 1 3750 ? 146.339 107.611 128.359 1.00 132.78 ? 3750 LEU A CB    1 
ATOM   16686 C  CG    . LEU A 1 3750 ? 145.486 107.367 129.608 1.00 133.32 ? 3750 LEU A CG    1 
ATOM   16687 C  CD1   . LEU A 1 3750 ? 145.562 105.915 130.050 1.00 131.16 ? 3750 LEU A CD1   1 
ATOM   16688 C  CD2   . LEU A 1 3750 ? 145.871 108.304 130.747 1.00 133.33 ? 3750 LEU A CD2   1 
ATOM   16689 N  N     . GLN A 1 3751 ? 146.093 108.036 125.272 1.00 136.23 ? 3751 GLN A N     1 
ATOM   16690 C  CA    . GLN A 1 3751 ? 145.410 108.648 124.137 1.00 135.47 ? 3751 GLN A CA    1 
ATOM   16691 C  C     . GLN A 1 3751 ? 145.045 107.610 123.082 1.00 137.78 ? 3751 GLN A C     1 
ATOM   16692 O  O     . GLN A 1 3751 ? 143.953 107.659 122.504 1.00 140.08 ? 3751 GLN A O     1 
ATOM   16693 C  CB    . GLN A 1 3751 ? 146.287 109.746 123.535 1.00 134.24 ? 3751 GLN A CB    1 
ATOM   16694 C  CG    . GLN A 1 3751 ? 145.844 110.234 122.166 1.00 137.60 ? 3751 GLN A CG    1 
ATOM   16695 C  CD    . GLN A 1 3751 ? 146.966 110.910 121.401 1.00 138.97 ? 3751 GLN A CD    1 
ATOM   16696 O  OE1   . GLN A 1 3751 ? 147.555 111.883 121.872 1.00 138.71 ? 3751 GLN A OE1   1 
ATOM   16697 N  NE2   . GLN A 1 3751 ? 147.262 110.402 120.211 1.00 139.07 ? 3751 GLN A NE2   1 
ATOM   16698 N  N     . ALA A 1 3752 ? 145.949 106.666 122.815 1.00 137.29 ? 3752 ALA A N     1 
ATOM   16699 C  CA    . ALA A 1 3752 ? 145.683 105.637 121.816 1.00 137.22 ? 3752 ALA A CA    1 
ATOM   16700 C  C     . ALA A 1 3752 ? 144.536 104.733 122.244 1.00 136.70 ? 3752 ALA A C     1 
ATOM   16701 O  O     . ALA A 1 3752 ? 143.681 104.375 121.425 1.00 137.71 ? 3752 ALA A O     1 
ATOM   16702 C  CB    . ALA A 1 3752 ? 146.946 104.815 121.560 1.00 138.06 ? 3752 ALA A CB    1 
ATOM   16703 N  N     . LEU A 1 3753 ? 144.497 104.349 123.522 1.00 139.32 ? 3753 LEU A N     1 
ATOM   16704 C  CA    . LEU A 1 3753 ? 143.402 103.506 123.986 1.00 140.14 ? 3753 LEU A CA    1 
ATOM   16705 C  C     . LEU A 1 3753 ? 142.090 104.270 124.103 1.00 141.39 ? 3753 LEU A C     1 
ATOM   16706 O  O     . LEU A 1 3753 ? 141.023 103.653 124.027 1.00 140.30 ? 3753 LEU A O     1 
ATOM   16707 C  CB    . LEU A 1 3753 ? 143.756 102.857 125.324 1.00 140.71 ? 3753 LEU A CB    1 
ATOM   16708 C  CG    . LEU A 1 3753 ? 144.588 101.580 125.194 1.00 141.25 ? 3753 LEU A CG    1 
ATOM   16709 C  CD1   . LEU A 1 3753 ? 144.566 100.785 126.487 1.00 141.32 ? 3753 LEU A CD1   1 
ATOM   16710 C  CD2   . LEU A 1 3753 ? 144.084 100.732 124.036 1.00 142.20 ? 3753 LEU A CD2   1 
ATOM   16711 N  N     . ASN A 1 3754 ? 142.139 105.590 124.293 1.00 141.74 ? 3754 ASN A N     1 
ATOM   16712 C  CA    . ASN A 1 3754 ? 140.905 106.368 124.298 1.00 139.40 ? 3754 ASN A CA    1 
ATOM   16713 C  C     . ASN A 1 3754 ? 140.370 106.580 122.887 1.00 139.63 ? 3754 ASN A C     1 
ATOM   16714 O  O     . ASN A 1 3754 ? 139.152 106.573 122.674 1.00 141.12 ? 3754 ASN A O     1 
ATOM   16715 C  CB    . ASN A 1 3754 ? 141.135 107.716 124.980 1.00 138.74 ? 3754 ASN A CB    1 
ATOM   16716 C  CG    . ASN A 1 3754 ? 141.420 107.578 126.459 1.00 139.54 ? 3754 ASN A CG    1 
ATOM   16717 O  OD1   . ASN A 1 3754 ? 142.110 108.409 127.047 1.00 141.15 ? 3754 ASN A OD1   1 
ATOM   16718 N  ND2   . ASN A 1 3754 ? 140.893 106.524 127.069 1.00 138.05 ? 3754 ASN A ND2   1 
ATOM   16719 N  N     . GLU A 1 3755 ? 141.260 106.768 121.916 1.00 146.43 ? 3755 GLU A N     1 
ATOM   16720 C  CA    . GLU A 1 3755 ? 140.885 107.103 120.550 1.00 147.31 ? 3755 GLU A CA    1 
ATOM   16721 C  C     . GLU A 1 3755 ? 140.371 105.907 119.755 1.00 147.58 ? 3755 GLU A C     1 
ATOM   16722 O  O     . GLU A 1 3755 ? 139.541 106.091 118.858 1.00 147.62 ? 3755 GLU A O     1 
ATOM   16723 C  CB    . GLU A 1 3755 ? 142.085 107.735 119.830 1.00 146.43 ? 3755 GLU A CB    1 
ATOM   16724 C  CG    . GLU A 1 3755 ? 141.907 107.959 118.335 1.00 147.40 ? 3755 GLU A CG    1 
ATOM   16725 C  CD    . GLU A 1 3755 ? 140.754 108.890 118.018 1.00 149.53 ? 3755 GLU A CD    1 
ATOM   16726 O  OE1   . GLU A 1 3755 ? 140.848 110.089 118.355 1.00 149.68 ? 3755 GLU A OE1   1 
ATOM   16727 O  OE2   . GLU A 1 3755 ? 139.756 108.429 117.426 1.00 149.02 ? 3755 GLU A OE2   1 
ATOM   16728 N  N     . VAL A 1 3756 ? 140.821 104.692 120.074 1.00 154.54 ? 3756 VAL A N     1 
ATOM   16729 C  CA    . VAL A 1 3756 ? 140.478 103.525 119.270 1.00 154.80 ? 3756 VAL A CA    1 
ATOM   16730 C  C     . VAL A 1 3756 ? 138.968 103.324 119.255 1.00 155.29 ? 3756 VAL A C     1 
ATOM   16731 O  O     . VAL A 1 3756 ? 138.288 103.456 120.282 1.00 154.82 ? 3756 VAL A O     1 
ATOM   16732 C  CB    . VAL A 1 3756 ? 141.211 102.276 119.795 1.00 156.22 ? 3756 VAL A CB    1 
ATOM   16733 C  CG1   . VAL A 1 3756 ? 140.886 102.029 121.262 1.00 154.72 ? 3756 VAL A CG1   1 
ATOM   16734 C  CG2   . VAL A 1 3756 ? 140.870 101.057 118.951 1.00 155.09 ? 3756 VAL A CG2   1 
ATOM   16735 N  N     . LYS A 1 3757 ? 138.433 103.022 118.074 1.00 153.70 ? 3757 LYS A N     1 
ATOM   16736 C  CA    . LYS A 1 3757 ? 137.001 102.861 117.870 1.00 152.91 ? 3757 LYS A CA    1 
ATOM   16737 C  C     . LYS A 1 3757 ? 136.665 101.382 117.735 1.00 152.66 ? 3757 LYS A C     1 
ATOM   16738 O  O     . LYS A 1 3757 ? 137.316 100.659 116.973 1.00 151.36 ? 3757 LYS A O     1 
ATOM   16739 C  CB    . LYS A 1 3757 ? 136.543 103.620 116.624 1.00 151.96 ? 3757 LYS A CB    1 
ATOM   16740 C  CG    . LYS A 1 3757 ? 136.852 105.107 116.655 1.00 151.84 ? 3757 LYS A CG    1 
ATOM   16741 C  CD    . LYS A 1 3757 ? 135.918 105.886 115.744 1.00 151.56 ? 3757 LYS A CD    1 
ATOM   16742 C  CE    . LYS A 1 3757 ? 134.462 105.560 116.030 1.00 151.81 ? 3757 LYS A CE    1 
ATOM   16743 N  NZ    . LYS A 1 3757 ? 133.597 106.768 115.940 1.00 151.69 ? 3757 LYS A NZ    1 
ATOM   16744 N  N     . GLY A 1 3758 ? 135.654 100.938 118.476 1.00 170.17 ? 3758 GLY A N     1 
ATOM   16745 C  CA    . GLY A 1 3758 ? 135.229 99.555  118.413 1.00 171.06 ? 3758 GLY A CA    1 
ATOM   16746 C  C     . GLY A 1 3758 ? 136.101 98.628  119.233 1.00 172.65 ? 3758 GLY A C     1 
ATOM   16747 O  O     . GLY A 1 3758 ? 136.044 98.637  120.466 1.00 171.47 ? 3758 GLY A O     1 
ATOM   16748 N  N     . ARG A 1 3759 ? 136.914 97.821  118.556 1.00 183.64 ? 3759 ARG A N     1 
ATOM   16749 C  CA    . ARG A 1 3759 ? 137.788 96.862  119.211 1.00 182.66 ? 3759 ARG A CA    1 
ATOM   16750 C  C     . ARG A 1 3759 ? 139.214 97.036  118.707 1.00 182.39 ? 3759 ARG A C     1 
ATOM   16751 O  O     . ARG A 1 3759 ? 139.450 97.489  117.584 1.00 182.65 ? 3759 ARG A O     1 
ATOM   16752 C  CB    . ARG A 1 3759 ? 137.320 95.418  118.976 1.00 182.18 ? 3759 ARG A CB    1 
ATOM   16753 C  CG    . ARG A 1 3759 ? 135.827 95.210  119.184 1.00 182.23 ? 3759 ARG A CG    1 
ATOM   16754 C  CD    . ARG A 1 3759 ? 135.375 93.851  118.678 1.00 182.10 ? 3759 ARG A CD    1 
ATOM   16755 N  NE    . ARG A 1 3759 ? 135.564 93.705  117.240 1.00 183.67 ? 3759 ARG A NE    1 
ATOM   16756 C  CZ    . ARG A 1 3759 ? 135.220 92.628  116.547 1.00 183.48 ? 3759 ARG A CZ    1 
ATOM   16757 N  NH1   . ARG A 1 3759 ? 134.667 91.577  117.132 1.00 183.06 ? 3759 ARG A NH1   1 
ATOM   16758 N  NH2   . ARG A 1 3759 ? 135.436 92.603  115.235 1.00 183.29 ? 3759 ARG A NH2   1 
ATOM   16759 N  N     . ILE A 1 3760 ? 140.169 96.671  119.564 1.00 180.59 ? 3760 ILE A N     1 
ATOM   16760 C  CA    . ILE A 1 3760 ? 141.577 96.769  119.196 1.00 181.18 ? 3760 ILE A CA    1 
ATOM   16761 C  C     . ILE A 1 3760 ? 141.907 95.792  118.074 1.00 181.85 ? 3760 ILE A C     1 
ATOM   16762 O  O     . ILE A 1 3760 ? 142.705 96.098  117.180 1.00 181.71 ? 3760 ILE A O     1 
ATOM   16763 C  CB    . ILE A 1 3760 ? 142.467 96.534  120.432 1.00 181.47 ? 3760 ILE A CB    1 
ATOM   16764 C  CG1   . ILE A 1 3760 ? 142.035 97.446  121.582 1.00 181.58 ? 3760 ILE A CG1   1 
ATOM   16765 C  CG2   . ILE A 1 3760 ? 143.932 96.755  120.092 1.00 180.36 ? 3760 ILE A CG2   1 
ATOM   16766 C  CD1   . ILE A 1 3760 ? 142.880 97.297  122.828 1.00 181.39 ? 3760 ILE A CD1   1 
ATOM   16767 N  N     . LEU A 1 3761 ? 141.297 94.605  118.098 1.00 180.40 ? 3761 LEU A N     1 
ATOM   16768 C  CA    . LEU A 1 3761 ? 141.623 93.584  117.108 1.00 179.87 ? 3761 LEU A CA    1 
ATOM   16769 C  C     . LEU A 1 3761 ? 141.082 93.928  115.727 1.00 179.01 ? 3761 LEU A C     1 
ATOM   16770 O  O     . LEU A 1 3761 ? 141.514 93.336  114.731 1.00 177.21 ? 3761 LEU A O     1 
ATOM   16771 C  CB    . LEU A 1 3761 ? 141.088 92.227  117.564 1.00 179.14 ? 3761 LEU A CB    1 
ATOM   16772 C  CG    . LEU A 1 3761 ? 141.789 91.641  118.788 1.00 178.23 ? 3761 LEU A CG    1 
ATOM   16773 C  CD1   . LEU A 1 3761 ? 141.090 90.376  119.267 1.00 177.73 ? 3761 LEU A CD1   1 
ATOM   16774 C  CD2   . LEU A 1 3761 ? 143.251 91.376  118.478 1.00 178.05 ? 3761 LEU A CD2   1 
ATOM   16775 N  N     . ASP A 1 3762 ? 140.136 94.867  115.643 1.00 184.91 ? 3762 ASP A N     1 
ATOM   16776 C  CA    . ASP A 1 3762 ? 139.547 95.209  114.351 1.00 184.67 ? 3762 ASP A CA    1 
ATOM   16777 C  C     . ASP A 1 3762 ? 140.582 95.801  113.403 1.00 184.99 ? 3762 ASP A C     1 
ATOM   16778 O  O     . ASP A 1 3762 ? 140.585 95.492  112.205 1.00 184.99 ? 3762 ASP A O     1 
ATOM   16779 C  CB    . ASP A 1 3762 ? 138.380 96.178  114.543 1.00 184.38 ? 3762 ASP A CB    1 
ATOM   16780 C  CG    . ASP A 1 3762 ? 137.114 95.482  115.002 1.00 184.53 ? 3762 ASP A CG    1 
ATOM   16781 O  OD1   . ASP A 1 3762 ? 136.758 94.443  114.408 1.00 184.93 ? 3762 ASP A OD1   1 
ATOM   16782 O  OD2   . ASP A 1 3762 ? 136.469 95.979  115.948 1.00 183.72 ? 3762 ASP A OD2   1 
ATOM   16783 N  N     . ASP A 1 3763 ? 141.465 96.655  113.913 1.00 183.92 ? 3763 ASP A N     1 
ATOM   16784 C  CA    . ASP A 1 3763 ? 142.477 97.324  113.104 1.00 183.47 ? 3763 ASP A CA    1 
ATOM   16785 C  C     . ASP A 1 3763 ? 143.863 96.900  113.576 1.00 183.80 ? 3763 ASP A C     1 
ATOM   16786 O  O     . ASP A 1 3763 ? 144.054 96.591  114.756 1.00 184.40 ? 3763 ASP A O     1 
ATOM   16787 C  CB    . ASP A 1 3763 ? 142.313 98.843  113.173 1.00 183.12 ? 3763 ASP A CB    1 
ATOM   16788 C  CG    . ASP A 1 3763 ? 142.954 99.448  114.405 1.00 183.61 ? 3763 ASP A CG    1 
ATOM   16789 O  OD1   . ASP A 1 3763 ? 142.738 98.916  115.514 1.00 182.91 ? 3763 ASP A OD1   1 
ATOM   16790 O  OD2   . ASP A 1 3763 ? 143.677 100.455 114.261 1.00 183.71 ? 3763 ASP A OD2   1 
ATOM   16791 N  N     . ASP A 1 3764 ? 144.822 96.874  112.647 1.00 175.75 ? 3764 ASP A N     1 
ATOM   16792 C  CA    . ASP A 1 3764 ? 146.168 96.425  112.985 1.00 175.43 ? 3764 ASP A CA    1 
ATOM   16793 C  C     . ASP A 1 3764 ? 147.084 97.591  113.338 1.00 175.56 ? 3764 ASP A C     1 
ATOM   16794 O  O     . ASP A 1 3764 ? 148.086 97.399  114.038 1.00 176.33 ? 3764 ASP A O     1 
ATOM   16795 C  CB    . ASP A 1 3764 ? 146.757 95.625  111.824 1.00 176.09 ? 3764 ASP A CB    1 
ATOM   16796 C  CG    . ASP A 1 3764 ? 146.599 94.132  112.011 1.00 177.13 ? 3764 ASP A CG    1 
ATOM   16797 O  OD1   . ASP A 1 3764 ? 147.168 93.367  111.203 1.00 176.52 ? 3764 ASP A OD1   1 
ATOM   16798 O  OD2   . ASP A 1 3764 ? 145.904 93.722  112.964 1.00 177.03 ? 3764 ASP A OD2   1 
ATOM   16799 N  N     . THR A 1 3765 ? 146.762 98.796  112.861 1.00 176.04 ? 3765 THR A N     1 
ATOM   16800 C  CA    . THR A 1 3765 ? 147.605 99.954  113.145 1.00 177.13 ? 3765 THR A CA    1 
ATOM   16801 C  C     . THR A 1 3765 ? 147.662 100.238 114.640 1.00 176.75 ? 3765 THR A C     1 
ATOM   16802 O  O     . THR A 1 3765 ? 148.734 100.527 115.184 1.00 176.33 ? 3765 THR A O     1 
ATOM   16803 C  CB    . THR A 1 3765 ? 147.091 101.179 112.390 1.00 175.19 ? 3765 THR A CB    1 
ATOM   16804 O  OG1   . THR A 1 3765 ? 146.787 100.818 111.038 1.00 174.90 ? 3765 THR A OG1   1 
ATOM   16805 C  CG2   . THR A 1 3765 ? 148.140 102.280 112.391 1.00 173.91 ? 3765 THR A CG2   1 
ATOM   16806 N  N     . ILE A 1 3766 ? 146.518 100.154 115.321 1.00 174.88 ? 3766 ILE A N     1 
ATOM   16807 C  CA    . ILE A 1 3766 ? 146.493 100.376 116.763 1.00 174.17 ? 3766 ILE A CA    1 
ATOM   16808 C  C     . ILE A 1 3766 ? 147.327 99.319  117.478 1.00 174.44 ? 3766 ILE A C     1 
ATOM   16809 O  O     . ILE A 1 3766 ? 148.108 99.629  118.389 1.00 176.21 ? 3766 ILE A O     1 
ATOM   16810 C  CB    . ILE A 1 3766 ? 145.038 100.403 117.268 1.00 174.34 ? 3766 ILE A CB    1 
ATOM   16811 C  CG1   . ILE A 1 3766 ? 144.441 101.799 117.081 1.00 173.22 ? 3766 ILE A CG1   1 
ATOM   16812 C  CG2   . ILE A 1 3766 ? 144.954 99.975  118.723 1.00 175.36 ? 3766 ILE A CG2   1 
ATOM   16813 C  CD1   . ILE A 1 3766 ? 145.103 102.865 117.923 1.00 172.28 ? 3766 ILE A CD1   1 
ATOM   16814 N  N     . ILE A 1 3767 ? 147.181 98.057  117.072 1.00 167.96 ? 3767 ILE A N     1 
ATOM   16815 C  CA    . ILE A 1 3767 ? 147.946 96.983  117.699 1.00 168.47 ? 3767 ILE A CA    1 
ATOM   16816 C  C     . ILE A 1 3767 ? 149.438 97.250  117.553 1.00 169.22 ? 3767 ILE A C     1 
ATOM   16817 O  O     . ILE A 1 3767 ? 150.207 97.128  118.515 1.00 168.11 ? 3767 ILE A O     1 
ATOM   16818 C  CB    . ILE A 1 3767 ? 147.553 95.622  117.099 1.00 168.96 ? 3767 ILE A CB    1 
ATOM   16819 C  CG1   . ILE A 1 3767 ? 146.115 95.262  117.479 1.00 168.62 ? 3767 ILE A CG1   1 
ATOM   16820 C  CG2   . ILE A 1 3767 ? 148.509 94.542  117.566 1.00 168.89 ? 3767 ILE A CG2   1 
ATOM   16821 C  CD1   . ILE A 1 3767 ? 145.631 93.959  116.875 1.00 168.30 ? 3767 ILE A CD1   1 
ATOM   16822 N  N     . THR A 1 3768 ? 149.862 97.649  116.350 1.00 167.67 ? 3768 THR A N     1 
ATOM   16823 C  CA    . THR A 1 3768 ? 151.269 97.973  116.133 1.00 166.85 ? 3768 THR A CA    1 
ATOM   16824 C  C     . THR A 1 3768 ? 151.709 99.146  117.000 1.00 165.89 ? 3768 THR A C     1 
ATOM   16825 O  O     . THR A 1 3768 ? 152.824 99.146  117.536 1.00 165.70 ? 3768 THR A O     1 
ATOM   16826 C  CB    . THR A 1 3768 ? 151.521 98.282  114.657 1.00 165.35 ? 3768 THR A CB    1 
ATOM   16827 O  OG1   . THR A 1 3768 ? 150.616 99.303  114.219 1.00 164.49 ? 3768 THR A OG1   1 
ATOM   16828 C  CG2   . THR A 1 3768 ? 151.326 97.038  113.808 1.00 165.70 ? 3768 THR A CG2   1 
ATOM   16829 N  N     . THR A 1 3769 ? 150.854 100.164 117.139 1.00 161.17 ? 3769 THR A N     1 
ATOM   16830 C  CA    . THR A 1 3769 ? 151.233 101.330 117.932 1.00 160.08 ? 3769 THR A CA    1 
ATOM   16831 C  C     . THR A 1 3769 ? 151.475 100.958 119.390 1.00 160.58 ? 3769 THR A C     1 
ATOM   16832 O  O     . THR A 1 3769 ? 152.493 101.351 119.970 1.00 162.24 ? 3769 THR A O     1 
ATOM   16833 C  CB    . THR A 1 3769 ? 150.170 102.423 117.837 1.00 160.26 ? 3769 THR A CB    1 
ATOM   16834 O  OG1   . THR A 1 3769 ? 148.881 101.866 118.115 1.00 162.33 ? 3769 THR A OG1   1 
ATOM   16835 C  CG2   . THR A 1 3769 ? 150.169 103.053 116.456 1.00 160.48 ? 3769 THR A CG2   1 
ATOM   16836 N  N     . LEU A 1 3770 ? 150.558 100.202 120.003 1.00 156.47 ? 3770 LEU A N     1 
ATOM   16837 C  CA    . LEU A 1 3770 ? 150.794 99.801  121.393 1.00 156.80 ? 3770 LEU A CA    1 
ATOM   16838 C  C     . LEU A 1 3770 ? 151.955 98.821  121.529 1.00 158.48 ? 3770 LEU A C     1 
ATOM   16839 O  O     . LEU A 1 3770 ? 152.676 98.858  122.532 1.00 160.15 ? 3770 LEU A O     1 
ATOM   16840 C  CB    . LEU A 1 3770 ? 149.536 99.247  122.076 1.00 155.01 ? 3770 LEU A CB    1 
ATOM   16841 C  CG    . LEU A 1 3770 ? 148.239 100.048 122.286 1.00 155.09 ? 3770 LEU A CG    1 
ATOM   16842 C  CD1   . LEU A 1 3770 ? 147.555 100.577 121.059 1.00 156.56 ? 3770 LEU A CD1   1 
ATOM   16843 C  CD2   . LEU A 1 3770 ? 147.259 99.224  123.120 1.00 156.75 ? 3770 LEU A CD2   1 
ATOM   16844 N  N     . GLU A 1 3771 ? 152.162 97.937  120.548 1.00 157.94 ? 3771 GLU A N     1 
ATOM   16845 C  CA    . GLU A 1 3771 ? 153.331 97.062  120.625 1.00 157.12 ? 3771 GLU A CA    1 
ATOM   16846 C  C     . GLU A 1 3771 ? 154.625 97.870  120.625 1.00 156.64 ? 3771 GLU A C     1 
ATOM   16847 O  O     . GLU A 1 3771 ? 155.515 97.635  121.455 1.00 156.73 ? 3771 GLU A O     1 
ATOM   16848 C  CB    . GLU A 1 3771 ? 153.325 96.054  119.474 1.00 156.95 ? 3771 GLU A CB    1 
ATOM   16849 C  CG    . GLU A 1 3771 ? 152.198 95.030  119.519 1.00 158.11 ? 3771 GLU A CG    1 
ATOM   16850 C  CD    . GLU A 1 3771 ? 152.450 93.923  120.525 1.00 158.98 ? 3771 GLU A CD    1 
ATOM   16851 O  OE1   . GLU A 1 3771 ? 152.632 92.764  120.096 1.00 157.49 ? 3771 GLU A OE1   1 
ATOM   16852 O  OE2   . GLU A 1 3771 ? 152.465 94.210  121.740 1.00 159.19 ? 3771 GLU A OE2   1 
ATOM   16853 N  N     . ASN A 1 3772 ? 154.736 98.843  119.717 1.00 148.46 ? 3772 ASN A N     1 
ATOM   16854 C  CA    . ASN A 1 3772 ? 155.922 99.693  119.683 1.00 148.70 ? 3772 ASN A CA    1 
ATOM   16855 C  C     . ASN A 1 3772 ? 156.053 100.501 120.967 1.00 146.64 ? 3772 ASN A C     1 
ATOM   16856 O  O     . ASN A 1 3772 ? 157.160 100.673 121.493 1.00 145.45 ? 3772 ASN A O     1 
ATOM   16857 C  CB    . ASN A 1 3772 ? 155.870 100.618 118.467 1.00 146.87 ? 3772 ASN A CB    1 
ATOM   16858 C  CG    . ASN A 1 3772 ? 155.934 99.860  117.155 1.00 146.22 ? 3772 ASN A CG    1 
ATOM   16859 O  OD1   . ASN A 1 3772 ? 156.014 98.632  117.136 1.00 145.97 ? 3772 ASN A OD1   1 
ATOM   16860 N  ND2   . ASN A 1 3772 ? 155.903 100.592 116.047 1.00 146.22 ? 3772 ASN A ND2   1 
ATOM   16861 N  N     . LEU A 1 3773 ? 154.931 101.006 121.486 1.00 143.29 ? 3773 LEU A N     1 
ATOM   16862 C  CA    . LEU A 1 3773 ? 154.964 101.784 122.720 1.00 142.78 ? 3773 LEU A CA    1 
ATOM   16863 C  C     . LEU A 1 3773 ? 155.483 100.952 123.885 1.00 142.66 ? 3773 LEU A C     1 
ATOM   16864 O  O     . LEU A 1 3773 ? 156.321 101.419 124.663 1.00 144.71 ? 3773 LEU A O     1 
ATOM   16865 C  CB    . LEU A 1 3773 ? 153.568 102.326 123.029 1.00 142.95 ? 3773 LEU A CB    1 
ATOM   16866 C  CG    . LEU A 1 3773 ? 153.285 103.789 122.689 1.00 144.04 ? 3773 LEU A CG    1 
ATOM   16867 C  CD1   . LEU A 1 3773 ? 153.761 104.127 121.285 1.00 142.32 ? 3773 LEU A CD1   1 
ATOM   16868 C  CD2   . LEU A 1 3773 ? 151.800 104.075 122.833 1.00 143.03 ? 3773 LEU A CD2   1 
ATOM   16869 N  N     . LYS A 1 3774 ? 155.000 99.715  124.019 1.00 142.96 ? 3774 LYS A N     1 
ATOM   16870 C  CA    . LYS A 1 3774 ? 155.455 98.860  125.111 1.00 143.85 ? 3774 LYS A CA    1 
ATOM   16871 C  C     . LYS A 1 3774 ? 156.920 98.474  124.951 1.00 145.67 ? 3774 LYS A C     1 
ATOM   16872 O  O     . LYS A 1 3774 ? 157.671 98.452  125.935 1.00 146.02 ? 3774 LYS A O     1 
ATOM   16873 C  CB    . LYS A 1 3774 ? 154.574 97.615  125.211 1.00 143.89 ? 3774 LYS A CB    1 
ATOM   16874 C  CG    . LYS A 1 3774 ? 153.113 97.911  125.512 1.00 144.33 ? 3774 LYS A CG    1 
ATOM   16875 C  CD    . LYS A 1 3774 ? 152.954 98.719  126.795 1.00 143.78 ? 3774 LYS A CD    1 
ATOM   16876 C  CE    . LYS A 1 3774 ? 153.692 98.074  127.963 1.00 144.25 ? 3774 LYS A CE    1 
ATOM   16877 N  NZ    . LYS A 1 3774 ? 153.241 96.680  128.204 1.00 144.30 ? 3774 LYS A NZ    1 
ATOM   16878 N  N     . ARG A 1 3775 ? 157.348 98.165  123.723 1.00 141.16 ? 3775 ARG A N     1 
ATOM   16879 C  CA    . ARG A 1 3775 ? 158.761 97.866  123.506 1.00 139.73 ? 3775 ARG A CA    1 
ATOM   16880 C  C     . ARG A 1 3775 ? 159.638 99.048  123.904 1.00 140.89 ? 3775 ARG A C     1 
ATOM   16881 O  O     . ARG A 1 3775 ? 160.639 98.882  124.617 1.00 141.76 ? 3775 ARG A O     1 
ATOM   16882 C  CB    . ARG A 1 3775 ? 159.003 97.495  122.044 1.00 140.21 ? 3775 ARG A CB    1 
ATOM   16883 C  CG    . ARG A 1 3775 ? 158.343 96.200  121.597 1.00 140.48 ? 3775 ARG A CG    1 
ATOM   16884 C  CD    . ARG A 1 3775 ? 158.226 96.100  120.074 1.00 141.01 ? 3775 ARG A CD    1 
ATOM   16885 N  NE    . ARG A 1 3775 ? 159.498 96.285  119.381 1.00 142.49 ? 3775 ARG A NE    1 
ATOM   16886 C  CZ    . ARG A 1 3775 ? 159.931 97.439  118.890 1.00 141.64 ? 3775 ARG A CZ    1 
ATOM   16887 N  NH1   . ARG A 1 3775 ? 159.206 98.543  118.973 1.00 141.85 ? 3775 ARG A NH1   1 
ATOM   16888 N  NH2   . ARG A 1 3775 ? 161.121 97.486  118.297 1.00 140.26 ? 3775 ARG A NH2   1 
ATOM   16889 N  N     . GLU A 1 3776 ? 159.265 100.253 123.469 1.00 131.70 ? 3776 GLU A N     1 
ATOM   16890 C  CA    . GLU A 1 3776 ? 160.074 101.426 123.773 1.00 130.86 ? 3776 GLU A CA    1 
ATOM   16891 C  C     . GLU A 1 3776 ? 160.052 101.737 125.264 1.00 130.24 ? 3776 GLU A C     1 
ATOM   16892 O  O     . GLU A 1 3776 ? 161.064 102.163 125.830 1.00 132.50 ? 3776 GLU A O     1 
ATOM   16893 C  CB    . GLU A 1 3776 ? 159.591 102.622 122.954 1.00 131.11 ? 3776 GLU A CB    1 
ATOM   16894 C  CG    . GLU A 1 3776 ? 160.607 103.743 122.854 1.00 131.63 ? 3776 GLU A CG    1 
ATOM   16895 C  CD    . GLU A 1 3776 ? 159.965 105.108 122.756 1.00 131.46 ? 3776 GLU A CD    1 
ATOM   16896 O  OE1   . GLU A 1 3776 ? 160.590 106.089 123.207 1.00 130.71 ? 3776 GLU A OE1   1 
ATOM   16897 O  OE2   . GLU A 1 3776 ? 158.842 105.204 122.219 1.00 133.12 ? 3776 GLU A OE2   1 
ATOM   16898 N  N     . ALA A 1 3777 ? 158.909 101.521 125.920 1.00 131.69 ? 3777 ALA A N     1 
ATOM   16899 C  CA    . ALA A 1 3777 ? 158.842 101.708 127.365 1.00 133.15 ? 3777 ALA A CA    1 
ATOM   16900 C  C     . ALA A 1 3777 ? 159.777 100.747 128.085 1.00 134.63 ? 3777 ALA A C     1 
ATOM   16901 O  O     . ALA A 1 3777 ? 160.461 101.135 129.040 1.00 136.34 ? 3777 ALA A O     1 
ATOM   16902 C  CB    . ALA A 1 3777 ? 157.405 101.528 127.852 1.00 132.87 ? 3777 ALA A CB    1 
ATOM   16903 N  N     . ALA A 1 3778 ? 159.825 99.489  127.640 1.00 133.66 ? 3778 ALA A N     1 
ATOM   16904 C  CA    . ALA A 1 3778 ? 160.733 98.527  128.258 1.00 133.07 ? 3778 ALA A CA    1 
ATOM   16905 C  C     . ALA A 1 3778 ? 162.190 98.935  128.063 1.00 133.19 ? 3778 ALA A C     1 
ATOM   16906 O  O     . ALA A 1 3778 ? 163.004 98.833  128.992 1.00 134.23 ? 3778 ALA A O     1 
ATOM   16907 C  CB    . ALA A 1 3778 ? 160.483 97.129  127.693 1.00 132.16 ? 3778 ALA A CB    1 
ATOM   16908 N  N     . GLU A 1 3779 ? 162.539 99.402  126.861 1.00 131.25 ? 3779 GLU A N     1 
ATOM   16909 C  CA    . GLU A 1 3779 ? 163.910 99.853  126.630 1.00 131.79 ? 3779 GLU A CA    1 
ATOM   16910 C  C     . GLU A 1 3779 ? 164.256 101.049 127.511 1.00 131.38 ? 3779 GLU A C     1 
ATOM   16911 O  O     . GLU A 1 3779 ? 165.349 101.111 128.093 1.00 131.87 ? 3779 GLU A O     1 
ATOM   16912 C  CB    . GLU A 1 3779 ? 164.118 100.195 125.154 1.00 131.84 ? 3779 GLU A CB    1 
ATOM   16913 C  CG    . GLU A 1 3779 ? 163.690 99.102  124.182 1.00 133.35 ? 3779 GLU A CG    1 
ATOM   16914 C  CD    . GLU A 1 3779 ? 164.484 97.809  124.315 1.00 133.21 ? 3779 GLU A CD    1 
ATOM   16915 O  OE1   . GLU A 1 3779 ? 164.137 96.836  123.615 1.00 131.55 ? 3779 GLU A OE1   1 
ATOM   16916 O  OE2   . GLU A 1 3779 ? 165.466 97.764  125.086 1.00 134.32 ? 3779 GLU A OE2   1 
ATOM   16917 N  N     . VAL A 1 3780 ? 163.334 102.008 127.625 1.00 127.60 ? 3780 VAL A N     1 
ATOM   16918 C  CA    . VAL A 1 3780 ? 163.578 103.173 128.470 1.00 126.58 ? 3780 VAL A CA    1 
ATOM   16919 C  C     . VAL A 1 3780 ? 163.749 102.747 129.920 1.00 126.31 ? 3780 VAL A C     1 
ATOM   16920 O  O     . VAL A 1 3780 ? 164.600 103.278 130.641 1.00 129.29 ? 3780 VAL A O     1 
ATOM   16921 C  CB    . VAL A 1 3780 ? 162.446 104.203 128.309 1.00 126.88 ? 3780 VAL A CB    1 
ATOM   16922 C  CG1   . VAL A 1 3780 ? 162.583 105.308 129.343 1.00 126.81 ? 3780 VAL A CG1   1 
ATOM   16923 C  CG2   . VAL A 1 3780 ? 162.474 104.790 126.914 1.00 127.94 ? 3780 VAL A CG2   1 
ATOM   16924 N  N     . THR A 1 3781 ? 162.966 101.763 130.363 1.00 125.98 ? 3781 THR A N     1 
ATOM   16925 C  CA    . THR A 1 3781 ? 163.099 101.264 131.728 1.00 127.42 ? 3781 THR A CA    1 
ATOM   16926 C  C     . THR A 1 3781 ? 164.469 100.628 131.953 1.00 130.20 ? 3781 THR A C     1 
ATOM   16927 O  O     . THR A 1 3781 ? 165.085 100.804 133.015 1.00 134.03 ? 3781 THR A O     1 
ATOM   16928 C  CB    . THR A 1 3781 ? 161.987 100.259 132.024 1.00 126.31 ? 3781 THR A CB    1 
ATOM   16929 O  OG1   . THR A 1 3781 ? 160.720 100.826 131.667 1.00 129.74 ? 3781 THR A OG1   1 
ATOM   16930 C  CG2   . THR A 1 3781 ? 161.972 99.908  133.503 1.00 125.60 ? 3781 THR A CG2   1 
ATOM   16931 N  N     . ARG A 1 3782 ? 164.949 99.855  130.971 1.00 128.44 ? 3782 ARG A N     1 
ATOM   16932 C  CA    . ARG A 1 3782 ? 166.262 99.228  131.119 1.00 127.78 ? 3782 ARG A CA    1 
ATOM   16933 C  C     . ARG A 1 3782 ? 167.364 100.282 131.209 1.00 127.40 ? 3782 ARG A C     1 
ATOM   16934 O  O     . ARG A 1 3782 ? 168.264 100.190 132.066 1.00 125.49 ? 3782 ARG A O     1 
ATOM   16935 C  CB    . ARG A 1 3782 ? 166.519 98.227  129.985 1.00 127.65 ? 3782 ARG A CB    1 
ATOM   16936 C  CG    . ARG A 1 3782 ? 167.229 98.757  128.744 1.00 128.05 ? 3782 ARG A CG    1 
ATOM   16937 C  CD    . ARG A 1 3782 ? 167.406 97.676  127.682 1.00 127.40 ? 3782 ARG A CD    1 
ATOM   16938 N  NE    . ARG A 1 3782 ? 168.073 98.186  126.488 1.00 128.49 ? 3782 ARG A NE    1 
ATOM   16939 C  CZ    . ARG A 1 3782 ? 169.369 98.457  126.401 1.00 128.47 ? 3782 ARG A CZ    1 
ATOM   16940 N  NH1   . ARG A 1 3782 ? 170.186 98.266  127.424 1.00 127.48 ? 3782 ARG A NH1   1 
ATOM   16941 N  NH2   . ARG A 1 3782 ? 169.856 98.937  125.261 1.00 127.62 ? 3782 ARG A NH2   1 
ATOM   16942 N  N     . LYS A 1 3783 ? 167.284 101.317 130.366 1.00 128.23 ? 3783 LYS A N     1 
ATOM   16943 C  CA    . LYS A 1 3783 ? 168.215 102.434 130.493 1.00 128.17 ? 3783 LYS A CA    1 
ATOM   16944 C  C     . LYS A 1 3783 ? 168.091 103.080 131.867 1.00 126.73 ? 3783 LYS A C     1 
ATOM   16945 O  O     . LYS A 1 3783 ? 169.091 103.510 132.457 1.00 130.26 ? 3783 LYS A O     1 
ATOM   16946 C  CB    . LYS A 1 3783 ? 167.963 103.466 129.392 1.00 125.91 ? 3783 LYS A CB    1 
ATOM   16947 C  CG    . LYS A 1 3783 ? 167.795 102.895 127.993 1.00 124.46 ? 3783 LYS A CG    1 
ATOM   16948 C  CD    . LYS A 1 3783 ? 168.948 101.992 127.577 1.00 126.35 ? 3783 LYS A CD    1 
ATOM   16949 C  CE    . LYS A 1 3783 ? 170.243 102.775 127.447 1.00 127.64 ? 3783 LYS A CE    1 
ATOM   16950 N  NZ    . LYS A 1 3783 ? 171.421 101.888 127.228 1.00 126.84 ? 3783 LYS A NZ    1 
ATOM   16951 N  N     . VAL A 1 3784 ? 166.866 103.142 132.395 1.00 124.65 ? 3784 VAL A N     1 
ATOM   16952 C  CA    . VAL A 1 3784 ? 166.626 103.800 133.675 1.00 124.89 ? 3784 VAL A CA    1 
ATOM   16953 C  C     . VAL A 1 3784 ? 167.363 103.083 134.798 1.00 125.82 ? 3784 VAL A C     1 
ATOM   16954 O  O     . VAL A 1 3784 ? 168.057 103.718 135.600 1.00 128.99 ? 3784 VAL A O     1 
ATOM   16955 C  CB    . VAL A 1 3784 ? 165.117 103.892 133.961 1.00 126.60 ? 3784 VAL A CB    1 
ATOM   16956 C  CG1   . VAL A 1 3784 ? 164.872 104.063 135.451 1.00 124.76 ? 3784 VAL A CG1   1 
ATOM   16957 C  CG2   . VAL A 1 3784 ? 164.516 105.058 133.210 1.00 125.52 ? 3784 VAL A CG2   1 
ATOM   16958 N  N     . GLU A 1 3785 ? 167.236 101.751 134.881 1.00 128.61 ? 3785 GLU A N     1 
ATOM   16959 C  CA    . GLU A 1 3785 ? 167.932 101.098 135.994 1.00 130.10 ? 3785 GLU A CA    1 
ATOM   16960 C  C     . GLU A 1 3785 ? 169.442 101.071 135.780 1.00 131.10 ? 3785 GLU A C     1 
ATOM   16961 O  O     . GLU A 1 3785 ? 170.201 101.109 136.757 1.00 130.78 ? 3785 GLU A O     1 
ATOM   16962 C  CB    . GLU A 1 3785 ? 167.452 99.673  136.319 1.00 129.27 ? 3785 GLU A CB    1 
ATOM   16963 C  CG    . GLU A 1 3785 ? 165.983 99.337  136.245 1.00 130.53 ? 3785 GLU A CG    1 
ATOM   16964 C  CD    . GLU A 1 3785 ? 165.625 98.703  134.941 1.00 133.55 ? 3785 GLU A CD    1 
ATOM   16965 O  OE1   . GLU A 1 3785 ? 164.569 98.042  134.864 1.00 132.78 ? 3785 GLU A OE1   1 
ATOM   16966 O  OE2   . GLU A 1 3785 ? 166.461 98.775  134.027 1.00 134.00 ? 3785 GLU A OE2   1 
ATOM   16967 N  N     . GLU A 1 3786 ? 169.916 100.991 134.530 1.00 131.23 ? 3786 GLU A N     1 
ATOM   16968 C  CA    . GLU A 1 3786 ? 171.369 101.045 134.365 1.00 131.16 ? 3786 GLU A CA    1 
ATOM   16969 C  C     . GLU A 1 3786 ? 171.919 102.403 134.810 1.00 132.34 ? 3786 GLU A C     1 
ATOM   16970 O  O     . GLU A 1 3786 ? 172.950 102.476 135.500 1.00 133.54 ? 3786 GLU A O     1 
ATOM   16971 C  CB    . GLU A 1 3786 ? 171.762 100.718 132.921 1.00 129.87 ? 3786 GLU A CB    1 
ATOM   16972 C  CG    . GLU A 1 3786 ? 171.904 101.899 131.979 1.00 128.74 ? 3786 GLU A CG    1 
ATOM   16973 C  CD    . GLU A 1 3786 ? 171.957 101.477 130.530 1.00 131.12 ? 3786 GLU A CD    1 
ATOM   16974 O  OE1   . GLU A 1 3786 ? 171.641 100.304 130.242 1.00 131.85 ? 3786 GLU A OE1   1 
ATOM   16975 O  OE2   . GLU A 1 3786 ? 172.338 102.310 129.683 1.00 131.53 ? 3786 GLU A OE2   1 
ATOM   16976 N  N     . THR A 1 3787 ? 171.216 103.487 134.471 1.00 127.48 ? 3787 THR A N     1 
ATOM   16977 C  CA    . THR A 1 3787 ? 171.631 104.804 134.933 1.00 125.97 ? 3787 THR A CA    1 
ATOM   16978 C  C     . THR A 1 3787 ? 171.485 104.924 136.444 1.00 124.98 ? 3787 THR A C     1 
ATOM   16979 O  O     . THR A 1 3787 ? 172.276 105.617 137.092 1.00 128.01 ? 3787 THR A O     1 
ATOM   16980 C  CB    . THR A 1 3787 ? 170.822 105.883 134.211 1.00 125.38 ? 3787 THR A CB    1 
ATOM   16981 O  OG1   . THR A 1 3787 ? 171.223 105.933 132.836 1.00 124.66 ? 3787 THR A OG1   1 
ATOM   16982 C  CG2   . THR A 1 3787 ? 171.050 107.242 134.835 1.00 127.13 ? 3787 THR A CG2   1 
ATOM   16983 N  N     . ASP A 1 3788 ? 170.499 104.237 137.022 1.00 120.75 ? 3788 ASP A N     1 
ATOM   16984 C  CA    . ASP A 1 3788 ? 170.346 104.216 138.473 1.00 122.86 ? 3788 ASP A CA    1 
ATOM   16985 C  C     . ASP A 1 3788 ? 171.563 103.570 139.126 1.00 126.68 ? 3788 ASP A C     1 
ATOM   16986 O  O     . ASP A 1 3788 ? 172.055 104.054 140.149 1.00 129.18 ? 3788 ASP A O     1 
ATOM   16987 C  CB    . ASP A 1 3788 ? 169.030 103.495 138.817 1.00 123.86 ? 3788 ASP A CB    1 
ATOM   16988 C  CG    . ASP A 1 3788 ? 168.884 103.092 140.299 1.00 125.75 ? 3788 ASP A CG    1 
ATOM   16989 O  OD1   . ASP A 1 3788 ? 167.718 102.927 140.714 1.00 126.55 ? 3788 ASP A OD1   1 
ATOM   16990 O  OD2   . ASP A 1 3788 ? 169.860 102.906 141.052 1.00 125.25 ? 3788 ASP A OD2   1 
ATOM   16991 N  N     . ILE A 1 3789 ? 172.063 102.481 138.542 1.00 123.37 ? 3789 ILE A N     1 
ATOM   16992 C  CA    . ILE A 1 3789 ? 173.258 101.828 139.076 1.00 122.58 ? 3789 ILE A CA    1 
ATOM   16993 C  C     . ILE A 1 3789 ? 174.462 102.763 139.000 1.00 122.25 ? 3789 ILE A C     1 
ATOM   16994 O  O     . ILE A 1 3789 ? 175.233 102.896 139.966 1.00 121.64 ? 3789 ILE A O     1 
ATOM   16995 C  CB    . ILE A 1 3789 ? 173.515 100.506 138.329 1.00 121.55 ? 3789 ILE A CB    1 
ATOM   16996 C  CG1   . ILE A 1 3789 ? 172.637 99.387  138.895 1.00 120.45 ? 3789 ILE A CG1   1 
ATOM   16997 C  CG2   . ILE A 1 3789 ? 174.986 100.123 138.399 1.00 122.09 ? 3789 ILE A CG2   1 
ATOM   16998 C  CD1   . ILE A 1 3789 ? 172.734 99.231  140.396 1.00 119.84 ? 3789 ILE A CD1   1 
ATOM   16999 N  N     . VAL A 1 3790 ? 174.645 103.428 137.856 1.00 116.70 ? 3790 VAL A N     1 
ATOM   17000 C  CA    . VAL A 1 3790 ? 175.780 104.344 137.734 1.00 116.14 ? 3790 VAL A CA    1 
ATOM   17001 C  C     . VAL A 1 3790 ? 175.651 105.501 138.725 1.00 115.33 ? 3790 VAL A C     1 
ATOM   17002 O  O     . VAL A 1 3790 ? 176.641 105.938 139.330 1.00 117.44 ? 3790 VAL A O     1 
ATOM   17003 C  CB    . VAL A 1 3790 ? 175.925 104.845 136.286 1.00 117.06 ? 3790 VAL A CB    1 
ATOM   17004 C  CG1   . VAL A 1 3790 ? 177.279 105.502 136.095 1.00 115.22 ? 3790 VAL A CG1   1 
ATOM   17005 C  CG2   . VAL A 1 3790 ? 175.777 103.694 135.313 1.00 116.91 ? 3790 VAL A CG2   1 
ATOM   17006 N  N     . MET A 1 3791 ? 174.431 106.006 138.921 1.00 117.36 ? 3791 MET A N     1 
ATOM   17007 C  CA    . MET A 1 3791 ? 174.218 107.079 139.887 1.00 117.72 ? 3791 MET A CA    1 
ATOM   17008 C  C     . MET A 1 3791 ? 174.470 106.599 141.310 1.00 116.68 ? 3791 MET A C     1 
ATOM   17009 O  O     . MET A 1 3791 ? 174.952 107.362 142.151 1.00 120.73 ? 3791 MET A O     1 
ATOM   17010 C  CB    . MET A 1 3791 ? 172.803 107.640 139.750 1.00 117.18 ? 3791 MET A CB    1 
ATOM   17011 C  CG    . MET A 1 3791 ? 172.528 108.831 140.654 1.00 120.01 ? 3791 MET A CG    1 
ATOM   17012 S  SD    . MET A 1 3791 ? 173.927 109.965 140.751 1.00 125.62 ? 3791 MET A SD    1 
ATOM   17013 C  CE    . MET A 1 3791 ? 173.086 111.540 140.833 1.00 118.03 ? 3791 MET A CE    1 
ATOM   17014 N  N     . GLN A 1 3792 ? 174.142 105.341 141.602 1.00 113.46 ? 3792 GLN A N     1 
ATOM   17015 C  CA    . GLN A 1 3792 ? 174.450 104.788 142.916 1.00 115.60 ? 3792 GLN A CA    1 
ATOM   17016 C  C     . GLN A 1 3792 ? 175.955 104.769 143.143 1.00 115.85 ? 3792 GLN A C     1 
ATOM   17017 O  O     . GLN A 1 3792 ? 176.433 105.112 144.232 1.00 118.08 ? 3792 GLN A O     1 
ATOM   17018 C  CB    . GLN A 1 3792 ? 173.822 103.392 143.044 1.00 116.25 ? 3792 GLN A CB    1 
ATOM   17019 C  CG    . GLN A 1 3792 ? 174.141 102.557 144.299 1.00 115.07 ? 3792 GLN A CG    1 
ATOM   17020 C  CD    . GLN A 1 3792 ? 175.570 102.040 144.384 1.00 115.86 ? 3792 GLN A CD    1 
ATOM   17021 O  OE1   . GLN A 1 3792 ? 176.274 101.938 143.379 1.00 116.22 ? 3792 GLN A OE1   1 
ATOM   17022 N  NE2   . GLN A 1 3792 ? 175.997 101.696 145.592 1.00 116.27 ? 3792 GLN A NE2   1 
ATOM   17023 N  N     . GLU A 1 3793 ? 176.716 104.382 142.117 1.00 114.26 ? 3793 GLU A N     1 
ATOM   17024 C  CA    . GLU A 1 3793 ? 178.174 104.460 142.212 1.00 115.69 ? 3793 GLU A CA    1 
ATOM   17025 C  C     . GLU A 1 3793 ? 178.631 105.894 142.471 1.00 114.90 ? 3793 GLU A C     1 
ATOM   17026 O  O     . GLU A 1 3793 ? 179.523 106.139 143.298 1.00 114.94 ? 3793 GLU A O     1 
ATOM   17027 C  CB    . GLU A 1 3793 ? 178.807 103.913 140.932 1.00 115.44 ? 3793 GLU A CB    1 
ATOM   17028 C  CG    . GLU A 1 3793 ? 180.312 103.715 141.002 1.00 115.71 ? 3793 GLU A CG    1 
ATOM   17029 C  CD    . GLU A 1 3793 ? 181.084 104.927 140.521 1.00 119.06 ? 3793 GLU A CD    1 
ATOM   17030 O  OE1   . GLU A 1 3793 ? 180.585 105.635 139.620 1.00 118.91 ? 3793 GLU A OE1   1 
ATOM   17031 O  OE2   . GLU A 1 3793 ? 182.195 105.169 141.039 1.00 120.52 ? 3793 GLU A OE2   1 
ATOM   17032 N  N     . VAL A 1 3794 ? 178.022 106.855 141.773 1.00 108.72 ? 3794 VAL A N     1 
ATOM   17033 C  CA    . VAL A 1 3794 ? 178.349 108.263 141.992 1.00 104.82 ? 3794 VAL A CA    1 
ATOM   17034 C  C     . VAL A 1 3794 ? 178.067 108.663 143.437 1.00 106.93 ? 3794 VAL A C     1 
ATOM   17035 O  O     . VAL A 1 3794 ? 178.822 109.432 144.044 1.00 109.03 ? 3794 VAL A O     1 
ATOM   17036 C  CB    . VAL A 1 3794 ? 177.581 109.148 140.991 1.00 109.05 ? 3794 VAL A CB    1 
ATOM   17037 C  CG1   . VAL A 1 3794 ? 177.520 110.588 141.474 1.00 108.63 ? 3794 VAL A CG1   1 
ATOM   17038 C  CG2   . VAL A 1 3794 ? 178.227 109.073 139.619 1.00 108.02 ? 3794 VAL A CG2   1 
ATOM   17039 N  N     . GLU A 1 3795 ? 176.972 108.156 144.008 1.00 108.99 ? 3795 GLU A N     1 
ATOM   17040 C  CA    . GLU A 1 3795 ? 176.643 108.471 145.398 1.00 106.86 ? 3795 GLU A CA    1 
ATOM   17041 C  C     . GLU A 1 3795 ? 177.663 107.881 146.365 1.00 109.29 ? 3795 GLU A C     1 
ATOM   17042 O  O     . GLU A 1 3795 ? 178.018 108.520 147.363 1.00 113.33 ? 3795 GLU A O     1 
ATOM   17043 C  CB    . GLU A 1 3795 ? 175.236 107.981 145.744 1.00 107.72 ? 3795 GLU A CB    1 
ATOM   17044 C  CG    . GLU A 1 3795 ? 174.138 108.525 144.848 1.00 111.57 ? 3795 GLU A CG    1 
ATOM   17045 C  CD    . GLU A 1 3795 ? 172.754 108.116 145.309 1.00 114.66 ? 3795 GLU A CD    1 
ATOM   17046 O  OE1   . GLU A 1 3795 ? 171.963 107.634 144.470 1.00 114.74 ? 3795 GLU A OE1   1 
ATOM   17047 O  OE2   . GLU A 1 3795 ? 172.455 108.278 146.511 1.00 114.99 ? 3795 GLU A OE2   1 
ATOM   17048 N  N     . THR A 1 3796 ? 178.131 106.656 146.103 1.00 104.95 ? 3796 THR A N     1 
ATOM   17049 C  CA    . THR A 1 3796 ? 179.207 106.114 146.935 1.00 104.58 ? 3796 THR A CA    1 
ATOM   17050 C  C     . THR A 1 3796 ? 180.451 106.985 146.848 1.00 105.91 ? 3796 THR A C     1 
ATOM   17051 O  O     . THR A 1 3796 ? 181.156 107.175 147.846 1.00 106.37 ? 3796 THR A O     1 
ATOM   17052 C  CB    . THR A 1 3796 ? 179.555 104.673 146.553 1.00 108.21 ? 3796 THR A CB    1 
ATOM   17053 O  OG1   . THR A 1 3796 ? 180.552 104.668 145.522 1.00 106.49 ? 3796 THR A OG1   1 
ATOM   17054 C  CG2   . THR A 1 3796 ? 178.339 103.892 146.122 1.00 110.06 ? 3796 THR A CG2   1 
ATOM   17055 N  N     . VAL A 1 3797 ? 180.745 107.515 145.659 1.00 105.65 ? 3797 VAL A N     1 
ATOM   17056 C  CA    . VAL A 1 3797 ? 181.881 108.427 145.532 1.00 100.80 ? 3797 VAL A CA    1 
ATOM   17057 C  C     . VAL A 1 3797 ? 181.650 109.699 146.345 1.00 101.73 ? 3797 VAL A C     1 
ATOM   17058 O  O     . VAL A 1 3797 ? 182.552 110.178 147.043 1.00 100.22 ? 3797 VAL A O     1 
ATOM   17059 C  CB    . VAL A 1 3797 ? 182.152 108.746 144.052 1.00 100.10 ? 3797 VAL A CB    1 
ATOM   17060 C  CG1   . VAL A 1 3797 ? 183.271 109.766 143.932 1.00 97.80  ? 3797 VAL A CG1   1 
ATOM   17061 C  CG2   . VAL A 1 3797 ? 182.505 107.480 143.296 1.00 102.83 ? 3797 VAL A CG2   1 
ATOM   17062 N  N     . SER A 1 3798 ? 180.441 110.260 146.274 1.00 99.45  ? 3798 SER A N     1 
ATOM   17063 C  CA    . SER A 1 3798 ? 180.150 111.540 146.916 1.00 92.49  ? 3798 SER A CA    1 
ATOM   17064 C  C     . SER A 1 3798 ? 180.041 111.433 148.432 1.00 88.97  ? 3798 SER A C     1 
ATOM   17065 O  O     . SER A 1 3798 ? 180.190 112.448 149.127 1.00 92.60  ? 3798 SER A O     1 
ATOM   17066 C  CB    . SER A 1 3798 ? 178.854 112.122 146.352 1.00 94.79  ? 3798 SER A CB    1 
ATOM   17067 O  OG    . SER A 1 3798 ? 178.907 112.211 144.939 1.00 94.63  ? 3798 SER A OG    1 
ATOM   17068 N  N     . GLN A 1 3799 ? 179.767 110.235 148.956 1.00 92.37  ? 3799 GLN A N     1 
ATOM   17069 C  CA    . GLN A 1 3799 ? 179.646 110.070 150.402 1.00 96.18  ? 3799 GLN A CA    1 
ATOM   17070 C  C     . GLN A 1 3799 ? 180.923 110.491 151.120 1.00 101.80 ? 3799 GLN A C     1 
ATOM   17071 O  O     . GLN A 1 3799 ? 180.865 110.969 152.259 1.00 103.71 ? 3799 GLN A O     1 
ATOM   17072 C  CB    . GLN A 1 3799 ? 179.273 108.617 150.723 1.00 96.52  ? 3799 GLN A CB    1 
ATOM   17073 C  CG    . GLN A 1 3799 ? 179.271 108.215 152.203 1.00 99.68  ? 3799 GLN A CG    1 
ATOM   17074 C  CD    . GLN A 1 3799 ? 180.657 107.973 152.774 1.00 104.05 ? 3799 GLN A CD    1 
ATOM   17075 O  OE1   . GLN A 1 3799 ? 181.426 107.169 152.248 1.00 105.30 ? 3799 GLN A OE1   1 
ATOM   17076 N  NE2   . GLN A 1 3799 ? 180.983 108.675 153.852 1.00 100.24 ? 3799 GLN A NE2   1 
ATOM   17077 N  N     . GLN A 1 3800 ? 182.079 110.329 150.472 1.00 97.27  ? 3800 GLN A N     1 
ATOM   17078 C  CA    . GLN A 1 3800 ? 183.336 110.753 151.080 1.00 93.71  ? 3800 GLN A CA    1 
ATOM   17079 C  C     . GLN A 1 3800 ? 183.363 112.260 151.308 1.00 92.20  ? 3800 GLN A C     1 
ATOM   17080 O  O     . GLN A 1 3800 ? 183.800 112.725 152.367 1.00 91.89  ? 3800 GLN A O     1 
ATOM   17081 C  CB    . GLN A 1 3800 ? 184.511 110.326 150.201 1.00 93.14  ? 3800 GLN A CB    1 
ATOM   17082 C  CG    . GLN A 1 3800 ? 185.868 110.458 150.867 1.00 95.04  ? 3800 GLN A CG    1 
ATOM   17083 C  CD    . GLN A 1 3800 ? 186.956 109.717 150.117 1.00 96.64  ? 3800 GLN A CD    1 
ATOM   17084 O  OE1   . GLN A 1 3800 ? 186.808 109.402 148.937 1.00 95.78  ? 3800 GLN A OE1   1 
ATOM   17085 N  NE2   . GLN A 1 3800 ? 188.059 109.435 150.800 1.00 96.06  ? 3800 GLN A NE2   1 
ATOM   17086 N  N     . TYR A 1 3801 ? 182.899 113.036 150.331 1.00 88.68  ? 3801 TYR A N     1 
ATOM   17087 C  CA    . TYR A 1 3801 ? 182.907 114.488 150.425 1.00 86.93  ? 3801 TYR A CA    1 
ATOM   17088 C  C     . TYR A 1 3801 ? 181.660 115.054 151.089 1.00 82.51  ? 3801 TYR A C     1 
ATOM   17089 O  O     . TYR A 1 3801 ? 181.571 116.275 151.256 1.00 80.63  ? 3801 TYR A O     1 
ATOM   17090 C  CB    . TYR A 1 3801 ? 183.061 115.109 149.033 1.00 85.22  ? 3801 TYR A CB    1 
ATOM   17091 C  CG    . TYR A 1 3801 ? 184.378 114.794 148.363 1.00 85.34  ? 3801 TYR A CG    1 
ATOM   17092 C  CD1   . TYR A 1 3801 ? 184.559 113.609 147.665 1.00 84.06  ? 3801 TYR A CD1   1 
ATOM   17093 C  CD2   . TYR A 1 3801 ? 185.441 115.685 148.428 1.00 84.89  ? 3801 TYR A CD2   1 
ATOM   17094 C  CE1   . TYR A 1 3801 ? 185.760 113.319 147.052 1.00 83.93  ? 3801 TYR A CE1   1 
ATOM   17095 C  CE2   . TYR A 1 3801 ? 186.645 115.403 147.818 1.00 84.44  ? 3801 TYR A CE2   1 
ATOM   17096 C  CZ    . TYR A 1 3801 ? 186.800 114.219 147.131 1.00 88.35  ? 3801 TYR A CZ    1 
ATOM   17097 O  OH    . TYR A 1 3801 ? 187.999 113.935 146.522 1.00 95.03  ? 3801 TYR A OH    1 
ATOM   17098 N  N     . LEU A 1 3802 ? 180.698 114.209 151.456 1.00 82.29  ? 3802 LEU A N     1 
ATOM   17099 C  CA    . LEU A 1 3802 ? 179.488 114.691 152.122 1.00 83.44  ? 3802 LEU A CA    1 
ATOM   17100 C  C     . LEU A 1 3802 ? 179.752 115.454 153.419 1.00 86.47  ? 3802 LEU A C     1 
ATOM   17101 O  O     . LEU A 1 3802 ? 179.156 116.528 153.599 1.00 90.06  ? 3802 LEU A O     1 
ATOM   17102 C  CB    . LEU A 1 3802 ? 178.538 113.508 152.358 1.00 84.71  ? 3802 LEU A CB    1 
ATOM   17103 C  CG    . LEU A 1 3802 ? 177.112 113.805 152.833 1.00 81.10  ? 3802 LEU A CG    1 
ATOM   17104 C  CD1   . LEU A 1 3802 ? 176.156 112.756 152.295 1.00 81.62  ? 3802 LEU A CD1   1 
ATOM   17105 C  CD2   . LEU A 1 3802 ? 177.023 113.857 154.353 1.00 82.21  ? 3802 LEU A CD2   1 
ATOM   17106 N  N     . PRO A 1 3803 ? 180.586 114.978 154.357 1.00 79.61  ? 3803 PRO A N     1 
ATOM   17107 C  CA    . PRO A 1 3803 ? 180.760 115.729 155.616 1.00 75.43  ? 3803 PRO A CA    1 
ATOM   17108 C  C     . PRO A 1 3803 ? 181.287 117.142 155.427 1.00 79.98  ? 3803 PRO A C     1 
ATOM   17109 O  O     . PRO A 1 3803 ? 180.916 118.042 156.195 1.00 82.12  ? 3803 PRO A O     1 
ATOM   17110 C  CB    . PRO A 1 3803 ? 181.753 114.865 156.404 1.00 69.40  ? 3803 PRO A CB    1 
ATOM   17111 C  CG    . PRO A 1 3803 ? 181.585 113.503 155.852 1.00 75.53  ? 3803 PRO A CG    1 
ATOM   17112 C  CD    . PRO A 1 3803 ? 181.325 113.703 154.391 1.00 77.13  ? 3803 PRO A CD    1 
ATOM   17113 N  N     . LEU A 1 3804 ? 182.148 117.362 154.432 1.00 74.11  ? 3804 LEU A N     1 
ATOM   17114 C  CA    . LEU A 1 3804 ? 182.683 118.698 154.199 1.00 66.03  ? 3804 LEU A CA    1 
ATOM   17115 C  C     . LEU A 1 3804 ? 181.576 119.676 153.825 1.00 72.83  ? 3804 LEU A C     1 
ATOM   17116 O  O     . LEU A 1 3804 ? 181.600 120.839 154.240 1.00 79.88  ? 3804 LEU A O     1 
ATOM   17117 C  CB    . LEU A 1 3804 ? 183.754 118.649 153.111 1.00 64.71  ? 3804 LEU A CB    1 
ATOM   17118 C  CG    . LEU A 1 3804 ? 184.239 119.989 152.559 1.00 63.36  ? 3804 LEU A CG    1 
ATOM   17119 C  CD1   . LEU A 1 3804 ? 184.876 120.818 153.658 1.00 66.58  ? 3804 LEU A CD1   1 
ATOM   17120 C  CD2   . LEU A 1 3804 ? 185.216 119.767 151.424 1.00 70.72  ? 3804 LEU A CD2   1 
ATOM   17121 N  N     . SER A 1 3805 ? 180.597 119.223 153.039 1.00 68.31  ? 3805 SER A N     1 
ATOM   17122 C  CA    . SER A 1 3805 ? 179.466 120.081 152.699 1.00 63.75  ? 3805 SER A CA    1 
ATOM   17123 C  C     . SER A 1 3805 ? 178.660 120.453 153.938 1.00 72.73  ? 3805 SER A C     1 
ATOM   17124 O  O     . SER A 1 3805 ? 178.214 121.599 154.078 1.00 85.01  ? 3805 SER A O     1 
ATOM   17125 C  CB    . SER A 1 3805 ? 178.576 119.390 151.668 1.00 71.86  ? 3805 SER A CB    1 
ATOM   17126 O  OG    . SER A 1 3805 ? 177.837 118.339 152.263 1.00 77.70  ? 3805 SER A OG    1 
ATOM   17127 N  N     . THR A 1 3806 ? 178.449 119.493 154.842 1.00 64.83  ? 3806 THR A N     1 
ATOM   17128 C  CA    . THR A 1 3806 ? 177.750 119.790 156.088 1.00 65.15  ? 3806 THR A CA    1 
ATOM   17129 C  C     . THR A 1 3806 ? 178.518 120.815 156.913 1.00 67.60  ? 3806 THR A C     1 
ATOM   17130 O  O     . THR A 1 3806 ? 177.925 121.749 157.470 1.00 76.90  ? 3806 THR A O     1 
ATOM   17131 C  CB    . THR A 1 3806 ? 177.536 118.503 156.887 1.00 65.31  ? 3806 THR A CB    1 
ATOM   17132 O  OG1   . THR A 1 3806 ? 176.408 117.794 156.360 1.00 73.70  ? 3806 THR A OG1   1 
ATOM   17133 C  CG2   . THR A 1 3806 ? 177.288 118.811 158.355 1.00 64.83  ? 3806 THR A CG2   1 
ATOM   17134 N  N     . ALA A 1 3807 ? 179.842 120.661 156.992 1.00 61.62  ? 3807 ALA A N     1 
ATOM   17135 C  CA    . ALA A 1 3807 ? 180.653 121.637 157.712 1.00 61.15  ? 3807 ALA A CA    1 
ATOM   17136 C  C     . ALA A 1 3807 ? 180.553 123.015 157.070 1.00 65.42  ? 3807 ALA A C     1 
ATOM   17137 O  O     . ALA A 1 3807 ? 180.472 124.029 157.771 1.00 73.52  ? 3807 ALA A O     1 
ATOM   17138 C  CB    . ALA A 1 3807 ? 182.108 121.173 157.767 1.00 64.36  ? 3807 ALA A CB    1 
ATOM   17139 N  N     . CYS A 1 3808 ? 180.556 123.069 155.736 1.00 65.34  ? 3808 CYS A N     1 
ATOM   17140 C  CA    . CYS A 1 3808 ? 180.423 124.344 155.036 1.00 57.97  ? 3808 CYS A CA    1 
ATOM   17141 C  C     . CYS A 1 3808 ? 179.089 125.008 155.350 1.00 61.56  ? 3808 CYS A C     1 
ATOM   17142 O  O     . CYS A 1 3808 ? 179.026 126.218 155.605 1.00 76.52  ? 3808 CYS A O     1 
ATOM   17143 C  CB    . CYS A 1 3808 ? 180.564 124.128 153.529 1.00 63.45  ? 3808 CYS A CB    1 
ATOM   17144 S  SG    . CYS A 1 3808 ? 182.219 123.685 152.981 1.00 91.48  ? 3808 CYS A SG    1 
ATOM   17145 N  N     . SER A 1 3809 ? 178.006 124.230 155.322 1.00 56.34  ? 3809 SER A N     1 
ATOM   17146 C  CA    . SER A 1 3809 ? 176.691 124.790 155.614 1.00 58.55  ? 3809 SER A CA    1 
ATOM   17147 C  C     . SER A 1 3809 ? 176.621 125.308 157.044 1.00 67.05  ? 3809 SER A C     1 
ATOM   17148 O  O     . SER A 1 3809 ? 176.090 126.398 157.294 1.00 74.74  ? 3809 SER A O     1 
ATOM   17149 C  CB    . SER A 1 3809 ? 175.605 123.744 155.370 1.00 62.45  ? 3809 SER A CB    1 
ATOM   17150 O  OG    . SER A 1 3809 ? 175.369 122.977 156.537 1.00 62.27  ? 3809 SER A OG    1 
ATOM   17151 N  N     . SER A 1 3810 ? 177.160 124.541 157.995 1.00 54.29  ? 3810 SER A N     1 
ATOM   17152 C  CA    . SER A 1 3810 ? 177.167 124.989 159.383 1.00 47.39  ? 3810 SER A CA    1 
ATOM   17153 C  C     . SER A 1 3810 ? 177.985 126.263 159.545 1.00 59.24  ? 3810 SER A C     1 
ATOM   17154 O  O     . SER A 1 3810 ? 177.581 127.180 160.269 1.00 65.41  ? 3810 SER A O     1 
ATOM   17155 C  CB    . SER A 1 3810 ? 177.708 123.884 160.289 1.00 56.38  ? 3810 SER A CB    1 
ATOM   17156 O  OG    . SER A 1 3810 ? 176.862 122.748 160.268 1.00 63.72  ? 3810 SER A OG    1 
ATOM   17157 N  N     . ILE A 1 3811 ? 179.132 126.344 158.867 1.00 62.27  ? 3811 ILE A N     1 
ATOM   17158 C  CA    . ILE A 1 3811 ? 179.971 127.535 158.956 1.00 54.42  ? 3811 ILE A CA    1 
ATOM   17159 C  C     . ILE A 1 3811 ? 179.234 128.749 158.408 1.00 49.26  ? 3811 ILE A C     1 
ATOM   17160 O  O     . ILE A 1 3811 ? 179.243 129.825 159.017 1.00 59.03  ? 3811 ILE A O     1 
ATOM   17161 C  CB    . ILE A 1 3811 ? 181.307 127.303 158.226 1.00 50.88  ? 3811 ILE A CB    1 
ATOM   17162 C  CG1   . ILE A 1 3811 ? 182.248 126.467 159.092 1.00 54.72  ? 3811 ILE A CG1   1 
ATOM   17163 C  CG2   . ILE A 1 3811 ? 181.960 128.625 157.864 1.00 49.76  ? 3811 ILE A CG2   1 
ATOM   17164 C  CD1   . ILE A 1 3811 ? 183.584 126.201 158.446 1.00 56.83  ? 3811 ILE A CD1   1 
ATOM   17165 N  N     . TYR A 1 3812 ? 178.579 128.599 157.253 1.00 48.22  ? 3812 TYR A N     1 
ATOM   17166 C  CA    . TYR A 1 3812 ? 177.867 129.737 156.681 1.00 47.67  ? 3812 TYR A CA    1 
ATOM   17167 C  C     . TYR A 1 3812 ? 176.714 130.174 157.571 1.00 56.50  ? 3812 TYR A C     1 
ATOM   17168 O  O     . TYR A 1 3812 ? 176.485 131.375 157.753 1.00 72.25  ? 3812 TYR A O     1 
ATOM   17169 C  CB    . TYR A 1 3812 ? 177.340 129.420 155.286 1.00 52.26  ? 3812 TYR A CB    1 
ATOM   17170 C  CG    . TYR A 1 3812 ? 176.319 130.440 154.826 1.00 54.97  ? 3812 TYR A CG    1 
ATOM   17171 C  CD1   . TYR A 1 3812 ? 176.712 131.716 154.448 1.00 61.48  ? 3812 TYR A CD1   1 
ATOM   17172 C  CD2   . TYR A 1 3812 ? 174.964 130.142 154.806 1.00 62.47  ? 3812 TYR A CD2   1 
ATOM   17173 C  CE1   . TYR A 1 3812 ? 175.787 132.656 154.040 1.00 61.59  ? 3812 TYR A CE1   1 
ATOM   17174 C  CE2   . TYR A 1 3812 ? 174.033 131.075 154.398 1.00 62.00  ? 3812 TYR A CE2   1 
ATOM   17175 C  CZ    . TYR A 1 3812 ? 174.449 132.330 154.017 1.00 59.16  ? 3812 TYR A CZ    1 
ATOM   17176 O  OH    . TYR A 1 3812 ? 173.523 133.263 153.613 1.00 67.25  ? 3812 TYR A OH    1 
ATOM   17177 N  N     . PHE A 1 3813 ? 175.960 129.219 158.119 1.00 59.48  ? 3813 PHE A N     1 
ATOM   17178 C  CA    . PHE A 1 3813 ? 174.809 129.601 158.930 1.00 61.46  ? 3813 PHE A CA    1 
ATOM   17179 C  C     . PHE A 1 3813 ? 175.233 130.140 160.289 1.00 61.83  ? 3813 PHE A C     1 
ATOM   17180 O  O     . PHE A 1 3813 ? 174.463 130.858 160.935 1.00 63.94  ? 3813 PHE A O     1 
ATOM   17181 C  CB    . PHE A 1 3813 ? 173.854 128.420 159.077 1.00 63.21  ? 3813 PHE A CB    1 
ATOM   17182 C  CG    . PHE A 1 3813 ? 172.881 128.298 157.942 1.00 62.57  ? 3813 PHE A CG    1 
ATOM   17183 C  CD1   . PHE A 1 3813 ? 171.679 128.983 157.968 1.00 64.62  ? 3813 PHE A CD1   1 
ATOM   17184 C  CD2   . PHE A 1 3813 ? 173.176 127.518 156.839 1.00 64.68  ? 3813 PHE A CD2   1 
ATOM   17185 C  CE1   . PHE A 1 3813 ? 170.786 128.882 156.923 1.00 65.70  ? 3813 PHE A CE1   1 
ATOM   17186 C  CE2   . PHE A 1 3813 ? 172.287 127.413 155.790 1.00 67.72  ? 3813 PHE A CE2   1 
ATOM   17187 C  CZ    . PHE A 1 3813 ? 171.091 128.095 155.832 1.00 65.55  ? 3813 PHE A CZ    1 
ATOM   17188 N  N     . THR A 1 3814 ? 176.445 129.809 160.739 1.00 60.23  ? 3814 THR A N     1 
ATOM   17189 C  CA    . THR A 1 3814 ? 177.008 130.497 161.895 1.00 52.71  ? 3814 THR A CA    1 
ATOM   17190 C  C     . THR A 1 3814 ? 177.415 131.919 161.530 1.00 56.36  ? 3814 THR A C     1 
ATOM   17191 O  O     . THR A 1 3814 ? 177.190 132.858 162.303 1.00 66.15  ? 3814 THR A O     1 
ATOM   17192 C  CB    . THR A 1 3814 ? 178.202 129.711 162.440 1.00 54.35  ? 3814 THR A CB    1 
ATOM   17193 O  OG1   . THR A 1 3814 ? 177.730 128.561 163.153 1.00 56.55  ? 3814 THR A OG1   1 
ATOM   17194 C  CG2   . THR A 1 3814 ? 179.034 130.569 163.377 1.00 52.76  ? 3814 THR A CG2   1 
ATOM   17195 N  N     . MET A 1 3815 ? 178.003 132.097 160.343 1.00 60.72  ? 3815 MET A N     1 
ATOM   17196 C  CA    . MET A 1 3815 ? 178.412 133.427 159.899 1.00 55.67  ? 3815 MET A CA    1 
ATOM   17197 C  C     . MET A 1 3815 ? 177.215 134.356 159.749 1.00 66.78  ? 3815 MET A C     1 
ATOM   17198 O  O     . MET A 1 3815 ? 177.282 135.534 160.119 1.00 70.77  ? 3815 MET A O     1 
ATOM   17199 C  CB    . MET A 1 3815 ? 179.169 133.324 158.576 1.00 49.17  ? 3815 MET A CB    1 
ATOM   17200 C  CG    . MET A 1 3815 ? 180.573 132.765 158.696 1.00 58.47  ? 3815 MET A CG    1 
ATOM   17201 S  SD    . MET A 1 3815 ? 181.445 132.745 157.119 1.00 78.92  ? 3815 MET A SD    1 
ATOM   17202 C  CE    . MET A 1 3815 ? 180.610 134.066 156.245 1.00 71.27  ? 3815 MET A CE    1 
ATOM   17203 N  N     . GLU A 1 3816 ? 176.113 133.847 159.195 1.00 73.30  ? 3816 GLU A N     1 
ATOM   17204 C  CA    . GLU A 1 3816 ? 174.920 134.668 159.018 1.00 70.02  ? 3816 GLU A CA    1 
ATOM   17205 C  C     . GLU A 1 3816 ? 174.345 135.101 160.360 1.00 74.53  ? 3816 GLU A C     1 
ATOM   17206 O  O     . GLU A 1 3816 ? 173.835 136.220 160.492 1.00 79.40  ? 3816 GLU A O     1 
ATOM   17207 C  CB    . GLU A 1 3816 ? 173.873 133.904 158.208 1.00 67.74  ? 3816 GLU A CB    1 
ATOM   17208 C  CG    . GLU A 1 3816 ? 172.690 134.747 157.770 1.00 77.78  ? 3816 GLU A CG    1 
ATOM   17209 C  CD    . GLU A 1 3816 ? 172.946 135.476 156.466 1.00 84.46  ? 3816 GLU A CD    1 
ATOM   17210 O  OE1   . GLU A 1 3816 ? 173.173 134.799 155.442 1.00 83.09  ? 3816 GLU A OE1   1 
ATOM   17211 O  OE2   . GLU A 1 3816 ? 172.920 136.724 156.466 1.00 83.35  ? 3816 GLU A OE2   1 
ATOM   17212 N  N     . SER A 1 3817 ? 174.417 134.230 161.367 1.00 69.00  ? 3817 SER A N     1 
ATOM   17213 C  CA    . SER A 1 3817 ? 173.892 134.548 162.688 1.00 70.30  ? 3817 SER A CA    1 
ATOM   17214 C  C     . SER A 1 3817 ? 174.779 135.514 163.461 1.00 72.71  ? 3817 SER A C     1 
ATOM   17215 O  O     . SER A 1 3817 ? 174.387 135.949 164.549 1.00 76.20  ? 3817 SER A O     1 
ATOM   17216 C  CB    . SER A 1 3817 ? 173.700 133.265 163.495 1.00 69.21  ? 3817 SER A CB    1 
ATOM   17217 O  OG    . SER A 1 3817 ? 173.505 133.555 164.866 1.00 79.73  ? 3817 SER A OG    1 
ATOM   17218 N  N     . LEU A 1 3818 ? 175.960 135.852 162.937 1.00 62.23  ? 3818 LEU A N     1 
ATOM   17219 C  CA    . LEU A 1 3818 ? 176.849 136.783 163.623 1.00 53.87  ? 3818 LEU A CA    1 
ATOM   17220 C  C     . LEU A 1 3818 ? 176.254 138.179 163.738 1.00 49.74  ? 3818 LEU A C     1 
ATOM   17221 O  O     . LEU A 1 3818 ? 176.712 138.967 164.572 1.00 60.37  ? 3818 LEU A O     1 
ATOM   17222 C  CB    . LEU A 1 3818 ? 178.193 136.853 162.896 1.00 52.56  ? 3818 LEU A CB    1 
ATOM   17223 C  CG    . LEU A 1 3818 ? 179.310 135.937 163.394 1.00 53.76  ? 3818 LEU A CG    1 
ATOM   17224 C  CD1   . LEU A 1 3818 ? 180.524 136.071 162.503 1.00 55.35  ? 3818 LEU A CD1   1 
ATOM   17225 C  CD2   . LEU A 1 3818 ? 179.671 136.278 164.825 1.00 62.04  ? 3818 LEU A CD2   1 
ATOM   17226 N  N     . LYS A 1 3819 ? 175.252 138.507 162.921 1.00 49.21  ? 3819 LYS A N     1 
ATOM   17227 C  CA    . LYS A 1 3819 ? 174.626 139.820 162.990 1.00 51.18  ? 3819 LYS A CA    1 
ATOM   17228 C  C     . LYS A 1 3819 ? 173.790 140.011 164.247 1.00 56.73  ? 3819 LYS A C     1 
ATOM   17229 O  O     . LYS A 1 3819 ? 173.383 141.142 164.531 1.00 63.47  ? 3819 LYS A O     1 
ATOM   17230 C  CB    . LYS A 1 3819 ? 173.757 140.051 161.753 1.00 58.87  ? 3819 LYS A CB    1 
ATOM   17231 C  CG    . LYS A 1 3819 ? 172.474 139.241 161.737 1.00 62.08  ? 3819 LYS A CG    1 
ATOM   17232 C  CD    . LYS A 1 3819 ? 171.505 139.768 160.695 1.00 60.45  ? 3819 LYS A CD    1 
ATOM   17233 C  CE    . LYS A 1 3819 ? 171.797 139.178 159.327 1.00 61.32  ? 3819 LYS A CE    1 
ATOM   17234 N  NZ    . LYS A 1 3819 ? 171.318 137.773 159.220 1.00 62.33  ? 3819 LYS A NZ    1 
ATOM   17235 N  N     . GLN A 1 3820 ? 173.522 138.943 165.000 1.00 65.36  ? 3820 GLN A N     1 
ATOM   17236 C  CA    . GLN A 1 3820 ? 172.759 139.072 166.235 1.00 68.03  ? 3820 GLN A CA    1 
ATOM   17237 C  C     . GLN A 1 3820 ? 173.562 139.728 167.350 1.00 67.67  ? 3820 GLN A C     1 
ATOM   17238 O  O     . GLN A 1 3820 ? 172.974 140.397 168.206 1.00 76.01  ? 3820 GLN A O     1 
ATOM   17239 C  CB    . GLN A 1 3820 ? 172.263 137.702 166.697 1.00 66.51  ? 3820 GLN A CB    1 
ATOM   17240 C  CG    . GLN A 1 3820 ? 171.452 136.949 165.659 1.00 63.21  ? 3820 GLN A CG    1 
ATOM   17241 C  CD    . GLN A 1 3820 ? 170.137 137.630 165.347 1.00 72.45  ? 3820 GLN A CD    1 
ATOM   17242 O  OE1   . GLN A 1 3820 ? 169.775 137.805 164.184 1.00 78.43  ? 3820 GLN A OE1   1 
ATOM   17243 N  NE2   . GLN A 1 3820 ? 169.414 138.023 166.388 1.00 74.32  ? 3820 GLN A NE2   1 
ATOM   17244 N  N     . ILE A 1 3821 ? 174.886 139.558 167.360 1.00 52.50  ? 3821 ILE A N     1 
ATOM   17245 C  CA    . ILE A 1 3821 ? 175.720 140.109 168.425 1.00 50.20  ? 3821 ILE A CA    1 
ATOM   17246 C  C     . ILE A 1 3821 ? 176.277 141.485 168.092 1.00 61.28  ? 3821 ILE A C     1 
ATOM   17247 O  O     . ILE A 1 3821 ? 176.804 142.158 168.992 1.00 72.32  ? 3821 ILE A O     1 
ATOM   17248 C  CB    . ILE A 1 3821 ? 176.878 139.152 168.777 1.00 49.48  ? 3821 ILE A CB    1 
ATOM   17249 C  CG1   . ILE A 1 3821 ? 178.000 139.268 167.745 1.00 61.08  ? 3821 ILE A CG1   1 
ATOM   17250 C  CG2   . ILE A 1 3821 ? 176.377 137.722 168.863 1.00 54.15  ? 3821 ILE A CG2   1 
ATOM   17251 C  CD1   . ILE A 1 3821 ? 179.130 138.286 167.958 1.00 60.75  ? 3821 ILE A CD1   1 
ATOM   17252 N  N     . HIS A 1 3822 ? 176.174 141.928 166.841 1.00 65.89  ? 3822 HIS A N     1 
ATOM   17253 C  CA    . HIS A 1 3822 ? 176.650 143.245 166.444 1.00 65.03  ? 3822 HIS A CA    1 
ATOM   17254 C  C     . HIS A 1 3822 ? 176.086 143.562 165.068 1.00 73.37  ? 3822 HIS A C     1 
ATOM   17255 O  O     . HIS A 1 3822 ? 176.038 142.689 164.198 1.00 81.57  ? 3822 HIS A O     1 
ATOM   17256 C  CB    . HIS A 1 3822 ? 178.181 143.307 166.422 1.00 61.25  ? 3822 HIS A CB    1 
ATOM   17257 C  CG    . HIS A 1 3822 ? 178.736 144.687 166.587 1.00 67.69  ? 3822 HIS A CG    1 
ATOM   17258 N  ND1   . HIS A 1 3822 ? 178.741 145.615 165.568 1.00 75.17  ? 3822 HIS A ND1   1 
ATOM   17259 C  CD2   . HIS A 1 3822 ? 179.316 145.293 167.650 1.00 70.55  ? 3822 HIS A CD2   1 
ATOM   17260 C  CE1   . HIS A 1 3822 ? 179.294 146.735 165.998 1.00 69.69  ? 3822 HIS A CE1   1 
ATOM   17261 N  NE2   . HIS A 1 3822 ? 179.651 146.566 167.257 1.00 71.98  ? 3822 HIS A NE2   1 
ATOM   17262 N  N     . PHE A 1 3823 ? 175.658 144.812 164.879 1.00 68.05  ? 3823 PHE A N     1 
ATOM   17263 C  CA    . PHE A 1 3823 ? 175.057 145.208 163.611 1.00 67.14  ? 3823 PHE A CA    1 
ATOM   17264 C  C     . PHE A 1 3823 ? 176.055 145.186 162.461 1.00 66.39  ? 3823 PHE A C     1 
ATOM   17265 O  O     . PHE A 1 3823 ? 175.647 145.034 161.306 1.00 72.14  ? 3823 PHE A O     1 
ATOM   17266 C  CB    . PHE A 1 3823 ? 174.436 146.602 163.734 1.00 66.81  ? 3823 PHE A CB    1 
ATOM   17267 C  CG    . PHE A 1 3823 ? 175.416 147.675 164.123 1.00 62.98  ? 3823 PHE A CG    1 
ATOM   17268 C  CD1   . PHE A 1 3823 ? 176.150 148.349 163.159 1.00 61.86  ? 3823 PHE A CD1   1 
ATOM   17269 C  CD2   . PHE A 1 3823 ? 175.599 148.015 165.452 1.00 68.93  ? 3823 PHE A CD2   1 
ATOM   17270 C  CE1   . PHE A 1 3823 ? 177.049 149.334 163.515 1.00 71.62  ? 3823 PHE A CE1   1 
ATOM   17271 C  CE2   . PHE A 1 3823 ? 176.497 149.000 165.813 1.00 69.35  ? 3823 PHE A CE2   1 
ATOM   17272 C  CZ    . PHE A 1 3823 ? 177.222 149.661 164.843 1.00 71.45  ? 3823 PHE A CZ    1 
ATOM   17273 N  N     . LEU A 1 3824 ? 177.346 145.336 162.750 1.00 60.68  ? 3824 LEU A N     1 
ATOM   17274 C  CA    . LEU A 1 3824 ? 178.370 145.400 161.718 1.00 59.25  ? 3824 LEU A CA    1 
ATOM   17275 C  C     . LEU A 1 3824 ? 178.654 144.054 161.066 1.00 63.23  ? 3824 LEU A C     1 
ATOM   17276 O  O     . LEU A 1 3824 ? 179.284 144.021 160.004 1.00 70.80  ? 3824 LEU A O     1 
ATOM   17277 C  CB    . LEU A 1 3824 ? 179.665 145.961 162.312 1.00 57.03  ? 3824 LEU A CB    1 
ATOM   17278 C  CG    . LEU A 1 3824 ? 180.690 146.551 161.346 1.00 58.81  ? 3824 LEU A CG    1 
ATOM   17279 C  CD1   . LEU A 1 3824 ? 180.272 147.946 160.920 1.00 66.03  ? 3824 LEU A CD1   1 
ATOM   17280 C  CD2   . LEU A 1 3824 ? 182.066 146.570 161.986 1.00 58.79  ? 3824 LEU A CD2   1 
ATOM   17281 N  N     . TYR A 1 3825 ? 178.203 142.950 161.659 1.00 60.59  ? 3825 TYR A N     1 
ATOM   17282 C  CA    . TYR A 1 3825 ? 178.584 141.616 161.193 1.00 59.31  ? 3825 TYR A CA    1 
ATOM   17283 C  C     . TYR A 1 3825 ? 177.580 141.127 160.148 1.00 68.54  ? 3825 TYR A C     1 
ATOM   17284 O  O     . TYR A 1 3825 ? 176.857 140.146 160.329 1.00 71.47  ? 3825 TYR A O     1 
ATOM   17285 C  CB    . TYR A 1 3825 ? 178.691 140.655 162.370 1.00 62.54  ? 3825 TYR A CB    1 
ATOM   17286 C  CG    . TYR A 1 3825 ? 179.686 141.080 163.432 1.00 63.29  ? 3825 TYR A CG    1 
ATOM   17287 C  CD1   . TYR A 1 3825 ? 180.646 142.047 163.168 1.00 62.26  ? 3825 TYR A CD1   1 
ATOM   17288 C  CD2   . TYR A 1 3825 ? 179.661 140.516 164.699 1.00 66.69  ? 3825 TYR A CD2   1 
ATOM   17289 C  CE1   . TYR A 1 3825 ? 181.548 142.441 164.133 1.00 62.83  ? 3825 TYR A CE1   1 
ATOM   17290 C  CE2   . TYR A 1 3825 ? 180.564 140.901 165.669 1.00 61.11  ? 3825 TYR A CE2   1 
ATOM   17291 C  CZ    . TYR A 1 3825 ? 181.502 141.866 165.381 1.00 65.42  ? 3825 TYR A CZ    1 
ATOM   17292 O  OH    . TYR A 1 3825 ? 182.404 142.255 166.343 1.00 74.49  ? 3825 TYR A OH    1 
ATOM   17293 N  N     . GLN A 1 3826 ? 177.554 141.843 159.026 1.00 62.81  ? 3826 GLN A N     1 
ATOM   17294 C  CA    . GLN A 1 3826 ? 176.694 141.510 157.896 1.00 61.89  ? 3826 GLN A CA    1 
ATOM   17295 C  C     . GLN A 1 3826 ? 177.529 140.769 156.858 1.00 66.26  ? 3826 GLN A C     1 
ATOM   17296 O  O     . GLN A 1 3826 ? 178.415 141.358 156.230 1.00 59.62  ? 3826 GLN A O     1 
ATOM   17297 C  CB    . GLN A 1 3826 ? 176.068 142.768 157.299 1.00 59.40  ? 3826 GLN A CB    1 
ATOM   17298 C  CG    . GLN A 1 3826 ? 175.379 143.665 158.312 1.00 60.24  ? 3826 GLN A CG    1 
ATOM   17299 C  CD    . GLN A 1 3826 ? 174.104 143.057 158.854 1.00 64.04  ? 3826 GLN A CD    1 
ATOM   17300 O  OE1   . GLN A 1 3826 ? 173.413 142.312 158.160 1.00 66.13  ? 3826 GLN A OE1   1 
ATOM   17301 N  NE2   . GLN A 1 3826 ? 173.780 143.375 160.102 1.00 67.02  ? 3826 GLN A NE2   1 
ATOM   17302 N  N     . TYR A 1 3827 ? 177.245 139.481 156.676 1.00 63.66  ? 3827 TYR A N     1 
ATOM   17303 C  CA    . TYR A 1 3827 ? 177.975 138.643 155.732 1.00 60.71  ? 3827 TYR A CA    1 
ATOM   17304 C  C     . TYR A 1 3827 ? 176.986 138.015 154.764 1.00 66.81  ? 3827 TYR A C     1 
ATOM   17305 O  O     . TYR A 1 3827 ? 176.002 137.401 155.189 1.00 70.74  ? 3827 TYR A O     1 
ATOM   17306 C  CB    . TYR A 1 3827 ? 178.778 137.562 156.460 1.00 55.14  ? 3827 TYR A CB    1 
ATOM   17307 C  CG    . TYR A 1 3827 ? 179.779 138.117 157.445 1.00 60.05  ? 3827 TYR A CG    1 
ATOM   17308 C  CD1   . TYR A 1 3827 ? 180.905 138.801 157.009 1.00 68.75  ? 3827 TYR A CD1   1 
ATOM   17309 C  CD2   . TYR A 1 3827 ? 179.598 137.961 158.811 1.00 62.72  ? 3827 TYR A CD2   1 
ATOM   17310 C  CE1   . TYR A 1 3827 ? 181.821 139.313 157.904 1.00 67.06  ? 3827 TYR A CE1   1 
ATOM   17311 C  CE2   . TYR A 1 3827 ? 180.510 138.468 159.714 1.00 66.15  ? 3827 TYR A CE2   1 
ATOM   17312 C  CZ    . TYR A 1 3827 ? 181.619 139.143 159.255 1.00 67.92  ? 3827 TYR A CZ    1 
ATOM   17313 O  OH    . TYR A 1 3827 ? 182.531 139.651 160.149 1.00 72.02  ? 3827 TYR A OH    1 
ATOM   17314 N  N     . SER A 1 3828 ? 177.246 138.170 153.471 1.00 75.24  ? 3828 SER A N     1 
ATOM   17315 C  CA    . SER A 1 3828 ? 176.380 137.620 152.443 1.00 72.87  ? 3828 SER A CA    1 
ATOM   17316 C  C     . SER A 1 3828 ? 176.805 136.198 152.086 1.00 78.40  ? 3828 SER A C     1 
ATOM   17317 O  O     . SER A 1 3828 ? 177.839 135.694 152.532 1.00 88.10  ? 3828 SER A O     1 
ATOM   17318 C  CB    . SER A 1 3828 ? 176.396 138.508 151.201 1.00 73.89  ? 3828 SER A CB    1 
ATOM   17319 O  OG    . SER A 1 3828 ? 177.697 138.578 150.645 1.00 73.73  ? 3828 SER A OG    1 
ATOM   17320 N  N     . LEU A 1 3829 ? 175.980 135.545 151.265 1.00 76.20  ? 3829 LEU A N     1 
ATOM   17321 C  CA    . LEU A 1 3829 ? 176.314 134.206 150.794 1.00 69.24  ? 3829 LEU A CA    1 
ATOM   17322 C  C     . LEU A 1 3829 ? 177.500 134.231 149.840 1.00 70.50  ? 3829 LEU A C     1 
ATOM   17323 O  O     . LEU A 1 3829 ? 178.299 133.286 149.818 1.00 79.36  ? 3829 LEU A O     1 
ATOM   17324 C  CB    . LEU A 1 3829 ? 175.099 133.571 150.120 1.00 67.09  ? 3829 LEU A CB    1 
ATOM   17325 C  CG    . LEU A 1 3829 ? 175.293 132.173 149.535 1.00 68.84  ? 3829 LEU A CG    1 
ATOM   17326 C  CD1   . LEU A 1 3829 ? 175.544 131.167 150.645 1.00 71.90  ? 3829 LEU A CD1   1 
ATOM   17327 C  CD2   . LEU A 1 3829 ? 174.092 131.766 148.699 1.00 74.65  ? 3829 LEU A CD2   1 
ATOM   17328 N  N     . GLN A 1 3830 ? 177.631 135.298 149.049 1.00 56.06  ? 3830 GLN A N     1 
ATOM   17329 C  CA    . GLN A 1 3830 ? 178.758 135.405 148.130 1.00 57.91  ? 3830 GLN A CA    1 
ATOM   17330 C  C     . GLN A 1 3830 ? 180.084 135.455 148.873 1.00 65.31  ? 3830 GLN A C     1 
ATOM   17331 O  O     . GLN A 1 3830 ? 181.097 134.979 148.356 1.00 76.11  ? 3830 GLN A O     1 
ATOM   17332 C  CB    . GLN A 1 3830 ? 178.598 136.639 147.243 1.00 69.15  ? 3830 GLN A CB    1 
ATOM   17333 C  CG    . GLN A 1 3830 ? 179.487 136.641 146.010 1.00 68.87  ? 3830 GLN A CG    1 
ATOM   17334 C  CD    . GLN A 1 3830 ? 179.615 135.270 145.379 1.00 73.56  ? 3830 GLN A CD    1 
ATOM   17335 O  OE1   . GLN A 1 3830 ? 178.629 134.684 144.932 1.00 75.77  ? 3830 GLN A OE1   1 
ATOM   17336 N  NE2   . GLN A 1 3830 ? 180.836 134.750 145.335 1.00 74.15  ? 3830 GLN A NE2   1 
ATOM   17337 N  N     . PHE A 1 3831 ? 180.098 136.014 150.084 1.00 63.22  ? 3831 PHE A N     1 
ATOM   17338 C  CA    . PHE A 1 3831 ? 181.320 136.034 150.883 1.00 62.93  ? 3831 PHE A CA    1 
ATOM   17339 C  C     . PHE A 1 3831 ? 181.779 134.618 151.215 1.00 65.21  ? 3831 PHE A C     1 
ATOM   17340 O  O     . PHE A 1 3831 ? 182.953 134.266 151.031 1.00 73.10  ? 3831 PHE A O     1 
ATOM   17341 C  CB    . PHE A 1 3831 ? 181.080 136.844 152.157 1.00 59.04  ? 3831 PHE A CB    1 
ATOM   17342 C  CG    . PHE A 1 3831 ? 182.313 137.072 152.977 1.00 61.20  ? 3831 PHE A CG    1 
ATOM   17343 C  CD1   . PHE A 1 3831 ? 183.402 137.737 152.445 1.00 71.63  ? 3831 PHE A CD1   1 
ATOM   17344 C  CD2   . PHE A 1 3831 ? 182.376 136.636 154.289 1.00 62.20  ? 3831 PHE A CD2   1 
ATOM   17345 C  CE1   . PHE A 1 3831 ? 184.535 137.953 153.201 1.00 74.13  ? 3831 PHE A CE1   1 
ATOM   17346 C  CE2   . PHE A 1 3831 ? 183.505 136.848 155.049 1.00 68.54  ? 3831 PHE A CE2   1 
ATOM   17347 C  CZ    . PHE A 1 3831 ? 184.586 137.508 154.505 1.00 73.62  ? 3831 PHE A CZ    1 
ATOM   17348 N  N     . PHE A 1 3832 ? 180.855 133.782 151.692 1.00 61.35  ? 3832 PHE A N     1 
ATOM   17349 C  CA    . PHE A 1 3832 ? 181.210 132.404 152.002 1.00 60.18  ? 3832 PHE A CA    1 
ATOM   17350 C  C     . PHE A 1 3832 ? 181.549 131.617 150.743 1.00 57.35  ? 3832 PHE A C     1 
ATOM   17351 O  O     . PHE A 1 3832 ? 182.419 130.740 150.780 1.00 64.11  ? 3832 PHE A O     1 
ATOM   17352 C  CB    . PHE A 1 3832 ? 180.079 131.720 152.764 1.00 47.99  ? 3832 PHE A CB    1 
ATOM   17353 C  CG    . PHE A 1 3832 ? 180.333 130.270 153.030 1.00 55.05  ? 3832 PHE A CG    1 
ATOM   17354 C  CD1   . PHE A 1 3832 ? 181.273 129.885 153.968 1.00 59.06  ? 3832 PHE A CD1   1 
ATOM   17355 C  CD2   . PHE A 1 3832 ? 179.647 129.292 152.334 1.00 59.58  ? 3832 PHE A CD2   1 
ATOM   17356 C  CE1   . PHE A 1 3832 ? 181.518 128.555 154.214 1.00 59.92  ? 3832 PHE A CE1   1 
ATOM   17357 C  CE2   . PHE A 1 3832 ? 179.889 127.958 152.577 1.00 60.37  ? 3832 PHE A CE2   1 
ATOM   17358 C  CZ    . PHE A 1 3832 ? 180.826 127.590 153.517 1.00 62.56  ? 3832 PHE A CZ    1 
ATOM   17359 N  N     . LEU A 1 3833 ? 180.877 131.906 149.627 1.00 63.03  ? 3833 LEU A N     1 
ATOM   17360 C  CA    . LEU A 1 3833 ? 181.232 131.243 148.376 1.00 60.94  ? 3833 LEU A CA    1 
ATOM   17361 C  C     . LEU A 1 3833 ? 182.641 131.616 147.931 1.00 68.91  ? 3833 LEU A C     1 
ATOM   17362 O  O     . LEU A 1 3833 ? 183.379 130.764 147.426 1.00 81.87  ? 3833 LEU A O     1 
ATOM   17363 C  CB    . LEU A 1 3833 ? 180.213 131.576 147.288 1.00 67.96  ? 3833 LEU A CB    1 
ATOM   17364 C  CG    . LEU A 1 3833 ? 179.136 130.513 147.063 1.00 70.98  ? 3833 LEU A CG    1 
ATOM   17365 C  CD1   . LEU A 1 3833 ? 179.775 129.159 146.809 1.00 68.92  ? 3833 LEU A CD1   1 
ATOM   17366 C  CD2   . LEU A 1 3833 ? 178.200 130.436 148.249 1.00 71.88  ? 3833 LEU A CD2   1 
ATOM   17367 N  N     . ASP A 1 3834 ? 183.033 132.880 148.107 1.00 69.03  ? 3834 ASP A N     1 
ATOM   17368 C  CA    . ASP A 1 3834 ? 184.404 133.277 147.801 1.00 71.33  ? 3834 ASP A CA    1 
ATOM   17369 C  C     . ASP A 1 3834 ? 185.397 132.583 148.722 1.00 73.69  ? 3834 ASP A C     1 
ATOM   17370 O  O     . ASP A 1 3834 ? 186.480 132.179 148.282 1.00 75.34  ? 3834 ASP A O     1 
ATOM   17371 C  CB    . ASP A 1 3834 ? 184.555 134.794 147.902 1.00 72.10  ? 3834 ASP A CB    1 
ATOM   17372 C  CG    . ASP A 1 3834 ? 183.662 135.534 146.932 1.00 83.37  ? 3834 ASP A CG    1 
ATOM   17373 O  OD1   . ASP A 1 3834 ? 183.579 136.776 147.027 1.00 79.87  ? 3834 ASP A OD1   1 
ATOM   17374 O  OD2   . ASP A 1 3834 ? 183.045 134.872 146.072 1.00 85.13  ? 3834 ASP A OD2   1 
ATOM   17375 N  N     . ILE A 1 3835 ? 185.052 132.440 150.003 1.00 68.04  ? 3835 ILE A N     1 
ATOM   17376 C  CA    . ILE A 1 3835 ? 185.929 131.719 150.925 1.00 66.20  ? 3835 ILE A CA    1 
ATOM   17377 C  C     . ILE A 1 3835 ? 186.106 130.276 150.467 1.00 69.44  ? 3835 ILE A C     1 
ATOM   17378 O  O     . ILE A 1 3835 ? 187.223 129.744 150.435 1.00 80.43  ? 3835 ILE A O     1 
ATOM   17379 C  CB    . ILE A 1 3835 ? 185.377 131.791 152.360 1.00 60.65  ? 3835 ILE A CB    1 
ATOM   17380 C  CG1   . ILE A 1 3835 ? 185.543 133.200 152.927 1.00 64.42  ? 3835 ILE A CG1   1 
ATOM   17381 C  CG2   . ILE A 1 3835 ? 186.073 130.775 153.251 1.00 55.78  ? 3835 ILE A CG2   1 
ATOM   17382 C  CD1   . ILE A 1 3835 ? 184.856 133.405 154.255 1.00 64.18  ? 3835 ILE A CD1   1 
ATOM   17383 N  N     . TYR A 1 3836 ? 185.001 129.625 150.097 1.00 66.17  ? 3836 TYR A N     1 
ATOM   17384 C  CA    . TYR A 1 3836 ? 185.061 128.241 149.637 1.00 67.81  ? 3836 TYR A CA    1 
ATOM   17385 C  C     . TYR A 1 3836 ? 185.867 128.118 148.349 1.00 69.83  ? 3836 TYR A C     1 
ATOM   17386 O  O     . TYR A 1 3836 ? 186.645 127.172 148.183 1.00 77.10  ? 3836 TYR A O     1 
ATOM   17387 C  CB    . TYR A 1 3836 ? 183.645 127.700 149.442 1.00 72.09  ? 3836 TYR A CB    1 
ATOM   17388 C  CG    . TYR A 1 3836 ? 183.539 126.196 149.500 1.00 63.35  ? 3836 TYR A CG    1 
ATOM   17389 C  CD1   . TYR A 1 3836 ? 184.409 125.448 150.278 1.00 67.94  ? 3836 TYR A CD1   1 
ATOM   17390 C  CD2   . TYR A 1 3836 ? 182.558 125.524 148.785 1.00 63.64  ? 3836 TYR A CD2   1 
ATOM   17391 C  CE1   . TYR A 1 3836 ? 184.313 124.073 150.334 1.00 73.55  ? 3836 TYR A CE1   1 
ATOM   17392 C  CE2   . TYR A 1 3836 ? 182.452 124.149 148.837 1.00 67.64  ? 3836 TYR A CE2   1 
ATOM   17393 C  CZ    . TYR A 1 3836 ? 183.332 123.429 149.614 1.00 71.32  ? 3836 TYR A CZ    1 
ATOM   17394 O  OH    . TYR A 1 3836 ? 183.232 122.059 149.670 1.00 74.82  ? 3836 TYR A OH    1 
ATOM   17395 N  N     . HIS A 1 3837 ? 185.685 129.062 147.423 1.00 75.55  ? 3837 HIS A N     1 
ATOM   17396 C  CA    . HIS A 1 3837 ? 186.445 129.053 146.177 1.00 79.54  ? 3837 HIS A CA    1 
ATOM   17397 C  C     . HIS A 1 3837 ? 187.935 129.218 146.443 1.00 84.40  ? 3837 HIS A C     1 
ATOM   17398 O  O     . HIS A 1 3837 ? 188.761 128.523 145.839 1.00 90.42  ? 3837 HIS A O     1 
ATOM   17399 C  CB    . HIS A 1 3837 ? 185.917 130.157 145.256 1.00 81.63  ? 3837 HIS A CB    1 
ATOM   17400 C  CG    . HIS A 1 3837 ? 186.578 130.218 143.912 1.00 85.03  ? 3837 HIS A CG    1 
ATOM   17401 N  ND1   . HIS A 1 3837 ? 187.944 130.306 143.748 1.00 87.53  ? 3837 HIS A ND1   1 
ATOM   17402 C  CD2   . HIS A 1 3837 ? 186.052 130.212 142.664 1.00 88.26  ? 3837 HIS A CD2   1 
ATOM   17403 C  CE1   . HIS A 1 3837 ? 188.231 130.352 142.460 1.00 90.62  ? 3837 HIS A CE1   1 
ATOM   17404 N  NE2   . HIS A 1 3837 ? 187.100 130.293 141.780 1.00 94.84  ? 3837 HIS A NE2   1 
ATOM   17405 N  N     . ASN A 1 3838 ? 188.299 130.134 147.343 1.00 74.61  ? 3838 ASN A N     1 
ATOM   17406 C  CA    . ASN A 1 3838 ? 189.706 130.330 147.672 1.00 75.92  ? 3838 ASN A CA    1 
ATOM   17407 C  C     . ASN A 1 3838 ? 190.295 129.088 148.324 1.00 77.37  ? 3838 ASN A C     1 
ATOM   17408 O  O     . ASN A 1 3838 ? 191.447 128.724 148.061 1.00 85.74  ? 3838 ASN A O     1 
ATOM   17409 C  CB    . ASN A 1 3838 ? 189.867 131.545 148.585 1.00 77.37  ? 3838 ASN A CB    1 
ATOM   17410 C  CG    . ASN A 1 3838 ? 191.279 131.695 149.112 1.00 77.82  ? 3838 ASN A CG    1 
ATOM   17411 O  OD1   . ASN A 1 3838 ? 191.569 131.342 150.255 1.00 80.25  ? 3838 ASN A OD1   1 
ATOM   17412 N  ND2   . ASN A 1 3838 ? 192.167 132.225 148.281 1.00 77.44  ? 3838 ASN A ND2   1 
ATOM   17413 N  N     . VAL A 1 3839 ? 189.521 128.427 149.186 1.00 64.58  ? 3839 VAL A N     1 
ATOM   17414 C  CA    . VAL A 1 3839 ? 190.010 127.221 149.846 1.00 59.30  ? 3839 VAL A CA    1 
ATOM   17415 C  C     . VAL A 1 3839 ? 190.195 126.090 148.840 1.00 66.67  ? 3839 VAL A C     1 
ATOM   17416 O  O     . VAL A 1 3839 ? 191.193 125.362 148.883 1.00 73.23  ? 3839 VAL A O     1 
ATOM   17417 C  CB    . VAL A 1 3839 ? 189.055 126.821 150.984 1.00 60.78  ? 3839 VAL A CB    1 
ATOM   17418 C  CG1   . VAL A 1 3839 ? 189.302 125.386 151.415 1.00 67.59  ? 3839 VAL A CG1   1 
ATOM   17419 C  CG2   . VAL A 1 3839 ? 189.217 127.770 152.154 1.00 68.31  ? 3839 VAL A CG2   1 
ATOM   17420 N  N     . LEU A 1 3840 ? 189.245 125.925 147.919 1.00 71.99  ? 3840 LEU A N     1 
ATOM   17421 C  CA    . LEU A 1 3840 ? 189.289 124.792 147.000 1.00 69.61  ? 3840 LEU A CA    1 
ATOM   17422 C  C     . LEU A 1 3840 ? 190.330 124.984 145.903 1.00 75.35  ? 3840 LEU A C     1 
ATOM   17423 O  O     . LEU A 1 3840 ? 191.110 124.070 145.614 1.00 79.84  ? 3840 LEU A O     1 
ATOM   17424 C  CB    . LEU A 1 3840 ? 187.907 124.565 146.386 1.00 66.82  ? 3840 LEU A CB    1 
ATOM   17425 C  CG    . LEU A 1 3840 ? 186.893 123.820 147.253 1.00 69.52  ? 3840 LEU A CG    1 
ATOM   17426 C  CD1   . LEU A 1 3840 ? 185.544 123.759 146.561 1.00 74.74  ? 3840 LEU A CD1   1 
ATOM   17427 C  CD2   . LEU A 1 3840 ? 187.394 122.426 147.581 1.00 72.55  ? 3840 LEU A CD2   1 
ATOM   17428 N  N     . TYR A 1 3841 ? 190.362 126.163 145.282 1.00 82.23  ? 3841 TYR A N     1 
ATOM   17429 C  CA    . TYR A 1 3841 ? 191.191 126.393 144.106 1.00 81.48  ? 3841 TYR A CA    1 
ATOM   17430 C  C     . TYR A 1 3841 ? 192.481 127.146 144.386 1.00 80.68  ? 3841 TYR A C     1 
ATOM   17431 O  O     . TYR A 1 3841 ? 193.493 126.862 143.743 1.00 83.92  ? 3841 TYR A O     1 
ATOM   17432 C  CB    . TYR A 1 3841 ? 190.396 127.160 143.042 1.00 81.15  ? 3841 TYR A CB    1 
ATOM   17433 C  CG    . TYR A 1 3841 ? 189.124 126.467 142.610 1.00 82.82  ? 3841 TYR A CG    1 
ATOM   17434 C  CD1   . TYR A 1 3841 ? 189.139 125.141 142.204 1.00 80.28  ? 3841 TYR A CD1   1 
ATOM   17435 C  CD2   . TYR A 1 3841 ? 187.908 127.134 142.620 1.00 83.74  ? 3841 TYR A CD2   1 
ATOM   17436 C  CE1   . TYR A 1 3841 ? 187.982 124.504 141.809 1.00 83.93  ? 3841 TYR A CE1   1 
ATOM   17437 C  CE2   . TYR A 1 3841 ? 186.744 126.504 142.229 1.00 83.21  ? 3841 TYR A CE2   1 
ATOM   17438 C  CZ    . TYR A 1 3841 ? 186.786 125.189 141.826 1.00 87.29  ? 3841 TYR A CZ    1 
ATOM   17439 O  OH    . TYR A 1 3841 ? 185.629 124.557 141.436 1.00 89.64  ? 3841 TYR A OH    1 
ATOM   17440 N  N     . GLU A 1 3842 ? 192.477 128.092 145.322 1.00 83.80  ? 3842 GLU A N     1 
ATOM   17441 C  CA    . GLU A 1 3842 ? 193.645 128.926 145.601 1.00 85.89  ? 3842 GLU A CA    1 
ATOM   17442 C  C     . GLU A 1 3842 ? 194.365 128.490 146.870 1.00 85.63  ? 3842 GLU A C     1 
ATOM   17443 O  O     . GLU A 1 3842 ? 194.856 129.325 147.634 1.00 86.70  ? 3842 GLU A O     1 
ATOM   17444 C  CB    . GLU A 1 3842 ? 193.234 130.392 145.694 1.00 87.43  ? 3842 GLU A CB    1 
ATOM   17445 C  CG    . GLU A 1 3842 ? 192.699 130.970 144.393 1.00 91.30  ? 3842 GLU A CG    1 
ATOM   17446 C  CD    . GLU A 1 3842 ? 193.798 131.502 143.495 1.00 93.98  ? 3842 GLU A CD    1 
ATOM   17447 O  OE1   . GLU A 1 3842 ? 194.009 130.926 142.407 1.00 93.60  ? 3842 GLU A OE1   1 
ATOM   17448 O  OE2   . GLU A 1 3842 ? 194.450 132.497 143.875 1.00 94.09  ? 3842 GLU A OE2   1 
ATOM   17449 N  N     . ASN A 1 3843 ? 194.443 127.183 147.118 1.00 82.10  ? 3843 ASN A N     1 
ATOM   17450 C  CA    . ASN A 1 3843 ? 195.043 126.672 148.342 1.00 83.01  ? 3843 ASN A CA    1 
ATOM   17451 C  C     . ASN A 1 3843 ? 196.528 126.421 148.117 1.00 88.54  ? 3843 ASN A C     1 
ATOM   17452 O  O     . ASN A 1 3843 ? 196.883 125.611 147.247 1.00 91.52  ? 3843 ASN A O     1 
ATOM   17453 C  CB    . ASN A 1 3843 ? 194.351 125.390 148.778 1.00 84.19  ? 3843 ASN A CB    1 
ATOM   17454 C  CG    . ASN A 1 3843 ? 194.094 125.349 150.267 1.00 85.41  ? 3843 ASN A CG    1 
ATOM   17455 O  OD1   . ASN A 1 3843 ? 193.980 126.388 150.916 1.00 83.42  ? 3843 ASN A OD1   1 
ATOM   17456 N  ND2   . ASN A 1 3843 ? 193.998 124.146 150.819 1.00 86.01  ? 3843 ASN A ND2   1 
ATOM   17457 N  N     . PRO A 1 3844 ? 197.424 127.082 148.856 1.00 96.11  ? 3844 PRO A N     1 
ATOM   17458 C  CA    . PRO A 1 3844 ? 198.858 126.793 148.702 1.00 95.55  ? 3844 PRO A CA    1 
ATOM   17459 C  C     . PRO A 1 3844 ? 199.255 125.408 149.182 1.00 95.24  ? 3844 PRO A C     1 
ATOM   17460 O  O     . PRO A 1 3844 ? 200.280 124.886 148.727 1.00 94.09  ? 3844 PRO A O     1 
ATOM   17461 C  CB    . PRO A 1 3844 ? 199.536 127.886 149.543 1.00 92.89  ? 3844 PRO A CB    1 
ATOM   17462 C  CG    . PRO A 1 3844 ? 198.466 128.909 149.812 1.00 92.53  ? 3844 PRO A CG    1 
ATOM   17463 C  CD    . PRO A 1 3844 ? 197.178 128.157 149.829 1.00 93.92  ? 3844 PRO A CD    1 
ATOM   17464 N  N     . ASN A 1 3845 ? 198.484 124.799 150.080 1.00 94.97  ? 3845 ASN A N     1 
ATOM   17465 C  CA    . ASN A 1 3845 ? 198.836 123.506 150.652 1.00 95.95  ? 3845 ASN A CA    1 
ATOM   17466 C  C     . ASN A 1 3845 ? 198.520 122.334 149.732 1.00 95.46  ? 3845 ASN A C     1 
ATOM   17467 O  O     . ASN A 1 3845 ? 198.886 121.200 150.057 1.00 98.60  ? 3845 ASN A O     1 
ATOM   17468 C  CB    . ASN A 1 3845 ? 198.119 123.313 151.992 1.00 92.22  ? 3845 ASN A CB    1 
ATOM   17469 C  CG    . ASN A 1 3845 ? 198.388 124.444 152.963 1.00 96.27  ? 3845 ASN A CG    1 
ATOM   17470 O  OD1   . ASN A 1 3845 ? 199.534 124.845 153.163 1.00 101.59 ? 3845 ASN A OD1   1 
ATOM   17471 N  ND2   . ASN A 1 3845 ? 197.332 124.962 153.574 1.00 94.81  ? 3845 ASN A ND2   1 
ATOM   17472 N  N     . LEU A 1 3846 ? 197.854 122.572 148.602 1.00 95.47  ? 3846 LEU A N     1 
ATOM   17473 C  CA    . LEU A 1 3846 ? 197.499 121.518 147.660 1.00 96.12  ? 3846 LEU A CA    1 
ATOM   17474 C  C     . LEU A 1 3846 ? 198.360 121.554 146.402 1.00 100.50 ? 3846 LEU A C     1 
ATOM   17475 O  O     . LEU A 1 3846 ? 197.925 121.097 145.339 1.00 104.82 ? 3846 LEU A O     1 
ATOM   17476 C  CB    . LEU A 1 3846 ? 196.020 121.616 147.292 1.00 95.42  ? 3846 LEU A CB    1 
ATOM   17477 C  CG    . LEU A 1 3846 ? 195.023 121.393 148.428 1.00 92.00  ? 3846 LEU A CG    1 
ATOM   17478 C  CD1   . LEU A 1 3846 ? 193.607 121.649 147.948 1.00 93.16  ? 3846 LEU A CD1   1 
ATOM   17479 C  CD2   . LEU A 1 3846 ? 195.157 119.984 148.974 1.00 95.68  ? 3846 LEU A CD2   1 
ATOM   17480 N  N     . LYS A 1 3847 ? 199.575 122.096 146.500 1.00 109.58 ? 3847 LYS A N     1 
ATOM   17481 C  CA    . LYS A 1 3847 ? 200.437 122.203 145.327 1.00 112.47 ? 3847 LYS A CA    1 
ATOM   17482 C  C     . LYS A 1 3847 ? 200.868 120.829 144.827 1.00 114.19 ? 3847 LYS A C     1 
ATOM   17483 O  O     . LYS A 1 3847 ? 200.751 120.526 143.634 1.00 115.48 ? 3847 LYS A O     1 
ATOM   17484 C  CB    . LYS A 1 3847 ? 201.656 123.067 145.650 1.00 110.53 ? 3847 LYS A CB    1 
ATOM   17485 C  CG    . LYS A 1 3847 ? 201.430 124.556 145.453 1.00 111.34 ? 3847 LYS A CG    1 
ATOM   17486 C  CD    . LYS A 1 3847 ? 201.289 124.902 143.980 1.00 110.35 ? 3847 LYS A CD    1 
ATOM   17487 C  CE    . LYS A 1 3847 ? 201.816 126.297 143.686 1.00 111.59 ? 3847 LYS A CE    1 
ATOM   17488 N  NZ    . LYS A 1 3847 ? 203.266 126.420 144.002 1.00 113.29 ? 3847 LYS A NZ    1 
ATOM   17489 N  N     . GLY A 1 3848 ? 201.365 119.981 145.724 1.00 107.80 ? 3848 GLY A N     1 
ATOM   17490 C  CA    . GLY A 1 3848 ? 201.879 118.687 145.321 1.00 107.98 ? 3848 GLY A CA    1 
ATOM   17491 C  C     . GLY A 1 3848 ? 201.105 117.503 145.861 1.00 109.20 ? 3848 GLY A C     1 
ATOM   17492 O  O     . GLY A 1 3848 ? 201.455 116.352 145.586 1.00 113.85 ? 3848 GLY A O     1 
ATOM   17493 N  N     . VAL A 1 3849 ? 200.053 117.765 146.630 1.00 102.78 ? 3849 VAL A N     1 
ATOM   17494 C  CA    . VAL A 1 3849 ? 199.254 116.694 147.213 1.00 103.50 ? 3849 VAL A CA    1 
ATOM   17495 C  C     . VAL A 1 3849 ? 198.326 116.126 146.148 1.00 105.56 ? 3849 VAL A C     1 
ATOM   17496 O  O     . VAL A 1 3849 ? 197.594 116.869 145.483 1.00 107.08 ? 3849 VAL A O     1 
ATOM   17497 C  CB    . VAL A 1 3849 ? 198.462 117.202 148.427 1.00 100.38 ? 3849 VAL A CB    1 
ATOM   17498 C  CG1   . VAL A 1 3849 ? 197.872 116.033 149.198 1.00 97.99  ? 3849 VAL A CG1   1 
ATOM   17499 C  CG2   . VAL A 1 3849 ? 199.356 118.040 149.324 1.00 102.14 ? 3849 VAL A CG2   1 
ATOM   17500 N  N     . THR A 1 3850 ? 198.355 114.803 145.983 1.00 105.20 ? 3850 THR A N     1 
ATOM   17501 C  CA    . THR A 1 3850 ? 197.519 114.123 145.006 1.00 104.82 ? 3850 THR A CA    1 
ATOM   17502 C  C     . THR A 1 3850 ? 196.532 113.140 145.617 1.00 105.49 ? 3850 THR A C     1 
ATOM   17503 O  O     . THR A 1 3850 ? 195.499 112.868 144.994 1.00 105.16 ? 3850 THR A O     1 
ATOM   17504 C  CB    . THR A 1 3850 ? 198.388 113.375 143.981 1.00 105.48 ? 3850 THR A CB    1 
ATOM   17505 O  OG1   . THR A 1 3850 ? 199.589 114.118 143.739 1.00 102.31 ? 3850 THR A OG1   1 
ATOM   17506 C  CG2   . THR A 1 3850 ? 197.640 113.203 142.667 1.00 105.43 ? 3850 THR A CG2   1 
ATOM   17507 N  N     . ASP A 1 3851 ? 196.811 112.605 146.804 1.00 107.40 ? 3851 ASP A N     1 
ATOM   17508 C  CA    . ASP A 1 3851 ? 195.895 111.669 147.443 1.00 107.49 ? 3851 ASP A CA    1 
ATOM   17509 C  C     . ASP A 1 3851 ? 194.576 112.361 147.764 1.00 109.61 ? 3851 ASP A C     1 
ATOM   17510 O  O     . ASP A 1 3851 ? 194.558 113.496 148.247 1.00 112.64 ? 3851 ASP A O     1 
ATOM   17511 C  CB    . ASP A 1 3851 ? 196.520 111.101 148.715 1.00 108.76 ? 3851 ASP A CB    1 
ATOM   17512 C  CG    . ASP A 1 3851 ? 195.697 109.980 149.319 1.00 108.95 ? 3851 ASP A CG    1 
ATOM   17513 O  OD1   . ASP A 1 3851 ? 194.775 109.481 148.640 1.00 110.06 ? 3851 ASP A OD1   1 
ATOM   17514 O  OD2   . ASP A 1 3851 ? 195.971 109.598 150.476 1.00 108.99 ? 3851 ASP A OD2   1 
ATOM   17515 N  N     . HIS A 1 3852 ? 193.467 111.668 147.498 1.00 104.80 ? 3852 HIS A N     1 
ATOM   17516 C  CA    . HIS A 1 3852 ? 192.154 112.289 147.643 1.00 102.63 ? 3852 HIS A CA    1 
ATOM   17517 C  C     . HIS A 1 3852 ? 191.802 112.531 149.106 1.00 101.40 ? 3852 HIS A C     1 
ATOM   17518 O  O     . HIS A 1 3852 ? 191.273 113.593 149.452 1.00 104.36 ? 3852 HIS A O     1 
ATOM   17519 C  CB    . HIS A 1 3852 ? 191.094 111.424 146.964 1.00 102.70 ? 3852 HIS A CB    1 
ATOM   17520 C  CG    . HIS A 1 3852 ? 191.234 111.360 145.475 1.00 107.44 ? 3852 HIS A CG    1 
ATOM   17521 N  ND1   . HIS A 1 3852 ? 191.373 112.486 144.692 1.00 106.39 ? 3852 HIS A ND1   1 
ATOM   17522 C  CD2   . HIS A 1 3852 ? 191.264 110.306 144.626 1.00 106.64 ? 3852 HIS A CD2   1 
ATOM   17523 C  CE1   . HIS A 1 3852 ? 191.478 112.128 143.425 1.00 103.85 ? 3852 HIS A CE1   1 
ATOM   17524 N  NE2   . HIS A 1 3852 ? 191.414 110.811 143.357 1.00 107.67 ? 3852 HIS A NE2   1 
ATOM   17525 N  N     . THR A 1 3853 ? 192.079 111.560 149.980 1.00 95.02  ? 3853 THR A N     1 
ATOM   17526 C  CA    . THR A 1 3853 ? 191.768 111.735 151.397 1.00 98.58  ? 3853 THR A CA    1 
ATOM   17527 C  C     . THR A 1 3853 ? 192.622 112.832 152.022 1.00 102.45 ? 3853 THR A C     1 
ATOM   17528 O  O     . THR A 1 3853 ? 192.120 113.650 152.806 1.00 102.98 ? 3853 THR A O     1 
ATOM   17529 C  CB    . THR A 1 3853 ? 191.963 110.416 152.144 1.00 97.22  ? 3853 THR A CB    1 
ATOM   17530 O  OG1   . THR A 1 3853 ? 191.330 109.356 151.417 1.00 97.60  ? 3853 THR A OG1   1 
ATOM   17531 C  CG2   . THR A 1 3853 ? 191.358 110.500 153.536 1.00 97.25  ? 3853 THR A CG2   1 
ATOM   17532 N  N     . GLN A 1 3854 ? 193.916 112.861 151.693 1.00 96.96  ? 3854 GLN A N     1 
ATOM   17533 C  CA    . GLN A 1 3854 ? 194.787 113.914 152.202 1.00 93.34  ? 3854 GLN A CA    1 
ATOM   17534 C  C     . GLN A 1 3854 ? 194.336 115.282 151.711 1.00 96.47  ? 3854 GLN A C     1 
ATOM   17535 O  O     . GLN A 1 3854 ? 194.316 116.253 152.480 1.00 99.13  ? 3854 GLN A O     1 
ATOM   17536 C  CB    . GLN A 1 3854 ? 196.232 113.643 151.783 1.00 93.78  ? 3854 GLN A CB    1 
ATOM   17537 C  CG    . GLN A 1 3854 ? 197.276 114.217 152.721 1.00 98.78  ? 3854 GLN A CG    1 
ATOM   17538 C  CD    . GLN A 1 3854 ? 198.678 114.120 152.155 1.00 101.99 ? 3854 GLN A CD    1 
ATOM   17539 O  OE1   . GLN A 1 3854 ? 199.050 113.111 151.556 1.00 99.19  ? 3854 GLN A OE1   1 
ATOM   17540 N  NE2   . GLN A 1 3854 ? 199.465 115.173 152.340 1.00 100.49 ? 3854 GLN A NE2   1 
ATOM   17541 N  N     . ARG A 1 3855 ? 193.968 115.377 150.431 1.00 86.11  ? 3855 ARG A N     1 
ATOM   17542 C  CA    . ARG A 1 3855 ? 193.474 116.640 149.897 1.00 79.04  ? 3855 ARG A CA    1 
ATOM   17543 C  C     . ARG A 1 3855 ? 192.188 117.064 150.591 1.00 80.45  ? 3855 ARG A C     1 
ATOM   17544 O  O     . ARG A 1 3855 ? 191.997 118.248 150.881 1.00 87.70  ? 3855 ARG A O     1 
ATOM   17545 C  CB    . ARG A 1 3855 ? 193.262 116.530 148.387 1.00 80.06  ? 3855 ARG A CB    1 
ATOM   17546 C  CG    . ARG A 1 3855 ? 194.546 116.595 147.579 1.00 83.41  ? 3855 ARG A CG    1 
ATOM   17547 C  CD    . ARG A 1 3855 ? 194.266 116.598 146.086 1.00 88.07  ? 3855 ARG A CD    1 
ATOM   17548 N  NE    . ARG A 1 3855 ? 193.538 117.789 145.663 1.00 87.75  ? 3855 ARG A NE    1 
ATOM   17549 C  CZ    . ARG A 1 3855 ? 194.035 118.725 144.867 1.00 85.67  ? 3855 ARG A CZ    1 
ATOM   17550 N  NH1   . ARG A 1 3855 ? 195.265 118.643 144.388 1.00 81.51  ? 3855 ARG A NH1   1 
ATOM   17551 N  NH2   . ARG A 1 3855 ? 193.279 119.770 144.543 1.00 86.23  ? 3855 ARG A NH2   1 
ATOM   17552 N  N     . LEU A 1 3856 ? 191.294 116.113 150.871 1.00 81.90  ? 3856 LEU A N     1 
ATOM   17553 C  CA    . LEU A 1 3856 ? 190.050 116.447 151.559 1.00 83.19  ? 3856 LEU A CA    1 
ATOM   17554 C  C     . LEU A 1 3856 ? 190.314 116.956 152.972 1.00 83.49  ? 3856 LEU A C     1 
ATOM   17555 O  O     . LEU A 1 3856 ? 189.696 117.933 153.415 1.00 80.78  ? 3856 LEU A O     1 
ATOM   17556 C  CB    . LEU A 1 3856 ? 189.127 115.230 151.590 1.00 82.88  ? 3856 LEU A CB    1 
ATOM   17557 C  CG    . LEU A 1 3856 ? 187.954 115.288 152.569 1.00 84.63  ? 3856 LEU A CG    1 
ATOM   17558 C  CD1   . LEU A 1 3856 ? 186.962 116.363 152.158 1.00 82.80  ? 3856 LEU A CD1   1 
ATOM   17559 C  CD2   . LEU A 1 3856 ? 187.271 113.934 152.670 1.00 87.89  ? 3856 LEU A CD2   1 
ATOM   17560 N  N     . SER A 1 3857 ? 191.225 116.303 153.698 1.00 84.17  ? 3857 SER A N     1 
ATOM   17561 C  CA    . SER A 1 3857 ? 191.549 116.758 155.048 1.00 83.41  ? 3857 SER A CA    1 
ATOM   17562 C  C     . SER A 1 3857 ? 192.179 118.146 155.025 1.00 86.77  ? 3857 SER A C     1 
ATOM   17563 O  O     . SER A 1 3857 ? 191.836 119.012 155.846 1.00 92.69  ? 3857 SER A O     1 
ATOM   17564 C  CB    . SER A 1 3857 ? 192.481 115.758 155.730 1.00 82.95  ? 3857 SER A CB    1 
ATOM   17565 O  OG    . SER A 1 3857 ? 193.765 115.774 155.131 1.00 87.47  ? 3857 SER A OG    1 
ATOM   17566 N  N     . ILE A 1 3858 ? 193.104 118.376 154.089 1.00 74.26  ? 3858 ILE A N     1 
ATOM   17567 C  CA    . ILE A 1 3858 ? 193.721 119.691 153.957 1.00 68.78  ? 3858 ILE A CA    1 
ATOM   17568 C  C     . ILE A 1 3858 ? 192.668 120.736 153.620 1.00 79.04  ? 3858 ILE A C     1 
ATOM   17569 O  O     . ILE A 1 3858 ? 192.689 121.853 154.148 1.00 80.38  ? 3858 ILE A O     1 
ATOM   17570 C  CB    . ILE A 1 3858 ? 194.842 119.652 152.902 1.00 70.44  ? 3858 ILE A CB    1 
ATOM   17571 C  CG1   . ILE A 1 3858 ? 196.068 118.924 153.452 1.00 77.92  ? 3858 ILE A CG1   1 
ATOM   17572 C  CG2   . ILE A 1 3858 ? 195.221 121.057 152.467 1.00 76.67  ? 3858 ILE A CG2   1 
ATOM   17573 C  CD1   . ILE A 1 3858 ? 197.171 118.740 152.434 1.00 77.73  ? 3858 ILE A CD1   1 
ATOM   17574 N  N     . ILE A 1 3859 ? 191.726 120.387 152.740 1.00 79.89  ? 3859 ILE A N     1 
ATOM   17575 C  CA    . ILE A 1 3859 ? 190.671 121.317 152.354 1.00 68.21  ? 3859 ILE A CA    1 
ATOM   17576 C  C     . ILE A 1 3859 ? 189.804 121.670 153.553 1.00 69.00  ? 3859 ILE A C     1 
ATOM   17577 O  O     . ILE A 1 3859 ? 189.443 122.832 153.746 1.00 79.16  ? 3859 ILE A O     1 
ATOM   17578 C  CB    . ILE A 1 3859 ? 189.836 120.730 151.201 1.00 69.58  ? 3859 ILE A CB    1 
ATOM   17579 C  CG1   . ILE A 1 3859 ? 190.576 120.889 149.873 1.00 71.79  ? 3859 ILE A CG1   1 
ATOM   17580 C  CG2   . ILE A 1 3859 ? 188.476 121.401 151.123 1.00 72.04  ? 3859 ILE A CG2   1 
ATOM   17581 C  CD1   . ILE A 1 3859 ? 189.986 120.071 148.751 1.00 72.99  ? 3859 ILE A CD1   1 
ATOM   17582 N  N     . THR A 1 3860 ? 189.457 120.681 154.378 1.00 62.63  ? 3860 THR A N     1 
ATOM   17583 C  CA    . THR A 1 3860 ? 188.640 120.960 155.558 1.00 65.63  ? 3860 THR A CA    1 
ATOM   17584 C  C     . THR A 1 3860 ? 189.369 121.883 156.531 1.00 66.51  ? 3860 THR A C     1 
ATOM   17585 O  O     . THR A 1 3860 ? 188.809 122.887 157.005 1.00 72.51  ? 3860 THR A O     1 
ATOM   17586 C  CB    . THR A 1 3860 ? 188.254 119.653 156.250 1.00 63.42  ? 3860 THR A CB    1 
ATOM   17587 O  OG1   . THR A 1 3860 ? 187.547 118.813 155.330 1.00 77.15  ? 3860 THR A OG1   1 
ATOM   17588 C  CG2   . THR A 1 3860 ? 187.371 119.930 157.455 1.00 64.72  ? 3860 THR A CG2   1 
ATOM   17589 N  N     . LYS A 1 3861 ? 190.627 121.555 156.844 1.00 68.67  ? 3861 LYS A N     1 
ATOM   17590 C  CA    . LYS A 1 3861 ? 191.388 122.375 157.783 1.00 69.57  ? 3861 LYS A CA    1 
ATOM   17591 C  C     . LYS A 1 3861 ? 191.553 123.796 157.257 1.00 73.58  ? 3861 LYS A C     1 
ATOM   17592 O  O     . LYS A 1 3861 ? 191.361 124.774 157.993 1.00 76.20  ? 3861 LYS A O     1 
ATOM   17593 C  CB    . LYS A 1 3861 ? 192.751 121.736 158.050 1.00 70.05  ? 3861 LYS A CB    1 
ATOM   17594 C  CG    . LYS A 1 3861 ? 192.803 120.887 159.311 1.00 71.88  ? 3861 LYS A CG    1 
ATOM   17595 C  CD    . LYS A 1 3861 ? 194.190 120.299 159.535 1.00 75.17  ? 3861 LYS A CD    1 
ATOM   17596 C  CE    . LYS A 1 3861 ? 195.290 121.303 159.221 1.00 73.31  ? 3861 LYS A CE    1 
ATOM   17597 N  NZ    . LYS A 1 3861 ? 195.247 122.483 160.127 1.00 73.71  ? 3861 LYS A NZ    1 
ATOM   17598 N  N     . ASP A 1 3862 ? 191.891 123.929 155.973 1.00 76.70  ? 3862 ASP A N     1 
ATOM   17599 C  CA    . ASP A 1 3862 ? 192.073 125.248 155.389 1.00 74.52  ? 3862 ASP A CA    1 
ATOM   17600 C  C     . ASP A 1 3862 ? 190.753 125.993 155.270 1.00 74.98  ? 3862 ASP A C     1 
ATOM   17601 O  O     . ASP A 1 3862 ? 190.737 127.221 155.347 1.00 76.15  ? 3862 ASP A O     1 
ATOM   17602 C  CB    . ASP A 1 3862 ? 192.751 125.125 154.027 1.00 77.49  ? 3862 ASP A CB    1 
ATOM   17603 C  CG    . ASP A 1 3862 ? 194.255 124.994 154.143 1.00 84.18  ? 3862 ASP A CG    1 
ATOM   17604 O  OD1   . ASP A 1 3862 ? 194.767 125.026 155.281 1.00 79.58  ? 3862 ASP A OD1   1 
ATOM   17605 O  OD2   . ASP A 1 3862 ? 194.927 124.852 153.101 1.00 89.56  ? 3862 ASP A OD2   1 
ATOM   17606 N  N     . LEU A 1 3863 ? 189.641 125.278 155.099 1.00 61.81  ? 3863 LEU A N     1 
ATOM   17607 C  CA    . LEU A 1 3863 ? 188.337 125.927 155.099 1.00 54.31  ? 3863 LEU A CA    1 
ATOM   17608 C  C     . LEU A 1 3863 ? 188.064 126.578 156.443 1.00 55.76  ? 3863 LEU A C     1 
ATOM   17609 O  O     . LEU A 1 3863 ? 187.689 127.754 156.511 1.00 64.61  ? 3863 LEU A O     1 
ATOM   17610 C  CB    . LEU A 1 3863 ? 187.244 124.912 154.769 1.00 56.59  ? 3863 LEU A CB    1 
ATOM   17611 C  CG    . LEU A 1 3863 ? 185.833 125.343 155.168 1.00 58.67  ? 3863 LEU A CG    1 
ATOM   17612 C  CD1   . LEU A 1 3863 ? 185.308 126.418 154.232 1.00 65.52  ? 3863 LEU A CD1   1 
ATOM   17613 C  CD2   . LEU A 1 3863 ? 184.898 124.150 155.212 1.00 57.72  ? 3863 LEU A CD2   1 
ATOM   17614 N  N     . PHE A 1 3864 ? 188.270 125.830 157.528 1.00 57.15  ? 3864 PHE A N     1 
ATOM   17615 C  CA    . PHE A 1 3864 ? 188.075 126.413 158.854 1.00 56.63  ? 3864 PHE A CA    1 
ATOM   17616 C  C     . PHE A 1 3864 ? 189.009 127.600 159.070 1.00 57.39  ? 3864 PHE A C     1 
ATOM   17617 O  O     . PHE A 1 3864 ? 188.582 128.674 159.524 1.00 56.73  ? 3864 PHE A O     1 
ATOM   17618 C  CB    . PHE A 1 3864 ? 188.288 125.353 159.934 1.00 61.90  ? 3864 PHE A CB    1 
ATOM   17619 C  CG    . PHE A 1 3864 ? 187.071 124.523 160.215 1.00 58.76  ? 3864 PHE A CG    1 
ATOM   17620 C  CD1   . PHE A 1 3864 ? 186.036 125.029 160.980 1.00 57.50  ? 3864 PHE A CD1   1 
ATOM   17621 C  CD2   . PHE A 1 3864 ? 186.962 123.238 159.717 1.00 62.58  ? 3864 PHE A CD2   1 
ATOM   17622 C  CE1   . PHE A 1 3864 ? 184.916 124.269 161.242 1.00 61.19  ? 3864 PHE A CE1   1 
ATOM   17623 C  CE2   . PHE A 1 3864 ? 185.843 122.473 159.976 1.00 60.47  ? 3864 PHE A CE2   1 
ATOM   17624 C  CZ    . PHE A 1 3864 ? 184.819 122.990 160.739 1.00 60.11  ? 3864 PHE A CZ    1 
ATOM   17625 N  N     . GLN A 1 3865 ? 190.287 127.431 158.719 1.00 69.39  ? 3865 GLN A N     1 
ATOM   17626 C  CA    . GLN A 1 3865 ? 191.269 128.484 158.956 1.00 63.33  ? 3865 GLN A CA    1 
ATOM   17627 C  C     . GLN A 1 3865 ? 190.936 129.747 158.169 1.00 69.96  ? 3865 GLN A C     1 
ATOM   17628 O  O     . GLN A 1 3865 ? 190.953 130.853 158.718 1.00 72.19  ? 3865 GLN A O     1 
ATOM   17629 C  CB    . GLN A 1 3865 ? 192.668 127.981 158.600 1.00 64.20  ? 3865 GLN A CB    1 
ATOM   17630 C  CG    . GLN A 1 3865 ? 193.774 128.979 158.881 1.00 65.71  ? 3865 GLN A CG    1 
ATOM   17631 C  CD    . GLN A 1 3865 ? 193.946 129.254 160.360 1.00 69.75  ? 3865 GLN A CD    1 
ATOM   17632 O  OE1   . GLN A 1 3865 ? 194.461 128.419 161.102 1.00 75.13  ? 3865 GLN A OE1   1 
ATOM   17633 N  NE2   . GLN A 1 3865 ? 193.514 130.430 160.797 1.00 72.56  ? 3865 GLN A NE2   1 
ATOM   17634 N  N     . VAL A 1 3866 ? 190.622 129.600 156.880 1.00 60.64  ? 3866 VAL A N     1 
ATOM   17635 C  CA    . VAL A 1 3866 ? 190.347 130.758 156.036 1.00 44.42  ? 3866 VAL A CA    1 
ATOM   17636 C  C     . VAL A 1 3866 ? 189.037 131.419 156.439 1.00 49.71  ? 3866 VAL A C     1 
ATOM   17637 O  O     . VAL A 1 3866 ? 188.919 132.649 156.410 1.00 66.24  ? 3866 VAL A O     1 
ATOM   17638 C  CB    . VAL A 1 3866 ? 190.350 130.349 154.552 1.00 46.22  ? 3866 VAL A CB    1 
ATOM   17639 C  CG1   . VAL A 1 3866 ? 189.848 131.486 153.681 1.00 50.44  ? 3866 VAL A CG1   1 
ATOM   17640 C  CG2   . VAL A 1 3866 ? 191.749 129.946 154.124 1.00 56.22  ? 3866 VAL A CG2   1 
ATOM   17641 N  N     . ALA A 1 3867 ? 188.030 130.626 156.817 1.00 52.00  ? 3867 ALA A N     1 
ATOM   17642 C  CA    . ALA A 1 3867 ? 186.781 131.213 157.285 1.00 50.44  ? 3867 ALA A CA    1 
ATOM   17643 C  C     . ALA A 1 3867 ? 187.021 132.084 158.509 1.00 56.24  ? 3867 ALA A C     1 
ATOM   17644 O  O     . ALA A 1 3867 ? 186.555 133.229 158.573 1.00 65.56  ? 3867 ALA A O     1 
ATOM   17645 C  CB    . ALA A 1 3867 ? 185.765 130.115 157.592 1.00 51.62  ? 3867 ALA A CB    1 
ATOM   17646 N  N     . PHE A 1 3868 ? 187.780 131.570 159.481 1.00 57.32  ? 3868 PHE A N     1 
ATOM   17647 C  CA    . PHE A 1 3868 ? 188.077 132.379 160.659 1.00 50.36  ? 3868 PHE A CA    1 
ATOM   17648 C  C     . PHE A 1 3868 ? 188.898 133.610 160.293 1.00 53.83  ? 3868 PHE A C     1 
ATOM   17649 O  O     . PHE A 1 3868 ? 188.636 134.711 160.787 1.00 62.26  ? 3868 PHE A O     1 
ATOM   17650 C  CB    . PHE A 1 3868 ? 188.805 131.551 161.715 1.00 53.83  ? 3868 PHE A CB    1 
ATOM   17651 C  CG    . PHE A 1 3868 ? 189.233 132.356 162.906 1.00 57.56  ? 3868 PHE A CG    1 
ATOM   17652 C  CD1   . PHE A 1 3868 ? 188.309 132.760 163.852 1.00 58.04  ? 3868 PHE A CD1   1 
ATOM   17653 C  CD2   . PHE A 1 3868 ? 190.555 132.730 163.067 1.00 57.66  ? 3868 PHE A CD2   1 
ATOM   17654 C  CE1   . PHE A 1 3868 ? 188.696 133.509 164.941 1.00 51.99  ? 3868 PHE A CE1   1 
ATOM   17655 C  CE2   . PHE A 1 3868 ? 190.948 133.479 164.154 1.00 55.02  ? 3868 PHE A CE2   1 
ATOM   17656 C  CZ    . PHE A 1 3868 ? 190.017 133.870 165.091 1.00 54.16  ? 3868 PHE A CZ    1 
ATOM   17657 N  N     . ASN A 1 3869 ? 189.901 133.443 159.428 1.00 56.78  ? 3869 ASN A N     1 
ATOM   17658 C  CA    . ASN A 1 3869 ? 190.786 134.555 159.096 1.00 52.92  ? 3869 ASN A CA    1 
ATOM   17659 C  C     . ASN A 1 3869 ? 190.028 135.676 158.397 1.00 58.51  ? 3869 ASN A C     1 
ATOM   17660 O  O     . ASN A 1 3869 ? 190.225 136.858 158.700 1.00 65.75  ? 3869 ASN A O     1 
ATOM   17661 C  CB    . ASN A 1 3869 ? 191.940 134.064 158.221 1.00 54.18  ? 3869 ASN A CB    1 
ATOM   17662 C  CG    . ASN A 1 3869 ? 192.892 133.158 158.969 1.00 65.37  ? 3869 ASN A CG    1 
ATOM   17663 O  OD1   . ASN A 1 3869 ? 192.655 132.811 160.126 1.00 69.95  ? 3869 ASN A OD1   1 
ATOM   17664 N  ND2   . ASN A 1 3869 ? 193.979 132.769 158.314 1.00 64.30  ? 3869 ASN A ND2   1 
ATOM   17665 N  N     . ARG A 1 3870 ? 189.155 135.324 157.452 1.00 56.45  ? 3870 ARG A N     1 
ATOM   17666 C  CA    . ARG A 1 3870 ? 188.431 136.343 156.703 1.00 50.55  ? 3870 ARG A CA    1 
ATOM   17667 C  C     . ARG A 1 3870 ? 187.330 136.975 157.544 1.00 61.75  ? 3870 ARG A C     1 
ATOM   17668 O  O     . ARG A 1 3870 ? 187.117 138.191 157.478 1.00 68.03  ? 3870 ARG A O     1 
ATOM   17669 C  CB    . ARG A 1 3870 ? 187.856 135.743 155.422 1.00 48.03  ? 3870 ARG A CB    1 
ATOM   17670 C  CG    . ARG A 1 3870 ? 188.912 135.363 154.400 1.00 59.09  ? 3870 ARG A CG    1 
ATOM   17671 C  CD    . ARG A 1 3870 ? 188.409 135.560 152.982 1.00 61.92  ? 3870 ARG A CD    1 
ATOM   17672 N  NE    . ARG A 1 3870 ? 189.382 135.109 151.996 1.00 60.22  ? 3870 ARG A NE    1 
ATOM   17673 C  CZ    . ARG A 1 3870 ? 189.213 135.195 150.684 1.00 67.56  ? 3870 ARG A CZ    1 
ATOM   17674 N  NH1   . ARG A 1 3870 ? 188.114 135.712 150.162 1.00 70.75  ? 3870 ARG A NH1   1 
ATOM   17675 N  NH2   . ARG A 1 3870 ? 190.171 134.751 149.876 1.00 66.81  ? 3870 ARG A NH2   1 
ATOM   17676 N  N     . VAL A 1 3871 ? 186.614 136.172 158.334 1.00 64.56  ? 3871 VAL A N     1 
ATOM   17677 C  CA    . VAL A 1 3871 ? 185.522 136.725 159.128 1.00 52.70  ? 3871 VAL A CA    1 
ATOM   17678 C  C     . VAL A 1 3871 ? 186.058 137.591 160.263 1.00 56.13  ? 3871 VAL A C     1 
ATOM   17679 O  O     . VAL A 1 3871 ? 185.545 138.686 160.518 1.00 66.41  ? 3871 VAL A O     1 
ATOM   17680 C  CB    . VAL A 1 3871 ? 184.618 135.596 159.650 1.00 47.00  ? 3871 VAL A CB    1 
ATOM   17681 C  CG1   . VAL A 1 3871 ? 183.684 136.122 160.718 1.00 51.72  ? 3871 VAL A CG1   1 
ATOM   17682 C  CG2   . VAL A 1 3871 ? 183.824 134.999 158.506 1.00 55.72  ? 3871 VAL A CG2   1 
ATOM   17683 N  N     . ALA A 1 3872 ? 187.101 137.125 160.954 1.00 55.87  ? 3872 ALA A N     1 
ATOM   17684 C  CA    . ALA A 1 3872 ? 187.582 137.838 162.132 1.00 53.19  ? 3872 ALA A CA    1 
ATOM   17685 C  C     . ALA A 1 3872 ? 188.364 139.099 161.787 1.00 60.77  ? 3872 ALA A C     1 
ATOM   17686 O  O     . ALA A 1 3872 ? 188.617 139.913 162.680 1.00 65.16  ? 3872 ALA A O     1 
ATOM   17687 C  CB    . ALA A 1 3872 ? 188.446 136.918 162.993 1.00 60.25  ? 3872 ALA A CB    1 
ATOM   17688 N  N     . ARG A 1 3873 ? 188.759 139.280 160.525 1.00 68.49  ? 3873 ARG A N     1 
ATOM   17689 C  CA    . ARG A 1 3873 ? 189.470 140.497 160.149 1.00 65.05  ? 3873 ARG A CA    1 
ATOM   17690 C  C     . ARG A 1 3873 ? 188.580 141.728 160.213 1.00 62.98  ? 3873 ARG A C     1 
ATOM   17691 O  O     . ARG A 1 3873 ? 189.091 142.843 160.356 1.00 65.58  ? 3873 ARG A O     1 
ATOM   17692 C  CB    . ARG A 1 3873 ? 190.065 140.353 158.748 1.00 64.86  ? 3873 ARG A CB    1 
ATOM   17693 C  CG    . ARG A 1 3873 ? 191.511 139.892 158.744 1.00 67.99  ? 3873 ARG A CG    1 
ATOM   17694 C  CD    . ARG A 1 3873 ? 192.338 140.731 159.703 1.00 68.01  ? 3873 ARG A CD    1 
ATOM   17695 N  NE    . ARG A 1 3873 ? 193.743 140.343 159.720 1.00 67.33  ? 3873 ARG A NE    1 
ATOM   17696 C  CZ    . ARG A 1 3873 ? 194.624 140.770 160.615 1.00 72.20  ? 3873 ARG A CZ    1 
ATOM   17697 N  NH1   . ARG A 1 3873 ? 194.276 141.600 161.584 1.00 69.77  ? 3873 ARG A NH1   1 
ATOM   17698 N  NH2   . ARG A 1 3873 ? 195.885 140.357 160.533 1.00 72.41  ? 3873 ARG A NH2   1 
ATOM   17699 N  N     . GLY A 1 3874 ? 187.267 141.554 160.108 1.00 50.18  ? 3874 GLY A N     1 
ATOM   17700 C  CA    . GLY A 1 3874 ? 186.340 142.656 160.259 1.00 58.33  ? 3874 GLY A CA    1 
ATOM   17701 C  C     . GLY A 1 3874 ? 185.463 142.470 161.476 1.00 58.24  ? 3874 GLY A C     1 
ATOM   17702 O  O     . GLY A 1 3874 ? 184.261 142.747 161.441 1.00 59.17  ? 3874 GLY A O     1 
ATOM   17703 N  N     . MET A 1 3875 ? 186.063 141.998 162.564 1.00 61.42  ? 3875 MET A N     1 
ATOM   17704 C  CA    . MET A 1 3875 ? 185.331 141.613 163.758 1.00 56.67  ? 3875 MET A CA    1 
ATOM   17705 C  C     . MET A 1 3875 ? 186.106 142.061 164.989 1.00 60.12  ? 3875 MET A C     1 
ATOM   17706 O  O     . MET A 1 3875 ? 187.328 141.911 165.058 1.00 70.90  ? 3875 MET A O     1 
ATOM   17707 C  CB    . MET A 1 3875 ? 185.106 140.097 163.770 1.00 58.56  ? 3875 MET A CB    1 
ATOM   17708 C  CG    . MET A 1 3875 ? 183.670 139.673 163.970 1.00 69.16  ? 3875 MET A CG    1 
ATOM   17709 S  SD    . MET A 1 3875 ? 183.496 137.884 163.941 1.00 76.58  ? 3875 MET A SD    1 
ATOM   17710 C  CE    . MET A 1 3875 ? 183.579 137.517 165.682 1.00 71.16  ? 3875 MET A CE    1 
ATOM   17711 N  N     . LEU A 1 3876 ? 185.385 142.617 165.960 1.00 56.76  ? 3876 LEU A N     1 
ATOM   17712 C  CA    . LEU A 1 3876 ? 186.020 143.154 167.156 1.00 63.42  ? 3876 LEU A CA    1 
ATOM   17713 C  C     . LEU A 1 3876 ? 186.729 142.052 167.937 1.00 72.57  ? 3876 LEU A C     1 
ATOM   17714 O  O     . LEU A 1 3876 ? 186.282 140.903 167.980 1.00 84.07  ? 3876 LEU A O     1 
ATOM   17715 C  CB    . LEU A 1 3876 ? 184.988 143.844 168.046 1.00 62.66  ? 3876 LEU A CB    1 
ATOM   17716 C  CG    . LEU A 1 3876 ? 184.253 145.044 167.447 1.00 62.21  ? 3876 LEU A CG    1 
ATOM   17717 C  CD1   . LEU A 1 3876 ? 183.182 145.539 168.403 1.00 68.94  ? 3876 LEU A CD1   1 
ATOM   17718 C  CD2   . LEU A 1 3876 ? 185.228 146.158 167.113 1.00 64.86  ? 3876 LEU A CD2   1 
ATOM   17719 N  N     . HIS A 1 3877 ? 187.849 142.420 168.568 1.00 65.16  ? 3877 HIS A N     1 
ATOM   17720 C  CA    . HIS A 1 3877 ? 188.702 141.419 169.201 1.00 71.60  ? 3877 HIS A CA    1 
ATOM   17721 C  C     . HIS A 1 3877 ? 188.007 140.722 170.361 1.00 76.51  ? 3877 HIS A C     1 
ATOM   17722 O  O     . HIS A 1 3877 ? 188.300 139.555 170.644 1.00 83.40  ? 3877 HIS A O     1 
ATOM   17723 C  CB    . HIS A 1 3877 ? 190.005 142.052 169.684 1.00 70.37  ? 3877 HIS A CB    1 
ATOM   17724 C  CG    . HIS A 1 3877 ? 191.103 141.061 169.905 1.00 75.25  ? 3877 HIS A CG    1 
ATOM   17725 N  ND1   . HIS A 1 3877 ? 191.291 140.416 171.109 1.00 75.47  ? 3877 HIS A ND1   1 
ATOM   17726 C  CD2   . HIS A 1 3877 ? 192.066 140.598 169.075 1.00 75.46  ? 3877 HIS A CD2   1 
ATOM   17727 C  CE1   . HIS A 1 3877 ? 192.325 139.600 171.010 1.00 77.25  ? 3877 HIS A CE1   1 
ATOM   17728 N  NE2   . HIS A 1 3877 ? 192.813 139.691 169.787 1.00 81.15  ? 3877 HIS A NE2   1 
ATOM   17729 N  N     . GLN A 1 3878 ? 187.096 141.409 171.049 1.00 70.84  ? 3878 GLN A N     1 
ATOM   17730 C  CA    . GLN A 1 3878 ? 186.361 140.759 172.125 1.00 73.08  ? 3878 GLN A CA    1 
ATOM   17731 C  C     . GLN A 1 3878 ? 185.364 139.733 171.609 1.00 77.96  ? 3878 GLN A C     1 
ATOM   17732 O  O     . GLN A 1 3878 ? 184.807 138.976 172.412 1.00 80.44  ? 3878 GLN A O     1 
ATOM   17733 C  CB    . GLN A 1 3878 ? 185.637 141.798 172.986 1.00 78.17  ? 3878 GLN A CB    1 
ATOM   17734 C  CG    . GLN A 1 3878 ? 184.466 142.480 172.305 1.00 75.85  ? 3878 GLN A CG    1 
ATOM   17735 C  CD    . GLN A 1 3878 ? 184.753 143.925 171.954 1.00 81.76  ? 3878 GLN A CD    1 
ATOM   17736 O  OE1   . GLN A 1 3878 ? 185.909 144.339 171.870 1.00 87.68  ? 3878 GLN A OE1   1 
ATOM   17737 N  NE2   . GLN A 1 3878 ? 183.698 144.706 171.755 1.00 78.81  ? 3878 GLN A NE2   1 
ATOM   17738 N  N     . ASP A 1 3879 ? 185.129 139.689 170.297 1.00 66.84  ? 3879 ASP A N     1 
ATOM   17739 C  CA    . ASP A 1 3879 ? 184.239 138.712 169.691 1.00 65.29  ? 3879 ASP A CA    1 
ATOM   17740 C  C     . ASP A 1 3879 ? 184.974 137.593 168.965 1.00 66.11  ? 3879 ASP A C     1 
ATOM   17741 O  O     . ASP A 1 3879 ? 184.328 136.626 168.548 1.00 74.80  ? 3879 ASP A O     1 
ATOM   17742 C  CB    . ASP A 1 3879 ? 183.281 139.402 168.711 1.00 61.55  ? 3879 ASP A CB    1 
ATOM   17743 C  CG    . ASP A 1 3879 ? 182.489 140.518 169.357 1.00 74.46  ? 3879 ASP A CG    1 
ATOM   17744 O  OD1   . ASP A 1 3879 ? 181.980 140.313 170.477 1.00 80.53  ? 3879 ASP A OD1   1 
ATOM   17745 O  OD2   . ASP A 1 3879 ? 182.371 141.599 168.745 1.00 74.22  ? 3879 ASP A OD2   1 
ATOM   17746 N  N     . HIS A 1 3880 ? 186.298 137.686 168.817 1.00 60.40  ? 3880 HIS A N     1 
ATOM   17747 C  CA    . HIS A 1 3880 ? 187.038 136.638 168.119 1.00 62.75  ? 3880 HIS A CA    1 
ATOM   17748 C  C     . HIS A 1 3880 ? 186.896 135.298 168.826 1.00 67.93  ? 3880 HIS A C     1 
ATOM   17749 O  O     . HIS A 1 3880 ? 186.768 134.254 168.175 1.00 74.58  ? 3880 HIS A O     1 
ATOM   17750 C  CB    . HIS A 1 3880 ? 188.514 137.016 167.999 1.00 60.69  ? 3880 HIS A CB    1 
ATOM   17751 C  CG    . HIS A 1 3880 ? 188.784 138.098 167.002 1.00 62.97  ? 3880 HIS A CG    1 
ATOM   17752 N  ND1   . HIS A 1 3880 ? 190.049 138.374 166.529 1.00 67.29  ? 3880 HIS A ND1   1 
ATOM   17753 C  CD2   . HIS A 1 3880 ? 187.954 138.971 166.385 1.00 65.71  ? 3880 HIS A CD2   1 
ATOM   17754 C  CE1   . HIS A 1 3880 ? 189.986 139.371 165.665 1.00 68.12  ? 3880 HIS A CE1   1 
ATOM   17755 N  NE2   . HIS A 1 3880 ? 188.726 139.752 165.560 1.00 69.12  ? 3880 HIS A NE2   1 
ATOM   17756 N  N     . ILE A 1 3881 ? 186.919 135.308 170.160 1.00 63.40  ? 3881 ILE A N     1 
ATOM   17757 C  CA    . ILE A 1 3881 ? 186.817 134.064 170.914 1.00 58.57  ? 3881 ILE A CA    1 
ATOM   17758 C  C     . ILE A 1 3881 ? 185.456 133.414 170.695 1.00 59.60  ? 3881 ILE A C     1 
ATOM   17759 O  O     . ILE A 1 3881 ? 185.347 132.185 170.648 1.00 71.62  ? 3881 ILE A O     1 
ATOM   17760 C  CB    . ILE A 1 3881 ? 187.103 134.317 172.406 1.00 61.81  ? 3881 ILE A CB    1 
ATOM   17761 C  CG1   . ILE A 1 3881 ? 187.068 133.004 173.189 1.00 62.33  ? 3881 ILE A CG1   1 
ATOM   17762 C  CG2   . ILE A 1 3881 ? 186.126 135.327 172.986 1.00 68.93  ? 3881 ILE A CG2   1 
ATOM   17763 C  CD1   . ILE A 1 3881 ? 187.970 131.935 172.618 1.00 65.42  ? 3881 ILE A CD1   1 
ATOM   17764 N  N     . THR A 1 3882 ? 184.403 134.219 170.540 1.00 52.55  ? 3882 THR A N     1 
ATOM   17765 C  CA    . THR A 1 3882 ? 183.073 133.662 170.307 1.00 58.89  ? 3882 THR A CA    1 
ATOM   17766 C  C     . THR A 1 3882 ? 183.017 132.898 168.988 1.00 70.62  ? 3882 THR A C     1 
ATOM   17767 O  O     . THR A 1 3882 ? 182.554 131.751 168.937 1.00 76.92  ? 3882 THR A O     1 
ATOM   17768 C  CB    . THR A 1 3882 ? 182.029 134.778 170.320 1.00 56.37  ? 3882 THR A CB    1 
ATOM   17769 O  OG1   . THR A 1 3882 ? 182.188 135.571 171.502 1.00 65.09  ? 3882 THR A OG1   1 
ATOM   17770 C  CG2   . THR A 1 3882 ? 180.628 134.195 170.291 1.00 59.61  ? 3882 THR A CG2   1 
ATOM   17771 N  N     . PHE A 1 3883 ? 183.488 133.522 167.907 1.00 58.35  ? 3883 PHE A N     1 
ATOM   17772 C  CA    . PHE A 1 3883 ? 183.471 132.855 166.610 1.00 47.21  ? 3883 PHE A CA    1 
ATOM   17773 C  C     . PHE A 1 3883 ? 184.405 131.653 166.598 1.00 59.64  ? 3883 PHE A C     1 
ATOM   17774 O  O     . PHE A 1 3883 ? 184.096 130.629 165.978 1.00 73.65  ? 3883 PHE A O     1 
ATOM   17775 C  CB    . PHE A 1 3883 ? 183.842 133.839 165.503 1.00 44.54  ? 3883 PHE A CB    1 
ATOM   17776 C  CG    . PHE A 1 3883 ? 183.601 133.307 164.121 1.00 56.78  ? 3883 PHE A CG    1 
ATOM   17777 C  CD1   . PHE A 1 3883 ? 182.382 132.746 163.786 1.00 61.79  ? 3883 PHE A CD1   1 
ATOM   17778 C  CD2   . PHE A 1 3883 ? 184.594 133.361 163.160 1.00 63.36  ? 3883 PHE A CD2   1 
ATOM   17779 C  CE1   . PHE A 1 3883 ? 182.156 132.251 162.518 1.00 58.79  ? 3883 PHE A CE1   1 
ATOM   17780 C  CE2   . PHE A 1 3883 ? 184.374 132.866 161.891 1.00 58.67  ? 3883 PHE A CE2   1 
ATOM   17781 C  CZ    . PHE A 1 3883 ? 183.153 132.312 161.569 1.00 54.29  ? 3883 PHE A CZ    1 
ATOM   17782 N  N     . ALA A 1 3884 ? 185.554 131.758 167.270 1.00 55.05  ? 3884 ALA A N     1 
ATOM   17783 C  CA    . ALA A 1 3884 ? 186.458 130.616 167.354 1.00 51.96  ? 3884 ALA A CA    1 
ATOM   17784 C  C     . ALA A 1 3884 ? 185.810 129.454 168.096 1.00 56.52  ? 3884 ALA A C     1 
ATOM   17785 O  O     . ALA A 1 3884 ? 185.955 128.295 167.692 1.00 69.07  ? 3884 ALA A O     1 
ATOM   17786 C  CB    . ALA A 1 3884 ? 187.764 131.026 168.031 1.00 60.65  ? 3884 ALA A CB    1 
ATOM   17787 N  N     . MET A 1 3885 ? 185.089 129.744 169.180 1.00 51.61  ? 3885 MET A N     1 
ATOM   17788 C  CA    . MET A 1 3885 ? 184.392 128.697 169.917 1.00 52.07  ? 3885 MET A CA    1 
ATOM   17789 C  C     . MET A 1 3885 ? 183.307 128.056 169.064 1.00 63.25  ? 3885 MET A C     1 
ATOM   17790 O  O     . MET A 1 3885 ? 183.130 126.832 169.085 1.00 74.55  ? 3885 MET A O     1 
ATOM   17791 C  CB    . MET A 1 3885 ? 183.794 129.275 171.198 1.00 51.59  ? 3885 MET A CB    1 
ATOM   17792 C  CG    . MET A 1 3885 ? 184.776 129.374 172.350 1.00 60.54  ? 3885 MET A CG    1 
ATOM   17793 S  SD    . MET A 1 3885 ? 184.928 127.839 173.273 1.00 82.60  ? 3885 MET A SD    1 
ATOM   17794 C  CE    . MET A 1 3885 ? 183.720 128.105 174.564 1.00 67.00  ? 3885 MET A CE    1 
ATOM   17795 N  N     . LEU A 1 3886 ? 182.565 128.870 168.309 1.00 58.61  ? 3886 LEU A N     1 
ATOM   17796 C  CA    . LEU A 1 3886 ? 181.536 128.318 167.433 1.00 59.16  ? 3886 LEU A CA    1 
ATOM   17797 C  C     . LEU A 1 3886 ? 182.143 127.431 166.352 1.00 62.28  ? 3886 LEU A C     1 
ATOM   17798 O  O     . LEU A 1 3886 ? 181.614 126.353 166.056 1.00 72.71  ? 3886 LEU A O     1 
ATOM   17799 C  CB    . LEU A 1 3886 ? 180.714 129.444 166.810 1.00 56.21  ? 3886 LEU A CB    1 
ATOM   17800 C  CG    . LEU A 1 3886 ? 179.880 130.255 167.800 1.00 58.80  ? 3886 LEU A CG    1 
ATOM   17801 C  CD1   . LEU A 1 3886 ? 179.386 131.531 167.154 1.00 63.72  ? 3886 LEU A CD1   1 
ATOM   17802 C  CD2   . LEU A 1 3886 ? 178.716 129.430 168.322 1.00 63.28  ? 3886 LEU A CD2   1 
ATOM   17803 N  N     . LEU A 1 3887 ? 183.257 127.862 165.756 1.00 51.00  ? 3887 LEU A N     1 
ATOM   17804 C  CA    . LEU A 1 3887 ? 183.921 127.038 164.751 1.00 47.66  ? 3887 LEU A CA    1 
ATOM   17805 C  C     . LEU A 1 3887 ? 184.443 125.741 165.357 1.00 54.39  ? 3887 LEU A C     1 
ATOM   17806 O  O     . LEU A 1 3887 ? 184.370 124.678 164.729 1.00 66.01  ? 3887 LEU A O     1 
ATOM   17807 C  CB    . LEU A 1 3887 ? 185.059 127.819 164.096 1.00 51.64  ? 3887 LEU A CB    1 
ATOM   17808 C  CG    . LEU A 1 3887 ? 184.656 128.973 163.179 1.00 53.11  ? 3887 LEU A CG    1 
ATOM   17809 C  CD1   . LEU A 1 3887 ? 185.849 129.452 162.375 1.00 63.70  ? 3887 LEU A CD1   1 
ATOM   17810 C  CD2   . LEU A 1 3887 ? 183.522 128.556 162.262 1.00 54.41  ? 3887 LEU A CD2   1 
ATOM   17811 N  N     . ALA A 1 3888 ? 184.981 125.810 166.577 1.00 53.69  ? 3888 ALA A N     1 
ATOM   17812 C  CA    . ALA A 1 3888 ? 185.444 124.603 167.252 1.00 58.65  ? 3888 ALA A CA    1 
ATOM   17813 C  C     . ALA A 1 3888 ? 184.292 123.641 167.508 1.00 65.01  ? 3888 ALA A C     1 
ATOM   17814 O  O     . ALA A 1 3888 ? 184.440 122.425 167.344 1.00 73.06  ? 3888 ALA A O     1 
ATOM   17815 C  CB    . ALA A 1 3888 ? 186.142 124.968 168.561 1.00 62.57  ? 3888 ALA A CB    1 
ATOM   17816 N  N     . ARG A 1 3889 ? 183.137 124.168 167.919 1.00 69.77  ? 3889 ARG A N     1 
ATOM   17817 C  CA    . ARG A 1 3889 ? 181.964 123.319 168.106 1.00 70.39  ? 3889 ARG A CA    1 
ATOM   17818 C  C     . ARG A 1 3889 ? 181.521 122.694 166.790 1.00 77.39  ? 3889 ARG A C     1 
ATOM   17819 O  O     . ARG A 1 3889 ? 181.117 121.525 166.755 1.00 80.94  ? 3889 ARG A O     1 
ATOM   17820 C  CB    . ARG A 1 3889 ? 180.822 124.122 168.726 1.00 67.62  ? 3889 ARG A CB    1 
ATOM   17821 C  CG    . ARG A 1 3889 ? 181.030 124.477 170.184 1.00 73.48  ? 3889 ARG A CG    1 
ATOM   17822 C  CD    . ARG A 1 3889 ? 179.698 124.718 170.870 1.00 80.21  ? 3889 ARG A CD    1 
ATOM   17823 N  NE    . ARG A 1 3889 ? 178.874 123.515 170.877 1.00 79.02  ? 3889 ARG A NE    1 
ATOM   17824 C  CZ    . ARG A 1 3889 ? 177.617 123.470 171.295 1.00 79.89  ? 3889 ARG A CZ    1 
ATOM   17825 N  NH1   . ARG A 1 3889 ? 177.001 124.548 171.750 1.00 77.66  ? 3889 ARG A NH1   1 
ATOM   17826 N  NH2   . ARG A 1 3889 ? 176.962 122.313 171.254 1.00 77.87  ? 3889 ARG A NH2   1 
ATOM   17827 N  N     . ILE A 1 3890 ? 181.576 123.460 165.699 1.00 70.52  ? 3890 ILE A N     1 
ATOM   17828 C  CA    . ILE A 1 3890 ? 181.203 122.919 164.393 1.00 63.64  ? 3890 ILE A CA    1 
ATOM   17829 C  C     . ILE A 1 3890 ? 182.136 121.782 163.998 1.00 63.68  ? 3890 ILE A C     1 
ATOM   17830 O  O     . ILE A 1 3890 ? 181.689 120.731 163.522 1.00 69.01  ? 3890 ILE A O     1 
ATOM   17831 C  CB    . ILE A 1 3890 ? 181.187 124.034 163.331 1.00 60.20  ? 3890 ILE A CB    1 
ATOM   17832 C  CG1   . ILE A 1 3890 ? 180.107 125.068 163.651 1.00 63.39  ? 3890 ILE A CG1   1 
ATOM   17833 C  CG2   . ILE A 1 3890 ? 180.978 123.449 161.946 1.00 60.58  ? 3890 ILE A CG2   1 
ATOM   17834 C  CD1   . ILE A 1 3890 ? 178.789 124.465 164.084 1.00 67.65  ? 3890 ILE A CD1   1 
ATOM   17835 N  N     . LYS A 1 3891 ? 183.444 121.968 164.188 1.00 66.50  ? 3891 LYS A N     1 
ATOM   17836 C  CA    . LYS A 1 3891 ? 184.388 120.907 163.848 1.00 69.75  ? 3891 LYS A CA    1 
ATOM   17837 C  C     . LYS A 1 3891 ? 184.228 119.705 164.770 1.00 74.29  ? 3891 LYS A C     1 
ATOM   17838 O  O     . LYS A 1 3891 ? 184.393 118.559 164.337 1.00 76.69  ? 3891 LYS A O     1 
ATOM   17839 C  CB    . LYS A 1 3891 ? 185.823 121.428 163.901 1.00 71.32  ? 3891 LYS A CB    1 
ATOM   17840 C  CG    . LYS A 1 3891 ? 186.846 120.418 163.404 1.00 70.40  ? 3891 LYS A CG    1 
ATOM   17841 C  CD    . LYS A 1 3891 ? 188.266 120.861 163.693 1.00 73.42  ? 3891 LYS A CD    1 
ATOM   17842 C  CE    . LYS A 1 3891 ? 189.269 120.009 162.934 1.00 77.68  ? 3891 LYS A CE    1 
ATOM   17843 N  NZ    . LYS A 1 3891 ? 189.008 120.026 161.468 1.00 79.44  ? 3891 LYS A NZ    1 
ATOM   17844 N  N     . LEU A 1 3892 ? 183.911 119.946 166.044 1.00 79.02  ? 3892 LEU A N     1 
ATOM   17845 C  CA    . LEU A 1 3892 ? 183.767 118.846 166.992 1.00 74.77  ? 3892 LEU A CA    1 
ATOM   17846 C  C     . LEU A 1 3892 ? 182.627 117.917 166.596 1.00 80.51  ? 3892 LEU A C     1 
ATOM   17847 O  O     . LEU A 1 3892 ? 182.748 116.692 166.706 1.00 84.65  ? 3892 LEU A O     1 
ATOM   17848 C  CB    . LEU A 1 3892 ? 183.549 119.394 168.401 1.00 70.88  ? 3892 LEU A CB    1 
ATOM   17849 C  CG    . LEU A 1 3892 ? 183.413 118.346 169.503 1.00 75.59  ? 3892 LEU A CG    1 
ATOM   17850 C  CD1   . LEU A 1 3892 ? 184.608 117.410 169.489 1.00 81.97  ? 3892 LEU A CD1   1 
ATOM   17851 C  CD2   . LEU A 1 3892 ? 183.269 119.015 170.859 1.00 79.32  ? 3892 LEU A CD2   1 
ATOM   17852 N  N     . LYS A 1 3893 ? 181.509 118.482 166.134 1.00 85.20  ? 3893 LYS A N     1 
ATOM   17853 C  CA    . LYS A 1 3893 ? 180.392 117.661 165.686 1.00 82.83  ? 3893 LYS A CA    1 
ATOM   17854 C  C     . LYS A 1 3893 ? 180.744 116.830 164.461 1.00 83.61  ? 3893 LYS A C     1 
ATOM   17855 O  O     . LYS A 1 3893 ? 180.129 115.781 164.238 1.00 87.84  ? 3893 LYS A O     1 
ATOM   17856 C  CB    . LYS A 1 3893 ? 179.181 118.543 165.386 1.00 81.84  ? 3893 LYS A CB    1 
ATOM   17857 C  CG    . LYS A 1 3893 ? 178.602 119.238 166.606 1.00 82.80  ? 3893 LYS A CG    1 
ATOM   17858 C  CD    . LYS A 1 3893 ? 177.087 119.338 166.522 1.00 85.24  ? 3893 LYS A CD    1 
ATOM   17859 C  CE    . LYS A 1 3893 ? 176.630 119.714 165.121 1.00 86.89  ? 3893 LYS A CE    1 
ATOM   17860 N  NZ    . LYS A 1 3893 ? 175.153 119.880 165.045 1.00 88.05  ? 3893 LYS A NZ    1 
ATOM   17861 N  N     . GLY A 1 3894 ? 181.714 117.268 163.666 1.00 92.64  ? 3894 GLY A N     1 
ATOM   17862 C  CA    . GLY A 1 3894 ? 182.131 116.564 162.475 1.00 93.98  ? 3894 GLY A CA    1 
ATOM   17863 C  C     . GLY A 1 3894 ? 183.146 115.465 162.694 1.00 96.87  ? 3894 GLY A C     1 
ATOM   17864 O  O     . GLY A 1 3894 ? 183.588 114.847 161.720 1.00 97.52  ? 3894 GLY A O     1 
ATOM   17865 N  N     . THR A 1 3895 ? 183.532 115.197 163.938 1.00 104.78 ? 3895 THR A N     1 
ATOM   17866 C  CA    . THR A 1 3895 ? 184.497 114.151 164.251 1.00 105.48 ? 3895 THR A CA    1 
ATOM   17867 C  C     . THR A 1 3895 ? 183.743 112.888 164.647 1.00 107.52 ? 3895 THR A C     1 
ATOM   17868 O  O     . THR A 1 3895 ? 182.951 112.904 165.596 1.00 106.36 ? 3895 THR A O     1 
ATOM   17869 C  CB    . THR A 1 3895 ? 185.439 114.587 165.372 1.00 104.94 ? 3895 THR A CB    1 
ATOM   17870 O  OG1   . THR A 1 3895 ? 186.100 115.802 164.998 1.00 105.63 ? 3895 THR A OG1   1 
ATOM   17871 C  CG2   . THR A 1 3895 ? 186.484 113.513 165.631 1.00 103.57 ? 3895 THR A CG2   1 
ATOM   17872 N  N     . VAL A 1 3896 ? 183.988 111.799 163.916 1.00 122.35 ? 3896 VAL A N     1 
ATOM   17873 C  CA    . VAL A 1 3896 ? 183.287 110.548 164.184 1.00 123.35 ? 3896 VAL A CA    1 
ATOM   17874 C  C     . VAL A 1 3896 ? 183.723 109.962 165.521 1.00 121.07 ? 3896 VAL A C     1 
ATOM   17875 O  O     . VAL A 1 3896 ? 182.911 109.390 166.258 1.00 118.90 ? 3896 VAL A O     1 
ATOM   17876 C  CB    . VAL A 1 3896 ? 183.513 109.555 163.029 1.00 120.75 ? 3896 VAL A CB    1 
ATOM   17877 C  CG1   . VAL A 1 3896 ? 182.543 108.388 163.134 1.00 118.85 ? 3896 VAL A CG1   1 
ATOM   17878 C  CG2   . VAL A 1 3896 ? 183.367 110.260 161.689 1.00 120.74 ? 3896 VAL A CG2   1 
ATOM   17879 N  N     . GLY A 1 3897 ? 185.002 110.096 165.858 1.00 111.47 ? 3897 GLY A N     1 
ATOM   17880 C  CA    . GLY A 1 3897 ? 185.542 109.511 167.067 1.00 111.28 ? 3897 GLY A CA    1 
ATOM   17881 C  C     . GLY A 1 3897 ? 185.275 110.266 168.347 1.00 112.54 ? 3897 GLY A C     1 
ATOM   17882 O  O     . GLY A 1 3897 ? 185.697 109.816 169.415 1.00 112.36 ? 3897 GLY A O     1 
ATOM   17883 N  N     . GLU A 1 3898 ? 184.585 111.407 168.280 1.00 114.31 ? 3898 GLU A N     1 
ATOM   17884 C  CA    . GLU A 1 3898 ? 184.325 112.185 169.478 1.00 113.79 ? 3898 GLU A CA    1 
ATOM   17885 C  C     . GLU A 1 3898 ? 182.865 112.067 169.897 1.00 111.03 ? 3898 GLU A C     1 
ATOM   17886 O  O     . GLU A 1 3898 ? 181.977 112.006 169.039 1.00 110.92 ? 3898 GLU A O     1 
ATOM   17887 C  CB    . GLU A 1 3898 ? 184.662 113.665 169.259 1.00 111.29 ? 3898 GLU A CB    1 
ATOM   17888 C  CG    . GLU A 1 3898 ? 186.148 113.975 169.260 1.00 113.40 ? 3898 GLU A CG    1 
ATOM   17889 C  CD    . GLU A 1 3898 ? 186.840 113.520 170.527 1.00 114.10 ? 3898 GLU A CD    1 
ATOM   17890 O  OE1   . GLU A 1 3898 ? 186.377 113.890 171.626 1.00 113.55 ? 3898 GLU A OE1   1 
ATOM   17891 O  OE2   . GLU A 1 3898 ? 187.849 112.793 170.421 1.00 114.60 ? 3898 GLU A OE2   1 
ATOM   17892 N  N     . PRO A 1 3899 ? 182.586 112.029 171.197 1.00 108.62 ? 3899 PRO A N     1 
ATOM   17893 C  CA    . PRO A 1 3899 ? 181.194 112.058 171.659 1.00 108.91 ? 3899 PRO A CA    1 
ATOM   17894 C  C     . PRO A 1 3899 ? 180.550 113.406 171.369 1.00 111.24 ? 3899 PRO A C     1 
ATOM   17895 O  O     . PRO A 1 3899 ? 181.195 114.365 170.941 1.00 113.01 ? 3899 PRO A O     1 
ATOM   17896 C  CB    . PRO A 1 3899 ? 181.306 111.803 173.166 1.00 108.70 ? 3899 PRO A CB    1 
ATOM   17897 C  CG    . PRO A 1 3899 ? 182.656 111.178 173.352 1.00 108.78 ? 3899 PRO A CG    1 
ATOM   17898 C  CD    . PRO A 1 3899 ? 183.528 111.791 172.301 1.00 108.29 ? 3899 PRO A CD    1 
ATOM   17899 N  N     . THR A 1 3900 ? 179.239 113.469 171.614 1.00 109.96 ? 3900 THR A N     1 
ATOM   17900 C  CA    . THR A 1 3900 ? 178.493 114.681 171.294 1.00 110.02 ? 3900 THR A CA    1 
ATOM   17901 C  C     . THR A 1 3900 ? 178.778 115.808 172.281 1.00 111.12 ? 3900 THR A C     1 
ATOM   17902 O  O     . THR A 1 3900 ? 178.800 116.979 171.884 1.00 111.43 ? 3900 THR A O     1 
ATOM   17903 C  CB    . THR A 1 3900 ? 176.993 114.381 171.244 1.00 111.77 ? 3900 THR A CB    1 
ATOM   17904 O  OG1   . THR A 1 3900 ? 176.262 115.604 171.087 1.00 111.81 ? 3900 THR A OG1   1 
ATOM   17905 C  CG2   . THR A 1 3900 ? 176.538 113.674 172.515 1.00 112.15 ? 3900 THR A CG2   1 
ATOM   17906 N  N     . TYR A 1 3901 ? 179.001 115.479 173.556 1.00 106.86 ? 3901 TYR A N     1 
ATOM   17907 C  CA    . TYR A 1 3901 ? 179.220 116.477 174.608 1.00 102.12 ? 3901 TYR A CA    1 
ATOM   17908 C  C     . TYR A 1 3901 ? 178.083 117.495 174.648 1.00 98.79  ? 3901 TYR A C     1 
ATOM   17909 O  O     . TYR A 1 3901 ? 178.297 118.692 174.851 1.00 96.62  ? 3901 TYR A O     1 
ATOM   17910 C  CB    . TYR A 1 3901 ? 180.569 117.179 174.440 1.00 100.74 ? 3901 TYR A CB    1 
ATOM   17911 C  CG    . TYR A 1 3901 ? 181.761 116.251 174.446 1.00 100.86 ? 3901 TYR A CG    1 
ATOM   17912 C  CD1   . TYR A 1 3901 ? 182.080 115.504 175.572 1.00 99.25  ? 3901 TYR A CD1   1 
ATOM   17913 C  CD2   . TYR A 1 3901 ? 182.575 116.129 173.328 1.00 100.67 ? 3901 TYR A CD2   1 
ATOM   17914 C  CE1   . TYR A 1 3901 ? 183.171 114.658 175.581 1.00 100.75 ? 3901 TYR A CE1   1 
ATOM   17915 C  CE2   . TYR A 1 3901 ? 183.668 115.286 173.328 1.00 101.20 ? 3901 TYR A CE2   1 
ATOM   17916 C  CZ    . TYR A 1 3901 ? 183.961 114.553 174.457 1.00 104.42 ? 3901 TYR A CZ    1 
ATOM   17917 O  OH    . TYR A 1 3901 ? 185.050 113.712 174.461 1.00 107.04 ? 3901 TYR A OH    1 
ATOM   17918 N  N     . ASP A 1 3902 ? 176.856 117.013 174.445 1.00 113.78 ? 3902 ASP A N     1 
ATOM   17919 C  CA    . ASP A 1 3902 ? 175.709 117.912 174.389 1.00 115.96 ? 3902 ASP A CA    1 
ATOM   17920 C  C     . ASP A 1 3902 ? 175.379 118.473 175.768 1.00 116.09 ? 3902 ASP A C     1 
ATOM   17921 O  O     . ASP A 1 3902 ? 175.154 119.679 175.920 1.00 114.75 ? 3902 ASP A O     1 
ATOM   17922 C  CB    . ASP A 1 3902 ? 174.502 117.184 173.798 1.00 118.72 ? 3902 ASP A CB    1 
ATOM   17923 C  CG    . ASP A 1 3902 ? 173.442 118.137 173.281 1.00 121.40 ? 3902 ASP A CG    1 
ATOM   17924 O  OD1   . ASP A 1 3902 ? 173.637 119.365 173.396 1.00 121.06 ? 3902 ASP A OD1   1 
ATOM   17925 O  OD2   . ASP A 1 3902 ? 172.415 117.657 172.756 1.00 120.33 ? 3902 ASP A OD2   1 
ATOM   17926 N  N     . ALA A 1 3903 ? 175.346 117.611 176.786 1.00 113.44 ? 3903 ALA A N     1 
ATOM   17927 C  CA    . ALA A 1 3903 ? 175.006 118.064 178.131 1.00 112.00 ? 3903 ALA A CA    1 
ATOM   17928 C  C     . ALA A 1 3903 ? 176.065 119.008 178.686 1.00 110.49 ? 3903 ALA A C     1 
ATOM   17929 O  O     . ALA A 1 3903 ? 175.738 119.981 179.376 1.00 109.33 ? 3903 ALA A O     1 
ATOM   17930 C  CB    . ALA A 1 3903 ? 174.819 116.863 179.058 1.00 110.70 ? 3903 ALA A CB    1 
ATOM   17931 N  N     . GLU A 1 3904 ? 177.340 118.730 178.403 1.00 105.88 ? 3904 GLU A N     1 
ATOM   17932 C  CA    . GLU A 1 3904 ? 178.414 119.580 178.903 1.00 105.08 ? 3904 GLU A CA    1 
ATOM   17933 C  C     . GLU A 1 3904 ? 178.281 121.001 178.370 1.00 104.99 ? 3904 GLU A C     1 
ATOM   17934 O  O     . GLU A 1 3904 ? 178.309 121.969 179.138 1.00 105.40 ? 3904 GLU A O     1 
ATOM   17935 C  CB    . GLU A 1 3904 ? 179.770 118.984 178.522 1.00 105.93 ? 3904 GLU A CB    1 
ATOM   17936 C  CG    . GLU A 1 3904 ? 179.794 117.463 178.468 1.00 107.59 ? 3904 GLU A CG    1 
ATOM   17937 C  CD    . GLU A 1 3904 ? 179.759 116.821 179.843 1.00 108.52 ? 3904 GLU A CD    1 
ATOM   17938 O  OE1   . GLU A 1 3904 ? 179.667 115.577 179.914 1.00 108.46 ? 3904 GLU A OE1   1 
ATOM   17939 O  OE2   . GLU A 1 3904 ? 179.838 117.552 180.851 1.00 108.55 ? 3904 GLU A OE2   1 
ATOM   17940 N  N     . PHE A 1 3905 ? 178.120 121.145 177.052 1.00 92.96  ? 3905 PHE A N     1 
ATOM   17941 C  CA    . PHE A 1 3905 ? 177.942 122.472 176.472 1.00 89.41  ? 3905 PHE A CA    1 
ATOM   17942 C  C     . PHE A 1 3905 ? 176.628 123.104 176.908 1.00 90.69  ? 3905 PHE A C     1 
ATOM   17943 O  O     . PHE A 1 3905 ? 176.556 124.326 177.078 1.00 93.05  ? 3905 PHE A O     1 
ATOM   17944 C  CB    . PHE A 1 3905 ? 178.010 122.397 174.948 1.00 90.75  ? 3905 PHE A CB    1 
ATOM   17945 C  CG    . PHE A 1 3905 ? 179.403 122.489 174.400 1.00 90.39  ? 3905 PHE A CG    1 
ATOM   17946 C  CD1   . PHE A 1 3905 ? 180.109 123.677 174.469 1.00 89.47  ? 3905 PHE A CD1   1 
ATOM   17947 C  CD2   . PHE A 1 3905 ? 180.003 121.391 173.811 1.00 92.38  ? 3905 PHE A CD2   1 
ATOM   17948 C  CE1   . PHE A 1 3905 ? 181.389 123.768 173.964 1.00 93.95  ? 3905 PHE A CE1   1 
ATOM   17949 C  CE2   . PHE A 1 3905 ? 181.284 121.476 173.302 1.00 93.96  ? 3905 PHE A CE2   1 
ATOM   17950 C  CZ    . PHE A 1 3905 ? 181.978 122.666 173.380 1.00 98.23  ? 3905 PHE A CZ    1 
ATOM   17951 N  N     . GLN A 1 3906 ? 175.582 122.295 177.089 1.00 103.71 ? 3906 GLN A N     1 
ATOM   17952 C  CA    . GLN A 1 3906 ? 174.306 122.825 177.554 1.00 103.93 ? 3906 GLN A CA    1 
ATOM   17953 C  C     . GLN A 1 3906 ? 174.452 123.477 178.922 1.00 103.67 ? 3906 GLN A C     1 
ATOM   17954 O  O     . GLN A 1 3906 ? 173.967 124.592 179.145 1.00 105.56 ? 3906 GLN A O     1 
ATOM   17955 C  CB    . GLN A 1 3906 ? 173.268 121.702 177.599 1.00 107.09 ? 3906 GLN A CB    1 
ATOM   17956 C  CG    . GLN A 1 3906 ? 171.803 122.125 177.741 1.00 108.20 ? 3906 GLN A CG    1 
ATOM   17957 C  CD    . GLN A 1 3906 ? 171.376 123.255 176.812 1.00 108.97 ? 3906 GLN A CD    1 
ATOM   17958 O  OE1   . GLN A 1 3906 ? 172.006 123.522 175.787 1.00 110.47 ? 3906 GLN A OE1   1 
ATOM   17959 N  NE2   . GLN A 1 3906 ? 170.280 123.913 177.165 1.00 104.22 ? 3906 GLN A NE2   1 
ATOM   17960 N  N     . HIS A 1 3907 ? 175.130 122.797 179.849 1.00 100.16 ? 3907 HIS A N     1 
ATOM   17961 C  CA    . HIS A 1 3907 ? 175.374 123.381 181.164 1.00 102.93 ? 3907 HIS A CA    1 
ATOM   17962 C  C     . HIS A 1 3907 ? 176.325 124.567 181.072 1.00 102.21 ? 3907 HIS A C     1 
ATOM   17963 O  O     . HIS A 1 3907 ? 176.162 125.564 181.784 1.00 102.11 ? 3907 HIS A O     1 
ATOM   17964 C  CB    . HIS A 1 3907 ? 175.926 122.327 182.122 1.00 104.29 ? 3907 HIS A CB    1 
ATOM   17965 C  CG    . HIS A 1 3907 ? 176.276 122.871 183.472 1.00 105.63 ? 3907 HIS A CG    1 
ATOM   17966 N  ND1   . HIS A 1 3907 ? 177.578 123.024 183.898 1.00 106.80 ? 3907 HIS A ND1   1 
ATOM   17967 C  CD2   . HIS A 1 3907 ? 175.494 123.306 184.488 1.00 103.63 ? 3907 HIS A CD2   1 
ATOM   17968 C  CE1   . HIS A 1 3907 ? 177.583 123.527 185.120 1.00 106.22 ? 3907 HIS A CE1   1 
ATOM   17969 N  NE2   . HIS A 1 3907 ? 176.331 123.707 185.501 1.00 105.61 ? 3907 HIS A NE2   1 
ATOM   17970 N  N     . PHE A 1 3908 ? 177.335 124.475 180.204 1.00 89.93  ? 3908 PHE A N     1 
ATOM   17971 C  CA    . PHE A 1 3908 ? 178.288 125.568 180.053 1.00 87.07  ? 3908 PHE A CA    1 
ATOM   17972 C  C     . PHE A 1 3908 ? 177.609 126.841 179.568 1.00 86.48  ? 3908 PHE A C     1 
ATOM   17973 O  O     . PHE A 1 3908 ? 178.014 127.945 179.949 1.00 90.56  ? 3908 PHE A O     1 
ATOM   17974 C  CB    . PHE A 1 3908 ? 179.400 125.149 179.092 1.00 86.14  ? 3908 PHE A CB    1 
ATOM   17975 C  CG    . PHE A 1 3908 ? 180.306 126.269 178.679 1.00 82.29  ? 3908 PHE A CG    1 
ATOM   17976 C  CD1   . PHE A 1 3908 ? 181.132 126.885 179.602 1.00 84.20  ? 3908 PHE A CD1   1 
ATOM   17977 C  CD2   . PHE A 1 3908 ? 180.344 126.695 177.364 1.00 84.41  ? 3908 PHE A CD2   1 
ATOM   17978 C  CE1   . PHE A 1 3908 ? 181.972 127.912 179.220 1.00 87.02  ? 3908 PHE A CE1   1 
ATOM   17979 C  CE2   . PHE A 1 3908 ? 181.180 127.720 176.978 1.00 84.31  ? 3908 PHE A CE2   1 
ATOM   17980 C  CZ    . PHE A 1 3908 ? 181.998 128.327 177.906 1.00 84.66  ? 3908 PHE A CZ    1 
ATOM   17981 N  N     . LEU A 1 3909 ? 176.580 126.711 178.734 1.00 86.62  ? 3909 LEU A N     1 
ATOM   17982 C  CA    . LEU A 1 3909 ? 175.879 127.876 178.211 1.00 86.63  ? 3909 LEU A CA    1 
ATOM   17983 C  C     . LEU A 1 3909 ? 174.735 128.340 179.102 1.00 90.04  ? 3909 LEU A C     1 
ATOM   17984 O  O     . LEU A 1 3909 ? 174.446 129.542 179.141 1.00 91.04  ? 3909 LEU A O     1 
ATOM   17985 C  CB    . LEU A 1 3909 ? 175.342 127.582 176.808 1.00 87.82  ? 3909 LEU A CB    1 
ATOM   17986 C  CG    . LEU A 1 3909 ? 176.390 127.601 175.697 1.00 86.03  ? 3909 LEU A CG    1 
ATOM   17987 C  CD1   . LEU A 1 3909 ? 175.739 127.402 174.339 1.00 87.12  ? 3909 LEU A CD1   1 
ATOM   17988 C  CD2   . LEU A 1 3909 ? 177.169 128.902 175.738 1.00 83.74  ? 3909 LEU A CD2   1 
ATOM   17989 N  N     . ARG A 1 3910 ? 174.073 127.430 179.818 1.00 103.46 ? 3910 ARG A N     1 
ATOM   17990 C  CA    . ARG A 1 3910 ? 172.933 127.799 180.653 1.00 101.64 ? 3910 ARG A CA    1 
ATOM   17991 C  C     . ARG A 1 3910 ? 173.083 127.234 182.058 1.00 104.86 ? 3910 ARG A C     1 
ATOM   17992 O  O     . ARG A 1 3910 ? 172.125 126.717 182.643 1.00 105.55 ? 3910 ARG A O     1 
ATOM   17993 C  CB    . ARG A 1 3910 ? 171.615 127.339 180.033 1.00 100.11 ? 3910 ARG A CB    1 
ATOM   17994 C  CG    . ARG A 1 3910 ? 171.377 127.846 178.624 1.00 101.78 ? 3910 ARG A CG    1 
ATOM   17995 C  CD    . ARG A 1 3910 ? 170.332 127.010 177.907 1.00 103.84 ? 3910 ARG A CD    1 
ATOM   17996 N  NE    . ARG A 1 3910 ? 169.769 127.691 176.747 1.00 105.32 ? 3910 ARG A NE    1 
ATOM   17997 C  CZ    . ARG A 1 3910 ? 168.925 128.711 176.810 1.00 106.43 ? 3910 ARG A CZ    1 
ATOM   17998 N  NH1   . ARG A 1 3910 ? 168.507 129.194 177.968 1.00 105.10 ? 3910 ARG A NH1   1 
ATOM   17999 N  NH2   . ARG A 1 3910 ? 168.485 129.260 175.680 1.00 106.38 ? 3910 ARG A NH2   1 
ATOM   18000 N  N     . GLY A 1 3911 ? 174.288 127.321 182.623 1.00 117.03 ? 3911 GLY A N     1 
ATOM   18001 C  CA    . GLY A 1 3911 ? 174.485 126.895 183.997 1.00 116.39 ? 3911 GLY A CA    1 
ATOM   18002 C  C     . GLY A 1 3911 ? 173.918 127.850 185.023 1.00 118.71 ? 3911 GLY A C     1 
ATOM   18003 O  O     . GLY A 1 3911 ? 173.646 127.437 186.155 1.00 120.58 ? 3911 GLY A O     1 
ATOM   18004 N  N     . ASN A 1 3912 ? 173.731 129.116 184.654 1.00 125.77 ? 3912 ASN A N     1 
ATOM   18005 C  CA    . ASN A 1 3912 ? 173.167 130.107 185.559 1.00 126.20 ? 3912 ASN A CA    1 
ATOM   18006 C  C     . ASN A 1 3912 ? 171.662 129.956 185.736 1.00 128.03 ? 3912 ASN A C     1 
ATOM   18007 O  O     . ASN A 1 3912 ? 171.119 130.446 186.732 1.00 130.64 ? 3912 ASN A O     1 
ATOM   18008 C  CB    . ASN A 1 3912 ? 173.497 131.515 185.050 1.00 125.67 ? 3912 ASN A CB    1 
ATOM   18009 C  CG    . ASN A 1 3912 ? 173.138 132.601 186.047 1.00 129.89 ? 3912 ASN A CG    1 
ATOM   18010 O  OD1   . ASN A 1 3912 ? 171.977 132.991 186.170 1.00 132.23 ? 3912 ASN A OD1   1 
ATOM   18011 N  ND2   . ASN A 1 3912 ? 174.138 133.095 186.768 1.00 128.42 ? 3912 ASN A ND2   1 
ATOM   18012 N  N     . GLU A 1 3913 ? 170.982 129.274 184.815 1.00 127.82 ? 3913 GLU A N     1 
ATOM   18013 C  CA    . GLU A 1 3913 ? 169.532 129.153 184.870 1.00 128.00 ? 3913 GLU A CA    1 
ATOM   18014 C  C     . GLU A 1 3913 ? 169.053 128.061 185.819 1.00 128.33 ? 3913 GLU A C     1 
ATOM   18015 O  O     . GLU A 1 3913 ? 167.843 127.942 186.035 1.00 127.89 ? 3913 GLU A O     1 
ATOM   18016 C  CB    . GLU A 1 3913 ? 168.977 128.893 183.468 1.00 127.73 ? 3913 GLU A CB    1 
ATOM   18017 C  CG    . GLU A 1 3913 ? 168.995 130.113 182.563 1.00 125.45 ? 3913 GLU A CG    1 
ATOM   18018 C  CD    . GLU A 1 3913 ? 168.583 129.790 181.141 1.00 128.00 ? 3913 GLU A CD    1 
ATOM   18019 O  OE1   . GLU A 1 3913 ? 167.542 129.124 180.960 1.00 130.79 ? 3913 GLU A OE1   1 
ATOM   18020 O  OE2   . GLU A 1 3913 ? 169.299 130.202 180.205 1.00 125.88 ? 3913 GLU A OE2   1 
ATOM   18021 N  N     . ILE A 1 3914 ? 169.959 127.266 186.386 1.00 130.00 ? 3914 ILE A N     1 
ATOM   18022 C  CA    . ILE A 1 3914 ? 169.585 126.216 187.332 1.00 129.24 ? 3914 ILE A CA    1 
ATOM   18023 C  C     . ILE A 1 3914 ? 169.247 126.900 188.654 1.00 131.64 ? 3914 ILE A C     1 
ATOM   18024 O  O     . ILE A 1 3914 ? 170.104 127.522 189.283 1.00 132.31 ? 3914 ILE A O     1 
ATOM   18025 C  CB    . ILE A 1 3914 ? 170.692 125.173 187.497 1.00 129.02 ? 3914 ILE A CB    1 
ATOM   18026 C  CG1   . ILE A 1 3914 ? 171.035 124.548 186.143 1.00 128.79 ? 3914 ILE A CG1   1 
ATOM   18027 C  CG2   . ILE A 1 3914 ? 170.269 124.101 188.488 1.00 129.58 ? 3914 ILE A CG2   1 
ATOM   18028 C  CD1   . ILE A 1 3914 ? 172.093 123.470 186.217 1.00 128.96 ? 3914 ILE A CD1   1 
ATOM   18029 N  N     . VAL A 1 3915 ? 167.989 126.784 189.080 1.00 145.93 ? 3915 VAL A N     1 
ATOM   18030 C  CA    . VAL A 1 3915 ? 167.530 127.475 190.279 1.00 146.14 ? 3915 VAL A CA    1 
ATOM   18031 C  C     . VAL A 1 3915 ? 168.021 126.737 191.517 1.00 146.49 ? 3915 VAL A C     1 
ATOM   18032 O  O     . VAL A 1 3915 ? 167.932 125.505 191.603 1.00 143.67 ? 3915 VAL A O     1 
ATOM   18033 C  CB    . VAL A 1 3915 ? 165.999 127.599 190.273 1.00 144.67 ? 3915 VAL A CB    1 
ATOM   18034 C  CG1   . VAL A 1 3915 ? 165.508 128.228 191.568 1.00 142.76 ? 3915 VAL A CG1   1 
ATOM   18035 C  CG2   . VAL A 1 3915 ? 165.539 128.411 189.073 1.00 145.12 ? 3915 VAL A CG2   1 
ATOM   18036 N  N     . LEU A 1 3916 ? 168.541 127.490 192.483 1.00 151.06 ? 3916 LEU A N     1 
ATOM   18037 C  CA    . LEU A 1 3916 ? 169.052 126.943 193.731 1.00 150.82 ? 3916 LEU A CA    1 
ATOM   18038 C  C     . LEU A 1 3916 ? 168.271 127.511 194.907 1.00 152.38 ? 3916 LEU A C     1 
ATOM   18039 O  O     . LEU A 1 3916 ? 167.944 128.702 194.930 1.00 151.39 ? 3916 LEU A O     1 
ATOM   18040 C  CB    . LEU A 1 3916 ? 170.537 127.259 193.910 1.00 148.02 ? 3916 LEU A CB    1 
ATOM   18041 C  CG    . LEU A 1 3916 ? 171.488 126.775 192.820 1.00 147.96 ? 3916 LEU A CG    1 
ATOM   18042 C  CD1   . LEU A 1 3916 ? 172.876 127.318 193.090 1.00 149.20 ? 3916 LEU A CD1   1 
ATOM   18043 C  CD2   . LEU A 1 3916 ? 171.499 125.257 192.755 1.00 146.37 ? 3916 LEU A CD2   1 
ATOM   18044 N  N     . SER A 1 3917 ? 167.975 126.654 195.880 1.00 172.43 ? 3917 SER A N     1 
ATOM   18045 C  CA    . SER A 1 3917 ? 167.326 127.089 197.106 1.00 172.01 ? 3917 SER A CA    1 
ATOM   18046 C  C     . SER A 1 3917 ? 168.371 127.585 198.103 1.00 174.35 ? 3917 SER A C     1 
ATOM   18047 O  O     . SER A 1 3917 ? 169.581 127.487 197.880 1.00 174.27 ? 3917 SER A O     1 
ATOM   18048 C  CB    . SER A 1 3917 ? 166.491 125.954 197.694 1.00 170.41 ? 3917 SER A CB    1 
ATOM   18049 O  OG    . SER A 1 3917 ? 165.439 125.592 196.817 1.00 169.91 ? 3917 SER A OG    1 
ATOM   18050 N  N     . ALA A 1 3918 ? 167.894 128.138 199.222 1.00 176.30 ? 3918 ALA A N     1 
ATOM   18051 C  CA    . ALA A 1 3918 ? 168.806 128.646 200.243 1.00 175.24 ? 3918 ALA A CA    1 
ATOM   18052 C  C     . ALA A 1 3918 ? 169.649 127.527 200.842 1.00 176.63 ? 3918 ALA A C     1 
ATOM   18053 O  O     . ALA A 1 3918 ? 170.855 127.694 201.057 1.00 175.59 ? 3918 ALA A O     1 
ATOM   18054 C  CB    . ALA A 1 3918 ? 168.020 129.372 201.334 1.00 173.99 ? 3918 ALA A CB    1 
ATOM   18055 N  N     . GLY A 1 3919 ? 169.033 126.376 201.117 1.00 176.45 ? 3919 GLY A N     1 
ATOM   18056 C  CA    . GLY A 1 3919 ? 169.754 125.241 201.660 1.00 175.01 ? 3919 GLY A CA    1 
ATOM   18057 C  C     . GLY A 1 3919 ? 170.550 124.444 200.652 1.00 175.23 ? 3919 GLY A C     1 
ATOM   18058 O  O     . GLY A 1 3919 ? 171.233 123.489 201.033 1.00 174.30 ? 3919 GLY A O     1 
ATOM   18059 N  N     . SER A 1 3920 ? 170.474 124.813 199.372 1.00 174.47 ? 3920 SER A N     1 
ATOM   18060 C  CA    . SER A 1 3920 ? 171.190 124.072 198.339 1.00 173.80 ? 3920 SER A CA    1 
ATOM   18061 C  C     . SER A 1 3920 ? 172.693 124.325 198.406 1.00 174.18 ? 3920 SER A C     1 
ATOM   18062 O  O     . SER A 1 3920 ? 173.466 123.671 197.697 1.00 173.55 ? 3920 SER A O     1 
ATOM   18063 C  CB    . SER A 1 3920 ? 170.644 124.439 196.959 1.00 173.25 ? 3920 SER A CB    1 
ATOM   18064 O  OG    . SER A 1 3920 ? 169.273 124.101 196.846 1.00 172.57 ? 3920 SER A OG    1 
ATOM   18065 N  N     . THR A 1 3921 ? 173.122 125.277 199.226 1.00 163.77 ? 3921 THR A N     1 
ATOM   18066 C  CA    . THR A 1 3921 ? 174.543 125.598 199.328 1.00 163.08 ? 3921 THR A CA    1 
ATOM   18067 C  C     . THR A 1 3921 ? 175.127 125.039 200.620 1.00 161.24 ? 3921 THR A C     1 
ATOM   18068 O  O     . THR A 1 3921 ? 174.835 125.567 201.701 1.00 158.90 ? 3921 THR A O     1 
ATOM   18069 C  CB    . THR A 1 3921 ? 174.746 127.109 199.270 1.00 161.39 ? 3921 THR A CB    1 
ATOM   18070 O  OG1   . THR A 1 3921 ? 174.262 127.608 198.017 1.00 159.32 ? 3921 THR A OG1   1 
ATOM   18071 C  CG2   . THR A 1 3921 ? 176.221 127.454 199.410 1.00 161.67 ? 3921 THR A CG2   1 
ATOM   18072 N  N     . PRO A 1 3922 ? 175.947 123.989 200.565 1.00 158.97 ? 3922 PRO A N     1 
ATOM   18073 C  CA    . PRO A 1 3922 ? 176.583 123.456 201.778 1.00 158.63 ? 3922 PRO A CA    1 
ATOM   18074 C  C     . PRO A 1 3922 ? 177.584 124.387 202.445 1.00 159.99 ? 3922 PRO A C     1 
ATOM   18075 O  O     . PRO A 1 3922 ? 178.004 124.094 203.570 1.00 160.14 ? 3922 PRO A O     1 
ATOM   18076 C  CB    . PRO A 1 3922 ? 177.302 122.207 201.250 1.00 157.35 ? 3922 PRO A CB    1 
ATOM   18077 C  CG    . PRO A 1 3922 ? 176.491 121.759 200.106 1.00 157.99 ? 3922 PRO A CG    1 
ATOM   18078 C  CD    . PRO A 1 3922 ? 175.952 123.010 199.465 1.00 158.39 ? 3922 PRO A CD    1 
ATOM   18079 N  N     . ARG A 1 3923 ? 177.979 125.479 201.786 1.00 153.41 ? 3923 ARG A N     1 
ATOM   18080 C  CA    . ARG A 1 3923 ? 179.051 126.357 202.257 1.00 151.55 ? 3923 ARG A CA    1 
ATOM   18081 C  C     . ARG A 1 3923 ? 180.358 125.576 202.412 1.00 150.71 ? 3923 ARG A C     1 
ATOM   18082 O  O     . ARG A 1 3923 ? 180.901 125.420 203.508 1.00 151.33 ? 3923 ARG A O     1 
ATOM   18083 C  CB    . ARG A 1 3923 ? 178.665 127.061 203.563 1.00 151.61 ? 3923 ARG A CB    1 
ATOM   18084 C  CG    . ARG A 1 3923 ? 178.178 128.487 203.379 1.00 150.68 ? 3923 ARG A CG    1 
ATOM   18085 C  CD    . ARG A 1 3923 ? 179.334 129.448 203.131 1.00 152.19 ? 3923 ARG A CD    1 
ATOM   18086 N  NE    . ARG A 1 3923 ? 180.299 129.458 204.226 1.00 153.30 ? 3923 ARG A NE    1 
ATOM   18087 C  CZ    . ARG A 1 3923 ? 181.486 128.868 204.185 1.00 151.94 ? 3923 ARG A CZ    1 
ATOM   18088 N  NH1   . ARG A 1 3923 ? 181.897 128.217 203.110 1.00 150.12 ? 3923 ARG A NH1   1 
ATOM   18089 N  NH2   . ARG A 1 3923 ? 182.281 128.935 205.249 1.00 150.62 ? 3923 ARG A NH2   1 
ATOM   18090 N  N     . ILE A 1 3924 ? 180.852 125.078 201.277 1.00 140.87 ? 3924 ILE A N     1 
ATOM   18091 C  CA    . ILE A 1 3924 ? 182.087 124.306 201.276 1.00 141.73 ? 3924 ILE A CA    1 
ATOM   18092 C  C     . ILE A 1 3924 ? 183.253 125.203 201.664 1.00 141.51 ? 3924 ILE A C     1 
ATOM   18093 O  O     . ILE A 1 3924 ? 183.336 126.367 201.251 1.00 140.15 ? 3924 ILE A O     1 
ATOM   18094 C  CB    . ILE A 1 3924 ? 182.311 123.656 199.901 1.00 141.74 ? 3924 ILE A CB    1 
ATOM   18095 C  CG1   . ILE A 1 3924 ? 181.042 122.939 199.435 1.00 141.44 ? 3924 ILE A CG1   1 
ATOM   18096 C  CG2   . ILE A 1 3924 ? 183.474 122.678 199.953 1.00 140.61 ? 3924 ILE A CG2   1 
ATOM   18097 C  CD1   . ILE A 1 3924 ? 180.279 123.681 198.357 1.00 139.88 ? 3924 ILE A CD1   1 
ATOM   18098 N  N     . GLN A 1 3925 ? 184.159 124.660 202.473 1.00 138.45 ? 3925 GLN A N     1 
ATOM   18099 C  CA    . GLN A 1 3925 ? 185.287 125.429 202.980 1.00 138.97 ? 3925 GLN A CA    1 
ATOM   18100 C  C     . GLN A 1 3925 ? 186.227 125.844 201.854 1.00 137.87 ? 3925 GLN A C     1 
ATOM   18101 O  O     . GLN A 1 3925 ? 186.532 125.058 200.953 1.00 136.34 ? 3925 GLN A O     1 
ATOM   18102 C  CB    . GLN A 1 3925 ? 186.047 124.610 204.027 1.00 136.68 ? 3925 GLN A CB    1 
ATOM   18103 C  CG    . GLN A 1 3925 ? 187.492 125.042 204.284 1.00 137.49 ? 3925 GLN A CG    1 
ATOM   18104 C  CD    . GLN A 1 3925 ? 187.618 126.372 205.014 1.00 137.09 ? 3925 GLN A CD    1 
ATOM   18105 O  OE1   . GLN A 1 3925 ? 186.681 127.168 205.065 1.00 136.46 ? 3925 GLN A OE1   1 
ATOM   18106 N  NE2   . GLN A 1 3925 ? 188.791 126.614 205.587 1.00 135.70 ? 3925 GLN A NE2   1 
ATOM   18107 N  N     . GLY A 1 3926 ? 186.688 127.093 201.914 1.00 129.94 ? 3926 GLY A N     1 
ATOM   18108 C  CA    . GLY A 1 3926 ? 187.698 127.591 201.005 1.00 126.65 ? 3926 GLY A CA    1 
ATOM   18109 C  C     . GLY A 1 3926 ? 187.191 128.299 199.768 1.00 128.49 ? 3926 GLY A C     1 
ATOM   18110 O  O     . GLY A 1 3926 ? 188.011 128.811 198.995 1.00 128.82 ? 3926 GLY A O     1 
ATOM   18111 N  N     . LEU A 1 3927 ? 185.880 128.353 199.550 1.00 126.83 ? 3927 LEU A N     1 
ATOM   18112 C  CA    . LEU A 1 3927 ? 185.313 128.988 198.369 1.00 124.84 ? 3927 LEU A CA    1 
ATOM   18113 C  C     . LEU A 1 3927 ? 184.270 130.021 198.772 1.00 124.71 ? 3927 LEU A C     1 
ATOM   18114 O  O     . LEU A 1 3927 ? 183.606 129.881 199.804 1.00 125.70 ? 3927 LEU A O     1 
ATOM   18115 C  CB    . LEU A 1 3927 ? 184.682 127.957 197.423 1.00 123.33 ? 3927 LEU A CB    1 
ATOM   18116 C  CG    . LEU A 1 3927 ? 185.423 126.635 197.213 1.00 126.70 ? 3927 LEU A CG    1 
ATOM   18117 C  CD1   . LEU A 1 3927 ? 184.891 125.559 198.142 1.00 125.81 ? 3927 LEU A CD1   1 
ATOM   18118 C  CD2   . LEU A 1 3927 ? 185.325 126.192 195.762 1.00 125.85 ? 3927 LEU A CD2   1 
ATOM   18119 N  N     . THR A 1 3928 ? 184.137 131.059 197.951 1.00 121.91 ? 3928 THR A N     1 
ATOM   18120 C  CA    . THR A 1 3928 ? 183.126 132.082 198.163 1.00 120.64 ? 3928 THR A CA    1 
ATOM   18121 C  C     . THR A 1 3928 ? 181.737 131.501 197.895 1.00 122.04 ? 3928 THR A C     1 
ATOM   18122 O  O     . THR A 1 3928 ? 181.588 130.449 197.267 1.00 125.06 ? 3928 THR A O     1 
ATOM   18123 C  CB    . THR A 1 3928 ? 183.397 133.287 197.258 1.00 120.69 ? 3928 THR A CB    1 
ATOM   18124 O  OG1   . THR A 1 3928 ? 184.800 133.574 197.260 1.00 119.92 ? 3928 THR A OG1   1 
ATOM   18125 C  CG2   . THR A 1 3928 ? 182.658 134.524 197.756 1.00 119.35 ? 3928 THR A CG2   1 
ATOM   18126 N  N     . VAL A 1 3929 ? 180.711 132.196 198.392 1.00 119.24 ? 3929 VAL A N     1 
ATOM   18127 C  CA    . VAL A 1 3929 ? 179.344 131.689 198.280 1.00 121.13 ? 3929 VAL A CA    1 
ATOM   18128 C  C     . VAL A 1 3929 ? 178.933 131.563 196.815 1.00 123.90 ? 3929 VAL A C     1 
ATOM   18129 O  O     . VAL A 1 3929 ? 178.253 130.606 196.427 1.00 124.55 ? 3929 VAL A O     1 
ATOM   18130 C  CB    . VAL A 1 3929 ? 178.370 132.569 199.089 1.00 120.75 ? 3929 VAL A CB    1 
ATOM   18131 C  CG1   . VAL A 1 3929 ? 178.081 133.892 198.386 1.00 117.47 ? 3929 VAL A CG1   1 
ATOM   18132 C  CG2   . VAL A 1 3929 ? 177.078 131.813 199.360 1.00 122.24 ? 3929 VAL A CG2   1 
ATOM   18133 N  N     . GLU A 1 3930 ? 179.350 132.516 195.975 1.00 122.35 ? 3930 GLU A N     1 
ATOM   18134 C  CA    . GLU A 1 3930 ? 179.099 132.389 194.543 1.00 120.51 ? 3930 GLU A CA    1 
ATOM   18135 C  C     . GLU A 1 3930 ? 179.825 131.180 193.972 1.00 118.47 ? 3930 GLU A C     1 
ATOM   18136 O  O     . GLU A 1 3930 ? 179.260 130.418 193.175 1.00 121.50 ? 3930 GLU A O     1 
ATOM   18137 C  CB    . GLU A 1 3930 ? 179.526 133.664 193.816 1.00 119.68 ? 3930 GLU A CB    1 
ATOM   18138 C  CG    . GLU A 1 3930 ? 178.605 134.857 194.033 1.00 121.40 ? 3930 GLU A CG    1 
ATOM   18139 C  CD    . GLU A 1 3930 ? 177.349 134.806 193.179 1.00 122.96 ? 3930 GLU A CD    1 
ATOM   18140 O  OE1   . GLU A 1 3930 ? 177.058 133.743 192.591 1.00 121.46 ? 3930 GLU A OE1   1 
ATOM   18141 O  OE2   . GLU A 1 3930 ? 176.650 135.837 193.095 1.00 123.47 ? 3930 GLU A OE2   1 
ATOM   18142 N  N     . GLN A 1 3931 ? 181.078 130.980 194.383 1.00 108.26 ? 3931 GLN A N     1 
ATOM   18143 C  CA    . GLN A 1 3931 ? 181.812 129.799 193.951 1.00 110.14 ? 3931 GLN A CA    1 
ATOM   18144 C  C     . GLN A 1 3931 ? 181.114 128.527 194.408 1.00 113.19 ? 3931 GLN A C     1 
ATOM   18145 O  O     . GLN A 1 3931 ? 181.002 127.568 193.640 1.00 117.82 ? 3931 GLN A O     1 
ATOM   18146 C  CB    . GLN A 1 3931 ? 183.247 129.849 194.476 1.00 111.32 ? 3931 GLN A CB    1 
ATOM   18147 C  CG    . GLN A 1 3931 ? 184.108 130.917 193.818 1.00 110.48 ? 3931 GLN A CG    1 
ATOM   18148 C  CD    . GLN A 1 3931 ? 185.584 130.744 194.117 1.00 112.72 ? 3931 GLN A CD    1 
ATOM   18149 O  OE1   . GLN A 1 3931 ? 185.986 129.794 194.788 1.00 115.60 ? 3931 GLN A OE1   1 
ATOM   18150 N  NE2   . GLN A 1 3931 ? 186.400 131.664 193.618 1.00 109.67 ? 3931 GLN A NE2   1 
ATOM   18151 N  N     . ALA A 1 3932 ? 180.622 128.506 195.650 1.00 118.24 ? 3932 ALA A N     1 
ATOM   18152 C  CA    . ALA A 1 3932 ? 179.934 127.322 196.159 1.00 119.40 ? 3932 ALA A CA    1 
ATOM   18153 C  C     . ALA A 1 3932 ? 178.661 127.034 195.371 1.00 121.07 ? 3932 ALA A C     1 
ATOM   18154 O  O     . ALA A 1 3932 ? 178.355 125.871 195.073 1.00 122.79 ? 3932 ALA A O     1 
ATOM   18155 C  CB    . ALA A 1 3932 ? 179.617 127.496 197.643 1.00 120.43 ? 3932 ALA A CB    1 
ATOM   18156 N  N     . GLU A 1 3933 ? 177.896 128.077 195.038 1.00 122.39 ? 3933 GLU A N     1 
ATOM   18157 C  CA    . GLU A 1 3933 ? 176.726 127.884 194.189 1.00 122.35 ? 3933 GLU A CA    1 
ATOM   18158 C  C     . GLU A 1 3933 ? 177.126 127.334 192.828 1.00 122.30 ? 3933 GLU A C     1 
ATOM   18159 O  O     . GLU A 1 3933 ? 176.415 126.505 192.250 1.00 122.83 ? 3933 GLU A O     1 
ATOM   18160 C  CB    . GLU A 1 3933 ? 175.956 129.195 194.031 1.00 120.02 ? 3933 GLU A CB    1 
ATOM   18161 C  CG    . GLU A 1 3933 ? 175.462 129.792 195.333 1.00 122.10 ? 3933 GLU A CG    1 
ATOM   18162 C  CD    . GLU A 1 3933 ? 174.224 130.645 195.144 1.00 123.14 ? 3933 GLU A CD    1 
ATOM   18163 O  OE1   . GLU A 1 3933 ? 173.743 130.748 193.997 1.00 121.75 ? 3933 GLU A OE1   1 
ATOM   18164 O  OE2   . GLU A 1 3933 ? 173.735 131.213 196.142 1.00 123.53 ? 3933 GLU A OE2   1 
ATOM   18165 N  N     . ALA A 1 3934 ? 178.263 127.787 192.298 1.00 115.51 ? 3934 ALA A N     1 
ATOM   18166 C  CA    . ALA A 1 3934 ? 178.753 127.228 191.042 1.00 113.94 ? 3934 ALA A CA    1 
ATOM   18167 C  C     . ALA A 1 3934 ? 179.088 125.746 191.187 1.00 116.45 ? 3934 ALA A C     1 
ATOM   18168 O  O     . ALA A 1 3934 ? 178.818 124.951 190.279 1.00 117.94 ? 3934 ALA A O     1 
ATOM   18169 C  CB    . ALA A 1 3934 ? 179.969 128.014 190.559 1.00 113.84 ? 3934 ALA A CB    1 
ATOM   18170 N  N     . VAL A 1 3935 ? 179.689 125.358 192.317 1.00 114.52 ? 3935 VAL A N     1 
ATOM   18171 C  CA    . VAL A 1 3935 ? 179.979 123.942 192.552 1.00 114.79 ? 3935 VAL A CA    1 
ATOM   18172 C  C     . VAL A 1 3935 ? 178.695 123.127 192.580 1.00 115.75 ? 3935 VAL A C     1 
ATOM   18173 O  O     . VAL A 1 3935 ? 178.598 122.072 191.941 1.00 118.68 ? 3935 VAL A O     1 
ATOM   18174 C  CB    . VAL A 1 3935 ? 180.787 123.735 193.849 1.00 114.38 ? 3935 VAL A CB    1 
ATOM   18175 C  CG1   . VAL A 1 3935 ? 181.502 122.402 193.805 1.00 117.19 ? 3935 VAL A CG1   1 
ATOM   18176 C  CG2   . VAL A 1 3935 ? 181.814 124.811 194.025 1.00 112.63 ? 3935 VAL A CG2   1 
ATOM   18177 N  N     . VAL A 1 3936 ? 177.691 123.593 193.325 1.00 119.17 ? 3936 VAL A N     1 
ATOM   18178 C  CA    . VAL A 1 3936 ? 176.466 122.807 193.458 1.00 122.38 ? 3936 VAL A CA    1 
ATOM   18179 C  C     . VAL A 1 3936 ? 175.700 122.769 192.139 1.00 123.52 ? 3936 VAL A C     1 
ATOM   18180 O  O     . VAL A 1 3936 ? 175.000 121.793 191.843 1.00 122.68 ? 3936 VAL A O     1 
ATOM   18181 C  CB    . VAL A 1 3936 ? 175.598 123.325 194.623 1.00 124.80 ? 3936 VAL A CB    1 
ATOM   18182 C  CG1   . VAL A 1 3936 ? 176.451 123.563 195.856 1.00 124.47 ? 3936 VAL A CG1   1 
ATOM   18183 C  CG2   . VAL A 1 3936 ? 174.859 124.588 194.238 1.00 122.92 ? 3936 VAL A CG2   1 
ATOM   18184 N  N     . ARG A 1 3937 ? 175.815 123.823 191.325 1.00 120.98 ? 3937 ARG A N     1 
ATOM   18185 C  CA    . ARG A 1 3937 ? 175.230 123.774 189.987 1.00 119.33 ? 3937 ARG A CA    1 
ATOM   18186 C  C     . ARG A 1 3937 ? 175.975 122.788 189.097 1.00 120.80 ? 3937 ARG A C     1 
ATOM   18187 O  O     . ARG A 1 3937 ? 175.355 122.026 188.346 1.00 123.32 ? 3937 ARG A O     1 
ATOM   18188 C  CB    . ARG A 1 3937 ? 175.223 125.163 189.351 1.00 117.36 ? 3937 ARG A CB    1 
ATOM   18189 C  CG    . ARG A 1 3937 ? 174.208 126.122 189.942 1.00 115.54 ? 3937 ARG A CG    1 
ATOM   18190 C  CD    . ARG A 1 3937 ? 174.365 127.512 189.349 1.00 118.39 ? 3937 ARG A CD    1 
ATOM   18191 N  NE    . ARG A 1 3937 ? 173.762 128.541 190.187 1.00 121.25 ? 3937 ARG A NE    1 
ATOM   18192 C  CZ    . ARG A 1 3937 ? 172.653 129.199 189.880 1.00 120.01 ? 3937 ARG A CZ    1 
ATOM   18193 N  NH1   . ARG A 1 3937 ? 171.992 128.955 188.761 1.00 120.32 ? 3937 ARG A NH1   1 
ATOM   18194 N  NH2   . ARG A 1 3937 ? 172.195 130.124 190.719 1.00 118.35 ? 3937 ARG A NH2   1 
ATOM   18195 N  N     . LEU A 1 3938 ? 177.308 122.791 189.166 1.00 113.11 ? 3938 LEU A N     1 
ATOM   18196 C  CA    . LEU A 1 3938 ? 178.095 121.873 188.351 1.00 110.77 ? 3938 LEU A CA    1 
ATOM   18197 C  C     . LEU A 1 3938 ? 177.891 120.425 188.780 1.00 116.90 ? 3938 LEU A C     1 
ATOM   18198 O  O     . LEU A 1 3938 ? 178.121 119.506 187.986 1.00 120.37 ? 3938 LEU A O     1 
ATOM   18199 C  CB    . LEU A 1 3938 ? 179.575 122.255 188.424 1.00 109.07 ? 3938 LEU A CB    1 
ATOM   18200 C  CG    . LEU A 1 3938 ? 180.571 121.446 187.591 1.00 112.82 ? 3938 LEU A CG    1 
ATOM   18201 C  CD1   . LEU A 1 3938 ? 180.150 121.420 186.133 1.00 115.44 ? 3938 LEU A CD1   1 
ATOM   18202 C  CD2   . LEU A 1 3938 ? 181.972 122.016 187.735 1.00 115.47 ? 3938 LEU A CD2   1 
ATOM   18203 N  N     . SER A 1 3939 ? 177.446 120.203 190.018 1.00 117.89 ? 3939 SER A N     1 
ATOM   18204 C  CA    . SER A 1 3939 ? 177.243 118.852 190.526 1.00 115.23 ? 3939 SER A CA    1 
ATOM   18205 C  C     . SER A 1 3939 ? 176.118 118.109 189.817 1.00 116.14 ? 3939 SER A C     1 
ATOM   18206 O  O     . SER A 1 3939 ? 176.039 116.883 189.942 1.00 116.87 ? 3939 SER A O     1 
ATOM   18207 C  CB    . SER A 1 3939 ? 176.960 118.896 192.028 1.00 114.14 ? 3939 SER A CB    1 
ATOM   18208 O  OG    . SER A 1 3939 ? 175.734 119.553 192.294 1.00 115.83 ? 3939 SER A OG    1 
ATOM   18209 N  N     . CYS A 1 3940 ? 175.248 118.814 189.088 1.00 117.48 ? 3940 CYS A N     1 
ATOM   18210 C  CA    . CYS A 1 3940 ? 174.156 118.144 188.389 1.00 118.25 ? 3940 CYS A CA    1 
ATOM   18211 C  C     . CYS A 1 3940 ? 174.671 117.221 187.292 1.00 116.59 ? 3940 CYS A C     1 
ATOM   18212 O  O     . CYS A 1 3940 ? 174.047 116.195 187.001 1.00 115.50 ? 3940 CYS A O     1 
ATOM   18213 C  CB    . CYS A 1 3940 ? 173.196 119.179 187.803 1.00 117.97 ? 3940 CYS A CB    1 
ATOM   18214 S  SG    . CYS A 1 3940 ? 172.427 120.259 189.030 1.00 120.54 ? 3940 CYS A SG    1 
ATOM   18215 N  N     . LEU A 1 3941 ? 175.796 117.567 186.674 1.00 114.94 ? 3941 LEU A N     1 
ATOM   18216 C  CA    . LEU A 1 3941 ? 176.354 116.740 185.618 1.00 116.35 ? 3941 LEU A CA    1 
ATOM   18217 C  C     . LEU A 1 3941 ? 176.854 115.413 186.190 1.00 116.46 ? 3941 LEU A C     1 
ATOM   18218 O  O     . LEU A 1 3941 ? 177.308 115.353 187.336 1.00 116.70 ? 3941 LEU A O     1 
ATOM   18219 C  CB    . LEU A 1 3941 ? 177.490 117.477 184.916 1.00 115.38 ? 3941 LEU A CB    1 
ATOM   18220 C  CG    . LEU A 1 3941 ? 177.093 118.759 184.180 1.00 113.85 ? 3941 LEU A CG    1 
ATOM   18221 C  CD1   . LEU A 1 3941 ? 178.139 119.122 183.146 1.00 116.23 ? 3941 LEU A CD1   1 
ATOM   18222 C  CD2   . LEU A 1 3941 ? 175.726 118.615 183.525 1.00 114.65 ? 3941 LEU A CD2   1 
ATOM   18223 N  N     . PRO A 1 3942 ? 176.777 114.329 185.410 1.00 115.40 ? 3942 PRO A N     1 
ATOM   18224 C  CA    . PRO A 1 3942 ? 177.144 113.013 185.959 1.00 116.17 ? 3942 PRO A CA    1 
ATOM   18225 C  C     . PRO A 1 3942 ? 178.616 112.881 186.305 1.00 115.82 ? 3942 PRO A C     1 
ATOM   18226 O  O     . PRO A 1 3942 ? 178.954 112.183 187.270 1.00 114.56 ? 3942 PRO A O     1 
ATOM   18227 C  CB    . PRO A 1 3942 ? 176.733 112.035 184.846 1.00 115.53 ? 3942 PRO A CB    1 
ATOM   18228 C  CG    . PRO A 1 3942 ? 176.092 112.871 183.760 1.00 114.74 ? 3942 PRO A CG    1 
ATOM   18229 C  CD    . PRO A 1 3942 ? 176.548 114.271 183.959 1.00 113.75 ? 3942 PRO A CD    1 
ATOM   18230 N  N     . ALA A 1 3943 ? 179.506 113.528 185.551 1.00 116.72 ? 3943 ALA A N     1 
ATOM   18231 C  CA    . ALA A 1 3943 ? 180.931 113.421 185.839 1.00 117.57 ? 3943 ALA A CA    1 
ATOM   18232 C  C     . ALA A 1 3943 ? 181.337 114.224 187.067 1.00 119.11 ? 3943 ALA A C     1 
ATOM   18233 O  O     . ALA A 1 3943 ? 182.422 113.995 187.611 1.00 119.44 ? 3943 ALA A O     1 
ATOM   18234 C  CB    . ALA A 1 3943 ? 181.749 113.871 184.628 1.00 117.54 ? 3943 ALA A CB    1 
ATOM   18235 N  N     . PHE A 1 3944 ? 180.496 115.157 187.513 1.00 111.08 ? 3944 PHE A N     1 
ATOM   18236 C  CA    . PHE A 1 3944 ? 180.781 115.995 188.671 1.00 106.99 ? 3944 PHE A CA    1 
ATOM   18237 C  C     . PHE A 1 3944 ? 179.849 115.684 189.839 1.00 110.26 ? 3944 PHE A C     1 
ATOM   18238 O  O     . PHE A 1 3944 ? 179.540 116.564 190.644 1.00 112.86 ? 3944 PHE A O     1 
ATOM   18239 C  CB    . PHE A 1 3944 ? 180.685 117.471 188.292 1.00 108.32 ? 3944 PHE A CB    1 
ATOM   18240 C  CG    . PHE A 1 3944 ? 181.690 117.901 187.262 1.00 110.09 ? 3944 PHE A CG    1 
ATOM   18241 C  CD1   . PHE A 1 3944 ? 183.008 118.130 187.613 1.00 111.78 ? 3944 PHE A CD1   1 
ATOM   18242 C  CD2   . PHE A 1 3944 ? 181.314 118.072 185.940 1.00 109.05 ? 3944 PHE A CD2   1 
ATOM   18243 C  CE1   . PHE A 1 3944 ? 183.933 118.525 186.665 1.00 110.38 ? 3944 PHE A CE1   1 
ATOM   18244 C  CE2   . PHE A 1 3944 ? 182.234 118.466 184.989 1.00 107.78 ? 3944 PHE A CE2   1 
ATOM   18245 C  CZ    . PHE A 1 3944 ? 183.545 118.693 185.353 1.00 109.16 ? 3944 PHE A CZ    1 
ATOM   18246 N  N     . LYS A 1 3945 ? 179.390 114.433 189.936 1.00 120.45 ? 3945 LYS A N     1 
ATOM   18247 C  CA    . LYS A 1 3945 ? 178.416 114.076 190.964 1.00 122.47 ? 3945 LYS A CA    1 
ATOM   18248 C  C     . LYS A 1 3945 ? 178.997 114.224 192.365 1.00 123.49 ? 3945 LYS A C     1 
ATOM   18249 O  O     . LYS A 1 3945 ? 178.343 114.772 193.261 1.00 123.02 ? 3945 LYS A O     1 
ATOM   18250 C  CB    . LYS A 1 3945 ? 177.919 112.648 190.737 1.00 119.34 ? 3945 LYS A CB    1 
ATOM   18251 C  CG    . LYS A 1 3945 ? 177.140 112.067 191.906 1.00 119.42 ? 3945 LYS A CG    1 
ATOM   18252 C  CD    . LYS A 1 3945 ? 175.918 111.289 191.438 1.00 119.15 ? 3945 LYS A CD    1 
ATOM   18253 C  CE    . LYS A 1 3945 ? 176.186 110.541 190.141 1.00 118.63 ? 3945 LYS A CE    1 
ATOM   18254 N  NZ    . LYS A 1 3945 ? 175.313 109.343 190.003 1.00 119.15 ? 3945 LYS A NZ    1 
ATOM   18255 N  N     . ASP A 1 3946 ? 180.224 113.752 192.573 1.00 122.70 ? 3946 ASP A N     1 
ATOM   18256 C  CA    . ASP A 1 3946 ? 180.887 113.807 193.875 1.00 121.87 ? 3946 ASP A CA    1 
ATOM   18257 C  C     . ASP A 1 3946 ? 181.935 114.910 193.925 1.00 120.54 ? 3946 ASP A C     1 
ATOM   18258 O  O     . ASP A 1 3946 ? 183.004 114.742 194.518 1.00 120.56 ? 3946 ASP A O     1 
ATOM   18259 C  CB    . ASP A 1 3946 ? 181.513 112.456 194.207 1.00 122.79 ? 3946 ASP A CB    1 
ATOM   18260 C  CG    . ASP A 1 3946 ? 181.216 112.011 195.624 1.00 123.77 ? 3946 ASP A CG    1 
ATOM   18261 O  OD1   . ASP A 1 3946 ? 181.507 110.842 195.955 1.00 124.22 ? 3946 ASP A OD1   1 
ATOM   18262 O  OD2   . ASP A 1 3946 ? 180.692 112.829 196.408 1.00 123.06 ? 3946 ASP A OD2   1 
ATOM   18263 N  N     . LEU A 1 3947 ? 181.644 116.050 193.296 1.00 120.49 ? 3947 LEU A N     1 
ATOM   18264 C  CA    . LEU A 1 3947 ? 182.634 117.115 193.179 1.00 123.53 ? 3947 LEU A CA    1 
ATOM   18265 C  C     . LEU A 1 3947 ? 182.986 117.705 194.540 1.00 123.11 ? 3947 LEU A C     1 
ATOM   18266 O  O     . LEU A 1 3947 ? 184.157 117.999 194.810 1.00 123.92 ? 3947 LEU A O     1 
ATOM   18267 C  CB    . LEU A 1 3947 ? 182.113 118.195 192.232 1.00 122.42 ? 3947 LEU A CB    1 
ATOM   18268 C  CG    . LEU A 1 3947 ? 183.072 119.313 191.833 1.00 119.43 ? 3947 LEU A CG    1 
ATOM   18269 C  CD1   . LEU A 1 3947 ? 184.201 118.731 191.015 1.00 121.61 ? 3947 LEU A CD1   1 
ATOM   18270 C  CD2   . LEU A 1 3947 ? 182.339 120.372 191.033 1.00 118.83 ? 3947 LEU A CD2   1 
ATOM   18271 N  N     . ILE A 1 3948 ? 181.989 117.870 195.413 1.00 121.69 ? 3948 ILE A N     1 
ATOM   18272 C  CA    . ILE A 1 3948 ? 182.228 118.480 196.719 1.00 120.99 ? 3948 ILE A CA    1 
ATOM   18273 C  C     . ILE A 1 3948 ? 183.215 117.647 197.526 1.00 121.24 ? 3948 ILE A C     1 
ATOM   18274 O  O     . ILE A 1 3948 ? 184.118 118.185 198.179 1.00 121.86 ? 3948 ILE A O     1 
ATOM   18275 C  CB    . ILE A 1 3948 ? 180.898 118.667 197.472 1.00 120.49 ? 3948 ILE A CB    1 
ATOM   18276 C  CG1   . ILE A 1 3948 ? 179.984 119.631 196.713 1.00 120.76 ? 3948 ILE A CG1   1 
ATOM   18277 C  CG2   . ILE A 1 3948 ? 181.147 119.177 198.881 1.00 120.45 ? 3948 ILE A CG2   1 
ATOM   18278 C  CD1   . ILE A 1 3948 ? 178.839 118.948 195.997 1.00 121.68 ? 3948 ILE A CD1   1 
ATOM   18279 N  N     . ALA A 1 3949 ? 183.059 116.322 197.493 1.00 122.32 ? 3949 ALA A N     1 
ATOM   18280 C  CA    . ALA A 1 3949 ? 183.983 115.450 198.210 1.00 121.75 ? 3949 ALA A CA    1 
ATOM   18281 C  C     . ALA A 1 3949 ? 185.403 115.594 197.678 1.00 123.40 ? 3949 ALA A C     1 
ATOM   18282 O  O     . ALA A 1 3949 ? 186.366 115.598 198.452 1.00 124.19 ? 3949 ALA A O     1 
ATOM   18283 C  CB    . ALA A 1 3949 ? 183.519 113.997 198.115 1.00 121.66 ? 3949 ALA A CB    1 
ATOM   18284 N  N     . LYS A 1 3950 ? 185.554 115.707 196.356 1.00 122.14 ? 3950 LYS A N     1 
ATOM   18285 C  CA    . LYS A 1 3950 ? 186.885 115.858 195.777 1.00 121.56 ? 3950 LYS A CA    1 
ATOM   18286 C  C     . LYS A 1 3950 ? 187.524 117.182 196.179 1.00 121.88 ? 3950 LYS A C     1 
ATOM   18287 O  O     . LYS A 1 3950 ? 188.718 117.228 196.497 1.00 122.11 ? 3950 LYS A O     1 
ATOM   18288 C  CB    . LYS A 1 3950 ? 186.816 115.732 194.255 1.00 120.44 ? 3950 LYS A CB    1 
ATOM   18289 C  CG    . LYS A 1 3950 ? 186.670 114.300 193.771 1.00 120.30 ? 3950 LYS A CG    1 
ATOM   18290 C  CD    . LYS A 1 3950 ? 186.982 114.173 192.292 1.00 121.19 ? 3950 LYS A CD    1 
ATOM   18291 C  CE    . LYS A 1 3950 ? 186.894 112.726 191.841 1.00 121.50 ? 3950 LYS A CE    1 
ATOM   18292 N  NZ    . LYS A 1 3950 ? 185.485 112.249 191.817 1.00 121.36 ? 3950 LYS A NZ    1 
ATOM   18293 N  N     . VAL A 1 3951 ? 186.752 118.273 196.168 1.00 122.87 ? 3951 VAL A N     1 
ATOM   18294 C  CA    . VAL A 1 3951 ? 187.326 119.566 196.544 1.00 124.13 ? 3951 VAL A CA    1 
ATOM   18295 C  C     . VAL A 1 3951 ? 187.635 119.609 198.037 1.00 123.69 ? 3951 VAL A C     1 
ATOM   18296 O  O     . VAL A 1 3951 ? 188.555 120.313 198.471 1.00 123.78 ? 3951 VAL A O     1 
ATOM   18297 C  CB    . VAL A 1 3951 ? 186.415 120.731 196.106 1.00 123.96 ? 3951 VAL A CB    1 
ATOM   18298 C  CG1   . VAL A 1 3951 ? 185.891 120.503 194.701 1.00 124.74 ? 3951 VAL A CG1   1 
ATOM   18299 C  CG2   . VAL A 1 3951 ? 185.266 120.937 197.082 1.00 122.21 ? 3951 VAL A CG2   1 
ATOM   18300 N  N     . GLN A 1 3952 ? 186.870 118.876 198.850 1.00 125.76 ? 3952 GLN A N     1 
ATOM   18301 C  CA    . GLN A 1 3952 ? 187.166 118.835 200.280 1.00 124.64 ? 3952 GLN A CA    1 
ATOM   18302 C  C     . GLN A 1 3952 ? 188.336 117.911 200.595 1.00 124.94 ? 3952 GLN A C     1 
ATOM   18303 O  O     . GLN A 1 3952 ? 189.020 118.105 201.606 1.00 123.85 ? 3952 GLN A O     1 
ATOM   18304 C  CB    . GLN A 1 3952 ? 185.925 118.412 201.065 1.00 123.46 ? 3952 GLN A CB    1 
ATOM   18305 C  CG    . GLN A 1 3952 ? 185.016 119.570 201.439 1.00 124.72 ? 3952 GLN A CG    1 
ATOM   18306 C  CD    . GLN A 1 3952 ? 183.631 119.119 201.855 1.00 126.12 ? 3952 GLN A CD    1 
ATOM   18307 O  OE1   . GLN A 1 3952 ? 183.330 117.925 201.864 1.00 127.78 ? 3952 GLN A OE1   1 
ATOM   18308 N  NE2   . GLN A 1 3952 ? 182.779 120.074 202.207 1.00 124.43 ? 3952 GLN A NE2   1 
ATOM   18309 N  N     . ALA A 1 3953 ? 188.578 116.904 199.756 1.00 131.10 ? 3953 ALA A N     1 
ATOM   18310 C  CA    . ALA A 1 3953 ? 189.618 115.918 200.016 1.00 130.58 ? 3953 ALA A CA    1 
ATOM   18311 C  C     . ALA A 1 3953 ? 190.980 116.315 199.465 1.00 130.71 ? 3953 ALA A C     1 
ATOM   18312 O  O     . ALA A 1 3953 ? 191.964 115.620 199.740 1.00 131.78 ? 3953 ALA A O     1 
ATOM   18313 C  CB    . ALA A 1 3953 ? 189.211 114.561 199.434 1.00 130.21 ? 3953 ALA A CB    1 
ATOM   18314 N  N     . ASP A 1 3954 ? 191.067 117.398 198.700 1.00 137.74 ? 3954 ASP A N     1 
ATOM   18315 C  CA    . ASP A 1 3954 ? 192.320 117.831 198.096 1.00 139.17 ? 3954 ASP A CA    1 
ATOM   18316 C  C     . ASP A 1 3954 ? 192.849 119.042 198.855 1.00 140.01 ? 3954 ASP A C     1 
ATOM   18317 O  O     . ASP A 1 3954 ? 192.276 120.134 198.768 1.00 137.64 ? 3954 ASP A O     1 
ATOM   18318 C  CB    . ASP A 1 3954 ? 192.126 118.161 196.616 1.00 138.96 ? 3954 ASP A CB    1 
ATOM   18319 C  CG    . ASP A 1 3954 ? 193.297 118.923 196.028 1.00 139.68 ? 3954 ASP A CG    1 
ATOM   18320 O  OD1   . ASP A 1 3954 ? 194.456 118.595 196.360 1.00 137.80 ? 3954 ASP A OD1   1 
ATOM   18321 O  OD2   . ASP A 1 3954 ? 193.058 119.851 195.227 1.00 139.34 ? 3954 ASP A OD2   1 
ATOM   18322 N  N     . GLU A 1 3955 ? 193.940 118.845 199.598 1.00 140.26 ? 3955 GLU A N     1 
ATOM   18323 C  CA    . GLU A 1 3955 ? 194.557 119.946 200.330 1.00 138.79 ? 3955 GLU A CA    1 
ATOM   18324 C  C     . GLU A 1 3955 ? 195.264 120.924 199.401 1.00 137.41 ? 3955 GLU A C     1 
ATOM   18325 O  O     . GLU A 1 3955 ? 195.390 122.107 199.735 1.00 135.01 ? 3955 GLU A O     1 
ATOM   18326 C  CB    . GLU A 1 3955 ? 195.542 119.410 201.374 1.00 138.61 ? 3955 GLU A CB    1 
ATOM   18327 C  CG    . GLU A 1 3955 ? 194.914 118.607 202.516 1.00 137.75 ? 3955 GLU A CG    1 
ATOM   18328 C  CD    . GLU A 1 3955 ? 194.325 117.277 202.076 1.00 138.88 ? 3955 GLU A CD    1 
ATOM   18329 O  OE1   . GLU A 1 3955 ? 193.587 116.662 202.874 1.00 138.86 ? 3955 GLU A OE1   1 
ATOM   18330 O  OE2   . GLU A 1 3955 ? 194.604 116.842 200.939 1.00 139.47 ? 3955 GLU A OE2   1 
ATOM   18331 N  N     . GLN A 1 3956 ? 195.726 120.457 198.242 1.00 134.00 ? 3956 GLN A N     1 
ATOM   18332 C  CA    . GLN A 1 3956 ? 196.372 121.319 197.260 1.00 133.36 ? 3956 GLN A CA    1 
ATOM   18333 C  C     . GLN A 1 3956 ? 195.377 122.114 196.427 1.00 132.91 ? 3956 GLN A C     1 
ATOM   18334 O  O     . GLN A 1 3956 ? 195.752 122.635 195.371 1.00 131.14 ? 3956 GLN A O     1 
ATOM   18335 C  CB    . GLN A 1 3956 ? 197.271 120.486 196.339 1.00 131.40 ? 3956 GLN A CB    1 
ATOM   18336 C  CG    . GLN A 1 3956 ? 198.271 119.562 197.045 1.00 131.88 ? 3956 GLN A CG    1 
ATOM   18337 C  CD    . GLN A 1 3956 ? 198.863 120.135 198.330 1.00 132.55 ? 3956 GLN A CD    1 
ATOM   18338 O  OE1   . GLN A 1 3956 ? 199.120 121.336 198.440 1.00 132.24 ? 3956 GLN A OE1   1 
ATOM   18339 N  NE2   . GLN A 1 3956 ? 199.080 119.267 199.311 1.00 132.70 ? 3956 GLN A NE2   1 
ATOM   18340 N  N     . PHE A 1 3957 ? 194.119 122.201 196.861 1.00 126.16 ? 3957 PHE A N     1 
ATOM   18341 C  CA    . PHE A 1 3957 ? 193.133 122.992 196.134 1.00 125.99 ? 3957 PHE A CA    1 
ATOM   18342 C  C     . PHE A 1 3957 ? 193.358 124.484 196.345 1.00 124.65 ? 3957 PHE A C     1 
ATOM   18343 O  O     . PHE A 1 3957 ? 193.132 125.290 195.434 1.00 127.70 ? 3957 PHE A O     1 
ATOM   18344 C  CB    . PHE A 1 3957 ? 191.726 122.588 196.572 1.00 124.11 ? 3957 PHE A CB    1 
ATOM   18345 C  CG    . PHE A 1 3957 ? 190.635 123.247 195.786 1.00 124.91 ? 3957 PHE A CG    1 
ATOM   18346 C  CD1   . PHE A 1 3957 ? 190.335 122.822 194.505 1.00 124.05 ? 3957 PHE A CD1   1 
ATOM   18347 C  CD2   . PHE A 1 3957 ? 189.903 124.287 196.332 1.00 123.06 ? 3957 PHE A CD2   1 
ATOM   18348 C  CE1   . PHE A 1 3957 ? 189.331 123.425 193.780 1.00 123.97 ? 3957 PHE A CE1   1 
ATOM   18349 C  CE2   . PHE A 1 3957 ? 188.896 124.894 195.612 1.00 122.71 ? 3957 PHE A CE2   1 
ATOM   18350 C  CZ    . PHE A 1 3957 ? 188.610 124.463 194.335 1.00 125.12 ? 3957 PHE A CZ    1 
ATOM   18351 N  N     . GLY A 1 3958 ? 193.802 124.870 197.544 1.00 113.79 ? 3958 GLY A N     1 
ATOM   18352 C  CA    . GLY A 1 3958 ? 193.975 126.281 197.846 1.00 114.78 ? 3958 GLY A CA    1 
ATOM   18353 C  C     . GLY A 1 3958 ? 195.023 126.962 196.989 1.00 115.97 ? 3958 GLY A C     1 
ATOM   18354 O  O     . GLY A 1 3958 ? 194.815 128.087 196.528 1.00 115.50 ? 3958 GLY A O     1 
ATOM   18355 N  N     . ILE A 1 3959 ? 196.162 126.302 196.770 1.00 113.46 ? 3959 ILE A N     1 
ATOM   18356 C  CA    . ILE A 1 3959 ? 197.222 126.899 195.961 1.00 113.69 ? 3959 ILE A CA    1 
ATOM   18357 C  C     . ILE A 1 3959 ? 196.750 127.076 194.522 1.00 113.55 ? 3959 ILE A C     1 
ATOM   18358 O  O     . ILE A 1 3959 ? 196.985 128.117 193.896 1.00 113.53 ? 3959 ILE A O     1 
ATOM   18359 C  CB    . ILE A 1 3959 ? 198.506 126.050 196.046 1.00 114.65 ? 3959 ILE A CB    1 
ATOM   18360 C  CG1   . ILE A 1 3959 ? 199.530 126.471 194.984 1.00 114.70 ? 3959 ILE A CG1   1 
ATOM   18361 C  CG2   . ILE A 1 3959 ? 198.188 124.568 195.933 1.00 112.03 ? 3959 ILE A CG2   1 
ATOM   18362 C  CD1   . ILE A 1 3959 ? 199.938 127.934 195.050 1.00 112.43 ? 3959 ILE A CD1   1 
ATOM   18363 N  N     . TRP A 1 3960 ? 196.068 126.065 193.979 1.00 103.62 ? 3960 TRP A N     1 
ATOM   18364 C  CA    . TRP A 1 3960 ? 195.581 126.163 192.607 1.00 101.25 ? 3960 TRP A CA    1 
ATOM   18365 C  C     . TRP A 1 3960 ? 194.526 127.252 192.467 1.00 103.46 ? 3960 TRP A C     1 
ATOM   18366 O  O     . TRP A 1 3960 ? 194.510 127.981 191.469 1.00 107.42 ? 3960 TRP A O     1 
ATOM   18367 C  CB    . TRP A 1 3960 ? 195.019 124.821 192.141 1.00 100.48 ? 3960 TRP A CB    1 
ATOM   18368 C  CG    . TRP A 1 3960 ? 194.342 124.912 190.809 1.00 102.47 ? 3960 TRP A CG    1 
ATOM   18369 C  CD1   . TRP A 1 3960 ? 194.942 124.893 189.585 1.00 101.90 ? 3960 TRP A CD1   1 
ATOM   18370 C  CD2   . TRP A 1 3960 ? 192.938 125.052 190.566 1.00 103.94 ? 3960 TRP A CD2   1 
ATOM   18371 N  NE1   . TRP A 1 3960 ? 193.998 125.005 188.594 1.00 101.55 ? 3960 TRP A NE1   1 
ATOM   18372 C  CE2   . TRP A 1 3960 ? 192.760 125.106 189.170 1.00 102.93 ? 3960 TRP A CE2   1 
ATOM   18373 C  CE3   . TRP A 1 3960 ? 191.814 125.135 191.393 1.00 101.29 ? 3960 TRP A CE3   1 
ATOM   18374 C  CZ2   . TRP A 1 3960 ? 191.504 125.236 188.583 1.00 100.03 ? 3960 TRP A CZ2   1 
ATOM   18375 C  CZ3   . TRP A 1 3960 ? 190.569 125.265 190.807 1.00 100.21 ? 3960 TRP A CZ3   1 
ATOM   18376 C  CH2   . TRP A 1 3960 ? 190.424 125.315 189.417 1.00 99.60  ? 3960 TRP A CH2   1 
ATOM   18377 N  N     . LEU A 1 3961 ? 193.633 127.376 193.453 1.00 102.32 ? 3961 LEU A N     1 
ATOM   18378 C  CA    . LEU A 1 3961 ? 192.571 128.372 193.370 1.00 100.37 ? 3961 LEU A CA    1 
ATOM   18379 C  C     . LEU A 1 3961 ? 193.110 129.796 193.344 1.00 101.84 ? 3961 LEU A C     1 
ATOM   18380 O  O     . LEU A 1 3961 ? 192.467 130.680 192.768 1.00 99.26  ? 3961 LEU A O     1 
ATOM   18381 C  CB    . LEU A 1 3961 ? 191.601 128.203 194.539 1.00 98.25  ? 3961 LEU A CB    1 
ATOM   18382 C  CG    . LEU A 1 3961 ? 190.267 128.943 194.423 1.00 100.92 ? 3961 LEU A CG    1 
ATOM   18383 C  CD1   . LEU A 1 3961 ? 189.686 128.781 193.028 1.00 103.60 ? 3961 LEU A CD1   1 
ATOM   18384 C  CD2   . LEU A 1 3961 ? 189.285 128.457 195.476 1.00 101.51 ? 3961 LEU A CD2   1 
ATOM   18385 N  N     . ASP A 1 3962 ? 194.272 130.039 193.949 1.00 112.45 ? 3962 ASP A N     1 
ATOM   18386 C  CA    . ASP A 1 3962 ? 194.880 131.362 193.977 1.00 112.41 ? 3962 ASP A CA    1 
ATOM   18387 C  C     . ASP A 1 3962 ? 196.017 131.507 192.974 1.00 112.77 ? 3962 ASP A C     1 
ATOM   18388 O  O     . ASP A 1 3962 ? 196.717 132.525 192.988 1.00 113.61 ? 3962 ASP A O     1 
ATOM   18389 C  CB    . ASP A 1 3962 ? 195.383 131.681 195.387 1.00 116.02 ? 3962 ASP A CB    1 
ATOM   18390 C  CG    . ASP A 1 3962 ? 194.253 131.863 196.380 1.00 118.15 ? 3962 ASP A CG    1 
ATOM   18391 O  OD1   . ASP A 1 3962 ? 193.417 132.767 196.173 1.00 117.14 ? 3962 ASP A OD1   1 
ATOM   18392 O  OD2   . ASP A 1 3962 ? 194.202 131.102 197.369 1.00 118.55 ? 3962 ASP A OD2   1 
ATOM   18393 N  N     . SER A 1 3963 ? 196.222 130.517 192.110 1.00 103.88 ? 3963 SER A N     1 
ATOM   18394 C  CA    . SER A 1 3963 ? 197.297 130.586 191.132 1.00 102.76 ? 3963 SER A CA    1 
ATOM   18395 C  C     . SER A 1 3963 ? 197.021 131.672 190.098 1.00 105.35 ? 3963 SER A C     1 
ATOM   18396 O  O     . SER A 1 3963 ? 195.871 132.025 189.824 1.00 103.68 ? 3963 SER A O     1 
ATOM   18397 C  CB    . SER A 1 3963 ? 197.477 129.235 190.440 1.00 103.15 ? 3963 SER A CB    1 
ATOM   18398 O  OG    . SER A 1 3963 ? 196.246 128.761 189.925 1.00 105.55 ? 3963 SER A OG    1 
ATOM   18399 N  N     . SER A 1 3964 ? 198.102 132.212 189.530 1.00 104.12 ? 3964 SER A N     1 
ATOM   18400 C  CA    . SER A 1 3964 ? 197.967 133.266 188.529 1.00 102.92 ? 3964 SER A CA    1 
ATOM   18401 C  C     . SER A 1 3964 ? 197.246 132.764 187.284 1.00 101.69 ? 3964 SER A C     1 
ATOM   18402 O  O     . SER A 1 3964 ? 196.388 133.463 186.734 1.00 101.27 ? 3964 SER A O     1 
ATOM   18403 C  CB    . SER A 1 3964 ? 199.343 133.822 188.165 1.00 100.73 ? 3964 SER A CB    1 
ATOM   18404 O  OG    . SER A 1 3964 ? 200.196 132.797 187.685 1.00 100.65 ? 3964 SER A OG    1 
ATOM   18405 N  N     . SER A 1 3965 ? 197.580 131.559 186.826 1.00 98.96  ? 3965 SER A N     1 
ATOM   18406 C  CA    . SER A 1 3965 ? 196.965 130.956 185.644 1.00 96.72  ? 3965 SER A CA    1 
ATOM   18407 C  C     . SER A 1 3965 ? 196.495 129.553 186.003 1.00 97.75  ? 3965 SER A C     1 
ATOM   18408 O  O     . SER A 1 3965 ? 197.155 128.560 185.671 1.00 98.57  ? 3965 SER A O     1 
ATOM   18409 C  CB    . SER A 1 3965 ? 197.939 130.928 184.466 1.00 97.86  ? 3965 SER A CB    1 
ATOM   18410 O  OG    . SER A 1 3965 ? 199.014 130.040 184.718 1.00 102.91 ? 3965 SER A OG    1 
ATOM   18411 N  N     . PRO A 1 3966 ? 195.359 129.435 186.695 1.00 94.10  ? 3966 PRO A N     1 
ATOM   18412 C  CA    . PRO A 1 3966 ? 194.852 128.098 187.043 1.00 93.44  ? 3966 PRO A CA    1 
ATOM   18413 C  C     . PRO A 1 3966 ? 194.495 127.251 185.836 1.00 94.63  ? 3966 PRO A C     1 
ATOM   18414 O  O     . PRO A 1 3966 ? 194.510 126.017 185.932 1.00 98.16  ? 3966 PRO A O     1 
ATOM   18415 C  CB    . PRO A 1 3966 ? 193.617 128.405 187.901 1.00 92.98  ? 3966 PRO A CB    1 
ATOM   18416 C  CG    . PRO A 1 3966 ? 193.205 129.777 187.492 1.00 91.28  ? 3966 PRO A CG    1 
ATOM   18417 C  CD    . PRO A 1 3966 ? 194.475 130.506 187.183 1.00 94.39  ? 3966 PRO A CD    1 
ATOM   18418 N  N     . GLU A 1 3967 ? 194.173 127.875 184.701 1.00 89.65  ? 3967 GLU A N     1 
ATOM   18419 C  CA    . GLU A 1 3967 ? 193.759 127.124 183.522 1.00 89.70  ? 3967 GLU A CA    1 
ATOM   18420 C  C     . GLU A 1 3967 ? 194.862 126.220 182.987 1.00 95.41  ? 3967 GLU A C     1 
ATOM   18421 O  O     . GLU A 1 3967 ? 194.567 125.264 182.263 1.00 99.44  ? 3967 GLU A O     1 
ATOM   18422 C  CB    . GLU A 1 3967 ? 193.294 128.087 182.428 1.00 89.68  ? 3967 GLU A CB    1 
ATOM   18423 C  CG    . GLU A 1 3967 ? 194.422 128.712 181.627 1.00 92.97  ? 3967 GLU A CG    1 
ATOM   18424 C  CD    . GLU A 1 3967 ? 194.772 130.105 182.106 1.00 98.15  ? 3967 GLU A CD    1 
ATOM   18425 O  OE1   . GLU A 1 3967 ? 193.998 130.672 182.904 1.00 97.74  ? 3967 GLU A OE1   1 
ATOM   18426 O  OE2   . GLU A 1 3967 ? 195.820 130.635 181.683 1.00 99.67  ? 3967 GLU A OE2   1 
ATOM   18427 N  N     . GLN A 1 3968 ? 196.124 126.499 183.322 1.00 94.76  ? 3968 GLN A N     1 
ATOM   18428 C  CA    . GLN A 1 3968 ? 197.217 125.664 182.835 1.00 94.56  ? 3968 GLN A CA    1 
ATOM   18429 C  C     . GLN A 1 3968 ? 197.265 124.326 183.563 1.00 96.64  ? 3968 GLN A C     1 
ATOM   18430 O  O     . GLN A 1 3968 ? 197.645 123.307 182.975 1.00 99.35  ? 3968 GLN A O     1 
ATOM   18431 C  CB    . GLN A 1 3968 ? 198.547 126.401 182.988 1.00 92.73  ? 3968 GLN A CB    1 
ATOM   18432 C  CG    . GLN A 1 3968 ? 198.677 127.641 182.123 1.00 92.59  ? 3968 GLN A CG    1 
ATOM   18433 C  CD    . GLN A 1 3968 ? 198.638 127.322 180.643 1.00 97.73  ? 3968 GLN A CD    1 
ATOM   18434 O  OE1   . GLN A 1 3968 ? 197.668 127.638 179.954 1.00 98.69  ? 3968 GLN A OE1   1 
ATOM   18435 N  NE2   . GLN A 1 3968 ? 199.695 126.691 180.146 1.00 98.83  ? 3968 GLN A NE2   1 
ATOM   18436 N  N     . THR A 1 3969 ? 196.885 124.307 184.838 1.00 95.49  ? 3969 THR A N     1 
ATOM   18437 C  CA    . THR A 1 3969 ? 197.050 123.141 185.701 1.00 98.37  ? 3969 THR A CA    1 
ATOM   18438 C  C     . THR A 1 3969 ? 195.756 122.826 186.443 1.00 99.41  ? 3969 THR A C     1 
ATOM   18439 O  O     . THR A 1 3969 ? 195.740 122.620 187.659 1.00 98.74  ? 3969 THR A O     1 
ATOM   18440 C  CB    . THR A 1 3969 ? 198.203 123.358 186.678 1.00 99.88  ? 3969 THR A CB    1 
ATOM   18441 O  OG1   . THR A 1 3969 ? 198.240 122.284 187.626 1.00 100.97 ? 3969 THR A OG1   1 
ATOM   18442 C  CG2   . THR A 1 3969 ? 198.054 124.690 187.407 1.00 97.86  ? 3969 THR A CG2   1 
ATOM   18443 N  N     . VAL A 1 3970 ? 194.647 122.780 185.712 1.00 99.60  ? 3970 VAL A N     1 
ATOM   18444 C  CA    . VAL A 1 3970 ? 193.372 122.422 186.345 1.00 98.91  ? 3970 VAL A CA    1 
ATOM   18445 C  C     . VAL A 1 3970 ? 193.450 120.986 186.849 1.00 99.87  ? 3970 VAL A C     1 
ATOM   18446 O  O     . VAL A 1 3970 ? 193.813 120.077 186.076 1.00 98.38  ? 3970 VAL A O     1 
ATOM   18447 C  CB    . VAL A 1 3970 ? 192.209 122.594 185.355 1.00 97.92  ? 3970 VAL A CB    1 
ATOM   18448 C  CG1   . VAL A 1 3970 ? 190.890 122.231 186.017 1.00 97.95  ? 3970 VAL A CG1   1 
ATOM   18449 C  CG2   . VAL A 1 3970 ? 192.169 124.015 184.824 1.00 101.91 ? 3970 VAL A CG2   1 
ATOM   18450 N  N     . PRO A 1 3971 ? 193.136 120.720 188.114 1.00 103.58 ? 3971 PRO A N     1 
ATOM   18451 C  CA    . PRO A 1 3971 ? 193.275 119.358 188.638 1.00 102.11 ? 3971 PRO A CA    1 
ATOM   18452 C  C     . PRO A 1 3971 ? 192.256 118.407 188.034 1.00 105.29 ? 3971 PRO A C     1 
ATOM   18453 O  O     . PRO A 1 3971 ? 191.184 118.809 187.576 1.00 107.06 ? 3971 PRO A O     1 
ATOM   18454 C  CB    . PRO A 1 3971 ? 193.044 119.532 190.143 1.00 99.27  ? 3971 PRO A CB    1 
ATOM   18455 C  CG    . PRO A 1 3971 ? 192.202 120.754 190.249 1.00 99.58  ? 3971 PRO A CG    1 
ATOM   18456 C  CD    . PRO A 1 3971 ? 192.652 121.660 189.139 1.00 101.98 ? 3971 PRO A CD    1 
ATOM   18457 N  N     . TYR A 1 3972 ? 192.610 117.121 188.041 1.00 115.87 ? 3972 TYR A N     1 
ATOM   18458 C  CA    . TYR A 1 3972 ? 191.723 116.059 187.570 1.00 114.74 ? 3972 TYR A CA    1 
ATOM   18459 C  C     . TYR A 1 3972 ? 190.647 115.855 188.632 1.00 114.82 ? 3972 TYR A C     1 
ATOM   18460 O  O     . TYR A 1 3972 ? 190.751 115.010 189.524 1.00 117.12 ? 3972 TYR A O     1 
ATOM   18461 C  CB    . TYR A 1 3972 ? 192.512 114.781 187.309 1.00 114.73 ? 3972 TYR A CB    1 
ATOM   18462 C  CG    . TYR A 1 3972 ? 191.960 113.920 186.197 1.00 116.10 ? 3972 TYR A CG    1 
ATOM   18463 C  CD1   . TYR A 1 3972 ? 190.603 113.905 185.906 1.00 114.16 ? 3972 TYR A CD1   1 
ATOM   18464 C  CD2   . TYR A 1 3972 ? 192.802 113.119 185.436 1.00 117.50 ? 3972 TYR A CD2   1 
ATOM   18465 C  CE1   . TYR A 1 3972 ? 190.100 113.118 184.889 1.00 116.87 ? 3972 TYR A CE1   1 
ATOM   18466 C  CE2   . TYR A 1 3972 ? 192.308 112.329 184.418 1.00 118.16 ? 3972 TYR A CE2   1 
ATOM   18467 C  CZ    . TYR A 1 3972 ? 190.957 112.332 184.148 1.00 119.73 ? 3972 TYR A CZ    1 
ATOM   18468 O  OH    . TYR A 1 3972 ? 190.463 111.545 183.134 1.00 119.98 ? 3972 TYR A OH    1 
ATOM   18469 N  N     . LEU A 1 3973 ? 189.586 116.654 188.528 1.00 111.66 ? 3973 LEU A N     1 
ATOM   18470 C  CA    . LEU A 1 3973 ? 188.580 116.761 189.576 1.00 111.73 ? 3973 LEU A CA    1 
ATOM   18471 C  C     . LEU A 1 3973 ? 187.237 116.163 189.160 1.00 111.96 ? 3973 LEU A C     1 
ATOM   18472 O  O     . LEU A 1 3973 ? 186.210 116.459 189.778 1.00 111.01 ? 3973 LEU A O     1 
ATOM   18473 C  CB    . LEU A 1 3973 ? 188.427 118.227 189.986 1.00 111.59 ? 3973 LEU A CB    1 
ATOM   18474 C  CG    . LEU A 1 3973 ? 187.864 118.572 191.364 1.00 113.00 ? 3973 LEU A CG    1 
ATOM   18475 C  CD1   . LEU A 1 3973 ? 188.887 118.259 192.438 1.00 115.77 ? 3973 LEU A CD1   1 
ATOM   18476 C  CD2   . LEU A 1 3973 ? 187.489 120.041 191.409 1.00 110.90 ? 3973 LEU A CD2   1 
ATOM   18477 N  N     . TRP A 1 3974 ? 187.223 115.324 188.127 1.00 111.77 ? 3974 TRP A N     1 
ATOM   18478 C  CA    . TRP A 1 3974 ? 186.011 114.648 187.690 1.00 110.39 ? 3974 TRP A CA    1 
ATOM   18479 C  C     . TRP A 1 3974 ? 186.298 113.165 187.501 1.00 113.87 ? 3974 TRP A C     1 
ATOM   18480 O  O     . TRP A 1 3974 ? 187.442 112.754 187.289 1.00 114.73 ? 3974 TRP A O     1 
ATOM   18481 C  CB    . TRP A 1 3974 ? 185.458 115.254 186.391 1.00 110.77 ? 3974 TRP A CB    1 
ATOM   18482 C  CG    . TRP A 1 3974 ? 186.375 115.119 185.218 1.00 111.41 ? 3974 TRP A CG    1 
ATOM   18483 C  CD1   . TRP A 1 3974 ? 186.381 114.114 184.297 1.00 112.65 ? 3974 TRP A CD1   1 
ATOM   18484 C  CD2   . TRP A 1 3974 ? 187.421 116.019 184.838 1.00 109.55 ? 3974 TRP A CD2   1 
ATOM   18485 N  NE1   . TRP A 1 3974 ? 187.366 114.332 183.365 1.00 112.53 ? 3974 TRP A NE1   1 
ATOM   18486 C  CE2   . TRP A 1 3974 ? 188.019 115.496 183.675 1.00 110.42 ? 3974 TRP A CE2   1 
ATOM   18487 C  CE3   . TRP A 1 3974 ? 187.910 117.216 185.367 1.00 110.50 ? 3974 TRP A CE3   1 
ATOM   18488 C  CZ2   . TRP A 1 3974 ? 189.080 116.127 183.034 1.00 111.71 ? 3974 TRP A CZ2   1 
ATOM   18489 C  CZ3   . TRP A 1 3974 ? 188.964 117.841 184.729 1.00 112.81 ? 3974 TRP A CZ3   1 
ATOM   18490 C  CH2   . TRP A 1 3974 ? 189.538 117.296 183.575 1.00 112.87 ? 3974 TRP A CH2   1 
ATOM   18491 N  N     . SER A 1 3975 ? 185.241 112.363 187.582 1.00 123.38 ? 3975 SER A N     1 
ATOM   18492 C  CA    . SER A 1 3975 ? 185.342 110.911 187.518 1.00 124.80 ? 3975 SER A CA    1 
ATOM   18493 C  C     . SER A 1 3975 ? 184.746 110.407 186.211 1.00 125.76 ? 3975 SER A C     1 
ATOM   18494 O  O     . SER A 1 3975 ? 183.638 110.804 185.835 1.00 124.73 ? 3975 SER A O     1 
ATOM   18495 C  CB    . SER A 1 3975 ? 184.630 110.261 188.705 1.00 123.34 ? 3975 SER A CB    1 
ATOM   18496 O  OG    . SER A 1 3975 ? 183.243 110.551 188.687 1.00 124.94 ? 3975 SER A OG    1 
ATOM   18497 N  N     . GLU A 1 3976 ? 185.484 109.537 185.524 1.00 135.67 ? 3976 GLU A N     1 
ATOM   18498 C  CA    . GLU A 1 3976 ? 185.026 108.918 184.289 1.00 136.49 ? 3976 GLU A CA    1 
ATOM   18499 C  C     . GLU A 1 3976 ? 185.385 107.440 184.296 1.00 138.61 ? 3976 GLU A C     1 
ATOM   18500 O  O     . GLU A 1 3976 ? 186.450 107.053 184.786 1.00 138.34 ? 3976 GLU A O     1 
ATOM   18501 C  CB    . GLU A 1 3976 ? 185.639 109.602 183.061 1.00 135.95 ? 3976 GLU A CB    1 
ATOM   18502 C  CG    . GLU A 1 3976 ? 187.138 109.821 183.156 1.00 136.50 ? 3976 GLU A CG    1 
ATOM   18503 C  CD    . GLU A 1 3976 ? 187.641 110.834 182.147 1.00 138.96 ? 3976 GLU A CD    1 
ATOM   18504 O  OE1   . GLU A 1 3976 ? 186.944 111.845 181.920 1.00 137.64 ? 3976 GLU A OE1   1 
ATOM   18505 O  OE2   . GLU A 1 3976 ? 188.735 110.620 181.583 1.00 139.13 ? 3976 GLU A OE2   1 
ATOM   18506 N  N     . GLU A 1 3977 ? 184.487 106.616 183.751 1.00 145.29 ? 3977 GLU A N     1 
ATOM   18507 C  CA    . GLU A 1 3977 ? 184.756 105.184 183.661 1.00 144.54 ? 3977 GLU A CA    1 
ATOM   18508 C  C     . GLU A 1 3977 ? 185.746 104.873 182.547 1.00 142.81 ? 3977 GLU A C     1 
ATOM   18509 O  O     . GLU A 1 3977 ? 186.564 103.955 182.680 1.00 141.86 ? 3977 GLU A O     1 
ATOM   18510 C  CB    . GLU A 1 3977 ? 183.454 104.414 183.436 1.00 143.75 ? 3977 GLU A CB    1 
ATOM   18511 C  CG    . GLU A 1 3977 ? 182.402 104.615 184.519 1.00 143.81 ? 3977 GLU A CG    1 
ATOM   18512 C  CD    . GLU A 1 3977 ? 181.578 105.873 184.314 1.00 144.03 ? 3977 GLU A CD    1 
ATOM   18513 O  OE1   . GLU A 1 3977 ? 181.813 106.584 183.314 1.00 143.82 ? 3977 GLU A OE1   1 
ATOM   18514 O  OE2   . GLU A 1 3977 ? 180.696 106.152 185.153 1.00 145.64 ? 3977 GLU A OE2   1 
ATOM   18515 N  N     . THR A 1 3978 ? 185.686 105.622 181.454 1.00 142.87 ? 3978 THR A N     1 
ATOM   18516 C  CA    . THR A 1 3978 ? 186.544 105.493 180.290 1.00 143.91 ? 3978 THR A CA    1 
ATOM   18517 C  C     . THR A 1 3978 ? 187.363 106.768 180.149 1.00 143.79 ? 3978 THR A C     1 
ATOM   18518 O  O     . THR A 1 3978 ? 186.834 107.867 180.355 1.00 142.34 ? 3978 THR A O     1 
ATOM   18519 C  CB    . THR A 1 3978 ? 185.697 105.240 179.027 1.00 145.65 ? 3978 THR A CB    1 
ATOM   18520 O  OG1   . THR A 1 3978 ? 186.518 105.265 177.853 1.00 144.55 ? 3978 THR A OG1   1 
ATOM   18521 C  CG2   . THR A 1 3978 ? 184.585 106.274 178.897 1.00 144.13 ? 3978 THR A CG2   1 
ATOM   18522 N  N     . PRO A 1 3979 ? 188.653 106.666 179.824 1.00 138.63 ? 3979 PRO A N     1 
ATOM   18523 C  CA    . PRO A 1 3979 ? 189.483 107.870 179.827 1.00 137.23 ? 3979 PRO A CA    1 
ATOM   18524 C  C     . PRO A 1 3979 ? 189.196 108.771 178.634 1.00 138.44 ? 3979 PRO A C     1 
ATOM   18525 O  O     . PRO A 1 3979 ? 189.134 108.329 177.483 1.00 137.48 ? 3979 PRO A O     1 
ATOM   18526 C  CB    . PRO A 1 3979 ? 190.903 107.296 179.815 1.00 135.54 ? 3979 PRO A CB    1 
ATOM   18527 C  CG    . PRO A 1 3979 ? 190.754 105.940 179.084 1.00 136.76 ? 3979 PRO A CG    1 
ATOM   18528 C  CD    . PRO A 1 3979 ? 189.256 105.701 178.890 1.00 136.89 ? 3979 PRO A CD    1 
ATOM   18529 N  N     . ALA A 1 3980 ? 189.033 110.056 178.926 1.00 129.92 ? 3980 ALA A N     1 
ATOM   18530 C  CA    . ALA A 1 3980 ? 188.459 111.000 177.983 1.00 127.73 ? 3980 ALA A CA    1 
ATOM   18531 C  C     . ALA A 1 3980 ? 189.484 111.458 176.956 1.00 124.68 ? 3980 ALA A C     1 
ATOM   18532 O  O     . ALA A 1 3980 ? 190.692 111.461 177.204 1.00 125.23 ? 3980 ALA A O     1 
ATOM   18533 C  CB    . ALA A 1 3980 ? 187.890 112.215 178.719 1.00 124.56 ? 3980 ALA A CB    1 
ATOM   18534 N  N     . THR A 1 3981 ? 188.976 111.838 175.788 1.00 106.25 ? 3981 THR A N     1 
ATOM   18535 C  CA    . THR A 1 3981 ? 189.799 112.426 174.752 1.00 109.53 ? 3981 THR A CA    1 
ATOM   18536 C  C     . THR A 1 3981 ? 190.255 113.819 175.179 1.00 109.83 ? 3981 THR A C     1 
ATOM   18537 O  O     . THR A 1 3981 ? 189.669 114.422 176.082 1.00 108.45 ? 3981 THR A O     1 
ATOM   18538 C  CB    . THR A 1 3981 ? 189.019 112.500 173.442 1.00 111.18 ? 3981 THR A CB    1 
ATOM   18539 O  OG1   . THR A 1 3981 ? 188.302 113.740 173.382 1.00 111.04 ? 3981 THR A OG1   1 
ATOM   18540 C  CG2   . THR A 1 3981 ? 188.033 111.347 173.347 1.00 111.70 ? 3981 THR A CG2   1 
ATOM   18541 N  N     . PRO A 1 3982 ? 191.317 114.345 174.560 1.00 102.90 ? 3982 PRO A N     1 
ATOM   18542 C  CA    . PRO A 1 3982 ? 191.767 115.700 174.919 1.00 100.68 ? 3982 PRO A CA    1 
ATOM   18543 C  C     . PRO A 1 3982 ? 190.681 116.755 174.795 1.00 97.41  ? 3982 PRO A C     1 
ATOM   18544 O  O     . PRO A 1 3982 ? 190.651 117.692 175.601 1.00 96.21  ? 3982 PRO A O     1 
ATOM   18545 C  CB    . PRO A 1 3982 ? 192.924 115.964 173.940 1.00 98.42  ? 3982 PRO A CB    1 
ATOM   18546 C  CG    . PRO A 1 3982 ? 192.890 114.836 172.943 1.00 94.85  ? 3982 PRO A CG    1 
ATOM   18547 C  CD    . PRO A 1 3982 ? 192.258 113.685 173.641 1.00 98.04  ? 3982 PRO A CD    1 
ATOM   18548 N  N     . ILE A 1 3983 ? 189.784 116.632 173.814 1.00 91.47  ? 3983 ILE A N     1 
ATOM   18549 C  CA    . ILE A 1 3983 ? 188.696 117.596 173.686 1.00 88.07  ? 3983 ILE A CA    1 
ATOM   18550 C  C     . ILE A 1 3983 ? 187.756 117.509 174.883 1.00 92.30  ? 3983 ILE A C     1 
ATOM   18551 O  O     . ILE A 1 3983 ? 187.337 118.533 175.435 1.00 100.04 ? 3983 ILE A O     1 
ATOM   18552 C  CB    . ILE A 1 3983 ? 187.944 117.392 172.359 1.00 88.52  ? 3983 ILE A CB    1 
ATOM   18553 C  CG1   . ILE A 1 3983 ? 188.873 117.632 171.167 1.00 90.14  ? 3983 ILE A CG1   1 
ATOM   18554 C  CG2   . ILE A 1 3983 ? 186.752 118.327 172.280 1.00 90.72  ? 3983 ILE A CG2   1 
ATOM   18555 C  CD1   . ILE A 1 3983 ? 189.498 116.373 170.602 1.00 93.41  ? 3983 ILE A CD1   1 
ATOM   18556 N  N     . GLY A 1 3984 ? 187.407 116.292 175.305 1.00 94.37  ? 3984 GLY A N     1 
ATOM   18557 C  CA    . GLY A 1 3984 ? 186.555 116.144 176.476 1.00 98.03  ? 3984 GLY A CA    1 
ATOM   18558 C  C     . GLY A 1 3984 ? 187.221 116.643 177.744 1.00 97.35  ? 3984 GLY A C     1 
ATOM   18559 O  O     . GLY A 1 3984 ? 186.572 117.244 178.607 1.00 93.03  ? 3984 GLY A O     1 
ATOM   18560 N  N     . GLN A 1 3985 ? 188.526 116.395 177.876 1.00 98.54  ? 3985 GLN A N     1 
ATOM   18561 C  CA    . GLN A 1 3985 ? 189.271 116.935 179.006 1.00 95.58  ? 3985 GLN A CA    1 
ATOM   18562 C  C     . GLN A 1 3985 ? 189.237 118.456 179.002 1.00 98.55  ? 3985 GLN A C     1 
ATOM   18563 O  O     . GLN A 1 3985 ? 189.054 119.084 180.051 1.00 101.19 ? 3985 GLN A O     1 
ATOM   18564 C  CB    . GLN A 1 3985 ? 190.713 116.429 178.968 1.00 93.23  ? 3985 GLN A CB    1 
ATOM   18565 C  CG    . GLN A 1 3985 ? 191.085 115.512 180.117 1.00 95.42  ? 3985 GLN A CG    1 
ATOM   18566 C  CD    . GLN A 1 3985 ? 192.581 115.450 180.347 1.00 100.90 ? 3985 GLN A CD    1 
ATOM   18567 O  OE1   . GLN A 1 3985 ? 193.369 115.813 179.474 1.00 102.64 ? 3985 GLN A OE1   1 
ATOM   18568 N  NE2   . GLN A 1 3985 ? 192.980 114.989 181.525 1.00 101.13 ? 3985 GLN A NE2   1 
ATOM   18569 N  N     . ALA A 1 3986 ? 189.404 119.066 177.826 1.00 87.70  ? 3986 ALA A N     1 
ATOM   18570 C  CA    . ALA A 1 3986 ? 189.333 120.519 177.726 1.00 80.59  ? 3986 ALA A CA    1 
ATOM   18571 C  C     . ALA A 1 3986 ? 187.946 121.031 178.088 1.00 81.55  ? 3986 ALA A C     1 
ATOM   18572 O  O     . ALA A 1 3986 ? 187.813 122.080 178.722 1.00 89.00  ? 3986 ALA A O     1 
ATOM   18573 C  CB    . ALA A 1 3986 ? 189.723 120.970 176.319 1.00 82.00  ? 3986 ALA A CB    1 
ATOM   18574 N  N     . ILE A 1 3987 ? 186.899 120.304 177.691 1.00 85.30  ? 3987 ILE A N     1 
ATOM   18575 C  CA    . ILE A 1 3987 ? 185.536 120.716 178.026 1.00 90.63  ? 3987 ILE A CA    1 
ATOM   18576 C  C     . ILE A 1 3987 ? 185.314 120.671 179.534 1.00 92.95  ? 3987 ILE A C     1 
ATOM   18577 O  O     . ILE A 1 3987 ? 184.727 121.590 180.123 1.00 93.28  ? 3987 ILE A O     1 
ATOM   18578 C  CB    . ILE A 1 3987 ? 184.515 119.835 177.282 1.00 87.44  ? 3987 ILE A CB    1 
ATOM   18579 C  CG1   . ILE A 1 3987 ? 184.627 120.043 175.773 1.00 86.50  ? 3987 ILE A CG1   1 
ATOM   18580 C  CG2   . ILE A 1 3987 ? 183.107 120.148 177.751 1.00 89.09  ? 3987 ILE A CG2   1 
ATOM   18581 C  CD1   . ILE A 1 3987 ? 183.534 119.369 174.981 1.00 88.81  ? 3987 ILE A CD1   1 
ATOM   18582 N  N     . HIS A 1 3988 ? 185.765 119.594 180.180 1.00 98.52  ? 3988 HIS A N     1 
ATOM   18583 C  CA    . HIS A 1 3988 ? 185.605 119.491 181.627 1.00 96.53  ? 3988 HIS A CA    1 
ATOM   18584 C  C     . HIS A 1 3988 ? 186.414 120.563 182.350 1.00 98.43  ? 3988 HIS A C     1 
ATOM   18585 O  O     . HIS A 1 3988 ? 185.948 121.142 183.339 1.00 99.43  ? 3988 HIS A O     1 
ATOM   18586 C  CB    . HIS A 1 3988 ? 185.997 118.093 182.100 1.00 96.59  ? 3988 HIS A CB    1 
ATOM   18587 C  CG    . HIS A 1 3988 ? 184.978 117.045 181.780 1.00 101.36 ? 3988 HIS A CG    1 
ATOM   18588 N  ND1   . HIS A 1 3988 ? 185.224 116.007 180.908 1.00 104.10 ? 3988 HIS A ND1   1 
ATOM   18589 C  CD2   . HIS A 1 3988 ? 183.704 116.881 182.210 1.00 102.03 ? 3988 HIS A CD2   1 
ATOM   18590 C  CE1   . HIS A 1 3988 ? 184.148 115.246 180.818 1.00 102.17 ? 3988 HIS A CE1   1 
ATOM   18591 N  NE2   . HIS A 1 3988 ? 183.212 115.754 181.598 1.00 100.84 ? 3988 HIS A NE2   1 
ATOM   18592 N  N     . ARG A 1 3989 ? 187.627 120.845 181.867 1.00 90.61  ? 3989 ARG A N     1 
ATOM   18593 C  CA    . ARG A 1 3989 ? 188.410 121.936 182.436 1.00 83.31  ? 3989 ARG A CA    1 
ATOM   18594 C  C     . ARG A 1 3989 ? 187.710 123.274 182.234 1.00 84.00  ? 3989 ARG A C     1 
ATOM   18595 O  O     . ARG A 1 3989 ? 187.777 124.151 183.099 1.00 91.57  ? 3989 ARG A O     1 
ATOM   18596 C  CB    . ARG A 1 3989 ? 189.808 121.961 181.819 1.00 86.50  ? 3989 ARG A CB    1 
ATOM   18597 C  CG    . ARG A 1 3989 ? 190.669 120.759 182.170 1.00 85.64  ? 3989 ARG A CG    1 
ATOM   18598 C  CD    . ARG A 1 3989 ? 192.146 121.091 182.059 1.00 88.71  ? 3989 ARG A CD    1 
ATOM   18599 N  NE    . ARG A 1 3989 ? 192.978 119.894 182.042 1.00 94.52  ? 3989 ARG A NE    1 
ATOM   18600 C  CZ    . ARG A 1 3989 ? 193.490 119.355 180.945 1.00 96.29  ? 3989 ARG A CZ    1 
ATOM   18601 N  NH1   . ARG A 1 3989 ? 193.279 119.884 179.751 1.00 91.61  ? 3989 ARG A NH1   1 
ATOM   18602 N  NH2   . ARG A 1 3989 ? 194.234 118.257 181.048 1.00 93.48  ? 3989 ARG A NH2   1 
ATOM   18603 N  N     . LEU A 1 3990 ? 187.045 123.450 181.091 1.00 78.03  ? 3990 LEU A N     1 
ATOM   18604 C  CA    . LEU A 1 3990 ? 186.278 124.666 180.846 1.00 75.35  ? 3990 LEU A CA    1 
ATOM   18605 C  C     . LEU A 1 3990 ? 185.160 124.822 181.863 1.00 77.25  ? 3990 LEU A C     1 
ATOM   18606 O  O     . LEU A 1 3990 ? 184.955 125.910 182.415 1.00 78.05  ? 3990 LEU A O     1 
ATOM   18607 C  CB    . LEU A 1 3990 ? 185.714 124.640 179.425 1.00 68.85  ? 3990 LEU A CB    1 
ATOM   18608 C  CG    . LEU A 1 3990 ? 184.881 125.821 178.929 1.00 71.15  ? 3990 LEU A CG    1 
ATOM   18609 C  CD1   . LEU A 1 3990 ? 185.710 127.087 178.867 1.00 75.68  ? 3990 LEU A CD1   1 
ATOM   18610 C  CD2   . LEU A 1 3990 ? 184.284 125.507 177.568 1.00 78.92  ? 3990 LEU A CD2   1 
ATOM   18611 N  N     . LEU A 1 3991 ? 184.429 123.738 182.127 1.00 88.58  ? 3991 LEU A N     1 
ATOM   18612 C  CA    . LEU A 1 3991 ? 183.371 123.788 183.132 1.00 87.94  ? 3991 LEU A CA    1 
ATOM   18613 C  C     . LEU A 1 3991 ? 183.936 124.114 184.509 1.00 89.45  ? 3991 LEU A C     1 
ATOM   18614 O  O     . LEU A 1 3991 ? 183.385 124.953 185.236 1.00 89.12  ? 3991 LEU A O     1 
ATOM   18615 C  CB    . LEU A 1 3991 ? 182.616 122.461 183.162 1.00 88.69  ? 3991 LEU A CB    1 
ATOM   18616 C  CG    . LEU A 1 3991 ? 181.690 122.198 181.976 1.00 91.49  ? 3991 LEU A CG    1 
ATOM   18617 C  CD1   . LEU A 1 3991 ? 181.147 120.785 182.031 1.00 90.76  ? 3991 LEU A CD1   1 
ATOM   18618 C  CD2   . LEU A 1 3991 ? 180.557 123.207 181.961 1.00 86.24  ? 3991 LEU A CD2   1 
ATOM   18619 N  N     . LEU A 1 3992 ? 185.045 123.468 184.879 1.00 88.16  ? 3992 LEU A N     1 
ATOM   18620 C  CA    . LEU A 1 3992 ? 185.647 123.714 186.186 1.00 86.21  ? 3992 LEU A CA    1 
ATOM   18621 C  C     . LEU A 1 3992 ? 186.122 125.155 186.317 1.00 87.75  ? 3992 LEU A C     1 
ATOM   18622 O  O     . LEU A 1 3992 ? 185.934 125.785 187.363 1.00 83.07  ? 3992 LEU A O     1 
ATOM   18623 C  CB    . LEU A 1 3992 ? 186.804 122.745 186.423 1.00 85.82  ? 3992 LEU A CB    1 
ATOM   18624 C  CG    . LEU A 1 3992 ? 186.419 121.346 186.903 1.00 86.98  ? 3992 LEU A CG    1 
ATOM   18625 C  CD1   . LEU A 1 3992 ? 187.647 120.457 186.999 1.00 85.81  ? 3992 LEU A CD1   1 
ATOM   18626 C  CD2   . LEU A 1 3992 ? 185.701 121.422 188.238 1.00 84.64  ? 3992 LEU A CD2   1 
ATOM   18627 N  N     . ILE A 1 3993 ? 186.745 125.694 185.267 1.00 84.59  ? 3993 ILE A N     1 
ATOM   18628 C  CA    . ILE A 1 3993 ? 187.240 127.065 185.312 1.00 74.78  ? 3993 ILE A CA    1 
ATOM   18629 C  C     . ILE A 1 3993 ? 186.082 128.048 185.397 1.00 77.06  ? 3993 ILE A C     1 
ATOM   18630 O  O     . ILE A 1 3993 ? 186.132 129.018 186.162 1.00 88.77  ? 3993 ILE A O     1 
ATOM   18631 C  CB    . ILE A 1 3993 ? 188.140 127.344 184.095 1.00 74.35  ? 3993 ILE A CB    1 
ATOM   18632 C  CG1   . ILE A 1 3993 ? 189.533 126.758 184.322 1.00 74.60  ? 3993 ILE A CG1   1 
ATOM   18633 C  CG2   . ILE A 1 3993 ? 188.235 128.836 183.824 1.00 77.30  ? 3993 ILE A CG2   1 
ATOM   18634 C  CD1   . ILE A 1 3993 ? 190.307 127.446 185.420 1.00 78.26  ? 3993 ILE A CD1   1 
ATOM   18635 N  N     . GLN A 1 3994 ? 185.018 127.814 184.625 1.00 77.77  ? 3994 GLN A N     1 
ATOM   18636 C  CA    . GLN A 1 3994 ? 183.857 128.694 184.696 1.00 80.27  ? 3994 GLN A CA    1 
ATOM   18637 C  C     . GLN A 1 3994 ? 183.247 128.682 186.090 1.00 83.67  ? 3994 GLN A C     1 
ATOM   18638 O  O     . GLN A 1 3994 ? 182.868 129.733 186.620 1.00 83.20  ? 3994 GLN A O     1 
ATOM   18639 C  CB    . GLN A 1 3994 ? 182.816 128.285 183.654 1.00 79.60  ? 3994 GLN A CB    1 
ATOM   18640 C  CG    . GLN A 1 3994 ? 181.408 128.752 183.982 1.00 76.39  ? 3994 GLN A CG    1 
ATOM   18641 C  CD    . GLN A 1 3994 ? 180.409 128.407 182.900 1.00 80.86  ? 3994 GLN A CD    1 
ATOM   18642 O  OE1   . GLN A 1 3994 ? 179.701 127.405 182.990 1.00 87.35  ? 3994 GLN A OE1   1 
ATOM   18643 N  NE2   . GLN A 1 3994 ? 180.344 129.239 181.868 1.00 82.93  ? 3994 GLN A NE2   1 
ATOM   18644 N  N     . ALA A 1 3995 ? 183.149 127.502 186.705 1.00 91.00  ? 3995 ALA A N     1 
ATOM   18645 C  CA    . ALA A 1 3995 ? 182.554 127.420 188.035 1.00 89.24  ? 3995 ALA A CA    1 
ATOM   18646 C  C     . ALA A 1 3995 ? 183.461 128.031 189.098 1.00 86.05  ? 3995 ALA A C     1 
ATOM   18647 O  O     . ALA A 1 3995 ? 182.977 128.621 190.069 1.00 82.17  ? 3995 ALA A O     1 
ATOM   18648 C  CB    . ALA A 1 3995 ? 182.232 125.966 188.376 1.00 89.06  ? 3995 ALA A CB    1 
ATOM   18649 N  N     . PHE A 1 3996 ? 184.777 127.913 188.931 1.00 95.79  ? 3996 PHE A N     1 
ATOM   18650 C  CA    . PHE A 1 3996 ? 185.719 128.236 189.997 1.00 96.08  ? 3996 PHE A CA    1 
ATOM   18651 C  C     . PHE A 1 3996 ? 186.390 129.591 189.810 1.00 98.17  ? 3996 PHE A C     1 
ATOM   18652 O  O     . PHE A 1 3996 ? 186.398 130.410 190.733 1.00 101.35 ? 3996 PHE A O     1 
ATOM   18653 C  CB    . PHE A 1 3996 ? 186.779 127.132 190.089 1.00 93.19  ? 3996 PHE A CB    1 
ATOM   18654 C  CG    . PHE A 1 3996 ? 186.306 125.901 190.806 1.00 96.69  ? 3996 PHE A CG    1 
ATOM   18655 C  CD1   . PHE A 1 3996 ? 184.994 125.795 191.236 1.00 97.50  ? 3996 PHE A CD1   1 
ATOM   18656 C  CD2   . PHE A 1 3996 ? 187.161 124.836 191.021 1.00 99.09  ? 3996 PHE A CD2   1 
ATOM   18657 C  CE1   . PHE A 1 3996 ? 184.553 124.663 191.885 1.00 97.10  ? 3996 PHE A CE1   1 
ATOM   18658 C  CE2   . PHE A 1 3996 ? 186.722 123.697 191.667 1.00 98.19  ? 3996 PHE A CE2   1 
ATOM   18659 C  CZ    . PHE A 1 3996 ? 185.417 123.613 192.102 1.00 97.96  ? 3996 PHE A CZ    1 
ATOM   18660 N  N     . ARG A 1 3997 ? 186.955 129.847 188.632 1.00 86.27  ? 3997 ARG A N     1 
ATOM   18661 C  CA    . ARG A 1 3997 ? 187.678 131.085 188.344 1.00 75.76  ? 3997 ARG A CA    1 
ATOM   18662 C  C     . ARG A 1 3997 ? 187.117 131.689 187.065 1.00 80.56  ? 3997 ARG A C     1 
ATOM   18663 O  O     . ARG A 1 3997 ? 187.694 131.525 185.981 1.00 87.53  ? 3997 ARG A O     1 
ATOM   18664 C  CB    . ARG A 1 3997 ? 189.181 130.831 188.224 1.00 77.92  ? 3997 ARG A CB    1 
ATOM   18665 C  CG    . ARG A 1 3997 ? 189.853 130.453 189.531 1.00 78.29  ? 3997 ARG A CG    1 
ATOM   18666 C  CD    . ARG A 1 3997 ? 190.025 131.668 190.424 1.00 79.42  ? 3997 ARG A CD    1 
ATOM   18667 N  NE    . ARG A 1 3997 ? 190.662 132.772 189.717 1.00 82.45  ? 3997 ARG A NE    1 
ATOM   18668 C  CZ    . ARG A 1 3997 ? 191.967 132.873 189.506 1.00 85.83  ? 3997 ARG A CZ    1 
ATOM   18669 N  NH1   . ARG A 1 3997 ? 192.811 131.956 189.948 1.00 82.35  ? 3997 ARG A NH1   1 
ATOM   18670 N  NH2   . ARG A 1 3997 ? 192.436 133.921 188.837 1.00 87.64  ? 3997 ARG A NH2   1 
ATOM   18671 N  N     . PRO A 1 3998 ? 185.983 132.388 187.151 1.00 72.45  ? 3998 PRO A N     1 
ATOM   18672 C  CA    . PRO A 1 3998 ? 185.386 132.962 185.934 1.00 73.07  ? 3998 PRO A CA    1 
ATOM   18673 C  C     . PRO A 1 3998 ? 186.263 133.999 185.255 1.00 82.04  ? 3998 PRO A C     1 
ATOM   18674 O  O     . PRO A 1 3998 ? 186.095 134.243 184.054 1.00 88.36  ? 3998 PRO A O     1 
ATOM   18675 C  CB    . PRO A 1 3998 ? 184.076 133.578 186.444 1.00 69.31  ? 3998 PRO A CB    1 
ATOM   18676 C  CG    . PRO A 1 3998 ? 184.296 133.800 187.899 1.00 79.11  ? 3998 PRO A CG    1 
ATOM   18677 C  CD    . PRO A 1 3998 ? 185.200 132.697 188.358 1.00 79.28  ? 3998 PRO A CD    1 
ATOM   18678 N  N     . ASP A 1 3999 ? 187.193 134.622 185.983 1.00 82.20  ? 3999 ASP A N     1 
ATOM   18679 C  CA    . ASP A 1 3999 ? 188.071 135.607 185.361 1.00 77.97  ? 3999 ASP A CA    1 
ATOM   18680 C  C     . ASP A 1 3999 ? 189.044 134.957 184.388 1.00 82.17  ? 3999 ASP A C     1 
ATOM   18681 O  O     . ASP A 1 3999 ? 189.560 135.626 183.487 1.00 86.84  ? 3999 ASP A O     1 
ATOM   18682 C  CB    . ASP A 1 3999 ? 188.830 136.388 186.433 1.00 80.32  ? 3999 ASP A CB    1 
ATOM   18683 C  CG    . ASP A 1 3999 ? 189.640 135.490 187.344 1.00 85.72  ? 3999 ASP A CG    1 
ATOM   18684 O  OD1   . ASP A 1 3999 ? 189.070 134.966 188.323 1.00 84.85  ? 3999 ASP A OD1   1 
ATOM   18685 O  OD2   . ASP A 1 3999 ? 190.847 135.310 187.082 1.00 90.42  ? 3999 ASP A OD2   1 
ATOM   18686 N  N     . ARG A 1 4000 ? 189.307 133.663 184.551 1.00 79.73  ? 4000 ARG A N     1 
ATOM   18687 C  CA    . ARG A 1 4000 ? 190.173 132.921 183.646 1.00 77.45  ? 4000 ARG A CA    1 
ATOM   18688 C  C     . ARG A 1 4000 ? 189.397 132.149 182.591 1.00 83.06  ? 4000 ARG A C     1 
ATOM   18689 O  O     . ARG A 1 4000 ? 189.979 131.294 181.915 1.00 91.75  ? 4000 ARG A O     1 
ATOM   18690 C  CB    . ARG A 1 4000 ? 191.062 131.959 184.438 1.00 74.96  ? 4000 ARG A CB    1 
ATOM   18691 C  CG    . ARG A 1 4000 ? 191.902 132.635 185.504 1.00 79.02  ? 4000 ARG A CG    1 
ATOM   18692 C  CD    . ARG A 1 4000 ? 192.796 133.707 184.902 1.00 79.28  ? 4000 ARG A CD    1 
ATOM   18693 N  NE    . ARG A 1 4000 ? 193.742 133.149 183.944 1.00 83.56  ? 4000 ARG A NE    1 
ATOM   18694 C  CZ    . ARG A 1 4000 ? 194.476 133.872 183.110 1.00 82.95  ? 4000 ARG A CZ    1 
ATOM   18695 N  NH1   . ARG A 1 4000 ? 194.401 135.192 183.089 1.00 85.39  ? 4000 ARG A NH1   1 
ATOM   18696 N  NH2   . ARG A 1 4000 ? 195.308 133.254 182.277 1.00 80.82  ? 4000 ARG A NH2   1 
ATOM   18697 N  N     . LEU A 1 4001 ? 188.100 132.425 182.439 1.00 73.29  ? 4001 LEU A N     1 
ATOM   18698 C  CA    . LEU A 1 4001 ? 187.282 131.686 181.484 1.00 71.96  ? 4001 LEU A CA    1 
ATOM   18699 C  C     . LEU A 1 4001 ? 187.761 131.904 180.053 1.00 80.75  ? 4001 LEU A C     1 
ATOM   18700 O  O     . LEU A 1 4001 ? 187.744 130.980 179.234 1.00 85.82  ? 4001 LEU A O     1 
ATOM   18701 C  CB    . LEU A 1 4001 ? 185.817 132.097 181.630 1.00 67.20  ? 4001 LEU A CB    1 
ATOM   18702 C  CG    . LEU A 1 4001 ? 184.815 131.364 180.740 1.00 68.65  ? 4001 LEU A CG    1 
ATOM   18703 C  CD1   . LEU A 1 4001 ? 184.856 129.878 181.026 1.00 76.50  ? 4001 LEU A CD1   1 
ATOM   18704 C  CD2   . LEU A 1 4001 ? 183.415 131.911 180.951 1.00 75.34  ? 4001 LEU A CD2   1 
ATOM   18705 N  N     . LEU A 1 4002 ? 188.180 133.129 179.730 1.00 75.41  ? 4002 LEU A N     1 
ATOM   18706 C  CA    . LEU A 1 4002 ? 188.620 133.432 178.371 1.00 74.63  ? 4002 LEU A CA    1 
ATOM   18707 C  C     . LEU A 1 4002 ? 189.885 132.662 178.005 1.00 78.61  ? 4002 LEU A C     1 
ATOM   18708 O  O     . LEU A 1 4002 ? 190.012 132.143 176.890 1.00 87.83  ? 4002 LEU A O     1 
ATOM   18709 C  CB    . LEU A 1 4002 ? 188.840 134.936 178.217 1.00 74.10  ? 4002 LEU A CB    1 
ATOM   18710 C  CG    . LEU A 1 4002 ? 187.587 135.765 177.934 1.00 76.15  ? 4002 LEU A CG    1 
ATOM   18711 C  CD1   . LEU A 1 4002 ? 187.964 137.190 177.567 1.00 81.42  ? 4002 LEU A CD1   1 
ATOM   18712 C  CD2   . LEU A 1 4002 ? 186.761 135.127 176.832 1.00 72.41  ? 4002 LEU A CD2   1 
ATOM   18713 N  N     . ALA A 1 4003 ? 190.843 132.589 178.932 1.00 68.41  ? 4003 ALA A N     1 
ATOM   18714 C  CA    . ALA A 1 4003 ? 192.075 131.853 178.664 1.00 72.70  ? 4003 ALA A CA    1 
ATOM   18715 C  C     . ALA A 1 4003 ? 191.794 130.368 178.469 1.00 76.87  ? 4003 ALA A C     1 
ATOM   18716 O  O     . ALA A 1 4003 ? 192.373 129.720 177.588 1.00 83.93  ? 4003 ALA A O     1 
ATOM   18717 C  CB    . ALA A 1 4003 ? 193.073 132.071 179.799 1.00 73.98  ? 4003 ALA A CB    1 
ATOM   18718 N  N     . MET A 1 4004 ? 190.899 129.809 179.284 1.00 70.14  ? 4004 MET A N     1 
ATOM   18719 C  CA    . MET A 1 4004 ? 190.558 128.400 179.131 1.00 74.53  ? 4004 MET A CA    1 
ATOM   18720 C  C     . MET A 1 4004 ? 189.783 128.160 177.839 1.00 81.88  ? 4004 MET A C     1 
ATOM   18721 O  O     . MET A 1 4004 ? 189.910 127.100 177.217 1.00 90.13  ? 4004 MET A O     1 
ATOM   18722 C  CB    . MET A 1 4004 ? 189.769 127.921 180.349 1.00 66.55  ? 4004 MET A CB    1 
ATOM   18723 C  CG    . MET A 1 4004 ? 189.005 126.641 180.124 1.00 75.31  ? 4004 MET A CG    1 
ATOM   18724 S  SD    . MET A 1 4004 ? 190.059 125.209 179.827 1.00 80.42  ? 4004 MET A SD    1 
ATOM   18725 C  CE    . MET A 1 4004 ? 191.242 125.374 181.157 1.00 74.32  ? 4004 MET A CE    1 
ATOM   18726 N  N     . ALA A 1 4005 ? 188.986 129.140 177.409 1.00 66.57  ? 4005 ALA A N     1 
ATOM   18727 C  CA    . ALA A 1 4005 ? 188.338 129.044 176.105 1.00 63.83  ? 4005 ALA A CA    1 
ATOM   18728 C  C     . ALA A 1 4005 ? 189.368 129.046 174.983 1.00 67.43  ? 4005 ALA A C     1 
ATOM   18729 O  O     . ALA A 1 4005 ? 189.229 128.311 173.998 1.00 79.14  ? 4005 ALA A O     1 
ATOM   18730 C  CB    . ALA A 1 4005 ? 187.343 130.189 175.925 1.00 60.07  ? 4005 ALA A CB    1 
ATOM   18731 N  N     . HIS A 1 4006 ? 190.405 129.876 175.113 1.00 65.43  ? 4006 HIS A N     1 
ATOM   18732 C  CA    . HIS A 1 4006 ? 191.504 129.843 174.153 1.00 66.59  ? 4006 HIS A CA    1 
ATOM   18733 C  C     . HIS A 1 4006 ? 192.168 128.474 174.136 1.00 73.59  ? 4006 HIS A C     1 
ATOM   18734 O  O     . HIS A 1 4006 ? 192.511 127.950 173.068 1.00 81.78  ? 4006 HIS A O     1 
ATOM   18735 C  CB    . HIS A 1 4006 ? 192.533 130.923 174.487 1.00 67.51  ? 4006 HIS A CB    1 
ATOM   18736 C  CG    . HIS A 1 4006 ? 192.185 132.279 173.958 1.00 74.68  ? 4006 HIS A CG    1 
ATOM   18737 N  ND1   . HIS A 1 4006 ? 191.283 133.112 174.583 1.00 77.35  ? 4006 HIS A ND1   1 
ATOM   18738 C  CD2   . HIS A 1 4006 ? 192.620 132.947 172.864 1.00 75.13  ? 4006 HIS A CD2   1 
ATOM   18739 C  CE1   . HIS A 1 4006 ? 191.177 134.236 173.897 1.00 74.30  ? 4006 HIS A CE1   1 
ATOM   18740 N  NE2   . HIS A 1 4006 ? 191.978 134.161 172.849 1.00 77.18  ? 4006 HIS A NE2   1 
ATOM   18741 N  N     . MET A 1 4007 ? 192.361 127.882 175.315 1.00 73.83  ? 4007 MET A N     1 
ATOM   18742 C  CA    . MET A 1 4007 ? 192.944 126.545 175.391 1.00 73.84  ? 4007 MET A CA    1 
ATOM   18743 C  C     . MET A 1 4007 ? 192.053 125.512 174.709 1.00 77.17  ? 4007 MET A C     1 
ATOM   18744 O  O     . MET A 1 4007 ? 192.546 124.612 174.022 1.00 85.35  ? 4007 MET A O     1 
ATOM   18745 C  CB    . MET A 1 4007 ? 193.188 126.160 176.849 1.00 71.37  ? 4007 MET A CB    1 
ATOM   18746 C  CG    . MET A 1 4007 ? 194.364 126.875 177.491 1.00 75.74  ? 4007 MET A CG    1 
ATOM   18747 S  SD    . MET A 1 4007 ? 195.332 125.806 178.572 1.00 93.94  ? 4007 MET A SD    1 
ATOM   18748 C  CE    . MET A 1 4007 ? 194.128 124.545 178.983 1.00 82.45  ? 4007 MET A CE    1 
ATOM   18749 N  N     . PHE A 1 4008 ? 190.737 125.621 174.900 1.00 61.32  ? 4008 PHE A N     1 
ATOM   18750 C  CA    . PHE A 1 4008 ? 189.808 124.705 174.243 1.00 62.83  ? 4008 PHE A CA    1 
ATOM   18751 C  C     . PHE A 1 4008 ? 189.868 124.851 172.726 1.00 71.77  ? 4008 PHE A C     1 
ATOM   18752 O  O     . PHE A 1 4008 ? 189.866 123.851 171.996 1.00 75.39  ? 4008 PHE A O     1 
ATOM   18753 C  CB    . PHE A 1 4008 ? 188.388 124.953 174.749 1.00 61.78  ? 4008 PHE A CB    1 
ATOM   18754 C  CG    . PHE A 1 4008 ? 187.334 124.190 174.002 1.00 67.90  ? 4008 PHE A CG    1 
ATOM   18755 C  CD1   . PHE A 1 4008 ? 187.174 122.831 174.198 1.00 70.34  ? 4008 PHE A CD1   1 
ATOM   18756 C  CD2   . PHE A 1 4008 ? 186.505 124.832 173.101 1.00 66.93  ? 4008 PHE A CD2   1 
ATOM   18757 C  CE1   . PHE A 1 4008 ? 186.203 122.129 173.511 1.00 67.64  ? 4008 PHE A CE1   1 
ATOM   18758 C  CE2   . PHE A 1 4008 ? 185.533 124.136 172.412 1.00 64.22  ? 4008 PHE A CE2   1 
ATOM   18759 C  CZ    . PHE A 1 4008 ? 185.383 122.783 172.616 1.00 63.40  ? 4008 PHE A CZ    1 
ATOM   18760 N  N     . VAL A 1 4009 ? 189.916 126.092 172.236 1.00 67.35  ? 4009 VAL A N     1 
ATOM   18761 C  CA    . VAL A 1 4009 ? 190.028 126.323 170.798 1.00 57.46  ? 4009 VAL A CA    1 
ATOM   18762 C  C     . VAL A 1 4009 ? 191.329 125.736 170.267 1.00 65.62  ? 4009 VAL A C     1 
ATOM   18763 O  O     . VAL A 1 4009 ? 191.366 125.152 169.177 1.00 77.75  ? 4009 VAL A O     1 
ATOM   18764 C  CB    . VAL A 1 4009 ? 189.912 127.826 170.485 1.00 60.28  ? 4009 VAL A CB    1 
ATOM   18765 C  CG1   . VAL A 1 4009 ? 190.168 128.083 169.011 1.00 68.48  ? 4009 VAL A CG1   1 
ATOM   18766 C  CG2   . VAL A 1 4009 ? 188.538 128.337 170.873 1.00 67.65  ? 4009 VAL A CG2   1 
ATOM   18767 N  N     . SER A 1 4010 ? 192.416 125.879 171.028 1.00 64.40  ? 4010 SER A N     1 
ATOM   18768 C  CA    . SER A 1 4010 ? 193.680 125.265 170.633 1.00 71.17  ? 4010 SER A CA    1 
ATOM   18769 C  C     . SER A 1 4010 ? 193.574 123.746 170.592 1.00 73.83  ? 4010 SER A C     1 
ATOM   18770 O  O     . SER A 1 4010 ? 194.136 123.108 169.695 1.00 71.82  ? 4010 SER A O     1 
ATOM   18771 C  CB    . SER A 1 4010 ? 194.792 125.694 171.589 1.00 73.38  ? 4010 SER A CB    1 
ATOM   18772 O  OG    . SER A 1 4010 ? 194.860 127.105 171.688 1.00 77.82  ? 4010 SER A OG    1 
ATOM   18773 N  N     . THR A 1 4011 ? 192.869 123.153 171.555 1.00 75.32  ? 4011 THR A N     1 
ATOM   18774 C  CA    . THR A 1 4011 ? 192.664 121.709 171.558 1.00 73.67  ? 4011 THR A CA    1 
ATOM   18775 C  C     . THR A 1 4011 ? 191.874 121.241 170.344 1.00 76.60  ? 4011 THR A C     1 
ATOM   18776 O  O     . THR A 1 4011 ? 192.209 120.207 169.755 1.00 76.88  ? 4011 THR A O     1 
ATOM   18777 C  CB    . THR A 1 4011 ? 191.944 121.277 172.837 1.00 75.40  ? 4011 THR A CB    1 
ATOM   18778 O  OG1   . THR A 1 4011 ? 192.573 121.886 173.971 1.00 81.39  ? 4011 THR A OG1   1 
ATOM   18779 C  CG2   . THR A 1 4011 ? 191.990 119.766 172.990 1.00 74.51  ? 4011 THR A CG2   1 
ATOM   18780 N  N     . ASN A 1 4012 ? 190.836 121.979 169.954 1.00 76.17  ? 4012 ASN A N     1 
ATOM   18781 C  CA    . ASN A 1 4012 ? 189.995 121.597 168.825 1.00 71.75  ? 4012 ASN A CA    1 
ATOM   18782 C  C     . ASN A 1 4012 ? 190.601 121.966 167.476 1.00 74.63  ? 4012 ASN A C     1 
ATOM   18783 O  O     . ASN A 1 4012 ? 190.739 121.105 166.604 1.00 77.51  ? 4012 ASN A O     1 
ATOM   18784 C  CB    . ASN A 1 4012 ? 188.611 122.240 168.958 1.00 67.87  ? 4012 ASN A CB    1 
ATOM   18785 C  CG    . ASN A 1 4012 ? 187.735 121.528 169.962 1.00 77.58  ? 4012 ASN A CG    1 
ATOM   18786 O  OD1   . ASN A 1 4012 ? 188.034 121.502 171.154 1.00 82.08  ? 4012 ASN A OD1   1 
ATOM   18787 N  ND2   . ASN A 1 4012 ? 186.642 120.945 169.485 1.00 82.61  ? 4012 ASN A ND2   1 
ATOM   18788 N  N     . LEU A 1 4013 ? 190.967 123.234 167.286 1.00 67.24  ? 4013 LEU A N     1 
ATOM   18789 C  CA    . LEU A 1 4013 ? 191.368 123.731 165.979 1.00 63.93  ? 4013 LEU A CA    1 
ATOM   18790 C  C     . LEU A 1 4013 ? 192.866 123.943 165.819 1.00 73.46  ? 4013 LEU A C     1 
ATOM   18791 O  O     . LEU A 1 4013 ? 193.308 124.261 164.711 1.00 81.09  ? 4013 LEU A O     1 
ATOM   18792 C  CB    . LEU A 1 4013 ? 190.643 125.050 165.676 1.00 66.38  ? 4013 LEU A CB    1 
ATOM   18793 C  CG    . LEU A 1 4013 ? 189.132 124.924 165.482 1.00 69.48  ? 4013 LEU A CG    1 
ATOM   18794 C  CD1   . LEU A 1 4013 ? 188.444 126.257 165.697 1.00 67.80  ? 4013 LEU A CD1   1 
ATOM   18795 C  CD2   . LEU A 1 4013 ? 188.825 124.389 164.096 1.00 72.54  ? 4013 LEU A CD2   1 
ATOM   18796 N  N     . GLY A 1 4014 ? 193.652 123.781 166.879 1.00 81.94  ? 4014 GLY A N     1 
ATOM   18797 C  CA    . GLY A 1 4014 ? 195.089 123.941 166.768 1.00 80.33  ? 4014 GLY A CA    1 
ATOM   18798 C  C     . GLY A 1 4014 ? 195.626 125.131 167.537 1.00 84.15  ? 4014 GLY A C     1 
ATOM   18799 O  O     . GLY A 1 4014 ? 194.903 126.102 167.776 1.00 88.39  ? 4014 GLY A O     1 
ATOM   18800 N  N     . GLU A 1 4015 ? 196.902 125.065 167.924 1.00 88.89  ? 4015 GLU A N     1 
ATOM   18801 C  CA    . GLU A 1 4015 ? 197.502 126.145 168.702 1.00 87.19  ? 4015 GLU A CA    1 
ATOM   18802 C  C     . GLU A 1 4015 ? 197.596 127.433 167.893 1.00 88.64  ? 4015 GLU A C     1 
ATOM   18803 O  O     . GLU A 1 4015 ? 197.379 128.526 168.429 1.00 87.21  ? 4015 GLU A O     1 
ATOM   18804 C  CB    . GLU A 1 4015 ? 198.885 125.726 169.201 1.00 85.21  ? 4015 GLU A CB    1 
ATOM   18805 C  CG    . GLU A 1 4015 ? 198.871 124.767 170.386 1.00 85.75  ? 4015 GLU A CG    1 
ATOM   18806 C  CD    . GLU A 1 4015 ? 198.537 123.337 169.995 1.00 93.35  ? 4015 GLU A CD    1 
ATOM   18807 O  OE1   . GLU A 1 4015 ? 198.597 122.453 170.876 1.00 90.45  ? 4015 GLU A OE1   1 
ATOM   18808 O  OE2   . GLU A 1 4015 ? 198.228 123.090 168.810 1.00 97.64  ? 4015 GLU A OE2   1 
ATOM   18809 N  N     . SER A 1 4016 ? 197.920 127.328 166.605 1.00 90.18  ? 4016 SER A N     1 
ATOM   18810 C  CA    . SER A 1 4016 ? 198.127 128.488 165.751 1.00 90.27  ? 4016 SER A CA    1 
ATOM   18811 C  C     . SER A 1 4016 ? 196.856 128.933 165.036 1.00 85.54  ? 4016 SER A C     1 
ATOM   18812 O  O     . SER A 1 4016 ? 196.942 129.542 163.963 1.00 83.72  ? 4016 SER A O     1 
ATOM   18813 C  CB    . SER A 1 4016 ? 199.225 128.197 164.726 1.00 92.83  ? 4016 SER A CB    1 
ATOM   18814 O  OG    . SER A 1 4016 ? 198.831 127.164 163.840 1.00 89.82  ? 4016 SER A OG    1 
ATOM   18815 N  N     . PHE A 1 4017 ? 195.683 128.640 165.599 1.00 71.27  ? 4017 PHE A N     1 
ATOM   18816 C  CA    . PHE A 1 4017 ? 194.438 129.039 164.952 1.00 72.37  ? 4017 PHE A CA    1 
ATOM   18817 C  C     . PHE A 1 4017 ? 194.223 130.544 165.059 1.00 80.34  ? 4017 PHE A C     1 
ATOM   18818 O  O     . PHE A 1 4017 ? 193.817 131.195 164.089 1.00 81.91  ? 4017 PHE A O     1 
ATOM   18819 C  CB    . PHE A 1 4017 ? 193.264 128.279 165.569 1.00 71.00  ? 4017 PHE A CB    1 
ATOM   18820 C  CG    . PHE A 1 4017 ? 191.998 128.367 164.769 1.00 72.31  ? 4017 PHE A CG    1 
ATOM   18821 C  CD1   . PHE A 1 4017 ? 191.854 127.637 163.602 1.00 76.22  ? 4017 PHE A CD1   1 
ATOM   18822 C  CD2   . PHE A 1 4017 ? 190.955 129.176 165.180 1.00 72.89  ? 4017 PHE A CD2   1 
ATOM   18823 C  CE1   . PHE A 1 4017 ? 190.692 127.712 162.862 1.00 78.78  ? 4017 PHE A CE1   1 
ATOM   18824 C  CE2   . PHE A 1 4017 ? 189.791 129.256 164.442 1.00 70.33  ? 4017 PHE A CE2   1 
ATOM   18825 C  CZ    . PHE A 1 4017 ? 189.660 128.522 163.282 1.00 75.81  ? 4017 PHE A CZ    1 
ATOM   18826 N  N     . MET A 1 4018 ? 194.493 131.112 166.231 1.00 79.59  ? 4018 MET A N     1 
ATOM   18827 C  CA    . MET A 1 4018 ? 194.323 132.536 166.483 1.00 72.91  ? 4018 MET A CA    1 
ATOM   18828 C  C     . MET A 1 4018 ? 195.602 133.329 166.243 1.00 77.44  ? 4018 MET A C     1 
ATOM   18829 O  O     . MET A 1 4018 ? 195.630 134.534 166.508 1.00 80.07  ? 4018 MET A O     1 
ATOM   18830 C  CB    . MET A 1 4018 ? 193.834 132.755 167.915 1.00 73.88  ? 4018 MET A CB    1 
ATOM   18831 C  CG    . MET A 1 4018 ? 192.659 131.873 168.303 1.00 72.95  ? 4018 MET A CG    1 
ATOM   18832 S  SD    . MET A 1 4018 ? 191.054 132.657 168.083 1.00 89.11  ? 4018 MET A SD    1 
ATOM   18833 C  CE    . MET A 1 4018 ? 190.795 133.365 169.704 1.00 75.63  ? 4018 MET A CE    1 
ATOM   18834 N  N     . SER A 1 4019 ? 196.662 132.676 165.757 1.00 90.29  ? 4019 SER A N     1 
ATOM   18835 C  CA    . SER A 1 4019 ? 197.953 133.341 165.613 1.00 90.63  ? 4019 SER A CA    1 
ATOM   18836 C  C     . SER A 1 4019 ? 197.915 134.451 164.571 1.00 91.70  ? 4019 SER A C     1 
ATOM   18837 O  O     . SER A 1 4019 ? 198.598 135.468 164.730 1.00 91.11  ? 4019 SER A O     1 
ATOM   18838 C  CB    . SER A 1 4019 ? 199.033 132.326 165.243 1.00 92.62  ? 4019 SER A CB    1 
ATOM   18839 O  OG    . SER A 1 4019 ? 198.980 132.013 163.861 1.00 90.33  ? 4019 SER A OG    1 
ATOM   18840 N  N     . ILE A 1 4020 ? 197.146 134.274 163.495 1.00 81.21  ? 4020 ILE A N     1 
ATOM   18841 C  CA    . ILE A 1 4020 ? 197.152 135.262 162.424 1.00 84.99  ? 4020 ILE A CA    1 
ATOM   18842 C  C     . ILE A 1 4020 ? 196.455 136.552 162.839 1.00 83.32  ? 4020 ILE A C     1 
ATOM   18843 O  O     . ILE A 1 4020 ? 196.686 137.602 162.230 1.00 87.07  ? 4020 ILE A O     1 
ATOM   18844 C  CB    . ILE A 1 4020 ? 196.526 134.657 161.148 1.00 83.92  ? 4020 ILE A CB    1 
ATOM   18845 C  CG1   . ILE A 1 4020 ? 196.991 135.419 159.904 1.00 86.44  ? 4020 ILE A CG1   1 
ATOM   18846 C  CG2   . ILE A 1 4020 ? 195.021 134.614 161.257 1.00 79.38  ? 4020 ILE A CG2   1 
ATOM   18847 C  CD1   . ILE A 1 4020 ? 198.470 135.253 159.615 1.00 79.94  ? 4020 ILE A CD1   1 
ATOM   18848 N  N     . MET A 1 4021 ? 195.617 136.508 163.876 1.00 78.53  ? 4021 MET A N     1 
ATOM   18849 C  CA    . MET A 1 4021 ? 194.961 137.715 164.366 1.00 81.51  ? 4021 MET A CA    1 
ATOM   18850 C  C     . MET A 1 4021 ? 195.862 138.568 165.252 1.00 83.03  ? 4021 MET A C     1 
ATOM   18851 O  O     . MET A 1 4021 ? 195.539 139.736 165.490 1.00 85.11  ? 4021 MET A O     1 
ATOM   18852 C  CB    . MET A 1 4021 ? 193.681 137.346 165.126 1.00 82.28  ? 4021 MET A CB    1 
ATOM   18853 C  CG    . MET A 1 4021 ? 192.418 137.004 164.296 1.00 82.73  ? 4021 MET A CG    1 
ATOM   18854 S  SD    . MET A 1 4021 ? 191.932 138.045 162.887 1.00 86.22  ? 4021 MET A SD    1 
ATOM   18855 C  CE    . MET A 1 4021 ? 193.040 137.544 161.571 1.00 81.51  ? 4021 MET A CE    1 
ATOM   18856 N  N     . GLU A 1 4022 ? 196.982 138.031 165.736 1.00 89.71  ? 4022 GLU A N     1 
ATOM   18857 C  CA    . GLU A 1 4022 ? 197.881 138.814 166.576 1.00 88.11  ? 4022 GLU A CA    1 
ATOM   18858 C  C     . GLU A 1 4022 ? 198.927 139.582 165.777 1.00 91.05  ? 4022 GLU A C     1 
ATOM   18859 O  O     . GLU A 1 4022 ? 199.663 140.384 166.362 1.00 92.35  ? 4022 GLU A O     1 
ATOM   18860 C  CB    . GLU A 1 4022 ? 198.589 137.915 167.596 1.00 89.26  ? 4022 GLU A CB    1 
ATOM   18861 C  CG    . GLU A 1 4022 ? 199.837 137.230 167.068 1.00 95.74  ? 4022 GLU A CG    1 
ATOM   18862 C  CD    . GLU A 1 4022 ? 200.371 136.180 168.018 1.00 97.34  ? 4022 GLU A CD    1 
ATOM   18863 O  OE1   . GLU A 1 4022 ? 201.387 135.536 167.683 1.00 91.61  ? 4022 GLU A OE1   1 
ATOM   18864 O  OE2   . GLU A 1 4022 ? 199.768 135.991 169.096 1.00 98.62  ? 4022 GLU A OE2   1 
ATOM   18865 N  N     . GLN A 1 4023 ? 199.010 139.360 164.464 1.00 93.09  ? 4023 GLN A N     1 
ATOM   18866 C  CA    . GLN A 1 4023 ? 199.937 140.019 163.560 1.00 89.51  ? 4023 GLN A CA    1 
ATOM   18867 C  C     . GLN A 1 4023 ? 199.292 141.247 162.926 1.00 93.04  ? 4023 GLN A C     1 
ATOM   18868 O  O     . GLN A 1 4023 ? 198.066 141.315 162.800 1.00 94.71  ? 4023 GLN A O     1 
ATOM   18869 C  CB    . GLN A 1 4023 ? 200.389 139.055 162.459 1.00 89.91  ? 4023 GLN A CB    1 
ATOM   18870 C  CG    . GLN A 1 4023 ? 200.570 137.620 162.925 1.00 90.71  ? 4023 GLN A CG    1 
ATOM   18871 C  CD    . GLN A 1 4023 ? 201.777 137.441 163.827 1.00 95.90  ? 4023 GLN A CD    1 
ATOM   18872 O  OE1   . GLN A 1 4023 ? 202.614 138.336 163.954 1.00 94.34  ? 4023 GLN A OE1   1 
ATOM   18873 N  NE2   . GLN A 1 4023 ? 201.873 136.279 164.461 1.00 95.46  ? 4023 GLN A NE2   1 
ATOM   18874 N  N     . PRO A 1 4024 ? 200.090 142.237 162.525 1.00 90.24  ? 4024 PRO A N     1 
ATOM   18875 C  CA    . PRO A 1 4024 ? 199.521 143.412 161.854 1.00 89.18  ? 4024 PRO A CA    1 
ATOM   18876 C  C     . PRO A 1 4024 ? 198.843 143.031 160.547 1.00 88.38  ? 4024 PRO A C     1 
ATOM   18877 O  O     . PRO A 1 4024 ? 199.238 142.076 159.875 1.00 90.98  ? 4024 PRO A O     1 
ATOM   18878 C  CB    . PRO A 1 4024 ? 200.738 144.313 161.616 1.00 87.37  ? 4024 PRO A CB    1 
ATOM   18879 C  CG    . PRO A 1 4024 ? 201.922 143.407 161.727 1.00 90.13  ? 4024 PRO A CG    1 
ATOM   18880 C  CD    . PRO A 1 4024 ? 201.541 142.371 162.732 1.00 90.79  ? 4024 PRO A CD    1 
ATOM   18881 N  N     . LEU A 1 4025 ? 197.805 143.787 160.197 1.00 80.88  ? 4025 LEU A N     1 
ATOM   18882 C  CA    . LEU A 1 4025 ? 197.055 143.516 158.978 1.00 84.06  ? 4025 LEU A CA    1 
ATOM   18883 C  C     . LEU A 1 4025 ? 197.941 143.687 157.751 1.00 87.88  ? 4025 LEU A C     1 
ATOM   18884 O  O     . LEU A 1 4025 ? 198.644 144.692 157.611 1.00 93.81  ? 4025 LEU A O     1 
ATOM   18885 C  CB    . LEU A 1 4025 ? 195.845 144.446 158.890 1.00 79.34  ? 4025 LEU A CB    1 
ATOM   18886 C  CG    . LEU A 1 4025 ? 194.984 144.334 157.632 1.00 79.57  ? 4025 LEU A CG    1 
ATOM   18887 C  CD1   . LEU A 1 4025 ? 194.397 142.939 157.511 1.00 79.18  ? 4025 LEU A CD1   1 
ATOM   18888 C  CD2   . LEU A 1 4025 ? 193.885 145.381 157.643 1.00 80.39  ? 4025 LEU A CD2   1 
ATOM   18889 N  N     . ASP A 1 4026 ? 197.903 142.699 156.859 1.00 92.36  ? 4026 ASP A N     1 
ATOM   18890 C  CA    . ASP A 1 4026 ? 198.667 142.729 155.613 1.00 90.57  ? 4026 ASP A CA    1 
ATOM   18891 C  C     . ASP A 1 4026 ? 197.708 143.150 154.505 1.00 93.91  ? 4026 ASP A C     1 
ATOM   18892 O  O     . ASP A 1 4026 ? 197.128 142.318 153.807 1.00 98.58  ? 4026 ASP A O     1 
ATOM   18893 C  CB    . ASP A 1 4026 ? 199.307 141.375 155.332 1.00 90.94  ? 4026 ASP A CB    1 
ATOM   18894 C  CG    . ASP A 1 4026 ? 200.187 141.392 154.101 1.00 96.90  ? 4026 ASP A CG    1 
ATOM   18895 O  OD1   . ASP A 1 4026 ? 201.278 141.998 154.156 1.00 98.68  ? 4026 ASP A OD1   1 
ATOM   18896 O  OD2   . ASP A 1 4026 ? 199.792 140.798 153.079 1.00 95.30  ? 4026 ASP A OD2   1 
ATOM   18897 N  N     . LEU A 1 4027 ? 197.544 144.465 154.348 1.00 80.99  ? 4027 LEU A N     1 
ATOM   18898 C  CA    . LEU A 1 4027 ? 196.557 144.988 153.410 1.00 76.42  ? 4027 LEU A CA    1 
ATOM   18899 C  C     . LEU A 1 4027 ? 196.940 144.717 151.961 1.00 81.13  ? 4027 LEU A C     1 
ATOM   18900 O  O     . LEU A 1 4027 ? 196.057 144.595 151.105 1.00 86.67  ? 4027 LEU A O     1 
ATOM   18901 C  CB    . LEU A 1 4027 ? 196.373 146.488 153.633 1.00 77.50  ? 4027 LEU A CB    1 
ATOM   18902 C  CG    . LEU A 1 4027 ? 195.130 146.919 154.409 1.00 79.18  ? 4027 LEU A CG    1 
ATOM   18903 C  CD1   . LEU A 1 4027 ? 195.174 148.408 154.703 1.00 80.43  ? 4027 LEU A CD1   1 
ATOM   18904 C  CD2   . LEU A 1 4027 ? 193.874 146.563 153.636 1.00 81.86  ? 4027 LEU A CD2   1 
ATOM   18905 N  N     . THR A 1 4028 ? 198.239 144.623 151.668 1.00 91.56  ? 4028 THR A N     1 
ATOM   18906 C  CA    . THR A 1 4028 ? 198.682 144.520 150.280 1.00 90.87  ? 4028 THR A CA    1 
ATOM   18907 C  C     . THR A 1 4028 ? 198.146 143.257 149.617 1.00 93.22  ? 4028 THR A C     1 
ATOM   18908 O  O     . THR A 1 4028 ? 197.517 143.321 148.554 1.00 97.28  ? 4028 THR A O     1 
ATOM   18909 C  CB    . THR A 1 4028 ? 200.209 144.550 150.215 1.00 91.41  ? 4028 THR A CB    1 
ATOM   18910 O  OG1   . THR A 1 4028 ? 200.690 145.782 150.767 1.00 95.01  ? 4028 THR A OG1   1 
ATOM   18911 C  CG2   . THR A 1 4028 ? 200.684 144.423 148.777 1.00 89.28  ? 4028 THR A CG2   1 
ATOM   18912 N  N     . HIS A 1 4029 ? 198.373 142.099 150.240 1.00 91.89  ? 4029 HIS A N     1 
ATOM   18913 C  CA    . HIS A 1 4029 ? 197.941 140.838 149.644 1.00 94.52  ? 4029 HIS A CA    1 
ATOM   18914 C  C     . HIS A 1 4029 ? 196.423 140.758 149.546 1.00 92.44  ? 4029 HIS A C     1 
ATOM   18915 O  O     . HIS A 1 4029 ? 195.884 140.315 148.523 1.00 92.39  ? 4029 HIS A O     1 
ATOM   18916 C  CB    . HIS A 1 4029 ? 198.485 139.662 150.454 1.00 89.52  ? 4029 HIS A CB    1 
ATOM   18917 C  CG    . HIS A 1 4029 ? 197.974 138.330 150.005 1.00 95.19  ? 4029 HIS A CG    1 
ATOM   18918 N  ND1   . HIS A 1 4029 ? 198.175 137.846 148.731 1.00 97.87  ? 4029 HIS A ND1   1 
ATOM   18919 C  CD2   . HIS A 1 4029 ? 197.268 137.379 150.661 1.00 93.50  ? 4029 HIS A CD2   1 
ATOM   18920 C  CE1   . HIS A 1 4029 ? 197.617 136.654 148.621 1.00 95.33  ? 4029 HIS A CE1   1 
ATOM   18921 N  NE2   . HIS A 1 4029 ? 197.059 136.347 149.778 1.00 95.19  ? 4029 HIS A NE2   1 
ATOM   18922 N  N     . ILE A 1 4030 ? 195.720 141.179 150.599 1.00 73.93  ? 4030 ILE A N     1 
ATOM   18923 C  CA    . ILE A 1 4030 ? 194.263 141.097 150.600 1.00 76.97  ? 4030 ILE A CA    1 
ATOM   18924 C  C     . ILE A 1 4030 ? 193.680 141.969 149.499 1.00 80.96  ? 4030 ILE A C     1 
ATOM   18925 O  O     . ILE A 1 4030 ? 192.828 141.523 148.721 1.00 82.32  ? 4030 ILE A O     1 
ATOM   18926 C  CB    . ILE A 1 4030 ? 193.706 141.482 151.982 1.00 75.13  ? 4030 ILE A CB    1 
ATOM   18927 C  CG1   . ILE A 1 4030 ? 194.333 140.608 153.068 1.00 81.22  ? 4030 ILE A CG1   1 
ATOM   18928 C  CG2   . ILE A 1 4030 ? 192.196 141.347 151.997 1.00 74.80  ? 4030 ILE A CG2   1 
ATOM   18929 C  CD1   . ILE A 1 4030 ? 193.815 140.898 154.456 1.00 81.45  ? 4030 ILE A CD1   1 
ATOM   18930 N  N     . VAL A 1 4031 ? 194.151 143.213 149.393 1.00 84.41  ? 4031 VAL A N     1 
ATOM   18931 C  CA    . VAL A 1 4031 ? 193.648 144.114 148.362 1.00 80.56  ? 4031 VAL A CA    1 
ATOM   18932 C  C     . VAL A 1 4031 ? 193.999 143.589 146.975 1.00 85.73  ? 4031 VAL A C     1 
ATOM   18933 O  O     . VAL A 1 4031 ? 193.183 143.656 146.048 1.00 88.26  ? 4031 VAL A O     1 
ATOM   18934 C  CB    . VAL A 1 4031 ? 194.191 145.537 148.590 1.00 73.25  ? 4031 VAL A CB    1 
ATOM   18935 C  CG1   . VAL A 1 4031 ? 194.017 146.386 147.342 1.00 76.14  ? 4031 VAL A CG1   1 
ATOM   18936 C  CG2   . VAL A 1 4031 ? 193.496 146.182 149.776 1.00 75.91  ? 4031 VAL A CG2   1 
ATOM   18937 N  N     . GLY A 1 4032 ? 195.207 143.049 146.810 1.00 88.25  ? 4032 GLY A N     1 
ATOM   18938 C  CA    . GLY A 1 4032 ? 195.617 142.573 145.500 1.00 86.32  ? 4032 GLY A CA    1 
ATOM   18939 C  C     . GLY A 1 4032 ? 194.827 141.370 145.020 1.00 88.32  ? 4032 GLY A C     1 
ATOM   18940 O  O     . GLY A 1 4032 ? 194.458 141.292 143.845 1.00 89.59  ? 4032 GLY A O     1 
ATOM   18941 N  N     . THR A 1 4033 ? 194.555 140.417 145.911 1.00 91.57  ? 4033 THR A N     1 
ATOM   18942 C  CA    . THR A 1 4033 ? 193.993 139.137 145.498 1.00 94.78  ? 4033 THR A CA    1 
ATOM   18943 C  C     . THR A 1 4033 ? 192.581 138.885 146.008 1.00 95.14  ? 4033 THR A C     1 
ATOM   18944 O  O     . THR A 1 4033 ? 191.695 138.548 145.217 1.00 95.13  ? 4033 THR A O     1 
ATOM   18945 C  CB    . THR A 1 4033 ? 194.912 137.992 145.949 1.00 92.82  ? 4033 THR A CB    1 
ATOM   18946 O  OG1   . THR A 1 4033 ? 194.603 137.629 147.299 1.00 91.17  ? 4033 THR A OG1   1 
ATOM   18947 C  CG2   . THR A 1 4033 ? 196.372 138.410 145.860 1.00 91.27  ? 4033 THR A CG2   1 
ATOM   18948 N  N     . GLU A 1 4034 ? 192.338 139.036 147.308 1.00 84.67  ? 4034 GLU A N     1 
ATOM   18949 C  CA    . GLU A 1 4034 ? 191.093 138.573 147.909 1.00 80.39  ? 4034 GLU A CA    1 
ATOM   18950 C  C     . GLU A 1 4034 ? 189.935 139.549 147.745 1.00 85.76  ? 4034 GLU A C     1 
ATOM   18951 O  O     . GLU A 1 4034 ? 188.818 139.229 148.165 1.00 82.91  ? 4034 GLU A O     1 
ATOM   18952 C  CB    . GLU A 1 4034 ? 191.300 138.281 149.399 1.00 75.86  ? 4034 GLU A CB    1 
ATOM   18953 C  CG    . GLU A 1 4034 ? 192.540 137.465 149.714 1.00 82.46  ? 4034 GLU A CG    1 
ATOM   18954 C  CD    . GLU A 1 4034 ? 192.680 137.168 151.194 1.00 89.12  ? 4034 GLU A CD    1 
ATOM   18955 O  OE1   . GLU A 1 4034 ? 191.772 137.542 151.965 1.00 86.36  ? 4034 GLU A OE1   1 
ATOM   18956 O  OE2   . GLU A 1 4034 ? 193.699 136.561 151.586 1.00 85.59  ? 4034 GLU A OE2   1 
ATOM   18957 N  N     . VAL A 1 4035 ? 190.159 140.717 147.152 1.00 80.47  ? 4035 VAL A N     1 
ATOM   18958 C  CA    . VAL A 1 4035 ? 189.117 141.724 146.985 1.00 71.03  ? 4035 VAL A CA    1 
ATOM   18959 C  C     . VAL A 1 4035 ? 188.879 141.925 145.496 1.00 75.15  ? 4035 VAL A C     1 
ATOM   18960 O  O     . VAL A 1 4035 ? 189.805 142.282 144.756 1.00 79.66  ? 4035 VAL A O     1 
ATOM   18961 C  CB    . VAL A 1 4035 ? 189.490 143.052 147.663 1.00 65.30  ? 4035 VAL A CB    1 
ATOM   18962 C  CG1   . VAL A 1 4035 ? 188.601 144.173 147.156 1.00 72.07  ? 4035 VAL A CG1   1 
ATOM   18963 C  CG2   . VAL A 1 4035 ? 189.378 142.923 149.171 1.00 71.13  ? 4035 VAL A CG2   1 
ATOM   18964 N  N     . LYS A 1 4036 ? 187.644 141.692 145.058 1.00 77.71  ? 4036 LYS A N     1 
ATOM   18965 C  CA    . LYS A 1 4036 ? 187.267 141.974 143.685 1.00 77.96  ? 4036 LYS A CA    1 
ATOM   18966 C  C     . LYS A 1 4036 ? 187.053 143.474 143.491 1.00 81.92  ? 4036 LYS A C     1 
ATOM   18967 O  O     . LYS A 1 4036 ? 186.677 144.179 144.431 1.00 85.49  ? 4036 LYS A O     1 
ATOM   18968 C  CB    . LYS A 1 4036 ? 185.994 141.219 143.315 1.00 72.96  ? 4036 LYS A CB    1 
ATOM   18969 C  CG    . LYS A 1 4036 ? 186.233 139.803 142.820 1.00 79.05  ? 4036 LYS A CG    1 
ATOM   18970 C  CD    . LYS A 1 4036 ? 185.074 138.889 143.179 1.00 82.92  ? 4036 LYS A CD    1 
ATOM   18971 C  CE    . LYS A 1 4036 ? 185.510 137.433 143.216 1.00 82.86  ? 4036 LYS A CE    1 
ATOM   18972 N  NZ    . LYS A 1 4036 ? 186.600 137.203 144.203 1.00 85.40  ? 4036 LYS A NZ    1 
ATOM   18973 N  N     . PRO A 1 4037 ? 187.296 143.986 142.282 1.00 72.95  ? 4037 PRO A N     1 
ATOM   18974 C  CA    . PRO A 1 4037 ? 187.079 145.423 142.045 1.00 67.82  ? 4037 PRO A CA    1 
ATOM   18975 C  C     . PRO A 1 4037 ? 185.648 145.867 142.286 1.00 69.06  ? 4037 PRO A C     1 
ATOM   18976 O  O     . PRO A 1 4037 ? 185.425 147.009 142.706 1.00 67.55  ? 4037 PRO A O     1 
ATOM   18977 C  CB    . PRO A 1 4037 ? 187.487 145.601 140.576 1.00 68.60  ? 4037 PRO A CB    1 
ATOM   18978 C  CG    . PRO A 1 4037 ? 187.418 144.233 139.983 1.00 73.95  ? 4037 PRO A CG    1 
ATOM   18979 C  CD    . PRO A 1 4037 ? 187.798 143.298 141.082 1.00 72.04  ? 4037 PRO A CD    1 
ATOM   18980 N  N     . ASN A 1 4038 ? 184.668 144.997 142.034 1.00 77.55  ? 4038 ASN A N     1 
ATOM   18981 C  CA    . ASN A 1 4038 ? 183.273 145.356 142.260 1.00 76.43  ? 4038 ASN A CA    1 
ATOM   18982 C  C     . ASN A 1 4038 ? 182.912 145.391 143.739 1.00 85.06  ? 4038 ASN A C     1 
ATOM   18983 O  O     . ASN A 1 4038 ? 181.818 145.846 144.085 1.00 81.93  ? 4038 ASN A O     1 
ATOM   18984 C  CB    . ASN A 1 4038 ? 182.357 144.377 141.527 1.00 78.06  ? 4038 ASN A CB    1 
ATOM   18985 C  CG    . ASN A 1 4038 ? 181.127 145.048 140.961 1.00 83.87  ? 4038 ASN A CG    1 
ATOM   18986 O  OD1   . ASN A 1 4038 ? 180.987 146.268 141.028 1.00 86.02  ? 4038 ASN A OD1   1 
ATOM   18987 N  ND2   . ASN A 1 4038 ? 180.224 144.254 140.399 1.00 84.12  ? 4038 ASN A ND2   1 
ATOM   18988 N  N     . THR A 1 4039 ? 183.799 144.919 144.613 1.00 80.18  ? 4039 THR A N     1 
ATOM   18989 C  CA    . THR A 1 4039 ? 183.518 144.872 146.041 1.00 67.57  ? 4039 THR A CA    1 
ATOM   18990 C  C     . THR A 1 4039 ? 184.215 146.030 146.741 1.00 64.70  ? 4039 THR A C     1 
ATOM   18991 O  O     . THR A 1 4039 ? 185.452 146.070 146.761 1.00 70.96  ? 4039 THR A O     1 
ATOM   18992 C  CB    . THR A 1 4039 ? 183.983 143.554 146.636 1.00 66.73  ? 4039 THR A CB    1 
ATOM   18993 O  OG1   . THR A 1 4039 ? 183.254 142.475 146.039 1.00 73.68  ? 4039 THR A OG1   1 
ATOM   18994 C  CG2   . THR A 1 4039 ? 183.761 143.537 148.136 1.00 63.87  ? 4039 THR A CG2   1 
ATOM   18995 N  N     . PRO A 1 4040 ? 183.483 146.984 147.312 1.00 57.75  ? 4040 PRO A N     1 
ATOM   18996 C  CA    . PRO A 1 4040 ? 184.137 148.068 148.049 1.00 58.63  ? 4040 PRO A CA    1 
ATOM   18997 C  C     . PRO A 1 4040 ? 184.820 147.550 149.302 1.00 65.13  ? 4040 PRO A C     1 
ATOM   18998 O  O     . PRO A 1 4040 ? 184.385 146.575 149.919 1.00 77.68  ? 4040 PRO A O     1 
ATOM   18999 C  CB    . PRO A 1 4040 ? 182.980 149.011 148.396 1.00 48.58  ? 4040 PRO A CB    1 
ATOM   19000 C  CG    . PRO A 1 4040 ? 181.777 148.140 148.398 1.00 52.94  ? 4040 PRO A CG    1 
ATOM   19001 C  CD    . PRO A 1 4040 ? 182.015 147.098 147.343 1.00 59.83  ? 4040 PRO A CD    1 
ATOM   19002 N  N     . VAL A 1 4041 ? 185.905 148.217 149.676 1.00 50.16  ? 4041 VAL A N     1 
ATOM   19003 C  CA    . VAL A 1 4041 ? 186.666 147.873 150.870 1.00 40.42  ? 4041 VAL A CA    1 
ATOM   19004 C  C     . VAL A 1 4041 ? 186.176 148.788 151.986 1.00 51.19  ? 4041 VAL A C     1 
ATOM   19005 O  O     . VAL A 1 4041 ? 186.541 149.964 152.049 1.00 62.57  ? 4041 VAL A O     1 
ATOM   19006 C  CB    . VAL A 1 4041 ? 188.173 148.006 150.642 1.00 43.88  ? 4041 VAL A CB    1 
ATOM   19007 C  CG1   . VAL A 1 4041 ? 188.930 147.631 151.902 1.00 48.70  ? 4041 VAL A CG1   1 
ATOM   19008 C  CG2   . VAL A 1 4041 ? 188.606 147.131 149.480 1.00 49.57  ? 4041 VAL A CG2   1 
ATOM   19009 N  N     . LEU A 1 4042 ? 185.344 148.246 152.870 1.00 56.53  ? 4042 LEU A N     1 
ATOM   19010 C  CA    . LEU A 1 4042 ? 184.793 149.001 153.990 1.00 51.12  ? 4042 LEU A CA    1 
ATOM   19011 C  C     . LEU A 1 4042 ? 185.779 148.934 155.147 1.00 59.01  ? 4042 LEU A C     1 
ATOM   19012 O  O     . LEU A 1 4042 ? 186.132 147.845 155.609 1.00 68.64  ? 4042 LEU A O     1 
ATOM   19013 C  CB    . LEU A 1 4042 ? 183.431 148.447 154.397 1.00 47.05  ? 4042 LEU A CB    1 
ATOM   19014 C  CG    . LEU A 1 4042 ? 182.362 148.449 153.307 1.00 52.33  ? 4042 LEU A CG    1 
ATOM   19015 C  CD1   . LEU A 1 4042 ? 181.098 147.782 153.806 1.00 61.54  ? 4042 LEU A CD1   1 
ATOM   19016 C  CD2   . LEU A 1 4042 ? 182.076 149.866 152.853 1.00 61.70  ? 4042 LEU A CD2   1 
ATOM   19017 N  N     . MET A 1 4043 ? 186.224 150.095 155.614 1.00 61.83  ? 4043 MET A N     1 
ATOM   19018 C  CA    . MET A 1 4043 ? 187.198 150.180 156.698 1.00 60.35  ? 4043 MET A CA    1 
ATOM   19019 C  C     . MET A 1 4043 ? 186.525 150.855 157.886 1.00 66.05  ? 4043 MET A C     1 
ATOM   19020 O  O     . MET A 1 4043 ? 186.637 152.069 158.070 1.00 75.30  ? 4043 MET A O     1 
ATOM   19021 C  CB    . MET A 1 4043 ? 188.435 150.943 156.246 1.00 48.43  ? 4043 MET A CB    1 
ATOM   19022 C  CG    . MET A 1 4043 ? 188.992 150.450 154.931 1.00 59.50  ? 4043 MET A CG    1 
ATOM   19023 S  SD    . MET A 1 4043 ? 190.660 151.039 154.633 1.00 86.29  ? 4043 MET A SD    1 
ATOM   19024 C  CE    . MET A 1 4043 ? 191.601 149.542 154.903 1.00 70.33  ? 4043 MET A CE    1 
ATOM   19025 N  N     . CYS A 1 4044 ? 185.833 150.062 158.696 1.00 56.70  ? 4044 CYS A N     1 
ATOM   19026 C  CA    . CYS A 1 4044 ? 185.145 150.557 159.878 1.00 58.02  ? 4044 CYS A CA    1 
ATOM   19027 C  C     . CYS A 1 4044 ? 186.130 150.633 161.035 1.00 59.54  ? 4044 CYS A C     1 
ATOM   19028 O  O     . CYS A 1 4044 ? 186.794 149.643 161.356 1.00 71.84  ? 4044 CYS A O     1 
ATOM   19029 C  CB    . CYS A 1 4044 ? 183.965 149.655 160.237 1.00 69.69  ? 4044 CYS A CB    1 
ATOM   19030 S  SG    . CYS A 1 4044 ? 182.981 149.129 158.816 1.00 80.85  ? 4044 CYS A SG    1 
ATOM   19031 N  N     . SER A 1 4045 ? 186.222 151.803 161.657 1.00 60.31  ? 4045 SER A N     1 
ATOM   19032 C  CA    . SER A 1 4045 ? 187.192 152.047 162.711 1.00 63.36  ? 4045 SER A CA    1 
ATOM   19033 C  C     . SER A 1 4045 ? 186.494 152.585 163.950 1.00 65.30  ? 4045 SER A C     1 
ATOM   19034 O  O     . SER A 1 4045 ? 185.575 153.402 163.861 1.00 67.12  ? 4045 SER A O     1 
ATOM   19035 C  CB    . SER A 1 4045 ? 188.272 153.031 162.254 1.00 65.52  ? 4045 SER A CB    1 
ATOM   19036 O  OG    . SER A 1 4045 ? 187.694 154.242 161.801 1.00 69.80  ? 4045 SER A OG    1 
ATOM   19037 N  N     . VAL A 1 4046 ? 186.947 152.119 165.109 1.00 70.46  ? 4046 VAL A N     1 
ATOM   19038 C  CA    . VAL A 1 4046 ? 186.427 152.577 166.395 1.00 71.46  ? 4046 VAL A CA    1 
ATOM   19039 C  C     . VAL A 1 4046 ? 186.845 154.031 166.583 1.00 79.84  ? 4046 VAL A C     1 
ATOM   19040 O  O     . VAL A 1 4046 ? 187.801 154.481 165.934 1.00 85.52  ? 4046 VAL A O     1 
ATOM   19041 C  CB    . VAL A 1 4046 ? 186.926 151.687 167.544 1.00 67.78  ? 4046 VAL A CB    1 
ATOM   19042 C  CG1   . VAL A 1 4046 ? 186.444 150.260 167.353 1.00 70.79  ? 4046 VAL A CG1   1 
ATOM   19043 C  CG2   . VAL A 1 4046 ? 188.439 151.734 167.629 1.00 73.85  ? 4046 VAL A CG2   1 
ATOM   19044 N  N     . PRO A 1 4047 ? 186.159 154.804 167.428 1.00 81.98  ? 4047 PRO A N     1 
ATOM   19045 C  CA    . PRO A 1 4047 ? 186.511 156.222 167.577 1.00 74.74  ? 4047 PRO A CA    1 
ATOM   19046 C  C     . PRO A 1 4047 ? 187.960 156.409 168.002 1.00 78.39  ? 4047 PRO A C     1 
ATOM   19047 O  O     . PRO A 1 4047 ? 188.499 155.642 168.803 1.00 77.58  ? 4047 PRO A O     1 
ATOM   19048 C  CB    . PRO A 1 4047 ? 185.543 156.713 168.657 1.00 78.42  ? 4047 PRO A CB    1 
ATOM   19049 C  CG    . PRO A 1 4047 ? 184.373 155.807 168.543 1.00 81.09  ? 4047 PRO A CG    1 
ATOM   19050 C  CD    . PRO A 1 4047 ? 184.930 154.464 168.166 1.00 82.93  ? 4047 PRO A CD    1 
ATOM   19051 N  N     . GLY A 1 4048 ? 188.588 157.447 167.451 1.00 79.22  ? 4048 GLY A N     1 
ATOM   19052 C  CA    . GLY A 1 4048 ? 189.978 157.744 167.713 1.00 76.76  ? 4048 GLY A CA    1 
ATOM   19053 C  C     . GLY A 1 4048 ? 190.967 157.089 166.775 1.00 80.57  ? 4048 GLY A C     1 
ATOM   19054 O  O     . GLY A 1 4048 ? 192.171 157.353 166.890 1.00 82.15  ? 4048 GLY A O     1 
ATOM   19055 N  N     . TYR A 1 4049 ? 190.507 156.244 165.857 1.00 84.42  ? 4049 TYR A N     1 
ATOM   19056 C  CA    . TYR A 1 4049 ? 191.368 155.576 164.892 1.00 85.19  ? 4049 TYR A CA    1 
ATOM   19057 C  C     . TYR A 1 4049 ? 190.819 155.777 163.488 1.00 85.92  ? 4049 TYR A C     1 
ATOM   19058 O  O     . TYR A 1 4049 ? 189.604 155.744 163.274 1.00 91.09  ? 4049 TYR A O     1 
ATOM   19059 C  CB    . TYR A 1 4049 ? 191.508 154.074 165.194 1.00 85.77  ? 4049 TYR A CB    1 
ATOM   19060 C  CG    . TYR A 1 4049 ? 192.025 153.763 166.584 1.00 87.54  ? 4049 TYR A CG    1 
ATOM   19061 C  CD1   . TYR A 1 4049 ? 191.244 153.983 167.711 1.00 90.92  ? 4049 TYR A CD1   1 
ATOM   19062 C  CD2   . TYR A 1 4049 ? 193.308 153.264 166.766 1.00 88.50  ? 4049 TYR A CD2   1 
ATOM   19063 C  CE1   . TYR A 1 4049 ? 191.720 153.707 168.975 1.00 93.31  ? 4049 TYR A CE1   1 
ATOM   19064 C  CE2   . TYR A 1 4049 ? 193.792 152.986 168.026 1.00 93.36  ? 4049 TYR A CE2   1 
ATOM   19065 C  CZ    . TYR A 1 4049 ? 192.995 153.209 169.126 1.00 94.80  ? 4049 TYR A CZ    1 
ATOM   19066 O  OH    . TYR A 1 4049 ? 193.477 152.936 170.384 1.00 95.38  ? 4049 TYR A OH    1 
ATOM   19067 N  N     . ASP A 1 4050 ? 191.724 155.991 162.535 1.00 90.04  ? 4050 ASP A N     1 
ATOM   19068 C  CA    . ASP A 1 4050 ? 191.356 156.224 161.143 1.00 92.74  ? 4050 ASP A CA    1 
ATOM   19069 C  C     . ASP A 1 4050 ? 192.169 155.288 160.265 1.00 92.42  ? 4050 ASP A C     1 
ATOM   19070 O  O     . ASP A 1 4050 ? 193.356 155.069 160.522 1.00 94.91  ? 4050 ASP A O     1 
ATOM   19071 C  CB    . ASP A 1 4050 ? 191.599 157.684 160.746 1.00 95.15  ? 4050 ASP A CB    1 
ATOM   19072 C  CG    . ASP A 1 4050 ? 190.935 158.054 159.430 1.00 98.68  ? 4050 ASP A CG    1 
ATOM   19073 O  OD1   . ASP A 1 4050 ? 190.762 157.171 158.564 1.00 101.08 ? 4050 ASP A OD1   1 
ATOM   19074 O  OD2   . ASP A 1 4050 ? 190.583 159.239 159.261 1.00 97.04  ? 4050 ASP A OD2   1 
ATOM   19075 N  N     . ALA A 1 4051 ? 191.530 154.739 159.237 1.00 78.78  ? 4051 ALA A N     1 
ATOM   19076 C  CA    . ALA A 1 4051 ? 192.194 153.862 158.285 1.00 84.59  ? 4051 ALA A CA    1 
ATOM   19077 C  C     . ALA A 1 4051 ? 192.672 154.592 157.037 1.00 84.73  ? 4051 ALA A C     1 
ATOM   19078 O  O     . ALA A 1 4051 ? 193.184 153.944 156.119 1.00 91.80  ? 4051 ALA A O     1 
ATOM   19079 C  CB    . ALA A 1 4051 ? 191.260 152.719 157.882 1.00 88.84  ? 4051 ALA A CB    1 
ATOM   19080 N  N     . SER A 1 4052 ? 192.507 155.915 156.976 1.00 71.39  ? 4052 SER A N     1 
ATOM   19081 C  CA    . SER A 1 4052 ? 192.920 156.657 155.789 1.00 76.15  ? 4052 SER A CA    1 
ATOM   19082 C  C     . SER A 1 4052 ? 194.423 156.552 155.565 1.00 80.39  ? 4052 SER A C     1 
ATOM   19083 O  O     . SER A 1 4052 ? 194.874 156.291 154.443 1.00 83.57  ? 4052 SER A O     1 
ATOM   19084 C  CB    . SER A 1 4052 ? 192.501 158.121 155.916 1.00 80.43  ? 4052 SER A CB    1 
ATOM   19085 O  OG    . SER A 1 4052 ? 191.120 158.232 156.213 1.00 86.53  ? 4052 SER A OG    1 
ATOM   19086 N  N     . GLY A 1 4053 ? 195.211 156.738 156.626 1.00 89.02  ? 4053 GLY A N     1 
ATOM   19087 C  CA    . GLY A 1 4053 ? 196.656 156.677 156.482 1.00 88.17  ? 4053 GLY A CA    1 
ATOM   19088 C  C     . GLY A 1 4053 ? 197.136 155.328 155.985 1.00 89.67  ? 4053 GLY A C     1 
ATOM   19089 O  O     . GLY A 1 4053 ? 198.077 155.247 155.192 1.00 96.25  ? 4053 GLY A O     1 
ATOM   19090 N  N     . HIS A 1 4054 ? 196.490 154.251 156.437 1.00 82.27  ? 4054 HIS A N     1 
ATOM   19091 C  CA    . HIS A 1 4054 ? 196.853 152.919 155.968 1.00 80.95  ? 4054 HIS A CA    1 
ATOM   19092 C  C     . HIS A 1 4054 ? 196.701 152.818 154.457 1.00 83.10  ? 4054 HIS A C     1 
ATOM   19093 O  O     . HIS A 1 4054 ? 197.590 152.312 153.763 1.00 79.29  ? 4054 HIS A O     1 
ATOM   19094 C  CB    . HIS A 1 4054 ? 195.992 151.865 156.663 1.00 78.46  ? 4054 HIS A CB    1 
ATOM   19095 C  CG    . HIS A 1 4054 ? 196.300 151.691 158.118 1.00 78.72  ? 4054 HIS A CG    1 
ATOM   19096 N  ND1   . HIS A 1 4054 ? 196.375 150.454 158.719 1.00 82.17  ? 4054 HIS A ND1   1 
ATOM   19097 C  CD2   . HIS A 1 4054 ? 196.546 152.598 159.092 1.00 78.93  ? 4054 HIS A CD2   1 
ATOM   19098 C  CE1   . HIS A 1 4054 ? 196.656 150.605 160.001 1.00 85.61  ? 4054 HIS A CE1   1 
ATOM   19099 N  NE2   . HIS A 1 4054 ? 196.766 151.897 160.253 1.00 88.42  ? 4054 HIS A NE2   1 
ATOM   19100 N  N     . VAL A 1 4055 ? 195.588 153.325 153.925 1.00 82.02  ? 4055 VAL A N     1 
ATOM   19101 C  CA    . VAL A 1 4055 ? 195.345 153.235 152.489 1.00 78.37  ? 4055 VAL A CA    1 
ATOM   19102 C  C     . VAL A 1 4055 ? 196.299 154.142 151.721 1.00 86.39  ? 4055 VAL A C     1 
ATOM   19103 O  O     . VAL A 1 4055 ? 196.777 153.782 150.640 1.00 86.93  ? 4055 VAL A O     1 
ATOM   19104 C  CB    . VAL A 1 4055 ? 193.873 153.553 152.177 1.00 73.03  ? 4055 VAL A CB    1 
ATOM   19105 C  CG1   . VAL A 1 4055 ? 193.698 153.882 150.711 1.00 81.20  ? 4055 VAL A CG1   1 
ATOM   19106 C  CG2   . VAL A 1 4055 ? 193.008 152.375 152.543 1.00 77.14  ? 4055 VAL A CG2   1 
ATOM   19107 N  N     . GLU A 1 4056 ? 196.588 155.334 152.253 1.00 98.88  ? 4056 GLU A N     1 
ATOM   19108 C  CA    . GLU A 1 4056 ? 197.532 156.212 151.566 1.00 95.04  ? 4056 GLU A CA    1 
ATOM   19109 C  C     . GLU A 1 4056 ? 198.920 155.585 151.492 1.00 100.20 ? 4056 GLU A C     1 
ATOM   19110 O  O     . GLU A 1 4056 ? 199.569 155.621 150.439 1.00 106.81 ? 4056 GLU A O     1 
ATOM   19111 C  CB    . GLU A 1 4056 ? 197.588 157.580 152.246 1.00 94.55  ? 4056 GLU A CB    1 
ATOM   19112 C  CG    . GLU A 1 4056 ? 196.228 158.206 152.495 1.00 99.76  ? 4056 GLU A CG    1 
ATOM   19113 C  CD    . GLU A 1 4056 ? 195.908 159.318 151.517 1.00 108.34 ? 4056 GLU A CD    1 
ATOM   19114 O  OE1   . GLU A 1 4056 ? 196.660 159.481 150.533 1.00 110.56 ? 4056 GLU A OE1   1 
ATOM   19115 O  OE2   . GLU A 1 4056 ? 194.902 160.028 151.729 1.00 105.95 ? 4056 GLU A OE2   1 
ATOM   19116 N  N     . ASP A 1 4057 ? 199.389 154.987 152.591 1.00 93.37  ? 4057 ASP A N     1 
ATOM   19117 C  CA    . ASP A 1 4057 ? 200.681 154.307 152.555 1.00 92.19  ? 4057 ASP A CA    1 
ATOM   19118 C  C     . ASP A 1 4057 ? 200.645 153.089 151.641 1.00 94.50  ? 4057 ASP A C     1 
ATOM   19119 O  O     . ASP A 1 4057 ? 201.635 152.783 150.967 1.00 99.18  ? 4057 ASP A O     1 
ATOM   19120 C  CB    . ASP A 1 4057 ? 201.121 153.913 153.965 1.00 95.61  ? 4057 ASP A CB    1 
ATOM   19121 C  CG    . ASP A 1 4057 ? 200.972 155.045 154.960 1.00 100.71 ? 4057 ASP A CG    1 
ATOM   19122 O  OD1   . ASP A 1 4057 ? 200.608 156.163 154.538 1.00 100.18 ? 4057 ASP A OD1   1 
ATOM   19123 O  OD2   . ASP A 1 4057 ? 201.218 154.818 156.163 1.00 98.76  ? 4057 ASP A OD2   1 
ATOM   19124 N  N     . LEU A 1 4058 ? 199.518 152.374 151.608 1.00 87.08  ? 4058 LEU A N     1 
ATOM   19125 C  CA    . LEU A 1 4058 ? 199.396 151.233 150.707 1.00 92.02  ? 4058 LEU A CA    1 
ATOM   19126 C  C     . LEU A 1 4058 ? 199.496 151.669 149.251 1.00 93.72  ? 4058 LEU A C     1 
ATOM   19127 O  O     . LEU A 1 4058 ? 200.161 151.014 148.441 1.00 96.85  ? 4058 LEU A O     1 
ATOM   19128 C  CB    . LEU A 1 4058 ? 198.076 150.507 150.964 1.00 88.45  ? 4058 LEU A CB    1 
ATOM   19129 C  CG    . LEU A 1 4058 ? 197.687 149.415 149.968 1.00 84.83  ? 4058 LEU A CG    1 
ATOM   19130 C  CD1   . LEU A 1 4058 ? 198.713 148.297 149.979 1.00 86.86  ? 4058 LEU A CD1   1 
ATOM   19131 C  CD2   . LEU A 1 4058 ? 196.302 148.877 150.283 1.00 83.88  ? 4058 LEU A CD2   1 
ATOM   19132 N  N     . ALA A 1 4059 ? 198.837 152.775 148.901 1.00 91.60  ? 4059 ALA A N     1 
ATOM   19133 C  CA    . ALA A 1 4059 ? 198.918 153.291 147.539 1.00 90.72  ? 4059 ALA A CA    1 
ATOM   19134 C  C     . ALA A 1 4059 ? 200.323 153.779 147.219 1.00 92.34  ? 4059 ALA A C     1 
ATOM   19135 O  O     . ALA A 1 4059 ? 200.811 153.598 146.098 1.00 98.67  ? 4059 ALA A O     1 
ATOM   19136 C  CB    . ALA A 1 4059 ? 197.899 154.412 147.339 1.00 90.61  ? 4059 ALA A CB    1 
ATOM   19137 N  N     . ALA A 1 4060 ? 200.987 154.412 148.190 1.00 94.18  ? 4060 ALA A N     1 
ATOM   19138 C  CA    . ALA A 1 4060 ? 202.358 154.863 147.974 1.00 97.10  ? 4060 ALA A CA    1 
ATOM   19139 C  C     . ALA A 1 4060 ? 203.297 153.687 147.736 1.00 98.54  ? 4060 ALA A C     1 
ATOM   19140 O  O     . ALA A 1 4060 ? 204.191 153.758 146.886 1.00 103.09 ? 4060 ALA A O     1 
ATOM   19141 C  CB    . ALA A 1 4060 ? 202.831 155.697 149.164 1.00 97.86  ? 4060 ALA A CB    1 
ATOM   19142 N  N     . GLU A 1 4061 ? 203.114 152.597 148.486 1.00 102.53 ? 4061 GLU A N     1 
ATOM   19143 C  CA    . GLU A 1 4061 ? 203.987 151.437 148.339 1.00 104.93 ? 4061 GLU A CA    1 
ATOM   19144 C  C     . GLU A 1 4061 ? 203.853 150.807 146.958 1.00 109.84 ? 4061 GLU A C     1 
ATOM   19145 O  O     . GLU A 1 4061 ? 204.857 150.465 146.323 1.00 111.70 ? 4061 GLU A O     1 
ATOM   19146 C  CB    . GLU A 1 4061 ? 203.678 150.409 149.427 1.00 108.66 ? 4061 GLU A CB    1 
ATOM   19147 C  CG    . GLU A 1 4061 ? 204.308 149.047 149.189 1.00 111.89 ? 4061 GLU A CG    1 
ATOM   19148 C  CD    . GLU A 1 4061 ? 204.457 148.242 150.464 1.00 111.09 ? 4061 GLU A CD    1 
ATOM   19149 O  OE1   . GLU A 1 4061 ? 203.603 147.367 150.719 1.00 109.92 ? 4061 GLU A OE1   1 
ATOM   19150 O  OE2   . GLU A 1 4061 ? 205.428 148.484 151.212 1.00 110.29 ? 4061 GLU A OE2   1 
ATOM   19151 N  N     . GLN A 1 4062 ? 202.624 150.649 146.474 1.00 105.88 ? 4062 GLN A N     1 
ATOM   19152 C  CA    . GLN A 1 4062 ? 202.373 150.004 145.193 1.00 102.73 ? 4062 GLN A CA    1 
ATOM   19153 C  C     . GLN A 1 4062 ? 202.531 150.946 144.008 1.00 103.51 ? 4062 GLN A C     1 
ATOM   19154 O  O     . GLN A 1 4062 ? 202.425 150.494 142.863 1.00 107.95 ? 4062 GLN A O     1 
ATOM   19155 C  CB    . GLN A 1 4062 ? 200.966 149.399 145.170 1.00 100.07 ? 4062 GLN A CB    1 
ATOM   19156 C  CG    . GLN A 1 4062 ? 200.657 148.473 146.330 1.00 99.87  ? 4062 GLN A CG    1 
ATOM   19157 C  CD    . GLN A 1 4062 ? 199.577 147.467 145.988 1.00 104.34 ? 4062 GLN A CD    1 
ATOM   19158 O  OE1   . GLN A 1 4062 ? 199.171 147.344 144.833 1.00 104.55 ? 4062 GLN A OE1   1 
ATOM   19159 N  NE2   . GLN A 1 4062 ? 199.102 146.743 146.994 1.00 108.77 ? 4062 GLN A NE2   1 
ATOM   19160 N  N     . ASN A 1 4063 ? 202.788 152.232 144.255 1.00 99.45  ? 4063 ASN A N     1 
ATOM   19161 C  CA    . ASN A 1 4063 ? 202.835 153.245 143.200 1.00 101.12 ? 4063 ASN A CA    1 
ATOM   19162 C  C     . ASN A 1 4063 ? 201.537 153.210 142.388 1.00 107.21 ? 4063 ASN A C     1 
ATOM   19163 O  O     . ASN A 1 4063 ? 201.500 152.785 141.232 1.00 108.56 ? 4063 ASN A O     1 
ATOM   19164 C  CB    . ASN A 1 4063 ? 204.086 153.073 142.324 1.00 102.78 ? 4063 ASN A CB    1 
ATOM   19165 C  CG    . ASN A 1 4063 ? 203.975 153.759 140.971 1.00 108.08 ? 4063 ASN A CG    1 
ATOM   19166 O  OD1   . ASN A 1 4063 ? 203.736 154.964 140.890 1.00 105.50 ? 4063 ASN A OD1   1 
ATOM   19167 N  ND2   . ASN A 1 4063 ? 204.144 152.989 139.901 1.00 107.33 ? 4063 ASN A ND2   1 
ATOM   19168 N  N     . THR A 1 4064 ? 200.437 153.574 143.040 1.00 102.54 ? 4064 THR A N     1 
ATOM   19169 C  CA    . THR A 1 4064 ? 199.120 153.597 142.422 1.00 98.90  ? 4064 THR A CA    1 
ATOM   19170 C  C     . THR A 1 4064 ? 198.460 154.939 142.701 1.00 94.81  ? 4064 THR A C     1 
ATOM   19171 O  O     . THR A 1 4064 ? 198.337 155.344 143.862 1.00 96.12  ? 4064 THR A O     1 
ATOM   19172 C  CB    . THR A 1 4064 ? 198.245 152.458 142.950 1.00 100.51 ? 4064 THR A CB    1 
ATOM   19173 O  OG1   . THR A 1 4064 ? 199.020 151.254 143.023 1.00 100.06 ? 4064 THR A OG1   1 
ATOM   19174 C  CG2   . THR A 1 4064 ? 197.058 152.230 142.030 1.00 99.23  ? 4064 THR A CG2   1 
ATOM   19175 N  N     . GLN A 1 4065 ? 198.042 155.625 141.640 1.00 99.78  ? 4065 GLN A N     1 
ATOM   19176 C  CA    . GLN A 1 4065 ? 197.385 156.914 141.800 1.00 105.80 ? 4065 GLN A CA    1 
ATOM   19177 C  C     . GLN A 1 4065 ? 196.043 156.732 142.495 1.00 102.93 ? 4065 GLN A C     1 
ATOM   19178 O  O     . GLN A 1 4065 ? 195.241 155.876 142.109 1.00 105.64 ? 4065 GLN A O     1 
ATOM   19179 C  CB    . GLN A 1 4065 ? 197.198 157.589 140.443 1.00 107.20 ? 4065 GLN A CB    1 
ATOM   19180 C  CG    . GLN A 1 4065 ? 198.329 158.531 140.061 1.00 106.13 ? 4065 GLN A CG    1 
ATOM   19181 C  CD    . GLN A 1 4065 ? 199.553 157.799 139.550 1.00 108.81 ? 4065 GLN A CD    1 
ATOM   19182 O  OE1   . GLN A 1 4065 ? 200.650 157.951 140.088 1.00 109.36 ? 4065 GLN A OE1   1 
ATOM   19183 N  NE2   . GLN A 1 4065 ? 199.373 157.000 138.506 1.00 105.59 ? 4065 GLN A NE2   1 
ATOM   19184 N  N     . ILE A 1 4066 ? 195.798 157.540 143.523 1.00 78.55  ? 4066 ILE A N     1 
ATOM   19185 C  CA    . ILE A 1 4066 ? 194.621 157.408 144.370 1.00 75.88  ? 4066 ILE A CA    1 
ATOM   19186 C  C     . ILE A 1 4066 ? 193.960 158.773 144.506 1.00 80.11  ? 4066 ILE A C     1 
ATOM   19187 O  O     . ILE A 1 4066 ? 194.646 159.786 144.680 1.00 84.21  ? 4066 ILE A O     1 
ATOM   19188 C  CB    . ILE A 1 4066 ? 194.980 156.833 145.754 1.00 73.04  ? 4066 ILE A CB    1 
ATOM   19189 C  CG1   . ILE A 1 4066 ? 193.753 156.812 146.664 1.00 74.14  ? 4066 ILE A CG1   1 
ATOM   19190 C  CG2   . ILE A 1 4066 ? 196.119 157.617 146.390 1.00 79.98  ? 4066 ILE A CG2   1 
ATOM   19191 C  CD1   . ILE A 1 4066 ? 193.998 156.140 147.984 1.00 73.86  ? 4066 ILE A CD1   1 
ATOM   19192 N  N     . THR A 1 4067 ? 192.634 158.799 144.409 1.00 74.90  ? 4067 THR A N     1 
ATOM   19193 C  CA    . THR A 1 4067 ? 191.851 160.015 144.592 1.00 73.86  ? 4067 THR A CA    1 
ATOM   19194 C  C     . THR A 1 4067 ? 191.094 159.899 145.909 1.00 73.01  ? 4067 THR A C     1 
ATOM   19195 O  O     . THR A 1 4067 ? 190.174 159.084 146.033 1.00 79.62  ? 4067 THR A O     1 
ATOM   19196 C  CB    . THR A 1 4067 ? 190.891 160.228 143.424 1.00 73.02  ? 4067 THR A CB    1 
ATOM   19197 O  OG1   . THR A 1 4067 ? 191.634 160.322 142.203 1.00 73.69  ? 4067 THR A OG1   1 
ATOM   19198 C  CG2   . THR A 1 4067 ? 190.092 161.505 143.622 1.00 74.45  ? 4067 THR A CG2   1 
ATOM   19199 N  N     . SER A 1 4068 ? 191.478 160.710 146.889 1.00 64.06  ? 4068 SER A N     1 
ATOM   19200 C  CA    . SER A 1 4068 ? 190.854 160.699 148.204 1.00 66.26  ? 4068 SER A CA    1 
ATOM   19201 C  C     . SER A 1 4068 ? 189.905 161.883 148.324 1.00 69.67  ? 4068 SER A C     1 
ATOM   19202 O  O     . SER A 1 4068 ? 190.311 163.033 148.131 1.00 79.15  ? 4068 SER A O     1 
ATOM   19203 C  CB    . SER A 1 4068 ? 191.909 160.750 149.310 1.00 72.59  ? 4068 SER A CB    1 
ATOM   19204 O  OG    . SER A 1 4068 ? 192.273 162.086 149.604 1.00 83.04  ? 4068 SER A OG    1 
ATOM   19205 N  N     . ILE A 1 4069 ? 188.645 161.598 148.645 1.00 61.72  ? 4069 ILE A N     1 
ATOM   19206 C  CA    . ILE A 1 4069 ? 187.599 162.609 148.730 1.00 63.82  ? 4069 ILE A CA    1 
ATOM   19207 C  C     . ILE A 1 4069 ? 186.918 162.487 150.085 1.00 64.10  ? 4069 ILE A C     1 
ATOM   19208 O  O     . ILE A 1 4069 ? 186.566 161.381 150.509 1.00 76.24  ? 4069 ILE A O     1 
ATOM   19209 C  CB    . ILE A 1 4069 ? 186.572 162.460 147.591 1.00 64.44  ? 4069 ILE A CB    1 
ATOM   19210 C  CG1   . ILE A 1 4069 ? 187.204 162.853 146.256 1.00 66.83  ? 4069 ILE A CG1   1 
ATOM   19211 C  CG2   . ILE A 1 4069 ? 185.336 163.298 147.864 1.00 67.21  ? 4069 ILE A CG2   1 
ATOM   19212 C  CD1   . ILE A 1 4069 ? 186.682 162.062 145.085 1.00 69.48  ? 4069 ILE A CD1   1 
ATOM   19213 N  N     . ALA A 1 4070 ? 186.737 163.617 150.761 1.00 58.15  ? 4070 ALA A N     1 
ATOM   19214 C  CA    . ALA A 1 4070 ? 186.061 163.661 152.050 1.00 55.11  ? 4070 ALA A CA    1 
ATOM   19215 C  C     . ALA A 1 4070 ? 184.571 163.878 151.819 1.00 64.02  ? 4070 ALA A C     1 
ATOM   19216 O  O     . ALA A 1 4070 ? 184.169 164.894 151.241 1.00 71.97  ? 4070 ALA A O     1 
ATOM   19217 C  CB    . ALA A 1 4070 ? 186.639 164.765 152.932 1.00 61.25  ? 4070 ALA A CB    1 
ATOM   19218 N  N     . ILE A 1 4071 ? 183.762 162.927 152.268 1.00 68.09  ? 4071 ILE A N     1 
ATOM   19219 C  CA    . ILE A 1 4071 ? 182.322 162.961 152.043 1.00 68.44  ? 4071 ILE A CA    1 
ATOM   19220 C  C     . ILE A 1 4071 ? 181.667 163.881 153.066 1.00 66.17  ? 4071 ILE A C     1 
ATOM   19221 O  O     . ILE A 1 4071 ? 182.111 163.986 154.215 1.00 70.88  ? 4071 ILE A O     1 
ATOM   19222 C  CB    . ILE A 1 4071 ? 181.750 161.529 152.101 1.00 66.06  ? 4071 ILE A CB    1 
ATOM   19223 C  CG1   . ILE A 1 4071 ? 182.274 160.707 150.925 1.00 63.93  ? 4071 ILE A CG1   1 
ATOM   19224 C  CG2   . ILE A 1 4071 ? 180.233 161.531 152.087 1.00 66.74  ? 4071 ILE A CG2   1 
ATOM   19225 C  CD1   . ILE A 1 4071 ? 182.114 161.390 149.587 1.00 59.35  ? 4071 ILE A CD1   1 
ATOM   19226 N  N     . GLY A 1 4072 ? 180.597 164.557 152.649 1.00 69.84  ? 4072 GLY A N     1 
ATOM   19227 C  CA    . GLY A 1 4072 ? 179.874 165.442 153.541 1.00 74.66  ? 4072 GLY A CA    1 
ATOM   19228 C  C     . GLY A 1 4072 ? 179.289 166.673 152.879 1.00 74.35  ? 4072 GLY A C     1 
ATOM   19229 O  O     . GLY A 1 4072 ? 178.396 167.313 153.441 1.00 78.53  ? 4072 GLY A O     1 
ATOM   19230 N  N     . SER A 1 4073 ? 179.773 167.015 151.689 1.00 81.84  ? 4073 SER A N     1 
ATOM   19231 C  CA    . SER A 1 4073 ? 179.289 168.176 150.957 1.00 85.08  ? 4073 SER A CA    1 
ATOM   19232 C  C     . SER A 1 4073 ? 178.804 167.748 149.578 1.00 89.38  ? 4073 SER A C     1 
ATOM   19233 O  O     . SER A 1 4073 ? 179.189 166.696 149.061 1.00 97.85  ? 4073 SER A O     1 
ATOM   19234 C  CB    . SER A 1 4073 ? 180.376 169.249 150.822 1.00 86.08  ? 4073 SER A CB    1 
ATOM   19235 O  OG    . SER A 1 4073 ? 181.573 168.695 150.308 1.00 91.22  ? 4073 SER A OG    1 
ATOM   19236 N  N     . ALA A 1 4074 ? 177.942 168.580 148.988 1.00 77.73  ? 4074 ALA A N     1 
ATOM   19237 C  CA    . ALA A 1 4074 ? 177.406 168.280 147.663 1.00 80.99  ? 4074 ALA A CA    1 
ATOM   19238 C  C     . ALA A 1 4074 ? 178.516 168.236 146.621 1.00 84.90  ? 4074 ALA A C     1 
ATOM   19239 O  O     . ALA A 1 4074 ? 178.542 167.350 145.756 1.00 88.25  ? 4074 ALA A O     1 
ATOM   19240 C  CB    . ALA A 1 4074 ? 176.345 169.311 147.281 1.00 81.50  ? 4074 ALA A CB    1 
ATOM   19241 N  N     . GLU A 1 4075 ? 179.445 169.192 146.687 1.00 90.12  ? 4075 GLU A N     1 
ATOM   19242 C  CA    . GLU A 1 4075 ? 180.618 169.130 145.824 1.00 90.26  ? 4075 GLU A CA    1 
ATOM   19243 C  C     . GLU A 1 4075 ? 181.430 167.874 146.098 1.00 91.55  ? 4075 GLU A C     1 
ATOM   19244 O  O     . GLU A 1 4075 ? 182.013 167.299 145.173 1.00 96.33  ? 4075 GLU A O     1 
ATOM   19245 C  CB    . GLU A 1 4075 ? 181.484 170.378 146.007 1.00 89.59  ? 4075 GLU A CB    1 
ATOM   19246 C  CG    . GLU A 1 4075 ? 180.716 171.696 146.014 1.00 95.06  ? 4075 GLU A CG    1 
ATOM   19247 C  CD    . GLU A 1 4075 ? 180.149 172.054 147.378 1.00 98.35  ? 4075 GLU A CD    1 
ATOM   19248 O  OE1   . GLU A 1 4075 ? 179.745 171.137 148.123 1.00 98.24  ? 4075 GLU A OE1   1 
ATOM   19249 O  OE2   . GLU A 1 4075 ? 180.105 173.259 147.704 1.00 95.80  ? 4075 GLU A OE2   1 
ATOM   19250 N  N     . GLY A 1 4076 ? 181.469 167.426 147.354 1.00 87.13  ? 4076 GLY A N     1 
ATOM   19251 C  CA    . GLY A 1 4076 ? 182.112 166.159 147.656 1.00 87.36  ? 4076 GLY A CA    1 
ATOM   19252 C  C     . GLY A 1 4076 ? 181.428 164.986 146.981 1.00 87.47  ? 4076 GLY A C     1 
ATOM   19253 O  O     . GLY A 1 4076 ? 182.089 164.084 146.465 1.00 90.84  ? 4076 GLY A O     1 
ATOM   19254 N  N     . PHE A 1 4077 ? 180.092 164.987 146.970 1.00 78.06  ? 4077 PHE A N     1 
ATOM   19255 C  CA    . PHE A 1 4077 ? 179.358 163.930 146.280 1.00 74.28  ? 4077 PHE A CA    1 
ATOM   19256 C  C     . PHE A 1 4077 ? 179.646 163.945 144.784 1.00 76.05  ? 4077 PHE A C     1 
ATOM   19257 O  O     . PHE A 1 4077 ? 179.851 162.889 144.173 1.00 81.48  ? 4077 PHE A O     1 
ATOM   19258 C  CB    . PHE A 1 4077 ? 177.858 164.078 146.532 1.00 70.91  ? 4077 PHE A CB    1 
ATOM   19259 C  CG    . PHE A 1 4077 ? 177.463 163.903 147.968 1.00 71.77  ? 4077 PHE A CG    1 
ATOM   19260 C  CD1   . PHE A 1 4077 ? 177.936 162.833 148.704 1.00 76.26  ? 4077 PHE A CD1   1 
ATOM   19261 C  CD2   . PHE A 1 4077 ? 176.610 164.806 148.579 1.00 76.25  ? 4077 PHE A CD2   1 
ATOM   19262 C  CE1   . PHE A 1 4077 ? 177.571 162.669 150.024 1.00 82.07  ? 4077 PHE A CE1   1 
ATOM   19263 C  CE2   . PHE A 1 4077 ? 176.242 164.647 149.899 1.00 76.70  ? 4077 PHE A CE2   1 
ATOM   19264 C  CZ    . PHE A 1 4077 ? 176.723 163.577 150.622 1.00 78.69  ? 4077 PHE A CZ    1 
ATOM   19265 N  N     . ASN A 1 4078 ? 179.661 165.134 144.177 1.00 78.89  ? 4078 ASN A N     1 
ATOM   19266 C  CA    . ASN A 1 4078 ? 179.948 165.224 142.747 1.00 82.44  ? 4078 ASN A CA    1 
ATOM   19267 C  C     . ASN A 1 4078 ? 181.366 164.759 142.438 1.00 84.54  ? 4078 ASN A C     1 
ATOM   19268 O  O     . ASN A 1 4078 ? 181.594 164.047 141.451 1.00 91.19  ? 4078 ASN A O     1 
ATOM   19269 C  CB    . ASN A 1 4078 ? 179.731 166.654 142.257 1.00 84.08  ? 4078 ASN A CB    1 
ATOM   19270 C  CG    . ASN A 1 4078 ? 178.331 167.158 142.537 1.00 90.17  ? 4078 ASN A CG    1 
ATOM   19271 O  OD1   . ASN A 1 4078 ? 177.541 166.491 143.205 1.00 92.86  ? 4078 ASN A OD1   1 
ATOM   19272 N  ND2   . ASN A 1 4078 ? 178.016 168.344 142.029 1.00 89.56  ? 4078 ASN A ND2   1 
ATOM   19273 N  N     . GLN A 1 4079 ? 182.333 165.152 143.272 1.00 74.57  ? 4079 GLN A N     1 
ATOM   19274 C  CA    . GLN A 1 4079 ? 183.707 164.709 143.073 1.00 75.54  ? 4079 GLN A CA    1 
ATOM   19275 C  C     . GLN A 1 4079 ? 183.826 163.199 143.219 1.00 82.49  ? 4079 GLN A C     1 
ATOM   19276 O  O     . GLN A 1 4079 ? 184.549 162.554 142.456 1.00 83.35  ? 4079 GLN A O     1 
ATOM   19277 C  CB    . GLN A 1 4079 ? 184.640 165.416 144.055 1.00 79.62  ? 4079 GLN A CB    1 
ATOM   19278 C  CG    . GLN A 1 4079 ? 184.895 166.875 143.732 1.00 83.34  ? 4079 GLN A CG    1 
ATOM   19279 C  CD    . GLN A 1 4079 ? 185.791 167.544 144.753 1.00 86.82  ? 4079 GLN A CD    1 
ATOM   19280 O  OE1   . GLN A 1 4079 ? 186.085 166.974 145.804 1.00 83.33  ? 4079 GLN A OE1   1 
ATOM   19281 N  NE2   . GLN A 1 4079 ? 186.230 168.759 144.450 1.00 84.83  ? 4079 GLN A NE2   1 
ATOM   19282 N  N     . ALA A 1 4080 ? 183.130 162.619 144.199 1.00 84.31  ? 4080 ALA A N     1 
ATOM   19283 C  CA    . ALA A 1 4080 ? 183.160 161.170 144.371 1.00 79.05  ? 4080 ALA A CA    1 
ATOM   19284 C  C     . ALA A 1 4080 ? 182.569 160.464 143.158 1.00 83.07  ? 4080 ALA A C     1 
ATOM   19285 O  O     . ALA A 1 4080 ? 183.118 159.465 142.677 1.00 87.74  ? 4080 ALA A O     1 
ATOM   19286 C  CB    . ALA A 1 4080 ? 182.412 160.777 145.644 1.00 79.29  ? 4080 ALA A CB    1 
ATOM   19287 N  N     . ASP A 1 4081 ? 181.447 160.976 142.646 1.00 89.83  ? 4081 ASP A N     1 
ATOM   19288 C  CA    . ASP A 1 4081 ? 180.821 160.376 141.472 1.00 87.81  ? 4081 ASP A CA    1 
ATOM   19289 C  C     . ASP A 1 4081 ? 181.776 160.423 140.284 1.00 87.60  ? 4081 ASP A C     1 
ATOM   19290 O  O     . ASP A 1 4081 ? 182.001 159.409 139.611 1.00 92.99  ? 4081 ASP A O     1 
ATOM   19291 C  CB    . ASP A 1 4081 ? 179.501 161.108 141.180 1.00 86.82  ? 4081 ASP A CB    1 
ATOM   19292 C  CG    . ASP A 1 4081 ? 178.968 160.905 139.751 1.00 92.73  ? 4081 ASP A CG    1 
ATOM   19293 O  OD1   . ASP A 1 4081 ? 177.950 161.553 139.430 1.00 93.34  ? 4081 ASP A OD1   1 
ATOM   19294 O  OD2   . ASP A 1 4081 ? 179.475 160.072 138.972 1.00 97.82  ? 4081 ASP A OD2   1 
ATOM   19295 N  N     . LYS A 1 4082 ? 182.366 161.594 140.027 1.00 70.54  ? 4082 LYS A N     1 
ATOM   19296 C  CA    . LYS A 1 4082 ? 183.272 161.726 138.890 1.00 71.19  ? 4082 LYS A CA    1 
ATOM   19297 C  C     . LYS A 1 4082 ? 184.506 160.848 139.056 1.00 75.58  ? 4082 LYS A C     1 
ATOM   19298 O  O     . LYS A 1 4082 ? 184.959 160.216 138.094 1.00 81.33  ? 4082 LYS A O     1 
ATOM   19299 C  CB    . LYS A 1 4082 ? 183.677 163.188 138.706 1.00 75.15  ? 4082 LYS A CB    1 
ATOM   19300 C  CG    . LYS A 1 4082 ? 182.619 164.047 138.033 1.00 76.40  ? 4082 LYS A CG    1 
ATOM   19301 C  CD    . LYS A 1 4082 ? 182.987 165.526 138.060 1.00 76.98  ? 4082 LYS A CD    1 
ATOM   19302 C  CE    . LYS A 1 4082 ? 184.495 165.741 138.059 1.00 77.07  ? 4082 LYS A CE    1 
ATOM   19303 N  NZ    . LYS A 1 4082 ? 185.112 165.404 136.745 1.00 79.63  ? 4082 LYS A NZ    1 
ATOM   19304 N  N     . ALA A 1 4083 ? 185.062 160.793 140.268 1.00 72.94  ? 4083 ALA A N     1 
ATOM   19305 C  CA    . ALA A 1 4083 ? 186.253 159.987 140.506 1.00 73.78  ? 4083 ALA A CA    1 
ATOM   19306 C  C     . ALA A 1 4083 ? 185.970 158.506 140.308 1.00 76.68  ? 4083 ALA A C     1 
ATOM   19307 O  O     . ALA A 1 4083 ? 186.784 157.792 139.716 1.00 78.79  ? 4083 ALA A O     1 
ATOM   19308 C  CB    . ALA A 1 4083 ? 186.791 160.247 141.911 1.00 73.32  ? 4083 ALA A CB    1 
ATOM   19309 N  N     . ILE A 1 4084 ? 184.825 158.024 140.797 1.00 76.13  ? 4084 ILE A N     1 
ATOM   19310 C  CA    . ILE A 1 4084 ? 184.476 156.620 140.598 1.00 75.90  ? 4084 ILE A CA    1 
ATOM   19311 C  C     . ILE A 1 4084 ? 184.261 156.330 139.119 1.00 76.55  ? 4084 ILE A C     1 
ATOM   19312 O  O     . ILE A 1 4084 ? 184.728 155.309 138.596 1.00 82.45  ? 4084 ILE A O     1 
ATOM   19313 C  CB    . ILE A 1 4084 ? 183.241 156.251 141.439 1.00 68.58  ? 4084 ILE A CB    1 
ATOM   19314 C  CG1   . ILE A 1 4084 ? 183.588 156.279 142.926 1.00 65.90  ? 4084 ILE A CG1   1 
ATOM   19315 C  CG2   . ILE A 1 4084 ? 182.719 154.880 141.050 1.00 73.18  ? 4084 ILE A CG2   1 
ATOM   19316 C  CD1   . ILE A 1 4084 ? 182.384 156.283 143.829 1.00 72.80  ? 4084 ILE A CD1   1 
ATOM   19317 N  N     . ASN A 1 4085 ? 183.559 157.225 138.417 1.00 75.24  ? 4085 ASN A N     1 
ATOM   19318 C  CA    . ASN A 1 4085 ? 183.305 157.011 136.995 1.00 75.95  ? 4085 ASN A CA    1 
ATOM   19319 C  C     . ASN A 1 4085 ? 184.603 156.990 136.198 1.00 75.70  ? 4085 ASN A C     1 
ATOM   19320 O  O     . ASN A 1 4085 ? 184.724 156.255 135.212 1.00 78.87  ? 4085 ASN A O     1 
ATOM   19321 C  CB    . ASN A 1 4085 ? 182.364 158.089 136.461 1.00 78.70  ? 4085 ASN A CB    1 
ATOM   19322 C  CG    . ASN A 1 4085 ? 180.923 157.853 136.861 1.00 82.98  ? 4085 ASN A CG    1 
ATOM   19323 O  OD1   . ASN A 1 4085 ? 180.560 156.763 137.300 1.00 79.82  ? 4085 ASN A OD1   1 
ATOM   19324 N  ND2   . ASN A 1 4085 ? 180.092 158.877 136.708 1.00 84.82  ? 4085 ASN A ND2   1 
ATOM   19325 N  N     . THR A 1 4086 ? 185.583 157.800 136.602 1.00 73.06  ? 4086 THR A N     1 
ATOM   19326 C  CA    . THR A 1 4086 ? 186.868 157.796 135.912 1.00 77.70  ? 4086 THR A CA    1 
ATOM   19327 C  C     . THR A 1 4086 ? 187.685 156.558 136.264 1.00 81.34  ? 4086 THR A C     1 
ATOM   19328 O  O     . THR A 1 4086 ? 188.324 155.959 135.391 1.00 85.69  ? 4086 THR A O     1 
ATOM   19329 C  CB    . THR A 1 4086 ? 187.649 159.065 136.249 1.00 78.65  ? 4086 THR A CB    1 
ATOM   19330 O  OG1   . THR A 1 4086 ? 186.843 160.214 135.962 1.00 84.09  ? 4086 THR A OG1   1 
ATOM   19331 C  CG2   . THR A 1 4086 ? 188.929 159.136 135.431 1.00 76.62  ? 4086 THR A CG2   1 
ATOM   19332 N  N     . ALA A 1 4087 ? 187.673 156.154 137.537 1.00 71.08  ? 4087 ALA A N     1 
ATOM   19333 C  CA    . ALA A 1 4087 ? 188.535 155.071 137.992 1.00 67.22  ? 4087 ALA A CA    1 
ATOM   19334 C  C     . ALA A 1 4087 ? 188.036 153.700 137.559 1.00 69.90  ? 4087 ALA A C     1 
ATOM   19335 O  O     . ALA A 1 4087 ? 188.847 152.782 137.397 1.00 73.92  ? 4087 ALA A O     1 
ATOM   19336 C  CB    . ALA A 1 4087 ? 188.674 155.116 139.512 1.00 64.77  ? 4087 ALA A CB    1 
ATOM   19337 N  N     . VAL A 1 4088 ? 186.724 153.527 137.376 1.00 71.62  ? 4088 VAL A N     1 
ATOM   19338 C  CA    . VAL A 1 4088 ? 186.229 152.238 136.904 1.00 67.78  ? 4088 VAL A CA    1 
ATOM   19339 C  C     . VAL A 1 4088 ? 186.705 151.948 135.489 1.00 79.49  ? 4088 VAL A C     1 
ATOM   19340 O  O     . VAL A 1 4088 ? 186.714 150.787 135.065 1.00 80.65  ? 4088 VAL A O     1 
ATOM   19341 C  CB    . VAL A 1 4088 ? 184.692 152.165 136.988 1.00 67.91  ? 4088 VAL A CB    1 
ATOM   19342 C  CG1   . VAL A 1 4088 ? 184.240 152.231 138.435 1.00 74.39  ? 4088 VAL A CG1   1 
ATOM   19343 C  CG2   . VAL A 1 4088 ? 184.057 153.271 136.167 1.00 74.09  ? 4088 VAL A CG2   1 
ATOM   19344 N  N     . LYS A 1 4089 ? 187.102 152.977 134.743 1.00 94.23  ? 4089 LYS A N     1 
ATOM   19345 C  CA    . LYS A 1 4089 ? 187.663 152.812 133.409 1.00 90.22  ? 4089 LYS A CA    1 
ATOM   19346 C  C     . LYS A 1 4089 ? 189.184 152.868 133.396 1.00 89.40  ? 4089 LYS A C     1 
ATOM   19347 O  O     . LYS A 1 4089 ? 189.819 152.109 132.659 1.00 95.51  ? 4089 LYS A O     1 
ATOM   19348 C  CB    . LYS A 1 4089 ? 187.111 153.885 132.465 1.00 85.86  ? 4089 LYS A CB    1 
ATOM   19349 C  CG    . LYS A 1 4089 ? 185.595 153.980 132.448 1.00 90.44  ? 4089 LYS A CG    1 
ATOM   19350 C  CD    . LYS A 1 4089 ? 185.102 154.651 131.176 1.00 91.46  ? 4089 LYS A CD    1 
ATOM   19351 C  CE    . LYS A 1 4089 ? 184.838 156.131 131.397 1.00 92.07  ? 4089 LYS A CE    1 
ATOM   19352 N  NZ    . LYS A 1 4089 ? 183.577 156.366 132.153 1.00 94.05  ? 4089 LYS A NZ    1 
ATOM   19353 N  N     . SER A 1 4090 ? 189.784 153.751 134.196 1.00 81.47  ? 4090 SER A N     1 
ATOM   19354 C  CA    . SER A 1 4090 ? 191.234 153.897 134.204 1.00 83.00  ? 4090 SER A CA    1 
ATOM   19355 C  C     . SER A 1 4090 ? 191.929 152.926 135.149 1.00 88.14  ? 4090 SER A C     1 
ATOM   19356 O  O     . SER A 1 4090 ? 193.150 152.763 135.057 1.00 91.67  ? 4090 SER A O     1 
ATOM   19357 C  CB    . SER A 1 4090 ? 191.616 155.330 134.579 1.00 85.39  ? 4090 SER A CB    1 
ATOM   19358 O  OG    . SER A 1 4090 ? 192.988 155.415 134.921 1.00 90.12  ? 4090 SER A OG    1 
ATOM   19359 N  N     . GLY A 1 4091 ? 191.190 152.284 136.051 1.00 87.57  ? 4091 GLY A N     1 
ATOM   19360 C  CA    . GLY A 1 4091 ? 191.792 151.332 136.962 1.00 83.42  ? 4091 GLY A CA    1 
ATOM   19361 C  C     . GLY A 1 4091 ? 192.491 151.932 138.159 1.00 85.59  ? 4091 GLY A C     1 
ATOM   19362 O  O     . GLY A 1 4091 ? 193.217 151.218 138.857 1.00 91.08  ? 4091 GLY A O     1 
ATOM   19363 N  N     . ARG A 1 4092 ? 192.298 153.219 138.421 1.00 83.61  ? 4092 ARG A N     1 
ATOM   19364 C  CA    . ARG A 1 4092 ? 192.916 153.873 139.564 1.00 81.60  ? 4092 ARG A CA    1 
ATOM   19365 C  C     . ARG A 1 4092 ? 192.107 153.613 140.833 1.00 85.57  ? 4092 ARG A C     1 
ATOM   19366 O  O     . ARG A 1 4092 ? 190.957 153.174 140.792 1.00 91.51  ? 4092 ARG A O     1 
ATOM   19367 C  CB    . ARG A 1 4092 ? 193.049 155.374 139.311 1.00 78.46  ? 4092 ARG A CB    1 
ATOM   19368 C  CG    . ARG A 1 4092 ? 194.067 155.732 138.242 1.00 83.99  ? 4092 ARG A CG    1 
ATOM   19369 C  CD    . ARG A 1 4092 ? 193.789 157.102 137.646 1.00 88.60  ? 4092 ARG A CD    1 
ATOM   19370 N  NE    . ARG A 1 4092 ? 194.435 158.168 138.401 1.00 93.43  ? 4092 ARG A NE    1 
ATOM   19371 C  CZ    . ARG A 1 4092 ? 193.838 158.886 139.343 1.00 92.03  ? 4092 ARG A CZ    1 
ATOM   19372 N  NH1   . ARG A 1 4092 ? 192.572 158.682 139.669 1.00 87.86  ? 4092 ARG A NH1   1 
ATOM   19373 N  NH2   . ARG A 1 4092 ? 194.528 159.833 139.972 1.00 87.39  ? 4092 ARG A NH2   1 
ATOM   19374 N  N     . TRP A 1 4093 ? 192.730 153.889 141.975 1.00 71.33  ? 4093 TRP A N     1 
ATOM   19375 C  CA    . TRP A 1 4093 ? 192.087 153.705 143.268 1.00 68.70  ? 4093 TRP A CA    1 
ATOM   19376 C  C     . TRP A 1 4093 ? 191.340 154.968 143.674 1.00 71.02  ? 4093 TRP A C     1 
ATOM   19377 O  O     . TRP A 1 4093 ? 191.750 156.082 143.337 1.00 77.79  ? 4093 TRP A O     1 
ATOM   19378 C  CB    . TRP A 1 4093 ? 193.117 153.350 144.340 1.00 70.55  ? 4093 TRP A CB    1 
ATOM   19379 C  CG    . TRP A 1 4093 ? 193.655 151.961 144.228 1.00 67.03  ? 4093 TRP A CG    1 
ATOM   19380 C  CD1   . TRP A 1 4093 ? 193.460 151.086 143.203 1.00 68.79  ? 4093 TRP A CD1   1 
ATOM   19381 C  CD2   . TRP A 1 4093 ? 194.479 151.284 145.183 1.00 63.70  ? 4093 TRP A CD2   1 
ATOM   19382 N  NE1   . TRP A 1 4093 ? 194.112 149.905 143.457 1.00 72.44  ? 4093 TRP A NE1   1 
ATOM   19383 C  CE2   . TRP A 1 4093 ? 194.746 150.002 144.668 1.00 68.74  ? 4093 TRP A CE2   1 
ATOM   19384 C  CE3   . TRP A 1 4093 ? 195.017 151.638 146.423 1.00 66.64  ? 4093 TRP A CE3   1 
ATOM   19385 C  CZ2   . TRP A 1 4093 ? 195.526 149.073 145.349 1.00 71.27  ? 4093 TRP A CZ2   1 
ATOM   19386 C  CZ3   . TRP A 1 4093 ? 195.791 150.716 147.097 1.00 71.67  ? 4093 TRP A CZ3   1 
ATOM   19387 C  CH2   . TRP A 1 4093 ? 196.039 149.448 146.560 1.00 71.98  ? 4093 TRP A CH2   1 
ATOM   19388 N  N     . VAL A 1 4094 ? 190.238 154.786 144.398 1.00 57.74  ? 4094 VAL A N     1 
ATOM   19389 C  CA    . VAL A 1 4094 ? 189.443 155.889 144.924 1.00 52.46  ? 4094 VAL A CA    1 
ATOM   19390 C  C     . VAL A 1 4094 ? 189.109 155.586 146.376 1.00 58.04  ? 4094 VAL A C     1 
ATOM   19391 O  O     . VAL A 1 4094 ? 188.619 154.496 146.690 1.00 71.66  ? 4094 VAL A O     1 
ATOM   19392 C  CB    . VAL A 1 4094 ? 188.155 156.111 144.108 1.00 55.12  ? 4094 VAL A CB    1 
ATOM   19393 C  CG1   . VAL A 1 4094 ? 187.214 157.045 144.846 1.00 58.95  ? 4094 VAL A CG1   1 
ATOM   19394 C  CG2   . VAL A 1 4094 ? 188.489 156.673 142.743 1.00 59.49  ? 4094 VAL A CG2   1 
ATOM   19395 N  N     . MET A 1 4095 ? 189.372 156.546 147.258 1.00 54.51  ? 4095 MET A N     1 
ATOM   19396 C  CA    . MET A 1 4095 ? 189.055 156.424 148.673 1.00 60.28  ? 4095 MET A CA    1 
ATOM   19397 C  C     . MET A 1 4095 ? 188.126 157.556 149.081 1.00 59.48  ? 4095 MET A C     1 
ATOM   19398 O  O     . MET A 1 4095 ? 188.361 158.715 148.727 1.00 67.30  ? 4095 MET A O     1 
ATOM   19399 C  CB    . MET A 1 4095 ? 190.320 156.451 149.534 1.00 62.92  ? 4095 MET A CB    1 
ATOM   19400 C  CG    . MET A 1 4095 ? 190.043 156.298 151.020 1.00 64.91  ? 4095 MET A CG    1 
ATOM   19401 S  SD    . MET A 1 4095 ? 191.534 156.338 152.024 1.00 75.61  ? 4095 MET A SD    1 
ATOM   19402 C  CE    . MET A 1 4095 ? 191.684 158.093 152.328 1.00 63.41  ? 4095 MET A CE    1 
ATOM   19403 N  N     . LEU A 1 4096 ? 187.070 157.217 149.815 1.00 47.03  ? 4096 LEU A N     1 
ATOM   19404 C  CA    . LEU A 1 4096 ? 186.130 158.194 150.349 1.00 45.85  ? 4096 LEU A CA    1 
ATOM   19405 C  C     . LEU A 1 4096 ? 186.153 158.102 151.867 1.00 50.35  ? 4096 LEU A C     1 
ATOM   19406 O  O     . LEU A 1 4096 ? 185.976 157.016 152.428 1.00 59.21  ? 4096 LEU A O     1 
ATOM   19407 C  CB    . LEU A 1 4096 ? 184.721 157.953 149.805 1.00 49.33  ? 4096 LEU A CB    1 
ATOM   19408 C  CG    . LEU A 1 4096 ? 184.649 157.690 148.300 1.00 46.32  ? 4096 LEU A CG    1 
ATOM   19409 C  CD1   . LEU A 1 4096 ? 183.237 157.335 147.879 1.00 39.95  ? 4096 LEU A CD1   1 
ATOM   19410 C  CD2   . LEU A 1 4096 ? 185.152 158.894 147.522 1.00 50.11  ? 4096 LEU A CD2   1 
ATOM   19411 N  N     . LYS A 1 4097 ? 186.368 159.236 152.526 1.00 59.85  ? 4097 LYS A N     1 
ATOM   19412 C  CA    . LYS A 1 4097 ? 186.511 159.277 153.972 1.00 58.16  ? 4097 LYS A CA    1 
ATOM   19413 C  C     . LYS A 1 4097 ? 185.209 159.704 154.635 1.00 63.01  ? 4097 LYS A C     1 
ATOM   19414 O  O     . LYS A 1 4097 ? 184.492 160.575 154.136 1.00 63.11  ? 4097 LYS A O     1 
ATOM   19415 C  CB    . LYS A 1 4097 ? 187.631 160.232 154.387 1.00 55.80  ? 4097 LYS A CB    1 
ATOM   19416 C  CG    . LYS A 1 4097 ? 188.884 160.148 153.539 1.00 57.95  ? 4097 LYS A CG    1 
ATOM   19417 C  CD    . LYS A 1 4097 ? 189.805 161.323 153.822 1.00 60.63  ? 4097 LYS A CD    1 
ATOM   19418 C  CE    . LYS A 1 4097 ? 190.746 161.589 152.662 1.00 73.15  ? 4097 LYS A CE    1 
ATOM   19419 N  NZ    . LYS A 1 4097 ? 191.583 162.798 152.895 1.00 69.28  ? 4097 LYS A NZ    1 
ATOM   19420 N  N     . ASN A 1 4098 ? 184.917 159.078 155.776 1.00 67.89  ? 4098 ASN A N     1 
ATOM   19421 C  CA    . ASN A 1 4098 ? 183.752 159.415 156.595 1.00 62.51  ? 4098 ASN A CA    1 
ATOM   19422 C  C     . ASN A 1 4098 ? 182.457 159.310 155.795 1.00 67.73  ? 4098 ASN A C     1 
ATOM   19423 O  O     . ASN A 1 4098 ? 181.696 160.271 155.681 1.00 77.33  ? 4098 ASN A O     1 
ATOM   19424 C  CB    . ASN A 1 4098 ? 183.900 160.806 157.214 1.00 56.84  ? 4098 ASN A CB    1 
ATOM   19425 C  CG    . ASN A 1 4098 ? 185.227 160.989 157.920 1.00 62.92  ? 4098 ASN A CG    1 
ATOM   19426 O  OD1   . ASN A 1 4098 ? 185.593 160.203 158.793 1.00 66.07  ? 4098 ASN A OD1   1 
ATOM   19427 N  ND2   . ASN A 1 4098 ? 185.958 162.031 157.544 1.00 67.00  ? 4098 ASN A ND2   1 
ATOM   19428 N  N     . VAL A 1 4099 ? 182.206 158.126 155.232 1.00 57.07  ? 4099 VAL A N     1 
ATOM   19429 C  CA    . VAL A 1 4099 ? 180.982 157.898 154.473 1.00 57.89  ? 4099 VAL A CA    1 
ATOM   19430 C  C     . VAL A 1 4099 ? 179.781 157.622 155.361 1.00 63.25  ? 4099 VAL A C     1 
ATOM   19431 O  O     . VAL A 1 4099 ? 178.658 157.537 154.854 1.00 75.62  ? 4099 VAL A O     1 
ATOM   19432 C  CB    . VAL A 1 4099 ? 181.168 156.733 153.482 1.00 61.35  ? 4099 VAL A CB    1 
ATOM   19433 C  CG1   . VAL A 1 4099 ? 182.468 156.894 152.718 1.00 70.04  ? 4099 VAL A CG1   1 
ATOM   19434 C  CG2   . VAL A 1 4099 ? 181.146 155.409 154.219 1.00 63.79  ? 4099 VAL A CG2   1 
ATOM   19435 N  N     . HIS A 1 4100 ? 179.983 157.479 156.672 1.00 62.11  ? 4100 HIS A N     1 
ATOM   19436 C  CA    . HIS A 1 4100 ? 178.866 157.251 157.579 1.00 63.75  ? 4100 HIS A CA    1 
ATOM   19437 C  C     . HIS A 1 4100 ? 178.013 158.494 157.787 1.00 66.70  ? 4100 HIS A C     1 
ATOM   19438 O  O     . HIS A 1 4100 ? 176.944 158.394 158.397 1.00 74.56  ? 4100 HIS A O     1 
ATOM   19439 C  CB    . HIS A 1 4100 ? 179.377 156.736 158.926 1.00 67.01  ? 4100 HIS A CB    1 
ATOM   19440 C  CG    . HIS A 1 4100 ? 180.218 157.722 159.673 1.00 67.87  ? 4100 HIS A CG    1 
ATOM   19441 N  ND1   . HIS A 1 4100 ? 181.544 157.946 159.372 1.00 71.90  ? 4100 HIS A ND1   1 
ATOM   19442 C  CD2   . HIS A 1 4100 ? 179.925 158.538 160.711 1.00 71.34  ? 4100 HIS A CD2   1 
ATOM   19443 C  CE1   . HIS A 1 4100 ? 182.031 158.861 160.191 1.00 68.74  ? 4100 HIS A CE1   1 
ATOM   19444 N  NE2   . HIS A 1 4100 ? 181.069 159.237 161.014 1.00 72.83  ? 4100 HIS A NE2   1 
ATOM   19445 N  N     . LEU A 1 4101 ? 178.455 159.654 157.303 1.00 64.25  ? 4101 LEU A N     1 
ATOM   19446 C  CA    . LEU A 1 4101 ? 177.678 160.880 157.420 1.00 65.62  ? 4101 LEU A CA    1 
ATOM   19447 C  C     . LEU A 1 4101 ? 176.612 161.014 156.342 1.00 72.01  ? 4101 LEU A C     1 
ATOM   19448 O  O     . LEU A 1 4101 ? 175.758 161.901 156.447 1.00 72.80  ? 4101 LEU A O     1 
ATOM   19449 C  CB    . LEU A 1 4101 ? 178.609 162.094 157.371 1.00 57.04  ? 4101 LEU A CB    1 
ATOM   19450 C  CG    . LEU A 1 4101 ? 179.715 162.138 158.426 1.00 57.76  ? 4101 LEU A CG    1 
ATOM   19451 C  CD1   . LEU A 1 4101 ? 180.846 163.046 157.979 1.00 62.62  ? 4101 LEU A CD1   1 
ATOM   19452 C  CD2   . LEU A 1 4101 ? 179.160 162.589 159.765 1.00 64.97  ? 4101 LEU A CD2   1 
ATOM   19453 N  N     . ALA A 1 4102 ? 176.640 160.168 155.313 1.00 68.62  ? 4102 ALA A N     1 
ATOM   19454 C  CA    . ALA A 1 4102 ? 175.677 160.212 154.213 1.00 64.12  ? 4102 ALA A CA    1 
ATOM   19455 C  C     . ALA A 1 4102 ? 175.154 158.806 153.954 1.00 72.60  ? 4102 ALA A C     1 
ATOM   19456 O  O     . ALA A 1 4102 ? 175.581 158.137 153.003 1.00 79.92  ? 4102 ALA A O     1 
ATOM   19457 C  CB    . ALA A 1 4102 ? 176.307 160.808 152.954 1.00 63.17  ? 4102 ALA A CB    1 
ATOM   19458 N  N     . PRO A 1 4103 ? 174.229 158.319 154.787 1.00 71.22  ? 4103 PRO A N     1 
ATOM   19459 C  CA    . PRO A 1 4103 ? 173.731 156.947 154.585 1.00 69.11  ? 4103 PRO A CA    1 
ATOM   19460 C  C     . PRO A 1 4103 ? 172.887 156.786 153.332 1.00 73.94  ? 4103 PRO A C     1 
ATOM   19461 O  O     . PRO A 1 4103 ? 172.969 155.744 152.669 1.00 80.96  ? 4103 PRO A O     1 
ATOM   19462 C  CB    . PRO A 1 4103 ? 172.921 156.679 155.861 1.00 66.07  ? 4103 PRO A CB    1 
ATOM   19463 C  CG    . PRO A 1 4103 ? 172.529 158.028 156.352 1.00 75.01  ? 4103 PRO A CG    1 
ATOM   19464 C  CD    . PRO A 1 4103 ? 173.635 158.964 155.970 1.00 74.35  ? 4103 PRO A CD    1 
ATOM   19465 N  N     . GLY A 1 4104 ? 172.064 157.779 152.990 1.00 74.79  ? 4104 GLY A N     1 
ATOM   19466 C  CA    . GLY A 1 4104 ? 171.280 157.681 151.769 1.00 78.43  ? 4104 GLY A CA    1 
ATOM   19467 C  C     . GLY A 1 4104 ? 172.147 157.665 150.525 1.00 78.04  ? 4104 GLY A C     1 
ATOM   19468 O  O     . GLY A 1 4104 ? 171.936 156.856 149.613 1.00 87.48  ? 4104 GLY A O     1 
ATOM   19469 N  N     . TRP A 1 4105 ? 173.139 158.556 150.470 1.00 67.05  ? 4105 TRP A N     1 
ATOM   19470 C  CA    . TRP A 1 4105 ? 174.093 158.506 149.373 1.00 69.29  ? 4105 TRP A CA    1 
ATOM   19471 C  C     . TRP A 1 4105 ? 174.889 157.211 149.400 1.00 77.37  ? 4105 TRP A C     1 
ATOM   19472 O  O     . TRP A 1 4105 ? 175.312 156.725 148.349 1.00 84.84  ? 4105 TRP A O     1 
ATOM   19473 C  CB    . TRP A 1 4105 ? 175.035 159.705 149.422 1.00 67.75  ? 4105 TRP A CB    1 
ATOM   19474 C  CG    . TRP A 1 4105 ? 176.003 159.712 148.288 1.00 61.43  ? 4105 TRP A CG    1 
ATOM   19475 C  CD1   . TRP A 1 4105 ? 175.771 160.150 147.018 1.00 71.10  ? 4105 TRP A CD1   1 
ATOM   19476 C  CD2   . TRP A 1 4105 ? 177.350 159.230 148.307 1.00 59.88  ? 4105 TRP A CD2   1 
ATOM   19477 N  NE1   . TRP A 1 4105 ? 176.895 159.986 146.248 1.00 77.95  ? 4105 TRP A NE1   1 
ATOM   19478 C  CE2   . TRP A 1 4105 ? 177.879 159.421 147.016 1.00 70.90  ? 4105 TRP A CE2   1 
ATOM   19479 C  CE3   . TRP A 1 4105 ? 178.163 158.663 149.291 1.00 67.25  ? 4105 TRP A CE3   1 
ATOM   19480 C  CZ2   . TRP A 1 4105 ? 179.183 159.066 146.684 1.00 73.78  ? 4105 TRP A CZ2   1 
ATOM   19481 C  CZ3   . TRP A 1 4105 ? 179.456 158.311 148.960 1.00 75.17  ? 4105 TRP A CZ3   1 
ATOM   19482 C  CH2   . TRP A 1 4105 ? 179.953 158.513 147.668 1.00 77.75  ? 4105 TRP A CH2   1 
ATOM   19483 N  N     . LEU A 1 4106 ? 175.096 156.635 150.586 1.00 73.66  ? 4106 LEU A N     1 
ATOM   19484 C  CA    . LEU A 1 4106 ? 175.745 155.331 150.673 1.00 70.95  ? 4106 LEU A CA    1 
ATOM   19485 C  C     . LEU A 1 4106 ? 174.906 154.252 149.999 1.00 75.70  ? 4106 LEU A C     1 
ATOM   19486 O  O     . LEU A 1 4106 ? 175.437 153.407 149.269 1.00 85.00  ? 4106 LEU A O     1 
ATOM   19487 C  CB    . LEU A 1 4106 ? 176.001 154.978 152.137 1.00 69.15  ? 4106 LEU A CB    1 
ATOM   19488 C  CG    . LEU A 1 4106 ? 177.397 155.263 152.685 1.00 72.07  ? 4106 LEU A CG    1 
ATOM   19489 C  CD1   . LEU A 1 4106 ? 177.633 154.466 153.953 1.00 75.75  ? 4106 LEU A CD1   1 
ATOM   19490 C  CD2   . LEU A 1 4106 ? 178.453 154.940 151.642 1.00 72.90  ? 4106 LEU A CD2   1 
ATOM   19491 N  N     . MET A 1 4107 ? 173.592 154.265 150.235 1.00 80.28  ? 4107 MET A N     1 
ATOM   19492 C  CA    . MET A 1 4107 ? 172.711 153.307 149.574 1.00 79.28  ? 4107 MET A CA    1 
ATOM   19493 C  C     . MET A 1 4107 ? 172.711 153.512 148.064 1.00 80.51  ? 4107 MET A C     1 
ATOM   19494 O  O     . MET A 1 4107 ? 172.750 152.542 147.293 1.00 88.70  ? 4107 MET A O     1 
ATOM   19495 C  CB    . MET A 1 4107 ? 171.294 153.432 150.133 1.00 79.28  ? 4107 MET A CB    1 
ATOM   19496 C  CG    . MET A 1 4107 ? 170.383 152.268 149.788 1.00 83.96  ? 4107 MET A CG    1 
ATOM   19497 S  SD    . MET A 1 4107 ? 169.026 152.052 150.959 1.00 99.73  ? 4107 MET A SD    1 
ATOM   19498 C  CE    . MET A 1 4107 ? 169.455 153.242 152.228 1.00 86.11  ? 4107 MET A CE    1 
ATOM   19499 N  N     . GLN A 1 4108 ? 172.666 154.772 147.623 1.00 78.80  ? 4108 GLN A N     1 
ATOM   19500 C  CA    . GLN A 1 4108 ? 172.721 155.049 146.190 1.00 79.74  ? 4108 GLN A CA    1 
ATOM   19501 C  C     . GLN A 1 4108 ? 174.035 154.566 145.587 1.00 80.97  ? 4108 GLN A C     1 
ATOM   19502 O  O     . GLN A 1 4108 ? 174.055 154.015 144.480 1.00 82.85  ? 4108 GLN A O     1 
ATOM   19503 C  CB    . GLN A 1 4108 ? 172.528 156.543 145.931 1.00 81.35  ? 4108 GLN A CB    1 
ATOM   19504 C  CG    . GLN A 1 4108 ? 171.224 157.102 146.472 1.00 86.86  ? 4108 GLN A CG    1 
ATOM   19505 C  CD    . GLN A 1 4108 ? 171.188 158.617 146.446 1.00 87.79  ? 4108 GLN A CD    1 
ATOM   19506 O  OE1   . GLN A 1 4108 ? 171.969 159.255 145.741 1.00 88.82  ? 4108 GLN A OE1   1 
ATOM   19507 N  NE2   . GLN A 1 4108 ? 170.280 159.200 147.218 1.00 83.62  ? 4108 GLN A NE2   1 
ATOM   19508 N  N     . LEU A 1 4109 ? 175.144 154.763 146.303 1.00 68.51  ? 4109 LEU A N     1 
ATOM   19509 C  CA    . LEU A 1 4109 ? 176.442 154.297 145.831 1.00 65.68  ? 4109 LEU A CA    1 
ATOM   19510 C  C     . LEU A 1 4109 ? 176.488 152.778 145.743 1.00 73.26  ? 4109 LEU A C     1 
ATOM   19511 O  O     . LEU A 1 4109 ? 177.064 152.226 144.801 1.00 76.26  ? 4109 LEU A O     1 
ATOM   19512 C  CB    . LEU A 1 4109 ? 177.546 154.816 146.751 1.00 63.16  ? 4109 LEU A CB    1 
ATOM   19513 C  CG    . LEU A 1 4109 ? 178.910 154.137 146.637 1.00 64.84  ? 4109 LEU A CG    1 
ATOM   19514 C  CD1   . LEU A 1 4109 ? 179.589 154.532 145.340 1.00 67.47  ? 4109 LEU A CD1   1 
ATOM   19515 C  CD2   . LEU A 1 4109 ? 179.781 154.487 147.831 1.00 67.56  ? 4109 LEU A CD2   1 
ATOM   19516 N  N     . GLU A 1 4110 ? 175.902 152.085 146.721 1.00 83.15  ? 4110 GLU A N     1 
ATOM   19517 C  CA    . GLU A 1 4110 ? 175.855 150.627 146.659 1.00 77.26  ? 4110 GLU A CA    1 
ATOM   19518 C  C     . GLU A 1 4110 ? 175.051 150.155 145.454 1.00 84.22  ? 4110 GLU A C     1 
ATOM   19519 O  O     . GLU A 1 4110 ? 175.464 149.228 144.743 1.00 86.40  ? 4110 GLU A O     1 
ATOM   19520 C  CB    . GLU A 1 4110 ? 175.269 150.063 147.952 1.00 74.29  ? 4110 GLU A CB    1 
ATOM   19521 C  CG    . GLU A 1 4110 ? 175.326 148.547 148.048 1.00 82.13  ? 4110 GLU A CG    1 
ATOM   19522 C  CD    . GLU A 1 4110 ? 174.069 147.881 147.524 1.00 90.58  ? 4110 GLU A CD    1 
ATOM   19523 O  OE1   . GLU A 1 4110 ? 172.963 148.295 147.929 1.00 89.75  ? 4110 GLU A OE1   1 
ATOM   19524 O  OE2   . GLU A 1 4110 ? 174.188 146.944 146.707 1.00 90.11  ? 4110 GLU A OE2   1 
ATOM   19525 N  N     . LYS A 1 4111 ? 173.899 150.786 145.207 1.00 85.96  ? 4111 LYS A N     1 
ATOM   19526 C  CA    . LYS A 1 4111 ? 173.099 150.425 144.039 1.00 82.42  ? 4111 LYS A CA    1 
ATOM   19527 C  C     . LYS A 1 4111 ? 173.862 150.687 142.746 1.00 85.79  ? 4111 LYS A C     1 
ATOM   19528 O  O     . LYS A 1 4111 ? 173.782 149.899 141.798 1.00 88.58  ? 4111 LYS A O     1 
ATOM   19529 C  CB    . LYS A 1 4111 ? 171.774 151.186 144.046 1.00 78.69  ? 4111 LYS A CB    1 
ATOM   19530 C  CG    . LYS A 1 4111 ? 170.698 150.548 144.907 1.00 81.40  ? 4111 LYS A CG    1 
ATOM   19531 C  CD    . LYS A 1 4111 ? 169.654 151.565 145.332 1.00 88.51  ? 4111 LYS A CD    1 
ATOM   19532 C  CE    . LYS A 1 4111 ? 168.503 150.900 146.067 1.00 86.62  ? 4111 LYS A CE    1 
ATOM   19533 N  NZ    . LYS A 1 4111 ? 168.981 150.002 147.154 1.00 83.74  ? 4111 LYS A NZ    1 
ATOM   19534 N  N     . LYS A 1 4112 ? 174.601 151.797 142.688 1.00 81.11  ? 4112 LYS A N     1 
ATOM   19535 C  CA    . LYS A 1 4112 ? 175.434 152.081 141.523 1.00 78.42  ? 4112 LYS A CA    1 
ATOM   19536 C  C     . LYS A 1 4112 ? 176.517 151.024 141.348 1.00 77.63  ? 4112 LYS A C     1 
ATOM   19537 O  O     . LYS A 1 4112 ? 176.796 150.587 140.225 1.00 76.15  ? 4112 LYS A O     1 
ATOM   19538 C  CB    . LYS A 1 4112 ? 176.058 153.469 141.660 1.00 78.01  ? 4112 LYS A CB    1 
ATOM   19539 C  CG    . LYS A 1 4112 ? 177.067 153.815 140.581 1.00 79.84  ? 4112 LYS A CG    1 
ATOM   19540 C  CD    . LYS A 1 4112 ? 177.657 155.195 140.816 1.00 77.92  ? 4112 LYS A CD    1 
ATOM   19541 C  CE    . LYS A 1 4112 ? 178.692 155.544 139.763 1.00 78.55  ? 4112 LYS A CE    1 
ATOM   19542 N  NZ    . LYS A 1 4112 ? 179.257 156.905 139.977 1.00 77.34  ? 4112 LYS A NZ    1 
ATOM   19543 N  N     . LEU A 1 4113 ? 177.141 150.607 142.450 1.00 76.26  ? 4113 LEU A N     1 
ATOM   19544 C  CA    . LEU A 1 4113 ? 178.241 149.652 142.380 1.00 75.91  ? 4113 LEU A CA    1 
ATOM   19545 C  C     . LEU A 1 4113 ? 177.765 148.277 141.931 1.00 77.62  ? 4113 LEU A C     1 
ATOM   19546 O  O     . LEU A 1 4113 ? 178.481 147.577 141.207 1.00 78.10  ? 4113 LEU A O     1 
ATOM   19547 C  CB    . LEU A 1 4113 ? 178.933 149.553 143.738 1.00 71.53  ? 4113 LEU A CB    1 
ATOM   19548 C  CG    . LEU A 1 4113 ? 180.253 150.302 143.908 1.00 70.63  ? 4113 LEU A CG    1 
ATOM   19549 C  CD1   . LEU A 1 4113 ? 180.835 150.013 145.278 1.00 76.41  ? 4113 LEU A CD1   1 
ATOM   19550 C  CD2   . LEU A 1 4113 ? 181.231 149.915 142.815 1.00 68.94  ? 4113 LEU A CD2   1 
ATOM   19551 N  N     . HIS A 1 4114 ? 176.568 147.866 142.362 1.00 82.13  ? 4114 HIS A N     1 
ATOM   19552 C  CA    . HIS A 1 4114 ? 176.111 146.512 142.055 1.00 83.69  ? 4114 HIS A CA    1 
ATOM   19553 C  C     . HIS A 1 4114 ? 176.017 146.280 140.551 1.00 83.09  ? 4114 HIS A C     1 
ATOM   19554 O  O     . HIS A 1 4114 ? 176.449 145.235 140.051 1.00 78.80  ? 4114 HIS A O     1 
ATOM   19555 C  CB    . HIS A 1 4114 ? 174.762 146.242 142.718 1.00 84.18  ? 4114 HIS A CB    1 
ATOM   19556 C  CG    . HIS A 1 4114 ? 174.159 144.928 142.334 1.00 86.43  ? 4114 HIS A CG    1 
ATOM   19557 N  ND1   . HIS A 1 4114 ? 174.654 143.723 142.784 1.00 86.69  ? 4114 HIS A ND1   1 
ATOM   19558 C  CD2   . HIS A 1 4114 ? 173.106 144.627 141.538 1.00 83.97  ? 4114 HIS A CD2   1 
ATOM   19559 C  CE1   . HIS A 1 4114 ? 173.931 142.737 142.283 1.00 84.63  ? 4114 HIS A CE1   1 
ATOM   19560 N  NE2   . HIS A 1 4114 ? 172.985 143.259 141.524 1.00 86.21  ? 4114 HIS A NE2   1 
ATOM   19561 N  N     . SER A 1 4115 ? 175.460 147.237 139.816 1.00 90.60  ? 4115 SER A N     1 
ATOM   19562 C  CA    . SER A 1 4115 ? 175.348 147.128 138.362 1.00 91.06  ? 4115 SER A CA    1 
ATOM   19563 C  C     . SER A 1 4115 ? 176.517 147.861 137.704 1.00 91.69  ? 4115 SER A C     1 
ATOM   19564 O  O     . SER A 1 4115 ? 176.370 148.908 137.072 1.00 91.03  ? 4115 SER A O     1 
ATOM   19565 C  CB    . SER A 1 4115 ? 174.003 147.674 137.891 1.00 89.18  ? 4115 SER A CB    1 
ATOM   19566 O  OG    . SER A 1 4115 ? 173.845 149.031 138.266 1.00 91.02  ? 4115 SER A OG    1 
ATOM   19567 N  N     . LEU A 1 4116 ? 177.702 147.277 137.865 1.00 88.93  ? 4116 LEU A N     1 
ATOM   19568 C  CA    . LEU A 1 4116 ? 178.921 147.895 137.367 1.00 86.71  ? 4116 LEU A CA    1 
ATOM   19569 C  C     . LEU A 1 4116 ? 179.960 146.815 137.104 1.00 87.64  ? 4116 LEU A C     1 
ATOM   19570 O  O     . LEU A 1 4116 ? 180.013 145.810 137.817 1.00 88.24  ? 4116 LEU A O     1 
ATOM   19571 C  CB    . LEU A 1 4116 ? 179.459 148.925 138.367 1.00 87.26  ? 4116 LEU A CB    1 
ATOM   19572 C  CG    . LEU A 1 4116 ? 180.527 149.901 137.879 1.00 84.99  ? 4116 LEU A CG    1 
ATOM   19573 C  CD1   . LEU A 1 4116 ? 179.979 150.777 136.767 1.00 85.79  ? 4116 LEU A CD1   1 
ATOM   19574 C  CD2   . LEU A 1 4116 ? 181.016 150.750 139.037 1.00 83.86  ? 4116 LEU A CD2   1 
ATOM   19575 N  N     . GLN A 1 4117 ? 180.779 147.032 136.076 1.00 99.71  ? 4117 GLN A N     1 
ATOM   19576 C  CA    . GLN A 1 4117 ? 181.850 146.112 135.692 1.00 99.84  ? 4117 GLN A CA    1 
ATOM   19577 C  C     . GLN A 1 4117 ? 183.139 146.914 135.581 1.00 101.09 ? 4117 GLN A C     1 
ATOM   19578 O  O     . GLN A 1 4117 ? 183.559 147.297 134.481 1.00 99.52  ? 4117 GLN A O     1 
ATOM   19579 C  CB    . GLN A 1 4117 ? 181.515 145.388 134.386 1.00 99.36  ? 4117 GLN A CB    1 
ATOM   19580 C  CG    . GLN A 1 4117 ? 180.815 146.255 133.351 1.00 101.05 ? 4117 GLN A CG    1 
ATOM   19581 C  CD    . GLN A 1 4117 ? 179.988 145.444 132.373 1.00 104.02 ? 4117 GLN A CD    1 
ATOM   19582 O  OE1   . GLN A 1 4117 ? 180.472 144.475 131.789 1.00 103.96 ? 4117 GLN A OE1   1 
ATOM   19583 N  NE2   . GLN A 1 4117 ? 178.733 145.837 132.191 1.00 100.81 ? 4117 GLN A NE2   1 
ATOM   19584 N  N     . PRO A 1 4118 ? 183.795 147.181 136.702 1.00 88.45  ? 4118 PRO A N     1 
ATOM   19585 C  CA    . PRO A 1 4118 ? 184.950 148.082 136.710 1.00 84.16  ? 4118 PRO A CA    1 
ATOM   19586 C  C     . PRO A 1 4118 ? 186.201 147.397 136.172 1.00 80.43  ? 4118 PRO A C     1 
ATOM   19587 O  O     . PRO A 1 4118 ? 186.201 146.221 135.815 1.00 84.07  ? 4118 PRO A O     1 
ATOM   19588 C  CB    . PRO A 1 4118 ? 185.098 148.433 138.189 1.00 85.57  ? 4118 PRO A CB    1 
ATOM   19589 C  CG    . PRO A 1 4118 ? 184.591 147.233 138.900 1.00 85.21  ? 4118 PRO A CG    1 
ATOM   19590 C  CD    . PRO A 1 4118 ? 183.498 146.649 138.043 1.00 86.15  ? 4118 PRO A CD    1 
ATOM   19591 N  N     . HIS A 1 4119 ? 187.282 148.171 136.120 1.00 85.04  ? 4119 HIS A N     1 
ATOM   19592 C  CA    . HIS A 1 4119 ? 188.568 147.670 135.665 1.00 83.06  ? 4119 HIS A CA    1 
ATOM   19593 C  C     . HIS A 1 4119 ? 189.128 146.661 136.665 1.00 81.50  ? 4119 HIS A C     1 
ATOM   19594 O  O     . HIS A 1 4119 ? 188.726 146.610 137.830 1.00 83.91  ? 4119 HIS A O     1 
ATOM   19595 C  CB    . HIS A 1 4119 ? 189.545 148.830 135.469 1.00 80.43  ? 4119 HIS A CB    1 
ATOM   19596 C  CG    . HIS A 1 4119 ? 190.814 148.448 134.775 1.00 82.34  ? 4119 HIS A CG    1 
ATOM   19597 N  ND1   . HIS A 1 4119 ? 191.971 148.137 135.456 1.00 84.62  ? 4119 HIS A ND1   1 
ATOM   19598 C  CD2   . HIS A 1 4119 ? 191.110 148.332 133.458 1.00 86.82  ? 4119 HIS A CD2   1 
ATOM   19599 C  CE1   . HIS A 1 4119 ? 192.924 147.844 134.589 1.00 87.48  ? 4119 HIS A CE1   1 
ATOM   19600 N  NE2   . HIS A 1 4119 ? 192.428 147.955 133.370 1.00 91.10  ? 4119 HIS A NE2   1 
ATOM   19601 N  N     . ALA A 1 4120 ? 190.070 145.843 136.188 1.00 73.14  ? 4120 ALA A N     1 
ATOM   19602 C  CA    . ALA A 1 4120 ? 190.617 144.776 137.020 1.00 76.77  ? 4120 ALA A CA    1 
ATOM   19603 C  C     . ALA A 1 4120 ? 191.361 145.319 138.232 1.00 77.07  ? 4120 ALA A C     1 
ATOM   19604 O  O     . ALA A 1 4120 ? 191.300 144.724 139.314 1.00 78.59  ? 4120 ALA A O     1 
ATOM   19605 C  CB    . ALA A 1 4120 ? 191.539 143.885 136.189 1.00 77.43  ? 4120 ALA A CB    1 
ATOM   19606 N  N     . CYS A 1 4121 ? 192.066 146.437 138.079 1.00 78.59  ? 4121 CYS A N     1 
ATOM   19607 C  CA    . CYS A 1 4121 ? 192.862 147.004 139.160 1.00 76.74  ? 4121 CYS A CA    1 
ATOM   19608 C  C     . CYS A 1 4121 ? 192.129 148.084 139.944 1.00 79.58  ? 4121 CYS A C     1 
ATOM   19609 O  O     . CYS A 1 4121 ? 192.724 148.679 140.849 1.00 80.36  ? 4121 CYS A O     1 
ATOM   19610 C  CB    . CYS A 1 4121 ? 194.171 147.574 138.607 1.00 81.14  ? 4121 CYS A CB    1 
ATOM   19611 S  SG    . CYS A 1 4121 ? 195.289 146.337 137.910 1.00 92.63  ? 4121 CYS A SG    1 
ATOM   19612 N  N     . PHE A 1 4122 ? 190.867 148.357 139.625 1.00 72.15  ? 4122 PHE A N     1 
ATOM   19613 C  CA    . PHE A 1 4122 ? 190.116 149.367 140.357 1.00 62.48  ? 4122 PHE A CA    1 
ATOM   19614 C  C     . PHE A 1 4122 ? 189.827 148.896 141.776 1.00 70.75  ? 4122 PHE A C     1 
ATOM   19615 O  O     . PHE A 1 4122 ? 189.453 147.743 142.002 1.00 80.26  ? 4122 PHE A O     1 
ATOM   19616 C  CB    . PHE A 1 4122 ? 188.809 149.686 139.635 1.00 62.21  ? 4122 PHE A CB    1 
ATOM   19617 C  CG    . PHE A 1 4122 ? 187.839 150.481 140.461 1.00 65.18  ? 4122 PHE A CG    1 
ATOM   19618 C  CD1   . PHE A 1 4122 ? 188.079 151.813 140.743 1.00 72.08  ? 4122 PHE A CD1   1 
ATOM   19619 C  CD2   . PHE A 1 4122 ? 186.684 149.897 140.952 1.00 69.76  ? 4122 PHE A CD2   1 
ATOM   19620 C  CE1   . PHE A 1 4122 ? 187.189 152.547 141.502 1.00 71.06  ? 4122 PHE A CE1   1 
ATOM   19621 C  CE2   . PHE A 1 4122 ? 185.790 150.627 141.710 1.00 68.71  ? 4122 PHE A CE2   1 
ATOM   19622 C  CZ    . PHE A 1 4122 ? 186.044 151.954 141.984 1.00 64.13  ? 4122 PHE A CZ    1 
ATOM   19623 N  N     . ARG A 1 4123 ? 190.005 149.799 142.736 1.00 65.51  ? 4123 ARG A N     1 
ATOM   19624 C  CA    . ARG A 1 4123 ? 189.713 149.521 144.134 1.00 66.23  ? 4123 ARG A CA    1 
ATOM   19625 C  C     . ARG A 1 4123 ? 189.038 150.737 144.746 1.00 64.07  ? 4123 ARG A C     1 
ATOM   19626 O  O     . ARG A 1 4123 ? 189.437 151.874 144.482 1.00 67.03  ? 4123 ARG A O     1 
ATOM   19627 C  CB    . ARG A 1 4123 ? 190.984 149.176 144.919 1.00 68.07  ? 4123 ARG A CB    1 
ATOM   19628 C  CG    . ARG A 1 4123 ? 191.627 147.858 144.523 1.00 63.40  ? 4123 ARG A CG    1 
ATOM   19629 C  CD    . ARG A 1 4123 ? 190.731 146.679 144.853 1.00 57.38  ? 4123 ARG A CD    1 
ATOM   19630 N  NE    . ARG A 1 4123 ? 191.379 145.409 144.550 1.00 65.53  ? 4123 ARG A NE    1 
ATOM   19631 C  CZ    . ARG A 1 4123 ? 191.455 144.876 143.338 1.00 65.15  ? 4123 ARG A CZ    1 
ATOM   19632 N  NH1   . ARG A 1 4123 ? 190.926 145.476 142.285 1.00 68.11  ? 4123 ARG A NH1   1 
ATOM   19633 N  NH2   . ARG A 1 4123 ? 192.077 143.712 143.179 1.00 67.90  ? 4123 ARG A NH2   1 
ATOM   19634 N  N     . LEU A 1 4124 ? 188.018 150.495 145.565 1.00 47.39  ? 4124 LEU A N     1 
ATOM   19635 C  CA    . LEU A 1 4124 ? 187.257 151.559 146.210 1.00 41.98  ? 4124 LEU A CA    1 
ATOM   19636 C  C     . LEU A 1 4124 ? 187.290 151.336 147.715 1.00 57.04  ? 4124 LEU A C     1 
ATOM   19637 O  O     . LEU A 1 4124 ? 186.783 150.322 148.208 1.00 71.91  ? 4124 LEU A O     1 
ATOM   19638 C  CB    . LEU A 1 4124 ? 185.821 151.599 145.694 1.00 46.17  ? 4124 LEU A CB    1 
ATOM   19639 C  CG    . LEU A 1 4124 ? 184.909 152.629 146.362 1.00 51.78  ? 4124 LEU A CG    1 
ATOM   19640 C  CD1   . LEU A 1 4124 ? 185.331 154.036 145.981 1.00 54.27  ? 4124 LEU A CD1   1 
ATOM   19641 C  CD2   . LEU A 1 4124 ? 183.463 152.385 145.982 1.00 57.32  ? 4124 LEU A CD2   1 
ATOM   19642 N  N     . PHE A 1 4125 ? 187.884 152.278 148.440 1.00 51.32  ? 4125 PHE A N     1 
ATOM   19643 C  CA    . PHE A 1 4125 ? 187.976 152.214 149.892 1.00 46.36  ? 4125 PHE A CA    1 
ATOM   19644 C  C     . PHE A 1 4125 ? 187.022 153.230 150.503 1.00 52.43  ? 4125 PHE A C     1 
ATOM   19645 O  O     . PHE A 1 4125 ? 187.036 154.406 150.126 1.00 64.15  ? 4125 PHE A O     1 
ATOM   19646 C  CB    . PHE A 1 4125 ? 189.406 152.484 150.365 1.00 48.89  ? 4125 PHE A CB    1 
ATOM   19647 C  CG    . PHE A 1 4125 ? 190.435 151.588 149.737 1.00 48.72  ? 4125 PHE A CG    1 
ATOM   19648 C  CD1   . PHE A 1 4125 ? 191.006 151.910 148.520 1.00 51.38  ? 4125 PHE A CD1   1 
ATOM   19649 C  CD2   . PHE A 1 4125 ? 190.834 150.425 150.370 1.00 52.46  ? 4125 PHE A CD2   1 
ATOM   19650 C  CE1   . PHE A 1 4125 ? 191.952 151.089 147.945 1.00 52.06  ? 4125 PHE A CE1   1 
ATOM   19651 C  CE2   . PHE A 1 4125 ? 191.780 149.600 149.798 1.00 56.11  ? 4125 PHE A CE2   1 
ATOM   19652 C  CZ    . PHE A 1 4125 ? 192.340 149.933 148.584 1.00 60.39  ? 4125 PHE A CZ    1 
ATOM   19653 N  N     . LEU A 1 4126 ? 186.197 152.777 151.441 1.00 48.41  ? 4126 LEU A N     1 
ATOM   19654 C  CA    . LEU A 1 4126 ? 185.237 153.635 152.132 1.00 48.58  ? 4126 LEU A CA    1 
ATOM   19655 C  C     . LEU A 1 4126 ? 185.577 153.612 153.617 1.00 57.66  ? 4126 LEU A C     1 
ATOM   19656 O  O     . LEU A 1 4126 ? 185.103 152.742 154.354 1.00 66.44  ? 4126 LEU A O     1 
ATOM   19657 C  CB    . LEU A 1 4126 ? 183.806 153.169 151.882 1.00 43.55  ? 4126 LEU A CB    1 
ATOM   19658 C  CG    . LEU A 1 4126 ? 183.402 152.936 150.427 1.00 48.68  ? 4126 LEU A CG    1 
ATOM   19659 C  CD1   . LEU A 1 4126 ? 181.937 152.549 150.334 1.00 55.09  ? 4126 LEU A CD1   1 
ATOM   19660 C  CD2   . LEU A 1 4126 ? 183.682 154.170 149.594 1.00 53.11  ? 4126 LEU A CD2   1 
ATOM   19661 N  N     . THR A 1 4127 ? 186.387 154.567 154.060 1.00 57.55  ? 4127 THR A N     1 
ATOM   19662 C  CA    . THR A 1 4127 ? 186.793 154.658 155.455 1.00 57.41  ? 4127 THR A CA    1 
ATOM   19663 C  C     . THR A 1 4127 ? 185.683 155.328 156.251 1.00 55.60  ? 4127 THR A C     1 
ATOM   19664 O  O     . THR A 1 4127 ? 185.222 156.415 155.889 1.00 60.34  ? 4127 THR A O     1 
ATOM   19665 C  CB    . THR A 1 4127 ? 188.096 155.442 155.605 1.00 59.84  ? 4127 THR A CB    1 
ATOM   19666 O  OG1   . THR A 1 4127 ? 187.812 156.845 155.619 1.00 57.01  ? 4127 THR A OG1   1 
ATOM   19667 C  CG2   . THR A 1 4127 ? 189.035 155.134 154.450 1.00 57.17  ? 4127 THR A CG2   1 
ATOM   19668 N  N     . MET A 1 4128 ? 185.260 154.678 157.331 1.00 63.15  ? 4128 MET A N     1 
ATOM   19669 C  CA    . MET A 1 4128 ? 184.139 155.159 158.121 1.00 60.15  ? 4128 MET A CA    1 
ATOM   19670 C  C     . MET A 1 4128 ? 184.309 154.695 159.559 1.00 60.28  ? 4128 MET A C     1 
ATOM   19671 O  O     . MET A 1 4128 ? 185.083 153.782 159.854 1.00 74.21  ? 4128 MET A O     1 
ATOM   19672 C  CB    . MET A 1 4128 ? 182.807 154.669 157.545 1.00 64.37  ? 4128 MET A CB    1 
ATOM   19673 C  CG    . MET A 1 4128 ? 182.286 153.393 158.186 1.00 62.28  ? 4128 MET A CG    1 
ATOM   19674 S  SD    . MET A 1 4128 ? 181.089 152.534 157.152 1.00 83.32  ? 4128 MET A SD    1 
ATOM   19675 C  CE    . MET A 1 4128 ? 182.108 152.123 155.740 1.00 68.25  ? 4128 MET A CE    1 
ATOM   19676 N  N     . GLU A 1 4129 ? 183.582 155.347 160.457 1.00 72.84  ? 4129 GLU A N     1 
ATOM   19677 C  CA    . GLU A 1 4129 ? 183.518 154.929 161.847 1.00 79.29  ? 4129 GLU A CA    1 
ATOM   19678 C  C     . GLU A 1 4129 ? 182.363 153.949 162.036 1.00 81.90  ? 4129 GLU A C     1 
ATOM   19679 O  O     . GLU A 1 4129 ? 181.346 154.014 161.342 1.00 88.45  ? 4129 GLU A O     1 
ATOM   19680 C  CB    . GLU A 1 4129 ? 183.362 156.146 162.764 1.00 83.51  ? 4129 GLU A CB    1 
ATOM   19681 C  CG    . GLU A 1 4129 ? 182.493 155.929 163.994 1.00 84.33  ? 4129 GLU A CG    1 
ATOM   19682 C  CD    . GLU A 1 4129 ? 182.267 157.202 164.783 1.00 90.93  ? 4129 GLU A CD    1 
ATOM   19683 O  OE1   . GLU A 1 4129 ? 183.179 158.055 164.810 1.00 94.74  ? 4129 GLU A OE1   1 
ATOM   19684 O  OE2   . GLU A 1 4129 ? 181.180 157.347 165.380 1.00 88.58  ? 4129 GLU A OE2   1 
ATOM   19685 N  N     . ILE A 1 4130 ? 182.541 153.022 162.975 1.00 74.38  ? 4130 ILE A N     1 
ATOM   19686 C  CA    . ILE A 1 4130 ? 181.512 152.026 163.262 1.00 72.15  ? 4130 ILE A CA    1 
ATOM   19687 C  C     . ILE A 1 4130 ? 180.262 152.770 163.723 1.00 74.77  ? 4130 ILE A C     1 
ATOM   19688 O  O     . ILE A 1 4130 ? 180.258 153.404 164.782 1.00 75.50  ? 4130 ILE A O     1 
ATOM   19689 C  CB    . ILE A 1 4130 ? 181.984 151.016 164.313 1.00 71.61  ? 4130 ILE A CB    1 
ATOM   19690 C  CG1   . ILE A 1 4130 ? 182.911 149.982 163.675 1.00 68.17  ? 4130 ILE A CG1   1 
ATOM   19691 C  CG2   . ILE A 1 4130 ? 180.798 150.314 164.952 1.00 78.50  ? 4130 ILE A CG2   1 
ATOM   19692 C  CD1   . ILE A 1 4130 ? 183.532 149.026 164.665 1.00 70.56  ? 4130 ILE A CD1   1 
ATOM   19693 N  N     . ASN A 1 4131 ? 179.201 152.708 162.916 1.00 80.54  ? 4131 ASN A N     1 
ATOM   19694 C  CA    . ASN A 1 4131 ? 178.008 153.507 163.132 1.00 81.14  ? 4131 ASN A CA    1 
ATOM   19695 C  C     . ASN A 1 4131 ? 176.792 152.698 162.696 1.00 81.04  ? 4131 ASN A C     1 
ATOM   19696 O  O     . ASN A 1 4131 ? 176.794 152.131 161.588 1.00 86.93  ? 4131 ASN A O     1 
ATOM   19697 C  CB    . ASN A 1 4131 ? 178.089 154.820 162.349 1.00 81.94  ? 4131 ASN A CB    1 
ATOM   19698 C  CG    . ASN A 1 4131 ? 177.389 155.966 163.050 1.00 88.38  ? 4131 ASN A CG    1 
ATOM   19699 O  OD1   . ASN A 1 4131 ? 176.905 155.822 164.170 1.00 90.57  ? 4131 ASN A OD1   1 
ATOM   19700 N  ND2   . ASN A 1 4131 ? 177.334 157.116 162.389 1.00 85.48  ? 4131 ASN A ND2   1 
ATOM   19701 N  N     . PRO A 1 4132 ? 175.751 152.613 163.527 1.00 71.90  ? 4132 PRO A N     1 
ATOM   19702 C  CA    . PRO A 1 4132 ? 174.540 151.883 163.114 1.00 70.09  ? 4132 PRO A CA    1 
ATOM   19703 C  C     . PRO A 1 4132 ? 173.837 152.490 161.914 1.00 74.77  ? 4132 PRO A C     1 
ATOM   19704 O  O     . PRO A 1 4132 ? 173.044 151.796 161.267 1.00 81.23  ? 4132 PRO A O     1 
ATOM   19705 C  CB    . PRO A 1 4132 ? 173.652 151.934 164.366 1.00 68.91  ? 4132 PRO A CB    1 
ATOM   19706 C  CG    . PRO A 1 4132 ? 174.218 153.037 165.207 1.00 71.58  ? 4132 PRO A CG    1 
ATOM   19707 C  CD    . PRO A 1 4132 ? 175.684 153.041 164.932 1.00 72.64  ? 4132 PRO A CD    1 
ATOM   19708 N  N     . LYS A 1 4133 ? 174.097 153.759 161.593 1.00 79.86  ? 4133 LYS A N     1 
ATOM   19709 C  CA    . LYS A 1 4133 ? 173.411 154.405 160.480 1.00 82.19  ? 4133 LYS A CA    1 
ATOM   19710 C  C     . LYS A 1 4133 ? 173.873 153.888 159.124 1.00 84.45  ? 4133 LYS A C     1 
ATOM   19711 O  O     . LYS A 1 4133 ? 173.215 154.165 158.116 1.00 88.34  ? 4133 LYS A O     1 
ATOM   19712 C  CB    . LYS A 1 4133 ? 173.609 155.919 160.548 1.00 82.99  ? 4133 LYS A CB    1 
ATOM   19713 C  CG    . LYS A 1 4133 ? 172.946 156.582 161.746 1.00 82.34  ? 4133 LYS A CG    1 
ATOM   19714 C  CD    . LYS A 1 4133 ? 173.525 157.965 162.031 1.00 85.86  ? 4133 LYS A CD    1 
ATOM   19715 C  CE    . LYS A 1 4133 ? 174.181 158.578 160.800 1.00 85.76  ? 4133 LYS A CE    1 
ATOM   19716 N  NZ    . LYS A 1 4133 ? 175.007 159.768 161.142 1.00 82.48  ? 4133 LYS A NZ    1 
ATOM   19717 N  N     . VAL A 1 4134 ? 174.984 153.159 159.073 1.00 72.90  ? 4134 VAL A N     1 
ATOM   19718 C  CA    . VAL A 1 4134 ? 175.481 152.646 157.791 1.00 68.64  ? 4134 VAL A CA    1 
ATOM   19719 C  C     . VAL A 1 4134 ? 174.493 151.622 157.242 1.00 66.97  ? 4134 VAL A C     1 
ATOM   19720 O  O     . VAL A 1 4134 ? 174.049 150.729 157.990 1.00 69.53  ? 4134 VAL A O     1 
ATOM   19721 C  CB    . VAL A 1 4134 ? 176.878 152.027 157.966 1.00 67.48  ? 4134 VAL A CB    1 
ATOM   19722 C  CG1   . VAL A 1 4134 ? 177.414 151.527 156.636 1.00 65.59  ? 4134 VAL A CG1   1 
ATOM   19723 C  CG2   . VAL A 1 4134 ? 177.827 153.040 158.582 1.00 69.39  ? 4134 VAL A CG2   1 
ATOM   19724 N  N     . PRO A 1 4135 ? 174.107 151.704 155.969 1.00 66.03  ? 4135 PRO A N     1 
ATOM   19725 C  CA    . PRO A 1 4135 ? 173.117 150.761 155.435 1.00 66.95  ? 4135 PRO A CA    1 
ATOM   19726 C  C     . PRO A 1 4135 ? 173.621 149.326 155.461 1.00 78.32  ? 4135 PRO A C     1 
ATOM   19727 O  O     . PRO A 1 4135 ? 174.813 149.055 155.296 1.00 87.53  ? 4135 PRO A O     1 
ATOM   19728 C  CB    . PRO A 1 4135 ? 172.897 151.251 153.999 1.00 66.14  ? 4135 PRO A CB    1 
ATOM   19729 C  CG    . PRO A 1 4135 ? 173.367 152.663 153.993 1.00 72.73  ? 4135 PRO A CG    1 
ATOM   19730 C  CD    . PRO A 1 4135 ? 174.488 152.724 154.979 1.00 72.42  ? 4135 PRO A CD    1 
ATOM   19731 N  N     . VAL A 1 4136 ? 172.684 148.400 155.671 1.00 70.86  ? 4136 VAL A N     1 
ATOM   19732 C  CA    . VAL A 1 4136 ? 173.030 146.985 155.762 1.00 64.02  ? 4136 VAL A CA    1 
ATOM   19733 C  C     . VAL A 1 4136 ? 173.471 146.447 154.406 1.00 65.79  ? 4136 VAL A C     1 
ATOM   19734 O  O     . VAL A 1 4136 ? 174.398 145.631 154.319 1.00 68.81  ? 4136 VAL A O     1 
ATOM   19735 C  CB    . VAL A 1 4136 ? 171.841 146.192 156.337 1.00 66.26  ? 4136 VAL A CB    1 
ATOM   19736 C  CG1   . VAL A 1 4136 ? 171.916 144.727 155.937 1.00 73.83  ? 4136 VAL A CG1   1 
ATOM   19737 C  CG2   . VAL A 1 4136 ? 171.795 146.336 157.849 1.00 63.13  ? 4136 VAL A CG2   1 
ATOM   19738 N  N     . ASN A 1 4137 ? 172.818 146.891 153.328 1.00 75.61  ? 4137 ASN A N     1 
ATOM   19739 C  CA    . ASN A 1 4137 ? 173.126 146.355 152.005 1.00 76.72  ? 4137 ASN A CA    1 
ATOM   19740 C  C     . ASN A 1 4137 ? 174.554 146.684 151.589 1.00 82.33  ? 4137 ASN A C     1 
ATOM   19741 O  O     . ASN A 1 4137 ? 175.224 145.867 150.947 1.00 87.10  ? 4137 ASN A O     1 
ATOM   19742 C  CB    . ASN A 1 4137 ? 172.126 146.882 150.976 1.00 75.13  ? 4137 ASN A CB    1 
ATOM   19743 C  CG    . ASN A 1 4137 ? 172.014 148.391 150.990 1.00 87.74  ? 4137 ASN A CG    1 
ATOM   19744 O  OD1   . ASN A 1 4137 ? 172.725 149.070 151.728 1.00 93.57  ? 4137 ASN A OD1   1 
ATOM   19745 N  ND2   . ASN A 1 4137 ? 171.115 148.925 150.172 1.00 86.44  ? 4137 ASN A ND2   1 
ATOM   19746 N  N     . LEU A 1 4138 ? 175.037 147.879 151.937 1.00 72.42  ? 4138 LEU A N     1 
ATOM   19747 C  CA    . LEU A 1 4138 ? 176.428 148.216 151.648 1.00 69.14  ? 4138 LEU A CA    1 
ATOM   19748 C  C     . LEU A 1 4138 ? 177.382 147.317 152.422 1.00 71.21  ? 4138 LEU A C     1 
ATOM   19749 O  O     . LEU A 1 4138 ? 178.403 146.872 151.883 1.00 77.09  ? 4138 LEU A O     1 
ATOM   19750 C  CB    . LEU A 1 4138 ? 176.700 149.682 151.971 1.00 66.86  ? 4138 LEU A CB    1 
ATOM   19751 C  CG    . LEU A 1 4138 ? 178.140 150.116 151.693 1.00 66.68  ? 4138 LEU A CG    1 
ATOM   19752 C  CD1   . LEU A 1 4138 ? 178.327 150.440 150.221 1.00 67.74  ? 4138 LEU A CD1   1 
ATOM   19753 C  CD2   . LEU A 1 4138 ? 178.529 151.295 152.559 1.00 69.40  ? 4138 LEU A CD2   1 
ATOM   19754 N  N     . LEU A 1 4139 ? 177.069 147.040 153.690 1.00 54.81  ? 4139 LEU A N     1 
ATOM   19755 C  CA    . LEU A 1 4139 ? 177.914 146.153 154.482 1.00 55.86  ? 4139 LEU A CA    1 
ATOM   19756 C  C     . LEU A 1 4139 ? 177.953 144.754 153.882 1.00 61.82  ? 4139 LEU A C     1 
ATOM   19757 O  O     . LEU A 1 4139 ? 179.013 144.121 153.832 1.00 61.85  ? 4139 LEU A O     1 
ATOM   19758 C  CB    . LEU A 1 4139 ? 177.416 146.105 155.925 1.00 56.17  ? 4139 LEU A CB    1 
ATOM   19759 C  CG    . LEU A 1 4139 ? 177.581 147.385 156.744 1.00 56.79  ? 4139 LEU A CG    1 
ATOM   19760 C  CD1   . LEU A 1 4139 ? 176.909 147.242 158.097 1.00 62.73  ? 4139 LEU A CD1   1 
ATOM   19761 C  CD2   . LEU A 1 4139 ? 179.049 147.729 156.908 1.00 55.21  ? 4139 LEU A CD2   1 
ATOM   19762 N  N     . ARG A 1 4140 ? 176.803 144.256 153.423 1.00 76.43  ? 4140 ARG A N     1 
ATOM   19763 C  CA    . ARG A 1 4140 ? 176.775 142.946 152.782 1.00 71.81  ? 4140 ARG A CA    1 
ATOM   19764 C  C     . ARG A 1 4140 ? 177.517 142.953 151.452 1.00 77.48  ? 4140 ARG A C     1 
ATOM   19765 O  O     . ARG A 1 4140 ? 178.106 141.937 151.068 1.00 82.67  ? 4140 ARG A O     1 
ATOM   19766 C  CB    . ARG A 1 4140 ? 175.331 142.490 152.579 1.00 65.75  ? 4140 ARG A CB    1 
ATOM   19767 C  CG    . ARG A 1 4140 ? 174.554 142.303 153.869 1.00 69.99  ? 4140 ARG A CG    1 
ATOM   19768 C  CD    . ARG A 1 4140 ? 173.169 141.736 153.606 1.00 75.17  ? 4140 ARG A CD    1 
ATOM   19769 N  NE    . ARG A 1 4140 ? 173.178 140.755 152.528 1.00 82.74  ? 4140 ARG A NE    1 
ATOM   19770 C  CZ    . ARG A 1 4140 ? 173.007 139.451 152.701 1.00 84.70  ? 4140 ARG A CZ    1 
ATOM   19771 N  NH1   . ARG A 1 4140 ? 172.814 138.933 153.902 1.00 82.03  ? 4140 ARG A NH1   1 
ATOM   19772 N  NH2   . ARG A 1 4140 ? 173.031 138.648 151.641 1.00 78.43  ? 4140 ARG A NH2   1 
ATOM   19773 N  N     . ALA A 1 4141 ? 177.498 144.079 150.737 1.00 67.05  ? 4141 ALA A N     1 
ATOM   19774 C  CA    . ALA A 1 4141 ? 178.162 144.151 149.441 1.00 60.59  ? 4141 ALA A CA    1 
ATOM   19775 C  C     . ALA A 1 4141 ? 179.679 144.158 149.562 1.00 60.83  ? 4141 ALA A C     1 
ATOM   19776 O  O     . ALA A 1 4141 ? 180.360 143.492 148.776 1.00 66.10  ? 4141 ALA A O     1 
ATOM   19777 C  CB    . ALA A 1 4141 ? 177.696 145.393 148.681 1.00 60.87  ? 4141 ALA A CB    1 
ATOM   19778 N  N     . GLY A 1 4142 ? 180.228 144.894 150.530 1.00 60.49  ? 4142 GLY A N     1 
ATOM   19779 C  CA    . GLY A 1 4142 ? 181.657 145.070 150.646 1.00 63.30  ? 4142 GLY A CA    1 
ATOM   19780 C  C     . GLY A 1 4142 ? 182.297 144.146 151.673 1.00 64.29  ? 4142 GLY A C     1 
ATOM   19781 O  O     . GLY A 1 4142 ? 181.641 143.374 152.368 1.00 74.26  ? 4142 GLY A O     1 
ATOM   19782 N  N     . ARG A 1 4143 ? 183.621 144.243 151.750 1.00 63.31  ? 4143 ARG A N     1 
ATOM   19783 C  CA    . ARG A 1 4143 ? 184.412 143.502 152.722 1.00 66.66  ? 4143 ARG A CA    1 
ATOM   19784 C  C     . ARG A 1 4143 ? 184.782 144.432 153.869 1.00 67.61  ? 4143 ARG A C     1 
ATOM   19785 O  O     . ARG A 1 4143 ? 185.260 145.547 153.640 1.00 74.76  ? 4143 ARG A O     1 
ATOM   19786 C  CB    . ARG A 1 4143 ? 185.671 142.919 152.080 1.00 68.35  ? 4143 ARG A CB    1 
ATOM   19787 C  CG    . ARG A 1 4143 ? 186.641 142.319 153.080 1.00 67.62  ? 4143 ARG A CG    1 
ATOM   19788 C  CD    . ARG A 1 4143 ? 187.292 141.055 152.545 1.00 66.13  ? 4143 ARG A CD    1 
ATOM   19789 N  NE    . ARG A 1 4143 ? 188.270 140.519 153.483 1.00 70.59  ? 4143 ARG A NE    1 
ATOM   19790 C  CZ    . ARG A 1 4143 ? 189.231 139.666 153.157 1.00 75.24  ? 4143 ARG A CZ    1 
ATOM   19791 N  NH1   . ARG A 1 4143 ? 189.370 139.221 151.920 1.00 73.07  ? 4143 ARG A NH1   1 
ATOM   19792 N  NH2   . ARG A 1 4143 ? 190.072 139.247 154.098 1.00 75.02  ? 4143 ARG A NH2   1 
ATOM   19793 N  N     . ILE A 1 4144 ? 184.561 143.973 155.095 1.00 56.65  ? 4144 ILE A N     1 
ATOM   19794 C  CA    . ILE A 1 4144 ? 184.696 144.813 156.277 1.00 52.90  ? 4144 ILE A CA    1 
ATOM   19795 C  C     . ILE A 1 4144 ? 186.043 144.552 156.935 1.00 60.01  ? 4144 ILE A C     1 
ATOM   19796 O  O     . ILE A 1 4144 ? 186.418 143.399 157.172 1.00 69.78  ? 4144 ILE A O     1 
ATOM   19797 C  CB    . ILE A 1 4144 ? 183.545 144.558 157.263 1.00 54.94  ? 4144 ILE A CB    1 
ATOM   19798 C  CG1   . ILE A 1 4144 ? 182.200 144.730 156.559 1.00 57.63  ? 4144 ILE A CG1   1 
ATOM   19799 C  CG2   . ILE A 1 4144 ? 183.645 145.496 158.451 1.00 57.44  ? 4144 ILE A CG2   1 
ATOM   19800 C  CD1   . ILE A 1 4144 ? 181.050 144.069 157.277 1.00 60.61  ? 4144 ILE A CD1   1 
ATOM   19801 N  N     . PHE A 1 4145 ? 186.777 145.626 157.217 1.00 60.15  ? 4145 PHE A N     1 
ATOM   19802 C  CA    . PHE A 1 4145 ? 187.996 145.576 158.014 1.00 56.15  ? 4145 PHE A CA    1 
ATOM   19803 C  C     . PHE A 1 4145 ? 187.810 146.484 159.219 1.00 61.42  ? 4145 PHE A C     1 
ATOM   19804 O  O     . PHE A 1 4145 ? 187.429 147.649 159.068 1.00 63.37  ? 4145 PHE A O     1 
ATOM   19805 C  CB    . PHE A 1 4145 ? 189.218 146.008 157.202 1.00 54.79  ? 4145 PHE A CB    1 
ATOM   19806 C  CG    . PHE A 1 4145 ? 189.531 145.101 156.051 1.00 56.64  ? 4145 PHE A CG    1 
ATOM   19807 C  CD1   . PHE A 1 4145 ? 190.199 143.909 156.257 1.00 62.55  ? 4145 PHE A CD1   1 
ATOM   19808 C  CD2   . PHE A 1 4145 ? 189.165 145.443 154.763 1.00 61.14  ? 4145 PHE A CD2   1 
ATOM   19809 C  CE1   . PHE A 1 4145 ? 190.492 143.073 155.202 1.00 65.22  ? 4145 PHE A CE1   1 
ATOM   19810 C  CE2   . PHE A 1 4145 ? 189.455 144.610 153.704 1.00 62.39  ? 4145 PHE A CE2   1 
ATOM   19811 C  CZ    . PHE A 1 4145 ? 190.118 143.424 153.924 1.00 64.51  ? 4145 PHE A CZ    1 
ATOM   19812 N  N     . VAL A 1 4146 ? 188.078 145.955 160.409 1.00 62.28  ? 4146 VAL A N     1 
ATOM   19813 C  CA    . VAL A 1 4146 ? 187.916 146.698 161.652 1.00 61.49  ? 4146 VAL A CA    1 
ATOM   19814 C  C     . VAL A 1 4146 ? 189.287 147.122 162.154 1.00 69.82  ? 4146 VAL A C     1 
ATOM   19815 O  O     . VAL A 1 4146 ? 190.169 146.281 162.366 1.00 77.32  ? 4146 VAL A O     1 
ATOM   19816 C  CB    . VAL A 1 4146 ? 187.174 145.864 162.709 1.00 59.90  ? 4146 VAL A CB    1 
ATOM   19817 C  CG1   . VAL A 1 4146 ? 187.380 146.459 164.089 1.00 59.76  ? 4146 VAL A CG1   1 
ATOM   19818 C  CG2   . VAL A 1 4146 ? 185.695 145.801 162.378 1.00 64.85  ? 4146 VAL A CG2   1 
ATOM   19819 N  N     . PHE A 1 4147 ? 189.467 148.426 162.339 1.00 62.64  ? 4147 PHE A N     1 
ATOM   19820 C  CA    . PHE A 1 4147 ? 190.689 148.990 162.891 1.00 59.23  ? 4147 PHE A CA    1 
ATOM   19821 C  C     . PHE A 1 4147 ? 190.408 149.465 164.308 1.00 67.12  ? 4147 PHE A C     1 
ATOM   19822 O  O     . PHE A 1 4147 ? 189.433 150.185 164.546 1.00 67.52  ? 4147 PHE A O     1 
ATOM   19823 C  CB    . PHE A 1 4147 ? 191.203 150.137 162.022 1.00 61.28  ? 4147 PHE A CB    1 
ATOM   19824 C  CG    . PHE A 1 4147 ? 191.721 149.688 160.691 1.00 54.36  ? 4147 PHE A CG    1 
ATOM   19825 C  CD1   . PHE A 1 4147 ? 190.880 149.616 159.597 1.00 59.29  ? 4147 PHE A CD1   1 
ATOM   19826 C  CD2   . PHE A 1 4147 ? 193.046 149.324 160.536 1.00 65.17  ? 4147 PHE A CD2   1 
ATOM   19827 C  CE1   . PHE A 1 4147 ? 191.351 149.196 158.373 1.00 61.54  ? 4147 PHE A CE1   1 
ATOM   19828 C  CE2   . PHE A 1 4147 ? 193.524 148.903 159.312 1.00 71.84  ? 4147 PHE A CE2   1 
ATOM   19829 C  CZ    . PHE A 1 4147 ? 192.675 148.840 158.230 1.00 66.04  ? 4147 PHE A CZ    1 
ATOM   19830 N  N     . GLU A 1 4148 ? 191.262 149.061 165.240 1.00 90.68  ? 4148 GLU A N     1 
ATOM   19831 C  CA    . GLU A 1 4148 ? 190.983 149.206 166.661 1.00 88.24  ? 4148 GLU A CA    1 
ATOM   19832 C  C     . GLU A 1 4148 ? 192.287 149.008 167.420 1.00 87.89  ? 4148 GLU A C     1 
ATOM   19833 O  O     . GLU A 1 4148 ? 193.314 148.660 166.819 1.00 91.70  ? 4148 GLU A O     1 
ATOM   19834 C  CB    . GLU A 1 4148 ? 189.909 148.201 167.113 1.00 78.72  ? 4148 GLU A CB    1 
ATOM   19835 C  CG    . GLU A 1 4148 ? 190.363 146.760 167.075 1.00 83.40  ? 4148 GLU A CG    1 
ATOM   19836 C  CD    . GLU A 1 4148 ? 189.565 145.880 168.007 1.00 92.87  ? 4148 GLU A CD    1 
ATOM   19837 O  OE1   . GLU A 1 4148 ? 188.691 146.408 168.726 1.00 92.79  ? 4148 GLU A OE1   1 
ATOM   19838 O  OE2   . GLU A 1 4148 ? 189.805 144.657 168.014 1.00 94.72  ? 4148 GLU A OE2   1 
ATOM   19839 N  N     . PRO A 1 4149 ? 192.294 149.248 168.731 1.00 84.03  ? 4149 PRO A N     1 
ATOM   19840 C  CA    . PRO A 1 4149 ? 193.510 149.019 169.520 1.00 81.91  ? 4149 PRO A CA    1 
ATOM   19841 C  C     . PRO A 1 4149 ? 194.004 147.591 169.378 1.00 88.30  ? 4149 PRO A C     1 
ATOM   19842 O  O     . PRO A 1 4149 ? 193.202 146.645 169.349 1.00 91.24  ? 4149 PRO A O     1 
ATOM   19843 C  CB    . PRO A 1 4149 ? 193.054 149.301 170.957 1.00 88.38  ? 4149 PRO A CB    1 
ATOM   19844 C  CG    . PRO A 1 4149 ? 191.967 150.283 170.812 1.00 89.87  ? 4149 PRO A CG    1 
ATOM   19845 C  CD    . PRO A 1 4149 ? 191.299 150.033 169.487 1.00 87.03  ? 4149 PRO A CD    1 
ATOM   19846 N  N     . PRO A 1 4150 ? 195.317 147.399 169.275 1.00 75.57  ? 4150 PRO A N     1 
ATOM   19847 C  CA    . PRO A 1 4150 ? 195.853 146.044 169.223 1.00 73.39  ? 4150 PRO A CA    1 
ATOM   19848 C  C     . PRO A 1 4150 ? 195.553 145.299 170.507 1.00 73.74  ? 4150 PRO A C     1 
ATOM   19849 O  O     . PRO A 1 4150 ? 195.401 145.911 171.581 1.00 72.92  ? 4150 PRO A O     1 
ATOM   19850 C  CB    . PRO A 1 4150 ? 197.362 146.265 169.039 1.00 74.10  ? 4150 PRO A CB    1 
ATOM   19851 C  CG    . PRO A 1 4150 ? 197.598 147.723 169.261 1.00 78.28  ? 4150 PRO A CG    1 
ATOM   19852 C  CD    . PRO A 1 4150 ? 196.328 148.417 168.956 1.00 74.23  ? 4150 PRO A CD    1 
ATOM   19853 N  N     . PRO A 1 4151 ? 195.443 143.970 170.443 1.00 73.65  ? 4151 PRO A N     1 
ATOM   19854 C  CA    . PRO A 1 4151 ? 195.043 143.204 171.637 1.00 74.63  ? 4151 PRO A CA    1 
ATOM   19855 C  C     . PRO A 1 4151 ? 195.980 143.355 172.823 1.00 77.43  ? 4151 PRO A C     1 
ATOM   19856 O  O     . PRO A 1 4151 ? 195.514 143.328 173.968 1.00 77.85  ? 4151 PRO A O     1 
ATOM   19857 C  CB    . PRO A 1 4151 ? 195.018 141.755 171.130 1.00 74.25  ? 4151 PRO A CB    1 
ATOM   19858 C  CG    . PRO A 1 4151 ? 195.822 141.760 169.869 1.00 74.86  ? 4151 PRO A CG    1 
ATOM   19859 C  CD    . PRO A 1 4151 ? 195.618 143.108 169.264 1.00 76.81  ? 4151 PRO A CD    1 
ATOM   19860 N  N     . GLY A 1 4152 ? 197.282 143.508 172.596 1.00 72.02  ? 4152 GLY A N     1 
ATOM   19861 C  CA    . GLY A 1 4152 ? 198.212 143.560 173.706 1.00 68.17  ? 4152 GLY A CA    1 
ATOM   19862 C  C     . GLY A 1 4152 ? 199.477 144.347 173.437 1.00 68.85  ? 4152 GLY A C     1 
ATOM   19863 O  O     . GLY A 1 4152 ? 199.607 144.994 172.393 1.00 74.38  ? 4152 GLY A O     1 
ATOM   19864 N  N     . VAL A 1 4153 ? 200.415 144.303 174.385 1.00 59.27  ? 4153 VAL A N     1 
ATOM   19865 C  CA    . VAL A 1 4153 ? 201.675 145.026 174.228 1.00 52.96  ? 4153 VAL A CA    1 
ATOM   19866 C  C     . VAL A 1 4153 ? 202.457 144.476 173.042 1.00 61.71  ? 4153 VAL A C     1 
ATOM   19867 O  O     . VAL A 1 4153 ? 202.988 145.232 172.221 1.00 73.26  ? 4153 VAL A O     1 
ATOM   19868 C  CB    . VAL A 1 4153 ? 202.499 144.955 175.526 1.00 53.70  ? 4153 VAL A CB    1 
ATOM   19869 C  CG1   . VAL A 1 4153 ? 203.935 145.377 175.268 1.00 55.29  ? 4153 VAL A CG1   1 
ATOM   19870 C  CG2   . VAL A 1 4153 ? 201.873 145.824 176.597 1.00 60.41  ? 4153 VAL A CG2   1 
ATOM   19871 N  N     . LYS A 1 4154 ? 202.536 143.148 172.936 1.00 63.77  ? 4154 LYS A N     1 
ATOM   19872 C  CA    . LYS A 1 4154 ? 203.296 142.532 171.853 1.00 58.58  ? 4154 LYS A CA    1 
ATOM   19873 C  C     . LYS A 1 4154 ? 202.730 142.915 170.492 1.00 62.83  ? 4154 LYS A C     1 
ATOM   19874 O  O     . LYS A 1 4154 ? 203.480 143.288 169.580 1.00 71.65  ? 4154 LYS A O     1 
ATOM   19875 C  CB    . LYS A 1 4154 ? 203.303 141.014 172.028 1.00 63.40  ? 4154 LYS A CB    1 
ATOM   19876 C  CG    . LYS A 1 4154 ? 203.845 140.238 170.843 1.00 67.99  ? 4154 LYS A CG    1 
ATOM   19877 C  CD    . LYS A 1 4154 ? 203.730 138.742 171.086 1.00 57.59  ? 4154 LYS A CD    1 
ATOM   19878 C  CE    . LYS A 1 4154 ? 204.169 137.944 169.873 1.00 67.09  ? 4154 LYS A CE    1 
ATOM   19879 N  NZ    . LYS A 1 4154 ? 204.190 136.484 170.160 1.00 74.85  ? 4154 LYS A NZ    1 
ATOM   19880 N  N     . ALA A 1 4155 ? 201.406 142.844 170.341 1.00 54.63  ? 4155 ALA A N     1 
ATOM   19881 C  CA    . ALA A 1 4155 ? 200.785 143.227 169.079 1.00 55.46  ? 4155 ALA A CA    1 
ATOM   19882 C  C     . ALA A 1 4155 ? 200.983 144.709 168.796 1.00 65.03  ? 4155 ALA A C     1 
ATOM   19883 O  O     . ALA A 1 4155 ? 201.185 145.106 167.643 1.00 71.14  ? 4155 ALA A O     1 
ATOM   19884 C  CB    . ALA A 1 4155 ? 199.298 142.878 169.097 1.00 59.71  ? 4155 ALA A CB    1 
ATOM   19885 N  N     . ASN A 1 4156 ? 200.927 145.544 169.836 1.00 63.55  ? 4156 ASN A N     1 
ATOM   19886 C  CA    . ASN A 1 4156 ? 201.135 146.976 169.646 1.00 58.37  ? 4156 ASN A CA    1 
ATOM   19887 C  C     . ASN A 1 4156 ? 202.542 147.271 169.141 1.00 62.64  ? 4156 ASN A C     1 
ATOM   19888 O  O     . ASN A 1 4156 ? 202.719 148.057 168.202 1.00 70.73  ? 4156 ASN A O     1 
ATOM   19889 C  CB    . ASN A 1 4156 ? 200.866 147.720 170.953 1.00 55.47  ? 4156 ASN A CB    1 
ATOM   19890 C  CG    . ASN A 1 4156 ? 200.420 149.148 170.728 1.00 60.42  ? 4156 ASN A CG    1 
ATOM   19891 O  OD1   . ASN A 1 4156 ? 201.038 149.890 169.967 1.00 68.77  ? 4156 ASN A OD1   1 
ATOM   19892 N  ND2   . ASN A 1 4156 ? 199.341 149.542 171.393 1.00 59.53  ? 4156 ASN A ND2   1 
ATOM   19893 N  N     . MET A 1 4157 ? 203.556 146.651 169.749 1.00 61.01  ? 4157 MET A N     1 
ATOM   19894 C  CA    . MET A 1 4157 ? 204.924 146.855 169.283 1.00 56.54  ? 4157 MET A CA    1 
ATOM   19895 C  C     . MET A 1 4157 ? 205.117 146.312 167.874 1.00 65.19  ? 4157 MET A C     1 
ATOM   19896 O  O     . MET A 1 4157 ? 205.812 146.930 167.059 1.00 70.84  ? 4157 MET A O     1 
ATOM   19897 C  CB    . MET A 1 4157 ? 205.922 146.211 170.243 1.00 54.94  ? 4157 MET A CB    1 
ATOM   19898 C  CG    . MET A 1 4157 ? 205.706 146.550 171.701 1.00 59.29  ? 4157 MET A CG    1 
ATOM   19899 S  SD    . MET A 1 4157 ? 207.008 145.879 172.746 1.00 82.01  ? 4157 MET A SD    1 
ATOM   19900 C  CE    . MET A 1 4157 ? 208.318 147.054 172.430 1.00 66.56  ? 4157 MET A CE    1 
ATOM   19901 N  N     . LEU A 1 4158 ? 204.523 145.156 167.568 1.00 69.53  ? 4158 LEU A N     1 
ATOM   19902 C  CA    . LEU A 1 4158 ? 204.639 144.612 166.219 1.00 63.65  ? 4158 LEU A CA    1 
ATOM   19903 C  C     . LEU A 1 4158 ? 204.024 145.554 165.194 1.00 66.99  ? 4158 LEU A C     1 
ATOM   19904 O  O     . LEU A 1 4158 ? 204.613 145.805 164.136 1.00 75.99  ? 4158 LEU A O     1 
ATOM   19905 C  CB    . LEU A 1 4158 ? 203.980 143.236 166.150 1.00 58.03  ? 4158 LEU A CB    1 
ATOM   19906 C  CG    . LEU A 1 4158 ? 204.795 142.071 166.708 1.00 59.51  ? 4158 LEU A CG    1 
ATOM   19907 C  CD1   . LEU A 1 4158 ? 204.042 140.764 166.534 1.00 70.67  ? 4158 LEU A CD1   1 
ATOM   19908 C  CD2   . LEU A 1 4158 ? 206.157 142.002 166.041 1.00 62.84  ? 4158 LEU A CD2   1 
ATOM   19909 N  N     . ARG A 1 4159 ? 202.844 146.099 165.499 1.00 61.71  ? 4159 ARG A N     1 
ATOM   19910 C  CA    . ARG A 1 4159 ? 202.197 147.041 164.594 1.00 67.57  ? 4159 ARG A CA    1 
ATOM   19911 C  C     . ARG A 1 4159 ? 203.030 148.304 164.422 1.00 78.23  ? 4159 ARG A C     1 
ATOM   19912 O  O     . ARG A 1 4159 ? 203.182 148.810 163.304 1.00 83.68  ? 4159 ARG A O     1 
ATOM   19913 C  CB    . ARG A 1 4159 ? 200.804 147.382 165.119 1.00 67.94  ? 4159 ARG A CB    1 
ATOM   19914 C  CG    . ARG A 1 4159 ? 200.200 148.645 164.537 1.00 68.48  ? 4159 ARG A CG    1 
ATOM   19915 C  CD    . ARG A 1 4159 ? 198.752 148.785 164.967 1.00 75.33  ? 4159 ARG A CD    1 
ATOM   19916 N  NE    . ARG A 1 4159 ? 198.090 147.489 165.057 1.00 81.71  ? 4159 ARG A NE    1 
ATOM   19917 C  CZ    . ARG A 1 4159 ? 196.776 147.314 165.031 1.00 80.81  ? 4159 ARG A CZ    1 
ATOM   19918 N  NH1   . ARG A 1 4159 ? 195.945 148.338 164.921 1.00 81.55  ? 4159 ARG A NH1   1 
ATOM   19919 N  NH2   . ARG A 1 4159 ? 196.283 146.082 165.118 1.00 75.56  ? 4159 ARG A NH2   1 
ATOM   19920 N  N     . THR A 1 4160 ? 203.579 148.829 165.522 1.00 76.20  ? 4160 THR A N     1 
ATOM   19921 C  CA    . THR A 1 4160 ? 204.390 150.039 165.436 1.00 64.25  ? 4160 THR A CA    1 
ATOM   19922 C  C     . THR A 1 4160 ? 205.638 149.809 164.593 1.00 58.64  ? 4160 THR A C     1 
ATOM   19923 O  O     . THR A 1 4160 ? 205.996 150.648 163.759 1.00 66.36  ? 4160 THR A O     1 
ATOM   19924 C  CB    . THR A 1 4160 ? 204.769 150.516 166.838 1.00 60.89  ? 4160 THR A CB    1 
ATOM   19925 O  OG1   . THR A 1 4160 ? 203.607 151.032 167.498 1.00 63.24  ? 4160 THR A OG1   1 
ATOM   19926 C  CG2   . THR A 1 4160 ? 205.824 151.607 166.763 1.00 57.27  ? 4160 THR A CG2   1 
ATOM   19927 N  N     . PHE A 1 4161 ? 206.308 148.670 164.787 1.00 58.52  ? 4161 PHE A N     1 
ATOM   19928 C  CA    . PHE A 1 4161 ? 207.504 148.381 164.005 1.00 67.38  ? 4161 PHE A CA    1 
ATOM   19929 C  C     . PHE A 1 4161 ? 207.173 148.118 162.542 1.00 68.80  ? 4161 PHE A C     1 
ATOM   19930 O  O     . PHE A 1 4161 ? 207.983 148.429 161.661 1.00 72.74  ? 4161 PHE A O     1 
ATOM   19931 C  CB    . PHE A 1 4161 ? 208.251 147.190 164.605 1.00 65.91  ? 4161 PHE A CB    1 
ATOM   19932 C  CG    . PHE A 1 4161 ? 209.176 147.561 165.725 1.00 66.09  ? 4161 PHE A CG    1 
ATOM   19933 C  CD1   . PHE A 1 4161 ? 210.280 148.362 165.490 1.00 67.34  ? 4161 PHE A CD1   1 
ATOM   19934 C  CD2   . PHE A 1 4161 ? 208.942 147.114 167.013 1.00 66.77  ? 4161 PHE A CD2   1 
ATOM   19935 C  CE1   . PHE A 1 4161 ? 211.133 148.707 166.517 1.00 68.16  ? 4161 PHE A CE1   1 
ATOM   19936 C  CE2   . PHE A 1 4161 ? 209.791 147.456 168.044 1.00 69.64  ? 4161 PHE A CE2   1 
ATOM   19937 C  CZ    . PHE A 1 4161 ? 210.888 148.254 167.795 1.00 74.39  ? 4161 PHE A CZ    1 
ATOM   19938 N  N     . SER A 1 4162 ? 206.001 147.545 162.261 1.00 66.49  ? 4162 SER A N     1 
ATOM   19939 C  CA    . SER A 1 4162 ? 205.607 147.326 160.874 1.00 71.36  ? 4162 SER A CA    1 
ATOM   19940 C  C     . SER A 1 4162 ? 205.274 148.639 160.178 1.00 74.44  ? 4162 SER A C     1 
ATOM   19941 O  O     . SER A 1 4162 ? 205.599 148.822 158.999 1.00 80.10  ? 4162 SER A O     1 
ATOM   19942 C  CB    . SER A 1 4162 ? 204.417 146.370 160.813 1.00 73.04  ? 4162 SER A CB    1 
ATOM   19943 O  OG    . SER A 1 4162 ? 203.195 147.071 160.958 1.00 80.41  ? 4162 SER A OG    1 
ATOM   19944 N  N     . SER A 1 4163 ? 204.622 149.563 160.888 1.00 66.84  ? 4163 SER A N     1 
ATOM   19945 C  CA    . SER A 1 4163 ? 204.215 150.821 160.269 1.00 71.56  ? 4163 SER A CA    1 
ATOM   19946 C  C     . SER A 1 4163 ? 205.419 151.672 159.880 1.00 75.50  ? 4163 SER A C     1 
ATOM   19947 O  O     . SER A 1 4163 ? 205.457 152.235 158.780 1.00 75.61  ? 4163 SER A O     1 
ATOM   19948 C  CB    . SER A 1 4163 ? 203.297 151.597 161.212 1.00 72.99  ? 4163 SER A CB    1 
ATOM   19949 O  OG    . SER A 1 4163 ? 204.037 152.193 162.262 1.00 84.05  ? 4163 SER A OG    1 
ATOM   19950 N  N     . ILE A 1 4164 ? 206.403 151.780 160.761 1.00 74.40  ? 4164 ILE A N     1 
ATOM   19951 C  CA    . ILE A 1 4164 ? 207.572 152.620 160.496 1.00 72.73  ? 4164 ILE A CA    1 
ATOM   19952 C  C     . ILE A 1 4164 ? 208.426 151.954 159.420 1.00 78.53  ? 4164 ILE A C     1 
ATOM   19953 O  O     . ILE A 1 4164 ? 208.743 150.760 159.545 1.00 75.86  ? 4164 ILE A O     1 
ATOM   19954 C  CB    . ILE A 1 4164 ? 208.374 152.844 161.772 1.00 71.10  ? 4164 ILE A CB    1 
ATOM   19955 C  CG1   . ILE A 1 4164 ? 207.521 153.569 162.814 1.00 69.18  ? 4164 ILE A CG1   1 
ATOM   19956 C  CG2   . ILE A 1 4164 ? 209.632 153.641 161.478 1.00 70.93  ? 4164 ILE A CG2   1 
ATOM   19957 C  CD1   . ILE A 1 4164 ? 208.189 153.698 164.162 1.00 74.95  ? 4164 ILE A CD1   1 
ATOM   19958 N  N     . PRO A 1 4165 ? 208.804 152.672 158.363 1.00 82.21  ? 4165 PRO A N     1 
ATOM   19959 C  CA    . PRO A 1 4165 ? 209.665 152.075 157.336 1.00 77.72  ? 4165 PRO A CA    1 
ATOM   19960 C  C     . PRO A 1 4165 ? 211.017 151.674 157.907 1.00 81.51  ? 4165 PRO A C     1 
ATOM   19961 O  O     . PRO A 1 4165 ? 211.541 152.304 158.828 1.00 84.43  ? 4165 PRO A O     1 
ATOM   19962 C  CB    . PRO A 1 4165 ? 209.805 153.191 156.294 1.00 76.12  ? 4165 PRO A CB    1 
ATOM   19963 C  CG    . PRO A 1 4165 ? 208.645 154.099 156.543 1.00 82.82  ? 4165 PRO A CG    1 
ATOM   19964 C  CD    . PRO A 1 4165 ? 208.397 154.043 158.017 1.00 78.59  ? 4165 PRO A CD    1 
ATOM   19965 N  N     . VAL A 1 4166 ? 211.578 150.602 157.343 1.00 82.72  ? 4166 VAL A N     1 
ATOM   19966 C  CA    . VAL A 1 4166 ? 212.849 150.076 157.834 1.00 83.14  ? 4166 VAL A CA    1 
ATOM   19967 C  C     . VAL A 1 4166 ? 213.970 151.083 157.613 1.00 85.68  ? 4166 VAL A C     1 
ATOM   19968 O  O     . VAL A 1 4166 ? 214.839 151.266 158.476 1.00 85.54  ? 4166 VAL A O     1 
ATOM   19969 C  CB    . VAL A 1 4166 ? 213.161 148.726 157.163 1.00 81.19  ? 4166 VAL A CB    1 
ATOM   19970 C  CG1   . VAL A 1 4166 ? 214.495 148.183 157.652 1.00 83.85  ? 4166 VAL A CG1   1 
ATOM   19971 C  CG2   . VAL A 1 4166 ? 212.043 147.732 157.430 1.00 81.19  ? 4166 VAL A CG2   1 
ATOM   19972 N  N     . SER A 1 4167 ? 213.974 151.748 156.455 1.00 86.10  ? 4167 SER A N     1 
ATOM   19973 C  CA    . SER A 1 4167 ? 215.041 152.695 156.147 1.00 84.65  ? 4167 SER A CA    1 
ATOM   19974 C  C     . SER A 1 4167 ? 215.073 153.856 157.132 1.00 84.15  ? 4167 SER A C     1 
ATOM   19975 O  O     . SER A 1 4167 ? 216.142 154.420 157.389 1.00 84.29  ? 4167 SER A O     1 
ATOM   19976 C  CB    . SER A 1 4167 ? 214.881 153.218 154.720 1.00 89.73  ? 4167 SER A CB    1 
ATOM   19977 O  OG    . SER A 1 4167 ? 213.588 153.761 154.519 1.00 90.94  ? 4167 SER A OG    1 
ATOM   19978 N  N     . ARG A 1 4168 ? 213.918 154.232 157.687 1.00 80.51  ? 4168 ARG A N     1 
ATOM   19979 C  CA    . ARG A 1 4168 ? 213.884 155.337 158.639 1.00 79.99  ? 4168 ARG A CA    1 
ATOM   19980 C  C     . ARG A 1 4168 ? 214.628 154.991 159.923 1.00 85.99  ? 4168 ARG A C     1 
ATOM   19981 O  O     . ARG A 1 4168 ? 215.401 155.807 160.437 1.00 88.78  ? 4168 ARG A O     1 
ATOM   19982 C  CB    . ARG A 1 4168 ? 212.437 155.720 158.946 1.00 79.78  ? 4168 ARG A CB    1 
ATOM   19983 C  CG    . ARG A 1 4168 ? 212.300 156.868 159.929 1.00 81.59  ? 4168 ARG A CG    1 
ATOM   19984 C  CD    . ARG A 1 4168 ? 210.843 157.170 160.224 1.00 85.34  ? 4168 ARG A CD    1 
ATOM   19985 N  NE    . ARG A 1 4168 ? 210.612 158.598 160.405 1.00 83.86  ? 4168 ARG A NE    1 
ATOM   19986 C  CZ    . ARG A 1 4168 ? 209.413 159.159 160.477 1.00 83.75  ? 4168 ARG A CZ    1 
ATOM   19987 N  NH1   . ARG A 1 4168 ? 208.307 158.439 160.389 1.00 81.45  ? 4168 ARG A NH1   1 
ATOM   19988 N  NH2   . ARG A 1 4168 ? 209.322 160.475 160.640 1.00 86.87  ? 4168 ARG A NH2   1 
ATOM   19989 N  N     . ILE A 1 4169 ? 214.407 153.788 160.455 1.00 86.96  ? 4169 ILE A N     1 
ATOM   19990 C  CA    . ILE A 1 4169 ? 215.065 153.396 161.697 1.00 82.96  ? 4169 ILE A CA    1 
ATOM   19991 C  C     . ILE A 1 4169 ? 216.558 153.193 161.474 1.00 83.30  ? 4169 ILE A C     1 
ATOM   19992 O  O     . ILE A 1 4169 ? 217.385 153.614 162.291 1.00 85.87  ? 4169 ILE A O     1 
ATOM   19993 C  CB    . ILE A 1 4169 ? 214.401 152.135 162.277 1.00 78.44  ? 4169 ILE A CB    1 
ATOM   19994 C  CG1   . ILE A 1 4169 ? 212.927 152.401 162.583 1.00 83.21  ? 4169 ILE A CG1   1 
ATOM   19995 C  CG2   . ILE A 1 4169 ? 215.126 151.676 163.528 1.00 81.04  ? 4169 ILE A CG2   1 
ATOM   19996 C  CD1   . ILE A 1 4169 ? 212.168 151.176 163.036 1.00 83.32  ? 4169 ILE A CD1   1 
ATOM   19997 N  N     . CYS A 1 4170 ? 216.929 152.552 160.367 1.00 97.89  ? 4170 CYS A N     1 
ATOM   19998 C  CA    . CYS A 1 4170 ? 218.331 152.236 160.088 1.00 98.63  ? 4170 CYS A CA    1 
ATOM   19999 C  C     . CYS A 1 4170 ? 219.000 153.418 159.384 1.00 98.39  ? 4170 CYS A C     1 
ATOM   20000 O  O     . CYS A 1 4170 ? 219.343 153.379 158.201 1.00 101.12 ? 4170 CYS A O     1 
ATOM   20001 C  CB    . CYS A 1 4170 ? 218.432 150.959 159.265 1.00 102.38 ? 4170 CYS A CB    1 
ATOM   20002 S  SG    . CYS A 1 4170 ? 217.922 149.464 160.145 1.00 112.77 ? 4170 CYS A SG    1 
ATOM   20003 N  N     . LYS A 1 4171 ? 219.180 154.489 160.148 1.00 89.29  ? 4171 LYS A N     1 
ATOM   20004 C  CA    . LYS A 1 4171 ? 219.885 155.670 159.683 1.00 88.63  ? 4171 LYS A CA    1 
ATOM   20005 C  C     . LYS A 1 4171 ? 221.301 155.668 160.261 1.00 91.70  ? 4171 LYS A C     1 
ATOM   20006 O  O     . LYS A 1 4171 ? 221.746 154.687 160.865 1.00 92.97  ? 4171 LYS A O     1 
ATOM   20007 C  CB    . LYS A 1 4171 ? 219.095 156.930 160.047 1.00 92.24  ? 4171 LYS A CB    1 
ATOM   20008 C  CG    . LYS A 1 4171 ? 219.342 158.111 159.116 1.00 90.70  ? 4171 LYS A CG    1 
ATOM   20009 C  CD    . LYS A 1 4171 ? 218.563 157.973 157.818 1.00 90.65  ? 4171 LYS A CD    1 
ATOM   20010 C  CE    . LYS A 1 4171 ? 217.235 158.708 157.881 1.00 93.45  ? 4171 LYS A CE    1 
ATOM   20011 N  NZ    . LYS A 1 4171 ? 216.572 158.758 156.549 1.00 91.52  ? 4171 LYS A NZ    1 
ATOM   20012 N  N     . SER A 1 4172 ? 222.024 156.773 160.068 1.00 101.09 ? 4172 SER A N     1 
ATOM   20013 C  CA    . SER A 1 4172 ? 223.438 156.818 160.438 1.00 104.11 ? 4172 SER A CA    1 
ATOM   20014 C  C     . SER A 1 4172 ? 223.692 156.545 161.918 1.00 103.55 ? 4172 SER A C     1 
ATOM   20015 O  O     . SER A 1 4172 ? 224.562 155.711 162.222 1.00 103.14 ? 4172 SER A O     1 
ATOM   20016 C  CB    . SER A 1 4172 ? 224.038 158.160 160.006 1.00 104.68 ? 4172 SER A CB    1 
ATOM   20017 O  OG    . SER A 1 4172 ? 223.985 158.311 158.598 1.00 106.88 ? 4172 SER A OG    1 
ATOM   20018 N  N     . PRO A 1 4173 ? 223.005 157.178 162.873 1.00 97.30  ? 4173 PRO A N     1 
ATOM   20019 C  CA    . PRO A 1 4173 ? 223.279 156.861 164.283 1.00 92.74  ? 4173 PRO A CA    1 
ATOM   20020 C  C     . PRO A 1 4173 ? 222.760 155.476 164.641 1.00 95.27  ? 4173 PRO A C     1 
ATOM   20021 O  O     . PRO A 1 4173 ? 221.587 155.163 164.428 1.00 100.64 ? 4173 PRO A O     1 
ATOM   20022 C  CB    . PRO A 1 4173 ? 222.534 157.961 165.053 1.00 88.49  ? 4173 PRO A CB    1 
ATOM   20023 C  CG    . PRO A 1 4173 ? 222.216 159.011 164.039 1.00 91.67  ? 4173 PRO A CG    1 
ATOM   20024 C  CD    . PRO A 1 4173 ? 222.030 158.276 162.757 1.00 92.57  ? 4173 PRO A CD    1 
ATOM   20025 N  N     . ASN A 1 4174 ? 223.649 154.643 165.187 1.00 97.81  ? 4174 ASN A N     1 
ATOM   20026 C  CA    . ASN A 1 4174 ? 223.255 153.304 165.606 1.00 100.17 ? 4174 ASN A CA    1 
ATOM   20027 C  C     . ASN A 1 4174 ? 222.342 153.326 166.823 1.00 100.04 ? 4174 ASN A C     1 
ATOM   20028 O  O     . ASN A 1 4174 ? 221.675 152.324 167.102 1.00 97.37  ? 4174 ASN A O     1 
ATOM   20029 C  CB    . ASN A 1 4174 ? 224.492 152.455 165.901 1.00 99.79  ? 4174 ASN A CB    1 
ATOM   20030 C  CG    . ASN A 1 4174 ? 225.222 152.033 164.643 1.00 101.73 ? 4174 ASN A CG    1 
ATOM   20031 O  OD1   . ASN A 1 4174 ? 224.758 152.279 163.530 1.00 102.19 ? 4174 ASN A OD1   1 
ATOM   20032 N  ND2   . ASN A 1 4174 ? 226.372 151.390 164.812 1.00 97.35  ? 4174 ASN A ND2   1 
ATOM   20033 N  N     . GLU A 1 4175 ? 222.298 154.441 167.552 1.00 93.06  ? 4175 GLU A N     1 
ATOM   20034 C  CA    . GLU A 1 4175 ? 221.425 154.571 168.709 1.00 84.24  ? 4175 GLU A CA    1 
ATOM   20035 C  C     . GLU A 1 4175 ? 219.992 154.917 168.331 1.00 85.57  ? 4175 GLU A C     1 
ATOM   20036 O  O     . GLU A 1 4175 ? 219.128 154.946 169.214 1.00 94.74  ? 4175 GLU A O     1 
ATOM   20037 C  CB    . GLU A 1 4175 ? 221.977 155.635 169.662 1.00 86.08  ? 4175 GLU A CB    1 
ATOM   20038 C  CG    . GLU A 1 4175 ? 223.157 155.171 170.507 1.00 92.12  ? 4175 GLU A CG    1 
ATOM   20039 C  CD    . GLU A 1 4175 ? 224.432 154.984 169.706 1.00 96.32  ? 4175 GLU A CD    1 
ATOM   20040 O  OE1   . GLU A 1 4175 ? 224.487 155.443 168.546 1.00 99.56  ? 4175 GLU A OE1   1 
ATOM   20041 O  OE2   . GLU A 1 4175 ? 225.382 154.375 170.241 1.00 93.80  ? 4175 GLU A OE2   1 
ATOM   20042 N  N     . ARG A 1 4176 ? 219.722 155.183 167.052 1.00 68.22  ? 4176 ARG A N     1 
ATOM   20043 C  CA    . ARG A 1 4176 ? 218.365 155.521 166.635 1.00 63.25  ? 4176 ARG A CA    1 
ATOM   20044 C  C     . ARG A 1 4176 ? 217.427 154.332 166.792 1.00 67.34  ? 4176 ARG A C     1 
ATOM   20045 O  O     . ARG A 1 4176 ? 216.251 154.501 167.133 1.00 73.60  ? 4176 ARG A O     1 
ATOM   20046 C  CB    . ARG A 1 4176 ? 218.368 156.015 165.189 1.00 64.65  ? 4176 ARG A CB    1 
ATOM   20047 C  CG    . ARG A 1 4176 ? 217.009 156.466 164.684 1.00 68.59  ? 4176 ARG A CG    1 
ATOM   20048 C  CD    . ARG A 1 4176 ? 217.104 157.047 163.285 1.00 71.86  ? 4176 ARG A CD    1 
ATOM   20049 N  NE    . ARG A 1 4176 ? 218.184 158.019 163.170 1.00 77.00  ? 4176 ARG A NE    1 
ATOM   20050 C  CZ    . ARG A 1 4176 ? 218.015 159.288 162.825 1.00 72.44  ? 4176 ARG A CZ    1 
ATOM   20051 N  NH1   . ARG A 1 4176 ? 216.816 159.776 162.552 1.00 63.56  ? 4176 ARG A NH1   1 
ATOM   20052 N  NH2   . ARG A 1 4176 ? 219.075 160.087 162.750 1.00 74.09  ? 4176 ARG A NH2   1 
ATOM   20053 N  N     . ALA A 1 4177 ? 217.927 153.120 166.540 1.00 69.77  ? 4177 ALA A N     1 
ATOM   20054 C  CA    . ALA A 1 4177 ? 217.085 151.935 166.656 1.00 69.44  ? 4177 ALA A CA    1 
ATOM   20055 C  C     . ALA A 1 4177 ? 216.605 151.732 168.086 1.00 70.01  ? 4177 ALA A C     1 
ATOM   20056 O  O     . ALA A 1 4177 ? 215.434 151.411 168.316 1.00 77.72  ? 4177 ALA A O     1 
ATOM   20057 C  CB    . ALA A 1 4177 ? 217.842 150.703 166.164 1.00 70.24  ? 4177 ALA A CB    1 
ATOM   20058 N  N     . ARG A 1 4178 ? 217.496 151.915 169.063 1.00 68.82  ? 4178 ARG A N     1 
ATOM   20059 C  CA    . ARG A 1 4178 ? 217.102 151.733 170.456 1.00 64.89  ? 4178 ARG A CA    1 
ATOM   20060 C  C     . ARG A 1 4178 ? 216.140 152.824 170.904 1.00 66.86  ? 4178 ARG A C     1 
ATOM   20061 O  O     . ARG A 1 4178 ? 215.224 152.565 171.692 1.00 74.36  ? 4178 ARG A O     1 
ATOM   20062 C  CB    . ARG A 1 4178 ? 218.338 151.700 171.352 1.00 67.10  ? 4178 ARG A CB    1 
ATOM   20063 C  CG    . ARG A 1 4178 ? 218.105 151.041 172.698 1.00 70.00  ? 4178 ARG A CG    1 
ATOM   20064 C  CD    . ARG A 1 4178 ? 219.421 150.638 173.331 1.00 72.40  ? 4178 ARG A CD    1 
ATOM   20065 N  NE    . ARG A 1 4178 ? 219.274 149.546 174.285 1.00 71.41  ? 4178 ARG A NE    1 
ATOM   20066 C  CZ    . ARG A 1 4178 ? 219.951 148.408 174.224 1.00 72.82  ? 4178 ARG A CZ    1 
ATOM   20067 N  NH1   . ARG A 1 4178 ? 220.820 148.173 173.254 1.00 76.97  ? 4178 ARG A NH1   1 
ATOM   20068 N  NH2   . ARG A 1 4178 ? 219.755 147.485 175.159 1.00 75.58  ? 4178 ARG A NH2   1 
ATOM   20069 N  N     . LEU A 1 4179 ? 216.330 154.052 170.414 1.00 64.20  ? 4179 LEU A N     1 
ATOM   20070 C  CA    . LEU A 1 4179 ? 215.381 155.119 170.715 1.00 56.78  ? 4179 LEU A CA    1 
ATOM   20071 C  C     . LEU A 1 4179 ? 214.000 154.795 170.161 1.00 64.35  ? 4179 LEU A C     1 
ATOM   20072 O  O     . LEU A 1 4179 ? 212.986 155.000 170.839 1.00 75.27  ? 4179 LEU A O     1 
ATOM   20073 C  CB    . LEU A 1 4179 ? 215.883 156.447 170.149 1.00 51.30  ? 4179 LEU A CB    1 
ATOM   20074 C  CG    . LEU A 1 4179 ? 217.051 157.111 170.875 1.00 59.83  ? 4179 LEU A CG    1 
ATOM   20075 C  CD1   . LEU A 1 4179 ? 217.198 158.555 170.432 1.00 64.58  ? 4179 LEU A CD1   1 
ATOM   20076 C  CD2   . LEU A 1 4179 ? 216.852 157.030 172.374 1.00 66.44  ? 4179 LEU A CD2   1 
ATOM   20077 N  N     . TYR A 1 4180 ? 213.942 154.283 168.930 1.00 60.35  ? 4180 TYR A N     1 
ATOM   20078 C  CA    . TYR A 1 4180 ? 212.661 153.895 168.352 1.00 56.81  ? 4180 TYR A CA    1 
ATOM   20079 C  C     . TYR A 1 4180 ? 212.031 152.743 169.122 1.00 66.25  ? 4180 TYR A C     1 
ATOM   20080 O  O     . TYR A 1 4180 ? 210.811 152.713 169.307 1.00 75.22  ? 4180 TYR A O     1 
ATOM   20081 C  CB    . TYR A 1 4180 ? 212.836 153.522 166.883 1.00 63.08  ? 4180 TYR A CB    1 
ATOM   20082 C  CG    . TYR A 1 4180 ? 212.642 154.680 165.937 1.00 65.15  ? 4180 TYR A CG    1 
ATOM   20083 C  CD1   . TYR A 1 4180 ? 213.527 155.748 165.923 1.00 65.61  ? 4180 TYR A CD1   1 
ATOM   20084 C  CD2   . TYR A 1 4180 ? 211.568 154.708 165.062 1.00 71.03  ? 4180 TYR A CD2   1 
ATOM   20085 C  CE1   . TYR A 1 4180 ? 213.348 156.807 165.060 1.00 62.32  ? 4180 TYR A CE1   1 
ATOM   20086 C  CE2   . TYR A 1 4180 ? 211.381 155.761 164.196 1.00 72.37  ? 4180 TYR A CE2   1 
ATOM   20087 C  CZ    . TYR A 1 4180 ? 212.273 156.808 164.198 1.00 71.87  ? 4180 TYR A CZ    1 
ATOM   20088 O  OH    . TYR A 1 4180 ? 212.083 157.857 163.333 1.00 78.62  ? 4180 TYR A OH    1 
ATOM   20089 N  N     . PHE A 1 4181 ? 212.840 151.780 169.567 1.00 61.69  ? 4181 PHE A N     1 
ATOM   20090 C  CA    . PHE A 1 4181 ? 212.298 150.676 170.353 1.00 51.46  ? 4181 PHE A CA    1 
ATOM   20091 C  C     . PHE A 1 4181 ? 211.735 151.171 171.679 1.00 57.17  ? 4181 PHE A C     1 
ATOM   20092 O  O     . PHE A 1 4181 ? 210.661 150.732 172.109 1.00 77.31  ? 4181 PHE A O     1 
ATOM   20093 C  CB    . PHE A 1 4181 ? 213.374 149.617 170.587 1.00 56.47  ? 4181 PHE A CB    1 
ATOM   20094 C  CG    . PHE A 1 4181 ? 212.967 148.548 171.559 1.00 60.66  ? 4181 PHE A CG    1 
ATOM   20095 C  CD1   . PHE A 1 4181 ? 212.178 147.489 171.148 1.00 60.13  ? 4181 PHE A CD1   1 
ATOM   20096 C  CD2   . PHE A 1 4181 ? 213.377 148.598 172.880 1.00 66.25  ? 4181 PHE A CD2   1 
ATOM   20097 C  CE1   . PHE A 1 4181 ? 211.802 146.504 172.035 1.00 61.70  ? 4181 PHE A CE1   1 
ATOM   20098 C  CE2   . PHE A 1 4181 ? 213.002 147.615 173.771 1.00 61.55  ? 4181 PHE A CE2   1 
ATOM   20099 C  CZ    . PHE A 1 4181 ? 212.214 146.567 173.347 1.00 61.22  ? 4181 PHE A CZ    1 
ATOM   20100 N  N     . LEU A 1 4182 ? 212.448 152.082 172.344 1.00 49.60  ? 4182 LEU A N     1 
ATOM   20101 C  CA    . LEU A 1 4182 ? 211.945 152.653 173.588 1.00 49.24  ? 4182 LEU A CA    1 
ATOM   20102 C  C     . LEU A 1 4182 ? 210.652 153.421 173.355 1.00 52.59  ? 4182 LEU A C     1 
ATOM   20103 O  O     . LEU A 1 4182 ? 209.711 153.322 174.150 1.00 67.07  ? 4182 LEU A O     1 
ATOM   20104 C  CB    . LEU A 1 4182 ? 212.998 153.565 174.215 1.00 50.66  ? 4182 LEU A CB    1 
ATOM   20105 C  CG    . LEU A 1 4182 ? 214.045 152.883 175.091 1.00 55.34  ? 4182 LEU A CG    1 
ATOM   20106 C  CD1   . LEU A 1 4182 ? 215.137 153.865 175.465 1.00 54.31  ? 4182 LEU A CD1   1 
ATOM   20107 C  CD2   . LEU A 1 4182 ? 213.392 152.306 176.332 1.00 61.36  ? 4182 LEU A CD2   1 
ATOM   20108 N  N     . LEU A 1 4183 ? 210.589 154.192 172.269 1.00 49.15  ? 4183 LEU A N     1 
ATOM   20109 C  CA    . LEU A 1 4183 ? 209.374 154.939 171.963 1.00 46.31  ? 4183 LEU A CA    1 
ATOM   20110 C  C     . LEU A 1 4183 ? 208.213 153.993 171.682 1.00 49.15  ? 4183 LEU A C     1 
ATOM   20111 O  O     . LEU A 1 4183 ? 207.087 154.234 172.128 1.00 62.37  ? 4183 LEU A O     1 
ATOM   20112 C  CB    . LEU A 1 4183 ? 209.635 155.874 170.778 1.00 42.13  ? 4183 LEU A CB    1 
ATOM   20113 C  CG    . LEU A 1 4183 ? 208.769 157.099 170.450 1.00 44.34  ? 4183 LEU A CG    1 
ATOM   20114 C  CD1   . LEU A 1 4183 ? 209.233 157.695 169.133 1.00 57.08  ? 4183 LEU A CD1   1 
ATOM   20115 C  CD2   . LEU A 1 4183 ? 207.279 156.812 170.384 1.00 55.62  ? 4183 LEU A CD2   1 
ATOM   20116 N  N     . ALA A 1 4184 ? 208.470 152.907 170.950 1.00 43.55  ? 4184 ALA A N     1 
ATOM   20117 C  CA    . ALA A 1 4184 ? 207.416 151.940 170.662 1.00 43.93  ? 4184 ALA A CA    1 
ATOM   20118 C  C     . ALA A 1 4184 ? 206.923 151.263 171.933 1.00 52.16  ? 4184 ALA A C     1 
ATOM   20119 O  O     . ALA A 1 4184 ? 205.715 151.071 172.114 1.00 62.68  ? 4184 ALA A O     1 
ATOM   20120 C  CB    . ALA A 1 4184 ? 207.919 150.900 169.662 1.00 52.23  ? 4184 ALA A CB    1 
ATOM   20121 N  N     . TRP A 1 4185 ? 207.845 150.888 172.824 1.00 54.11  ? 4185 TRP A N     1 
ATOM   20122 C  CA    . TRP A 1 4185 ? 207.437 150.285 174.088 1.00 49.82  ? 4185 TRP A CA    1 
ATOM   20123 C  C     . TRP A 1 4185 ? 206.633 151.268 174.928 1.00 50.48  ? 4185 TRP A C     1 
ATOM   20124 O  O     . TRP A 1 4185 ? 205.641 150.889 175.558 1.00 59.40  ? 4185 TRP A O     1 
ATOM   20125 C  CB    . TRP A 1 4185 ? 208.656 149.790 174.865 1.00 46.02  ? 4185 TRP A CB    1 
ATOM   20126 C  CG    . TRP A 1 4185 ? 208.333 149.386 176.271 1.00 50.85  ? 4185 TRP A CG    1 
ATOM   20127 C  CD1   . TRP A 1 4185 ? 208.396 150.170 177.384 1.00 55.12  ? 4185 TRP A CD1   1 
ATOM   20128 C  CD2   . TRP A 1 4185 ? 207.884 148.099 176.712 1.00 55.16  ? 4185 TRP A CD2   1 
ATOM   20129 N  NE1   . TRP A 1 4185 ? 208.019 149.451 178.492 1.00 57.14  ? 4185 TRP A NE1   1 
ATOM   20130 C  CE2   . TRP A 1 4185 ? 207.699 148.177 178.105 1.00 51.11  ? 4185 TRP A CE2   1 
ATOM   20131 C  CE3   . TRP A 1 4185 ? 207.622 146.889 176.064 1.00 53.67  ? 4185 TRP A CE3   1 
ATOM   20132 C  CZ2   . TRP A 1 4185 ? 207.266 147.092 178.861 1.00 53.32  ? 4185 TRP A CZ2   1 
ATOM   20133 C  CZ3   . TRP A 1 4185 ? 207.192 145.814 176.817 1.00 46.49  ? 4185 TRP A CZ3   1 
ATOM   20134 C  CH2   . TRP A 1 4185 ? 207.018 145.922 178.200 1.00 53.05  ? 4185 TRP A CH2   1 
ATOM   20135 N  N     . PHE A 1 4186 ? 207.048 152.536 174.951 1.00 44.23  ? 4186 PHE A N     1 
ATOM   20136 C  CA    . PHE A 1 4186 ? 206.304 153.551 175.688 1.00 43.45  ? 4186 PHE A CA    1 
ATOM   20137 C  C     . PHE A 1 4186 ? 204.904 153.725 175.115 1.00 42.41  ? 4186 PHE A C     1 
ATOM   20138 O  O     . PHE A 1 4186 ? 203.925 153.832 175.861 1.00 56.12  ? 4186 PHE A O     1 
ATOM   20139 C  CB    . PHE A 1 4186 ? 207.070 154.874 175.666 1.00 40.41  ? 4186 PHE A CB    1 
ATOM   20140 C  CG    . PHE A 1 4186 ? 206.304 156.030 176.234 1.00 41.47  ? 4186 PHE A CG    1 
ATOM   20141 C  CD1   . PHE A 1 4186 ? 206.157 156.176 177.602 1.00 53.01  ? 4186 PHE A CD1   1 
ATOM   20142 C  CD2   . PHE A 1 4186 ? 205.739 156.980 175.402 1.00 46.52  ? 4186 PHE A CD2   1 
ATOM   20143 C  CE1   . PHE A 1 4186 ? 205.456 157.241 178.127 1.00 55.23  ? 4186 PHE A CE1   1 
ATOM   20144 C  CE2   . PHE A 1 4186 ? 205.037 158.047 175.922 1.00 48.21  ? 4186 PHE A CE2   1 
ATOM   20145 C  CZ    . PHE A 1 4186 ? 204.896 158.177 177.285 1.00 42.89  ? 4186 PHE A CZ    1 
ATOM   20146 N  N     . HIS A 1 4187 ? 204.790 153.752 173.786 1.00 39.02  ? 4187 HIS A N     1 
ATOM   20147 C  CA    . HIS A 1 4187 ? 203.483 153.895 173.154 1.00 37.08  ? 4187 HIS A CA    1 
ATOM   20148 C  C     . HIS A 1 4187 ? 202.585 152.706 173.466 1.00 44.40  ? 4187 HIS A C     1 
ATOM   20149 O  O     . HIS A 1 4187 ? 201.397 152.878 173.763 1.00 56.85  ? 4187 HIS A O     1 
ATOM   20150 C  CB    . HIS A 1 4187 ? 203.645 154.061 171.645 1.00 45.14  ? 4187 HIS A CB    1 
ATOM   20151 C  CG    . HIS A 1 4187 ? 202.364 154.354 170.929 1.00 48.11  ? 4187 HIS A CG    1 
ATOM   20152 N  ND1   . HIS A 1 4187 ? 201.657 155.522 171.117 1.00 55.57  ? 4187 HIS A ND1   1 
ATOM   20153 C  CD2   . HIS A 1 4187 ? 201.662 153.631 170.026 1.00 53.32  ? 4187 HIS A CD2   1 
ATOM   20154 C  CE1   . HIS A 1 4187 ? 200.575 155.505 170.360 1.00 55.17  ? 4187 HIS A CE1   1 
ATOM   20155 N  NE2   . HIS A 1 4187 ? 200.554 154.368 169.687 1.00 53.53  ? 4187 HIS A NE2   1 
ATOM   20156 N  N     . ALA A 1 4188 ? 203.134 151.491 173.401 1.00 45.43  ? 4188 ALA A N     1 
ATOM   20157 C  CA    . ALA A 1 4188 ? 202.350 150.308 173.738 1.00 44.35  ? 4188 ALA A CA    1 
ATOM   20158 C  C     . ALA A 1 4188 ? 201.909 150.340 175.195 1.00 46.77  ? 4188 ALA A C     1 
ATOM   20159 O  O     . ALA A 1 4188 ? 200.757 150.020 175.512 1.00 54.94  ? 4188 ALA A O     1 
ATOM   20160 C  CB    . ALA A 1 4188 ? 203.157 149.044 173.450 1.00 47.01  ? 4188 ALA A CB    1 
ATOM   20161 N  N     . ILE A 1 4189 ? 202.811 150.739 176.094 1.00 42.36  ? 4189 ILE A N     1 
ATOM   20162 C  CA    . ILE A 1 4189 ? 202.488 150.808 177.514 1.00 38.60  ? 4189 ILE A CA    1 
ATOM   20163 C  C     . ILE A 1 4189 ? 201.374 151.818 177.751 1.00 46.32  ? 4189 ILE A C     1 
ATOM   20164 O  O     . ILE A 1 4189 ? 200.437 151.570 178.519 1.00 52.36  ? 4189 ILE A O     1 
ATOM   20165 C  CB    . ILE A 1 4189 ? 203.754 151.162 178.317 1.00 38.02  ? 4189 ILE A CB    1 
ATOM   20166 C  CG1   . ILE A 1 4189 ? 204.553 149.901 178.639 1.00 50.40  ? 4189 ILE A CG1   1 
ATOM   20167 C  CG2   . ILE A 1 4189 ? 203.395 151.903 179.596 1.00 40.47  ? 4189 ILE A CG2   1 
ATOM   20168 C  CD1   . ILE A 1 4189 ? 203.944 149.047 179.698 1.00 53.65  ? 4189 ILE A CD1   1 
ATOM   20169 N  N     . ILE A 1 4190 ? 201.459 152.972 177.086 1.00 51.19  ? 4190 ILE A N     1 
ATOM   20170 C  CA    . ILE A 1 4190 ? 200.466 154.026 177.270 1.00 38.75  ? 4190 ILE A CA    1 
ATOM   20171 C  C     . ILE A 1 4190 ? 199.112 153.582 176.730 1.00 53.03  ? 4190 ILE A C     1 
ATOM   20172 O  O     . ILE A 1 4190 ? 198.073 153.782 177.369 1.00 66.44  ? 4190 ILE A O     1 
ATOM   20173 C  CB    . ILE A 1 4190 ? 200.943 155.327 176.601 1.00 37.55  ? 4190 ILE A CB    1 
ATOM   20174 C  CG1   . ILE A 1 4190 ? 202.122 155.919 177.371 1.00 50.81  ? 4190 ILE A CG1   1 
ATOM   20175 C  CG2   . ILE A 1 4190 ? 199.819 156.330 176.520 1.00 43.49  ? 4190 ILE A CG2   1 
ATOM   20176 C  CD1   . ILE A 1 4190 ? 201.812 156.250 178.804 1.00 57.33  ? 4190 ILE A CD1   1 
ATOM   20177 N  N     . GLN A 1 4191 ? 199.103 152.970 175.543 1.00 52.36  ? 4191 GLN A N     1 
ATOM   20178 C  CA    . GLN A 1 4191 ? 197.839 152.597 174.918 1.00 41.13  ? 4191 GLN A CA    1 
ATOM   20179 C  C     . GLN A 1 4191 ? 197.171 151.437 175.647 1.00 56.73  ? 4191 GLN A C     1 
ATOM   20180 O  O     . GLN A 1 4191 ? 195.939 151.374 175.717 1.00 66.71  ? 4191 GLN A O     1 
ATOM   20181 C  CB    . GLN A 1 4191 ? 198.058 152.247 173.448 1.00 48.40  ? 4191 GLN A CB    1 
ATOM   20182 C  CG    . GLN A 1 4191 ? 197.987 153.440 172.515 1.00 53.14  ? 4191 GLN A CG    1 
ATOM   20183 C  CD    . GLN A 1 4191 ? 197.609 153.048 171.103 1.00 65.63  ? 4191 GLN A CD    1 
ATOM   20184 O  OE1   . GLN A 1 4191 ? 198.295 152.251 170.464 1.00 63.00  ? 4191 GLN A OE1   1 
ATOM   20185 N  NE2   . GLN A 1 4191 ? 196.512 153.606 170.608 1.00 62.55  ? 4191 GLN A NE2   1 
ATOM   20186 N  N     . GLU A 1 4192 ? 197.958 150.501 176.181 1.00 59.94  ? 4192 GLU A N     1 
ATOM   20187 C  CA    . GLU A 1 4192 ? 197.356 149.371 176.880 1.00 56.91  ? 4192 GLU A CA    1 
ATOM   20188 C  C     . GLU A 1 4192 ? 196.752 149.786 178.215 1.00 62.13  ? 4192 GLU A C     1 
ATOM   20189 O  O     . GLU A 1 4192 ? 195.757 149.196 178.650 1.00 69.78  ? 4192 GLU A O     1 
ATOM   20190 C  CB    . GLU A 1 4192 ? 198.386 148.260 177.076 1.00 56.66  ? 4192 GLU A CB    1 
ATOM   20191 C  CG    . GLU A 1 4192 ? 198.795 147.561 175.786 1.00 71.02  ? 4192 GLU A CG    1 
ATOM   20192 C  CD    . GLU A 1 4192 ? 197.620 146.980 175.016 1.00 77.24  ? 4192 GLU A CD    1 
ATOM   20193 O  OE1   . GLU A 1 4192 ? 196.583 146.663 175.637 1.00 79.33  ? 4192 GLU A OE1   1 
ATOM   20194 O  OE2   . GLU A 1 4192 ? 197.734 146.846 173.780 1.00 77.02  ? 4192 GLU A OE2   1 
ATOM   20195 N  N     . ARG A 1 4193 ? 197.334 150.786 178.880 1.00 53.85  ? 4193 ARG A N     1 
ATOM   20196 C  CA    . ARG A 1 4193 ? 196.741 151.291 180.114 1.00 46.02  ? 4193 ARG A CA    1 
ATOM   20197 C  C     . ARG A 1 4193 ? 195.380 151.924 179.862 1.00 53.11  ? 4193 ARG A C     1 
ATOM   20198 O  O     . ARG A 1 4193 ? 194.564 152.024 180.784 1.00 70.92  ? 4193 ARG A O     1 
ATOM   20199 C  CB    . ARG A 1 4193 ? 197.677 152.300 180.776 1.00 50.34  ? 4193 ARG A CB    1 
ATOM   20200 C  CG    . ARG A 1 4193 ? 198.867 151.674 181.475 1.00 54.77  ? 4193 ARG A CG    1 
ATOM   20201 C  CD    . ARG A 1 4193 ? 199.658 152.715 182.241 1.00 51.57  ? 4193 ARG A CD    1 
ATOM   20202 N  NE    . ARG A 1 4193 ? 198.894 153.264 183.354 1.00 48.10  ? 4193 ARG A NE    1 
ATOM   20203 C  CZ    . ARG A 1 4193 ? 199.177 153.053 184.632 1.00 50.58  ? 4193 ARG A CZ    1 
ATOM   20204 N  NH1   . ARG A 1 4193 ? 200.210 152.314 184.998 1.00 61.10  ? 4193 ARG A NH1   1 
ATOM   20205 N  NH2   . ARG A 1 4193 ? 198.402 153.596 185.566 1.00 50.35  ? 4193 ARG A NH2   1 
ATOM   20206 N  N     . LEU A 1 4194 ? 195.122 152.359 178.627 1.00 55.55  ? 4194 LEU A N     1 
ATOM   20207 C  CA    . LEU A 1 4194 ? 193.832 152.941 178.280 1.00 50.66  ? 4194 LEU A CA    1 
ATOM   20208 C  C     . LEU A 1 4194 ? 192.688 151.954 178.451 1.00 58.16  ? 4194 LEU A C     1 
ATOM   20209 O  O     . LEU A 1 4194 ? 191.550 152.376 178.682 1.00 61.84  ? 4194 LEU A O     1 
ATOM   20210 C  CB    . LEU A 1 4194 ? 193.865 153.443 176.838 1.00 56.08  ? 4194 LEU A CB    1 
ATOM   20211 C  CG    . LEU A 1 4194 ? 193.381 154.855 176.530 1.00 53.04  ? 4194 LEU A CG    1 
ATOM   20212 C  CD1   . LEU A 1 4194 ? 194.056 155.864 177.434 1.00 50.64  ? 4194 LEU A CD1   1 
ATOM   20213 C  CD2   . LEU A 1 4194 ? 193.662 155.166 175.074 1.00 60.40  ? 4194 LEU A CD2   1 
ATOM   20214 N  N     . ARG A 1 4195 ? 192.962 150.653 178.333 1.00 65.54  ? 4195 ARG A N     1 
ATOM   20215 C  CA    . ARG A 1 4195 ? 191.904 149.654 178.440 1.00 63.78  ? 4195 ARG A CA    1 
ATOM   20216 C  C     . ARG A 1 4195 ? 191.269 149.670 179.825 1.00 65.21  ? 4195 ARG A C     1 
ATOM   20217 O  O     . ARG A 1 4195 ? 190.044 149.565 179.954 1.00 70.96  ? 4195 ARG A O     1 
ATOM   20218 C  CB    . ARG A 1 4195 ? 192.465 148.270 178.120 1.00 60.06  ? 4195 ARG A CB    1 
ATOM   20219 C  CG    . ARG A 1 4195 ? 191.415 147.238 177.762 1.00 71.38  ? 4195 ARG A CG    1 
ATOM   20220 C  CD    . ARG A 1 4195 ? 192.043 146.064 177.031 1.00 72.56  ? 4195 ARG A CD    1 
ATOM   20221 N  NE    . ARG A 1 4195 ? 193.090 146.494 176.113 1.00 70.89  ? 4195 ARG A NE    1 
ATOM   20222 C  CZ    . ARG A 1 4195 ? 192.873 146.979 174.898 1.00 72.90  ? 4195 ARG A CZ    1 
ATOM   20223 N  NH1   . ARG A 1 4195 ? 191.648 147.115 174.417 1.00 68.16  ? 4195 ARG A NH1   1 
ATOM   20224 N  NH2   . ARG A 1 4195 ? 193.910 147.338 174.147 1.00 71.97  ? 4195 ARG A NH2   1 
ATOM   20225 N  N     . TYR A 1 4196 ? 192.086 149.798 180.868 1.00 66.26  ? 4196 TYR A N     1 
ATOM   20226 C  CA    . TYR A 1 4196 ? 191.602 149.916 182.242 1.00 68.30  ? 4196 TYR A CA    1 
ATOM   20227 C  C     . TYR A 1 4196 ? 191.425 151.401 182.529 1.00 67.53  ? 4196 TYR A C     1 
ATOM   20228 O  O     . TYR A 1 4196 ? 192.321 152.072 183.043 1.00 68.36  ? 4196 TYR A O     1 
ATOM   20229 C  CB    . TYR A 1 4196 ? 192.571 149.247 183.207 1.00 58.55  ? 4196 TYR A CB    1 
ATOM   20230 C  CG    . TYR A 1 4196 ? 193.256 148.040 182.607 1.00 64.47  ? 4196 TYR A CG    1 
ATOM   20231 C  CD1   . TYR A 1 4196 ? 192.631 146.802 182.590 1.00 73.61  ? 4196 TYR A CD1   1 
ATOM   20232 C  CD2   . TYR A 1 4196 ? 194.519 148.142 182.045 1.00 68.43  ? 4196 TYR A CD2   1 
ATOM   20233 C  CE1   . TYR A 1 4196 ? 193.250 145.698 182.037 1.00 74.25  ? 4196 TYR A CE1   1 
ATOM   20234 C  CE2   . TYR A 1 4196 ? 195.144 147.044 181.490 1.00 69.85  ? 4196 TYR A CE2   1 
ATOM   20235 C  CZ    . TYR A 1 4196 ? 194.506 145.826 181.488 1.00 70.10  ? 4196 TYR A CZ    1 
ATOM   20236 O  OH    . TYR A 1 4196 ? 195.128 144.730 180.936 1.00 74.73  ? 4196 TYR A OH    1 
ATOM   20237 N  N     . ALA A 1 4197 ? 190.243 151.915 182.188 1.00 70.29  ? 4197 ALA A N     1 
ATOM   20238 C  CA    . ALA A 1 4197 ? 190.023 153.360 182.170 1.00 71.44  ? 4197 ALA A CA    1 
ATOM   20239 C  C     . ALA A 1 4197 ? 190.213 154.037 183.522 1.00 83.34  ? 4197 ALA A C     1 
ATOM   20240 O  O     . ALA A 1 4197 ? 190.905 155.067 183.573 1.00 86.78  ? 4197 ALA A O     1 
ATOM   20241 C  CB    . ALA A 1 4197 ? 188.634 153.655 181.595 1.00 74.26  ? 4197 ALA A CB    1 
ATOM   20242 N  N     . PRO A 1 4198 ? 189.643 153.549 184.641 1.00 85.24  ? 4198 PRO A N     1 
ATOM   20243 C  CA    . PRO A 1 4198 ? 189.754 154.315 185.892 1.00 78.19  ? 4198 PRO A CA    1 
ATOM   20244 C  C     . PRO A 1 4198 ? 191.131 154.243 186.534 1.00 78.97  ? 4198 PRO A C     1 
ATOM   20245 O  O     . PRO A 1 4198 ? 191.560 155.198 187.189 1.00 82.19  ? 4198 PRO A O     1 
ATOM   20246 C  CB    . PRO A 1 4198 ? 188.687 153.677 186.796 1.00 76.51  ? 4198 PRO A CB    1 
ATOM   20247 C  CG    . PRO A 1 4198 ? 187.870 152.791 185.900 1.00 79.11  ? 4198 PRO A CG    1 
ATOM   20248 C  CD    . PRO A 1 4198 ? 188.801 152.357 184.827 1.00 76.88  ? 4198 PRO A CD    1 
ATOM   20249 N  N     . LEU A 1 4199 ? 191.833 153.123 186.362 1.00 69.70  ? 4199 LEU A N     1 
ATOM   20250 C  CA    . LEU A 1 4199 ? 193.131 152.919 186.994 1.00 62.83  ? 4199 LEU A CA    1 
ATOM   20251 C  C     . LEU A 1 4199 ? 194.296 153.290 186.085 1.00 64.54  ? 4199 LEU A C     1 
ATOM   20252 O  O     . LEU A 1 4199 ? 195.208 154.004 186.512 1.00 72.48  ? 4199 LEU A O     1 
ATOM   20253 C  CB    . LEU A 1 4199 ? 193.277 151.463 187.452 1.00 60.00  ? 4199 LEU A CB    1 
ATOM   20254 C  CG    . LEU A 1 4199 ? 192.674 151.097 188.808 1.00 64.80  ? 4199 LEU A CG    1 
ATOM   20255 C  CD1   . LEU A 1 4199 ? 191.159 150.998 188.727 1.00 74.39  ? 4199 LEU A CD1   1 
ATOM   20256 C  CD2   . LEU A 1 4199 ? 193.272 149.799 189.322 1.00 66.66  ? 4199 LEU A CD2   1 
ATOM   20257 N  N     . GLY A 1 4200 ? 194.290 152.808 184.842 1.00 63.94  ? 4200 GLY A N     1 
ATOM   20258 C  CA    . GLY A 1 4200 ? 195.383 153.120 183.936 1.00 67.50  ? 4200 GLY A CA    1 
ATOM   20259 C  C     . GLY A 1 4200 ? 195.514 154.606 183.672 1.00 68.05  ? 4200 GLY A C     1 
ATOM   20260 O  O     . GLY A 1 4200 ? 196.624 155.136 183.578 1.00 76.71  ? 4200 GLY A O     1 
ATOM   20261 N  N     . TRP A 1 4201 ? 194.386 155.297 183.549 1.00 52.59  ? 4201 TRP A N     1 
ATOM   20262 C  CA    . TRP A 1 4201 ? 194.357 156.738 183.354 1.00 62.14  ? 4201 TRP A CA    1 
ATOM   20263 C  C     . TRP A 1 4201 ? 193.158 157.287 184.117 1.00 69.67  ? 4201 TRP A C     1 
ATOM   20264 O  O     . TRP A 1 4201 ? 192.592 156.619 184.987 1.00 74.65  ? 4201 TRP A O     1 
ATOM   20265 C  CB    . TRP A 1 4201 ? 194.318 157.083 181.860 1.00 54.19  ? 4201 TRP A CB    1 
ATOM   20266 C  CG    . TRP A 1 4201 ? 195.626 156.861 181.171 1.00 56.23  ? 4201 TRP A CG    1 
ATOM   20267 C  CD1   . TRP A 1 4201 ? 195.934 155.858 180.302 1.00 60.91  ? 4201 TRP A CD1   1 
ATOM   20268 C  CD2   . TRP A 1 4201 ? 196.805 157.662 181.294 1.00 56.67  ? 4201 TRP A CD2   1 
ATOM   20269 N  NE1   . TRP A 1 4201 ? 197.233 155.984 179.875 1.00 62.09  ? 4201 TRP A NE1   1 
ATOM   20270 C  CE2   . TRP A 1 4201 ? 197.789 157.085 180.471 1.00 56.97  ? 4201 TRP A CE2   1 
ATOM   20271 C  CE3   . TRP A 1 4201 ? 197.124 158.812 182.021 1.00 66.21  ? 4201 TRP A CE3   1 
ATOM   20272 C  CZ2   . TRP A 1 4201 ? 199.068 157.617 180.354 1.00 56.84  ? 4201 TRP A CZ2   1 
ATOM   20273 C  CZ3   . TRP A 1 4201 ? 198.394 159.338 181.903 1.00 71.37  ? 4201 TRP A CZ3   1 
ATOM   20274 C  CH2   . TRP A 1 4201 ? 199.351 158.742 181.076 1.00 64.14  ? 4201 TRP A CH2   1 
ATOM   20275 N  N     . SER A 1 4202 ? 192.781 158.527 183.814 1.00 62.72  ? 4202 SER A N     1 
ATOM   20276 C  CA    . SER A 1 4202 ? 191.560 159.096 184.365 1.00 59.05  ? 4202 SER A CA    1 
ATOM   20277 C  C     . SER A 1 4202 ? 190.435 159.180 183.346 1.00 65.09  ? 4202 SER A C     1 
ATOM   20278 O  O     . SER A 1 4202 ? 189.274 159.331 183.740 1.00 77.78  ? 4202 SER A O     1 
ATOM   20279 C  CB    . SER A 1 4202 ? 191.830 160.493 184.933 1.00 67.58  ? 4202 SER A CB    1 
ATOM   20280 O  OG    . SER A 1 4202 ? 192.594 160.416 186.123 1.00 76.08  ? 4202 SER A OG    1 
ATOM   20281 N  N     . LYS A 1 4203 ? 190.750 159.081 182.057 1.00 67.57  ? 4203 LYS A N     1 
ATOM   20282 C  CA    . LYS A 1 4203 ? 189.747 159.120 181.005 1.00 69.57  ? 4203 LYS A CA    1 
ATOM   20283 C  C     . LYS A 1 4203 ? 190.334 158.486 179.753 1.00 69.22  ? 4203 LYS A C     1 
ATOM   20284 O  O     . LYS A 1 4203 ? 191.541 158.249 179.658 1.00 76.34  ? 4203 LYS A O     1 
ATOM   20285 C  CB    . LYS A 1 4203 ? 189.276 160.551 180.728 1.00 70.31  ? 4203 LYS A CB    1 
ATOM   20286 C  CG    . LYS A 1 4203 ? 190.404 161.543 180.517 1.00 67.90  ? 4203 LYS A CG    1 
ATOM   20287 C  CD    . LYS A 1 4203 ? 189.867 162.917 180.156 1.00 71.42  ? 4203 LYS A CD    1 
ATOM   20288 C  CE    . LYS A 1 4203 ? 189.168 163.564 181.339 1.00 72.53  ? 4203 LYS A CE    1 
ATOM   20289 N  NZ    . LYS A 1 4203 ? 190.116 163.871 182.445 1.00 72.35  ? 4203 LYS A NZ    1 
ATOM   20290 N  N     . LYS A 1 4204 ? 189.461 158.207 178.786 1.00 68.11  ? 4204 LYS A N     1 
ATOM   20291 C  CA    . LYS A 1 4204 ? 189.872 157.592 177.526 1.00 71.12  ? 4204 LYS A CA    1 
ATOM   20292 C  C     . LYS A 1 4204 ? 190.501 158.664 176.640 1.00 74.30  ? 4204 LYS A C     1 
ATOM   20293 O  O     . LYS A 1 4204 ? 189.853 159.286 175.794 1.00 77.56  ? 4204 LYS A O     1 
ATOM   20294 C  CB    . LYS A 1 4204 ? 188.687 156.920 176.843 1.00 74.87  ? 4204 LYS A CB    1 
ATOM   20295 C  CG    . LYS A 1 4204 ? 188.356 155.539 177.383 1.00 75.68  ? 4204 LYS A CG    1 
ATOM   20296 C  CD    . LYS A 1 4204 ? 189.343 154.500 176.876 1.00 74.75  ? 4204 LYS A CD    1 
ATOM   20297 C  CE    . LYS A 1 4204 ? 188.711 153.120 176.803 1.00 75.28  ? 4204 LYS A CE    1 
ATOM   20298 N  NZ    . LYS A 1 4204 ? 188.261 152.643 178.138 1.00 73.28  ? 4204 LYS A NZ    1 
ATOM   20299 N  N     . TYR A 1 4205 ? 191.796 158.881 176.848 1.00 64.39  ? 4205 TYR A N     1 
ATOM   20300 C  CA    . TYR A 1 4205 ? 192.542 159.805 176.006 1.00 60.62  ? 4205 TYR A CA    1 
ATOM   20301 C  C     . TYR A 1 4205 ? 192.680 159.243 174.597 1.00 68.93  ? 4205 TYR A C     1 
ATOM   20302 O  O     . TYR A 1 4205 ? 192.605 158.033 174.376 1.00 76.90  ? 4205 TYR A O     1 
ATOM   20303 C  CB    . TYR A 1 4205 ? 193.925 160.073 176.593 1.00 59.06  ? 4205 TYR A CB    1 
ATOM   20304 C  CG    . TYR A 1 4205 ? 193.909 160.812 177.907 1.00 61.64  ? 4205 TYR A CG    1 
ATOM   20305 C  CD1   . TYR A 1 4205 ? 193.508 162.138 177.975 1.00 67.15  ? 4205 TYR A CD1   1 
ATOM   20306 C  CD2   . TYR A 1 4205 ? 194.298 160.186 179.081 1.00 63.78  ? 4205 TYR A CD2   1 
ATOM   20307 C  CE1   . TYR A 1 4205 ? 193.494 162.817 179.174 1.00 65.38  ? 4205 TYR A CE1   1 
ATOM   20308 C  CE2   . TYR A 1 4205 ? 194.287 160.857 180.284 1.00 65.15  ? 4205 TYR A CE2   1 
ATOM   20309 C  CZ    . TYR A 1 4205 ? 193.885 162.172 180.325 1.00 68.33  ? 4205 TYR A CZ    1 
ATOM   20310 O  OH    . TYR A 1 4205 ? 193.872 162.844 181.524 1.00 76.83  ? 4205 TYR A OH    1 
ATOM   20311 N  N     . GLU A 1 4206 ? 192.875 160.137 173.636 1.00 73.01  ? 4206 GLU A N     1 
ATOM   20312 C  CA    . GLU A 1 4206 ? 193.017 159.729 172.240 1.00 69.21  ? 4206 GLU A CA    1 
ATOM   20313 C  C     . GLU A 1 4206 ? 194.481 159.538 171.854 1.00 70.41  ? 4206 GLU A C     1 
ATOM   20314 O  O     . GLU A 1 4206 ? 194.974 160.127 170.894 1.00 77.66  ? 4206 GLU A O     1 
ATOM   20315 C  CB    . GLU A 1 4206 ? 192.338 160.747 171.332 1.00 74.23  ? 4206 GLU A CB    1 
ATOM   20316 C  CG    . GLU A 1 4206 ? 190.864 160.960 171.641 1.00 73.30  ? 4206 GLU A CG    1 
ATOM   20317 C  CD    . GLU A 1 4206 ? 190.027 159.720 171.394 1.00 77.45  ? 4206 GLU A CD    1 
ATOM   20318 O  OE1   . GLU A 1 4206 ? 190.451 158.863 170.592 1.00 81.46  ? 4206 GLU A OE1   1 
ATOM   20319 O  OE2   . GLU A 1 4206 ? 188.942 159.603 172.001 1.00 80.68  ? 4206 GLU A OE2   1 
ATOM   20320 N  N     . PHE A 1 4207 ? 195.191 158.703 172.610 1.00 57.32  ? 4207 PHE A N     1 
ATOM   20321 C  CA    . PHE A 1 4207 ? 196.579 158.382 172.296 1.00 54.77  ? 4207 PHE A CA    1 
ATOM   20322 C  C     . PHE A 1 4207 ? 196.613 157.472 171.075 1.00 68.40  ? 4207 PHE A C     1 
ATOM   20323 O  O     . PHE A 1 4207 ? 196.398 156.261 171.188 1.00 72.34  ? 4207 PHE A O     1 
ATOM   20324 C  CB    . PHE A 1 4207 ? 197.252 157.717 173.492 1.00 53.31  ? 4207 PHE A CB    1 
ATOM   20325 C  CG    . PHE A 1 4207 ? 197.427 158.627 174.674 1.00 56.56  ? 4207 PHE A CG    1 
ATOM   20326 C  CD1   . PHE A 1 4207 ? 197.975 159.888 174.521 1.00 64.59  ? 4207 PHE A CD1   1 
ATOM   20327 C  CD2   . PHE A 1 4207 ? 197.041 158.222 175.939 1.00 61.38  ? 4207 PHE A CD2   1 
ATOM   20328 C  CE1   . PHE A 1 4207 ? 198.138 160.724 175.607 1.00 59.72  ? 4207 PHE A CE1   1 
ATOM   20329 C  CE2   . PHE A 1 4207 ? 197.206 159.052 177.029 1.00 59.11  ? 4207 PHE A CE2   1 
ATOM   20330 C  CZ    . PHE A 1 4207 ? 197.753 160.306 176.862 1.00 51.78  ? 4207 PHE A CZ    1 
ATOM   20331 N  N     . GLY A 1 4208 ? 196.884 158.048 169.907 1.00 69.58  ? 4208 GLY A N     1 
ATOM   20332 C  CA    . GLY A 1 4208 ? 196.800 157.298 168.669 1.00 68.45  ? 4208 GLY A CA    1 
ATOM   20333 C  C     . GLY A 1 4208 ? 198.060 157.302 167.829 1.00 64.38  ? 4208 GLY A C     1 
ATOM   20334 O  O     . GLY A 1 4208 ? 199.160 157.542 168.335 1.00 68.12  ? 4208 GLY A O     1 
ATOM   20335 N  N     . GLU A 1 4209 ? 197.902 157.028 166.532 1.00 70.04  ? 4209 GLU A N     1 
ATOM   20336 C  CA    . GLU A 1 4209 ? 199.051 156.941 165.638 1.00 63.61  ? 4209 GLU A CA    1 
ATOM   20337 C  C     . GLU A 1 4209 ? 199.669 158.308 165.371 1.00 65.29  ? 4209 GLU A C     1 
ATOM   20338 O  O     . GLU A 1 4209 ? 200.866 158.396 165.072 1.00 73.96  ? 4209 GLU A O     1 
ATOM   20339 C  CB    . GLU A 1 4209 ? 198.634 156.275 164.327 1.00 72.79  ? 4209 GLU A CB    1 
ATOM   20340 C  CG    . GLU A 1 4209 ? 199.757 155.566 163.592 1.00 78.66  ? 4209 GLU A CG    1 
ATOM   20341 C  CD    . GLU A 1 4209 ? 200.372 156.422 162.505 1.00 83.44  ? 4209 GLU A CD    1 
ATOM   20342 O  OE1   . GLU A 1 4209 ? 201.440 156.043 161.981 1.00 84.23  ? 4209 GLU A OE1   1 
ATOM   20343 O  OE2   . GLU A 1 4209 ? 199.784 157.471 162.171 1.00 80.53  ? 4209 GLU A OE2   1 
ATOM   20344 N  N     . SER A 1 4210 ? 198.877 159.378 165.465 1.00 63.97  ? 4210 SER A N     1 
ATOM   20345 C  CA    . SER A 1 4210 ? 199.417 160.718 165.256 1.00 64.46  ? 4210 SER A CA    1 
ATOM   20346 C  C     . SER A 1 4210 ? 200.466 161.057 166.307 1.00 70.80  ? 4210 SER A C     1 
ATOM   20347 O  O     . SER A 1 4210 ? 201.505 161.650 165.991 1.00 81.44  ? 4210 SER A O     1 
ATOM   20348 C  CB    . SER A 1 4210 ? 198.288 161.747 165.272 1.00 67.11  ? 4210 SER A CB    1 
ATOM   20349 O  OG    . SER A 1 4210 ? 197.591 161.720 166.504 1.00 71.81  ? 4210 SER A OG    1 
ATOM   20350 N  N     . ASP A 1 4211 ? 200.211 160.688 167.564 1.00 68.26  ? 4211 ASP A N     1 
ATOM   20351 C  CA    . ASP A 1 4211 ? 201.197 160.912 168.616 1.00 62.55  ? 4211 ASP A CA    1 
ATOM   20352 C  C     . ASP A 1 4211 ? 202.472 160.123 168.350 1.00 69.31  ? 4211 ASP A C     1 
ATOM   20353 O  O     . ASP A 1 4211 ? 203.579 160.628 168.567 1.00 78.97  ? 4211 ASP A O     1 
ATOM   20354 C  CB    . ASP A 1 4211 ? 200.608 160.539 169.975 1.00 63.06  ? 4211 ASP A CB    1 
ATOM   20355 C  CG    . ASP A 1 4211 ? 199.444 161.422 170.366 1.00 73.16  ? 4211 ASP A CG    1 
ATOM   20356 O  OD1   . ASP A 1 4211 ? 199.416 162.595 169.938 1.00 72.86  ? 4211 ASP A OD1   1 
ATOM   20357 O  OD2   . ASP A 1 4211 ? 198.555 160.945 171.101 1.00 76.99  ? 4211 ASP A OD2   1 
ATOM   20358 N  N     . LEU A 1 4212 ? 202.335 158.880 167.884 1.00 65.49  ? 4212 LEU A N     1 
ATOM   20359 C  CA    . LEU A 1 4212 ? 203.510 158.080 167.555 1.00 58.45  ? 4212 LEU A CA    1 
ATOM   20360 C  C     . LEU A 1 4212 ? 204.324 158.723 166.440 1.00 56.87  ? 4212 LEU A C     1 
ATOM   20361 O  O     . LEU A 1 4212 ? 205.556 158.793 166.522 1.00 69.05  ? 4212 LEU A O     1 
ATOM   20362 C  CB    . LEU A 1 4212 ? 203.083 156.667 167.158 1.00 61.03  ? 4212 LEU A CB    1 
ATOM   20363 C  CG    . LEU A 1 4212 ? 204.187 155.738 166.654 1.00 56.44  ? 4212 LEU A CG    1 
ATOM   20364 C  CD1   . LEU A 1 4212 ? 205.139 155.380 167.779 1.00 56.73  ? 4212 LEU A CD1   1 
ATOM   20365 C  CD2   . LEU A 1 4212 ? 203.585 154.489 166.032 1.00 65.23  ? 4212 LEU A CD2   1 
ATOM   20366 N  N     . ARG A 1 4213 ? 203.653 159.202 165.389 1.00 58.17  ? 4213 ARG A N     1 
ATOM   20367 C  CA    . ARG A 1 4213 ? 204.369 159.846 164.293 1.00 59.44  ? 4213 ARG A CA    1 
ATOM   20368 C  C     . ARG A 1 4213 ? 205.061 161.121 164.758 1.00 63.63  ? 4213 ARG A C     1 
ATOM   20369 O  O     . ARG A 1 4213 ? 206.207 161.387 164.377 1.00 75.22  ? 4213 ARG A O     1 
ATOM   20370 C  CB    . ARG A 1 4213 ? 203.415 160.146 163.138 1.00 64.88  ? 4213 ARG A CB    1 
ATOM   20371 C  CG    . ARG A 1 4213 ? 202.809 158.911 162.502 1.00 69.37  ? 4213 ARG A CG    1 
ATOM   20372 C  CD    . ARG A 1 4213 ? 202.326 159.193 161.088 1.00 72.20  ? 4213 ARG A CD    1 
ATOM   20373 N  NE    . ARG A 1 4213 ? 203.417 159.582 160.203 1.00 76.67  ? 4213 ARG A NE    1 
ATOM   20374 C  CZ    . ARG A 1 4213 ? 203.255 160.027 158.965 1.00 80.21  ? 4213 ARG A CZ    1 
ATOM   20375 N  NH1   . ARG A 1 4213 ? 202.053 160.154 158.428 1.00 80.81  ? 4213 ARG A NH1   1 
ATOM   20376 N  NH2   . ARG A 1 4213 ? 204.327 160.352 158.247 1.00 79.63  ? 4213 ARG A NH2   1 
ATOM   20377 N  N     . SER A 1 4214 ? 204.382 161.924 165.581 1.00 48.83  ? 4214 SER A N     1 
ATOM   20378 C  CA    . SER A 1 4214 ? 204.994 163.151 166.079 1.00 44.89  ? 4214 SER A CA    1 
ATOM   20379 C  C     . SER A 1 4214 ? 206.204 162.850 166.953 1.00 63.25  ? 4214 SER A C     1 
ATOM   20380 O  O     . SER A 1 4214 ? 207.233 163.528 166.857 1.00 73.05  ? 4214 SER A O     1 
ATOM   20381 C  CB    . SER A 1 4214 ? 203.965 163.976 166.849 1.00 53.47  ? 4214 SER A CB    1 
ATOM   20382 O  OG    . SER A 1 4214 ? 202.841 164.270 166.038 1.00 67.15  ? 4214 SER A OG    1 
ATOM   20383 N  N     . ALA A 1 4215 ? 206.100 161.834 167.813 1.00 63.81  ? 4215 ALA A N     1 
ATOM   20384 C  CA    . ALA A 1 4215 ? 207.230 161.461 168.657 1.00 53.72  ? 4215 ALA A CA    1 
ATOM   20385 C  C     . ALA A 1 4215 ? 208.400 160.957 167.822 1.00 53.96  ? 4215 ALA A C     1 
ATOM   20386 O  O     . ALA A 1 4215 ? 209.558 161.283 168.108 1.00 63.36  ? 4215 ALA A O     1 
ATOM   20387 C  CB    . ALA A 1 4215 ? 206.799 160.408 169.675 1.00 53.87  ? 4215 ALA A CB    1 
ATOM   20388 N  N     . CYS A 1 4216 ? 208.119 160.159 166.789 1.00 58.33  ? 4216 CYS A N     1 
ATOM   20389 C  CA    . CYS A 1 4216 ? 209.185 159.689 165.911 1.00 55.39  ? 4216 CYS A CA    1 
ATOM   20390 C  C     . CYS A 1 4216 ? 209.855 160.851 165.188 1.00 59.31  ? 4216 CYS A C     1 
ATOM   20391 O  O     . CYS A 1 4216 ? 211.084 160.880 165.048 1.00 69.38  ? 4216 CYS A O     1 
ATOM   20392 C  CB    . CYS A 1 4216 ? 208.631 158.679 164.907 1.00 60.22  ? 4216 CYS A CB    1 
ATOM   20393 S  SG    . CYS A 1 4216 ? 208.195 157.079 165.622 1.00 77.37  ? 4216 CYS A SG    1 
ATOM   20394 N  N     . ASP A 1 4217 ? 209.062 161.817 164.717 1.00 65.48  ? 4217 ASP A N     1 
ATOM   20395 C  CA    . ASP A 1 4217 ? 209.634 162.983 164.052 1.00 70.00  ? 4217 ASP A CA    1 
ATOM   20396 C  C     . ASP A 1 4217 ? 210.502 163.793 165.007 1.00 73.35  ? 4217 ASP A C     1 
ATOM   20397 O  O     . ASP A 1 4217 ? 211.576 164.271 164.626 1.00 79.25  ? 4217 ASP A O     1 
ATOM   20398 C  CB    . ASP A 1 4217 ? 208.522 163.854 163.468 1.00 71.65  ? 4217 ASP A CB    1 
ATOM   20399 C  CG    . ASP A 1 4217 ? 207.740 163.147 162.380 1.00 73.41  ? 4217 ASP A CG    1 
ATOM   20400 O  OD1   . ASP A 1 4217 ? 208.218 162.106 161.886 1.00 74.59  ? 4217 ASP A OD1   1 
ATOM   20401 O  OD2   . ASP A 1 4217 ? 206.649 163.634 162.017 1.00 74.69  ? 4217 ASP A OD2   1 
ATOM   20402 N  N     . THR A 1 4218 ? 210.048 163.962 166.251 1.00 61.69  ? 4218 THR A N     1 
ATOM   20403 C  CA    . THR A 1 4218 ? 210.847 164.676 167.243 1.00 60.58  ? 4218 THR A CA    1 
ATOM   20404 C  C     . THR A 1 4218 ? 212.158 163.951 167.520 1.00 65.66  ? 4218 THR A C     1 
ATOM   20405 O  O     . THR A 1 4218 ? 213.223 164.581 167.605 1.00 73.22  ? 4218 THR A O     1 
ATOM   20406 C  CB    . THR A 1 4218 ? 210.044 164.844 168.533 1.00 60.70  ? 4218 THR A CB    1 
ATOM   20407 O  OG1   . THR A 1 4218 ? 209.036 165.845 168.345 1.00 69.81  ? 4218 THR A OG1   1 
ATOM   20408 C  CG2   . THR A 1 4218 ? 210.949 165.247 169.684 1.00 63.98  ? 4218 THR A CG2   1 
ATOM   20409 N  N     . VAL A 1 4219 ? 212.100 162.625 167.656 1.00 63.51  ? 4219 VAL A N     1 
ATOM   20410 C  CA    . VAL A 1 4219 ? 213.310 161.842 167.894 1.00 52.88  ? 4219 VAL A CA    1 
ATOM   20411 C  C     . VAL A 1 4219 ? 214.279 162.006 166.731 1.00 56.25  ? 4219 VAL A C     1 
ATOM   20412 O  O     . VAL A 1 4219 ? 215.479 162.229 166.928 1.00 69.54  ? 4219 VAL A O     1 
ATOM   20413 C  CB    . VAL A 1 4219 ? 212.954 160.363 168.129 1.00 49.62  ? 4219 VAL A CB    1 
ATOM   20414 C  CG1   . VAL A 1 4219 ? 214.171 159.480 167.911 1.00 52.11  ? 4219 VAL A CG1   1 
ATOM   20415 C  CG2   . VAL A 1 4219 ? 212.395 160.168 169.527 1.00 55.09  ? 4219 VAL A CG2   1 
ATOM   20416 N  N     . ASP A 1 4220 ? 213.767 161.914 165.501 1.00 65.24  ? 4220 ASP A N     1 
ATOM   20417 C  CA    . ASP A 1 4220 ? 214.617 162.086 164.327 1.00 68.13  ? 4220 ASP A CA    1 
ATOM   20418 C  C     . ASP A 1 4220 ? 215.263 163.464 164.314 1.00 72.83  ? 4220 ASP A C     1 
ATOM   20419 O  O     . ASP A 1 4220 ? 216.475 163.593 164.104 1.00 78.61  ? 4220 ASP A O     1 
ATOM   20420 C  CB    . ASP A 1 4220 ? 213.802 161.874 163.051 1.00 71.68  ? 4220 ASP A CB    1 
ATOM   20421 C  CG    . ASP A 1 4220 ? 213.495 160.419 162.792 1.00 82.46  ? 4220 ASP A CG    1 
ATOM   20422 O  OD1   . ASP A 1 4220 ? 213.542 159.623 163.751 1.00 86.75  ? 4220 ASP A OD1   1 
ATOM   20423 O  OD2   . ASP A 1 4220 ? 213.203 160.070 161.629 1.00 84.20  ? 4220 ASP A OD2   1 
ATOM   20424 N  N     . THR A 1 4221 ? 214.464 164.508 164.543 1.00 63.49  ? 4221 THR A N     1 
ATOM   20425 C  CA    . THR A 1 4221 ? 214.978 165.870 164.467 1.00 59.84  ? 4221 THR A CA    1 
ATOM   20426 C  C     . THR A 1 4221 ? 216.067 166.105 165.503 1.00 59.69  ? 4221 THR A C     1 
ATOM   20427 O  O     . THR A 1 4221 ? 217.139 166.632 165.186 1.00 68.44  ? 4221 THR A O     1 
ATOM   20428 C  CB    . THR A 1 4221 ? 213.837 166.871 164.652 1.00 65.98  ? 4221 THR A CB    1 
ATOM   20429 O  OG1   . THR A 1 4221 ? 212.890 166.721 163.587 1.00 69.58  ? 4221 THR A OG1   1 
ATOM   20430 C  CG2   . THR A 1 4221 ? 214.373 168.293 164.648 1.00 68.38  ? 4221 THR A CG2   1 
ATOM   20431 N  N     . TRP A 1 4222 ? 215.824 165.692 166.748 1.00 64.22  ? 4222 TRP A N     1 
ATOM   20432 C  CA    . TRP A 1 4222 ? 216.804 165.970 167.790 1.00 64.72  ? 4222 TRP A CA    1 
ATOM   20433 C  C     . TRP A 1 4222 ? 218.026 165.065 167.697 1.00 68.44  ? 4222 TRP A C     1 
ATOM   20434 O  O     . TRP A 1 4222 ? 219.128 165.490 168.063 1.00 76.16  ? 4222 TRP A O     1 
ATOM   20435 C  CB    . TRP A 1 4222 ? 216.148 165.871 169.166 1.00 62.41  ? 4222 TRP A CB    1 
ATOM   20436 C  CG    . TRP A 1 4222 ? 215.284 167.057 169.439 1.00 63.84  ? 4222 TRP A CG    1 
ATOM   20437 C  CD1   . TRP A 1 4222 ? 213.938 167.148 169.259 1.00 65.22  ? 4222 TRP A CD1   1 
ATOM   20438 C  CD2   . TRP A 1 4222 ? 215.716 168.341 169.904 1.00 68.47  ? 4222 TRP A CD2   1 
ATOM   20439 N  NE1   . TRP A 1 4222 ? 213.500 168.404 169.599 1.00 62.06  ? 4222 TRP A NE1   1 
ATOM   20440 C  CE2   . TRP A 1 4222 ? 214.572 169.155 169.999 1.00 66.01  ? 4222 TRP A CE2   1 
ATOM   20441 C  CE3   . TRP A 1 4222 ? 216.957 168.878 170.257 1.00 70.69  ? 4222 TRP A CE3   1 
ATOM   20442 C  CZ2   . TRP A 1 4222 ? 214.632 170.476 170.432 1.00 68.65  ? 4222 TRP A CZ2   1 
ATOM   20443 C  CZ3   . TRP A 1 4222 ? 217.014 170.189 170.687 1.00 68.52  ? 4222 TRP A CZ3   1 
ATOM   20444 C  CH2   . TRP A 1 4222 ? 215.859 170.973 170.771 1.00 70.11  ? 4222 TRP A CH2   1 
ATOM   20445 N  N     . LEU A 1 4223 ? 217.873 163.838 167.194 1.00 67.37  ? 4223 LEU A N     1 
ATOM   20446 C  CA    . LEU A 1 4223 ? 219.041 162.992 166.982 1.00 62.85  ? 4223 LEU A CA    1 
ATOM   20447 C  C     . LEU A 1 4223 ? 219.906 163.525 165.848 1.00 69.70  ? 4223 LEU A C     1 
ATOM   20448 O  O     . LEU A 1 4223 ? 221.138 163.480 165.929 1.00 75.47  ? 4223 LEU A O     1 
ATOM   20449 C  CB    . LEU A 1 4223 ? 218.607 161.555 166.704 1.00 62.37  ? 4223 LEU A CB    1 
ATOM   20450 C  CG    . LEU A 1 4223 ? 219.567 160.476 167.201 1.00 65.14  ? 4223 LEU A CG    1 
ATOM   20451 C  CD1   . LEU A 1 4223 ? 219.972 160.746 168.639 1.00 69.64  ? 4223 LEU A CD1   1 
ATOM   20452 C  CD2   . LEU A 1 4223 ? 218.930 159.109 167.076 1.00 65.44  ? 4223 LEU A CD2   1 
ATOM   20453 N  N     . ASP A 1 4224 ? 219.282 164.034 164.782 1.00 80.65  ? 4224 ASP A N     1 
ATOM   20454 C  CA    . ASP A 1 4224 ? 220.058 164.643 163.707 1.00 80.58  ? 4224 ASP A CA    1 
ATOM   20455 C  C     . ASP A 1 4224 ? 220.707 165.945 164.155 1.00 80.31  ? 4224 ASP A C     1 
ATOM   20456 O  O     . ASP A 1 4224 ? 221.809 166.273 163.701 1.00 80.37  ? 4224 ASP A O     1 
ATOM   20457 C  CB    . ASP A 1 4224 ? 219.172 164.881 162.485 1.00 81.84  ? 4224 ASP A CB    1 
ATOM   20458 C  CG    . ASP A 1 4224 ? 218.613 163.594 161.911 1.00 88.38  ? 4224 ASP A CG    1 
ATOM   20459 O  OD1   . ASP A 1 4224 ? 218.945 162.512 162.441 1.00 89.69  ? 4224 ASP A OD1   1 
ATOM   20460 O  OD2   . ASP A 1 4224 ? 217.843 163.663 160.931 1.00 87.41  ? 4224 ASP A OD2   1 
ATOM   20461 N  N     . ASP A 1 4225 ? 220.043 166.702 165.030 1.00 85.48  ? 4225 ASP A N     1 
ATOM   20462 C  CA    . ASP A 1 4225 ? 220.644 167.924 165.552 1.00 84.34  ? 4225 ASP A CA    1 
ATOM   20463 C  C     . ASP A 1 4225 ? 221.847 167.613 166.435 1.00 82.77  ? 4225 ASP A C     1 
ATOM   20464 O  O     . ASP A 1 4225 ? 222.905 168.240 166.303 1.00 89.91  ? 4225 ASP A O     1 
ATOM   20465 C  CB    . ASP A 1 4225 ? 219.602 168.732 166.326 1.00 88.97  ? 4225 ASP A CB    1 
ATOM   20466 C  CG    . ASP A 1 4225 ? 218.962 169.816 165.483 1.00 91.34  ? 4225 ASP A CG    1 
ATOM   20467 O  OD1   . ASP A 1 4225 ? 218.216 170.645 166.044 1.00 91.02  ? 4225 ASP A OD1   1 
ATOM   20468 O  OD2   . ASP A 1 4225 ? 219.204 169.839 164.258 1.00 88.97  ? 4225 ASP A OD2   1 
ATOM   20469 N  N     . THR A 1 4226 ? 221.705 166.646 167.345 1.00 75.58  ? 4226 THR A N     1 
ATOM   20470 C  CA    . THR A 1 4226 ? 222.806 166.322 168.247 1.00 78.72  ? 4226 THR A CA    1 
ATOM   20471 C  C     . THR A 1 4226 ? 223.925 165.585 167.522 1.00 86.28  ? 4226 THR A C     1 
ATOM   20472 O  O     . THR A 1 4226 ? 225.105 165.907 167.702 1.00 90.49  ? 4226 THR A O     1 
ATOM   20473 C  CB    . THR A 1 4226 ? 222.295 165.493 169.423 1.00 84.16  ? 4226 THR A CB    1 
ATOM   20474 O  OG1   . THR A 1 4226 ? 221.202 166.175 170.050 1.00 89.80  ? 4226 THR A OG1   1 
ATOM   20475 C  CG2   . THR A 1 4226 ? 223.403 165.282 170.441 1.00 81.36  ? 4226 THR A CG2   1 
ATOM   20476 N  N     . ALA A 1 4227 ? 223.581 164.596 166.701 1.00 93.69  ? 4227 ALA A N     1 
ATOM   20477 C  CA    . ALA A 1 4227 ? 224.561 163.805 165.966 1.00 90.67  ? 4227 ALA A CA    1 
ATOM   20478 C  C     . ALA A 1 4227 ? 224.650 164.345 164.544 1.00 93.81  ? 4227 ALA A C     1 
ATOM   20479 O  O     . ALA A 1 4227 ? 223.734 164.149 163.739 1.00 97.24  ? 4227 ALA A O     1 
ATOM   20480 C  CB    . ALA A 1 4227 ? 224.183 162.326 165.972 1.00 85.76  ? 4227 ALA A CB    1 
ATOM   20481 N  N     . LYS A 1 4228 ? 225.757 165.020 164.234 1.00 99.72  ? 4228 LYS A N     1 
ATOM   20482 C  CA    . LYS A 1 4228 ? 225.958 165.625 162.919 1.00 102.99 ? 4228 LYS A CA    1 
ATOM   20483 C  C     . LYS A 1 4228 ? 226.430 164.576 161.908 1.00 103.29 ? 4228 LYS A C     1 
ATOM   20484 O  O     . LYS A 1 4228 ? 227.521 164.648 161.343 1.00 104.50 ? 4228 LYS A O     1 
ATOM   20485 C  CB    . LYS A 1 4228 ? 226.946 166.781 163.020 1.00 104.68 ? 4228 LYS A CB    1 
ATOM   20486 C  CG    . LYS A 1 4228 ? 226.665 167.742 164.164 1.00 101.15 ? 4228 LYS A CG    1 
ATOM   20487 C  CD    . LYS A 1 4228 ? 225.297 168.388 164.025 1.00 100.99 ? 4228 LYS A CD    1 
ATOM   20488 C  CE    . LYS A 1 4228 ? 225.225 169.271 162.791 1.00 102.72 ? 4228 LYS A CE    1 
ATOM   20489 N  NZ    . LYS A 1 4228 ? 223.881 169.889 162.630 1.00 103.08 ? 4228 LYS A NZ    1 
ATOM   20490 N  N     . GLY A 1 4229 ? 225.572 163.583 161.686 1.00 107.10 ? 4229 GLY A N     1 
ATOM   20491 C  CA    . GLY A 1 4229 ? 225.862 162.531 160.736 1.00 107.42 ? 4229 GLY A CA    1 
ATOM   20492 C  C     . GLY A 1 4229 ? 226.831 161.476 161.216 1.00 107.44 ? 4229 GLY A C     1 
ATOM   20493 O  O     . GLY A 1 4229 ? 227.207 160.601 160.427 1.00 108.33 ? 4229 GLY A O     1 
ATOM   20494 N  N     . ARG A 1 4230 ? 227.248 161.528 162.477 1.00 102.81 ? 4230 ARG A N     1 
ATOM   20495 C  CA    . ARG A 1 4230 ? 228.191 160.549 162.997 1.00 104.13 ? 4230 ARG A CA    1 
ATOM   20496 C  C     . ARG A 1 4230 ? 227.552 159.167 163.069 1.00 104.79 ? 4230 ARG A C     1 
ATOM   20497 O  O     . ARG A 1 4230 ? 226.357 159.022 163.342 1.00 105.95 ? 4230 ARG A O     1 
ATOM   20498 C  CB    . ARG A 1 4230 ? 228.690 160.971 164.379 1.00 102.41 ? 4230 ARG A CB    1 
ATOM   20499 C  CG    . ARG A 1 4230 ? 229.227 162.392 164.432 1.00 101.21 ? 4230 ARG A CG    1 
ATOM   20500 C  CD    . ARG A 1 4230 ? 230.185 162.578 165.596 1.00 103.47 ? 4230 ARG A CD    1 
ATOM   20501 N  NE    . ARG A 1 4230 ? 229.481 162.741 166.862 1.00 109.09 ? 4230 ARG A NE    1 
ATOM   20502 C  CZ    . ARG A 1 4230 ? 229.103 163.908 167.365 1.00 107.61 ? 4230 ARG A CZ    1 
ATOM   20503 N  NH1   . ARG A 1 4230 ? 229.344 165.044 166.731 1.00 105.34 ? 4230 ARG A NH1   1 
ATOM   20504 N  NH2   . ARG A 1 4230 ? 228.466 163.936 168.532 1.00 103.23 ? 4230 ARG A NH2   1 
ATOM   20505 N  N     . GLN A 1 4231 ? 228.368 158.143 162.812 1.00 106.94 ? 4231 GLN A N     1 
ATOM   20506 C  CA    . GLN A 1 4231 ? 227.865 156.772 162.826 1.00 105.14 ? 4231 GLN A CA    1 
ATOM   20507 C  C     . GLN A 1 4231 ? 227.422 156.356 164.222 1.00 105.39 ? 4231 GLN A C     1 
ATOM   20508 O  O     . GLN A 1 4231 ? 226.410 155.663 164.377 1.00 106.52 ? 4231 GLN A O     1 
ATOM   20509 C  CB    . GLN A 1 4231 ? 228.934 155.816 162.296 1.00 106.61 ? 4231 GLN A CB    1 
ATOM   20510 C  CG    . GLN A 1 4231 ? 228.416 154.426 161.959 1.00 105.97 ? 4231 GLN A CG    1 
ATOM   20511 C  CD    . GLN A 1 4231 ? 227.711 154.373 160.617 1.00 106.58 ? 4231 GLN A CD    1 
ATOM   20512 O  OE1   . GLN A 1 4231 ? 226.616 154.909 160.455 1.00 104.23 ? 4231 GLN A OE1   1 
ATOM   20513 N  NE2   . GLN A 1 4231 ? 228.340 153.721 159.645 1.00 109.06 ? 4231 GLN A NE2   1 
ATOM   20514 N  N     . ASN A 1 4232 ? 228.163 156.763 165.249 1.00 101.89 ? 4232 ASN A N     1 
ATOM   20515 C  CA    . ASN A 1 4232 ? 227.851 156.406 166.625 1.00 102.68 ? 4232 ASN A CA    1 
ATOM   20516 C  C     . ASN A 1 4232 ? 227.854 157.654 167.494 1.00 102.08 ? 4232 ASN A C     1 
ATOM   20517 O  O     . ASN A 1 4232 ? 228.668 158.560 167.295 1.00 98.33  ? 4232 ASN A O     1 
ATOM   20518 C  CB    . ASN A 1 4232 ? 228.850 155.382 167.176 1.00 102.78 ? 4232 ASN A CB    1 
ATOM   20519 C  CG    . ASN A 1 4232 ? 228.853 154.090 166.386 1.00 104.85 ? 4232 ASN A CG    1 
ATOM   20520 O  OD1   . ASN A 1 4232 ? 229.390 154.026 165.281 1.00 107.60 ? 4232 ASN A OD1   1 
ATOM   20521 N  ND2   . ASN A 1 4232 ? 228.251 153.050 166.951 1.00 103.18 ? 4232 ASN A ND2   1 
ATOM   20522 N  N     . ILE A 1 4233 ? 226.937 157.691 168.457 1.00 94.10  ? 4233 ILE A N     1 
ATOM   20523 C  CA    . ILE A 1 4233 ? 226.808 158.798 169.396 1.00 90.28  ? 4233 ILE A CA    1 
ATOM   20524 C  C     . ILE A 1 4233 ? 226.758 158.217 170.801 1.00 89.58  ? 4233 ILE A C     1 
ATOM   20525 O  O     . ILE A 1 4233 ? 226.057 157.227 171.042 1.00 92.36  ? 4233 ILE A O     1 
ATOM   20526 C  CB    . ILE A 1 4233 ? 225.558 159.652 169.107 1.00 90.67  ? 4233 ILE A CB    1 
ATOM   20527 C  CG1   . ILE A 1 4233 ? 225.264 160.600 170.271 1.00 89.96  ? 4233 ILE A CG1   1 
ATOM   20528 C  CG2   . ILE A 1 4233 ? 224.356 158.765 168.814 1.00 91.29  ? 4233 ILE A CG2   1 
ATOM   20529 C  CD1   . ILE A 1 4233 ? 224.144 161.576 169.991 1.00 90.60  ? 4233 ILE A CD1   1 
ATOM   20530 N  N     . SER A 1 4234 ? 227.510 158.816 171.718 1.00 89.55  ? 4234 SER A N     1 
ATOM   20531 C  CA    . SER A 1 4234 ? 227.550 158.315 173.082 1.00 91.16  ? 4234 SER A CA    1 
ATOM   20532 C  C     . SER A 1 4234 ? 226.167 158.423 173.721 1.00 93.55  ? 4234 SER A C     1 
ATOM   20533 O  O     . SER A 1 4234 ? 225.458 159.414 173.503 1.00 94.77  ? 4234 SER A O     1 
ATOM   20534 C  CB    . SER A 1 4234 ? 228.573 159.094 173.910 1.00 91.82  ? 4234 SER A CB    1 
ATOM   20535 O  OG    . SER A 1 4234 ? 228.532 158.702 175.271 1.00 92.30  ? 4234 SER A OG    1 
ATOM   20536 N  N     . PRO A 1 4235 ? 225.746 157.423 174.500 1.00 91.76  ? 4235 PRO A N     1 
ATOM   20537 C  CA    . PRO A 1 4235 ? 224.428 157.504 175.153 1.00 88.81  ? 4235 PRO A CA    1 
ATOM   20538 C  C     . PRO A 1 4235 ? 224.287 158.690 176.087 1.00 92.93  ? 4235 PRO A C     1 
ATOM   20539 O  O     . PRO A 1 4235 ? 223.165 159.171 176.286 1.00 96.83  ? 4235 PRO A O     1 
ATOM   20540 C  CB    . PRO A 1 4235 ? 224.332 156.176 175.916 1.00 90.01  ? 4235 PRO A CB    1 
ATOM   20541 C  CG    . PRO A 1 4235 ? 225.294 155.266 175.223 1.00 91.45  ? 4235 PRO A CG    1 
ATOM   20542 C  CD    . PRO A 1 4235 ? 226.418 156.142 174.768 1.00 91.86  ? 4235 PRO A CD    1 
ATOM   20543 N  N     . ASP A 1 4236 ? 225.385 159.173 176.672 1.00 97.30  ? 4236 ASP A N     1 
ATOM   20544 C  CA    . ASP A 1 4236 ? 225.320 160.384 177.482 1.00 97.90  ? 4236 ASP A CA    1 
ATOM   20545 C  C     . ASP A 1 4236 ? 224.939 161.597 176.645 1.00 94.40  ? 4236 ASP A C     1 
ATOM   20546 O  O     . ASP A 1 4236 ? 224.201 162.469 177.118 1.00 93.12  ? 4236 ASP A O     1 
ATOM   20547 C  CB    . ASP A 1 4236 ? 226.661 160.625 178.175 1.00 100.34 ? 4236 ASP A CB    1 
ATOM   20548 C  CG    . ASP A 1 4236 ? 226.957 159.598 179.249 1.00 101.85 ? 4236 ASP A CG    1 
ATOM   20549 O  OD1   . ASP A 1 4236 ? 226.006 159.138 179.913 1.00 102.65 ? 4236 ASP A OD1   1 
ATOM   20550 O  OD2   . ASP A 1 4236 ? 228.143 159.249 179.427 1.00 101.86 ? 4236 ASP A OD2   1 
ATOM   20551 N  N     . LYS A 1 4237 ? 225.427 161.669 175.407 1.00 87.84  ? 4237 LYS A N     1 
ATOM   20552 C  CA    . LYS A 1 4237 ? 225.204 162.831 174.558 1.00 93.02  ? 4237 LYS A CA    1 
ATOM   20553 C  C     . LYS A 1 4237 ? 223.815 162.863 173.936 1.00 88.75  ? 4237 LYS A C     1 
ATOM   20554 O  O     . LYS A 1 4237 ? 223.441 163.891 173.361 1.00 91.46  ? 4237 LYS A O     1 
ATOM   20555 C  CB    . LYS A 1 4237 ? 226.260 162.878 173.451 1.00 96.22  ? 4237 LYS A CB    1 
ATOM   20556 C  CG    . LYS A 1 4237 ? 227.693 162.825 173.955 1.00 88.75  ? 4237 LYS A CG    1 
ATOM   20557 C  CD    . LYS A 1 4237 ? 228.101 164.127 174.623 1.00 90.37  ? 4237 LYS A CD    1 
ATOM   20558 C  CE    . LYS A 1 4237 ? 228.304 163.940 176.119 1.00 92.31  ? 4237 LYS A CE    1 
ATOM   20559 N  NZ    . LYS A 1 4237 ? 228.770 165.190 176.780 1.00 92.54  ? 4237 LYS A NZ    1 
ATOM   20560 N  N     . ILE A 1 4238 ? 223.054 161.781 174.025 1.00 78.54  ? 4238 ILE A N     1 
ATOM   20561 C  CA    . ILE A 1 4238 ? 221.703 161.767 173.452 1.00 83.03  ? 4238 ILE A CA    1 
ATOM   20562 C  C     . ILE A 1 4238 ? 220.829 162.764 174.207 1.00 85.18  ? 4238 ILE A C     1 
ATOM   20563 O  O     . ILE A 1 4238 ? 220.805 162.743 175.451 1.00 87.64  ? 4238 ILE A O     1 
ATOM   20564 C  CB    . ILE A 1 4238 ? 221.113 160.357 173.513 1.00 85.96  ? 4238 ILE A CB    1 
ATOM   20565 C  CG1   . ILE A 1 4238 ? 221.817 159.445 172.508 1.00 88.23  ? 4238 ILE A CG1   1 
ATOM   20566 C  CG2   . ILE A 1 4238 ? 219.620 160.385 173.238 1.00 81.52  ? 4238 ILE A CG2   1 
ATOM   20567 C  CD1   . ILE A 1 4238 ? 221.264 158.040 172.469 1.00 83.73  ? 4238 ILE A CD1   1 
ATOM   20568 N  N     . PRO A 1 4239 ? 220.104 163.648 173.518 1.00 75.61  ? 4239 PRO A N     1 
ATOM   20569 C  CA    . PRO A 1 4239 ? 219.303 164.658 174.224 1.00 72.76  ? 4239 PRO A CA    1 
ATOM   20570 C  C     . PRO A 1 4239 ? 218.095 164.062 174.927 1.00 75.61  ? 4239 PRO A C     1 
ATOM   20571 O  O     . PRO A 1 4239 ? 216.966 164.180 174.443 1.00 78.79  ? 4239 PRO A O     1 
ATOM   20572 C  CB    . PRO A 1 4239 ? 218.881 165.614 173.102 1.00 69.81  ? 4239 PRO A CB    1 
ATOM   20573 C  CG    . PRO A 1 4239 ? 218.897 164.773 171.874 1.00 76.33  ? 4239 PRO A CG    1 
ATOM   20574 C  CD    . PRO A 1 4239 ? 220.027 163.802 172.055 1.00 74.29  ? 4239 PRO A CD    1 
ATOM   20575 N  N     . TRP A 1 4240 ? 218.327 163.416 176.072 1.00 76.57  ? 4240 TRP A N     1 
ATOM   20576 C  CA    . TRP A 1 4240 ? 217.226 162.832 176.831 1.00 68.94  ? 4240 TRP A CA    1 
ATOM   20577 C  C     . TRP A 1 4240 ? 216.262 163.903 177.322 1.00 63.97  ? 4240 TRP A C     1 
ATOM   20578 O  O     . TRP A 1 4240 ? 215.040 163.710 177.293 1.00 69.93  ? 4240 TRP A O     1 
ATOM   20579 C  CB    . TRP A 1 4240 ? 217.771 162.028 178.009 1.00 69.89  ? 4240 TRP A CB    1 
ATOM   20580 C  CG    . TRP A 1 4240 ? 218.585 160.850 177.598 1.00 72.18  ? 4240 TRP A CG    1 
ATOM   20581 C  CD1   . TRP A 1 4240 ? 219.925 160.680 177.772 1.00 73.01  ? 4240 TRP A CD1   1 
ATOM   20582 C  CD2   . TRP A 1 4240 ? 218.111 159.668 176.946 1.00 72.27  ? 4240 TRP A CD2   1 
ATOM   20583 N  NE1   . TRP A 1 4240 ? 220.317 159.465 177.266 1.00 76.77  ? 4240 TRP A NE1   1 
ATOM   20584 C  CE2   . TRP A 1 4240 ? 219.221 158.825 176.753 1.00 73.62  ? 4240 TRP A CE2   1 
ATOM   20585 C  CE3   . TRP A 1 4240 ? 216.855 159.241 176.505 1.00 73.10  ? 4240 TRP A CE3   1 
ATOM   20586 C  CZ2   . TRP A 1 4240 ? 219.113 157.582 176.140 1.00 74.41  ? 4240 TRP A CZ2   1 
ATOM   20587 C  CZ3   . TRP A 1 4240 ? 216.751 158.007 175.896 1.00 69.65  ? 4240 TRP A CZ3   1 
ATOM   20588 C  CH2   . TRP A 1 4240 ? 217.873 157.191 175.720 1.00 70.10  ? 4240 TRP A CH2   1 
ATOM   20589 N  N     . SER A 1 4241 ? 216.794 165.036 177.786 1.00 64.12  ? 4241 SER A N     1 
ATOM   20590 C  CA    . SER A 1 4241 ? 215.941 166.098 178.308 1.00 67.00  ? 4241 SER A CA    1 
ATOM   20591 C  C     . SER A 1 4241 ? 214.995 166.623 177.238 1.00 67.78  ? 4241 SER A C     1 
ATOM   20592 O  O     . SER A 1 4241 ? 213.809 166.848 177.505 1.00 70.06  ? 4241 SER A O     1 
ATOM   20593 C  CB    . SER A 1 4241 ? 216.798 167.232 178.867 1.00 65.54  ? 4241 SER A CB    1 
ATOM   20594 O  OG    . SER A 1 4241 ? 217.728 166.746 179.819 1.00 72.55  ? 4241 SER A OG    1 
ATOM   20595 N  N     . ALA A 1 4242 ? 215.500 166.819 176.019 1.00 66.03  ? 4242 ALA A N     1 
ATOM   20596 C  CA    . ALA A 1 4242 ? 214.665 167.339 174.941 1.00 61.80  ? 4242 ALA A CA    1 
ATOM   20597 C  C     . ALA A 1 4242 ? 213.502 166.402 174.647 1.00 59.66  ? 4242 ALA A C     1 
ATOM   20598 O  O     . ALA A 1 4242 ? 212.341 166.829 174.602 1.00 64.66  ? 4242 ALA A O     1 
ATOM   20599 C  CB    . ALA A 1 4242 ? 215.509 167.559 173.686 1.00 66.21  ? 4242 ALA A CB    1 
ATOM   20600 N  N     . LEU A 1 4243 ? 213.795 165.115 174.450 1.00 63.09  ? 4243 LEU A N     1 
ATOM   20601 C  CA    . LEU A 1 4243 ? 212.744 164.154 174.135 1.00 63.18  ? 4243 LEU A CA    1 
ATOM   20602 C  C     . LEU A 1 4243 ? 211.744 164.040 175.278 1.00 68.34  ? 4243 LEU A C     1 
ATOM   20603 O  O     . LEU A 1 4243 ? 210.527 164.037 175.055 1.00 68.67  ? 4243 LEU A O     1 
ATOM   20604 C  CB    . LEU A 1 4243 ? 213.357 162.790 173.817 1.00 56.73  ? 4243 LEU A CB    1 
ATOM   20605 C  CG    . LEU A 1 4243 ? 214.525 162.770 172.831 1.00 56.94  ? 4243 LEU A CG    1 
ATOM   20606 C  CD1   . LEU A 1 4243 ? 215.046 161.356 172.653 1.00 62.90  ? 4243 LEU A CD1   1 
ATOM   20607 C  CD2   . LEU A 1 4243 ? 214.112 163.364 171.496 1.00 59.81  ? 4243 LEU A CD2   1 
ATOM   20608 N  N     . LYS A 1 4244 ? 212.240 163.954 176.515 1.00 65.63  ? 4244 LYS A N     1 
ATOM   20609 C  CA    . LYS A 1 4244 ? 211.341 163.814 177.655 1.00 55.16  ? 4244 LYS A CA    1 
ATOM   20610 C  C     . LYS A 1 4244 ? 210.419 165.019 177.776 1.00 58.76  ? 4244 LYS A C     1 
ATOM   20611 O  O     . LYS A 1 4244 ? 209.197 164.870 177.882 1.00 68.15  ? 4244 LYS A O     1 
ATOM   20612 C  CB    . LYS A 1 4244 ? 212.142 163.623 178.943 1.00 53.09  ? 4244 LYS A CB    1 
ATOM   20613 C  CG    . LYS A 1 4244 ? 212.564 162.190 179.207 1.00 59.88  ? 4244 LYS A CG    1 
ATOM   20614 C  CD    . LYS A 1 4244 ? 213.288 162.064 180.537 1.00 64.94  ? 4244 LYS A CD    1 
ATOM   20615 C  CE    . LYS A 1 4244 ? 214.613 162.804 180.525 1.00 66.28  ? 4244 LYS A CE    1 
ATOM   20616 N  NZ    . LYS A 1 4244 ? 215.435 162.475 181.722 1.00 61.91  ? 4244 LYS A NZ    1 
ATOM   20617 N  N     . THR A 1 4245 ? 210.986 166.228 177.737 1.00 60.83  ? 4245 THR A N     1 
ATOM   20618 C  CA    . THR A 1 4245 ? 210.173 167.429 177.887 1.00 62.60  ? 4245 THR A CA    1 
ATOM   20619 C  C     . THR A 1 4245 ? 209.174 167.572 176.747 1.00 60.73  ? 4245 THR A C     1 
ATOM   20620 O  O     . THR A 1 4245 ? 208.007 167.908 176.979 1.00 66.34  ? 4245 THR A O     1 
ATOM   20621 C  CB    . THR A 1 4245 ? 211.069 168.663 177.970 1.00 60.58  ? 4245 THR A CB    1 
ATOM   20622 O  OG1   . THR A 1 4245 ? 212.082 168.453 178.961 1.00 70.18  ? 4245 THR A OG1   1 
ATOM   20623 C  CG2   . THR A 1 4245 ? 210.251 169.887 178.341 1.00 63.66  ? 4245 THR A CG2   1 
ATOM   20624 N  N     . LEU A 1 4246 ? 209.603 167.313 175.508 1.00 55.90  ? 4246 LEU A N     1 
ATOM   20625 C  CA    . LEU A 1 4246 ? 208.682 167.461 174.389 1.00 49.45  ? 4246 LEU A CA    1 
ATOM   20626 C  C     . LEU A 1 4246 ? 207.548 166.448 174.448 1.00 55.28  ? 4246 LEU A C     1 
ATOM   20627 O  O     . LEU A 1 4246 ? 206.380 166.831 174.335 1.00 67.24  ? 4246 LEU A O     1 
ATOM   20628 C  CB    . LEU A 1 4246 ? 209.435 167.349 173.065 1.00 52.21  ? 4246 LEU A CB    1 
ATOM   20629 C  CG    . LEU A 1 4246 ? 210.193 168.617 172.670 1.00 52.79  ? 4246 LEU A CG    1 
ATOM   20630 C  CD1   . LEU A 1 4246 ? 210.738 168.500 171.265 1.00 53.64  ? 4246 LEU A CD1   1 
ATOM   20631 C  CD2   . LEU A 1 4246 ? 209.300 169.837 172.796 1.00 59.83  ? 4246 LEU A CD2   1 
ATOM   20632 N  N     . MET A 1 4247 ? 207.852 165.164 174.646 1.00 54.02  ? 4247 MET A N     1 
ATOM   20633 C  CA    . MET A 1 4247 ? 206.774 164.183 174.688 1.00 54.94  ? 4247 MET A CA    1 
ATOM   20634 C  C     . MET A 1 4247 ? 205.984 164.251 175.989 1.00 55.85  ? 4247 MET A C     1 
ATOM   20635 O  O     . MET A 1 4247 ? 204.947 163.592 176.110 1.00 59.79  ? 4247 MET A O     1 
ATOM   20636 C  CB    . MET A 1 4247 ? 207.324 162.773 174.462 1.00 43.96  ? 4247 MET A CB    1 
ATOM   20637 C  CG    . MET A 1 4247 ? 208.305 162.685 173.302 1.00 54.55  ? 4247 MET A CG    1 
ATOM   20638 S  SD    . MET A 1 4247 ? 209.068 161.066 173.090 1.00 75.93  ? 4247 MET A SD    1 
ATOM   20639 C  CE    . MET A 1 4247 ? 208.103 160.076 174.224 1.00 60.18  ? 4247 MET A CE    1 
ATOM   20640 N  N     . ALA A 1 4248 ? 206.448 165.031 176.968 1.00 58.21  ? 4248 ALA A N     1 
ATOM   20641 C  CA    . ALA A 1 4248 ? 205.653 165.240 178.170 1.00 48.74  ? 4248 ALA A CA    1 
ATOM   20642 C  C     . ALA A 1 4248 ? 204.768 166.475 178.075 1.00 60.63  ? 4248 ALA A C     1 
ATOM   20643 O  O     . ALA A 1 4248 ? 203.741 166.546 178.757 1.00 70.49  ? 4248 ALA A O     1 
ATOM   20644 C  CB    . ALA A 1 4248 ? 206.565 165.355 179.392 1.00 49.55  ? 4248 ALA A CB    1 
ATOM   20645 N  N     . GLN A 1 4249 ? 205.141 167.455 177.251 1.00 69.45  ? 4249 GLN A N     1 
ATOM   20646 C  CA    . GLN A 1 4249 ? 204.435 168.729 177.240 1.00 62.00  ? 4249 GLN A CA    1 
ATOM   20647 C  C     . GLN A 1 4249 ? 203.659 169.021 175.964 1.00 63.26  ? 4249 GLN A C     1 
ATOM   20648 O  O     . GLN A 1 4249 ? 202.653 169.729 176.030 1.00 68.19  ? 4249 GLN A O     1 
ATOM   20649 C  CB    . GLN A 1 4249 ? 205.420 169.879 177.488 1.00 61.45  ? 4249 GLN A CB    1 
ATOM   20650 C  CG    . GLN A 1 4249 ? 205.683 170.150 178.959 1.00 62.94  ? 4249 GLN A CG    1 
ATOM   20651 C  CD    . GLN A 1 4249 ? 206.784 171.166 179.178 1.00 70.10  ? 4249 GLN A CD    1 
ATOM   20652 O  OE1   . GLN A 1 4249 ? 206.993 172.059 178.358 1.00 69.82  ? 4249 GLN A OE1   1 
ATOM   20653 N  NE2   . GLN A 1 4249 ? 207.496 171.035 180.290 1.00 69.75  ? 4249 GLN A NE2   1 
ATOM   20654 N  N     . SER A 1 4250 ? 204.081 168.509 174.808 1.00 57.59  ? 4250 SER A N     1 
ATOM   20655 C  CA    . SER A 1 4250 ? 203.453 168.882 173.547 1.00 52.13  ? 4250 SER A CA    1 
ATOM   20656 C  C     . SER A 1 4250 ? 202.908 167.695 172.769 1.00 58.50  ? 4250 SER A C     1 
ATOM   20657 O  O     . SER A 1 4250 ? 201.826 167.797 172.179 1.00 62.86  ? 4250 SER A O     1 
ATOM   20658 C  CB    . SER A 1 4250 ? 204.455 169.658 172.679 1.00 55.75  ? 4250 SER A CB    1 
ATOM   20659 O  OG    . SER A 1 4250 ? 205.720 169.022 172.673 1.00 59.80  ? 4250 SER A OG    1 
ATOM   20660 N  N     . ILE A 1 4251 ? 203.621 166.570 172.741 1.00 55.89  ? 4251 ILE A N     1 
ATOM   20661 C  CA    . ILE A 1 4251 ? 203.209 165.453 171.895 1.00 52.18  ? 4251 ILE A CA    1 
ATOM   20662 C  C     . ILE A 1 4251 ? 202.178 164.585 172.606 1.00 56.13  ? 4251 ILE A C     1 
ATOM   20663 O  O     . ILE A 1 4251 ? 201.032 164.460 172.158 1.00 66.65  ? 4251 ILE A O     1 
ATOM   20664 C  CB    . ILE A 1 4251 ? 204.433 164.629 171.458 1.00 43.35  ? 4251 ILE A CB    1 
ATOM   20665 C  CG1   . ILE A 1 4251 ? 205.415 165.510 170.686 1.00 48.20  ? 4251 ILE A CG1   1 
ATOM   20666 C  CG2   . ILE A 1 4251 ? 204.002 163.452 170.606 1.00 44.77  ? 4251 ILE A CG2   1 
ATOM   20667 C  CD1   . ILE A 1 4251 ? 206.820 164.961 170.641 1.00 51.52  ? 4251 ILE A CD1   1 
ATOM   20668 N  N     . TYR A 1 4252 ? 202.566 163.976 173.725 1.00 57.99  ? 4252 TYR A N     1 
ATOM   20669 C  CA    . TYR A 1 4252 ? 201.644 163.142 174.485 1.00 51.36  ? 4252 TYR A CA    1 
ATOM   20670 C  C     . TYR A 1 4252 ? 200.937 163.906 175.593 1.00 61.40  ? 4252 TYR A C     1 
ATOM   20671 O  O     . TYR A 1 4252 ? 199.777 163.609 175.895 1.00 72.94  ? 4252 TYR A O     1 
ATOM   20672 C  CB    . TYR A 1 4252 ? 202.381 161.944 175.091 1.00 52.18  ? 4252 TYR A CB    1 
ATOM   20673 C  CG    . TYR A 1 4252 ? 202.636 160.818 174.119 1.00 53.01  ? 4252 TYR A CG    1 
ATOM   20674 C  CD1   . TYR A 1 4252 ? 201.648 159.888 173.832 1.00 49.75  ? 4252 TYR A CD1   1 
ATOM   20675 C  CD2   . TYR A 1 4252 ? 203.866 160.680 173.492 1.00 60.32  ? 4252 TYR A CD2   1 
ATOM   20676 C  CE1   . TYR A 1 4252 ? 201.876 158.856 172.947 1.00 53.14  ? 4252 TYR A CE1   1 
ATOM   20677 C  CE2   . TYR A 1 4252 ? 204.103 159.650 172.605 1.00 51.64  ? 4252 TYR A CE2   1 
ATOM   20678 C  CZ    . TYR A 1 4252 ? 203.104 158.742 172.336 1.00 56.69  ? 4252 TYR A CZ    1 
ATOM   20679 O  OH    . TYR A 1 4252 ? 203.334 157.714 171.453 1.00 67.75  ? 4252 TYR A OH    1 
ATOM   20680 N  N     . GLY A 1 4253 ? 201.607 164.880 176.205 1.00 62.18  ? 4253 GLY A N     1 
ATOM   20681 C  CA    . GLY A 1 4253 ? 201.002 165.643 177.278 1.00 62.16  ? 4253 GLY A CA    1 
ATOM   20682 C  C     . GLY A 1 4253 ? 199.991 166.676 176.842 1.00 61.02  ? 4253 GLY A C     1 
ATOM   20683 O  O     . GLY A 1 4253 ? 199.329 167.272 177.696 1.00 67.98  ? 4253 GLY A O     1 
ATOM   20684 N  N     . GLY A 1 4254 ? 199.860 166.908 175.535 1.00 57.36  ? 4254 GLY A N     1 
ATOM   20685 C  CA    . GLY A 1 4254 ? 198.865 167.855 175.063 1.00 60.88  ? 4254 GLY A CA    1 
ATOM   20686 C  C     . GLY A 1 4254 ? 197.448 167.404 175.354 1.00 62.42  ? 4254 GLY A C     1 
ATOM   20687 O  O     . GLY A 1 4254 ? 196.605 168.203 175.768 1.00 71.78  ? 4254 GLY A O     1 
ATOM   20688 N  N     . ARG A 1 4255 ? 197.165 166.117 175.146 1.00 61.06  ? 4255 ARG A N     1 
ATOM   20689 C  CA    . ARG A 1 4255 ? 195.831 165.594 175.408 1.00 63.19  ? 4255 ARG A CA    1 
ATOM   20690 C  C     . ARG A 1 4255 ? 195.557 165.420 176.895 1.00 64.89  ? 4255 ARG A C     1 
ATOM   20691 O  O     . ARG A 1 4255 ? 194.396 165.251 177.282 1.00 70.91  ? 4255 ARG A O     1 
ATOM   20692 C  CB    . ARG A 1 4255 ? 195.640 164.259 174.688 1.00 62.47  ? 4255 ARG A CB    1 
ATOM   20693 C  CG    . ARG A 1 4255 ? 196.326 164.181 173.336 1.00 63.30  ? 4255 ARG A CG    1 
ATOM   20694 C  CD    . ARG A 1 4255 ? 196.202 162.792 172.736 1.00 62.73  ? 4255 ARG A CD    1 
ATOM   20695 N  NE    . ARG A 1 4255 ? 196.590 162.766 171.331 1.00 65.69  ? 4255 ARG A NE    1 
ATOM   20696 C  CZ    . ARG A 1 4255 ? 195.808 163.152 170.332 1.00 65.89  ? 4255 ARG A CZ    1 
ATOM   20697 N  NH1   . ARG A 1 4255 ? 194.583 163.603 170.547 1.00 64.76  ? 4255 ARG A NH1   1 
ATOM   20698 N  NH2   . ARG A 1 4255 ? 196.265 163.081 169.086 1.00 65.05  ? 4255 ARG A NH2   1 
ATOM   20699 N  N     . VAL A 1 4256 ? 196.589 165.462 177.732 1.00 67.26  ? 4256 VAL A N     1 
ATOM   20700 C  CA    . VAL A 1 4256 ? 196.425 165.251 179.166 1.00 64.99  ? 4256 VAL A CA    1 
ATOM   20701 C  C     . VAL A 1 4256 ? 195.924 166.543 179.800 1.00 69.67  ? 4256 VAL A C     1 
ATOM   20702 O  O     . VAL A 1 4256 ? 196.564 167.593 179.684 1.00 68.86  ? 4256 VAL A O     1 
ATOM   20703 C  CB    . VAL A 1 4256 ? 197.740 164.792 179.811 1.00 63.77  ? 4256 VAL A CB    1 
ATOM   20704 C  CG1   . VAL A 1 4256 ? 197.642 164.866 181.324 1.00 72.63  ? 4256 VAL A CG1   1 
ATOM   20705 C  CG2   . VAL A 1 4256 ? 198.082 163.381 179.364 1.00 61.00  ? 4256 VAL A CG2   1 
ATOM   20706 N  N     . ASP A 1 4257 ? 194.776 166.465 180.476 1.00 79.85  ? 4257 ASP A N     1 
ATOM   20707 C  CA    . ASP A 1 4257 ? 194.167 167.618 181.131 1.00 81.86  ? 4257 ASP A CA    1 
ATOM   20708 C  C     . ASP A 1 4257 ? 194.129 167.474 182.648 1.00 84.11  ? 4257 ASP A C     1 
ATOM   20709 O  O     . ASP A 1 4257 ? 193.550 168.321 183.335 1.00 86.43  ? 4257 ASP A O     1 
ATOM   20710 C  CB    . ASP A 1 4257 ? 192.763 167.867 180.568 1.00 83.42  ? 4257 ASP A CB    1 
ATOM   20711 C  CG    . ASP A 1 4257 ? 191.775 166.744 180.883 1.00 88.51  ? 4257 ASP A CG    1 
ATOM   20712 O  OD1   . ASP A 1 4257 ? 192.000 165.945 181.816 1.00 91.36  ? 4257 ASP A OD1   1 
ATOM   20713 O  OD2   . ASP A 1 4257 ? 190.748 166.663 180.178 1.00 88.72  ? 4257 ASP A OD2   1 
ATOM   20714 N  N     . ASN A 1 4258 ? 194.735 166.421 183.184 1.00 79.78  ? 4258 ASN A N     1 
ATOM   20715 C  CA    . ASN A 1 4258 ? 194.724 166.144 184.611 1.00 75.24  ? 4258 ASN A CA    1 
ATOM   20716 C  C     . ASN A 1 4258 ? 196.143 166.223 185.152 1.00 79.41  ? 4258 ASN A C     1 
ATOM   20717 O  O     . ASN A 1 4258 ? 197.092 165.777 184.501 1.00 86.42  ? 4258 ASN A O     1 
ATOM   20718 C  CB    . ASN A 1 4258 ? 194.124 164.763 184.896 1.00 72.52  ? 4258 ASN A CB    1 
ATOM   20719 C  CG    . ASN A 1 4258 ? 193.831 164.543 186.367 1.00 82.02  ? 4258 ASN A CG    1 
ATOM   20720 O  OD1   . ASN A 1 4258 ? 194.721 164.636 187.212 1.00 85.36  ? 4258 ASN A OD1   1 
ATOM   20721 N  ND2   . ASN A 1 4258 ? 192.576 164.245 186.680 1.00 84.30  ? 4258 ASN A ND2   1 
ATOM   20722 N  N     . GLU A 1 4259 ? 196.279 166.796 186.349 1.00 76.67  ? 4259 GLU A N     1 
ATOM   20723 C  CA    . GLU A 1 4259 ? 197.594 166.902 186.971 1.00 76.81  ? 4259 GLU A CA    1 
ATOM   20724 C  C     . GLU A 1 4259 ? 198.175 165.526 187.269 1.00 80.98  ? 4259 GLU A C     1 
ATOM   20725 O  O     . GLU A 1 4259 ? 199.371 165.290 187.067 1.00 81.58  ? 4259 GLU A O     1 
ATOM   20726 C  CB    . GLU A 1 4259 ? 197.495 167.743 188.247 1.00 77.98  ? 4259 GLU A CB    1 
ATOM   20727 C  CG    . GLU A 1 4259 ? 198.640 167.615 189.274 1.00 81.57  ? 4259 GLU A CG    1 
ATOM   20728 C  CD    . GLU A 1 4259 ? 200.057 167.667 188.698 1.00 85.58  ? 4259 GLU A CD    1 
ATOM   20729 O  OE1   . GLU A 1 4259 ? 201.002 167.379 189.463 1.00 85.91  ? 4259 GLU A OE1   1 
ATOM   20730 O  OE2   . GLU A 1 4259 ? 200.248 168.030 187.518 1.00 87.85  ? 4259 GLU A OE2   1 
ATOM   20731 N  N     . PHE A 1 4260 ? 197.341 164.598 187.738 1.00 75.32  ? 4260 PHE A N     1 
ATOM   20732 C  CA    . PHE A 1 4260 ? 197.839 163.286 188.128 1.00 70.31  ? 4260 PHE A CA    1 
ATOM   20733 C  C     . PHE A 1 4260 ? 198.154 162.411 186.921 1.00 72.59  ? 4260 PHE A C     1 
ATOM   20734 O  O     . PHE A 1 4260 ? 199.114 161.633 186.958 1.00 78.86  ? 4260 PHE A O     1 
ATOM   20735 C  CB    . PHE A 1 4260 ? 196.825 162.613 189.050 1.00 71.77  ? 4260 PHE A CB    1 
ATOM   20736 C  CG    . PHE A 1 4260 ? 196.555 163.395 190.300 1.00 77.61  ? 4260 PHE A CG    1 
ATOM   20737 C  CD1   . PHE A 1 4260 ? 197.342 163.232 191.425 1.00 76.20  ? 4260 PHE A CD1   1 
ATOM   20738 C  CD2   . PHE A 1 4260 ? 195.532 164.323 190.338 1.00 75.65  ? 4260 PHE A CD2   1 
ATOM   20739 C  CE1   . PHE A 1 4260 ? 197.102 163.964 192.569 1.00 74.89  ? 4260 PHE A CE1   1 
ATOM   20740 C  CE2   . PHE A 1 4260 ? 195.289 165.057 191.476 1.00 74.43  ? 4260 PHE A CE2   1 
ATOM   20741 C  CZ    . PHE A 1 4260 ? 196.075 164.878 192.594 1.00 77.12  ? 4260 PHE A CZ    1 
ATOM   20742 N  N     . ASP A 1 4261 ? 197.379 162.537 185.841 1.00 67.31  ? 4261 ASP A N     1 
ATOM   20743 C  CA    . ASP A 1 4261 ? 197.745 161.871 184.595 1.00 64.56  ? 4261 ASP A CA    1 
ATOM   20744 C  C     . ASP A 1 4261 ? 199.067 162.410 184.063 1.00 64.19  ? 4261 ASP A C     1 
ATOM   20745 O  O     . ASP A 1 4261 ? 199.898 161.650 183.550 1.00 72.47  ? 4261 ASP A O     1 
ATOM   20746 C  CB    . ASP A 1 4261 ? 196.638 162.049 183.558 1.00 59.28  ? 4261 ASP A CB    1 
ATOM   20747 C  CG    . ASP A 1 4261 ? 195.379 161.286 183.910 1.00 70.89  ? 4261 ASP A CG    1 
ATOM   20748 O  OD1   . ASP A 1 4261 ? 195.459 160.337 184.717 1.00 73.98  ? 4261 ASP A OD1   1 
ATOM   20749 O  OD2   . ASP A 1 4261 ? 194.307 161.637 183.377 1.00 74.62  ? 4261 ASP A OD2   1 
ATOM   20750 N  N     . GLN A 1 4262 ? 199.277 163.723 184.179 1.00 56.69  ? 4262 GLN A N     1 
ATOM   20751 C  CA    . GLN A 1 4262 ? 200.560 164.307 183.806 1.00 59.42  ? 4262 GLN A CA    1 
ATOM   20752 C  C     . GLN A 1 4262 ? 201.689 163.748 184.662 1.00 69.65  ? 4262 GLN A C     1 
ATOM   20753 O  O     . GLN A 1 4262 ? 202.782 163.473 184.155 1.00 79.15  ? 4262 GLN A O     1 
ATOM   20754 C  CB    . GLN A 1 4262 ? 200.500 165.828 183.929 1.00 62.03  ? 4262 GLN A CB    1 
ATOM   20755 C  CG    . GLN A 1 4262 ? 201.749 166.542 183.442 1.00 66.42  ? 4262 GLN A CG    1 
ATOM   20756 C  CD    . GLN A 1 4262 ? 201.936 166.439 181.945 1.00 68.51  ? 4262 GLN A CD    1 
ATOM   20757 O  OE1   . GLN A 1 4262 ? 201.030 166.747 181.172 1.00 68.44  ? 4262 GLN A OE1   1 
ATOM   20758 N  NE2   . GLN A 1 4262 ? 203.118 166.006 181.526 1.00 69.00  ? 4262 GLN A NE2   1 
ATOM   20759 N  N     . ARG A 1 4263 ? 201.446 163.583 185.965 1.00 70.51  ? 4263 ARG A N     1 
ATOM   20760 C  CA    . ARG A 1 4263 ? 202.470 163.018 186.837 1.00 63.51  ? 4263 ARG A CA    1 
ATOM   20761 C  C     . ARG A 1 4263 ? 202.804 161.590 186.428 1.00 66.55  ? 4263 ARG A C     1 
ATOM   20762 O  O     . ARG A 1 4263 ? 203.975 161.195 186.417 1.00 72.64  ? 4263 ARG A O     1 
ATOM   20763 C  CB    . ARG A 1 4263 ? 202.008 163.049 188.292 1.00 63.79  ? 4263 ARG A CB    1 
ATOM   20764 C  CG    . ARG A 1 4263 ? 202.287 164.351 189.019 1.00 70.81  ? 4263 ARG A CG    1 
ATOM   20765 C  CD    . ARG A 1 4263 ? 202.054 164.207 190.515 1.00 75.59  ? 4263 ARG A CD    1 
ATOM   20766 N  NE    . ARG A 1 4263 ? 200.890 163.384 190.823 1.00 79.19  ? 4263 ARG A NE    1 
ATOM   20767 C  CZ    . ARG A 1 4263 ? 200.968 162.178 191.369 1.00 75.13  ? 4263 ARG A CZ    1 
ATOM   20768 N  NH1   . ARG A 1 4263 ? 202.132 161.639 191.679 1.00 69.56  ? 4263 ARG A NH1   1 
ATOM   20769 N  NH2   . ARG A 1 4263 ? 199.852 161.495 191.602 1.00 68.44  ? 4263 ARG A NH2   1 
ATOM   20770 N  N     . LEU A 1 4264 ? 201.782 160.801 186.094 1.00 57.59  ? 4264 LEU A N     1 
ATOM   20771 C  CA    . LEU A 1 4264 ? 202.009 159.432 185.637 1.00 56.74  ? 4264 LEU A CA    1 
ATOM   20772 C  C     . LEU A 1 4264 ? 202.816 159.402 184.344 1.00 63.75  ? 4264 LEU A C     1 
ATOM   20773 O  O     . LEU A 1 4264 ? 203.739 158.587 184.195 1.00 74.46  ? 4264 LEU A O     1 
ATOM   20774 C  CB    . LEU A 1 4264 ? 200.669 158.725 185.448 1.00 47.33  ? 4264 LEU A CB    1 
ATOM   20775 C  CG    . LEU A 1 4264 ? 200.701 157.298 184.909 1.00 50.97  ? 4264 LEU A CG    1 
ATOM   20776 C  CD1   . LEU A 1 4264 ? 201.628 156.442 185.746 1.00 62.75  ? 4264 LEU A CD1   1 
ATOM   20777 C  CD2   . LEU A 1 4264 ? 199.299 156.719 184.891 1.00 52.96  ? 4264 LEU A CD2   1 
ATOM   20778 N  N     . LEU A 1 4265 ? 202.478 160.278 183.398 1.00 50.19  ? 4265 LEU A N     1 
ATOM   20779 C  CA    . LEU A 1 4265 ? 203.218 160.337 182.142 1.00 46.02  ? 4265 LEU A CA    1 
ATOM   20780 C  C     . LEU A 1 4265 ? 204.671 160.729 182.381 1.00 55.82  ? 4265 LEU A C     1 
ATOM   20781 O  O     . LEU A 1 4265 ? 205.587 160.156 181.775 1.00 65.20  ? 4265 LEU A O     1 
ATOM   20782 C  CB    . LEU A 1 4265 ? 202.542 161.321 181.191 1.00 39.88  ? 4265 LEU A CB    1 
ATOM   20783 C  CG    . LEU A 1 4265 ? 203.046 161.343 179.752 1.00 45.39  ? 4265 LEU A CG    1 
ATOM   20784 C  CD1   . LEU A 1 4265 ? 202.497 160.149 179.001 1.00 50.70  ? 4265 LEU A CD1   1 
ATOM   20785 C  CD2   . LEU A 1 4265 ? 202.637 162.636 179.075 1.00 54.85  ? 4265 LEU A CD2   1 
ATOM   20786 N  N     . ASN A 1 4266 ? 204.900 161.702 183.265 1.00 58.35  ? 4266 ASN A N     1 
ATOM   20787 C  CA    . ASN A 1 4266 ? 206.263 162.104 183.594 1.00 57.33  ? 4266 ASN A CA    1 
ATOM   20788 C  C     . ASN A 1 4266 ? 207.023 160.970 184.266 1.00 63.37  ? 4266 ASN A C     1 
ATOM   20789 O  O     . ASN A 1 4266 ? 208.223 160.796 184.033 1.00 68.87  ? 4266 ASN A O     1 
ATOM   20790 C  CB    . ASN A 1 4266 ? 206.244 163.341 184.490 1.00 58.88  ? 4266 ASN A CB    1 
ATOM   20791 C  CG    . ASN A 1 4266 ? 205.728 164.569 183.775 1.00 64.41  ? 4266 ASN A CG    1 
ATOM   20792 O  OD1   . ASN A 1 4266 ? 205.519 164.554 182.562 1.00 65.93  ? 4266 ASN A OD1   1 
ATOM   20793 N  ND2   . ASN A 1 4266 ? 205.516 165.644 184.524 1.00 63.88  ? 4266 ASN A ND2   1 
ATOM   20794 N  N     . THR A 1 4267 ? 206.344 160.196 185.115 1.00 60.77  ? 4267 THR A N     1 
ATOM   20795 C  CA    . THR A 1 4267 ? 206.984 159.049 185.750 1.00 64.28  ? 4267 THR A CA    1 
ATOM   20796 C  C     . THR A 1 4267 ? 207.415 158.022 184.710 1.00 68.95  ? 4267 THR A C     1 
ATOM   20797 O  O     . THR A 1 4267 ? 208.541 157.511 184.753 1.00 76.71  ? 4267 THR A O     1 
ATOM   20798 C  CB    . THR A 1 4267 ? 206.032 158.416 186.765 1.00 62.36  ? 4267 THR A CB    1 
ATOM   20799 O  OG1   . THR A 1 4267 ? 205.759 159.354 187.813 1.00 73.97  ? 4267 THR A OG1   1 
ATOM   20800 C  CG2   . THR A 1 4267 ? 206.646 157.160 187.362 1.00 65.67  ? 4267 THR A CG2   1 
ATOM   20801 N  N     . PHE A 1 4268 ? 206.530 157.716 183.758 1.00 54.19  ? 4268 PHE A N     1 
ATOM   20802 C  CA    . PHE A 1 4268 ? 206.889 156.777 182.699 1.00 52.09  ? 4268 PHE A CA    1 
ATOM   20803 C  C     . PHE A 1 4268 ? 208.064 157.290 181.878 1.00 59.26  ? 4268 PHE A C     1 
ATOM   20804 O  O     . PHE A 1 4268 ? 208.989 156.532 181.559 1.00 66.98  ? 4268 PHE A O     1 
ATOM   20805 C  CB    . PHE A 1 4268 ? 205.691 156.509 181.791 1.00 52.24  ? 4268 PHE A CB    1 
ATOM   20806 C  CG    . PHE A 1 4268 ? 204.772 155.443 182.299 1.00 60.33  ? 4268 PHE A CG    1 
ATOM   20807 C  CD1   . PHE A 1 4268 ? 205.275 154.231 182.736 1.00 66.69  ? 4268 PHE A CD1   1 
ATOM   20808 C  CD2   . PHE A 1 4268 ? 203.405 155.645 182.325 1.00 52.37  ? 4268 PHE A CD2   1 
ATOM   20809 C  CE1   . PHE A 1 4268 ? 204.433 153.245 183.202 1.00 62.10  ? 4268 PHE A CE1   1 
ATOM   20810 C  CE2   . PHE A 1 4268 ? 202.558 154.662 182.788 1.00 58.04  ? 4268 PHE A CE2   1 
ATOM   20811 C  CZ    . PHE A 1 4268 ? 203.073 153.460 183.227 1.00 60.93  ? 4268 PHE A CZ    1 
ATOM   20812 N  N     . LEU A 1 4269 ? 208.046 158.577 181.526 1.00 53.16  ? 4269 LEU A N     1 
ATOM   20813 C  CA    . LEU A 1 4269 ? 209.119 159.126 180.705 1.00 44.55  ? 4269 LEU A CA    1 
ATOM   20814 C  C     . LEU A 1 4269 ? 210.444 159.134 181.455 1.00 57.40  ? 4269 LEU A C     1 
ATOM   20815 O  O     . LEU A 1 4269 ? 211.495 158.850 180.870 1.00 70.00  ? 4269 LEU A O     1 
ATOM   20816 C  CB    . LEU A 1 4269 ? 208.749 160.529 180.235 1.00 50.24  ? 4269 LEU A CB    1 
ATOM   20817 C  CG    . LEU A 1 4269 ? 207.664 160.519 179.162 1.00 46.30  ? 4269 LEU A CG    1 
ATOM   20818 C  CD1   . LEU A 1 4269 ? 206.903 161.822 179.154 1.00 51.70  ? 4269 LEU A CD1   1 
ATOM   20819 C  CD2   . LEU A 1 4269 ? 208.276 160.249 177.810 1.00 57.32  ? 4269 LEU A CD2   1 
ATOM   20820 N  N     . GLU A 1 4270 ? 210.416 159.463 182.748 1.00 66.27  ? 4270 GLU A N     1 
ATOM   20821 C  CA    . GLU A 1 4270 ? 211.628 159.404 183.554 1.00 66.96  ? 4270 GLU A CA    1 
ATOM   20822 C  C     . GLU A 1 4270 ? 212.151 157.980 183.670 1.00 69.92  ? 4270 GLU A C     1 
ATOM   20823 O  O     . GLU A 1 4270 ? 213.367 157.763 183.640 1.00 70.19  ? 4270 GLU A O     1 
ATOM   20824 C  CB    . GLU A 1 4270 ? 211.364 159.987 184.944 1.00 72.01  ? 4270 GLU A CB    1 
ATOM   20825 C  CG    . GLU A 1 4270 ? 211.579 161.501 185.101 1.00 73.30  ? 4270 GLU A CG    1 
ATOM   20826 C  CD    . GLU A 1 4270 ? 212.960 162.014 184.680 1.00 78.12  ? 4270 GLU A CD    1 
ATOM   20827 O  OE1   . GLU A 1 4270 ? 213.172 163.240 184.784 1.00 78.08  ? 4270 GLU A OE1   1 
ATOM   20828 O  OE2   . GLU A 1 4270 ? 213.841 161.222 184.283 1.00 76.41  ? 4270 GLU A OE2   1 
ATOM   20829 N  N     . ARG A 1 4271 ? 211.254 157.000 183.805 1.00 69.36  ? 4271 ARG A N     1 
ATOM   20830 C  CA    . ARG A 1 4271 ? 211.688 155.612 183.917 1.00 67.05  ? 4271 ARG A CA    1 
ATOM   20831 C  C     . ARG A 1 4271 ? 212.304 155.108 182.620 1.00 68.79  ? 4271 ARG A C     1 
ATOM   20832 O  O     . ARG A 1 4271 ? 213.300 154.377 182.644 1.00 70.71  ? 4271 ARG A O     1 
ATOM   20833 C  CB    . ARG A 1 4271 ? 210.511 154.727 184.320 1.00 72.60  ? 4271 ARG A CB    1 
ATOM   20834 C  CG    . ARG A 1 4271 ? 210.894 153.583 185.233 1.00 80.63  ? 4271 ARG A CG    1 
ATOM   20835 C  CD    . ARG A 1 4271 ? 209.704 152.687 185.522 1.00 80.54  ? 4271 ARG A CD    1 
ATOM   20836 N  NE    . ARG A 1 4271 ? 209.019 152.274 184.303 1.00 80.35  ? 4271 ARG A NE    1 
ATOM   20837 C  CZ    . ARG A 1 4271 ? 209.442 151.312 183.495 1.00 81.89  ? 4271 ARG A CZ    1 
ATOM   20838 N  NH1   . ARG A 1 4271 ? 210.549 150.634 183.748 1.00 74.75  ? 4271 ARG A NH1   1 
ATOM   20839 N  NH2   . ARG A 1 4271 ? 208.736 151.023 182.406 1.00 82.75  ? 4271 ARG A NH2   1 
ATOM   20840 N  N     . LEU A 1 4272 ? 211.729 155.482 181.478 1.00 59.47  ? 4272 LEU A N     1 
ATOM   20841 C  CA    . LEU A 1 4272 ? 212.150 154.886 180.216 1.00 60.27  ? 4272 LEU A CA    1 
ATOM   20842 C  C     . LEU A 1 4272 ? 213.281 155.658 179.543 1.00 56.09  ? 4272 LEU A C     1 
ATOM   20843 O  O     . LEU A 1 4272 ? 214.336 155.086 179.252 1.00 60.42  ? 4272 LEU A O     1 
ATOM   20844 C  CB    . LEU A 1 4272 ? 210.953 154.771 179.270 1.00 59.74  ? 4272 LEU A CB    1 
ATOM   20845 C  CG    . LEU A 1 4272 ? 209.975 153.643 179.602 1.00 55.27  ? 4272 LEU A CG    1 
ATOM   20846 C  CD1   . LEU A 1 4272 ? 208.778 153.682 178.674 1.00 60.29  ? 4272 LEU A CD1   1 
ATOM   20847 C  CD2   . LEU A 1 4272 ? 210.671 152.296 179.526 1.00 53.15  ? 4272 LEU A CD2   1 
ATOM   20848 N  N     . PHE A 1 4273 ? 213.086 156.953 179.292 1.00 58.65  ? 4273 PHE A N     1 
ATOM   20849 C  CA    . PHE A 1 4273 ? 214.051 157.744 178.527 1.00 53.10  ? 4273 PHE A CA    1 
ATOM   20850 C  C     . PHE A 1 4273 ? 215.138 158.264 179.463 1.00 60.67  ? 4273 PHE A C     1 
ATOM   20851 O  O     . PHE A 1 4273 ? 215.118 159.405 179.929 1.00 70.42  ? 4273 PHE A O     1 
ATOM   20852 C  CB    . PHE A 1 4273 ? 213.348 158.876 177.788 1.00 53.48  ? 4273 PHE A CB    1 
ATOM   20853 C  CG    . PHE A 1 4273 ? 212.486 158.410 176.652 1.00 59.91  ? 4273 PHE A CG    1 
ATOM   20854 C  CD1   . PHE A 1 4273 ? 211.170 158.043 176.866 1.00 59.97  ? 4273 PHE A CD1   1 
ATOM   20855 C  CD2   . PHE A 1 4273 ? 212.996 158.336 175.367 1.00 65.80  ? 4273 PHE A CD2   1 
ATOM   20856 C  CE1   . PHE A 1 4273 ? 210.379 157.612 175.821 1.00 60.74  ? 4273 PHE A CE1   1 
ATOM   20857 C  CE2   . PHE A 1 4273 ? 212.210 157.906 174.319 1.00 64.96  ? 4273 PHE A CE2   1 
ATOM   20858 C  CZ    . PHE A 1 4273 ? 210.900 157.544 174.546 1.00 65.57  ? 4273 PHE A CZ    1 
ATOM   20859 N  N     . THR A 1 4274 ? 216.110 157.397 179.734 1.00 72.76  ? 4274 THR A N     1 
ATOM   20860 C  CA    . THR A 1 4274 ? 217.287 157.751 180.514 1.00 75.81  ? 4274 THR A CA    1 
ATOM   20861 C  C     . THR A 1 4274 ? 218.505 157.069 179.909 1.00 74.83  ? 4274 THR A C     1 
ATOM   20862 O  O     . THR A 1 4274 ? 218.390 156.139 179.108 1.00 74.49  ? 4274 THR A O     1 
ATOM   20863 C  CB    . THR A 1 4274 ? 217.139 157.360 181.990 1.00 80.33  ? 4274 THR A CB    1 
ATOM   20864 O  OG1   . THR A 1 4274 ? 216.452 156.107 182.091 1.00 80.19  ? 4274 THR A OG1   1 
ATOM   20865 C  CG2   . THR A 1 4274 ? 216.374 158.427 182.754 1.00 77.35  ? 4274 THR A CG2   1 
ATOM   20866 N  N     . THR A 1 4275 ? 219.686 157.551 180.301 1.00 80.68  ? 4275 THR A N     1 
ATOM   20867 C  CA    . THR A 1 4275 ? 220.925 156.962 179.804 1.00 81.53  ? 4275 THR A CA    1 
ATOM   20868 C  C     . THR A 1 4275 ? 221.080 155.515 180.253 1.00 84.82  ? 4275 THR A C     1 
ATOM   20869 O  O     . THR A 1 4275 ? 221.703 154.712 179.549 1.00 90.40  ? 4275 THR A O     1 
ATOM   20870 C  CB    . THR A 1 4275 ? 222.124 157.790 180.265 1.00 84.45  ? 4275 THR A CB    1 
ATOM   20871 O  OG1   . THR A 1 4275 ? 221.847 159.181 180.069 1.00 88.19  ? 4275 THR A OG1   1 
ATOM   20872 C  CG2   . THR A 1 4275 ? 223.362 157.415 179.468 1.00 82.11  ? 4275 THR A CG2   1 
ATOM   20873 N  N     . ARG A 1 4276 ? 220.517 155.160 181.410 1.00 82.83  ? 4276 ARG A N     1 
ATOM   20874 C  CA    . ARG A 1 4276 ? 220.590 153.788 181.896 1.00 79.89  ? 4276 ARG A CA    1 
ATOM   20875 C  C     . ARG A 1 4276 ? 219.832 152.807 181.014 1.00 84.83  ? 4276 ARG A C     1 
ATOM   20876 O  O     . ARG A 1 4276 ? 220.038 151.596 181.149 1.00 87.94  ? 4276 ARG A O     1 
ATOM   20877 C  CB    . ARG A 1 4276 ? 220.058 153.708 183.327 1.00 80.59  ? 4276 ARG A CB    1 
ATOM   20878 C  CG    . ARG A 1 4276 ? 221.137 153.786 184.394 1.00 85.63  ? 4276 ARG A CG    1 
ATOM   20879 C  CD    . ARG A 1 4276 ? 220.545 153.664 185.788 1.00 90.01  ? 4276 ARG A CD    1 
ATOM   20880 N  NE    . ARG A 1 4276 ? 219.865 152.389 185.982 1.00 92.40  ? 4276 ARG A NE    1 
ATOM   20881 C  CZ    . ARG A 1 4276 ? 218.552 152.251 186.099 1.00 89.56  ? 4276 ARG A CZ    1 
ATOM   20882 N  NH1   . ARG A 1 4276 ? 217.740 153.294 186.048 1.00 86.19  ? 4276 ARG A NH1   1 
ATOM   20883 N  NH2   . ARG A 1 4276 ? 218.040 151.035 186.269 1.00 85.75  ? 4276 ARG A NH2   1 
ATOM   20884 N  N     . SER A 1 4277 ? 218.964 153.292 180.123 1.00 81.53  ? 4277 SER A N     1 
ATOM   20885 C  CA    . SER A 1 4277 ? 218.232 152.402 179.230 1.00 79.21  ? 4277 SER A CA    1 
ATOM   20886 C  C     . SER A 1 4277 ? 219.142 151.711 178.226 1.00 83.33  ? 4277 SER A C     1 
ATOM   20887 O  O     . SER A 1 4277 ? 218.722 150.730 177.602 1.00 87.43  ? 4277 SER A O     1 
ATOM   20888 C  CB    . SER A 1 4277 ? 217.145 153.178 178.490 1.00 75.70  ? 4277 SER A CB    1 
ATOM   20889 O  OG    . SER A 1 4277 ? 217.705 153.961 177.451 1.00 81.66  ? 4277 SER A OG    1 
ATOM   20890 N  N     . PHE A 1 4278 ? 220.367 152.196 178.050 1.00 79.74  ? 4278 PHE A N     1 
ATOM   20891 C  CA    . PHE A 1 4278 ? 221.327 151.569 177.152 1.00 79.51  ? 4278 PHE A CA    1 
ATOM   20892 C  C     . PHE A 1 4278 ? 222.208 150.545 177.853 1.00 83.22  ? 4278 PHE A C     1 
ATOM   20893 O  O     . PHE A 1 4278 ? 223.073 149.947 177.205 1.00 83.80  ? 4278 PHE A O     1 
ATOM   20894 C  CB    . PHE A 1 4278 ? 222.198 152.636 176.484 1.00 75.49  ? 4278 PHE A CB    1 
ATOM   20895 C  CG    . PHE A 1 4278 ? 221.552 153.277 175.293 1.00 76.01  ? 4278 PHE A CG    1 
ATOM   20896 C  CD1   . PHE A 1 4278 ? 220.537 154.203 175.453 1.00 81.58  ? 4278 PHE A CD1   1 
ATOM   20897 C  CD2   . PHE A 1 4278 ? 221.955 152.949 174.012 1.00 77.36  ? 4278 PHE A CD2   1 
ATOM   20898 C  CE1   . PHE A 1 4278 ? 219.939 154.790 174.358 1.00 83.57  ? 4278 PHE A CE1   1 
ATOM   20899 C  CE2   . PHE A 1 4278 ? 221.360 153.533 172.915 1.00 81.76  ? 4278 PHE A CE2   1 
ATOM   20900 C  CZ    . PHE A 1 4278 ? 220.351 154.455 173.088 1.00 83.98  ? 4278 PHE A CZ    1 
ATOM   20901 N  N     . ASP A 1 4279 ? 222.014 150.333 179.151 1.00 96.36  ? 4279 ASP A N     1 
ATOM   20902 C  CA    . ASP A 1 4279 ? 222.736 149.285 179.851 1.00 94.08  ? 4279 ASP A CA    1 
ATOM   20903 C  C     . ASP A 1 4279 ? 222.186 147.915 179.465 1.00 99.27  ? 4279 ASP A C     1 
ATOM   20904 O  O     . ASP A 1 4279 ? 221.067 147.782 178.961 1.00 100.47 ? 4279 ASP A O     1 
ATOM   20905 C  CB    . ASP A 1 4279 ? 222.642 149.483 181.363 1.00 93.57  ? 4279 ASP A CB    1 
ATOM   20906 C  CG    . ASP A 1 4279 ? 223.526 150.609 181.859 1.00 100.02 ? 4279 ASP A CG    1 
ATOM   20907 O  OD1   . ASP A 1 4279 ? 224.389 151.073 181.085 1.00 94.28  ? 4279 ASP A OD1   1 
ATOM   20908 O  OD2   . ASP A 1 4279 ? 223.359 151.028 183.023 1.00 102.64 ? 4279 ASP A OD2   1 
ATOM   20909 N  N     . SER A 1 4280 ? 222.993 146.884 179.709 1.00 110.70 ? 4280 SER A N     1 
ATOM   20910 C  CA    . SER A 1 4280 ? 222.596 145.523 179.377 1.00 112.21 ? 4280 SER A CA    1 
ATOM   20911 C  C     . SER A 1 4280 ? 221.677 144.900 180.419 1.00 111.51 ? 4280 SER A C     1 
ATOM   20912 O  O     . SER A 1 4280 ? 221.189 143.787 180.201 1.00 113.82 ? 4280 SER A O     1 
ATOM   20913 C  CB    . SER A 1 4280 ? 223.836 144.644 179.194 1.00 109.77 ? 4280 SER A CB    1 
ATOM   20914 O  OG    . SER A 1 4280 ? 224.535 144.484 180.415 1.00 110.74 ? 4280 SER A OG    1 
ATOM   20915 N  N     . GLU A 1 4281 ? 221.428 145.584 181.536 1.00 110.89 ? 4281 GLU A N     1 
ATOM   20916 C  CA    . GLU A 1 4281 ? 220.576 145.062 182.598 1.00 112.75 ? 4281 GLU A CA    1 
ATOM   20917 C  C     . GLU A 1 4281 ? 219.350 145.932 182.848 1.00 112.24 ? 4281 GLU A C     1 
ATOM   20918 O  O     . GLU A 1 4281 ? 218.774 145.870 183.940 1.00 111.35 ? 4281 GLU A O     1 
ATOM   20919 C  CB    . GLU A 1 4281 ? 221.374 144.907 183.898 1.00 117.41 ? 4281 GLU A CB    1 
ATOM   20920 C  CG    . GLU A 1 4281 ? 222.704 144.176 183.753 1.00 115.48 ? 4281 GLU A CG    1 
ATOM   20921 C  CD    . GLU A 1 4281 ? 223.842 145.086 183.326 1.00 116.03 ? 4281 GLU A CD    1 
ATOM   20922 O  OE1   . GLU A 1 4281 ? 225.013 144.731 183.576 1.00 117.23 ? 4281 GLU A OE1   1 
ATOM   20923 O  OE2   . GLU A 1 4281 ? 223.570 146.154 182.738 1.00 114.54 ? 4281 GLU A OE2   1 
ATOM   20924 N  N     . PHE A 1 4282 ? 218.940 146.740 181.874 1.00 99.18  ? 4282 PHE A N     1 
ATOM   20925 C  CA    . PHE A 1 4282 ? 217.795 147.619 182.066 1.00 96.12  ? 4282 PHE A CA    1 
ATOM   20926 C  C     . PHE A 1 4282 ? 216.503 146.814 182.120 1.00 96.54  ? 4282 PHE A C     1 
ATOM   20927 O  O     . PHE A 1 4282 ? 216.277 145.914 181.306 1.00 98.76  ? 4282 PHE A O     1 
ATOM   20928 C  CB    . PHE A 1 4282 ? 217.731 148.650 180.940 1.00 92.89  ? 4282 PHE A CB    1 
ATOM   20929 C  CG    . PHE A 1 4282 ? 216.671 149.693 181.133 1.00 89.39  ? 4282 PHE A CG    1 
ATOM   20930 C  CD1   . PHE A 1 4282 ? 216.673 150.500 182.256 1.00 91.69  ? 4282 PHE A CD1   1 
ATOM   20931 C  CD2   . PHE A 1 4282 ? 215.677 149.873 180.186 1.00 92.18  ? 4282 PHE A CD2   1 
ATOM   20932 C  CE1   . PHE A 1 4282 ? 215.700 151.463 182.435 1.00 97.56  ? 4282 PHE A CE1   1 
ATOM   20933 C  CE2   . PHE A 1 4282 ? 214.703 150.834 180.360 1.00 93.68  ? 4282 PHE A CE2   1 
ATOM   20934 C  CZ    . PHE A 1 4282 ? 214.714 151.630 181.485 1.00 95.25  ? 4282 PHE A CZ    1 
ATOM   20935 N  N     . LYS A 1 4283 ? 215.649 147.145 183.086 1.00 90.58  ? 4283 LYS A N     1 
ATOM   20936 C  CA    . LYS A 1 4283 ? 214.379 146.458 183.297 1.00 88.00  ? 4283 LYS A CA    1 
ATOM   20937 C  C     . LYS A 1 4283 ? 213.256 147.332 182.754 1.00 92.09  ? 4283 LYS A C     1 
ATOM   20938 O  O     . LYS A 1 4283 ? 212.952 148.385 183.324 1.00 95.31  ? 4283 LYS A O     1 
ATOM   20939 C  CB    . LYS A 1 4283 ? 214.160 146.154 184.777 1.00 84.80  ? 4283 LYS A CB    1 
ATOM   20940 C  CG    . LYS A 1 4283 ? 215.415 145.760 185.532 1.00 91.63  ? 4283 LYS A CG    1 
ATOM   20941 C  CD    . LYS A 1 4283 ? 215.885 144.376 185.126 1.00 92.81  ? 4283 LYS A CD    1 
ATOM   20942 C  CE    . LYS A 1 4283 ? 216.879 143.812 186.126 1.00 92.26  ? 4283 LYS A CE    1 
ATOM   20943 N  NZ    . LYS A 1 4283 ? 216.276 143.665 187.479 1.00 92.24  ? 4283 LYS A NZ    1 
ATOM   20944 N  N     . LEU A 1 4284 ? 212.643 146.897 181.651 1.00 80.47  ? 4284 LEU A N     1 
ATOM   20945 C  CA    . LEU A 1 4284 ? 211.488 147.614 181.123 1.00 73.08  ? 4284 LEU A CA    1 
ATOM   20946 C  C     . LEU A 1 4284 ? 210.309 147.541 182.085 1.00 75.18  ? 4284 LEU A C     1 
ATOM   20947 O  O     . LEU A 1 4284 ? 209.616 148.540 182.305 1.00 82.50  ? 4284 LEU A O     1 
ATOM   20948 C  CB    . LEU A 1 4284 ? 211.104 147.056 179.754 1.00 66.40  ? 4284 LEU A CB    1 
ATOM   20949 C  CG    . LEU A 1 4284 ? 212.092 147.339 178.622 1.00 69.25  ? 4284 LEU A CG    1 
ATOM   20950 C  CD1   . LEU A 1 4284 ? 211.673 146.616 177.353 1.00 76.41  ? 4284 LEU A CD1   1 
ATOM   20951 C  CD2   . LEU A 1 4284 ? 212.219 148.833 178.376 1.00 74.75  ? 4284 LEU A CD2   1 
ATOM   20952 N  N     . ALA A 1 4285 ? 210.063 146.367 182.660 1.00 85.65  ? 4285 ALA A N     1 
ATOM   20953 C  CA    . ALA A 1 4285 ? 209.050 146.189 183.688 1.00 87.28  ? 4285 ALA A CA    1 
ATOM   20954 C  C     . ALA A 1 4285 ? 209.619 145.295 184.779 1.00 93.12  ? 4285 ALA A C     1 
ATOM   20955 O  O     . ALA A 1 4285 ? 210.315 144.317 184.495 1.00 96.77  ? 4285 ALA A O     1 
ATOM   20956 C  CB    . ALA A 1 4285 ? 207.760 145.584 183.121 1.00 86.53  ? 4285 ALA A CB    1 
ATOM   20957 N  N     . CYS A 1 4286 ? 209.315 145.634 186.028 1.00 107.67 ? 4286 CYS A N     1 
ATOM   20958 C  CA    . CYS A 1 4286 ? 209.880 144.953 187.186 1.00 107.24 ? 4286 CYS A CA    1 
ATOM   20959 C  C     . CYS A 1 4286 ? 208.827 144.064 187.831 1.00 110.37 ? 4286 CYS A C     1 
ATOM   20960 O  O     . CYS A 1 4286 ? 207.739 144.536 188.177 1.00 107.61 ? 4286 CYS A O     1 
ATOM   20961 C  CB    . CYS A 1 4286 ? 210.415 145.961 188.207 1.00 107.84 ? 4286 CYS A CB    1 
ATOM   20962 S  SG    . CYS A 1 4286 ? 211.400 147.297 187.492 1.00 115.52 ? 4286 CYS A SG    1 
ATOM   20963 N  N     . LYS A 1 4287 ? 209.161 142.782 187.992 1.00 119.90 ? 4287 LYS A N     1 
ATOM   20964 C  CA    . LYS A 1 4287 ? 208.320 141.812 188.695 1.00 118.52 ? 4287 LYS A CA    1 
ATOM   20965 C  C     . LYS A 1 4287 ? 206.927 141.724 188.067 1.00 115.62 ? 4287 LYS A C     1 
ATOM   20966 O  O     . LYS A 1 4287 ? 205.913 142.067 188.677 1.00 114.43 ? 4287 LYS A O     1 
ATOM   20967 C  CB    . LYS A 1 4287 ? 208.238 142.145 190.189 1.00 118.91 ? 4287 LYS A CB    1 
ATOM   20968 C  CG    . LYS A 1 4287 ? 209.211 141.358 191.054 1.00 118.13 ? 4287 LYS A CG    1 
ATOM   20969 C  CD    . LYS A 1 4287 ? 210.655 141.737 190.763 1.00 118.68 ? 4287 LYS A CD    1 
ATOM   20970 C  CE    . LYS A 1 4287 ? 210.951 143.165 191.190 1.00 117.02 ? 4287 LYS A CE    1 
ATOM   20971 N  NZ    . LYS A 1 4287 ? 212.354 143.556 190.878 1.00 116.53 ? 4287 LYS A NZ    1 
ATOM   20972 N  N     . VAL A 1 4288 ? 206.899 141.257 186.817 1.00 109.24 ? 4288 VAL A N     1 
ATOM   20973 C  CA    . VAL A 1 4288 ? 205.631 141.113 186.108 1.00 107.17 ? 4288 VAL A CA    1 
ATOM   20974 C  C     . VAL A 1 4288 ? 204.758 140.052 186.770 1.00 110.40 ? 4288 VAL A C     1 
ATOM   20975 O  O     . VAL A 1 4288 ? 203.528 140.171 186.794 1.00 112.06 ? 4288 VAL A O     1 
ATOM   20976 C  CB    . VAL A 1 4288 ? 205.880 140.810 184.618 1.00 107.61 ? 4288 VAL A CB    1 
ATOM   20977 C  CG1   . VAL A 1 4288 ? 206.717 141.911 183.995 1.00 107.98 ? 4288 VAL A CG1   1 
ATOM   20978 C  CG2   . VAL A 1 4288 ? 206.566 139.464 184.443 1.00 109.47 ? 4288 VAL A CG2   1 
ATOM   20979 N  N     . ASP A 1 4289 ? 205.371 138.999 187.314 1.00 129.39 ? 4289 ASP A N     1 
ATOM   20980 C  CA    . ASP A 1 4289 ? 204.633 137.951 188.010 1.00 130.04 ? 4289 ASP A CA    1 
ATOM   20981 C  C     . ASP A 1 4289 ? 205.280 137.618 189.349 1.00 130.77 ? 4289 ASP A C     1 
ATOM   20982 O  O     . ASP A 1 4289 ? 205.054 136.540 189.904 1.00 128.99 ? 4289 ASP A O     1 
ATOM   20983 C  CB    . ASP A 1 4289 ? 204.507 136.698 187.143 1.00 128.76 ? 4289 ASP A CB    1 
ATOM   20984 C  CG    . ASP A 1 4289 ? 205.820 136.298 186.498 1.00 129.96 ? 4289 ASP A CG    1 
ATOM   20985 O  OD1   . ASP A 1 4289 ? 206.808 136.084 187.231 1.00 130.54 ? 4289 ASP A OD1   1 
ATOM   20986 O  OD2   . ASP A 1 4289 ? 205.860 136.194 185.254 1.00 130.35 ? 4289 ASP A OD2   1 
ATOM   20987 N  N     . GLY A 1 4290 ? 206.087 138.536 189.880 1.00 128.24 ? 4290 GLY A N     1 
ATOM   20988 C  CA    . GLY A 1 4290 ? 206.695 138.388 191.180 1.00 127.46 ? 4290 GLY A CA    1 
ATOM   20989 C  C     . GLY A 1 4290 ? 208.120 137.870 191.169 1.00 128.28 ? 4290 GLY A C     1 
ATOM   20990 O  O     . GLY A 1 4290 ? 208.879 138.157 192.100 1.00 129.25 ? 4290 GLY A O     1 
ATOM   20991 N  N     . HIS A 1 4291 ? 208.505 137.114 190.141 1.00 132.00 ? 4291 HIS A N     1 
ATOM   20992 C  CA    . HIS A 1 4291 ? 209.846 136.550 190.052 1.00 133.83 ? 4291 HIS A CA    1 
ATOM   20993 C  C     . HIS A 1 4291 ? 210.633 137.113 188.876 1.00 134.25 ? 4291 HIS A C     1 
ATOM   20994 O  O     . HIS A 1 4291 ? 211.732 137.644 189.064 1.00 132.91 ? 4291 HIS A O     1 
ATOM   20995 C  CB    . HIS A 1 4291 ? 209.771 135.019 189.959 1.00 132.27 ? 4291 HIS A CB    1 
ATOM   20996 C  CG    . HIS A 1 4291 ? 208.951 134.387 191.040 1.00 131.80 ? 4291 HIS A CG    1 
ATOM   20997 N  ND1   . HIS A 1 4291 ? 207.573 134.411 191.040 1.00 132.00 ? 4291 HIS A ND1   1 
ATOM   20998 C  CD2   . HIS A 1 4291 ? 209.315 133.713 192.156 1.00 131.22 ? 4291 HIS A CD2   1 
ATOM   20999 C  CE1   . HIS A 1 4291 ? 207.124 133.779 192.110 1.00 131.47 ? 4291 HIS A CE1   1 
ATOM   21000 N  NE2   . HIS A 1 4291 ? 208.161 133.346 192.804 1.00 131.50 ? 4291 HIS A NE2   1 
ATOM   21001 N  N     . LYS A 1 4292 ? 210.101 137.014 187.662 1.00 124.88 ? 4292 LYS A N     1 
ATOM   21002 C  CA    . LYS A 1 4292 ? 210.825 137.458 186.483 1.00 122.60 ? 4292 LYS A CA    1 
ATOM   21003 C  C     . LYS A 1 4292 ? 210.468 138.901 186.141 1.00 122.11 ? 4292 LYS A C     1 
ATOM   21004 O  O     . LYS A 1 4292 ? 209.505 139.475 186.653 1.00 122.22 ? 4292 LYS A O     1 
ATOM   21005 C  CB    . LYS A 1 4292 ? 210.532 136.542 185.294 1.00 120.06 ? 4292 LYS A CB    1 
ATOM   21006 C  CG    . LYS A 1 4292 ? 209.067 136.482 184.902 1.00 120.66 ? 4292 LYS A CG    1 
ATOM   21007 C  CD    . LYS A 1 4292 ? 208.907 136.097 183.440 1.00 123.61 ? 4292 LYS A CD    1 
ATOM   21008 C  CE    . LYS A 1 4292 ? 208.957 137.321 182.540 1.00 123.12 ? 4292 LYS A CE    1 
ATOM   21009 N  NZ    . LYS A 1 4292 ? 208.497 137.017 181.157 1.00 122.42 ? 4292 LYS A NZ    1 
ATOM   21010 N  N     . ASP A 1 4293 ? 211.269 139.488 185.256 1.00 111.07 ? 4293 ASP A N     1 
ATOM   21011 C  CA    . ASP A 1 4293 ? 211.066 140.854 184.802 1.00 106.44 ? 4293 ASP A CA    1 
ATOM   21012 C  C     . ASP A 1 4293 ? 211.503 140.959 183.348 1.00 111.29 ? 4293 ASP A C     1 
ATOM   21013 O  O     . ASP A 1 4293 ? 212.334 140.183 182.871 1.00 117.50 ? 4293 ASP A O     1 
ATOM   21014 C  CB    . ASP A 1 4293 ? 211.834 141.855 185.674 1.00 106.07 ? 4293 ASP A CB    1 
ATOM   21015 C  CG    . ASP A 1 4293 ? 213.191 141.335 186.098 1.00 113.57 ? 4293 ASP A CG    1 
ATOM   21016 O  OD1   . ASP A 1 4293 ? 213.512 140.172 185.772 1.00 113.10 ? 4293 ASP A OD1   1 
ATOM   21017 O  OD2   . ASP A 1 4293 ? 213.938 142.087 186.759 1.00 114.96 ? 4293 ASP A OD2   1 
ATOM   21018 N  N     . ILE A 1 4294 ? 210.934 141.934 182.647 1.00 83.89  ? 4294 ILE A N     1 
ATOM   21019 C  CA    . ILE A 1 4294 ? 211.209 142.112 181.225 1.00 82.32  ? 4294 ILE A CA    1 
ATOM   21020 C  C     . ILE A 1 4294 ? 212.574 142.768 181.065 1.00 82.54  ? 4294 ILE A C     1 
ATOM   21021 O  O     . ILE A 1 4294 ? 212.842 143.822 181.652 1.00 85.55  ? 4294 ILE A O     1 
ATOM   21022 C  CB    . ILE A 1 4294 ? 210.112 142.944 180.549 1.00 78.36  ? 4294 ILE A CB    1 
ATOM   21023 C  CG1   . ILE A 1 4294 ? 208.733 142.505 181.044 1.00 78.15  ? 4294 ILE A CG1   1 
ATOM   21024 C  CG2   . ILE A 1 4294 ? 210.205 142.814 179.039 1.00 79.50  ? 4294 ILE A CG2   1 
ATOM   21025 C  CD1   . ILE A 1 4294 ? 207.592 142.940 180.153 1.00 79.70  ? 4294 ILE A CD1   1 
ATOM   21026 N  N     . GLN A 1 4295 ? 213.438 142.146 180.271 1.00 89.62  ? 4295 GLN A N     1 
ATOM   21027 C  CA    . GLN A 1 4295 ? 214.790 142.637 180.062 1.00 91.82  ? 4295 GLN A CA    1 
ATOM   21028 C  C     . GLN A 1 4295 ? 214.877 143.453 178.779 1.00 93.80  ? 4295 GLN A C     1 
ATOM   21029 O  O     . GLN A 1 4295 ? 214.218 143.154 177.780 1.00 97.48  ? 4295 GLN A O     1 
ATOM   21030 C  CB    . GLN A 1 4295 ? 215.783 141.475 179.999 1.00 97.17  ? 4295 GLN A CB    1 
ATOM   21031 C  CG    . GLN A 1 4295 ? 215.936 140.708 181.299 1.00 94.99  ? 4295 GLN A CG    1 
ATOM   21032 C  CD    . GLN A 1 4295 ? 216.686 141.494 182.354 1.00 97.34  ? 4295 GLN A CD    1 
ATOM   21033 O  OE1   . GLN A 1 4295 ? 216.190 141.697 183.460 1.00 94.61  ? 4295 GLN A OE1   1 
ATOM   21034 N  NE2   . GLN A 1 4295 ? 217.889 141.942 182.014 1.00 99.54  ? 4295 GLN A NE2   1 
ATOM   21035 N  N     . MET A 1 4296 ? 215.698 144.491 178.819 1.00 79.72  ? 4296 MET A N     1 
ATOM   21036 C  CA    . MET A 1 4296 ? 215.963 145.277 177.623 1.00 79.36  ? 4296 MET A CA    1 
ATOM   21037 C  C     . MET A 1 4296 ? 216.797 144.455 176.646 1.00 86.36  ? 4296 MET A C     1 
ATOM   21038 O  O     . MET A 1 4296 ? 217.788 143.839 177.054 1.00 86.75  ? 4296 MET A O     1 
ATOM   21039 C  CB    . MET A 1 4296 ? 216.692 146.568 177.987 1.00 87.96  ? 4296 MET A CB    1 
ATOM   21040 C  CG    . MET A 1 4296 ? 216.923 147.505 176.817 1.00 87.78  ? 4296 MET A CG    1 
ATOM   21041 S  SD    . MET A 1 4296 ? 215.418 148.294 176.221 1.00 94.55  ? 4296 MET A SD    1 
ATOM   21042 C  CE    . MET A 1 4296 ? 216.076 149.856 175.648 1.00 82.19  ? 4296 MET A CE    1 
ATOM   21043 N  N     . PRO A 1 4297 ? 216.428 144.405 175.367 1.00 85.09  ? 4297 PRO A N     1 
ATOM   21044 C  CA    . PRO A 1 4297 ? 217.233 143.650 174.400 1.00 82.07  ? 4297 PRO A CA    1 
ATOM   21045 C  C     . PRO A 1 4297 ? 218.632 144.233 174.271 1.00 84.61  ? 4297 PRO A C     1 
ATOM   21046 O  O     . PRO A 1 4297 ? 218.834 145.444 174.377 1.00 94.12  ? 4297 PRO A O     1 
ATOM   21047 C  CB    . PRO A 1 4297 ? 216.445 143.786 173.092 1.00 81.54  ? 4297 PRO A CB    1 
ATOM   21048 C  CG    . PRO A 1 4297 ? 215.075 144.206 173.497 1.00 85.14  ? 4297 PRO A CG    1 
ATOM   21049 C  CD    . PRO A 1 4297 ? 215.229 144.995 174.753 1.00 83.24  ? 4297 PRO A CD    1 
ATOM   21050 N  N     . ASP A 1 4298 ? 219.603 143.355 174.039 1.00 93.97  ? 4298 ASP A N     1 
ATOM   21051 C  CA    . ASP A 1 4298 ? 220.999 143.753 173.925 1.00 100.71 ? 4298 ASP A CA    1 
ATOM   21052 C  C     . ASP A 1 4298 ? 221.400 144.122 172.503 1.00 98.36  ? 4298 ASP A C     1 
ATOM   21053 O  O     . ASP A 1 4298 ? 222.547 144.524 172.285 1.00 95.93  ? 4298 ASP A O     1 
ATOM   21054 C  CB    . ASP A 1 4298 ? 221.909 142.633 174.439 1.00 102.58 ? 4298 ASP A CB    1 
ATOM   21055 C  CG    . ASP A 1 4298 ? 221.998 142.605 175.950 1.00 101.90 ? 4298 ASP A CG    1 
ATOM   21056 O  OD1   . ASP A 1 4298 ? 222.094 143.690 176.560 1.00 98.22  ? 4298 ASP A OD1   1 
ATOM   21057 O  OD2   . ASP A 1 4298 ? 221.970 141.498 176.527 1.00 102.21 ? 4298 ASP A OD2   1 
ATOM   21058 N  N     . GLY A 1 4299 ? 220.496 143.996 171.539 1.00 90.25  ? 4299 GLY A N     1 
ATOM   21059 C  CA    . GLY A 1 4299 ? 220.831 144.291 170.164 1.00 91.54  ? 4299 GLY A CA    1 
ATOM   21060 C  C     . GLY A 1 4299 ? 221.011 145.776 169.911 1.00 93.01  ? 4299 GLY A C     1 
ATOM   21061 O  O     . GLY A 1 4299 ? 220.615 146.636 170.697 1.00 93.85  ? 4299 GLY A O     1 
ATOM   21062 N  N     . ILE A 1 4300 ? 221.636 146.075 168.772 1.00 97.32  ? 4300 ILE A N     1 
ATOM   21063 C  CA    . ILE A 1 4300 ? 221.877 147.443 168.336 1.00 97.17  ? 4300 ILE A CA    1 
ATOM   21064 C  C     . ILE A 1 4300 ? 221.274 147.719 166.966 1.00 97.47  ? 4300 ILE A C     1 
ATOM   21065 O  O     . ILE A 1 4300 ? 221.485 148.795 166.406 1.00 102.97 ? 4300 ILE A O     1 
ATOM   21066 C  CB    . ILE A 1 4300 ? 223.383 147.776 168.348 1.00 99.67  ? 4300 ILE A CB    1 
ATOM   21067 C  CG1   . ILE A 1 4300 ? 224.126 146.967 167.281 1.00 100.40 ? 4300 ILE A CG1   1 
ATOM   21068 C  CG2   . ILE A 1 4300 ? 223.978 147.523 169.724 1.00 97.66  ? 4300 ILE A CG2   1 
ATOM   21069 C  CD1   . ILE A 1 4300 ? 224.569 147.784 166.082 1.00 98.38  ? 4300 ILE A CD1   1 
ATOM   21070 N  N     . ARG A 1 4301 ? 220.523 146.770 166.414 1.00 91.26  ? 4301 ARG A N     1 
ATOM   21071 C  CA    . ARG A 1 4301 ? 219.894 146.925 165.113 1.00 94.30  ? 4301 ARG A CA    1 
ATOM   21072 C  C     . ARG A 1 4301 ? 218.402 146.652 165.236 1.00 92.57  ? 4301 ARG A C     1 
ATOM   21073 O  O     . ARG A 1 4301 ? 217.942 146.022 166.192 1.00 96.35  ? 4301 ARG A O     1 
ATOM   21074 C  CB    . ARG A 1 4301 ? 220.515 145.992 164.064 1.00 96.26  ? 4301 ARG A CB    1 
ATOM   21075 C  CG    . ARG A 1 4301 ? 222.030 146.080 163.971 1.00 98.62  ? 4301 ARG A CG    1 
ATOM   21076 C  CD    . ARG A 1 4301 ? 222.572 145.362 162.740 1.00 97.20  ? 4301 ARG A CD    1 
ATOM   21077 N  NE    . ARG A 1 4301 ? 221.585 144.493 162.109 1.00 96.82  ? 4301 ARG A NE    1 
ATOM   21078 C  CZ    . ARG A 1 4301 ? 221.405 143.215 162.415 1.00 101.37 ? 4301 ARG A CZ    1 
ATOM   21079 N  NH1   . ARG A 1 4301 ? 222.130 142.619 163.347 1.00 100.82 ? 4301 ARG A NH1   1 
ATOM   21080 N  NH2   . ARG A 1 4301 ? 220.474 142.518 161.770 1.00 100.82 ? 4301 ARG A NH2   1 
ATOM   21081 N  N     . ARG A 1 4302 ? 217.649 147.142 164.249 1.00 82.51  ? 4302 ARG A N     1 
ATOM   21082 C  CA    . ARG A 1 4302 ? 216.197 147.006 164.287 1.00 82.05  ? 4302 ARG A CA    1 
ATOM   21083 C  C     . ARG A 1 4302 ? 215.775 145.543 164.256 1.00 84.80  ? 4302 ARG A C     1 
ATOM   21084 O  O     . ARG A 1 4302 ? 214.826 145.149 164.946 1.00 91.41  ? 4302 ARG A O     1 
ATOM   21085 C  CB    . ARG A 1 4302 ? 215.569 147.770 163.122 1.00 84.74  ? 4302 ARG A CB    1 
ATOM   21086 C  CG    . ARG A 1 4302 ? 214.109 147.430 162.873 1.00 86.83  ? 4302 ARG A CG    1 
ATOM   21087 C  CD    . ARG A 1 4302 ? 213.683 147.789 161.460 1.00 86.54  ? 4302 ARG A CD    1 
ATOM   21088 N  NE    . ARG A 1 4302 ? 212.263 147.540 161.242 1.00 87.29  ? 4302 ARG A NE    1 
ATOM   21089 C  CZ    . ARG A 1 4302 ? 211.737 146.343 161.022 1.00 87.98  ? 4302 ARG A CZ    1 
ATOM   21090 N  NH1   . ARG A 1 4302 ? 212.487 145.254 160.982 1.00 85.58  ? 4302 ARG A NH1   1 
ATOM   21091 N  NH2   . ARG A 1 4302 ? 210.424 146.236 160.836 1.00 85.47  ? 4302 ARG A NH2   1 
ATOM   21092 N  N     . GLU A 1 4303 ? 216.472 144.722 163.466 1.00 95.38  ? 4303 GLU A N     1 
ATOM   21093 C  CA    . GLU A 1 4303 ? 216.079 143.324 163.311 1.00 97.94  ? 4303 GLU A CA    1 
ATOM   21094 C  C     . GLU A 1 4303 ? 216.099 142.590 164.646 1.00 96.21  ? 4303 GLU A C     1 
ATOM   21095 O  O     . GLU A 1 4303 ? 215.193 141.802 164.941 1.00 99.77  ? 4303 GLU A O     1 
ATOM   21096 C  CB    . GLU A 1 4303 ? 216.997 142.628 162.306 1.00 100.51 ? 4303 GLU A CB    1 
ATOM   21097 C  CG    . GLU A 1 4303 ? 216.722 142.982 160.853 1.00 102.84 ? 4303 GLU A CG    1 
ATOM   21098 C  CD    . GLU A 1 4303 ? 217.304 144.326 160.458 1.00 105.70 ? 4303 GLU A CD    1 
ATOM   21099 O  OE1   . GLU A 1 4303 ? 218.366 144.697 161.000 1.00 105.67 ? 4303 GLU A OE1   1 
ATOM   21100 O  OE2   . GLU A 1 4303 ? 216.700 145.010 159.605 1.00 103.15 ? 4303 GLU A OE2   1 
ATOM   21101 N  N     . GLU A 1 4304 ? 217.122 142.836 165.466 1.00 90.35  ? 4304 GLU A N     1 
ATOM   21102 C  CA    . GLU A 1 4304 ? 217.198 142.184 166.769 1.00 89.30  ? 4304 GLU A CA    1 
ATOM   21103 C  C     . GLU A 1 4304 ? 216.038 142.599 167.666 1.00 90.81  ? 4304 GLU A C     1 
ATOM   21104 O  O     . GLU A 1 4304 ? 215.468 141.766 168.381 1.00 95.89  ? 4304 GLU A O     1 
ATOM   21105 C  CB    . GLU A 1 4304 ? 218.537 142.501 167.434 1.00 90.55  ? 4304 GLU A CB    1 
ATOM   21106 C  CG    . GLU A 1 4304 ? 219.732 142.334 166.510 1.00 95.67  ? 4304 GLU A CG    1 
ATOM   21107 C  CD    . GLU A 1 4304 ? 221.055 142.495 167.230 1.00 97.92  ? 4304 GLU A CD    1 
ATOM   21108 O  OE1   . GLU A 1 4304 ? 221.345 141.684 168.134 1.00 97.46  ? 4304 GLU A OE1   1 
ATOM   21109 O  OE2   . GLU A 1 4304 ? 221.806 143.435 166.893 1.00 95.65  ? 4304 GLU A OE2   1 
ATOM   21110 N  N     . PHE A 1 4305 ? 215.674 143.883 167.645 1.00 77.96  ? 4305 PHE A N     1 
ATOM   21111 C  CA    . PHE A 1 4305 ? 214.552 144.343 168.457 1.00 71.37  ? 4305 PHE A CA    1 
ATOM   21112 C  C     . PHE A 1 4305 ? 213.238 143.724 167.994 1.00 71.91  ? 4305 PHE A C     1 
ATOM   21113 O  O     . PHE A 1 4305 ? 212.409 143.330 168.822 1.00 81.05  ? 4305 PHE A O     1 
ATOM   21114 C  CB    . PHE A 1 4305 ? 214.470 145.868 168.431 1.00 69.38  ? 4305 PHE A CB    1 
ATOM   21115 C  CG    . PHE A 1 4305 ? 215.582 146.544 169.177 1.00 67.58  ? 4305 PHE A CG    1 
ATOM   21116 C  CD1   . PHE A 1 4305 ? 215.800 146.271 170.515 1.00 71.21  ? 4305 PHE A CD1   1 
ATOM   21117 C  CD2   . PHE A 1 4305 ? 216.407 147.455 168.543 1.00 73.69  ? 4305 PHE A CD2   1 
ATOM   21118 C  CE1   . PHE A 1 4305 ? 216.821 146.890 171.206 1.00 74.51  ? 4305 PHE A CE1   1 
ATOM   21119 C  CE2   . PHE A 1 4305 ? 217.429 148.077 169.228 1.00 77.59  ? 4305 PHE A CE2   1 
ATOM   21120 C  CZ    . PHE A 1 4305 ? 217.636 147.794 170.562 1.00 77.60  ? 4305 PHE A CZ    1 
ATOM   21121 N  N     . VAL A 1 4306 ? 213.027 143.629 166.679 1.00 71.86  ? 4306 VAL A N     1 
ATOM   21122 C  CA    . VAL A 1 4306 ? 211.805 143.000 166.182 1.00 74.16  ? 4306 VAL A CA    1 
ATOM   21123 C  C     . VAL A 1 4306 ? 211.775 141.523 166.555 1.00 75.70  ? 4306 VAL A C     1 
ATOM   21124 O  O     . VAL A 1 4306 ? 210.719 140.977 166.899 1.00 77.58  ? 4306 VAL A O     1 
ATOM   21125 C  CB    . VAL A 1 4306 ? 211.662 143.206 164.662 1.00 80.48  ? 4306 VAL A CB    1 
ATOM   21126 C  CG1   . VAL A 1 4306 ? 210.295 142.739 164.199 1.00 74.55  ? 4306 VAL A CG1   1 
ATOM   21127 C  CG2   . VAL A 1 4306 ? 211.845 144.667 164.310 1.00 82.66  ? 4306 VAL A CG2   1 
ATOM   21128 N  N     . GLN A 1 4307 ? 212.927 140.852 166.490 1.00 85.47  ? 4307 GLN A N     1 
ATOM   21129 C  CA    . GLN A 1 4307 ? 212.985 139.451 166.897 1.00 80.79  ? 4307 GLN A CA    1 
ATOM   21130 C  C     . GLN A 1 4307 ? 212.657 139.295 168.376 1.00 82.18  ? 4307 GLN A C     1 
ATOM   21131 O  O     . GLN A 1 4307 ? 211.945 138.363 168.767 1.00 89.11  ? 4307 GLN A O     1 
ATOM   21132 C  CB    . GLN A 1 4307 ? 214.363 138.867 166.587 1.00 81.22  ? 4307 GLN A CB    1 
ATOM   21133 C  CG    . GLN A 1 4307 ? 214.633 138.666 165.104 1.00 88.87  ? 4307 GLN A CG    1 
ATOM   21134 C  CD    . GLN A 1 4307 ? 215.978 138.020 164.839 1.00 92.66  ? 4307 GLN A CD    1 
ATOM   21135 O  OE1   . GLN A 1 4307 ? 217.026 138.623 165.069 1.00 94.19  ? 4307 GLN A OE1   1 
ATOM   21136 N  NE2   . GLN A 1 4307 ? 215.956 136.787 164.347 1.00 90.79  ? 4307 GLN A NE2   1 
ATOM   21137 N  N     . TRP A 1 4308 ? 213.174 140.196 169.216 1.00 79.26  ? 4308 TRP A N     1 
ATOM   21138 C  CA    . TRP A 1 4308 ? 212.858 140.143 170.640 1.00 77.53  ? 4308 TRP A CA    1 
ATOM   21139 C  C     . TRP A 1 4308 ? 211.374 140.376 170.887 1.00 71.44  ? 4308 TRP A C     1 
ATOM   21140 O  O     . TRP A 1 4308 ? 210.764 139.709 171.731 1.00 69.03  ? 4308 TRP A O     1 
ATOM   21141 C  CB    . TRP A 1 4308 ? 213.691 141.168 171.406 1.00 72.42  ? 4308 TRP A CB    1 
ATOM   21142 C  CG    . TRP A 1 4308 ? 213.393 141.191 172.872 1.00 74.01  ? 4308 TRP A CG    1 
ATOM   21143 C  CD1   . TRP A 1 4308 ? 213.998 140.448 173.841 1.00 78.81  ? 4308 TRP A CD1   1 
ATOM   21144 C  CD2   . TRP A 1 4308 ? 212.411 141.994 173.537 1.00 77.20  ? 4308 TRP A CD2   1 
ATOM   21145 N  NE1   . TRP A 1 4308 ? 213.457 140.739 175.069 1.00 78.44  ? 4308 TRP A NE1   1 
ATOM   21146 C  CE2   . TRP A 1 4308 ? 212.480 141.687 174.909 1.00 80.45  ? 4308 TRP A CE2   1 
ATOM   21147 C  CE3   . TRP A 1 4308 ? 211.483 142.946 173.105 1.00 74.31  ? 4308 TRP A CE3   1 
ATOM   21148 C  CZ2   . TRP A 1 4308 ? 211.657 142.295 175.852 1.00 75.65  ? 4308 TRP A CZ2   1 
ATOM   21149 C  CZ3   . TRP A 1 4308 ? 210.665 143.548 174.044 1.00 73.16  ? 4308 TRP A CZ3   1 
ATOM   21150 C  CH2   . TRP A 1 4308 ? 210.758 143.220 175.401 1.00 70.12  ? 4308 TRP A CH2   1 
ATOM   21151 N  N     . VAL A 1 4309 ? 210.777 141.328 170.165 1.00 75.08  ? 4309 VAL A N     1 
ATOM   21152 C  CA    . VAL A 1 4309 ? 209.347 141.588 170.311 1.00 72.52  ? 4309 VAL A CA    1 
ATOM   21153 C  C     . VAL A 1 4309 ? 208.539 140.363 169.904 1.00 76.50  ? 4309 VAL A C     1 
ATOM   21154 O  O     . VAL A 1 4309 ? 207.565 139.993 170.570 1.00 78.12  ? 4309 VAL A O     1 
ATOM   21155 C  CB    . VAL A 1 4309 ? 208.943 142.830 169.495 1.00 68.49  ? 4309 VAL A CB    1 
ATOM   21156 C  CG1   . VAL A 1 4309 ? 207.433 142.963 169.445 1.00 66.22  ? 4309 VAL A CG1   1 
ATOM   21157 C  CG2   . VAL A 1 4309 ? 209.562 144.078 170.097 1.00 72.83  ? 4309 VAL A CG2   1 
ATOM   21158 N  N     . GLU A 1 4310 ? 208.934 139.711 168.809 1.00 85.07  ? 4310 GLU A N     1 
ATOM   21159 C  CA    . GLU A 1 4310 ? 208.231 138.512 168.364 1.00 79.67  ? 4310 GLU A CA    1 
ATOM   21160 C  C     . GLU A 1 4310 ? 208.374 137.369 169.361 1.00 82.17  ? 4310 GLU A C     1 
ATOM   21161 O  O     . GLU A 1 4310 ? 207.584 136.419 169.328 1.00 83.65  ? 4310 GLU A O     1 
ATOM   21162 C  CB    . GLU A 1 4310 ? 208.746 138.082 166.991 1.00 84.78  ? 4310 GLU A CB    1 
ATOM   21163 C  CG    . GLU A 1 4310 ? 207.918 138.594 165.826 1.00 87.01  ? 4310 GLU A CG    1 
ATOM   21164 C  CD    . GLU A 1 4310 ? 208.721 138.697 164.544 1.00 90.79  ? 4310 GLU A CD    1 
ATOM   21165 O  OE1   . GLU A 1 4310 ? 209.780 138.042 164.450 1.00 89.89  ? 4310 GLU A OE1   1 
ATOM   21166 O  OE2   . GLU A 1 4310 ? 208.294 139.433 163.630 1.00 89.11  ? 4310 GLU A OE2   1 
ATOM   21167 N  N     . LEU A 1 4311 ? 209.366 137.437 170.246 1.00 75.40  ? 4311 LEU A N     1 
ATOM   21168 C  CA    . LEU A 1 4311 ? 209.620 136.391 171.227 1.00 74.11  ? 4311 LEU A CA    1 
ATOM   21169 C  C     . LEU A 1 4311 ? 209.000 136.685 172.587 1.00 76.51  ? 4311 LEU A C     1 
ATOM   21170 O  O     . LEU A 1 4311 ? 209.241 135.933 173.537 1.00 76.71  ? 4311 LEU A O     1 
ATOM   21171 C  CB    . LEU A 1 4311 ? 211.127 136.170 171.383 1.00 73.25  ? 4311 LEU A CB    1 
ATOM   21172 C  CG    . LEU A 1 4311 ? 211.843 135.408 170.265 1.00 73.83  ? 4311 LEU A CG    1 
ATOM   21173 C  CD1   . LEU A 1 4311 ? 213.034 134.645 170.822 1.00 76.15  ? 4311 LEU A CD1   1 
ATOM   21174 C  CD2   . LEU A 1 4311 ? 210.891 134.466 169.540 1.00 73.96  ? 4311 LEU A CD2   1 
ATOM   21175 N  N     . LEU A 1 4312 ? 208.224 137.757 172.708 1.00 81.47  ? 4312 LEU A N     1 
ATOM   21176 C  CA    . LEU A 1 4312 ? 207.586 138.069 173.977 1.00 79.93  ? 4312 LEU A CA    1 
ATOM   21177 C  C     . LEU A 1 4312 ? 206.577 136.980 174.337 1.00 83.58  ? 4312 LEU A C     1 
ATOM   21178 O  O     . LEU A 1 4312 ? 205.871 136.473 173.460 1.00 82.09  ? 4312 LEU A O     1 
ATOM   21179 C  CB    . LEU A 1 4312 ? 206.886 139.426 173.908 1.00 78.49  ? 4312 LEU A CB    1 
ATOM   21180 C  CG    . LEU A 1 4312 ? 207.658 140.645 174.417 1.00 77.05  ? 4312 LEU A CG    1 
ATOM   21181 C  CD1   . LEU A 1 4312 ? 206.756 141.867 174.465 1.00 74.99  ? 4312 LEU A CD1   1 
ATOM   21182 C  CD2   . LEU A 1 4312 ? 208.268 140.377 175.781 1.00 78.14  ? 4312 LEU A CD2   1 
ATOM   21183 N  N     . PRO A 1 4313 ? 206.492 136.594 175.609 1.00 89.06  ? 4313 PRO A N     1 
ATOM   21184 C  CA    . PRO A 1 4313 ? 205.535 135.554 175.999 1.00 85.98  ? 4313 PRO A CA    1 
ATOM   21185 C  C     . PRO A 1 4313 ? 204.099 136.007 175.803 1.00 82.70  ? 4313 PRO A C     1 
ATOM   21186 O  O     . PRO A 1 4313 ? 203.774 137.193 175.898 1.00 87.95  ? 4313 PRO A O     1 
ATOM   21187 C  CB    . PRO A 1 4313 ? 205.844 135.320 177.483 1.00 86.09  ? 4313 PRO A CB    1 
ATOM   21188 C  CG    . PRO A 1 4313 ? 207.201 135.911 177.703 1.00 88.04  ? 4313 PRO A CG    1 
ATOM   21189 C  CD    . PRO A 1 4313 ? 207.305 137.051 176.746 1.00 85.36  ? 4313 PRO A CD    1 
ATOM   21190 N  N     . ASP A 1 4314 ? 203.230 135.034 175.524 1.00 93.08  ? 4314 ASP A N     1 
ATOM   21191 C  CA    . ASP A 1 4314 ? 201.812 135.317 175.346 1.00 98.07  ? 4314 ASP A CA    1 
ATOM   21192 C  C     . ASP A 1 4314 ? 201.098 135.575 176.666 1.00 98.44  ? 4314 ASP A C     1 
ATOM   21193 O  O     . ASP A 1 4314 ? 199.965 136.067 176.652 1.00 97.28  ? 4314 ASP A O     1 
ATOM   21194 C  CB    . ASP A 1 4314 ? 201.141 134.156 174.609 1.00 100.99 ? 4314 ASP A CB    1 
ATOM   21195 C  CG    . ASP A 1 4314 ? 199.959 134.600 173.769 1.00 103.47 ? 4314 ASP A CG    1 
ATOM   21196 O  OD1   . ASP A 1 4314 ? 199.513 133.811 172.910 1.00 103.06 ? 4314 ASP A OD1   1 
ATOM   21197 O  OD2   . ASP A 1 4314 ? 199.481 135.737 173.958 1.00 103.85 ? 4314 ASP A OD2   1 
ATOM   21198 N  N     . THR A 1 4315 ? 201.729 135.263 177.798 1.00 101.11 ? 4315 THR A N     1 
ATOM   21199 C  CA    . THR A 1 4315 ? 201.117 135.455 179.113 1.00 102.68 ? 4315 THR A CA    1 
ATOM   21200 C  C     . THR A 1 4315 ? 201.316 136.905 179.549 1.00 101.69 ? 4315 THR A C     1 
ATOM   21201 O  O     . THR A 1 4315 ? 202.162 137.239 180.382 1.00 99.03  ? 4315 THR A O     1 
ATOM   21202 C  CB    . THR A 1 4315 ? 201.695 134.467 180.121 1.00 103.51 ? 4315 THR A CB    1 
ATOM   21203 O  OG1   . THR A 1 4315 ? 201.328 134.859 181.450 1.00 105.01 ? 4315 THR A OG1   1 
ATOM   21204 C  CG2   . THR A 1 4315 ? 203.216 134.378 180.000 1.00 100.55 ? 4315 THR A CG2   1 
ATOM   21205 N  N     . GLN A 1 4316 ? 200.501 137.784 178.972 1.00 92.20  ? 4316 GLN A N     1 
ATOM   21206 C  CA    . GLN A 1 4316 ? 200.557 139.204 179.281 1.00 88.95  ? 4316 GLN A CA    1 
ATOM   21207 C  C     . GLN A 1 4316 ? 199.588 139.534 180.408 1.00 90.31  ? 4316 GLN A C     1 
ATOM   21208 O  O     . GLN A 1 4316 ? 198.426 139.118 180.388 1.00 94.47  ? 4316 GLN A O     1 
ATOM   21209 C  CB    . GLN A 1 4316 ? 200.231 140.041 178.043 1.00 88.38  ? 4316 GLN A CB    1 
ATOM   21210 C  CG    . GLN A 1 4316 ? 200.465 141.532 178.219 1.00 85.64  ? 4316 GLN A CG    1 
ATOM   21211 C  CD    . GLN A 1 4316 ? 199.174 142.310 178.370 1.00 90.25  ? 4316 GLN A CD    1 
ATOM   21212 O  OE1   . GLN A 1 4316 ? 198.092 141.731 178.440 1.00 97.36  ? 4316 GLN A OE1   1 
ATOM   21213 N  NE2   . GLN A 1 4316 ? 199.283 143.632 178.416 1.00 86.59  ? 4316 GLN A NE2   1 
ATOM   21214 N  N     . THR A 1 4317 ? 200.073 140.284 181.385 1.00 87.51  ? 4317 THR A N     1 
ATOM   21215 C  CA    . THR A 1 4317 ? 199.322 140.662 182.570 1.00 85.48  ? 4317 THR A CA    1 
ATOM   21216 C  C     . THR A 1 4317 ? 199.412 142.167 182.759 1.00 85.85  ? 4317 THR A C     1 
ATOM   21217 O  O     . THR A 1 4317 ? 200.339 142.808 182.253 1.00 91.57  ? 4317 THR A O     1 
ATOM   21218 C  CB    . THR A 1 4317 ? 199.860 139.945 183.818 1.00 89.40  ? 4317 THR A CB    1 
ATOM   21219 O  OG1   . THR A 1 4317 ? 201.292 139.959 183.800 1.00 93.26  ? 4317 THR A OG1   1 
ATOM   21220 C  CG2   . THR A 1 4317 ? 199.372 138.507 183.857 1.00 90.08  ? 4317 THR A CG2   1 
ATOM   21221 N  N     . PRO A 1 4318 ? 198.457 142.767 183.476 1.00 74.06  ? 4318 PRO A N     1 
ATOM   21222 C  CA    . PRO A 1 4318 ? 198.510 144.223 183.687 1.00 73.48  ? 4318 PRO A CA    1 
ATOM   21223 C  C     . PRO A 1 4318 ? 199.755 144.691 184.419 1.00 77.22  ? 4318 PRO A C     1 
ATOM   21224 O  O     . PRO A 1 4318 ? 200.083 145.881 184.342 1.00 83.90  ? 4318 PRO A O     1 
ATOM   21225 C  CB    . PRO A 1 4318 ? 197.240 144.515 184.501 1.00 71.46  ? 4318 PRO A CB    1 
ATOM   21226 C  CG    . PRO A 1 4318 ? 196.737 143.186 184.963 1.00 79.04  ? 4318 PRO A CG    1 
ATOM   21227 C  CD    . PRO A 1 4318 ? 197.194 142.187 183.958 1.00 79.20  ? 4318 PRO A CD    1 
ATOM   21228 N  N     . SER A 1 4319 ? 200.457 143.804 185.129 1.00 69.73  ? 4319 SER A N     1 
ATOM   21229 C  CA    . SER A 1 4319 ? 201.708 144.197 185.767 1.00 68.49  ? 4319 SER A CA    1 
ATOM   21230 C  C     . SER A 1 4319 ? 202.782 144.564 184.753 1.00 73.44  ? 4319 SER A C     1 
ATOM   21231 O  O     . SER A 1 4319 ? 203.778 145.193 185.126 1.00 78.16  ? 4319 SER A O     1 
ATOM   21232 C  CB    . SER A 1 4319 ? 202.214 143.081 186.678 1.00 73.10  ? 4319 SER A CB    1 
ATOM   21233 O  OG    . SER A 1 4319 ? 202.159 141.826 186.025 1.00 81.90  ? 4319 SER A OG    1 
ATOM   21234 N  N     . TRP A 1 4320 ? 202.608 144.180 183.486 1.00 71.11  ? 4320 TRP A N     1 
ATOM   21235 C  CA    . TRP A 1 4320 ? 203.489 144.680 182.437 1.00 72.01  ? 4320 TRP A CA    1 
ATOM   21236 C  C     . TRP A 1 4320 ? 203.405 146.195 182.328 1.00 75.13  ? 4320 TRP A C     1 
ATOM   21237 O  O     . TRP A 1 4320 ? 204.403 146.853 182.013 1.00 78.82  ? 4320 TRP A O     1 
ATOM   21238 C  CB    . TRP A 1 4320 ? 203.131 144.041 181.096 1.00 71.51  ? 4320 TRP A CB    1 
ATOM   21239 C  CG    . TRP A 1 4320 ? 203.589 142.627 180.940 1.00 73.99  ? 4320 TRP A CG    1 
ATOM   21240 C  CD1   . TRP A 1 4320 ? 203.755 141.703 181.928 1.00 74.88  ? 4320 TRP A CD1   1 
ATOM   21241 C  CD2   . TRP A 1 4320 ? 203.928 141.969 179.714 1.00 76.20  ? 4320 TRP A CD2   1 
ATOM   21242 N  NE1   . TRP A 1 4320 ? 204.184 140.512 181.394 1.00 79.67  ? 4320 TRP A NE1   1 
ATOM   21243 C  CE2   . TRP A 1 4320 ? 204.297 140.650 180.036 1.00 80.36  ? 4320 TRP A CE2   1 
ATOM   21244 C  CE3   . TRP A 1 4320 ? 203.958 142.370 178.375 1.00 72.40  ? 4320 TRP A CE3   1 
ATOM   21245 C  CZ2   . TRP A 1 4320 ? 204.690 139.729 179.069 1.00 79.90  ? 4320 TRP A CZ2   1 
ATOM   21246 C  CZ3   . TRP A 1 4320 ? 204.348 141.455 177.418 1.00 70.53  ? 4320 TRP A CZ3   1 
ATOM   21247 C  CH2   . TRP A 1 4320 ? 204.709 140.150 177.769 1.00 76.65  ? 4320 TRP A CH2   1 
ATOM   21248 N  N     . LEU A 1 4321 ? 202.230 146.760 182.589 1.00 61.41  ? 4321 LEU A N     1 
ATOM   21249 C  CA    . LEU A 1 4321 ? 201.995 148.193 182.499 1.00 52.22  ? 4321 LEU A CA    1 
ATOM   21250 C  C     . LEU A 1 4321 ? 202.201 148.911 183.824 1.00 55.98  ? 4321 LEU A C     1 
ATOM   21251 O  O     . LEU A 1 4321 ? 201.948 150.117 183.905 1.00 62.16  ? 4321 LEU A O     1 
ATOM   21252 C  CB    . LEU A 1 4321 ? 200.576 148.459 181.987 1.00 52.91  ? 4321 LEU A CB    1 
ATOM   21253 C  CG    . LEU A 1 4321 ? 199.966 147.409 181.057 1.00 57.85  ? 4321 LEU A CG    1 
ATOM   21254 C  CD1   . LEU A 1 4321 ? 198.514 147.740 180.778 1.00 57.04  ? 4321 LEU A CD1   1 
ATOM   21255 C  CD2   . LEU A 1 4321 ? 200.743 147.301 179.757 1.00 59.68  ? 4321 LEU A CD2   1 
ATOM   21256 N  N     . GLY A 1 4322 ? 202.646 148.203 184.860 1.00 65.28  ? 4322 GLY A N     1 
ATOM   21257 C  CA    . GLY A 1 4322 ? 202.794 148.774 186.178 1.00 67.74  ? 4322 GLY A CA    1 
ATOM   21258 C  C     . GLY A 1 4322 ? 201.564 148.676 187.052 1.00 68.41  ? 4322 GLY A C     1 
ATOM   21259 O  O     . GLY A 1 4322 ? 201.661 148.918 188.260 1.00 73.91  ? 4322 GLY A O     1 
ATOM   21260 N  N     . LEU A 1 4323 ? 200.417 148.327 186.483 1.00 58.80  ? 4323 LEU A N     1 
ATOM   21261 C  CA    . LEU A 1 4323 ? 199.182 148.184 187.230 1.00 50.65  ? 4323 LEU A CA    1 
ATOM   21262 C  C     . LEU A 1 4323 ? 199.207 146.911 188.070 1.00 60.18  ? 4323 LEU A C     1 
ATOM   21263 O  O     . LEU A 1 4323 ? 199.994 145.999 187.808 1.00 66.54  ? 4323 LEU A O     1 
ATOM   21264 C  CB    . LEU A 1 4323 ? 197.998 148.159 186.269 1.00 51.17  ? 4323 LEU A CB    1 
ATOM   21265 C  CG    . LEU A 1 4323 ? 197.532 149.518 185.749 1.00 55.77  ? 4323 LEU A CG    1 
ATOM   21266 C  CD1   . LEU A 1 4323 ? 196.842 149.363 184.409 1.00 60.31  ? 4323 LEU A CD1   1 
ATOM   21267 C  CD2   . LEU A 1 4323 ? 196.612 150.180 186.754 1.00 68.24  ? 4323 LEU A CD2   1 
ATOM   21268 N  N     . PRO A 1 4324 ? 198.364 146.828 189.100 1.00 70.16  ? 4324 PRO A N     1 
ATOM   21269 C  CA    . PRO A 1 4324 ? 198.266 145.578 189.862 1.00 68.35  ? 4324 PRO A CA    1 
ATOM   21270 C  C     . PRO A 1 4324 ? 197.718 144.449 189.002 1.00 76.75  ? 4324 PRO A C     1 
ATOM   21271 O  O     . PRO A 1 4324 ? 196.959 144.670 188.056 1.00 83.60  ? 4324 PRO A O     1 
ATOM   21272 C  CB    . PRO A 1 4324 ? 197.308 145.931 191.006 1.00 70.03  ? 4324 PRO A CB    1 
ATOM   21273 C  CG    . PRO A 1 4324 ? 196.546 147.113 190.513 1.00 73.40  ? 4324 PRO A CG    1 
ATOM   21274 C  CD    . PRO A 1 4324 ? 197.513 147.884 189.672 1.00 75.11  ? 4324 PRO A CD    1 
ATOM   21275 N  N     . ASN A 1 4325 ? 198.117 143.222 189.346 1.00 85.85  ? 4325 ASN A N     1 
ATOM   21276 C  CA    . ASN A 1 4325 ? 197.737 142.054 188.558 1.00 83.16  ? 4325 ASN A CA    1 
ATOM   21277 C  C     . ASN A 1 4325 ? 196.233 141.813 188.538 1.00 85.04  ? 4325 ASN A C     1 
ATOM   21278 O  O     . ASN A 1 4325 ? 195.747 141.103 187.651 1.00 89.49  ? 4325 ASN A O     1 
ATOM   21279 C  CB    . ASN A 1 4325 ? 198.446 140.808 189.090 1.00 85.47  ? 4325 ASN A CB    1 
ATOM   21280 C  CG    . ASN A 1 4325 ? 199.893 140.731 188.655 1.00 89.55  ? 4325 ASN A CG    1 
ATOM   21281 O  OD1   . ASN A 1 4325 ? 200.802 140.686 189.484 1.00 90.86  ? 4325 ASN A OD1   1 
ATOM   21282 N  ND2   . ASN A 1 4325 ? 200.115 140.703 187.347 1.00 86.99  ? 4325 ASN A ND2   1 
ATOM   21283 N  N     . ASN A 1 4326 ? 195.488 142.379 189.483 1.00 84.97  ? 4326 ASN A N     1 
ATOM   21284 C  CA    . ASN A 1 4326 ? 194.052 142.154 189.569 1.00 85.63  ? 4326 ASN A CA    1 
ATOM   21285 C  C     . ASN A 1 4326 ? 193.231 143.243 188.892 1.00 86.53  ? 4326 ASN A C     1 
ATOM   21286 O  O     . ASN A 1 4326 ? 192.005 143.253 189.038 1.00 90.66  ? 4326 ASN A O     1 
ATOM   21287 C  CB    . ASN A 1 4326 ? 193.625 142.023 191.034 1.00 88.46  ? 4326 ASN A CB    1 
ATOM   21288 C  CG    . ASN A 1 4326 ? 194.009 143.231 191.867 1.00 92.05  ? 4326 ASN A CG    1 
ATOM   21289 O  OD1   . ASN A 1 4326 ? 194.405 144.269 191.340 1.00 92.96  ? 4326 ASN A OD1   1 
ATOM   21290 N  ND2   . ASN A 1 4326 ? 193.892 143.098 193.181 1.00 95.15  ? 4326 ASN A ND2   1 
ATOM   21291 N  N     . ALA A 1 4327 ? 193.872 144.164 188.168 1.00 84.45  ? 4327 ALA A N     1 
ATOM   21292 C  CA    . ALA A 1 4327 ? 193.125 145.221 187.496 1.00 87.53  ? 4327 ALA A CA    1 
ATOM   21293 C  C     . ALA A 1 4327 ? 192.256 144.671 186.373 1.00 91.02  ? 4327 ALA A C     1 
ATOM   21294 O  O     . ALA A 1 4327 ? 191.205 145.244 186.064 1.00 93.27  ? 4327 ALA A O     1 
ATOM   21295 C  CB    . ALA A 1 4327 ? 194.083 146.280 186.955 1.00 82.01  ? 4327 ALA A CB    1 
ATOM   21296 N  N     . GLU A 1 4328 ? 192.672 143.568 185.752 1.00 88.78  ? 4328 GLU A N     1 
ATOM   21297 C  CA    . GLU A 1 4328 ? 191.921 142.981 184.652 1.00 88.18  ? 4328 GLU A CA    1 
ATOM   21298 C  C     . GLU A 1 4328 ? 190.951 141.896 185.097 1.00 96.97  ? 4328 GLU A C     1 
ATOM   21299 O  O     . GLU A 1 4328 ? 190.276 141.307 184.246 1.00 103.55 ? 4328 GLU A O     1 
ATOM   21300 C  CB    . GLU A 1 4328 ? 192.880 142.393 183.613 1.00 89.02  ? 4328 GLU A CB    1 
ATOM   21301 C  CG    . GLU A 1 4328 ? 193.596 141.135 184.077 1.00 88.38  ? 4328 GLU A CG    1 
ATOM   21302 C  CD    . GLU A 1 4328 ? 194.288 140.405 182.944 1.00 96.63  ? 4328 GLU A CD    1 
ATOM   21303 O  OE1   . GLU A 1 4328 ? 194.223 140.890 181.795 1.00 100.39 ? 4328 GLU A OE1   1 
ATOM   21304 O  OE2   . GLU A 1 4328 ? 194.897 139.345 183.201 1.00 94.56  ? 4328 GLU A OE2   1 
ATOM   21305 N  N     . ARG A 1 4329 ? 190.865 141.618 186.399 1.00 96.30  ? 4329 ARG A N     1 
ATOM   21306 C  CA    . ARG A 1 4329 ? 190.046 140.512 186.882 1.00 90.68  ? 4329 ARG A CA    1 
ATOM   21307 C  C     . ARG A 1 4329 ? 188.569 140.736 186.573 1.00 90.80  ? 4329 ARG A C     1 
ATOM   21308 O  O     . ARG A 1 4329 ? 187.903 139.880 185.977 1.00 96.29  ? 4329 ARG A O     1 
ATOM   21309 C  CB    . ARG A 1 4329 ? 190.265 140.336 188.386 1.00 90.14  ? 4329 ARG A CB    1 
ATOM   21310 C  CG    . ARG A 1 4329 ? 189.349 139.327 189.050 1.00 89.74  ? 4329 ARG A CG    1 
ATOM   21311 C  CD    . ARG A 1 4329 ? 189.816 139.037 190.467 1.00 91.96  ? 4329 ARG A CD    1 
ATOM   21312 N  NE    . ARG A 1 4329 ? 191.175 138.510 190.494 1.00 95.22  ? 4329 ARG A NE    1 
ATOM   21313 C  CZ    . ARG A 1 4329 ? 191.519 137.348 191.031 1.00 96.64  ? 4329 ARG A CZ    1 
ATOM   21314 N  NH1   . ARG A 1 4329 ? 190.624 136.557 191.599 1.00 95.21  ? 4329 ARG A NH1   1 
ATOM   21315 N  NH2   . ARG A 1 4329 ? 192.794 136.971 190.998 1.00 94.11  ? 4329 ARG A NH2   1 
ATOM   21316 N  N     . VAL A 1 4330 ? 188.044 141.899 186.963 1.00 85.70  ? 4330 VAL A N     1 
ATOM   21317 C  CA    . VAL A 1 4330 ? 186.630 142.191 186.742 1.00 88.23  ? 4330 VAL A CA    1 
ATOM   21318 C  C     . VAL A 1 4330 ? 186.344 142.332 185.252 1.00 91.58  ? 4330 VAL A C     1 
ATOM   21319 O  O     . VAL A 1 4330 ? 185.303 141.885 184.754 1.00 96.67  ? 4330 VAL A O     1 
ATOM   21320 C  CB    . VAL A 1 4330 ? 186.213 143.449 187.527 1.00 87.67  ? 4330 VAL A CB    1 
ATOM   21321 C  CG1   . VAL A 1 4330 ? 187.218 144.571 187.315 1.00 89.48  ? 4330 VAL A CG1   1 
ATOM   21322 C  CG2   . VAL A 1 4330 ? 184.814 143.892 187.131 1.00 88.09  ? 4330 VAL A CG2   1 
ATOM   21323 N  N     . LEU A 1 4331 ? 187.270 142.951 184.516 1.00 88.28  ? 4331 LEU A N     1 
ATOM   21324 C  CA    . LEU A 1 4331 ? 187.099 143.099 183.075 1.00 88.41  ? 4331 LEU A CA    1 
ATOM   21325 C  C     . LEU A 1 4331 ? 187.056 141.741 182.387 1.00 88.89  ? 4331 LEU A C     1 
ATOM   21326 O  O     . LEU A 1 4331 ? 186.222 141.502 181.507 1.00 91.62  ? 4331 LEU A O     1 
ATOM   21327 C  CB    . LEU A 1 4331 ? 188.225 143.962 182.503 1.00 89.56  ? 4331 LEU A CB    1 
ATOM   21328 C  CG    . LEU A 1 4331 ? 188.034 144.521 181.092 1.00 91.11  ? 4331 LEU A CG    1 
ATOM   21329 C  CD1   . LEU A 1 4331 ? 186.565 144.796 180.803 1.00 89.57  ? 4331 LEU A CD1   1 
ATOM   21330 C  CD2   . LEU A 1 4331 ? 188.862 145.781 180.909 1.00 90.60  ? 4331 LEU A CD2   1 
ATOM   21331 N  N     . LEU A 1 4332 ? 187.949 140.832 182.784 1.00 82.79  ? 4332 LEU A N     1 
ATOM   21332 C  CA    . LEU A 1 4332 ? 187.956 139.495 182.200 1.00 81.78  ? 4332 LEU A CA    1 
ATOM   21333 C  C     . LEU A 1 4332 ? 186.689 138.728 182.559 1.00 85.71  ? 4332 LEU A C     1 
ATOM   21334 O  O     . LEU A 1 4332 ? 186.140 137.992 181.731 1.00 93.57  ? 4332 LEU A O     1 
ATOM   21335 C  CB    . LEU A 1 4332 ? 189.198 138.728 182.652 1.00 80.03  ? 4332 LEU A CB    1 
ATOM   21336 C  CG    . LEU A 1 4332 ? 190.497 139.077 181.925 1.00 84.14  ? 4332 LEU A CG    1 
ATOM   21337 C  CD1   . LEU A 1 4332 ? 191.570 138.045 182.226 1.00 86.79  ? 4332 LEU A CD1   1 
ATOM   21338 C  CD2   . LEU A 1 4332 ? 190.263 139.191 180.427 1.00 83.25  ? 4332 LEU A CD2   1 
ATOM   21339 N  N     . THR A 1 4333 ? 186.212 138.879 183.797 1.00 80.07  ? 4333 THR A N     1 
ATOM   21340 C  CA    . THR A 1 4333 ? 184.970 138.221 184.192 1.00 80.56  ? 4333 THR A CA    1 
ATOM   21341 C  C     . THR A 1 4333 ? 183.796 138.716 183.353 1.00 83.93  ? 4333 THR A C     1 
ATOM   21342 O  O     . THR A 1 4333 ? 182.976 137.924 182.868 1.00 89.23  ? 4333 THR A O     1 
ATOM   21343 C  CB    . THR A 1 4333 ? 184.703 138.457 185.679 1.00 82.23  ? 4333 THR A CB    1 
ATOM   21344 O  OG1   . THR A 1 4333 ? 185.800 137.951 186.449 1.00 89.61  ? 4333 THR A OG1   1 
ATOM   21345 C  CG2   . THR A 1 4333 ? 183.424 137.758 186.108 1.00 86.25  ? 4333 THR A CG2   1 
ATOM   21346 N  N     . THR A 1 4334 ? 183.710 140.035 183.164 1.00 84.32  ? 4334 THR A N     1 
ATOM   21347 C  CA    . THR A 1 4334 ? 182.634 140.603 182.358 1.00 83.54  ? 4334 THR A CA    1 
ATOM   21348 C  C     . THR A 1 4334 ? 182.742 140.149 180.908 1.00 83.61  ? 4334 THR A C     1 
ATOM   21349 O  O     . THR A 1 4334 ? 181.731 139.859 180.259 1.00 85.25  ? 4334 THR A O     1 
ATOM   21350 C  CB    . THR A 1 4334 ? 182.658 142.129 182.451 1.00 87.53  ? 4334 THR A CB    1 
ATOM   21351 O  OG1   . THR A 1 4334 ? 182.512 142.527 183.819 1.00 92.06  ? 4334 THR A OG1   1 
ATOM   21352 C  CG2   . THR A 1 4334 ? 181.526 142.731 181.635 1.00 86.89  ? 4334 THR A CG2   1 
ATOM   21353 N  N     . GLN A 1 4335 ? 183.966 140.077 180.380 1.00 85.33  ? 4335 GLN A N     1 
ATOM   21354 C  CA    . GLN A 1 4335 ? 184.153 139.619 179.008 1.00 84.11  ? 4335 GLN A CA    1 
ATOM   21355 C  C     . GLN A 1 4335 ? 183.754 138.156 178.852 1.00 87.33  ? 4335 GLN A C     1 
ATOM   21356 O  O     . GLN A 1 4335 ? 183.179 137.770 177.829 1.00 94.68  ? 4335 GLN A O     1 
ATOM   21357 C  CB    . GLN A 1 4335 ? 185.602 139.835 178.574 1.00 82.92  ? 4335 GLN A CB    1 
ATOM   21358 C  CG    . GLN A 1 4335 ? 185.892 141.250 178.103 1.00 88.95  ? 4335 GLN A CG    1 
ATOM   21359 C  CD    . GLN A 1 4335 ? 187.271 141.390 177.493 1.00 91.04  ? 4335 GLN A CD    1 
ATOM   21360 O  OE1   . GLN A 1 4335 ? 188.274 141.441 178.203 1.00 92.58  ? 4335 GLN A OE1   1 
ATOM   21361 N  NE2   . GLN A 1 4335 ? 187.327 141.455 176.168 1.00 90.11  ? 4335 GLN A NE2   1 
ATOM   21362 N  N     . GLY A 1 4336 ? 184.055 137.326 179.851 1.00 84.62  ? 4336 GLY A N     1 
ATOM   21363 C  CA    . GLY A 1 4336 ? 183.624 135.937 179.797 1.00 84.08  ? 4336 GLY A CA    1 
ATOM   21364 C  C     . GLY A 1 4336 ? 182.114 135.798 179.841 1.00 83.15  ? 4336 GLY A C     1 
ATOM   21365 O  O     . GLY A 1 4336 ? 181.525 134.993 179.111 1.00 84.87  ? 4336 GLY A O     1 
ATOM   21366 N  N     . VAL A 1 4337 ? 181.465 136.585 180.703 1.00 84.66  ? 4337 VAL A N     1 
ATOM   21367 C  CA    . VAL A 1 4337 ? 180.004 136.581 180.751 1.00 85.38  ? 4337 VAL A CA    1 
ATOM   21368 C  C     . VAL A 1 4337 ? 179.428 137.028 179.411 1.00 85.29  ? 4337 VAL A C     1 
ATOM   21369 O  O     . VAL A 1 4337 ? 178.445 136.461 178.916 1.00 90.89  ? 4337 VAL A O     1 
ATOM   21370 C  CB    . VAL A 1 4337 ? 179.506 137.463 181.910 1.00 84.26  ? 4337 VAL A CB    1 
ATOM   21371 C  CG1   . VAL A 1 4337 ? 178.009 137.697 181.801 1.00 81.02  ? 4337 VAL A CG1   1 
ATOM   21372 C  CG2   . VAL A 1 4337 ? 179.850 136.822 183.244 1.00 87.03  ? 4337 VAL A CG2   1 
ATOM   21373 N  N     . ASP A 1 4338 ? 180.035 138.048 178.801 1.00 83.81  ? 4338 ASP A N     1 
ATOM   21374 C  CA    . ASP A 1 4338 ? 179.577 138.515 177.498 1.00 80.88  ? 4338 ASP A CA    1 
ATOM   21375 C  C     . ASP A 1 4338 ? 179.768 137.448 176.429 1.00 79.87  ? 4338 ASP A C     1 
ATOM   21376 O  O     . ASP A 1 4338 ? 178.928 137.300 175.537 1.00 83.99  ? 4338 ASP A O     1 
ATOM   21377 C  CB    . ASP A 1 4338 ? 180.311 139.799 177.112 1.00 86.35  ? 4338 ASP A CB    1 
ATOM   21378 C  CG    . ASP A 1 4338 ? 179.485 141.041 177.375 1.00 90.92  ? 4338 ASP A CG    1 
ATOM   21379 O  OD1   . ASP A 1 4338 ? 178.314 140.900 177.786 1.00 92.65  ? 4338 ASP A OD1   1 
ATOM   21380 O  OD2   . ASP A 1 4338 ? 180.006 142.158 177.173 1.00 88.53  ? 4338 ASP A OD2   1 
ATOM   21381 N  N     . MET A 1 4339 ? 180.877 136.709 176.488 1.00 74.98  ? 4339 MET A N     1 
ATOM   21382 C  CA    . MET A 1 4339 ? 181.092 135.622 175.538 1.00 71.00  ? 4339 MET A CA    1 
ATOM   21383 C  C     . MET A 1 4339 ? 180.026 134.548 175.700 1.00 75.36  ? 4339 MET A C     1 
ATOM   21384 O  O     . MET A 1 4339 ? 179.512 134.009 174.712 1.00 81.45  ? 4339 MET A O     1 
ATOM   21385 C  CB    . MET A 1 4339 ? 182.489 135.027 175.719 1.00 70.75  ? 4339 MET A CB    1 
ATOM   21386 C  CG    . MET A 1 4339 ? 182.598 133.570 175.299 1.00 70.34  ? 4339 MET A CG    1 
ATOM   21387 S  SD    . MET A 1 4339 ? 184.150 132.797 175.788 1.00 94.73  ? 4339 MET A SD    1 
ATOM   21388 C  CE    . MET A 1 4339 ? 183.606 131.795 177.169 1.00 83.21  ? 4339 MET A CE    1 
ATOM   21389 N  N     . ILE A 1 4340 ? 179.679 134.226 176.948 1.00 82.52  ? 4340 ILE A N     1 
ATOM   21390 C  CA    . ILE A 1 4340 ? 178.603 133.269 177.200 1.00 79.53  ? 4340 ILE A CA    1 
ATOM   21391 C  C     . ILE A 1 4340 ? 177.301 133.770 176.589 1.00 75.94  ? 4340 ILE A C     1 
ATOM   21392 O  O     . ILE A 1 4340 ? 176.573 133.022 175.922 1.00 81.58  ? 4340 ILE A O     1 
ATOM   21393 C  CB    . ILE A 1 4340 ? 178.452 133.016 178.710 1.00 76.45  ? 4340 ILE A CB    1 
ATOM   21394 C  CG1   . ILE A 1 4340 ? 179.646 132.227 179.242 1.00 75.66  ? 4340 ILE A CG1   1 
ATOM   21395 C  CG2   . ILE A 1 4340 ? 177.156 132.277 179.000 1.00 73.09  ? 4340 ILE A CG2   1 
ATOM   21396 C  CD1   . ILE A 1 4340 ? 179.995 131.036 178.399 1.00 79.14  ? 4340 ILE A CD1   1 
ATOM   21397 N  N     . SER A 1 4341 ? 176.996 135.051 176.799 1.00 77.75  ? 4341 SER A N     1 
ATOM   21398 C  CA    . SER A 1 4341 ? 175.758 135.619 176.274 1.00 76.47  ? 4341 SER A CA    1 
ATOM   21399 C  C     . SER A 1 4341 ? 175.733 135.581 174.750 1.00 78.20  ? 4341 SER A C     1 
ATOM   21400 O  O     . SER A 1 4341 ? 174.706 135.261 174.143 1.00 83.76  ? 4341 SER A O     1 
ATOM   21401 C  CB    . SER A 1 4341 ? 175.583 137.050 176.781 1.00 80.84  ? 4341 SER A CB    1 
ATOM   21402 O  OG    . SER A 1 4341 ? 175.665 137.104 178.194 1.00 88.71  ? 4341 SER A OG    1 
ATOM   21403 N  N     . LYS A 1 4342 ? 176.858 135.915 174.114 1.00 71.38  ? 4342 LYS A N     1 
ATOM   21404 C  CA    . LYS A 1 4342 ? 176.913 135.924 172.655 1.00 69.10  ? 4342 LYS A CA    1 
ATOM   21405 C  C     . LYS A 1 4342 ? 176.783 134.516 172.089 1.00 72.86  ? 4342 LYS A C     1 
ATOM   21406 O  O     . LYS A 1 4342 ? 176.097 134.301 171.083 1.00 80.30  ? 4342 LYS A O     1 
ATOM   21407 C  CB    . LYS A 1 4342 ? 178.207 136.583 172.179 1.00 69.08  ? 4342 LYS A CB    1 
ATOM   21408 C  CG    . LYS A 1 4342 ? 178.333 138.044 172.568 1.00 72.53  ? 4342 LYS A CG    1 
ATOM   21409 C  CD    . LYS A 1 4342 ? 179.713 138.587 172.246 1.00 72.98  ? 4342 LYS A CD    1 
ATOM   21410 C  CE    . LYS A 1 4342 ? 179.962 139.898 172.968 1.00 70.76  ? 4342 LYS A CE    1 
ATOM   21411 N  NZ    . LYS A 1 4342 ? 178.827 140.845 172.799 1.00 76.00  ? 4342 LYS A NZ    1 
ATOM   21412 N  N     . MET A 1 4343 ? 177.441 133.538 172.718 1.00 76.14  ? 4343 MET A N     1 
ATOM   21413 C  CA    . MET A 1 4343 ? 177.297 132.160 172.268 1.00 76.93  ? 4343 MET A CA    1 
ATOM   21414 C  C     . MET A 1 4343 ? 175.882 131.639 172.470 1.00 84.08  ? 4343 MET A C     1 
ATOM   21415 O  O     . MET A 1 4343 ? 175.418 130.817 171.673 1.00 86.99  ? 4343 MET A O     1 
ATOM   21416 C  CB    . MET A 1 4343 ? 178.294 131.252 172.988 1.00 75.51  ? 4343 MET A CB    1 
ATOM   21417 C  CG    . MET A 1 4343 ? 179.747 131.538 172.650 1.00 80.39  ? 4343 MET A CG    1 
ATOM   21418 S  SD    . MET A 1 4343 ? 180.876 130.232 173.169 1.00 100.34 ? 4343 MET A SD    1 
ATOM   21419 C  CE    . MET A 1 4343 ? 179.782 128.815 173.182 1.00 85.57  ? 4343 MET A CE    1 
ATOM   21420 N  N     . LEU A 1 4344 ? 175.189 132.095 173.512 1.00 84.62  ? 4344 LEU A N     1 
ATOM   21421 C  CA    . LEU A 1 4344 ? 173.800 131.711 173.721 1.00 78.59  ? 4344 LEU A CA    1 
ATOM   21422 C  C     . LEU A 1 4344 ? 172.840 132.384 172.751 1.00 78.01  ? 4344 LEU A C     1 
ATOM   21423 O  O     . LEU A 1 4344 ? 171.863 131.754 172.331 1.00 83.20  ? 4344 LEU A O     1 
ATOM   21424 C  CB    . LEU A 1 4344 ? 173.375 132.035 175.155 1.00 79.33  ? 4344 LEU A CB    1 
ATOM   21425 C  CG    . LEU A 1 4344 ? 171.972 131.576 175.545 1.00 81.94  ? 4344 LEU A CG    1 
ATOM   21426 C  CD1   . LEU A 1 4344 ? 171.998 130.111 175.927 1.00 82.41  ? 4344 LEU A CD1   1 
ATOM   21427 C  CD2   . LEU A 1 4344 ? 171.427 132.423 176.684 1.00 81.85  ? 4344 LEU A CD2   1 
ATOM   21428 N  N     . LYS A 1 4345 ? 173.097 133.637 172.378 1.00 72.88  ? 4345 LYS A N     1 
ATOM   21429 C  CA    . LYS A 1 4345 ? 172.189 134.387 171.521 1.00 76.34  ? 4345 LYS A CA    1 
ATOM   21430 C  C     . LYS A 1 4345 ? 172.153 133.875 170.088 1.00 77.86  ? 4345 LYS A C     1 
ATOM   21431 O  O     . LYS A 1 4345 ? 171.268 134.281 169.328 1.00 84.20  ? 4345 LYS A O     1 
ATOM   21432 C  CB    . LYS A 1 4345 ? 172.574 135.868 171.519 1.00 73.44  ? 4345 LYS A CB    1 
ATOM   21433 C  CG    . LYS A 1 4345 ? 171.403 136.814 171.314 1.00 72.09  ? 4345 LYS A CG    1 
ATOM   21434 C  CD    . LYS A 1 4345 ? 171.857 138.265 171.281 1.00 71.99  ? 4345 LYS A CD    1 
ATOM   21435 C  CE    . LYS A 1 4345 ? 172.854 138.564 172.387 1.00 74.42  ? 4345 LYS A CE    1 
ATOM   21436 N  NZ    . LYS A 1 4345 ? 173.566 139.850 172.152 1.00 77.78  ? 4345 LYS A NZ    1 
ATOM   21437 N  N     . MET A 1 4346 ? 173.081 133.003 169.699 1.00 73.91  ? 4346 MET A N     1 
ATOM   21438 C  CA    . MET A 1 4346 ? 173.142 132.490 168.338 1.00 75.00  ? 4346 MET A CA    1 
ATOM   21439 C  C     . MET A 1 4346 ? 172.775 131.015 168.247 1.00 81.31  ? 4346 MET A C     1 
ATOM   21440 O  O     . MET A 1 4346 ? 173.162 130.349 167.281 1.00 82.82  ? 4346 MET A O     1 
ATOM   21441 C  CB    . MET A 1 4346 ? 174.532 132.724 167.748 1.00 71.17  ? 4346 MET A CB    1 
ATOM   21442 C  CG    . MET A 1 4346 ? 175.041 134.140 167.931 1.00 74.43  ? 4346 MET A CG    1 
ATOM   21443 S  SD    . MET A 1 4346 ? 176.836 134.226 167.897 1.00 87.97  ? 4346 MET A SD    1 
ATOM   21444 C  CE    . MET A 1 4346 ? 177.119 134.105 166.136 1.00 65.59  ? 4346 MET A CE    1 
ATOM   21445 N  N     . GLN A 1 4347 ? 172.043 130.489 169.223 1.00 83.14  ? 4347 GLN A N     1 
ATOM   21446 C  CA    . GLN A 1 4347 ? 171.605 129.100 169.182 1.00 81.26  ? 4347 GLN A CA    1 
ATOM   21447 C  C     . GLN A 1 4347 ? 170.266 128.975 168.464 1.00 78.44  ? 4347 GLN A C     1 
ATOM   21448 O  O     . GLN A 1 4347 ? 169.657 129.977 168.087 1.00 73.90  ? 4347 GLN A O     1 
ATOM   21449 C  CB    . GLN A 1 4347 ? 171.501 128.527 170.596 1.00 77.65  ? 4347 GLN A CB    1 
ATOM   21450 C  CG    . GLN A 1 4347 ? 172.832 128.415 171.317 1.00 80.24  ? 4347 GLN A CG    1 
ATOM   21451 C  CD    . GLN A 1 4347 ? 173.802 127.493 170.605 1.00 84.88  ? 4347 GLN A CD    1 
ATOM   21452 O  OE1   . GLN A 1 4347 ? 174.801 127.939 170.042 1.00 86.47  ? 4347 GLN A OE1   1 
ATOM   21453 N  NE2   . GLN A 1 4347 ? 173.509 126.198 170.625 1.00 82.20  ? 4347 GLN A NE2   1 
ATOM   21454 N  N     . PRO A 1 4374 ? 146.409 146.472 186.248 1.00 139.45 ? 4374 PRO A N     1 
ATOM   21455 C  CA    . PRO A 1 4374 ? 147.425 145.795 185.440 1.00 141.55 ? 4374 PRO A CA    1 
ATOM   21456 C  C     . PRO A 1 4374 ? 148.640 145.369 186.259 1.00 142.73 ? 4374 PRO A C     1 
ATOM   21457 O  O     . PRO A 1 4374 ? 148.790 145.794 187.404 1.00 142.32 ? 4374 PRO A O     1 
ATOM   21458 C  CB    . PRO A 1 4374 ? 147.804 146.856 184.403 1.00 138.78 ? 4374 PRO A CB    1 
ATOM   21459 C  CG    . PRO A 1 4374 ? 146.612 147.804 184.343 1.00 136.99 ? 4374 PRO A CG    1 
ATOM   21460 C  CD    . PRO A 1 4374 ? 145.650 147.447 185.450 1.00 138.05 ? 4374 PRO A CD    1 
ATOM   21461 N  N     . ALA A 1 4375 ? 149.495 144.531 185.668 1.00 142.30 ? 4375 ALA A N     1 
ATOM   21462 C  CA    . ALA A 1 4375 ? 150.639 143.995 186.399 1.00 142.34 ? 4375 ALA A CA    1 
ATOM   21463 C  C     . ALA A 1 4375 ? 151.660 145.083 186.713 1.00 143.51 ? 4375 ALA A C     1 
ATOM   21464 O  O     . ALA A 1 4375 ? 152.147 145.182 187.847 1.00 141.81 ? 4375 ALA A O     1 
ATOM   21465 C  CB    . ALA A 1 4375 ? 151.286 142.863 185.601 1.00 139.45 ? 4375 ALA A CB    1 
ATOM   21466 N  N     . TRP A 1 4376 ? 152.004 145.904 185.716 1.00 140.46 ? 4376 TRP A N     1 
ATOM   21467 C  CA    . TRP A 1 4376 ? 153.005 146.941 185.936 1.00 137.91 ? 4376 TRP A CA    1 
ATOM   21468 C  C     . TRP A 1 4376 ? 152.530 147.965 186.958 1.00 137.38 ? 4376 TRP A C     1 
ATOM   21469 O  O     . TRP A 1 4376 ? 153.337 148.463 187.749 1.00 138.00 ? 4376 TRP A O     1 
ATOM   21470 C  CB    . TRP A 1 4376 ? 153.375 147.614 184.609 1.00 136.59 ? 4376 TRP A CB    1 
ATOM   21471 C  CG    . TRP A 1 4376 ? 152.412 148.665 184.121 1.00 138.73 ? 4376 TRP A CG    1 
ATOM   21472 C  CD1   . TRP A 1 4376 ? 151.472 148.521 183.142 1.00 140.92 ? 4376 TRP A CD1   1 
ATOM   21473 C  CD2   . TRP A 1 4376 ? 152.334 150.033 184.549 1.00 138.46 ? 4376 TRP A CD2   1 
ATOM   21474 N  NE1   . TRP A 1 4376 ? 150.795 149.701 182.957 1.00 142.52 ? 4376 TRP A NE1   1 
ATOM   21475 C  CE2   . TRP A 1 4376 ? 151.306 150.645 183.807 1.00 139.36 ? 4376 TRP A CE2   1 
ATOM   21476 C  CE3   . TRP A 1 4376 ? 153.024 150.793 185.499 1.00 138.51 ? 4376 TRP A CE3   1 
ATOM   21477 C  CZ2   . TRP A 1 4376 ? 150.953 151.981 183.982 1.00 136.90 ? 4376 TRP A CZ2   1 
ATOM   21478 C  CZ3   . TRP A 1 4376 ? 152.670 152.116 185.673 1.00 136.56 ? 4376 TRP A CZ3   1 
ATOM   21479 C  CH2   . TRP A 1 4376 ? 151.645 152.698 184.918 1.00 137.13 ? 4376 TRP A CH2   1 
ATOM   21480 N  N     . MET A 1 4377 ? 151.233 148.283 186.963 1.00 142.70 ? 4377 MET A N     1 
ATOM   21481 C  CA    . MET A 1 4377 ? 150.709 149.230 187.942 1.00 144.98 ? 4377 MET A CA    1 
ATOM   21482 C  C     . MET A 1 4377 ? 150.906 148.714 189.361 1.00 147.93 ? 4377 MET A C     1 
ATOM   21483 O  O     . MET A 1 4377 ? 151.368 149.448 190.241 1.00 149.20 ? 4377 MET A O     1 
ATOM   21484 C  CB    . MET A 1 4377 ? 149.231 149.507 187.669 1.00 143.52 ? 4377 MET A CB    1 
ATOM   21485 C  CG    . MET A 1 4377 ? 148.975 150.389 186.459 1.00 144.62 ? 4377 MET A CG    1 
ATOM   21486 S  SD    . MET A 1 4377 ? 147.231 150.792 186.247 1.00 149.84 ? 4377 MET A SD    1 
ATOM   21487 C  CE    . MET A 1 4377 ? 147.316 151.960 184.892 1.00 143.56 ? 4377 MET A CE    1 
ATOM   21488 N  N     . ARG A 1 4378 ? 150.577 147.442 189.599 1.00 139.73 ? 4378 ARG A N     1 
ATOM   21489 C  CA    . ARG A 1 4378 ? 150.729 146.880 190.939 1.00 138.07 ? 4378 ARG A CA    1 
ATOM   21490 C  C     . ARG A 1 4378 ? 152.198 146.750 191.324 1.00 138.58 ? 4378 ARG A C     1 
ATOM   21491 O  O     . ARG A 1 4378 ? 152.568 147.005 192.479 1.00 139.64 ? 4378 ARG A O     1 
ATOM   21492 C  CB    . ARG A 1 4378 ? 150.025 145.525 191.022 1.00 135.06 ? 4378 ARG A CB    1 
ATOM   21493 C  CG    . ARG A 1 4378 ? 148.616 145.592 191.599 1.00 135.55 ? 4378 ARG A CG    1 
ATOM   21494 C  CD    . ARG A 1 4378 ? 147.719 146.505 190.777 1.00 136.75 ? 4378 ARG A CD    1 
ATOM   21495 N  NE    . ARG A 1 4378 ? 146.352 146.542 191.282 1.00 137.86 ? 4378 ARG A NE    1 
ATOM   21496 C  CZ    . ARG A 1 4378 ? 145.365 147.223 190.717 1.00 137.28 ? 4378 ARG A CZ    1 
ATOM   21497 N  NH1   . ARG A 1 4378 ? 145.558 147.940 189.623 1.00 136.91 ? 4378 ARG A NH1   1 
ATOM   21498 N  NH2   . ARG A 1 4378 ? 144.153 147.184 191.264 1.00 135.39 ? 4378 ARG A NH2   1 
ATOM   21499 N  N     . THR A 1 4379 ? 153.049 146.354 190.374 1.00 131.13 ? 4379 THR A N     1 
ATOM   21500 C  CA    . THR A 1 4379 ? 154.477 146.258 190.662 1.00 132.62 ? 4379 THR A CA    1 
ATOM   21501 C  C     . THR A 1 4379 ? 155.053 147.615 191.045 1.00 133.19 ? 4379 THR A C     1 
ATOM   21502 O  O     . THR A 1 4379 ? 155.804 147.728 192.023 1.00 134.53 ? 4379 THR A O     1 
ATOM   21503 C  CB    . THR A 1 4379 ? 155.220 145.686 189.455 1.00 131.24 ? 4379 THR A CB    1 
ATOM   21504 O  OG1   . THR A 1 4379 ? 154.564 144.493 189.009 1.00 132.39 ? 4379 THR A OG1   1 
ATOM   21505 C  CG2   . THR A 1 4379 ? 156.659 145.360 189.824 1.00 131.12 ? 4379 THR A CG2   1 
ATOM   21506 N  N     . LEU A 1 4380 ? 154.699 148.660 190.295 1.00 120.29 ? 4380 LEU A N     1 
ATOM   21507 C  CA    . LEU A 1 4380 ? 155.191 149.994 190.611 1.00 120.27 ? 4380 LEU A CA    1 
ATOM   21508 C  C     . LEU A 1 4380 ? 154.592 150.506 191.914 1.00 120.09 ? 4380 LEU A C     1 
ATOM   21509 O  O     . LEU A 1 4380 ? 155.255 151.234 192.659 1.00 123.56 ? 4380 LEU A O     1 
ATOM   21510 C  CB    . LEU A 1 4380 ? 154.890 150.949 189.458 1.00 119.52 ? 4380 LEU A CB    1 
ATOM   21511 C  CG    . LEU A 1 4380 ? 155.629 152.286 189.480 1.00 121.05 ? 4380 LEU A CG    1 
ATOM   21512 C  CD1   . LEU A 1 4380 ? 157.130 152.066 189.452 1.00 120.30 ? 4380 LEU A CD1   1 
ATOM   21513 C  CD2   . LEU A 1 4380 ? 155.199 153.132 188.301 1.00 121.67 ? 4380 LEU A CD2   1 
ATOM   21514 N  N     . HIS A 1 4381 ? 153.347 150.128 192.212 1.00 118.00 ? 4381 HIS A N     1 
ATOM   21515 C  CA    . HIS A 1 4381 ? 152.746 150.494 193.490 1.00 122.25 ? 4381 HIS A CA    1 
ATOM   21516 C  C     . HIS A 1 4381 ? 153.538 149.908 194.651 1.00 125.50 ? 4381 HIS A C     1 
ATOM   21517 O  O     . HIS A 1 4381 ? 153.862 150.611 195.616 1.00 128.74 ? 4381 HIS A O     1 
ATOM   21518 C  CB    . HIS A 1 4381 ? 151.292 150.018 193.530 1.00 120.69 ? 4381 HIS A CB    1 
ATOM   21519 C  CG    . HIS A 1 4381 ? 150.531 150.484 194.732 1.00 122.81 ? 4381 HIS A CG    1 
ATOM   21520 N  ND1   . HIS A 1 4381 ? 150.767 149.997 196.000 1.00 124.81 ? 4381 HIS A ND1   1 
ATOM   21521 C  CD2   . HIS A 1 4381 ? 149.531 151.389 194.858 1.00 123.45 ? 4381 HIS A CD2   1 
ATOM   21522 C  CE1   . HIS A 1 4381 ? 149.949 150.584 196.854 1.00 125.86 ? 4381 HIS A CE1   1 
ATOM   21523 N  NE2   . HIS A 1 4381 ? 149.189 151.433 196.187 1.00 126.04 ? 4381 HIS A NE2   1 
ATOM   21524 N  N     . THR A 1 4382 ? 153.869 148.618 194.566 1.00 118.20 ? 4382 THR A N     1 
ATOM   21525 C  CA    . THR A 1 4382 ? 154.648 147.986 195.628 1.00 117.65 ? 4382 THR A CA    1 
ATOM   21526 C  C     . THR A 1 4382 ? 156.039 148.600 195.736 1.00 120.24 ? 4382 THR A C     1 
ATOM   21527 O  O     . THR A 1 4382 ? 156.525 148.869 196.844 1.00 120.11 ? 4382 THR A O     1 
ATOM   21528 C  CB    . THR A 1 4382 ? 154.748 146.480 195.387 1.00 116.11 ? 4382 THR A CB    1 
ATOM   21529 O  OG1   . THR A 1 4382 ? 155.381 146.237 194.125 1.00 118.91 ? 4382 THR A OG1   1 
ATOM   21530 C  CG2   . THR A 1 4382 ? 153.367 145.846 195.392 1.00 116.76 ? 4382 THR A CG2   1 
ATOM   21531 N  N     . THR A 1 4383 ? 156.694 148.833 194.595 1.00 115.88 ? 4383 THR A N     1 
ATOM   21532 C  CA    . THR A 1 4383 ? 158.028 149.424 194.618 1.00 112.44 ? 4383 THR A CA    1 
ATOM   21533 C  C     . THR A 1 4383 ? 158.005 150.811 195.247 1.00 112.05 ? 4383 THR A C     1 
ATOM   21534 O  O     . THR A 1 4383 ? 158.862 151.143 196.074 1.00 114.57 ? 4383 THR A O     1 
ATOM   21535 C  CB    . THR A 1 4383 ? 158.599 149.492 193.202 1.00 109.27 ? 4383 THR A CB    1 
ATOM   21536 O  OG1   . THR A 1 4383 ? 158.425 148.226 192.554 1.00 111.84 ? 4383 THR A OG1   1 
ATOM   21537 C  CG2   . THR A 1 4383 ? 160.077 149.833 193.243 1.00 111.94 ? 4383 THR A CG2   1 
ATOM   21538 N  N     . ALA A 1 4384 ? 157.020 151.631 194.876 1.00 108.53 ? 4384 ALA A N     1 
ATOM   21539 C  CA    . ALA A 1 4384 ? 156.927 152.978 195.421 1.00 111.53 ? 4384 ALA A CA    1 
ATOM   21540 C  C     . ALA A 1 4384 ? 156.594 152.956 196.906 1.00 112.28 ? 4384 ALA A C     1 
ATOM   21541 O  O     . ALA A 1 4384 ? 157.102 153.784 197.668 1.00 115.10 ? 4384 ALA A O     1 
ATOM   21542 C  CB    . ALA A 1 4384 ? 155.890 153.782 194.641 1.00 113.07 ? 4384 ALA A CB    1 
ATOM   21543 N  N     . SER A 1 4385 ? 155.739 152.026 197.341 1.00 110.36 ? 4385 SER A N     1 
ATOM   21544 C  CA    . SER A 1 4385 ? 155.446 151.917 198.767 1.00 115.33 ? 4385 SER A CA    1 
ATOM   21545 C  C     . SER A 1 4385 ? 156.695 151.550 199.559 1.00 114.82 ? 4385 SER A C     1 
ATOM   21546 O  O     . SER A 1 4385 ? 156.971 152.137 200.615 1.00 115.20 ? 4385 SER A O     1 
ATOM   21547 C  CB    . SER A 1 4385 ? 154.340 150.887 198.998 1.00 114.04 ? 4385 SER A CB    1 
ATOM   21548 O  OG    . SER A 1 4385 ? 153.160 151.239 198.298 1.00 112.09 ? 4385 SER A OG    1 
ATOM   21549 N  N     . ASN A 1 4386 ? 157.474 150.590 199.054 1.00 110.27 ? 4386 ASN A N     1 
ATOM   21550 C  CA    . ASN A 1 4386 ? 158.723 150.238 199.722 1.00 110.37 ? 4386 ASN A CA    1 
ATOM   21551 C  C     . ASN A 1 4386 ? 159.689 151.416 199.739 1.00 109.46 ? 4386 ASN A C     1 
ATOM   21552 O  O     . ASN A 1 4386 ? 160.387 151.643 200.734 1.00 110.39 ? 4386 ASN A O     1 
ATOM   21553 C  CB    . ASN A 1 4386 ? 159.359 149.024 199.047 1.00 112.48 ? 4386 ASN A CB    1 
ATOM   21554 C  CG    . ASN A 1 4386 ? 158.515 147.773 199.189 1.00 113.40 ? 4386 ASN A CG    1 
ATOM   21555 O  OD1   . ASN A 1 4386 ? 157.291 147.844 199.301 1.00 110.94 ? 4386 ASN A OD1   1 
ATOM   21556 N  ND2   . ASN A 1 4386 ? 159.167 146.617 199.185 1.00 113.99 ? 4386 ASN A ND2   1 
ATOM   21557 N  N     . TRP A 1 4387 ? 159.743 152.179 198.644 1.00 105.50 ? 4387 TRP A N     1 
ATOM   21558 C  CA    . TRP A 1 4387 ? 160.623 153.341 198.599 1.00 107.31 ? 4387 TRP A CA    1 
ATOM   21559 C  C     . TRP A 1 4387 ? 160.202 154.399 199.615 1.00 109.94 ? 4387 TRP A C     1 
ATOM   21560 O  O     . TRP A 1 4387 ? 161.053 154.997 200.284 1.00 113.31 ? 4387 TRP A O     1 
ATOM   21561 C  CB    . TRP A 1 4387 ? 160.650 153.921 197.187 1.00 107.24 ? 4387 TRP A CB    1 
ATOM   21562 C  CG    . TRP A 1 4387 ? 161.507 153.139 196.244 1.00 105.48 ? 4387 TRP A CG    1 
ATOM   21563 C  CD1   . TRP A 1 4387 ? 162.395 152.158 196.570 1.00 107.14 ? 4387 TRP A CD1   1 
ATOM   21564 C  CD2   . TRP A 1 4387 ? 161.558 153.269 194.819 1.00 108.65 ? 4387 TRP A CD2   1 
ATOM   21565 N  NE1   . TRP A 1 4387 ? 162.997 151.669 195.437 1.00 109.61 ? 4387 TRP A NE1   1 
ATOM   21566 C  CE2   . TRP A 1 4387 ? 162.500 152.335 194.348 1.00 109.49 ? 4387 TRP A CE2   1 
ATOM   21567 C  CE3   . TRP A 1 4387 ? 160.899 154.085 193.895 1.00 110.40 ? 4387 TRP A CE3   1 
ATOM   21568 C  CZ2   . TRP A 1 4387 ? 162.800 152.193 192.996 1.00 106.36 ? 4387 TRP A CZ2   1 
ATOM   21569 C  CZ3   . TRP A 1 4387 ? 161.198 153.942 192.553 1.00 110.90 ? 4387 TRP A CZ3   1 
ATOM   21570 C  CH2   . TRP A 1 4387 ? 162.140 153.004 192.116 1.00 105.85 ? 4387 TRP A CH2   1 
ATOM   21571 N  N     . LEU A 1 4388 ? 158.896 154.645 199.746 1.00 100.99 ? 4388 LEU A N     1 
ATOM   21572 C  CA    . LEU A 1 4388 ? 158.423 155.567 200.777 1.00 102.61 ? 4388 LEU A CA    1 
ATOM   21573 C  C     . LEU A 1 4388 ? 158.785 155.069 202.167 1.00 103.18 ? 4388 LEU A C     1 
ATOM   21574 O  O     . LEU A 1 4388 ? 159.129 155.865 203.049 1.00 101.65 ? 4388 LEU A O     1 
ATOM   21575 C  CB    . LEU A 1 4388 ? 156.912 155.778 200.672 1.00 100.74 ? 4388 LEU A CB    1 
ATOM   21576 C  CG    . LEU A 1 4388 ? 156.316 156.249 199.349 1.00 99.56  ? 4388 LEU A CG    1 
ATOM   21577 C  CD1   . LEU A 1 4388 ? 154.801 156.247 199.424 1.00 103.13 ? 4388 LEU A CD1   1 
ATOM   21578 C  CD2   . LEU A 1 4388 ? 156.829 157.638 199.039 1.00 102.41 ? 4388 LEU A CD2   1 
ATOM   21579 N  N     . HIS A 1 4389 ? 158.701 153.756 202.388 1.00 109.40 ? 4389 HIS A N     1 
ATOM   21580 C  CA    . HIS A 1 4389 ? 159.111 153.212 203.679 1.00 109.84 ? 4389 HIS A CA    1 
ATOM   21581 C  C     . HIS A 1 4389 ? 160.598 153.440 203.930 1.00 108.94 ? 4389 HIS A C     1 
ATOM   21582 O  O     . HIS A 1 4389 ? 161.003 153.755 205.055 1.00 110.41 ? 4389 HIS A O     1 
ATOM   21583 C  CB    . HIS A 1 4389 ? 158.770 151.725 203.758 1.00 112.36 ? 4389 HIS A CB    1 
ATOM   21584 C  CG    . HIS A 1 4389 ? 157.389 151.450 204.267 1.00 113.45 ? 4389 HIS A CG    1 
ATOM   21585 N  ND1   . HIS A 1 4389 ? 157.041 151.606 205.591 1.00 111.89 ? 4389 HIS A ND1   1 
ATOM   21586 C  CD2   . HIS A 1 4389 ? 156.269 151.034 203.630 1.00 110.59 ? 4389 HIS A CD2   1 
ATOM   21587 C  CE1   . HIS A 1 4389 ? 155.767 151.295 205.749 1.00 112.53 ? 4389 HIS A CE1   1 
ATOM   21588 N  NE2   . HIS A 1 4389 ? 155.275 150.945 204.575 1.00 111.61 ? 4389 HIS A NE2   1 
ATOM   21589 N  N     . LEU A 1 4390 ? 161.427 153.284 202.895 1.00 103.62 ? 4390 LEU A N     1 
ATOM   21590 C  CA    . LEU A 1 4390 ? 162.870 153.429 203.072 1.00 102.84 ? 4390 LEU A CA    1 
ATOM   21591 C  C     . LEU A 1 4390 ? 163.265 154.882 203.315 1.00 105.61 ? 4390 LEU A C     1 
ATOM   21592 O  O     . LEU A 1 4390 ? 164.042 155.179 204.229 1.00 105.74 ? 4390 LEU A O     1 
ATOM   21593 C  CB    . LEU A 1 4390 ? 163.606 152.874 201.852 1.00 101.64 ? 4390 LEU A CB    1 
ATOM   21594 C  CG    . LEU A 1 4390 ? 163.512 151.366 201.620 1.00 104.07 ? 4390 LEU A CG    1 
ATOM   21595 C  CD1   . LEU A 1 4390 ? 164.223 150.981 200.332 1.00 103.50 ? 4390 LEU A CD1   1 
ATOM   21596 C  CD2   . LEU A 1 4390 ? 164.083 150.605 202.805 1.00 105.33 ? 4390 LEU A CD2   1 
ATOM   21597 N  N     . ILE A 1 4391 ? 162.747 155.798 202.506 1.00 96.45  ? 4391 ILE A N     1 
ATOM   21598 C  CA    . ILE A 1 4391 ? 163.193 157.196 202.576 1.00 92.44  ? 4391 ILE A CA    1 
ATOM   21599 C  C     . ILE A 1 4391 ? 162.637 157.847 203.836 1.00 92.01  ? 4391 ILE A C     1 
ATOM   21600 O  O     . ILE A 1 4391 ? 161.440 157.687 204.136 1.00 94.08  ? 4391 ILE A O     1 
ATOM   21601 C  CB    . ILE A 1 4391 ? 162.756 157.956 201.323 1.00 89.07  ? 4391 ILE A CB    1 
ATOM   21602 C  CG1   . ILE A 1 4391 ? 163.216 157.221 200.064 1.00 89.23  ? 4391 ILE A CG1   1 
ATOM   21603 C  CG2   . ILE A 1 4391 ? 163.311 159.366 201.340 1.00 91.33  ? 4391 ILE A CG2   1 
ATOM   21604 C  CD1   . ILE A 1 4391 ? 162.751 157.866 198.780 1.00 92.67  ? 4391 ILE A CD1   1 
ATOM   21605 N  N     . PRO A 1 4392 ? 163.453 158.578 204.605 1.00 96.80  ? 4392 PRO A N     1 
ATOM   21606 C  CA    . PRO A 1 4392 ? 162.920 159.326 205.753 1.00 99.74  ? 4392 PRO A CA    1 
ATOM   21607 C  C     . PRO A 1 4392 ? 161.997 160.459 205.326 1.00 103.17 ? 4392 PRO A C     1 
ATOM   21608 O  O     . PRO A 1 4392 ? 161.842 160.718 204.129 1.00 108.42 ? 4392 PRO A O     1 
ATOM   21609 C  CB    . PRO A 1 4392 ? 164.183 159.855 206.445 1.00 102.33 ? 4392 PRO A CB    1 
ATOM   21610 C  CG    . PRO A 1 4392 ? 165.279 158.944 205.981 1.00 100.81 ? 4392 PRO A CG    1 
ATOM   21611 C  CD    . PRO A 1 4392 ? 164.923 158.593 204.571 1.00 99.33  ? 4392 PRO A CD    1 
ATOM   21612 N  N     . GLN A 1 4393 ? 161.383 161.149 206.293 1.00 104.72 ? 4393 GLN A N     1 
ATOM   21613 C  CA    . GLN A 1 4393 ? 160.343 162.121 205.987 1.00 102.39 ? 4393 GLN A CA    1 
ATOM   21614 C  C     . GLN A 1 4393 ? 160.684 163.563 206.335 1.00 104.98 ? 4393 GLN A C     1 
ATOM   21615 O  O     . GLN A 1 4393 ? 160.163 164.468 205.674 1.00 109.98 ? 4393 GLN A O     1 
ATOM   21616 C  CB    . GLN A 1 4393 ? 159.034 161.765 206.715 1.00 104.13 ? 4393 GLN A CB    1 
ATOM   21617 C  CG    . GLN A 1 4393 ? 158.357 160.485 206.248 1.00 105.60 ? 4393 GLN A CG    1 
ATOM   21618 C  CD    . GLN A 1 4393 ? 158.895 159.243 206.937 1.00 106.97 ? 4393 GLN A CD    1 
ATOM   21619 O  OE1   . GLN A 1 4393 ? 160.095 159.108 207.161 1.00 104.09 ? 4393 GLN A OE1   1 
ATOM   21620 N  NE2   . GLN A 1 4393 ? 157.998 158.325 207.276 1.00 105.19 ? 4393 GLN A NE2   1 
ATOM   21621 N  N     . THR A 1 4394 ? 161.532 163.812 207.330 1.00 118.26 ? 4394 THR A N     1 
ATOM   21622 C  CA    . THR A 1 4394 ? 161.683 165.150 207.887 1.00 120.43 ? 4394 THR A CA    1 
ATOM   21623 C  C     . THR A 1 4394 ? 163.112 165.651 207.740 1.00 118.70 ? 4394 THR A C     1 
ATOM   21624 O  O     . THR A 1 4394 ? 164.067 164.870 207.804 1.00 120.77 ? 4394 THR A O     1 
ATOM   21625 C  CB    . THR A 1 4394 ? 161.283 165.182 209.368 1.00 122.06 ? 4394 THR A CB    1 
ATOM   21626 O  OG1   . THR A 1 4394 ? 162.012 164.176 210.083 1.00 121.00 ? 4394 THR A OG1   1 
ATOM   21627 C  CG2   . THR A 1 4394 ? 159.792 164.928 209.522 1.00 117.58 ? 4394 THR A CG2   1 
ATOM   21628 N  N     . LEU A 1 4395 ? 163.244 166.962 207.540 1.00 121.88 ? 4395 LEU A N     1 
ATOM   21629 C  CA    . LEU A 1 4395 ? 164.551 167.613 207.478 1.00 124.89 ? 4395 LEU A CA    1 
ATOM   21630 C  C     . LEU A 1 4395 ? 164.332 169.105 207.699 1.00 129.76 ? 4395 LEU A C     1 
ATOM   21631 O  O     . LEU A 1 4395 ? 163.645 169.751 206.902 1.00 131.49 ? 4395 LEU A O     1 
ATOM   21632 C  CB    . LEU A 1 4395 ? 165.232 167.342 206.142 1.00 125.45 ? 4395 LEU A CB    1 
ATOM   21633 C  CG    . LEU A 1 4395 ? 166.737 167.603 206.077 1.00 126.50 ? 4395 LEU A CG    1 
ATOM   21634 C  CD1   . LEU A 1 4395 ? 167.441 166.953 207.258 1.00 124.90 ? 4395 LEU A CD1   1 
ATOM   21635 C  CD2   . LEU A 1 4395 ? 167.309 167.096 204.765 1.00 123.92 ? 4395 LEU A CD2   1 
ATOM   21636 N  N     . SER A 1 4396 ? 164.905 169.646 208.773 1.00 128.78 ? 4396 SER A N     1 
ATOM   21637 C  CA    . SER A 1 4396 ? 164.719 171.047 209.130 1.00 124.57 ? 4396 SER A CA    1 
ATOM   21638 C  C     . SER A 1 4396 ? 165.900 171.889 208.665 1.00 127.61 ? 4396 SER A C     1 
ATOM   21639 O  O     . SER A 1 4396 ? 167.057 171.483 208.800 1.00 131.95 ? 4396 SER A O     1 
ATOM   21640 C  CB    . SER A 1 4396 ? 164.543 171.197 210.641 1.00 126.54 ? 4396 SER A CB    1 
ATOM   21641 O  OG    . SER A 1 4396 ? 165.679 170.711 211.333 1.00 130.51 ? 4396 SER A OG    1 
ATOM   21642 N  N     . HIS A 1 4397 ? 165.600 173.076 208.143 1.00 136.02 ? 4397 HIS A N     1 
ATOM   21643 C  CA    . HIS A 1 4397 ? 166.632 173.957 207.614 1.00 140.39 ? 4397 HIS A CA    1 
ATOM   21644 C  C     . HIS A 1 4397 ? 167.492 174.530 208.737 1.00 138.89 ? 4397 HIS A C     1 
ATOM   21645 O  O     . HIS A 1 4397 ? 167.126 174.490 209.915 1.00 134.05 ? 4397 HIS A O     1 
ATOM   21646 C  CB    . HIS A 1 4397 ? 166.001 175.097 206.815 1.00 138.58 ? 4397 HIS A CB    1 
ATOM   21647 C  CG    . HIS A 1 4397 ? 165.889 174.821 205.348 1.00 139.76 ? 4397 HIS A CG    1 
ATOM   21648 N  ND1   . HIS A 1 4397 ? 165.528 175.788 204.435 1.00 139.05 ? 4397 HIS A ND1   1 
ATOM   21649 C  CD2   . HIS A 1 4397 ? 166.083 173.685 204.636 1.00 138.77 ? 4397 HIS A CD2   1 
ATOM   21650 C  CE1   . HIS A 1 4397 ? 165.507 175.261 203.224 1.00 138.66 ? 4397 HIS A CE1   1 
ATOM   21651 N  NE2   . HIS A 1 4397 ? 165.839 173.986 203.318 1.00 137.42 ? 4397 HIS A NE2   1 
ATOM   21652 N  N     . LEU A 1 4398 ? 168.651 175.064 208.359 1.00 141.55 ? 4398 LEU A N     1 
ATOM   21653 C  CA    . LEU A 1 4398 ? 169.560 175.652 209.333 1.00 142.01 ? 4398 LEU A CA    1 
ATOM   21654 C  C     . LEU A 1 4398 ? 169.257 177.134 209.536 1.00 141.88 ? 4398 LEU A C     1 
ATOM   21655 O  O     . LEU A 1 4398 ? 168.963 177.870 208.590 1.00 138.53 ? 4398 LEU A O     1 
ATOM   21656 C  CB    . LEU A 1 4398 ? 171.012 175.465 208.894 1.00 139.23 ? 4398 LEU A CB    1 
ATOM   21657 C  CG    . LEU A 1 4398 ? 171.527 174.022 208.897 1.00 138.08 ? 4398 LEU A CG    1 
ATOM   21658 C  CD1   . LEU A 1 4398 ? 173.046 173.981 208.930 1.00 137.43 ? 4398 LEU A CD1   1 
ATOM   21659 C  CD2   . LEU A 1 4398 ? 170.943 173.233 210.063 1.00 134.90 ? 4398 LEU A CD2   1 
ATOM   21660 N  N     . LYS A 1 4399 ? 169.344 177.569 210.792 1.00 146.16 ? 4399 LYS A N     1 
ATOM   21661 C  CA    . LYS A 1 4399 ? 168.953 178.912 211.201 1.00 142.61 ? 4399 LYS A CA    1 
ATOM   21662 C  C     . LYS A 1 4399 ? 170.109 179.888 211.029 1.00 144.00 ? 4399 LYS A C     1 
ATOM   21663 O  O     . LYS A 1 4399 ? 171.234 179.609 211.455 1.00 145.76 ? 4399 LYS A O     1 
ATOM   21664 C  CB    . LYS A 1 4399 ? 168.490 178.917 212.658 1.00 138.38 ? 4399 LYS A CB    1 
ATOM   21665 C  CG    . LYS A 1 4399 ? 167.502 180.017 212.989 1.00 138.06 ? 4399 LYS A CG    1 
ATOM   21666 C  CD    . LYS A 1 4399 ? 167.529 180.332 214.473 1.00 140.69 ? 4399 LYS A CD    1 
ATOM   21667 C  CE    . LYS A 1 4399 ? 168.716 181.218 214.819 1.00 139.90 ? 4399 LYS A CE    1 
ATOM   21668 N  NZ    . LYS A 1 4399 ? 168.554 181.885 216.139 1.00 140.85 ? 4399 LYS A NZ    1 
ATOM   21669 N  N     . ARG A 1 4400 ? 169.820 181.040 210.427 1.00 144.73 ? 4400 ARG A N     1 
ATOM   21670 C  CA    . ARG A 1 4400 ? 170.815 182.089 210.260 1.00 145.48 ? 4400 ARG A CA    1 
ATOM   21671 C  C     . ARG A 1 4400 ? 171.019 182.841 211.569 1.00 145.94 ? 4400 ARG A C     1 
ATOM   21672 O  O     . ARG A 1 4400 ? 170.061 183.090 212.309 1.00 147.06 ? 4400 ARG A O     1 
ATOM   21673 C  CB    . ARG A 1 4400 ? 170.386 183.060 209.161 1.00 145.43 ? 4400 ARG A CB    1 
ATOM   21674 C  CG    . ARG A 1 4400 ? 170.243 182.431 207.788 1.00 143.92 ? 4400 ARG A CG    1 
ATOM   21675 C  CD    . ARG A 1 4400 ? 171.590 181.968 207.270 1.00 143.19 ? 4400 ARG A CD    1 
ATOM   21676 N  NE    . ARG A 1 4400 ? 171.527 181.517 205.886 1.00 144.28 ? 4400 ARG A NE    1 
ATOM   21677 C  CZ    . ARG A 1 4400 ? 171.740 182.296 204.834 1.00 142.94 ? 4400 ARG A CZ    1 
ATOM   21678 N  NH1   . ARG A 1 4400 ? 172.035 183.578 204.973 1.00 140.57 ? 4400 ARG A NH1   1 
ATOM   21679 N  NH2   . ARG A 1 4400 ? 171.656 181.776 203.613 1.00 143.66 ? 4400 ARG A NH2   1 
ATOM   21680 N  N     . THR A 1 4401 ? 172.269 183.200 211.856 1.00 152.42 ? 4401 THR A N     1 
ATOM   21681 C  CA    . THR A 1 4401 ? 172.605 184.010 213.017 1.00 155.21 ? 4401 THR A CA    1 
ATOM   21682 C  C     . THR A 1 4401 ? 173.756 184.934 212.649 1.00 155.56 ? 4401 THR A C     1 
ATOM   21683 O  O     . THR A 1 4401 ? 174.492 184.677 211.692 1.00 154.41 ? 4401 THR A O     1 
ATOM   21684 C  CB    . THR A 1 4401 ? 172.982 183.147 214.232 1.00 155.08 ? 4401 THR A CB    1 
ATOM   21685 O  OG1   . THR A 1 4401 ? 172.181 181.960 214.246 1.00 155.68 ? 4401 THR A OG1   1 
ATOM   21686 C  CG2   . THR A 1 4401 ? 172.747 183.911 215.530 1.00 151.14 ? 4401 THR A CG2   1 
ATOM   21687 N  N     . VAL A 1 4402 ? 173.902 186.019 213.415 1.00 156.97 ? 4402 VAL A N     1 
ATOM   21688 C  CA    . VAL A 1 4402 ? 174.926 187.016 213.110 1.00 155.98 ? 4402 VAL A CA    1 
ATOM   21689 C  C     . VAL A 1 4402 ? 176.321 186.409 213.210 1.00 154.52 ? 4402 VAL A C     1 
ATOM   21690 O  O     . VAL A 1 4402 ? 177.175 186.636 212.345 1.00 152.74 ? 4402 VAL A O     1 
ATOM   21691 C  CB    . VAL A 1 4402 ? 174.768 188.246 214.024 1.00 154.58 ? 4402 VAL A CB    1 
ATOM   21692 C  CG1   . VAL A 1 4402 ? 173.564 189.069 213.595 1.00 153.17 ? 4402 VAL A CG1   1 
ATOM   21693 C  CG2   . VAL A 1 4402 ? 174.620 187.821 215.478 1.00 154.57 ? 4402 VAL A CG2   1 
ATOM   21694 N  N     . GLU A 1 4403 ? 176.579 185.632 214.263 1.00 150.86 ? 4403 GLU A N     1 
ATOM   21695 C  CA    . GLU A 1 4403 ? 177.870 184.976 214.417 1.00 150.31 ? 4403 GLU A CA    1 
ATOM   21696 C  C     . GLU A 1 4403 ? 177.965 183.662 213.653 1.00 150.97 ? 4403 GLU A C     1 
ATOM   21697 O  O     . GLU A 1 4403 ? 179.076 183.154 213.461 1.00 148.48 ? 4403 GLU A O     1 
ATOM   21698 C  CB    . GLU A 1 4403 ? 178.167 184.732 215.901 1.00 149.41 ? 4403 GLU A CB    1 
ATOM   21699 C  CG    . GLU A 1 4403 ? 177.168 183.830 216.608 1.00 149.94 ? 4403 GLU A CG    1 
ATOM   21700 C  CD    . GLU A 1 4403 ? 177.697 182.424 216.816 1.00 150.47 ? 4403 GLU A CD    1 
ATOM   21701 O  OE1   . GLU A 1 4403 ? 178.921 182.221 216.671 1.00 150.85 ? 4403 GLU A OE1   1 
ATOM   21702 O  OE2   . GLU A 1 4403 ? 176.891 181.524 217.132 1.00 148.23 ? 4403 GLU A OE2   1 
ATOM   21703 N  N     . ASN A 1 4404 ? 176.834 183.103 213.216 1.00 144.33 ? 4404 ASN A N     1 
ATOM   21704 C  CA    . ASN A 1 4404 ? 176.872 181.870 212.438 1.00 139.96 ? 4404 ASN A CA    1 
ATOM   21705 C  C     . ASN A 1 4404 ? 177.407 182.106 211.032 1.00 138.64 ? 4404 ASN A C     1 
ATOM   21706 O  O     . ASN A 1 4404 ? 178.103 181.244 210.484 1.00 139.38 ? 4404 ASN A O     1 
ATOM   21707 C  CB    . ASN A 1 4404 ? 175.480 181.240 212.376 1.00 139.75 ? 4404 ASN A CB    1 
ATOM   21708 C  CG    . ASN A 1 4404 ? 175.097 180.541 213.666 1.00 141.33 ? 4404 ASN A CG    1 
ATOM   21709 O  OD1   . ASN A 1 4404 ? 175.491 180.962 214.754 1.00 140.40 ? 4404 ASN A OD1   1 
ATOM   21710 N  ND2   . ASN A 1 4404 ? 174.322 179.470 213.552 1.00 141.33 ? 4404 ASN A ND2   1 
ATOM   21711 N  N     . ILE A 1 4405 ? 177.093 183.259 210.435 1.00 141.69 ? 4405 ILE A N     1 
ATOM   21712 C  CA    . ILE A 1 4405 ? 177.553 183.553 209.080 1.00 145.09 ? 4405 ILE A CA    1 
ATOM   21713 C  C     . ILE A 1 4405 ? 179.071 183.641 209.032 1.00 145.80 ? 4405 ILE A C     1 
ATOM   21714 O  O     . ILE A 1 4405 ? 179.694 183.237 208.042 1.00 144.82 ? 4405 ILE A O     1 
ATOM   21715 C  CB    . ILE A 1 4405 ? 176.892 184.845 208.560 1.00 143.79 ? 4405 ILE A CB    1 
ATOM   21716 C  CG1   . ILE A 1 4405 ? 175.371 184.707 208.584 1.00 143.77 ? 4405 ILE A CG1   1 
ATOM   21717 C  CG2   . ILE A 1 4405 ? 177.354 185.154 207.148 1.00 142.82 ? 4405 ILE A CG2   1 
ATOM   21718 C  CD1   . ILE A 1 4405 ? 174.865 183.471 207.875 1.00 142.95 ? 4405 ILE A CD1   1 
ATOM   21719 N  N     . LYS A 1 4406 ? 179.694 184.159 210.093 1.00 142.63 ? 4406 LYS A N     1 
ATOM   21720 C  CA    . LYS A 1 4406 ? 181.148 184.202 210.157 1.00 140.59 ? 4406 LYS A CA    1 
ATOM   21721 C  C     . LYS A 1 4406 ? 181.777 182.816 210.175 1.00 140.45 ? 4406 LYS A C     1 
ATOM   21722 O  O     . LYS A 1 4406 ? 182.979 182.700 209.914 1.00 136.02 ? 4406 LYS A O     1 
ATOM   21723 C  CB    . LYS A 1 4406 ? 181.601 184.989 211.388 1.00 140.75 ? 4406 LYS A CB    1 
ATOM   21724 C  CG    . LYS A 1 4406 ? 181.113 186.428 211.421 1.00 139.75 ? 4406 LYS A CG    1 
ATOM   21725 C  CD    . LYS A 1 4406 ? 181.475 187.103 212.734 1.00 139.14 ? 4406 LYS A CD    1 
ATOM   21726 C  CE    . LYS A 1 4406 ? 180.359 188.015 213.214 1.00 140.31 ? 4406 LYS A CE    1 
ATOM   21727 N  NZ    . LYS A 1 4406 ? 180.620 188.529 214.587 1.00 141.40 ? 4406 LYS A NZ    1 
ATOM   21728 N  N     . ASP A 1 4407 ? 181.004 181.772 210.470 1.00 136.48 ? 4407 ASP A N     1 
ATOM   21729 C  CA    . ASP A 1 4407 ? 181.527 180.413 210.470 1.00 133.84 ? 4407 ASP A CA    1 
ATOM   21730 C  C     . ASP A 1 4407 ? 181.331 179.791 209.095 1.00 129.33 ? 4407 ASP A C     1 
ATOM   21731 O  O     . ASP A 1 4407 ? 180.185 179.535 208.702 1.00 124.62 ? 4407 ASP A O     1 
ATOM   21732 C  CB    . ASP A 1 4407 ? 180.831 179.571 211.525 1.00 132.82 ? 4407 ASP A CB    1 
ATOM   21733 C  CG    . ASP A 1 4407 ? 181.534 178.252 211.773 1.00 134.36 ? 4407 ASP A CG    1 
ATOM   21734 O  OD1   . ASP A 1 4407 ? 182.639 178.056 211.226 1.00 131.60 ? 4407 ASP A OD1   1 
ATOM   21735 O  OD2   . ASP A 1 4407 ? 180.984 177.412 212.516 1.00 135.78 ? 4407 ASP A OD2   1 
ATOM   21736 N  N     . PRO A 1 4408 ? 182.402 179.535 208.340 1.00 131.75 ? 4408 PRO A N     1 
ATOM   21737 C  CA    . PRO A 1 4408 ? 182.238 178.892 207.024 1.00 132.62 ? 4408 PRO A CA    1 
ATOM   21738 C  C     . PRO A 1 4408 ? 181.625 177.505 207.105 1.00 130.88 ? 4408 PRO A C     1 
ATOM   21739 O  O     . PRO A 1 4408 ? 180.956 177.071 206.153 1.00 129.52 ? 4408 PRO A O     1 
ATOM   21740 C  CB    . PRO A 1 4408 ? 183.672 178.853 206.476 1.00 129.40 ? 4408 PRO A CB    1 
ATOM   21741 C  CG    . PRO A 1 4408 ? 184.545 178.965 207.686 1.00 126.94 ? 4408 PRO A CG    1 
ATOM   21742 C  CD    . PRO A 1 4408 ? 183.809 179.826 208.651 1.00 129.12 ? 4408 PRO A CD    1 
ATOM   21743 N  N     . LEU A 1 4409 ? 181.840 176.796 208.218 1.00 127.29 ? 4409 LEU A N     1 
ATOM   21744 C  CA    . LEU A 1 4409 ? 181.196 175.502 208.411 1.00 126.52 ? 4409 LEU A CA    1 
ATOM   21745 C  C     . LEU A 1 4409 ? 179.688 175.625 208.281 1.00 124.89 ? 4409 LEU A C     1 
ATOM   21746 O  O     . LEU A 1 4409 ? 179.059 174.867 207.536 1.00 125.14 ? 4409 LEU A O     1 
ATOM   21747 C  CB    . LEU A 1 4409 ? 181.562 174.929 209.780 1.00 120.95 ? 4409 LEU A CB    1 
ATOM   21748 C  CG    . LEU A 1 4409 ? 181.558 173.406 209.906 1.00 118.60 ? 4409 LEU A CG    1 
ATOM   21749 C  CD1   . LEU A 1 4409 ? 182.587 172.799 208.972 1.00 123.24 ? 4409 LEU A CD1   1 
ATOM   21750 C  CD2   . LEU A 1 4409 ? 181.813 172.990 211.343 1.00 119.43 ? 4409 LEU A CD2   1 
ATOM   21751 N  N     . PHE A 1 4410 ? 179.093 176.598 208.972 1.00 121.97 ? 4410 PHE A N     1 
ATOM   21752 C  CA    . PHE A 1 4410 ? 177.659 176.819 208.839 1.00 119.66 ? 4410 PHE A CA    1 
ATOM   21753 C  C     . PHE A 1 4410 ? 177.302 177.300 207.437 1.00 121.53 ? 4410 PHE A C     1 
ATOM   21754 O  O     . PHE A 1 4410 ? 176.237 176.956 206.917 1.00 112.76 ? 4410 PHE A O     1 
ATOM   21755 C  CB    . PHE A 1 4410 ? 177.179 177.819 209.889 1.00 122.59 ? 4410 PHE A CB    1 
ATOM   21756 C  CG    . PHE A 1 4410 ? 175.810 177.520 210.418 1.00 122.30 ? 4410 PHE A CG    1 
ATOM   21757 C  CD1   . PHE A 1 4410 ? 174.699 178.144 209.882 1.00 124.56 ? 4410 PHE A CD1   1 
ATOM   21758 C  CD2   . PHE A 1 4410 ? 175.633 176.622 211.456 1.00 119.95 ? 4410 PHE A CD2   1 
ATOM   21759 C  CE1   . PHE A 1 4410 ? 173.438 177.871 210.360 1.00 123.76 ? 4410 PHE A CE1   1 
ATOM   21760 C  CE2   . PHE A 1 4410 ? 174.372 176.347 211.942 1.00 121.16 ? 4410 PHE A CE2   1 
ATOM   21761 C  CZ    . PHE A 1 4410 ? 173.273 176.974 211.393 1.00 120.47 ? 4410 PHE A CZ    1 
ATOM   21762 N  N     . ARG A 1 4411 ? 178.181 178.091 206.811 1.00 134.89 ? 4411 ARG A N     1 
ATOM   21763 C  CA    . ARG A 1 4411 ? 177.911 178.616 205.472 1.00 133.24 ? 4411 ARG A CA    1 
ATOM   21764 C  C     . ARG A 1 4411 ? 177.737 177.500 204.449 1.00 131.85 ? 4411 ARG A C     1 
ATOM   21765 O  O     . ARG A 1 4411 ? 176.880 177.597 203.562 1.00 131.25 ? 4411 ARG A O     1 
ATOM   21766 C  CB    . ARG A 1 4411 ? 179.044 179.550 205.042 1.00 127.81 ? 4411 ARG A CB    1 
ATOM   21767 C  CG    . ARG A 1 4411 ? 179.088 180.871 205.788 1.00 126.63 ? 4411 ARG A CG    1 
ATOM   21768 C  CD    . ARG A 1 4411 ? 179.915 181.916 205.053 1.00 126.24 ? 4411 ARG A CD    1 
ATOM   21769 N  NE    . ARG A 1 4411 ? 181.342 181.626 205.122 1.00 129.71 ? 4411 ARG A NE    1 
ATOM   21770 C  CZ    . ARG A 1 4411 ? 182.241 182.449 205.645 1.00 130.25 ? 4411 ARG A CZ    1 
ATOM   21771 N  NH1   . ARG A 1 4411 ? 181.891 183.616 206.161 1.00 127.23 ? 4411 ARG A NH1   1 
ATOM   21772 N  NH2   . ARG A 1 4411 ? 183.522 182.091 205.654 1.00 128.61 ? 4411 ARG A NH2   1 
ATOM   21773 N  N     . PHE A 1 4412 ? 178.542 176.443 204.556 1.00 126.64 ? 4412 PHE A N     1 
ATOM   21774 C  CA    . PHE A 1 4412 ? 178.396 175.219 203.774 1.00 126.36 ? 4412 PHE A CA    1 
ATOM   21775 C  C     . PHE A 1 4412 ? 177.248 174.346 204.269 1.00 120.87 ? 4412 PHE A C     1 
ATOM   21776 O  O     . PHE A 1 4412 ? 176.535 173.711 203.475 1.00 122.94 ? 4412 PHE A O     1 
ATOM   21777 C  CB    . PHE A 1 4412 ? 179.712 174.430 203.822 1.00 125.89 ? 4412 PHE A CB    1 
ATOM   21778 C  CG    . PHE A 1 4412 ? 179.567 172.978 203.483 1.00 124.58 ? 4412 PHE A CG    1 
ATOM   21779 C  CD1   . PHE A 1 4412 ? 179.484 172.573 202.170 1.00 124.31 ? 4412 PHE A CD1   1 
ATOM   21780 C  CD2   . PHE A 1 4412 ? 179.542 172.014 204.481 1.00 120.57 ? 4412 PHE A CD2   1 
ATOM   21781 C  CE1   . PHE A 1 4412 ? 179.353 171.246 201.851 1.00 126.27 ? 4412 PHE A CE1   1 
ATOM   21782 C  CE2   . PHE A 1 4412 ? 179.408 170.684 204.165 1.00 121.92 ? 4412 PHE A CE2   1 
ATOM   21783 C  CZ    . PHE A 1 4412 ? 179.324 170.301 202.847 1.00 125.21 ? 4412 PHE A CZ    1 
ATOM   21784 N  N     . PHE A 1 4413 ? 177.050 174.327 205.582 1.00 109.61 ? 4413 PHE A N     1 
ATOM   21785 C  CA    . PHE A 1 4413 ? 176.217 173.320 206.210 1.00 114.53 ? 4413 PHE A CA    1 
ATOM   21786 C  C     . PHE A 1 4413 ? 174.749 173.651 205.966 1.00 116.43 ? 4413 PHE A C     1 
ATOM   21787 O  O     . PHE A 1 4413 ? 173.915 172.752 205.781 1.00 114.39 ? 4413 PHE A O     1 
ATOM   21788 C  CB    . PHE A 1 4413 ? 176.569 173.343 207.693 1.00 117.84 ? 4413 PHE A CB    1 
ATOM   21789 C  CG    . PHE A 1 4413 ? 176.849 172.011 208.292 1.00 116.27 ? 4413 PHE A CG    1 
ATOM   21790 C  CD1   . PHE A 1 4413 ? 175.857 171.229 208.829 1.00 110.66 ? 4413 PHE A CD1   1 
ATOM   21791 C  CD2   . PHE A 1 4413 ? 178.166 171.570 208.338 1.00 116.13 ? 4413 PHE A CD2   1 
ATOM   21792 C  CE1   . PHE A 1 4413 ? 176.165 170.042 209.403 1.00 112.38 ? 4413 PHE A CE1   1 
ATOM   21793 C  CE2   . PHE A 1 4413 ? 178.482 170.356 208.887 1.00 110.54 ? 4413 PHE A CE2   1 
ATOM   21794 C  CZ    . PHE A 1 4413 ? 177.473 169.589 209.434 1.00 108.62 ? 4413 PHE A CZ    1 
ATOM   21795 N  N     . GLU A 1 4414 ? 174.433 174.952 205.946 1.00 133.33 ? 4414 GLU A N     1 
ATOM   21796 C  CA    . GLU A 1 4414 ? 173.103 175.425 205.579 1.00 132.68 ? 4414 GLU A CA    1 
ATOM   21797 C  C     . GLU A 1 4414 ? 172.760 175.059 204.140 1.00 131.36 ? 4414 GLU A C     1 
ATOM   21798 O  O     . GLU A 1 4414 ? 171.634 174.641 203.857 1.00 128.28 ? 4414 GLU A O     1 
ATOM   21799 C  CB    . GLU A 1 4414 ? 173.016 176.941 205.788 1.00 134.83 ? 4414 GLU A CB    1 
ATOM   21800 C  CG    . GLU A 1 4414 ? 173.959 177.763 204.907 1.00 135.18 ? 4414 GLU A CG    1 
ATOM   21801 C  CD    . GLU A 1 4414 ? 174.002 179.230 205.281 1.00 137.54 ? 4414 GLU A CD    1 
ATOM   21802 O  OE1   . GLU A 1 4414 ? 173.385 179.602 206.297 1.00 142.10 ? 4414 GLU A OE1   1 
ATOM   21803 O  OE2   . GLU A 1 4414 ? 174.628 180.018 204.538 1.00 136.61 ? 4414 GLU A OE2   1 
ATOM   21804 N  N     . ARG A 1 4415 ? 173.710 175.225 203.215 1.00 125.67 ? 4415 ARG A N     1 
ATOM   21805 C  CA    . ARG A 1 4415 ? 173.476 174.829 201.830 1.00 123.58 ? 4415 ARG A CA    1 
ATOM   21806 C  C     . ARG A 1 4415 ? 173.183 173.339 201.735 1.00 126.69 ? 4415 ARG A C     1 
ATOM   21807 O  O     . ARG A 1 4415 ? 172.284 172.917 200.993 1.00 128.99 ? 4415 ARG A O     1 
ATOM   21808 C  CB    . ARG A 1 4415 ? 174.690 175.187 200.969 1.00 121.52 ? 4415 ARG A CB    1 
ATOM   21809 C  CG    . ARG A 1 4415 ? 174.851 176.660 200.626 1.00 117.90 ? 4415 ARG A CG    1 
ATOM   21810 C  CD    . ARG A 1 4415 ? 176.085 176.867 199.754 1.00 119.74 ? 4415 ARG A CD    1 
ATOM   21811 N  NE    . ARG A 1 4415 ? 176.271 175.769 198.812 1.00 124.34 ? 4415 ARG A NE    1 
ATOM   21812 C  CZ    . ARG A 1 4415 ? 177.169 175.753 197.835 1.00 128.50 ? 4415 ARG A CZ    1 
ATOM   21813 N  NH1   . ARG A 1 4415 ? 177.986 176.774 197.627 1.00 126.73 ? 4415 ARG A NH1   1 
ATOM   21814 N  NH2   . ARG A 1 4415 ? 177.254 174.682 197.051 1.00 125.85 ? 4415 ARG A NH2   1 
ATOM   21815 N  N     . GLU A 1 4416 ? 173.941 172.527 202.478 1.00 123.69 ? 4416 GLU A N     1 
ATOM   21816 C  CA    . GLU A 1 4416 ? 173.693 171.088 202.479 1.00 117.78 ? 4416 GLU A CA    1 
ATOM   21817 C  C     . GLU A 1 4416 ? 172.280 170.767 202.943 1.00 113.98 ? 4416 GLU A C     1 
ATOM   21818 O  O     . GLU A 1 4416 ? 171.546 170.038 202.262 1.00 117.28 ? 4416 GLU A O     1 
ATOM   21819 C  CB    . GLU A 1 4416 ? 174.712 170.372 203.358 1.00 119.53 ? 4416 GLU A CB    1 
ATOM   21820 C  CG    . GLU A 1 4416 ? 176.061 170.226 202.723 1.00 121.21 ? 4416 GLU A CG    1 
ATOM   21821 C  CD    . GLU A 1 4416 ? 175.993 169.636 201.326 1.00 124.87 ? 4416 GLU A CD    1 
ATOM   21822 O  OE1   . GLU A 1 4416 ? 175.399 168.547 201.166 1.00 126.72 ? 4416 GLU A OE1   1 
ATOM   21823 O  OE2   . GLU A 1 4416 ? 176.545 170.253 200.391 1.00 122.80 ? 4416 GLU A OE2   1 
ATOM   21824 N  N     . VAL A 1 4417 ? 171.875 171.297 204.100 1.00 115.59 ? 4417 VAL A N     1 
ATOM   21825 C  CA    . VAL A 1 4417 ? 170.540 170.960 204.592 1.00 119.25 ? 4417 VAL A CA    1 
ATOM   21826 C  C     . VAL A 1 4417 ? 169.466 171.527 203.669 1.00 120.42 ? 4417 VAL A C     1 
ATOM   21827 O  O     . VAL A 1 4417 ? 168.405 170.919 203.490 1.00 118.34 ? 4417 VAL A O     1 
ATOM   21828 C  CB    . VAL A 1 4417 ? 170.344 171.419 206.048 1.00 121.89 ? 4417 VAL A CB    1 
ATOM   21829 C  CG1   . VAL A 1 4417 ? 169.104 170.760 206.625 1.00 114.31 ? 4417 VAL A CG1   1 
ATOM   21830 C  CG2   . VAL A 1 4417 ? 171.543 171.035 206.883 1.00 124.78 ? 4417 VAL A CG2   1 
ATOM   21831 N  N     . LYS A 1 4418 ? 169.729 172.680 203.049 1.00 130.37 ? 4418 LYS A N     1 
ATOM   21832 C  CA    . LYS A 1 4418 ? 168.763 173.265 202.125 1.00 130.74 ? 4418 LYS A CA    1 
ATOM   21833 C  C     . LYS A 1 4418 ? 168.517 172.351 200.932 1.00 128.90 ? 4418 LYS A C     1 
ATOM   21834 O  O     . LYS A 1 4418 ? 167.366 172.004 200.627 1.00 125.97 ? 4418 LYS A O     1 
ATOM   21835 C  CB    . LYS A 1 4418 ? 169.263 174.633 201.657 1.00 129.87 ? 4418 LYS A CB    1 
ATOM   21836 C  CG    . LYS A 1 4418 ? 168.194 175.547 201.090 1.00 127.44 ? 4418 LYS A CG    1 
ATOM   21837 C  CD    . LYS A 1 4418 ? 168.713 176.970 200.968 1.00 128.43 ? 4418 LYS A CD    1 
ATOM   21838 C  CE    . LYS A 1 4418 ? 169.271 177.466 202.293 1.00 130.33 ? 4418 LYS A CE    1 
ATOM   21839 N  NZ    . LYS A 1 4418 ? 169.804 178.854 202.201 1.00 128.97 ? 4418 LYS A NZ    1 
ATOM   21840 N  N     . MET A 1 4419 ? 169.592 171.944 200.249 1.00 119.34 ? 4419 MET A N     1 
ATOM   21841 C  CA    . MET A 1 4419 ? 169.429 171.058 199.101 1.00 116.10 ? 4419 MET A CA    1 
ATOM   21842 C  C     . MET A 1 4419 ? 168.817 169.728 199.517 1.00 116.53 ? 4419 MET A C     1 
ATOM   21843 O  O     . MET A 1 4419 ? 167.954 169.187 198.812 1.00 116.54 ? 4419 MET A O     1 
ATOM   21844 C  CB    . MET A 1 4419 ? 170.764 170.831 198.386 1.00 115.61 ? 4419 MET A CB    1 
ATOM   21845 C  CG    . MET A 1 4419 ? 171.484 172.093 197.938 1.00 116.57 ? 4419 MET A CG    1 
ATOM   21846 S  SD    . MET A 1 4419 ? 173.276 171.893 197.894 1.00 130.89 ? 4419 MET A SD    1 
ATOM   21847 C  CE    . MET A 1 4419 ? 173.809 173.602 197.883 1.00 120.82 ? 4419 MET A CE    1 
ATOM   21848 N  N     . GLY A 1 4420 ? 169.245 169.189 200.660 1.00 116.83 ? 4420 GLY A N     1 
ATOM   21849 C  CA    . GLY A 1 4420 ? 168.689 167.927 201.113 1.00 115.40 ? 4420 GLY A CA    1 
ATOM   21850 C  C     . GLY A 1 4420 ? 167.194 168.000 201.343 1.00 113.44 ? 4420 GLY A C     1 
ATOM   21851 O  O     . GLY A 1 4420 ? 166.444 167.143 200.871 1.00 113.52 ? 4420 GLY A O     1 
ATOM   21852 N  N     . ALA A 1 4421 ? 166.736 169.038 202.048 1.00 118.69 ? 4421 ALA A N     1 
ATOM   21853 C  CA    . ALA A 1 4421 ? 165.310 169.173 202.321 1.00 119.32 ? 4421 ALA A CA    1 
ATOM   21854 C  C     . ALA A 1 4421 ? 164.516 169.387 201.039 1.00 119.73 ? 4421 ALA A C     1 
ATOM   21855 O  O     . ALA A 1 4421 ? 163.453 168.780 200.856 1.00 114.56 ? 4421 ALA A O     1 
ATOM   21856 C  CB    . ALA A 1 4421 ? 165.068 170.319 203.302 1.00 120.02 ? 4421 ALA A CB    1 
ATOM   21857 N  N     . LYS A 1 4422 ? 165.013 170.240 200.137 1.00 118.96 ? 4422 LYS A N     1 
ATOM   21858 C  CA    . LYS A 1 4422 ? 164.285 170.498 198.897 1.00 114.65 ? 4422 LYS A CA    1 
ATOM   21859 C  C     . LYS A 1 4422 ? 164.141 169.221 198.076 1.00 115.54 ? 4422 LYS A C     1 
ATOM   21860 O  O     . LYS A 1 4422 ? 163.041 168.878 197.617 1.00 110.80 ? 4422 LYS A O     1 
ATOM   21861 C  CB    . LYS A 1 4422 ? 164.997 171.589 198.093 1.00 115.84 ? 4422 LYS A CB    1 
ATOM   21862 C  CG    . LYS A 1 4422 ? 164.518 171.774 196.652 1.00 114.99 ? 4422 LYS A CG    1 
ATOM   21863 C  CD    . LYS A 1 4422 ? 163.000 171.886 196.544 1.00 115.98 ? 4422 LYS A CD    1 
ATOM   21864 C  CE    . LYS A 1 4422 ? 162.493 173.174 197.171 1.00 117.75 ? 4422 LYS A CE    1 
ATOM   21865 N  NZ    . LYS A 1 4422 ? 161.114 173.506 196.717 1.00 118.50 ? 4422 LYS A NZ    1 
ATOM   21866 N  N     . LEU A 1 4423 ? 165.244 168.488 197.895 1.00 110.78 ? 4423 LEU A N     1 
ATOM   21867 C  CA    . LEU A 1 4423 ? 165.192 167.288 197.070 1.00 105.39 ? 4423 LEU A CA    1 
ATOM   21868 C  C     . LEU A 1 4423 ? 164.372 166.191 197.739 1.00 101.43 ? 4423 LEU A C     1 
ATOM   21869 O  O     . LEU A 1 4423 ? 163.661 165.440 197.061 1.00 101.72 ? 4423 LEU A O     1 
ATOM   21870 C  CB    . LEU A 1 4423 ? 166.609 166.809 196.755 1.00 100.47 ? 4423 LEU A CB    1 
ATOM   21871 C  CG    . LEU A 1 4423 ? 166.806 165.355 196.337 1.00 100.34 ? 4423 LEU A CG    1 
ATOM   21872 C  CD1   . LEU A 1 4423 ? 166.334 165.155 194.911 1.00 100.91 ? 4423 LEU A CD1   1 
ATOM   21873 C  CD2   . LEU A 1 4423 ? 168.271 164.988 196.460 1.00 103.83 ? 4423 LEU A CD2   1 
ATOM   21874 N  N     . LEU A 1 4424 ? 164.441 166.092 199.070 1.00 96.44  ? 4424 LEU A N     1 
ATOM   21875 C  CA    . LEU A 1 4424 ? 163.619 165.118 199.778 1.00 94.62  ? 4424 LEU A CA    1 
ATOM   21876 C  C     . LEU A 1 4424 ? 162.139 165.420 199.595 1.00 97.68  ? 4424 LEU A C     1 
ATOM   21877 O  O     . LEU A 1 4424 ? 161.341 164.512 199.339 1.00 95.97  ? 4424 LEU A O     1 
ATOM   21878 C  CB    . LEU A 1 4424 ? 163.987 165.106 201.262 1.00 98.51  ? 4424 LEU A CB    1 
ATOM   21879 C  CG    . LEU A 1 4424 ? 163.130 164.307 202.251 1.00 97.04  ? 4424 LEU A CG    1 
ATOM   21880 C  CD1   . LEU A 1 4424 ? 162.754 162.935 201.709 1.00 93.43  ? 4424 LEU A CD1   1 
ATOM   21881 C  CD2   . LEU A 1 4424 ? 163.842 164.177 203.588 1.00 99.68  ? 4424 LEU A CD2   1 
ATOM   21882 N  N     . GLN A 1 4425 ? 161.753 166.693 199.719 1.00 109.14 ? 4425 GLN A N     1 
ATOM   21883 C  CA    . GLN A 1 4425 ? 160.355 167.058 199.520 1.00 106.94 ? 4425 GLN A CA    1 
ATOM   21884 C  C     . GLN A 1 4425 ? 159.904 166.744 198.101 1.00 103.96 ? 4425 GLN A C     1 
ATOM   21885 O  O     . GLN A 1 4425 ? 158.813 166.197 197.894 1.00 97.58  ? 4425 GLN A O     1 
ATOM   21886 C  CB    . GLN A 1 4425 ? 160.149 168.541 199.832 1.00 107.18 ? 4425 GLN A CB    1 
ATOM   21887 C  CG    . GLN A 1 4425 ? 158.720 168.930 200.200 1.00 104.36 ? 4425 GLN A CG    1 
ATOM   21888 C  CD    . GLN A 1 4425 ? 158.313 168.500 201.602 1.00 105.42 ? 4425 GLN A CD    1 
ATOM   21889 O  OE1   . GLN A 1 4425 ? 158.789 167.493 202.127 1.00 103.93 ? 4425 GLN A OE1   1 
ATOM   21890 N  NE2   . GLN A 1 4425 ? 157.423 169.271 202.215 1.00 103.80 ? 4425 GLN A NE2   1 
ATOM   21891 N  N     . ASP A 1 4426 ? 160.738 167.072 197.110 1.00 105.90 ? 4426 ASP A N     1 
ATOM   21892 C  CA    . ASP A 1 4426 ? 160.378 166.804 195.721 1.00 103.24 ? 4426 ASP A CA    1 
ATOM   21893 C  C     . ASP A 1 4426 ? 160.194 165.308 195.479 1.00 104.14 ? 4426 ASP A C     1 
ATOM   21894 O  O     . ASP A 1 4426 ? 159.203 164.880 194.873 1.00 104.28 ? 4426 ASP A O     1 
ATOM   21895 C  CB    . ASP A 1 4426 ? 161.448 167.378 194.790 1.00 103.36 ? 4426 ASP A CB    1 
ATOM   21896 C  CG    . ASP A 1 4426 ? 160.994 167.451 193.344 1.00 107.25 ? 4426 ASP A CG    1 
ATOM   21897 O  OD1   . ASP A 1 4426 ? 161.722 168.052 192.526 1.00 109.92 ? 4426 ASP A OD1   1 
ATOM   21898 O  OD2   . ASP A 1 4426 ? 159.910 166.921 193.021 1.00 105.10 ? 4426 ASP A OD2   1 
ATOM   21899 N  N     . VAL A 1 4427 ? 161.139 164.496 195.961 1.00 98.03  ? 4427 VAL A N     1 
ATOM   21900 C  CA    . VAL A 1 4427 ? 161.070 163.054 195.744 1.00 92.30  ? 4427 VAL A CA    1 
ATOM   21901 C  C     . VAL A 1 4427 ? 159.859 162.461 196.452 1.00 93.63  ? 4427 VAL A C     1 
ATOM   21902 O  O     . VAL A 1 4427 ? 159.152 161.612 195.895 1.00 96.94  ? 4427 VAL A O     1 
ATOM   21903 C  CB    . VAL A 1 4427 ? 162.381 162.387 196.200 1.00 87.84  ? 4427 VAL A CB    1 
ATOM   21904 C  CG1   . VAL A 1 4427 ? 162.156 160.918 196.519 1.00 83.65  ? 4427 VAL A CG1   1 
ATOM   21905 C  CG2   . VAL A 1 4427 ? 163.450 162.546 195.133 1.00 94.02  ? 4427 VAL A CG2   1 
ATOM   21906 N  N     . ARG A 1 4428 ? 159.603 162.891 197.690 1.00 102.86 ? 4428 ARG A N     1 
ATOM   21907 C  CA    . ARG A 1 4428 ? 158.459 162.372 198.430 1.00 102.73 ? 4428 ARG A CA    1 
ATOM   21908 C  C     . ARG A 1 4428 ? 157.151 162.725 197.736 1.00 103.11 ? 4428 ARG A C     1 
ATOM   21909 O  O     . ARG A 1 4428 ? 156.258 161.878 197.616 1.00 98.00  ? 4428 ARG A O     1 
ATOM   21910 C  CB    . ARG A 1 4428 ? 158.474 162.910 199.860 1.00 105.05 ? 4428 ARG A CB    1 
ATOM   21911 C  CG    . ARG A 1 4428 ? 157.773 162.018 200.868 1.00 101.32 ? 4428 ARG A CG    1 
ATOM   21912 C  CD    . ARG A 1 4428 ? 158.696 160.914 201.353 1.00 97.79  ? 4428 ARG A CD    1 
ATOM   21913 N  NE    . ARG A 1 4428 ? 157.956 159.788 201.908 1.00 99.30  ? 4428 ARG A NE    1 
ATOM   21914 C  CZ    . ARG A 1 4428 ? 158.398 159.011 202.887 1.00 102.52 ? 4428 ARG A CZ    1 
ATOM   21915 N  NH1   . ARG A 1 4428 ? 159.581 159.208 203.445 1.00 104.45 ? 4428 ARG A NH1   1 
ATOM   21916 N  NH2   . ARG A 1 4428 ? 157.635 158.009 203.315 1.00 102.09 ? 4428 ARG A NH2   1 
ATOM   21917 N  N     . GLN A 1 4429 ? 157.022 163.968 197.261 1.00 110.31 ? 4429 GLN A N     1 
ATOM   21918 C  CA    . GLN A 1 4429 ? 155.813 164.363 196.547 1.00 108.63 ? 4429 GLN A CA    1 
ATOM   21919 C  C     . GLN A 1 4429 ? 155.631 163.547 195.274 1.00 102.86 ? 4429 GLN A C     1 
ATOM   21920 O  O     . GLN A 1 4429 ? 154.525 163.071 194.984 1.00 103.11 ? 4429 GLN A O     1 
ATOM   21921 C  CB    . GLN A 1 4429 ? 155.863 165.856 196.222 1.00 111.03 ? 4429 GLN A CB    1 
ATOM   21922 C  CG    . GLN A 1 4429 ? 154.606 166.394 195.561 1.00 107.71 ? 4429 GLN A CG    1 
ATOM   21923 C  CD    . GLN A 1 4429 ? 153.406 166.368 196.484 1.00 110.68 ? 4429 GLN A CD    1 
ATOM   21924 O  OE1   . GLN A 1 4429 ? 152.564 165.474 196.401 1.00 110.75 ? 4429 GLN A OE1   1 
ATOM   21925 N  NE2   . GLN A 1 4429 ? 153.320 167.353 197.371 1.00 109.97 ? 4429 GLN A NE2   1 
ATOM   21926 N  N     . ASP A 1 4430 ? 156.708 163.365 194.505 1.00 94.97  ? 4430 ASP A N     1 
ATOM   21927 C  CA    . ASP A 1 4430 ? 156.604 162.615 193.257 1.00 94.01  ? 4430 ASP A CA    1 
ATOM   21928 C  C     . ASP A 1 4430 ? 156.214 161.164 193.510 1.00 99.46  ? 4430 ASP A C     1 
ATOM   21929 O  O     . ASP A 1 4430 ? 155.358 160.608 192.809 1.00 103.61 ? 4430 ASP A O     1 
ATOM   21930 C  CB    . ASP A 1 4430 ? 157.925 162.689 192.494 1.00 97.99  ? 4430 ASP A CB    1 
ATOM   21931 C  CG    . ASP A 1 4430 ? 157.946 163.813 191.483 1.00 104.67 ? 4430 ASP A CG    1 
ATOM   21932 O  OD1   . ASP A 1 4430 ? 156.862 164.174 190.982 1.00 106.41 ? 4430 ASP A OD1   1 
ATOM   21933 O  OD2   . ASP A 1 4430 ? 159.043 164.334 191.191 1.00 106.62 ? 4430 ASP A OD2   1 
ATOM   21934 N  N     . LEU A 1 4431 ? 156.822 160.536 194.516 1.00 102.26 ? 4431 LEU A N     1 
ATOM   21935 C  CA    . LEU A 1 4431 ? 156.523 159.135 194.789 1.00 100.04 ? 4431 LEU A CA    1 
ATOM   21936 C  C     . LEU A 1 4431 ? 155.121 158.972 195.366 1.00 100.10 ? 4431 LEU A C     1 
ATOM   21937 O  O     . LEU A 1 4431 ? 154.439 157.980 195.084 1.00 96.16  ? 4431 LEU A O     1 
ATOM   21938 C  CB    . LEU A 1 4431 ? 157.577 158.559 195.729 1.00 99.90  ? 4431 LEU A CB    1 
ATOM   21939 C  CG    . LEU A 1 4431 ? 158.677 157.746 195.047 1.00 96.09  ? 4431 LEU A CG    1 
ATOM   21940 C  CD1   . LEU A 1 4431 ? 159.551 157.075 196.083 1.00 99.39  ? 4431 LEU A CD1   1 
ATOM   21941 C  CD2   . LEU A 1 4431 ? 158.083 156.724 194.094 1.00 93.51  ? 4431 LEU A CD2   1 
ATOM   21942 N  N     . ALA A 1 4432 ? 154.670 159.939 196.171 1.00 113.19 ? 4432 ALA A N     1 
ATOM   21943 C  CA    . ALA A 1 4432 ? 153.293 159.915 196.649 1.00 110.07 ? 4432 ALA A CA    1 
ATOM   21944 C  C     . ALA A 1 4432 ? 152.313 160.039 195.492 1.00 112.36 ? 4432 ALA A C     1 
ATOM   21945 O  O     . ALA A 1 4432 ? 151.279 159.363 195.472 1.00 111.11 ? 4432 ALA A O     1 
ATOM   21946 C  CB    . ALA A 1 4432 ? 153.070 161.031 197.669 1.00 110.67 ? 4432 ALA A CB    1 
ATOM   21947 N  N     . ASP A 1 4433 ? 152.620 160.899 194.517 1.00 120.39 ? 4433 ASP A N     1 
ATOM   21948 C  CA    . ASP A 1 4433 ? 151.771 161.003 193.333 1.00 112.26 ? 4433 ASP A CA    1 
ATOM   21949 C  C     . ASP A 1 4433 ? 151.759 159.700 192.542 1.00 108.64 ? 4433 ASP A C     1 
ATOM   21950 O  O     . ASP A 1 4433 ? 150.718 159.297 192.011 1.00 111.12 ? 4433 ASP A O     1 
ATOM   21951 C  CB    . ASP A 1 4433 ? 152.237 162.162 192.453 1.00 114.22 ? 4433 ASP A CB    1 
ATOM   21952 C  CG    . ASP A 1 4433 ? 151.941 163.514 193.067 1.00 118.88 ? 4433 ASP A CG    1 
ATOM   21953 O  OD1   . ASP A 1 4433 ? 151.834 163.595 194.308 1.00 117.14 ? 4433 ASP A OD1   1 
ATOM   21954 O  OD2   . ASP A 1 4433 ? 151.814 164.498 192.307 1.00 121.79 ? 4433 ASP A OD2   1 
ATOM   21955 N  N     . VAL A 1 4434 ? 152.912 159.034 192.442 1.00 105.40 ? 4434 VAL A N     1 
ATOM   21956 C  CA    . VAL A 1 4434 ? 152.968 157.751 191.742 1.00 107.51 ? 4434 VAL A CA    1 
ATOM   21957 C  C     . VAL A 1 4434 ? 152.096 156.717 192.446 1.00 109.03 ? 4434 VAL A C     1 
ATOM   21958 O  O     . VAL A 1 4434 ? 151.331 155.984 191.804 1.00 109.30 ? 4434 VAL A O     1 
ATOM   21959 C  CB    . VAL A 1 4434 ? 154.426 157.273 191.618 1.00 109.35 ? 4434 VAL A CB    1 
ATOM   21960 C  CG1   . VAL A 1 4434 ? 154.475 155.810 191.214 1.00 106.36 ? 4434 VAL A CG1   1 
ATOM   21961 C  CG2   . VAL A 1 4434 ? 155.177 158.129 190.616 1.00 106.20 ? 4434 VAL A CG2   1 
ATOM   21962 N  N     . VAL A 1 4435 ? 152.195 156.644 193.776 1.00 119.08 ? 4435 VAL A N     1 
ATOM   21963 C  CA    . VAL A 1 4435 ? 151.346 155.732 194.541 1.00 117.66 ? 4435 VAL A CA    1 
ATOM   21964 C  C     . VAL A 1 4435 ? 149.877 156.074 194.332 1.00 119.56 ? 4435 VAL A C     1 
ATOM   21965 O  O     . VAL A 1 4435 ? 149.031 155.186 194.167 1.00 119.24 ? 4435 VAL A O     1 
ATOM   21966 C  CB    . VAL A 1 4435 ? 151.723 155.769 196.034 1.00 119.76 ? 4435 VAL A CB    1 
ATOM   21967 C  CG1   . VAL A 1 4435 ? 150.708 154.996 196.860 1.00 118.38 ? 4435 VAL A CG1   1 
ATOM   21968 C  CG2   . VAL A 1 4435 ? 153.111 155.206 196.246 1.00 119.06 ? 4435 VAL A CG2   1 
ATOM   21969 N  N     . GLN A 1 4436 ? 149.552 157.369 194.332 1.00 121.62 ? 4436 GLN A N     1 
ATOM   21970 C  CA    . GLN A 1 4436 ? 148.172 157.799 194.148 1.00 117.48 ? 4436 GLN A CA    1 
ATOM   21971 C  C     . GLN A 1 4436 ? 147.640 157.359 192.790 1.00 116.12 ? 4436 GLN A C     1 
ATOM   21972 O  O     . GLN A 1 4436 ? 146.498 156.900 192.679 1.00 116.48 ? 4436 GLN A O     1 
ATOM   21973 C  CB    . GLN A 1 4436 ? 148.087 159.320 194.285 1.00 121.00 ? 4436 GLN A CB    1 
ATOM   21974 C  CG    . GLN A 1 4436 ? 148.008 159.832 195.719 1.00 121.00 ? 4436 GLN A CG    1 
ATOM   21975 C  CD    . GLN A 1 4436 ? 146.645 159.649 196.344 1.00 120.23 ? 4436 GLN A CD    1 
ATOM   21976 O  OE1   . GLN A 1 4436 ? 146.228 158.528 196.627 1.00 119.45 ? 4436 GLN A OE1   1 
ATOM   21977 N  NE2   . GLN A 1 4436 ? 145.944 160.753 196.573 1.00 120.17 ? 4436 GLN A NE2   1 
ATOM   21978 N  N     . VAL A 1 4437 ? 148.460 157.495 191.745 1.00 114.73 ? 4437 VAL A N     1 
ATOM   21979 C  CA    . VAL A 1 4437 ? 148.050 157.071 190.408 1.00 114.45 ? 4437 VAL A CA    1 
ATOM   21980 C  C     . VAL A 1 4437 ? 147.853 155.564 190.360 1.00 117.86 ? 4437 VAL A C     1 
ATOM   21981 O  O     . VAL A 1 4437 ? 146.876 155.070 189.783 1.00 120.73 ? 4437 VAL A O     1 
ATOM   21982 C  CB    . VAL A 1 4437 ? 149.075 157.537 189.358 1.00 112.59 ? 4437 VAL A CB    1 
ATOM   21983 C  CG1   . VAL A 1 4437 ? 148.830 156.838 188.027 1.00 109.17 ? 4437 VAL A CG1   1 
ATOM   21984 C  CG2   . VAL A 1 4437 ? 148.992 159.029 189.185 1.00 116.30 ? 4437 VAL A CG2   1 
ATOM   21985 N  N     . CYS A 1 4438 ? 148.775 154.808 190.964 1.00 130.93 ? 4438 CYS A N     1 
ATOM   21986 C  CA    . CYS A 1 4438 ? 148.666 153.352 190.929 1.00 128.94 ? 4438 CYS A CA    1 
ATOM   21987 C  C     . CYS A 1 4438 ? 147.386 152.865 191.596 1.00 130.52 ? 4438 CYS A C     1 
ATOM   21988 O  O     . CYS A 1 4438 ? 146.889 151.782 191.268 1.00 127.83 ? 4438 CYS A O     1 
ATOM   21989 C  CB    . CYS A 1 4438 ? 149.887 152.717 191.589 1.00 129.52 ? 4438 CYS A CB    1 
ATOM   21990 S  SG    . CYS A 1 4438 ? 151.396 152.813 190.601 1.00 137.35 ? 4438 CYS A SG    1 
ATOM   21991 N  N     . GLU A 1 4439 ? 146.841 153.642 192.529 1.00 135.13 ? 4439 GLU A N     1 
ATOM   21992 C  CA    . GLU A 1 4439 ? 145.548 153.349 193.129 1.00 131.62 ? 4439 GLU A CA    1 
ATOM   21993 C  C     . GLU A 1 4439 ? 144.385 153.944 192.344 1.00 132.69 ? 4439 GLU A C     1 
ATOM   21994 O  O     . GLU A 1 4439 ? 143.228 153.660 192.668 1.00 133.87 ? 4439 GLU A O     1 
ATOM   21995 C  CB    . GLU A 1 4439 ? 145.511 153.853 194.576 1.00 131.49 ? 4439 GLU A CB    1 
ATOM   21996 C  CG    . GLU A 1 4439 ? 146.218 152.939 195.566 1.00 131.61 ? 4439 GLU A CG    1 
ATOM   21997 C  CD    . GLU A 1 4439 ? 146.684 153.670 196.811 1.00 134.31 ? 4439 GLU A CD    1 
ATOM   21998 O  OE1   . GLU A 1 4439 ? 146.073 154.701 197.163 1.00 136.04 ? 4439 GLU A OE1   1 
ATOM   21999 O  OE2   . GLU A 1 4439 ? 147.662 153.211 197.438 1.00 133.85 ? 4439 GLU A OE2   1 
ATOM   22000 N  N     . GLY A 1 4440 ? 144.663 154.759 191.327 1.00 127.89 ? 4440 GLY A N     1 
ATOM   22001 C  CA    . GLY A 1 4440 ? 143.627 155.316 190.482 1.00 123.22 ? 4440 GLY A CA    1 
ATOM   22002 C  C     . GLY A 1 4440 ? 142.913 156.530 191.030 1.00 123.84 ? 4440 GLY A C     1 
ATOM   22003 O  O     . GLY A 1 4440 ? 141.925 156.967 190.430 1.00 126.22 ? 4440 GLY A O     1 
ATOM   22004 N  N     . LYS A 1 4441 ? 143.373 157.091 192.150 1.00 130.53 ? 4441 LYS A N     1 
ATOM   22005 C  CA    . LYS A 1 4441 ? 142.659 158.212 192.751 1.00 131.67 ? 4441 LYS A CA    1 
ATOM   22006 C  C     . LYS A 1 4441 ? 142.857 159.508 191.971 1.00 132.01 ? 4441 LYS A C     1 
ATOM   22007 O  O     . LYS A 1 4441 ? 141.981 160.380 191.998 1.00 131.13 ? 4441 LYS A O     1 
ATOM   22008 C  CB    . LYS A 1 4441 ? 143.089 158.391 194.208 1.00 131.19 ? 4441 LYS A CB    1 
ATOM   22009 C  CG    . LYS A 1 4441 ? 142.758 157.201 195.101 1.00 131.02 ? 4441 LYS A CG    1 
ATOM   22010 C  CD    . LYS A 1 4441 ? 143.426 157.333 196.458 1.00 131.91 ? 4441 LYS A CD    1 
ATOM   22011 C  CE    . LYS A 1 4441 ? 142.836 156.382 197.483 1.00 130.09 ? 4441 LYS A CE    1 
ATOM   22012 N  NZ    . LYS A 1 4441 ? 143.590 156.442 198.767 1.00 128.42 ? 4441 LYS A NZ    1 
ATOM   22013 N  N     . LYS A 1 4442 ? 143.984 159.662 191.278 1.00 120.13 ? 4442 LYS A N     1 
ATOM   22014 C  CA    . LYS A 1 4442 ? 144.268 160.882 190.535 1.00 120.06 ? 4442 LYS A CA    1 
ATOM   22015 C  C     . LYS A 1 4442 ? 144.672 160.543 189.106 1.00 117.30 ? 4442 LYS A C     1 
ATOM   22016 O  O     . LYS A 1 4442 ? 145.118 159.433 188.806 1.00 115.37 ? 4442 LYS A O     1 
ATOM   22017 C  CB    . LYS A 1 4442 ? 145.366 161.717 191.214 1.00 120.47 ? 4442 LYS A CB    1 
ATOM   22018 C  CG    . LYS A 1 4442 ? 146.781 161.308 190.854 1.00 118.18 ? 4442 LYS A CG    1 
ATOM   22019 C  CD    . LYS A 1 4442 ? 147.803 162.139 191.610 1.00 118.65 ? 4442 LYS A CD    1 
ATOM   22020 C  CE    . LYS A 1 4442 ? 147.643 163.620 191.310 1.00 117.77 ? 4442 LYS A CE    1 
ATOM   22021 N  NZ    . LYS A 1 4442 ? 148.417 164.025 190.104 1.00 116.40 ? 4442 LYS A NZ    1 
ATOM   22022 N  N     . LYS A 1 4443 ? 144.496 161.523 188.223 1.00 116.12 ? 4443 LYS A N     1 
ATOM   22023 C  CA    . LYS A 1 4443 ? 144.771 161.348 186.805 1.00 115.93 ? 4443 LYS A CA    1 
ATOM   22024 C  C     . LYS A 1 4443 ? 146.253 161.563 186.512 1.00 113.21 ? 4443 LYS A C     1 
ATOM   22025 O  O     . LYS A 1 4443 ? 146.985 162.165 187.303 1.00 112.88 ? 4443 LYS A O     1 
ATOM   22026 C  CB    . LYS A 1 4443 ? 143.919 162.318 185.982 1.00 117.92 ? 4443 LYS A CB    1 
ATOM   22027 C  CG    . LYS A 1 4443 ? 143.838 162.009 184.495 1.00 116.42 ? 4443 LYS A CG    1 
ATOM   22028 C  CD    . LYS A 1 4443 ? 142.537 162.517 183.900 1.00 116.10 ? 4443 LYS A CD    1 
ATOM   22029 C  CE    . LYS A 1 4443 ? 142.330 161.983 182.494 1.00 117.20 ? 4443 LYS A CE    1 
ATOM   22030 N  NZ    . LYS A 1 4443 ? 143.174 162.708 181.504 1.00 114.68 ? 4443 LYS A NZ    1 
ATOM   22031 N  N     . GLN A 1 4444 ? 146.692 161.059 185.360 1.00 105.36 ? 4444 GLN A N     1 
ATOM   22032 C  CA    . GLN A 1 4444 ? 148.083 161.181 184.947 1.00 108.82 ? 4444 GLN A CA    1 
ATOM   22033 C  C     . GLN A 1 4444 ? 148.296 162.461 184.148 1.00 110.15 ? 4444 GLN A C     1 
ATOM   22034 O  O     . GLN A 1 4444 ? 147.492 162.799 183.274 1.00 112.05 ? 4444 GLN A O     1 
ATOM   22035 C  CB    . GLN A 1 4444 ? 148.496 159.971 184.110 1.00 107.12 ? 4444 GLN A CB    1 
ATOM   22036 C  CG    . GLN A 1 4444 ? 148.085 158.634 184.695 1.00 112.06 ? 4444 GLN A CG    1 
ATOM   22037 C  CD    . GLN A 1 4444 ? 148.617 157.466 183.890 1.00 113.16 ? 4444 GLN A CD    1 
ATOM   22038 O  OE1   . GLN A 1 4444 ? 147.871 156.558 183.525 1.00 112.24 ? 4444 GLN A OE1   1 
ATOM   22039 N  NE2   . GLN A 1 4444 ? 149.913 157.486 183.605 1.00 111.60 ? 4444 GLN A NE2   1 
ATOM   22040 N  N     . THR A 1 4445 ? 149.381 163.168 184.446 1.00 101.61 ? 4445 THR A N     1 
ATOM   22041 C  CA    . THR A 1 4445 ? 149.786 164.362 183.720 1.00 99.86  ? 4445 THR A CA    1 
ATOM   22042 C  C     . THR A 1 4445 ? 151.009 164.045 182.864 1.00 100.70 ? 4445 THR A C     1 
ATOM   22043 O  O     . THR A 1 4445 ? 151.534 162.930 182.883 1.00 106.14 ? 4445 THR A O     1 
ATOM   22044 C  CB    . THR A 1 4445 ? 150.073 165.512 184.688 1.00 98.22  ? 4445 THR A CB    1 
ATOM   22045 O  OG1   . THR A 1 4445 ? 151.355 165.316 185.297 1.00 98.41  ? 4445 THR A OG1   1 
ATOM   22046 C  CG2   . THR A 1 4445 ? 149.009 165.569 185.773 1.00 99.21  ? 4445 THR A CG2   1 
ATOM   22047 N  N     . ASN A 1 4446 ? 151.461 165.043 182.100 1.00 89.65  ? 4446 ASN A N     1 
ATOM   22048 C  CA    . ASN A 1 4446 ? 152.623 164.844 181.236 1.00 87.40  ? 4446 ASN A CA    1 
ATOM   22049 C  C     . ASN A 1 4446 ? 153.867 164.520 182.052 1.00 87.51  ? 4446 ASN A C     1 
ATOM   22050 O  O     . ASN A 1 4446 ? 154.547 163.517 181.802 1.00 87.87  ? 4446 ASN A O     1 
ATOM   22051 C  CB    . ASN A 1 4446 ? 152.861 166.087 180.380 1.00 90.78  ? 4446 ASN A CB    1 
ATOM   22052 C  CG    . ASN A 1 4446 ? 151.902 166.187 179.219 1.00 88.86  ? 4446 ASN A CG    1 
ATOM   22053 O  OD1   . ASN A 1 4446 ? 150.738 166.536 179.394 1.00 91.05  ? 4446 ASN A OD1   1 
ATOM   22054 N  ND2   . ASN A 1 4446 ? 152.386 165.881 178.021 1.00 84.96  ? 4446 ASN A ND2   1 
ATOM   22055 N  N     . TYR A 1 4447 ? 154.176 165.360 183.041 1.00 94.63  ? 4447 TYR A N     1 
ATOM   22056 C  CA    . TYR A 1 4447 ? 155.333 165.105 183.892 1.00 96.07  ? 4447 TYR A CA    1 
ATOM   22057 C  C     . TYR A 1 4447 ? 155.151 163.827 184.694 1.00 91.02  ? 4447 TYR A C     1 
ATOM   22058 O  O     . TYR A 1 4447 ? 156.101 163.057 184.878 1.00 95.52  ? 4447 TYR A O     1 
ATOM   22059 C  CB    . TYR A 1 4447 ? 155.571 166.288 184.827 1.00 96.92  ? 4447 TYR A CB    1 
ATOM   22060 C  CG    . TYR A 1 4447 ? 156.547 165.984 185.939 1.00 93.22  ? 4447 TYR A CG    1 
ATOM   22061 C  CD1   . TYR A 1 4447 ? 157.903 165.846 185.681 1.00 95.78  ? 4447 TYR A CD1   1 
ATOM   22062 C  CD2   . TYR A 1 4447 ? 156.109 165.824 187.246 1.00 93.05  ? 4447 TYR A CD2   1 
ATOM   22063 C  CE1   . TYR A 1 4447 ? 158.797 165.564 186.695 1.00 96.73  ? 4447 TYR A CE1   1 
ATOM   22064 C  CE2   . TYR A 1 4447 ? 156.994 165.543 188.264 1.00 95.85  ? 4447 TYR A CE2   1 
ATOM   22065 C  CZ    . TYR A 1 4447 ? 158.337 165.413 187.985 1.00 99.03  ? 4447 TYR A CZ    1 
ATOM   22066 O  OH    . TYR A 1 4447 ? 159.223 165.132 188.999 1.00 103.27 ? 4447 TYR A OH    1 
ATOM   22067 N  N     . LEU A 1 4448 ? 153.937 163.589 185.192 1.00 95.03  ? 4448 LEU A N     1 
ATOM   22068 C  CA    . LEU A 1 4448 ? 153.678 162.375 185.956 1.00 94.09  ? 4448 LEU A CA    1 
ATOM   22069 C  C     . LEU A 1 4448 ? 153.823 161.135 185.082 1.00 96.60  ? 4448 LEU A C     1 
ATOM   22070 O  O     . LEU A 1 4448 ? 154.396 160.128 185.513 1.00 102.59 ? 4448 LEU A O     1 
ATOM   22071 C  CB    . LEU A 1 4448 ? 152.288 162.452 186.581 1.00 93.33  ? 4448 LEU A CB    1 
ATOM   22072 C  CG    . LEU A 1 4448 ? 151.967 161.506 187.732 1.00 94.62  ? 4448 LEU A CG    1 
ATOM   22073 C  CD1   . LEU A 1 4448 ? 153.101 161.490 188.737 1.00 97.44  ? 4448 LEU A CD1   1 
ATOM   22074 C  CD2   . LEU A 1 4448 ? 150.693 161.981 188.394 1.00 99.02  ? 4448 LEU A CD2   1 
ATOM   22075 N  N     . ARG A 1 4449 ? 153.324 161.195 183.845 1.00 96.11  ? 4449 ARG A N     1 
ATOM   22076 C  CA    . ARG A 1 4449 ? 153.494 160.077 182.919 1.00 92.79  ? 4449 ARG A CA    1 
ATOM   22077 C  C     . ARG A 1 4449 ? 154.967 159.837 182.619 1.00 93.23  ? 4449 ARG A C     1 
ATOM   22078 O  O     . ARG A 1 4449 ? 155.424 158.689 182.564 1.00 95.76  ? 4449 ARG A O     1 
ATOM   22079 C  CB    . ARG A 1 4449 ? 152.725 160.342 181.625 1.00 96.97  ? 4449 ARG A CB    1 
ATOM   22080 C  CG    . ARG A 1 4449 ? 152.758 159.191 180.635 1.00 96.73  ? 4449 ARG A CG    1 
ATOM   22081 C  CD    . ARG A 1 4449 ? 152.087 159.569 179.324 1.00 97.93  ? 4449 ARG A CD    1 
ATOM   22082 N  NE    . ARG A 1 4449 ? 151.061 160.590 179.501 1.00 99.74  ? 4449 ARG A NE    1 
ATOM   22083 C  CZ    . ARG A 1 4449 ? 149.774 160.335 179.690 1.00 97.79  ? 4449 ARG A CZ    1 
ATOM   22084 N  NH1   . ARG A 1 4449 ? 149.313 159.095 179.723 1.00 98.19  ? 4449 ARG A NH1   1 
ATOM   22085 N  NH2   . ARG A 1 4449 ? 148.928 161.349 179.846 1.00 93.43  ? 4449 ARG A NH2   1 
ATOM   22086 N  N     . THR A 1 4450 ? 155.726 160.914 182.411 1.00 96.37  ? 4450 THR A N     1 
ATOM   22087 C  CA    . THR A 1 4450 ? 157.154 160.776 182.142 1.00 96.07  ? 4450 THR A CA    1 
ATOM   22088 C  C     . THR A 1 4450 ? 157.877 160.140 183.326 1.00 92.00  ? 4450 THR A C     1 
ATOM   22089 O  O     . THR A 1 4450 ? 158.721 159.251 183.150 1.00 92.70  ? 4450 THR A O     1 
ATOM   22090 C  CB    . THR A 1 4450 ? 157.747 162.147 181.812 1.00 96.62  ? 4450 THR A CB    1 
ATOM   22091 O  OG1   . THR A 1 4450 ? 156.991 162.749 180.754 1.00 98.29  ? 4450 THR A OG1   1 
ATOM   22092 C  CG2   . THR A 1 4450 ? 159.184 162.016 181.357 1.00 94.14  ? 4450 THR A CG2   1 
ATOM   22093 N  N     . LEU A 1 4451 ? 157.549 160.581 184.543 1.00 93.04  ? 4451 LEU A N     1 
ATOM   22094 C  CA    . LEU A 1 4451 ? 158.162 160.010 185.737 1.00 88.07  ? 4451 LEU A CA    1 
ATOM   22095 C  C     . LEU A 1 4451 ? 157.808 158.536 185.884 1.00 89.43  ? 4451 LEU A C     1 
ATOM   22096 O  O     . LEU A 1 4451 ? 158.665 157.718 186.238 1.00 98.46  ? 4451 LEU A O     1 
ATOM   22097 C  CB    . LEU A 1 4451 ? 157.724 160.798 186.972 1.00 91.58  ? 4451 LEU A CB    1 
ATOM   22098 C  CG    . LEU A 1 4451 ? 157.802 160.109 188.334 1.00 88.82  ? 4451 LEU A CG    1 
ATOM   22099 C  CD1   . LEU A 1 4451 ? 159.246 159.838 188.718 1.00 92.00  ? 4451 LEU A CD1   1 
ATOM   22100 C  CD2   . LEU A 1 4451 ? 157.118 160.957 189.388 1.00 92.40  ? 4451 LEU A CD2   1 
ATOM   22101 N  N     . ILE A 1 4452 ? 156.551 158.179 185.611 1.00 92.21  ? 4452 ILE A N     1 
ATOM   22102 C  CA    . ILE A 1 4452 ? 156.153 156.773 185.629 1.00 92.42  ? 4452 ILE A CA    1 
ATOM   22103 C  C     . ILE A 1 4452 ? 156.971 155.981 184.619 1.00 95.43  ? 4452 ILE A C     1 
ATOM   22104 O  O     . ILE A 1 4452 ? 157.435 154.869 184.904 1.00 98.10  ? 4452 ILE A O     1 
ATOM   22105 C  CB    . ILE A 1 4452 ? 154.642 156.644 185.353 1.00 93.91  ? 4452 ILE A CB    1 
ATOM   22106 C  CG1   . ILE A 1 4452 ? 153.826 157.235 186.505 1.00 94.75  ? 4452 ILE A CG1   1 
ATOM   22107 C  CG2   . ILE A 1 4452 ? 154.265 155.193 185.109 1.00 92.24  ? 4452 ILE A CG2   1 
ATOM   22108 C  CD1   . ILE A 1 4452 ? 153.690 156.327 187.697 1.00 96.44  ? 4452 ILE A CD1   1 
ATOM   22109 N  N     . ASN A 1 4453 ? 157.164 156.544 183.424 1.00 108.02 ? 4453 ASN A N     1 
ATOM   22110 C  CA    . ASN A 1 4453 ? 157.909 155.845 182.382 1.00 107.50 ? 4453 ASN A CA    1 
ATOM   22111 C  C     . ASN A 1 4453 ? 159.352 155.593 182.800 1.00 107.65 ? 4453 ASN A C     1 
ATOM   22112 O  O     . ASN A 1 4453 ? 159.878 154.493 182.595 1.00 105.05 ? 4453 ASN A O     1 
ATOM   22113 C  CB    . ASN A 1 4453 ? 157.859 156.642 181.079 1.00 106.03 ? 4453 ASN A CB    1 
ATOM   22114 C  CG    . ASN A 1 4453 ? 158.441 155.878 179.909 1.00 107.72 ? 4453 ASN A CG    1 
ATOM   22115 O  OD1   . ASN A 1 4453 ? 159.655 155.860 179.706 1.00 109.05 ? 4453 ASN A OD1   1 
ATOM   22116 N  ND2   . ASN A 1 4453 ? 157.576 155.236 179.133 1.00 109.07 ? 4453 ASN A ND2   1 
ATOM   22117 N  N     . GLU A 1 4454 ? 160.014 156.597 183.383 1.00 107.32 ? 4454 GLU A N     1 
ATOM   22118 C  CA    . GLU A 1 4454 ? 161.379 156.364 183.856 1.00 100.65 ? 4454 GLU A CA    1 
ATOM   22119 C  C     . GLU A 1 4454 ? 161.414 155.372 185.013 1.00 98.53  ? 4454 GLU A C     1 
ATOM   22120 O  O     . GLU A 1 4454 ? 162.333 154.550 185.098 1.00 103.09 ? 4454 GLU A O     1 
ATOM   22121 C  CB    . GLU A 1 4454 ? 162.074 157.665 184.262 1.00 104.03 ? 4454 GLU A CB    1 
ATOM   22122 C  CG    . GLU A 1 4454 ? 162.666 158.459 183.108 1.00 105.10 ? 4454 GLU A CG    1 
ATOM   22123 C  CD    . GLU A 1 4454 ? 161.640 159.236 182.330 1.00 110.38 ? 4454 GLU A CD    1 
ATOM   22124 O  OE1   . GLU A 1 4454 ? 161.353 158.868 181.172 1.00 110.05 ? 4454 GLU A OE1   1 
ATOM   22125 O  OE2   . GLU A 1 4454 ? 161.154 160.246 182.873 1.00 110.65 ? 4454 GLU A OE2   1 
ATOM   22126 N  N     . LEU A 1 4455 ? 160.435 155.433 185.918 1.00 86.56  ? 4455 LEU A N     1 
ATOM   22127 C  CA    . LEU A 1 4455 ? 160.439 154.519 187.057 1.00 87.33  ? 4455 LEU A CA    1 
ATOM   22128 C  C     . LEU A 1 4455 ? 160.255 153.073 186.613 1.00 98.42  ? 4455 LEU A C     1 
ATOM   22129 O  O     . LEU A 1 4455 ? 160.859 152.161 187.191 1.00 98.29  ? 4455 LEU A O     1 
ATOM   22130 C  CB    . LEU A 1 4455 ? 159.357 154.916 188.059 1.00 87.74  ? 4455 LEU A CB    1 
ATOM   22131 C  CG    . LEU A 1 4455 ? 159.635 156.167 188.894 1.00 91.36  ? 4455 LEU A CG    1 
ATOM   22132 C  CD1   . LEU A 1 4455 ? 158.695 156.235 190.087 1.00 92.92  ? 4455 LEU A CD1   1 
ATOM   22133 C  CD2   . LEU A 1 4455 ? 161.085 156.205 189.345 1.00 92.85  ? 4455 LEU A CD2   1 
ATOM   22134 N  N     . VAL A 1 4456 ? 159.420 152.841 185.598 1.00 106.59 ? 4456 VAL A N     1 
ATOM   22135 C  CA    . VAL A 1 4456 ? 159.169 151.474 185.144 1.00 101.50 ? 4456 VAL A CA    1 
ATOM   22136 C  C     . VAL A 1 4456 ? 160.442 150.846 184.588 1.00 102.61 ? 4456 VAL A C     1 
ATOM   22137 O  O     . VAL A 1 4456 ? 160.779 149.701 184.913 1.00 106.04 ? 4456 VAL A O     1 
ATOM   22138 C  CB    . VAL A 1 4456 ? 158.028 151.454 184.110 1.00 96.49  ? 4456 VAL A CB    1 
ATOM   22139 C  CG1   . VAL A 1 4456 ? 157.983 150.115 183.396 1.00 97.15  ? 4456 VAL A CG1   1 
ATOM   22140 C  CG2   . VAL A 1 4456 ? 156.700 151.734 184.791 1.00 100.99 ? 4456 VAL A CG2   1 
ATOM   22141 N  N     . LYS A 1 4457 ? 161.177 151.584 183.759 1.00 104.06 ? 4457 LYS A N     1 
ATOM   22142 C  CA    . LYS A 1 4457 ? 162.384 151.060 183.129 1.00 101.43 ? 4457 LYS A CA    1 
ATOM   22143 C  C     . LYS A 1 4457 ? 163.601 151.089 184.046 1.00 100.19 ? 4457 LYS A C     1 
ATOM   22144 O  O     . LYS A 1 4457 ? 164.704 150.768 183.591 1.00 103.81 ? 4457 LYS A O     1 
ATOM   22145 C  CB    . LYS A 1 4457 ? 162.691 151.835 181.845 1.00 101.34 ? 4457 LYS A CB    1 
ATOM   22146 C  CG    . LYS A 1 4457 ? 161.464 152.216 181.040 1.00 104.56 ? 4457 LYS A CG    1 
ATOM   22147 C  CD    . LYS A 1 4457 ? 161.814 152.450 179.580 1.00 102.42 ? 4457 LYS A CD    1 
ATOM   22148 C  CE    . LYS A 1 4457 ? 162.863 153.539 179.434 1.00 103.37 ? 4457 LYS A CE    1 
ATOM   22149 N  NZ    . LYS A 1 4457 ? 162.817 154.179 178.090 1.00 105.37 ? 4457 LYS A NZ    1 
ATOM   22150 N  N     . GLY A 1 4458 ? 163.432 151.457 185.311 1.00 100.82 ? 4458 GLY A N     1 
ATOM   22151 C  CA    . GLY A 1 4458 ? 164.555 151.518 186.230 1.00 105.07 ? 4458 GLY A CA    1 
ATOM   22152 C  C     . GLY A 1 4458 ? 165.603 152.543 185.857 1.00 103.84 ? 4458 GLY A C     1 
ATOM   22153 O  O     . GLY A 1 4458 ? 166.804 152.270 185.980 1.00 107.40 ? 4458 GLY A O     1 
ATOM   22154 N  N     . ILE A 1 4459 ? 165.180 153.717 185.402 1.00 103.39 ? 4459 ILE A N     1 
ATOM   22155 C  CA    . ILE A 1 4459 ? 166.078 154.804 185.032 1.00 103.55 ? 4459 ILE A CA    1 
ATOM   22156 C  C     . ILE A 1 4459 ? 165.821 155.969 185.975 1.00 107.98 ? 4459 ILE A C     1 
ATOM   22157 O  O     . ILE A 1 4459 ? 164.666 156.355 186.193 1.00 113.88 ? 4459 ILE A O     1 
ATOM   22158 C  CB    . ILE A 1 4459 ? 165.882 155.224 183.564 1.00 106.11 ? 4459 ILE A CB    1 
ATOM   22159 C  CG1   . ILE A 1 4459 ? 166.576 154.234 182.629 1.00 107.55 ? 4459 ILE A CG1   1 
ATOM   22160 C  CG2   . ILE A 1 4459 ? 166.410 156.632 183.330 1.00 104.81 ? 4459 ILE A CG2   1 
ATOM   22161 C  CD1   . ILE A 1 4459 ? 166.165 154.376 181.180 1.00 109.12 ? 4459 ILE A CD1   1 
ATOM   22162 N  N     . LEU A 1 4460 ? 166.889 156.516 186.539 1.00 99.94  ? 4460 LEU A N     1 
ATOM   22163 C  CA    . LEU A 1 4460 ? 166.770 157.641 187.454 1.00 97.08  ? 4460 LEU A CA    1 
ATOM   22164 C  C     . LEU A 1 4460 ? 166.184 158.848 186.730 1.00 101.89 ? 4460 LEU A C     1 
ATOM   22165 O  O     . LEU A 1 4460 ? 166.735 159.270 185.701 1.00 102.01 ? 4460 LEU A O     1 
ATOM   22166 C  CB    . LEU A 1 4460 ? 168.135 157.990 188.038 1.00 92.97  ? 4460 LEU A CB    1 
ATOM   22167 C  CG    . LEU A 1 4460 ? 168.182 159.242 188.912 1.00 91.25  ? 4460 LEU A CG    1 
ATOM   22168 C  CD1   . LEU A 1 4460 ? 167.394 159.022 190.188 1.00 97.01  ? 4460 LEU A CD1   1 
ATOM   22169 C  CD2   . LEU A 1 4460 ? 169.619 159.623 189.220 1.00 94.22  ? 4460 LEU A CD2   1 
ATOM   22170 N  N     . PRO A 1 4461 ? 165.083 159.421 187.213 1.00 99.99  ? 4461 PRO A N     1 
ATOM   22171 C  CA    . PRO A 1 4461 ? 164.515 160.599 186.548 1.00 96.31  ? 4461 PRO A CA    1 
ATOM   22172 C  C     . PRO A 1 4461 ? 165.477 161.777 186.592 1.00 100.51 ? 4461 PRO A C     1 
ATOM   22173 O  O     . PRO A 1 4461 ? 166.244 161.943 187.542 1.00 105.54 ? 4461 PRO A O     1 
ATOM   22174 C  CB    . PRO A 1 4461 ? 163.240 160.882 187.351 1.00 96.79  ? 4461 PRO A CB    1 
ATOM   22175 C  CG    . PRO A 1 4461 ? 162.923 159.593 188.036 1.00 95.55  ? 4461 PRO A CG    1 
ATOM   22176 C  CD    . PRO A 1 4461 ? 164.244 158.959 188.330 1.00 97.16  ? 4461 PRO A CD    1 
ATOM   22177 N  N     . ARG A 1 4462 ? 165.430 162.598 185.541 1.00 107.48 ? 4462 ARG A N     1 
ATOM   22178 C  CA    . ARG A 1 4462 ? 166.305 163.764 185.472 1.00 109.55 ? 4462 ARG A CA    1 
ATOM   22179 C  C     . ARG A 1 4462 ? 165.981 164.776 186.563 1.00 109.66 ? 4462 ARG A C     1 
ATOM   22180 O  O     . ARG A 1 4462 ? 166.863 165.534 186.984 1.00 110.44 ? 4462 ARG A O     1 
ATOM   22181 C  CB    . ARG A 1 4462 ? 166.197 164.420 184.095 1.00 111.44 ? 4462 ARG A CB    1 
ATOM   22182 C  CG    . ARG A 1 4462 ? 166.711 163.566 182.944 1.00 110.70 ? 4462 ARG A CG    1 
ATOM   22183 C  CD    . ARG A 1 4462 ? 168.123 163.959 182.520 1.00 110.83 ? 4462 ARG A CD    1 
ATOM   22184 N  NE    . ARG A 1 4462 ? 169.060 164.026 183.636 1.00 113.85 ? 4462 ARG A NE    1 
ATOM   22185 C  CZ    . ARG A 1 4462 ? 169.524 162.973 184.296 1.00 114.05 ? 4462 ARG A CZ    1 
ATOM   22186 N  NH1   . ARG A 1 4462 ? 169.165 161.741 183.975 1.00 113.34 ? 4462 ARG A NH1   1 
ATOM   22187 N  NH2   . ARG A 1 4462 ? 170.377 163.162 185.299 1.00 113.72 ? 4462 ARG A NH2   1 
ATOM   22188 N  N     . SER A 1 4463 ? 164.730 164.808 187.026 1.00 103.33 ? 4463 SER A N     1 
ATOM   22189 C  CA    . SER A 1 4463 ? 164.342 165.760 188.062 1.00 103.68 ? 4463 SER A CA    1 
ATOM   22190 C  C     . SER A 1 4463 ? 165.033 165.461 189.386 1.00 105.29 ? 4463 SER A C     1 
ATOM   22191 O  O     . SER A 1 4463 ? 165.438 166.384 190.103 1.00 105.19 ? 4463 SER A O     1 
ATOM   22192 C  CB    . SER A 1 4463 ? 162.824 165.751 188.238 1.00 100.41 ? 4463 SER A CB    1 
ATOM   22193 O  OG    . SER A 1 4463 ? 162.431 166.602 189.301 1.00 102.99 ? 4463 SER A OG    1 
ATOM   22194 N  N     . TRP A 1 4464 ? 165.173 164.180 189.731 1.00 95.96  ? 4464 TRP A N     1 
ATOM   22195 C  CA    . TRP A 1 4464 ? 165.744 163.823 191.025 1.00 92.95  ? 4464 TRP A CA    1 
ATOM   22196 C  C     . TRP A 1 4464 ? 167.255 164.013 191.053 1.00 95.78  ? 4464 TRP A C     1 
ATOM   22197 O  O     . TRP A 1 4464 ? 167.816 164.334 192.106 1.00 98.28  ? 4464 TRP A O     1 
ATOM   22198 C  CB    . TRP A 1 4464 ? 165.390 162.378 191.376 1.00 92.01  ? 4464 TRP A CB    1 
ATOM   22199 C  CG    . TRP A 1 4464 ? 163.919 162.113 191.473 1.00 91.86  ? 4464 TRP A CG    1 
ATOM   22200 C  CD1   . TRP A 1 4464 ? 162.911 163.025 191.369 1.00 93.17  ? 4464 TRP A CD1   1 
ATOM   22201 C  CD2   . TRP A 1 4464 ? 163.290 160.844 191.690 1.00 94.04  ? 4464 TRP A CD2   1 
ATOM   22202 N  NE1   . TRP A 1 4464 ? 161.694 162.405 191.509 1.00 98.97  ? 4464 TRP A NE1   1 
ATOM   22203 C  CE2   . TRP A 1 4464 ? 161.900 161.065 191.707 1.00 95.53  ? 4464 TRP A CE2   1 
ATOM   22204 C  CE3   . TRP A 1 4464 ? 163.769 159.544 191.872 1.00 95.12  ? 4464 TRP A CE3   1 
ATOM   22205 C  CZ2   . TRP A 1 4464 ? 160.984 160.035 191.900 1.00 92.88  ? 4464 TRP A CZ2   1 
ATOM   22206 C  CZ3   . TRP A 1 4464 ? 162.858 158.523 192.063 1.00 94.78  ? 4464 TRP A CZ3   1 
ATOM   22207 C  CH2   . TRP A 1 4464 ? 161.481 158.774 192.075 1.00 93.05  ? 4464 TRP A CH2   1 
ATOM   22208 N  N     . SER A 1 4465 ? 167.927 163.819 189.923 1.00 98.19  ? 4465 SER A N     1 
ATOM   22209 C  CA    . SER A 1 4465 ? 169.385 163.886 189.874 1.00 98.71  ? 4465 SER A CA    1 
ATOM   22210 C  C     . SER A 1 4465 ? 169.828 165.336 190.006 1.00 100.42 ? 4465 SER A C     1 
ATOM   22211 O  O     . SER A 1 4465 ? 169.789 166.104 189.043 1.00 102.82 ? 4465 SER A O     1 
ATOM   22212 C  CB    . SER A 1 4465 ? 169.902 163.270 188.580 1.00 101.04 ? 4465 SER A CB    1 
ATOM   22213 O  OG    . SER A 1 4465 ? 171.317 163.317 188.524 1.00 102.21 ? 4465 SER A OG    1 
ATOM   22214 N  N     . HIS A 1 4466 ? 170.256 165.717 191.208 1.00 101.40 ? 4466 HIS A N     1 
ATOM   22215 C  CA    . HIS A 1 4466 ? 170.786 167.048 191.473 1.00 102.57 ? 4466 HIS A CA    1 
ATOM   22216 C  C     . HIS A 1 4466 ? 172.274 167.030 191.785 1.00 105.05 ? 4466 HIS A C     1 
ATOM   22217 O  O     . HIS A 1 4466 ? 173.051 167.741 191.141 1.00 102.85 ? 4466 HIS A O     1 
ATOM   22218 C  CB    . HIS A 1 4466 ? 170.018 167.700 192.631 1.00 100.50 ? 4466 HIS A CB    1 
ATOM   22219 C  CG    . HIS A 1 4466 ? 168.589 168.005 192.309 1.00 102.45 ? 4466 HIS A CG    1 
ATOM   22220 N  ND1   . HIS A 1 4466 ? 167.678 168.402 193.264 1.00 107.47 ? 4466 HIS A ND1   1 
ATOM   22221 C  CD2   . HIS A 1 4466 ? 167.913 167.973 191.136 1.00 102.97 ? 4466 HIS A CD2   1 
ATOM   22222 C  CE1   . HIS A 1 4466 ? 166.503 168.601 192.694 1.00 106.92 ? 4466 HIS A CE1   1 
ATOM   22223 N  NE2   . HIS A 1 4466 ? 166.618 168.347 191.403 1.00 105.42 ? 4466 HIS A NE2   1 
ATOM   22224 N  N     . TYR A 1 4467 ? 172.692 166.231 192.761 1.00 103.07 ? 4467 TYR A N     1 
ATOM   22225 C  CA    . TYR A 1 4467 ? 174.103 166.103 193.081 1.00 100.37 ? 4467 TYR A CA    1 
ATOM   22226 C  C     . TYR A 1 4467 ? 174.798 165.212 192.053 1.00 100.76 ? 4467 TYR A C     1 
ATOM   22227 O  O     . TYR A 1 4467 ? 174.162 164.526 191.249 1.00 105.60 ? 4467 TYR A O     1 
ATOM   22228 C  CB    . TYR A 1 4467 ? 174.290 165.543 194.491 1.00 97.54  ? 4467 TYR A CB    1 
ATOM   22229 C  CG    . TYR A 1 4467 ? 173.431 164.339 194.808 1.00 95.02  ? 4467 TYR A CG    1 
ATOM   22230 C  CD1   . TYR A 1 4467 ? 172.120 164.489 195.241 1.00 97.34  ? 4467 TYR A CD1   1 
ATOM   22231 C  CD2   . TYR A 1 4467 ? 173.933 163.052 194.679 1.00 99.99  ? 4467 TYR A CD2   1 
ATOM   22232 C  CE1   . TYR A 1 4467 ? 171.335 163.391 195.532 1.00 99.95  ? 4467 TYR A CE1   1 
ATOM   22233 C  CE2   . TYR A 1 4467 ? 173.154 161.949 194.969 1.00 103.23 ? 4467 TYR A CE2   1 
ATOM   22234 C  CZ    . TYR A 1 4467 ? 171.857 162.125 195.394 1.00 99.93  ? 4467 TYR A CZ    1 
ATOM   22235 O  OH    . TYR A 1 4467 ? 171.077 161.030 195.683 1.00 100.11 ? 4467 TYR A OH    1 
ATOM   22236 N  N     . THR A 1 4468 ? 176.127 165.236 192.084 1.00 92.04  ? 4468 THR A N     1 
ATOM   22237 C  CA    . THR A 1 4468 ? 176.912 164.447 191.145 1.00 92.51  ? 4468 THR A CA    1 
ATOM   22238 C  C     . THR A 1 4468 ? 176.720 162.958 191.409 1.00 93.81  ? 4468 THR A C     1 
ATOM   22239 O  O     . THR A 1 4468 ? 176.831 162.495 192.548 1.00 91.51  ? 4468 THR A O     1 
ATOM   22240 C  CB    . THR A 1 4468 ? 178.387 164.822 191.248 1.00 91.58  ? 4468 THR A CB    1 
ATOM   22241 O  OG1   . THR A 1 4468 ? 178.747 164.950 192.628 1.00 96.87  ? 4468 THR A OG1   1 
ATOM   22242 C  CG2   . THR A 1 4468 ? 178.650 166.139 190.535 1.00 89.48  ? 4468 THR A CG2   1 
ATOM   22243 N  N     . VAL A 1 4469 ? 176.433 162.211 190.345 1.00 97.88  ? 4469 VAL A N     1 
ATOM   22244 C  CA    . VAL A 1 4469 ? 176.099 160.789 190.452 1.00 96.49  ? 4469 VAL A CA    1 
ATOM   22245 C  C     . VAL A 1 4469 ? 176.851 160.021 189.382 1.00 99.67  ? 4469 VAL A C     1 
ATOM   22246 O  O     . VAL A 1 4469 ? 177.038 160.502 188.255 1.00 96.63  ? 4469 VAL A O     1 
ATOM   22247 C  CB    . VAL A 1 4469 ? 174.577 160.554 190.292 1.00 93.80  ? 4469 VAL A CB    1 
ATOM   22248 C  CG1   . VAL A 1 4469 ? 174.234 159.076 190.259 1.00 93.97  ? 4469 VAL A CG1   1 
ATOM   22249 C  CG2   . VAL A 1 4469 ? 173.811 161.245 191.409 1.00 92.76  ? 4469 VAL A CG2   1 
ATOM   22250 N  N     . PRO A 1 4470 ? 177.320 158.817 189.718 1.00 104.57 ? 4470 PRO A N     1 
ATOM   22251 C  CA    . PRO A 1 4470 ? 177.895 157.946 188.688 1.00 102.29 ? 4470 PRO A CA    1 
ATOM   22252 C  C     . PRO A 1 4470 ? 176.894 157.689 187.572 1.00 107.66 ? 4470 PRO A C     1 
ATOM   22253 O  O     . PRO A 1 4470 ? 175.695 157.526 187.808 1.00 109.92 ? 4470 PRO A O     1 
ATOM   22254 C  CB    . PRO A 1 4470 ? 178.227 156.660 189.452 1.00 97.85  ? 4470 PRO A CB    1 
ATOM   22255 C  CG    . PRO A 1 4470 ? 178.443 157.108 190.851 1.00 98.06  ? 4470 PRO A CG    1 
ATOM   22256 C  CD    . PRO A 1 4470 ? 177.526 158.279 191.075 1.00 102.84 ? 4470 PRO A CD    1 
ATOM   22257 N  N     . ALA A 1 4471 ? 177.406 157.661 186.339 1.00 106.63 ? 4471 ALA A N     1 
ATOM   22258 C  CA    . ALA A 1 4471 ? 176.536 157.628 185.167 1.00 103.33 ? 4471 ALA A CA    1 
ATOM   22259 C  C     . ALA A 1 4471 ? 175.666 156.376 185.151 1.00 104.13 ? 4471 ALA A C     1 
ATOM   22260 O  O     . ALA A 1 4471 ? 174.461 156.447 184.882 1.00 104.26 ? 4471 ALA A O     1 
ATOM   22261 C  CB    . ALA A 1 4471 ? 177.374 157.720 183.893 1.00 100.64 ? 4471 ALA A CB    1 
ATOM   22262 N  N     . GLY A 1 4472 ? 176.257 155.221 185.437 1.00 108.81 ? 4472 GLY A N     1 
ATOM   22263 C  CA    . GLY A 1 4472 ? 175.514 153.978 185.403 1.00 112.12 ? 4472 GLY A CA    1 
ATOM   22264 C  C     . GLY A 1 4472 ? 174.931 153.573 186.740 1.00 113.56 ? 4472 GLY A C     1 
ATOM   22265 O  O     . GLY A 1 4472 ? 175.297 152.528 187.287 1.00 112.20 ? 4472 GLY A O     1 
ATOM   22266 N  N     . MET A 1 4473 ? 174.025 154.383 187.280 1.00 112.80 ? 4473 MET A N     1 
ATOM   22267 C  CA    . MET A 1 4473 ? 173.380 154.097 188.554 1.00 112.75 ? 4473 MET A CA    1 
ATOM   22268 C  C     . MET A 1 4473 ? 171.888 153.882 188.342 1.00 108.71 ? 4473 MET A C     1 
ATOM   22269 O  O     . MET A 1 4473 ? 171.200 154.750 187.793 1.00 105.64 ? 4473 MET A O     1 
ATOM   22270 C  CB    . MET A 1 4473 ? 173.613 155.226 189.560 1.00 111.50 ? 4473 MET A CB    1 
ATOM   22271 C  CG    . MET A 1 4473 ? 173.206 154.860 190.979 1.00 113.12 ? 4473 MET A CG    1 
ATOM   22272 S  SD    . MET A 1 4473 ? 173.216 156.250 192.125 1.00 119.18 ? 4473 MET A SD    1 
ATOM   22273 C  CE    . MET A 1 4473 ? 174.924 156.240 192.658 1.00 110.96 ? 4473 MET A CE    1 
ATOM   22274 N  N     . THR A 1 4474 ? 171.397 152.726 188.778 1.00 104.81 ? 4474 THR A N     1 
ATOM   22275 C  CA    . THR A 1 4474 ? 169.983 152.399 188.716 1.00 104.79 ? 4474 THR A CA    1 
ATOM   22276 C  C     . THR A 1 4474 ? 169.228 153.178 189.795 1.00 108.15 ? 4474 THR A C     1 
ATOM   22277 O  O     . THR A 1 4474 ? 169.793 153.585 190.814 1.00 110.87 ? 4474 THR A O     1 
ATOM   22278 C  CB    . THR A 1 4474 ? 169.795 150.885 188.869 1.00 108.41 ? 4474 THR A CB    1 
ATOM   22279 O  OG1   . THR A 1 4474 ? 170.463 150.217 187.793 1.00 109.83 ? 4474 THR A OG1   1 
ATOM   22280 C  CG2   . THR A 1 4474 ? 168.323 150.488 188.832 1.00 107.02 ? 4474 THR A CG2   1 
ATOM   22281 N  N     . VAL A 1 4475 ? 167.932 153.399 189.554 1.00 105.45 ? 4475 VAL A N     1 
ATOM   22282 C  CA    . VAL A 1 4475 ? 167.116 154.174 190.484 1.00 104.11 ? 4475 VAL A CA    1 
ATOM   22283 C  C     . VAL A 1 4475 ? 167.106 153.542 191.873 1.00 107.32 ? 4475 VAL A C     1 
ATOM   22284 O  O     . VAL A 1 4475 ? 166.967 154.248 192.877 1.00 110.45 ? 4475 VAL A O     1 
ATOM   22285 C  CB    . VAL A 1 4475 ? 165.690 154.341 189.923 1.00 98.98  ? 4475 VAL A CB    1 
ATOM   22286 C  CG1   . VAL A 1 4475 ? 165.006 152.991 189.776 1.00 101.68 ? 4475 VAL A CG1   1 
ATOM   22287 C  CG2   . VAL A 1 4475 ? 164.868 155.274 190.800 1.00 99.99  ? 4475 VAL A CG2   1 
ATOM   22288 N  N     . ILE A 1 4476 ? 167.265 152.220 191.965 1.00 102.98 ? 4476 ILE A N     1 
ATOM   22289 C  CA    . ILE A 1 4476 ? 167.304 151.568 193.272 1.00 103.54 ? 4476 ILE A CA    1 
ATOM   22290 C  C     . ILE A 1 4476 ? 168.556 151.979 194.042 1.00 104.80 ? 4476 ILE A C     1 
ATOM   22291 O  O     . ILE A 1 4476 ? 168.492 152.320 195.232 1.00 107.06 ? 4476 ILE A O     1 
ATOM   22292 C  CB    . ILE A 1 4476 ? 167.213 150.041 193.104 1.00 101.35 ? 4476 ILE A CB    1 
ATOM   22293 C  CG1   . ILE A 1 4476 ? 165.766 149.621 192.842 1.00 102.66 ? 4476 ILE A CG1   1 
ATOM   22294 C  CG2   . ILE A 1 4476 ? 167.759 149.331 194.333 1.00 103.59 ? 4476 ILE A CG2   1 
ATOM   22295 C  CD1   . ILE A 1 4476 ? 165.615 148.172 192.442 1.00 103.03 ? 4476 ILE A CD1   1 
ATOM   22296 N  N     . GLN A 1 4477 ? 169.713 151.950 193.377 1.00 102.74 ? 4477 GLN A N     1 
ATOM   22297 C  CA    . GLN A 1 4477 ? 170.948 152.384 194.021 1.00 102.45 ? 4477 GLN A CA    1 
ATOM   22298 C  C     . GLN A 1 4477 ? 170.878 153.857 194.395 1.00 103.83 ? 4477 GLN A C     1 
ATOM   22299 O  O     . GLN A 1 4477 ? 171.364 154.260 195.460 1.00 106.88 ? 4477 GLN A O     1 
ATOM   22300 C  CB    . GLN A 1 4477 ? 172.140 152.120 193.103 1.00 102.80 ? 4477 GLN A CB    1 
ATOM   22301 C  CG    . GLN A 1 4477 ? 171.945 150.952 192.154 1.00 105.53 ? 4477 GLN A CG    1 
ATOM   22302 C  CD    . GLN A 1 4477 ? 173.137 150.741 191.242 1.00 105.24 ? 4477 GLN A CD    1 
ATOM   22303 O  OE1   . GLN A 1 4477 ? 174.085 151.525 191.249 1.00 102.23 ? 4477 GLN A OE1   1 
ATOM   22304 N  NE2   . GLN A 1 4477 ? 173.094 149.676 190.451 1.00 105.38 ? 4477 GLN A NE2   1 
ATOM   22305 N  N     . TRP A 1 4478 ? 170.281 154.677 193.527 1.00 94.07  ? 4478 TRP A N     1 
ATOM   22306 C  CA    . TRP A 1 4478 ? 170.115 156.090 193.847 1.00 92.37  ? 4478 TRP A CA    1 
ATOM   22307 C  C     . TRP A 1 4478 ? 169.224 156.275 195.065 1.00 98.69  ? 4478 TRP A C     1 
ATOM   22308 O  O     . TRP A 1 4478 ? 169.488 157.139 195.904 1.00 103.28 ? 4478 TRP A O     1 
ATOM   22309 C  CB    . TRP A 1 4478 ? 169.542 156.847 192.651 1.00 88.90  ? 4478 TRP A CB    1 
ATOM   22310 C  CG    . TRP A 1 4478 ? 169.498 158.328 192.873 1.00 91.91  ? 4478 TRP A CG    1 
ATOM   22311 C  CD1   . TRP A 1 4478 ? 170.470 159.232 192.560 1.00 95.91  ? 4478 TRP A CD1   1 
ATOM   22312 C  CD2   . TRP A 1 4478 ? 168.433 159.076 193.472 1.00 91.86  ? 4478 TRP A CD2   1 
ATOM   22313 N  NE1   . TRP A 1 4478 ? 170.074 160.497 192.918 1.00 94.54  ? 4478 TRP A NE1   1 
ATOM   22314 C  CE2   . TRP A 1 4478 ? 168.826 160.428 193.481 1.00 91.90  ? 4478 TRP A CE2   1 
ATOM   22315 C  CE3   . TRP A 1 4478 ? 167.183 158.735 193.996 1.00 93.47  ? 4478 TRP A CE3   1 
ATOM   22316 C  CZ2   . TRP A 1 4478 ? 168.016 161.437 193.994 1.00 92.48  ? 4478 TRP A CZ2   1 
ATOM   22317 C  CZ3   . TRP A 1 4478 ? 166.381 159.738 194.505 1.00 93.44  ? 4478 TRP A CZ3   1 
ATOM   22318 C  CH2   . TRP A 1 4478 ? 166.800 161.072 194.500 1.00 93.89  ? 4478 TRP A CH2   1 
ATOM   22319 N  N     . VAL A 1 4479 ? 168.160 155.477 195.177 1.00 97.00  ? 4479 VAL A N     1 
ATOM   22320 C  CA    . VAL A 1 4479 ? 167.276 155.574 196.335 1.00 97.39  ? 4479 VAL A CA    1 
ATOM   22321 C  C     . VAL A 1 4479 ? 168.021 155.194 197.607 1.00 100.84 ? 4479 VAL A C     1 
ATOM   22322 O  O     . VAL A 1 4479 ? 167.883 155.853 198.644 1.00 104.19 ? 4479 VAL A O     1 
ATOM   22323 C  CB    . VAL A 1 4479 ? 166.023 154.704 196.126 1.00 93.66  ? 4479 VAL A CB    1 
ATOM   22324 C  CG1   . VAL A 1 4479 ? 165.352 154.404 197.456 1.00 96.26  ? 4479 VAL A CG1   1 
ATOM   22325 C  CG2   . VAL A 1 4479 ? 165.051 155.401 195.191 1.00 95.70  ? 4479 VAL A CG2   1 
ATOM   22326 N  N     . SER A 1 4480 ? 168.825 154.129 197.551 1.00 94.51  ? 4480 SER A N     1 
ATOM   22327 C  CA    . SER A 1 4480 ? 169.595 153.732 198.729 1.00 93.06  ? 4480 SER A CA    1 
ATOM   22328 C  C     . SER A 1 4480 ? 170.591 154.816 199.136 1.00 98.25  ? 4480 SER A C     1 
ATOM   22329 O  O     . SER A 1 4480 ? 170.690 155.174 200.320 1.00 104.39 ? 4480 SER A O     1 
ATOM   22330 C  CB    . SER A 1 4480 ? 170.321 152.414 198.461 1.00 94.98  ? 4480 SER A CB    1 
ATOM   22331 O  OG    . SER A 1 4480 ? 169.409 151.397 198.088 1.00 100.21 ? 4480 SER A OG    1 
ATOM   22332 N  N     . ASP A 1 4481 ? 171.334 155.354 198.165 1.00 98.33  ? 4481 ASP A N     1 
ATOM   22333 C  CA    . ASP A 1 4481 ? 172.299 156.406 198.467 1.00 100.54 ? 4481 ASP A CA    1 
ATOM   22334 C  C     . ASP A 1 4481 ? 171.604 157.651 199.000 1.00 101.08 ? 4481 ASP A C     1 
ATOM   22335 O  O     . ASP A 1 4481 ? 172.099 158.299 199.927 1.00 105.37 ? 4481 ASP A O     1 
ATOM   22336 C  CB    . ASP A 1 4481 ? 173.118 156.741 197.221 1.00 101.15 ? 4481 ASP A CB    1 
ATOM   22337 C  CG    . ASP A 1 4481 ? 174.290 157.653 197.523 1.00 103.81 ? 4481 ASP A CG    1 
ATOM   22338 O  OD1   . ASP A 1 4481 ? 174.406 158.711 196.871 1.00 102.55 ? 4481 ASP A OD1   1 
ATOM   22339 O  OD2   . ASP A 1 4481 ? 175.097 157.311 198.413 1.00 101.73 ? 4481 ASP A OD2   1 
ATOM   22340 N  N     . PHE A 1 4482 ? 170.452 157.998 198.423 1.00 89.09  ? 4482 PHE A N     1 
ATOM   22341 C  CA    . PHE A 1 4482 ? 169.695 159.153 198.883 1.00 90.34  ? 4482 PHE A CA    1 
ATOM   22342 C  C     . PHE A 1 4482 ? 169.185 158.949 200.301 1.00 91.80  ? 4482 PHE A C     1 
ATOM   22343 O  O     . PHE A 1 4482 ? 169.171 159.889 201.101 1.00 100.46 ? 4482 PHE A O     1 
ATOM   22344 C  CB    . PHE A 1 4482 ? 168.539 159.421 197.921 1.00 90.61  ? 4482 PHE A CB    1 
ATOM   22345 C  CG    . PHE A 1 4482 ? 167.597 160.487 198.385 1.00 89.91  ? 4482 PHE A CG    1 
ATOM   22346 C  CD1   . PHE A 1 4482 ? 166.314 160.163 198.787 1.00 92.29  ? 4482 PHE A CD1   1 
ATOM   22347 C  CD2   . PHE A 1 4482 ? 167.989 161.813 198.416 1.00 90.57  ? 4482 PHE A CD2   1 
ATOM   22348 C  CE1   . PHE A 1 4482 ? 165.441 161.140 199.211 1.00 96.25  ? 4482 PHE A CE1   1 
ATOM   22349 C  CE2   . PHE A 1 4482 ? 167.119 162.793 198.842 1.00 92.86  ? 4482 PHE A CE2   1 
ATOM   22350 C  CZ    . PHE A 1 4482 ? 165.844 162.456 199.238 1.00 97.87  ? 4482 PHE A CZ    1 
ATOM   22351 N  N     . SER A 1 4483 ? 168.755 157.730 200.631 1.00 91.16  ? 4483 SER A N     1 
ATOM   22352 C  CA    . SER A 1 4483 ? 168.331 157.444 201.997 1.00 94.56  ? 4483 SER A CA    1 
ATOM   22353 C  C     . SER A 1 4483 ? 169.489 157.596 202.974 1.00 98.59  ? 4483 SER A C     1 
ATOM   22354 O  O     . SER A 1 4483 ? 169.323 158.159 204.063 1.00 103.15 ? 4483 SER A O     1 
ATOM   22355 C  CB    . SER A 1 4483 ? 167.741 156.037 202.081 1.00 96.53  ? 4483 SER A CB    1 
ATOM   22356 O  OG    . SER A 1 4483 ? 166.813 155.811 201.036 1.00 101.32 ? 4483 SER A OG    1 
ATOM   22357 N  N     . GLU A 1 4484 ? 170.672 157.099 202.603 1.00 101.82 ? 4484 GLU A N     1 
ATOM   22358 C  CA    . GLU A 1 4484 ? 171.834 157.273 203.472 1.00 100.76 ? 4484 GLU A CA    1 
ATOM   22359 C  C     . GLU A 1 4484 ? 172.179 158.749 203.645 1.00 103.47 ? 4484 GLU A C     1 
ATOM   22360 O  O     . GLU A 1 4484 ? 172.461 159.206 204.762 1.00 105.08 ? 4484 GLU A O     1 
ATOM   22361 C  CB    . GLU A 1 4484 ? 173.033 156.505 202.919 1.00 102.23 ? 4484 GLU A CB    1 
ATOM   22362 C  CG    . GLU A 1 4484 ? 173.940 155.937 203.996 1.00 105.17 ? 4484 GLU A CG    1 
ATOM   22363 C  CD    . GLU A 1 4484 ? 175.305 155.551 203.467 1.00 109.37 ? 4484 GLU A CD    1 
ATOM   22364 O  OE1   . GLU A 1 4484 ? 175.402 155.179 202.279 1.00 109.90 ? 4484 GLU A OE1   1 
ATOM   22365 O  OE2   . GLU A 1 4484 ? 176.284 155.623 204.240 1.00 109.04 ? 4484 GLU A OE2   1 
ATOM   22366 N  N     . ARG A 1 4485 ? 172.149 159.512 202.549 1.00 91.97  ? 4485 ARG A N     1 
ATOM   22367 C  CA    . ARG A 1 4485 ? 172.442 160.939 202.624 1.00 88.56  ? 4485 ARG A CA    1 
ATOM   22368 C  C     . ARG A 1 4485 ? 171.422 161.664 203.491 1.00 90.96  ? 4485 ARG A C     1 
ATOM   22369 O  O     . ARG A 1 4485 ? 171.777 162.568 204.254 1.00 93.56  ? 4485 ARG A O     1 
ATOM   22370 C  CB    . ARG A 1 4485 ? 172.473 161.545 201.221 1.00 88.14  ? 4485 ARG A CB    1 
ATOM   22371 C  CG    . ARG A 1 4485 ? 173.582 161.014 200.330 1.00 89.64  ? 4485 ARG A CG    1 
ATOM   22372 C  CD    . ARG A 1 4485 ? 173.549 161.672 198.961 1.00 88.29  ? 4485 ARG A CD    1 
ATOM   22373 N  NE    . ARG A 1 4485 ? 174.490 161.052 198.037 1.00 87.03  ? 4485 ARG A NE    1 
ATOM   22374 C  CZ    . ARG A 1 4485 ? 175.513 161.679 197.475 1.00 92.57  ? 4485 ARG A CZ    1 
ATOM   22375 N  NH1   . ARG A 1 4485 ? 175.765 162.953 197.725 1.00 94.67  ? 4485 ARG A NH1   1 
ATOM   22376 N  NH2   . ARG A 1 4485 ? 176.305 161.011 196.641 1.00 92.53  ? 4485 ARG A NH2   1 
ATOM   22377 N  N     . ILE A 1 4486 ? 170.148 161.284 203.385 1.00 94.23  ? 4486 ILE A N     1 
ATOM   22378 C  CA    . ILE A 1 4486 ? 169.104 161.947 204.156 1.00 91.95  ? 4486 ILE A CA    1 
ATOM   22379 C  C     . ILE A 1 4486 ? 169.227 161.607 205.636 1.00 95.58  ? 4486 ILE A C     1 
ATOM   22380 O  O     . ILE A 1 4486 ? 169.003 162.462 206.495 1.00 104.19 ? 4486 ILE A O     1 
ATOM   22381 C  CB    . ILE A 1 4486 ? 167.716 161.591 203.596 1.00 89.60  ? 4486 ILE A CB    1 
ATOM   22382 C  CG1   . ILE A 1 4486 ? 167.475 162.338 202.286 1.00 93.83  ? 4486 ILE A CG1   1 
ATOM   22383 C  CG2   . ILE A 1 4486 ? 166.627 161.958 204.583 1.00 91.12  ? 4486 ILE A CG2   1 
ATOM   22384 C  CD1   . ILE A 1 4486 ? 167.722 163.828 202.375 1.00 98.82  ? 4486 ILE A CD1   1 
ATOM   22385 N  N     . LYS A 1 4487 ? 169.572 160.360 205.964 1.00 95.72  ? 4487 LYS A N     1 
ATOM   22386 C  CA    . LYS A 1 4487 ? 169.809 160.020 207.366 1.00 98.50  ? 4487 LYS A CA    1 
ATOM   22387 C  C     . LYS A 1 4487 ? 170.994 160.800 207.926 1.00 101.83 ? 4487 LYS A C     1 
ATOM   22388 O  O     . LYS A 1 4487 ? 170.946 161.305 209.061 1.00 104.02 ? 4487 LYS A O     1 
ATOM   22389 C  CB    . LYS A 1 4487 ? 170.036 158.516 207.513 1.00 97.60  ? 4487 LYS A CB    1 
ATOM   22390 C  CG    . LYS A 1 4487 ? 168.784 157.678 207.333 1.00 101.39 ? 4487 LYS A CG    1 
ATOM   22391 C  CD    . LYS A 1 4487 ? 169.123 156.199 207.256 1.00 101.31 ? 4487 LYS A CD    1 
ATOM   22392 C  CE    . LYS A 1 4487 ? 168.064 155.438 206.485 1.00 101.59 ? 4487 LYS A CE    1 
ATOM   22393 N  NZ    . LYS A 1 4487 ? 166.700 155.817 206.940 1.00 102.69 ? 4487 LYS A NZ    1 
ATOM   22394 N  N     . GLN A 1 4488 ? 172.068 160.915 207.138 1.00 100.78 ? 4488 GLN A N     1 
ATOM   22395 C  CA    . GLN A 1 4488 ? 173.206 161.721 207.562 1.00 99.80  ? 4488 GLN A CA    1 
ATOM   22396 C  C     . GLN A 1 4488 ? 172.798 163.171 207.777 1.00 100.87 ? 4488 GLN A C     1 
ATOM   22397 O  O     . GLN A 1 4488 ? 173.202 163.796 208.761 1.00 105.07 ? 4488 GLN A O     1 
ATOM   22398 C  CB    . GLN A 1 4488 ? 174.332 161.631 206.536 1.00 102.03 ? 4488 GLN A CB    1 
ATOM   22399 C  CG    . GLN A 1 4488 ? 175.581 162.386 206.948 1.00 102.73 ? 4488 GLN A CG    1 
ATOM   22400 C  CD    . GLN A 1 4488 ? 176.537 162.608 205.798 1.00 104.25 ? 4488 GLN A CD    1 
ATOM   22401 O  OE1   . GLN A 1 4488 ? 177.693 162.191 205.849 1.00 105.40 ? 4488 GLN A OE1   1 
ATOM   22402 N  NE2   . GLN A 1 4488 ? 176.059 163.268 204.750 1.00 101.22 ? 4488 GLN A NE2   1 
ATOM   22403 N  N     . LEU A 1 4489 ? 171.980 163.717 206.874 1.00 102.23 ? 4489 LEU A N     1 
ATOM   22404 C  CA    . LEU A 1 4489 ? 171.528 165.098 207.011 1.00 102.18 ? 4489 LEU A CA    1 
ATOM   22405 C  C     . LEU A 1 4489 ? 170.587 165.270 208.198 1.00 104.52 ? 4489 LEU A C     1 
ATOM   22406 O  O     . LEU A 1 4489 ? 170.550 166.339 208.810 1.00 111.24 ? 4489 LEU A O     1 
ATOM   22407 C  CB    . LEU A 1 4489 ? 170.849 165.558 205.723 1.00 101.33 ? 4489 LEU A CB    1 
ATOM   22408 C  CG    . LEU A 1 4489 ? 171.797 165.970 204.598 1.00 102.15 ? 4489 LEU A CG    1 
ATOM   22409 C  CD1   . LEU A 1 4489 ? 171.023 166.483 203.402 1.00 103.47 ? 4489 LEU A CD1   1 
ATOM   22410 C  CD2   . LEU A 1 4489 ? 172.775 167.022 205.084 1.00 101.55 ? 4489 LEU A CD2   1 
ATOM   22411 N  N     . GLN A 1 4490 ? 169.795 164.247 208.518 1.00 101.54 ? 4490 GLN A N     1 
ATOM   22412 C  CA    . GLN A 1 4490 ? 168.924 164.328 209.686 1.00 102.41 ? 4490 GLN A CA    1 
ATOM   22413 C  C     . GLN A 1 4490 ? 169.739 164.391 210.971 1.00 106.77 ? 4490 GLN A C     1 
ATOM   22414 O  O     . GLN A 1 4490 ? 169.476 165.232 211.842 1.00 111.91 ? 4490 GLN A O     1 
ATOM   22415 C  CB    . GLN A 1 4490 ? 167.958 163.141 209.714 1.00 101.25 ? 4490 GLN A CB    1 
ATOM   22416 C  CG    . GLN A 1 4490 ? 166.823 163.223 208.703 1.00 106.16 ? 4490 GLN A CG    1 
ATOM   22417 C  CD    . GLN A 1 4490 ? 165.819 162.097 208.860 1.00 105.45 ? 4490 GLN A CD    1 
ATOM   22418 O  OE1   . GLN A 1 4490 ? 166.186 160.951 209.116 1.00 104.35 ? 4490 GLN A OE1   1 
ATOM   22419 N  NE2   . GLN A 1 4490 ? 164.540 162.425 208.727 1.00 107.18 ? 4490 GLN A NE2   1 
ATOM   22420 N  N     . ASN A 1 4491 ? 170.745 163.516 211.103 1.00 101.97 ? 4491 ASN A N     1 
ATOM   22421 C  CA    . ASN A 1 4491 ? 171.648 163.622 212.250 1.00 103.62 ? 4491 ASN A CA    1 
ATOM   22422 C  C     . ASN A 1 4491 ? 172.406 164.947 212.233 1.00 104.12 ? 4491 ASN A C     1 
ATOM   22423 O  O     . ASN A 1 4491 ? 172.665 165.537 213.289 1.00 106.25 ? 4491 ASN A O     1 
ATOM   22424 C  CB    . ASN A 1 4491 ? 172.626 162.450 212.288 1.00 100.65 ? 4491 ASN A CB    1 
ATOM   22425 C  CG    . ASN A 1 4491 ? 171.936 161.127 212.453 1.00 101.25 ? 4491 ASN A CG    1 
ATOM   22426 O  OD1   . ASN A 1 4491 ? 170.711 161.047 212.470 1.00 100.58 ? 4491 ASN A OD1   1 
ATOM   22427 N  ND2   . ASN A 1 4491 ? 172.722 160.076 212.611 1.00 105.59 ? 4491 ASN A ND2   1 
ATOM   22428 N  N     . ILE A 1 4492 ? 172.733 165.439 211.034 1.00 106.23 ? 4492 ILE A N     1 
ATOM   22429 C  CA    . ILE A 1 4492 ? 173.360 166.748 210.861 1.00 102.58 ? 4492 ILE A CA    1 
ATOM   22430 C  C     . ILE A 1 4492 ? 172.486 167.857 211.437 1.00 104.14 ? 4492 ILE A C     1 
ATOM   22431 O  O     . ILE A 1 4492 ? 172.954 168.688 212.221 1.00 104.63 ? 4492 ILE A O     1 
ATOM   22432 C  CB    . ILE A 1 4492 ? 173.669 166.970 209.368 1.00 107.80 ? 4492 ILE A CB    1 
ATOM   22433 C  CG1   . ILE A 1 4492 ? 175.080 166.463 209.046 1.00 108.09 ? 4492 ILE A CG1   1 
ATOM   22434 C  CG2   . ILE A 1 4492 ? 173.362 168.405 208.909 1.00 109.53 ? 4492 ILE A CG2   1 
ATOM   22435 C  CD1   . ILE A 1 4492 ? 175.433 166.551 207.567 1.00 107.36 ? 4492 ILE A CD1   1 
ATOM   22436 N  N     . SER A 1 4493 ? 171.204 167.884 211.064 1.00 121.52 ? 4493 SER A N     1 
ATOM   22437 C  CA    . SER A 1 4493 ? 170.325 168.956 211.522 1.00 122.77 ? 4493 SER A CA    1 
ATOM   22438 C  C     . SER A 1 4493 ? 170.081 168.848 213.016 1.00 123.22 ? 4493 SER A C     1 
ATOM   22439 O  O     . SER A 1 4493 ? 170.032 169.865 213.717 1.00 125.64 ? 4493 SER A O     1 
ATOM   22440 C  CB    . SER A 1 4493 ? 168.999 168.932 210.759 1.00 122.22 ? 4493 SER A CB    1 
ATOM   22441 O  OG    . SER A 1 4493 ? 168.261 170.129 210.959 1.00 130.31 ? 4493 SER A OG    1 
ATOM   22442 N  N     . LEU A 1 4494 ? 169.939 167.620 213.523 1.00 114.19 ? 4494 LEU A N     1 
ATOM   22443 C  CA    . LEU A 1 4494 ? 169.762 167.439 214.960 1.00 117.67 ? 4494 LEU A CA    1 
ATOM   22444 C  C     . LEU A 1 4494 ? 170.973 167.952 215.730 1.00 118.38 ? 4494 LEU A C     1 
ATOM   22445 O  O     . LEU A 1 4494 ? 170.830 168.626 216.757 1.00 118.32 ? 4494 LEU A O     1 
ATOM   22446 C  CB    . LEU A 1 4494 ? 169.512 165.966 215.276 1.00 112.23 ? 4494 LEU A CB    1 
ATOM   22447 C  CG    . LEU A 1 4494 ? 169.362 165.652 216.762 1.00 112.34 ? 4494 LEU A CG    1 
ATOM   22448 C  CD1   . LEU A 1 4494 ? 168.194 166.422 217.331 1.00 115.15 ? 4494 LEU A CD1   1 
ATOM   22449 C  CD2   . LEU A 1 4494 ? 169.132 164.178 216.962 1.00 111.93 ? 4494 LEU A CD2   1 
ATOM   22450 N  N     . ALA A 1 4495 ? 172.176 167.643 215.246 1.00 117.96 ? 4495 ALA A N     1 
ATOM   22451 C  CA    . ALA A 1 4495 ? 173.384 168.146 215.886 1.00 114.75 ? 4495 ALA A CA    1 
ATOM   22452 C  C     . ALA A 1 4495 ? 173.475 169.663 215.783 1.00 117.99 ? 4495 ALA A C     1 
ATOM   22453 O  O     . ALA A 1 4495 ? 173.871 170.336 216.742 1.00 119.63 ? 4495 ALA A O     1 
ATOM   22454 C  CB    . ALA A 1 4495 ? 174.610 167.491 215.253 1.00 118.67 ? 4495 ALA A CB    1 
ATOM   22455 N  N     . ALA A 1 4496 ? 173.126 170.216 214.621 1.00 128.50 ? 4496 ALA A N     1 
ATOM   22456 C  CA    . ALA A 1 4496 ? 173.233 171.655 214.407 1.00 129.07 ? 4496 ALA A CA    1 
ATOM   22457 C  C     . ALA A 1 4496 ? 172.290 172.421 215.321 1.00 128.59 ? 4496 ALA A C     1 
ATOM   22458 O  O     . ALA A 1 4496 ? 172.666 173.453 215.891 1.00 128.52 ? 4496 ALA A O     1 
ATOM   22459 C  CB    . ALA A 1 4496 ? 172.945 171.983 212.943 1.00 128.63 ? 4496 ALA A CB    1 
ATOM   22460 N  N     . ALA A 1 4497 ? 171.059 171.928 215.470 1.00 129.41 ? 4497 ALA A N     1 
ATOM   22461 C  CA    . ALA A 1 4497 ? 170.056 172.635 216.256 1.00 130.96 ? 4497 ALA A CA    1 
ATOM   22462 C  C     . ALA A 1 4497 ? 170.441 172.698 217.728 1.00 133.21 ? 4497 ALA A C     1 
ATOM   22463 O  O     . ALA A 1 4497 ? 170.250 173.730 218.382 1.00 133.81 ? 4497 ALA A O     1 
ATOM   22464 C  CB    . ALA A 1 4497 ? 168.694 171.965 216.086 1.00 128.23 ? 4497 ALA A CB    1 
ATOM   22465 N  N     . SER A 1 4498 ? 170.984 171.610 218.267 1.00 131.25 ? 4498 SER A N     1 
ATOM   22466 C  CA    . SER A 1 4498 ? 171.335 171.525 219.683 1.00 129.70 ? 4498 SER A CA    1 
ATOM   22467 C  C     . SER A 1 4498 ? 172.855 171.504 219.797 1.00 128.20 ? 4498 SER A C     1 
ATOM   22468 O  O     . SER A 1 4498 ? 173.490 170.452 219.709 1.00 127.72 ? 4498 SER A O     1 
ATOM   22469 C  CB    . SER A 1 4498 ? 170.701 170.295 220.322 1.00 127.67 ? 4498 SER A CB    1 
ATOM   22470 O  OG    . SER A 1 4498 ? 169.346 170.159 219.931 1.00 127.13 ? 4498 SER A OG    1 
ATOM   22471 N  N     . GLY A 1 4499 ? 173.442 172.681 220.000 1.00 129.93 ? 4499 GLY A N     1 
ATOM   22472 C  CA    . GLY A 1 4499 ? 174.875 172.783 220.191 1.00 131.54 ? 4499 GLY A CA    1 
ATOM   22473 C  C     . GLY A 1 4499 ? 175.520 173.919 219.427 1.00 132.85 ? 4499 GLY A C     1 
ATOM   22474 O  O     . GLY A 1 4499 ? 176.514 174.494 219.881 1.00 132.35 ? 4499 GLY A O     1 
ATOM   22475 N  N     . GLY A 1 4500 ? 174.971 174.251 218.262 1.00 131.68 ? 4500 GLY A N     1 
ATOM   22476 C  CA    . GLY A 1 4500 ? 175.496 175.352 217.480 1.00 130.96 ? 4500 GLY A CA    1 
ATOM   22477 C  C     . GLY A 1 4500 ? 176.679 174.969 216.614 1.00 133.17 ? 4500 GLY A C     1 
ATOM   22478 O  O     . GLY A 1 4500 ? 176.689 173.899 215.999 1.00 134.88 ? 4500 GLY A O     1 
ATOM   22479 N  N     . ALA A 1 4501 ? 177.686 175.843 216.561 1.00 131.57 ? 4501 ALA A N     1 
ATOM   22480 C  CA    . ALA A 1 4501 ? 178.847 175.602 215.712 1.00 130.64 ? 4501 ALA A CA    1 
ATOM   22481 C  C     . ALA A 1 4501 ? 179.797 174.565 216.300 1.00 130.56 ? 4501 ALA A C     1 
ATOM   22482 O  O     . ALA A 1 4501 ? 180.453 173.839 215.543 1.00 131.21 ? 4501 ALA A O     1 
ATOM   22483 C  CB    . ALA A 1 4501 ? 179.596 176.912 215.463 1.00 127.42 ? 4501 ALA A CB    1 
ATOM   22484 N  N     . LYS A 1 4502 ? 179.896 174.486 217.630 1.00 128.50 ? 4502 LYS A N     1 
ATOM   22485 C  CA    . LYS A 1 4502 ? 180.833 173.549 218.245 1.00 129.02 ? 4502 LYS A CA    1 
ATOM   22486 C  C     . LYS A 1 4502 ? 180.468 172.104 217.921 1.00 128.26 ? 4502 LYS A C     1 
ATOM   22487 O  O     . LYS A 1 4502 ? 181.346 171.291 217.602 1.00 129.23 ? 4502 LYS A O     1 
ATOM   22488 C  CB    . LYS A 1 4502 ? 180.905 173.792 219.759 1.00 128.04 ? 4502 LYS A CB    1 
ATOM   22489 C  CG    . LYS A 1 4502 ? 179.624 173.540 220.559 1.00 129.42 ? 4502 LYS A CG    1 
ATOM   22490 C  CD    . LYS A 1 4502 ? 179.552 172.123 221.120 1.00 128.74 ? 4502 LYS A CD    1 
ATOM   22491 C  CE    . LYS A 1 4502 ? 178.384 171.971 222.084 1.00 127.63 ? 4502 LYS A CE    1 
ATOM   22492 N  NZ    . LYS A 1 4502 ? 178.336 170.615 222.696 1.00 125.92 ? 4502 LYS A NZ    1 
ATOM   22493 N  N     . GLU A 1 4503 ? 179.179 171.765 217.985 1.00 121.34 ? 4503 GLU A N     1 
ATOM   22494 C  CA    . GLU A 1 4503 ? 178.770 170.415 217.622 1.00 122.09 ? 4503 GLU A CA    1 
ATOM   22495 C  C     . GLU A 1 4503 ? 179.033 170.145 216.148 1.00 123.32 ? 4503 GLU A C     1 
ATOM   22496 O  O     . GLU A 1 4503 ? 179.529 169.073 215.786 1.00 125.40 ? 4503 GLU A O     1 
ATOM   22497 C  CB    . GLU A 1 4503 ? 177.296 170.193 217.960 1.00 120.57 ? 4503 GLU A CB    1 
ATOM   22498 C  CG    . GLU A 1 4503 ? 176.891 168.724 218.059 1.00 121.09 ? 4503 GLU A CG    1 
ATOM   22499 C  CD    . GLU A 1 4503 ? 177.612 167.962 219.165 1.00 121.80 ? 4503 GLU A CD    1 
ATOM   22500 O  OE1   . GLU A 1 4503 ? 177.454 166.725 219.226 1.00 119.78 ? 4503 GLU A OE1   1 
ATOM   22501 O  OE2   . GLU A 1 4503 ? 178.308 168.590 219.991 1.00 124.18 ? 4503 GLU A OE2   1 
ATOM   22502 N  N     . LEU A 1 4504 ? 178.733 171.118 215.285 1.00 115.69 ? 4504 LEU A N     1 
ATOM   22503 C  CA    . LEU A 1 4504 ? 179.006 170.947 213.863 1.00 116.13 ? 4504 LEU A CA    1 
ATOM   22504 C  C     . LEU A 1 4504 ? 180.487 170.713 213.609 1.00 117.83 ? 4504 LEU A C     1 
ATOM   22505 O  O     . LEU A 1 4504 ? 180.853 169.996 212.671 1.00 119.35 ? 4504 LEU A O     1 
ATOM   22506 C  CB    . LEU A 1 4504 ? 178.521 172.166 213.082 1.00 117.70 ? 4504 LEU A CB    1 
ATOM   22507 C  CG    . LEU A 1 4504 ? 177.004 172.260 212.917 1.00 115.73 ? 4504 LEU A CG    1 
ATOM   22508 C  CD1   . LEU A 1 4504 ? 176.638 173.244 211.815 1.00 117.70 ? 4504 LEU A CD1   1 
ATOM   22509 C  CD2   . LEU A 1 4504 ? 176.396 170.890 212.672 1.00 118.03 ? 4504 LEU A CD2   1 
ATOM   22510 N  N     . LYS A 1 4505 ? 181.352 171.314 214.426 1.00 111.20 ? 4505 LYS A N     1 
ATOM   22511 C  CA    . LYS A 1 4505 ? 182.775 171.019 214.345 1.00 111.18 ? 4505 LYS A CA    1 
ATOM   22512 C  C     . LYS A 1 4505 ? 183.090 169.625 214.868 1.00 111.29 ? 4505 LYS A C     1 
ATOM   22513 O  O     . LYS A 1 4505 ? 184.013 168.973 214.368 1.00 114.39 ? 4505 LYS A O     1 
ATOM   22514 C  CB    . LYS A 1 4505 ? 183.575 172.073 215.118 1.00 111.80 ? 4505 LYS A CB    1 
ATOM   22515 C  CG    . LYS A 1 4505 ? 185.092 171.888 215.079 1.00 113.13 ? 4505 LYS A CG    1 
ATOM   22516 C  CD    . LYS A 1 4505 ? 185.615 171.147 216.303 1.00 111.24 ? 4505 LYS A CD    1 
ATOM   22517 C  CE    . LYS A 1 4505 ? 187.105 170.871 216.187 1.00 111.40 ? 4505 LYS A CE    1 
ATOM   22518 N  NZ    . LYS A 1 4505 ? 187.753 170.736 217.521 1.00 111.63 ? 4505 LYS A NZ    1 
ATOM   22519 N  N     . ASN A 1 4506 ? 182.337 169.148 215.857 1.00 108.94 ? 4506 ASN A N     1 
ATOM   22520 C  CA    . ASN A 1 4506 ? 182.671 167.908 216.545 1.00 109.12 ? 4506 ASN A CA    1 
ATOM   22521 C  C     . ASN A 1 4506 ? 182.175 166.655 215.828 1.00 109.33 ? 4506 ASN A C     1 
ATOM   22522 O  O     . ASN A 1 4506 ? 182.863 165.631 215.870 1.00 110.46 ? 4506 ASN A O     1 
ATOM   22523 C  CB    . ASN A 1 4506 ? 182.119 167.950 217.979 1.00 108.86 ? 4506 ASN A CB    1 
ATOM   22524 C  CG    . ASN A 1 4506 ? 182.236 166.616 218.701 1.00 111.78 ? 4506 ASN A CG    1 
ATOM   22525 O  OD1   . ASN A 1 4506 ? 181.525 165.657 218.397 1.00 113.89 ? 4506 ASN A OD1   1 
ATOM   22526 N  ND2   . ASN A 1 4506 ? 183.146 166.552 219.665 1.00 110.49 ? 4506 ASN A ND2   1 
ATOM   22527 N  N     . ILE A 1 4507 ? 181.017 166.703 215.169 1.00 106.24 ? 4507 ILE A N     1 
ATOM   22528 C  CA    . ILE A 1 4507 ? 180.411 165.510 214.580 1.00 107.10 ? 4507 ILE A CA    1 
ATOM   22529 C  C     . ILE A 1 4507 ? 181.267 164.999 213.430 1.00 108.66 ? 4507 ILE A C     1 
ATOM   22530 O  O     . ILE A 1 4507 ? 181.991 165.760 212.778 1.00 109.02 ? 4507 ILE A O     1 
ATOM   22531 C  CB    . ILE A 1 4507 ? 178.968 165.788 214.114 1.00 105.50 ? 4507 ILE A CB    1 
ATOM   22532 C  CG1   . ILE A 1 4507 ? 178.963 166.620 212.828 1.00 104.63 ? 4507 ILE A CG1   1 
ATOM   22533 C  CG2   . ILE A 1 4507 ? 178.148 166.423 215.223 1.00 108.99 ? 4507 ILE A CG2   1 
ATOM   22534 C  CD1   . ILE A 1 4507 ? 177.644 166.602 212.095 1.00 104.79 ? 4507 ILE A CD1   1 
ATOM   22535 N  N     . HIS A 1 4508 ? 181.190 163.691 213.196 1.00 100.57 ? 4508 HIS A N     1 
ATOM   22536 C  CA    . HIS A 1 4508 ? 181.877 163.066 212.076 1.00 97.96  ? 4508 HIS A CA    1 
ATOM   22537 C  C     . HIS A 1 4508 ? 180.972 163.050 210.854 1.00 95.60  ? 4508 HIS A C     1 
ATOM   22538 O  O     . HIS A 1 4508 ? 179.765 162.814 210.961 1.00 100.26 ? 4508 HIS A O     1 
ATOM   22539 C  CB    . HIS A 1 4508 ? 182.299 161.642 212.437 1.00 96.50  ? 4508 HIS A CB    1 
ATOM   22540 C  CG    . HIS A 1 4508 ? 183.255 161.569 213.585 1.00 97.87  ? 4508 HIS A CG    1 
ATOM   22541 N  ND1   . HIS A 1 4508 ? 183.632 160.377 214.164 1.00 98.97  ? 4508 HIS A ND1   1 
ATOM   22542 C  CD2   . HIS A 1 4508 ? 183.913 162.540 214.261 1.00 99.36  ? 4508 HIS A CD2   1 
ATOM   22543 C  CE1   . HIS A 1 4508 ? 184.480 160.616 215.148 1.00 102.25 ? 4508 HIS A CE1   1 
ATOM   22544 N  NE2   . HIS A 1 4508 ? 184.668 161.921 215.227 1.00 101.40 ? 4508 HIS A NE2   1 
ATOM   22545 N  N     . VAL A 1 4509 ? 181.559 163.302 209.688 1.00 90.49  ? 4509 VAL A N     1 
ATOM   22546 C  CA    . VAL A 1 4509 ? 180.800 163.433 208.453 1.00 90.83  ? 4509 VAL A CA    1 
ATOM   22547 C  C     . VAL A 1 4509 ? 181.407 162.539 207.381 1.00 94.46  ? 4509 VAL A C     1 
ATOM   22548 O  O     . VAL A 1 4509 ? 182.623 162.533 207.163 1.00 98.71  ? 4509 VAL A O     1 
ATOM   22549 C  CB    . VAL A 1 4509 ? 180.754 164.900 207.975 1.00 91.92  ? 4509 VAL A CB    1 
ATOM   22550 C  CG1   . VAL A 1 4509 ? 180.380 164.970 206.512 1.00 89.51  ? 4509 VAL A CG1   1 
ATOM   22551 C  CG2   . VAL A 1 4509 ? 179.773 165.697 208.816 1.00 98.44  ? 4509 VAL A CG2   1 
ATOM   22552 N  N     . CYS A 1 4510 ? 180.546 161.777 206.711 1.00 95.57  ? 4510 CYS A N     1 
ATOM   22553 C  CA    . CYS A 1 4510 ? 180.931 160.975 205.555 1.00 94.80  ? 4510 CYS A CA    1 
ATOM   22554 C  C     . CYS A 1 4510 ? 180.919 161.884 204.332 1.00 98.11  ? 4510 CYS A C     1 
ATOM   22555 O  O     . CYS A 1 4510 ? 179.862 162.383 203.932 1.00 100.90 ? 4510 CYS A O     1 
ATOM   22556 C  CB    . CYS A 1 4510 ? 179.987 159.789 205.373 1.00 96.76  ? 4510 CYS A CB    1 
ATOM   22557 S  SG    . CYS A 1 4510 ? 179.877 159.174 203.678 1.00 109.76 ? 4510 CYS A SG    1 
ATOM   22558 N  N     . LEU A 1 4511 ? 182.098 162.105 203.744 1.00 89.68  ? 4511 LEU A N     1 
ATOM   22559 C  CA    . LEU A 1 4511 ? 182.205 163.040 202.629 1.00 84.54  ? 4511 LEU A CA    1 
ATOM   22560 C  C     . LEU A 1 4511 ? 181.412 162.570 201.417 1.00 86.99  ? 4511 LEU A C     1 
ATOM   22561 O  O     . LEU A 1 4511 ? 180.987 163.393 200.598 1.00 89.56  ? 4511 LEU A O     1 
ATOM   22562 C  CB    . LEU A 1 4511 ? 183.672 163.247 202.255 1.00 83.99  ? 4511 LEU A CB    1 
ATOM   22563 C  CG    . LEU A 1 4511 ? 184.383 164.395 202.972 1.00 85.86  ? 4511 LEU A CG    1 
ATOM   22564 C  CD1   . LEU A 1 4511 ? 185.734 164.671 202.334 1.00 89.07  ? 4511 LEU A CD1   1 
ATOM   22565 C  CD2   . LEU A 1 4511 ? 183.523 165.646 202.984 1.00 88.15  ? 4511 LEU A CD2   1 
ATOM   22566 N  N     . GLY A 1 4512 ? 181.204 161.260 201.282 1.00 94.51  ? 4512 GLY A N     1 
ATOM   22567 C  CA    . GLY A 1 4512 ? 180.445 160.758 200.150 1.00 93.35  ? 4512 GLY A CA    1 
ATOM   22568 C  C     . GLY A 1 4512 ? 178.998 161.212 200.164 1.00 94.08  ? 4512 GLY A C     1 
ATOM   22569 O  O     . GLY A 1 4512 ? 178.418 161.497 199.112 1.00 95.38  ? 4512 GLY A O     1 
ATOM   22570 N  N     . GLY A 1 4513 ? 178.393 161.281 201.351 1.00 94.42  ? 4513 GLY A N     1 
ATOM   22571 C  CA    . GLY A 1 4513 ? 176.997 161.668 201.457 1.00 95.14  ? 4513 GLY A CA    1 
ATOM   22572 C  C     . GLY A 1 4513 ? 176.734 163.138 201.204 1.00 96.04  ? 4513 GLY A C     1 
ATOM   22573 O  O     . GLY A 1 4513 ? 175.610 163.503 200.845 1.00 98.50  ? 4513 GLY A O     1 
ATOM   22574 N  N     . LEU A 1 4514 ? 177.739 163.987 201.387 1.00 102.87 ? 4514 LEU A N     1 
ATOM   22575 C  CA    . LEU A 1 4514 ? 177.559 165.415 201.173 1.00 101.80 ? 4514 LEU A CA    1 
ATOM   22576 C  C     . LEU A 1 4514 ? 177.394 165.715 199.688 1.00 101.94 ? 4514 LEU A C     1 
ATOM   22577 O  O     . LEU A 1 4514 ? 177.938 165.013 198.832 1.00 106.29 ? 4514 LEU A O     1 
ATOM   22578 C  CB    . LEU A 1 4514 ? 178.751 166.183 201.731 1.00 101.75 ? 4514 LEU A CB    1 
ATOM   22579 C  CG    . LEU A 1 4514 ? 178.938 166.113 203.247 1.00 99.77  ? 4514 LEU A CG    1 
ATOM   22580 C  CD1   . LEU A 1 4514 ? 180.052 167.047 203.680 1.00 102.23 ? 4514 LEU A CD1   1 
ATOM   22581 C  CD2   . LEU A 1 4514 ? 177.648 166.422 203.986 1.00 100.22 ? 4514 LEU A CD2   1 
ATOM   22582 N  N     . PHE A 1 4515 ? 176.630 166.764 199.382 1.00 103.22 ? 4515 PHE A N     1 
ATOM   22583 C  CA    . PHE A 1 4515 ? 176.410 167.118 197.983 1.00 107.31 ? 4515 PHE A CA    1 
ATOM   22584 C  C     . PHE A 1 4515 ? 177.646 167.757 197.366 1.00 109.35 ? 4515 PHE A C     1 
ATOM   22585 O  O     . PHE A 1 4515 ? 177.959 167.506 196.196 1.00 112.45 ? 4515 PHE A O     1 
ATOM   22586 C  CB    . PHE A 1 4515 ? 175.202 168.039 197.864 1.00 108.36 ? 4515 PHE A CB    1 
ATOM   22587 C  CG    . PHE A 1 4515 ? 173.946 167.424 198.384 1.00 106.44 ? 4515 PHE A CG    1 
ATOM   22588 C  CD1   . PHE A 1 4515 ? 173.672 166.091 198.137 1.00 106.22 ? 4515 PHE A CD1   1 
ATOM   22589 C  CD2   . PHE A 1 4515 ? 173.053 168.160 199.138 1.00 106.73 ? 4515 PHE A CD2   1 
ATOM   22590 C  CE1   . PHE A 1 4515 ? 172.523 165.504 198.624 1.00 103.51 ? 4515 PHE A CE1   1 
ATOM   22591 C  CE2   . PHE A 1 4515 ? 171.902 167.578 199.628 1.00 105.29 ? 4515 PHE A CE2   1 
ATOM   22592 C  CZ    . PHE A 1 4515 ? 171.636 166.249 199.371 1.00 100.07 ? 4515 PHE A CZ    1 
ATOM   22593 N  N     . VAL A 1 4516 ? 178.344 168.604 198.114 1.00 102.70 ? 4516 VAL A N     1 
ATOM   22594 C  CA    . VAL A 1 4516 ? 179.592 169.178 197.617 1.00 105.94 ? 4516 VAL A CA    1 
ATOM   22595 C  C     . VAL A 1 4516 ? 180.675 169.012 198.679 1.00 103.31 ? 4516 VAL A C     1 
ATOM   22596 O  O     . VAL A 1 4516 ? 180.933 169.937 199.462 1.00 107.47 ? 4516 VAL A O     1 
ATOM   22597 C  CB    . VAL A 1 4516 ? 179.407 170.644 197.188 1.00 109.80 ? 4516 VAL A CB    1 
ATOM   22598 C  CG1   . VAL A 1 4516 ? 178.824 170.709 195.778 1.00 107.37 ? 4516 VAL A CG1   1 
ATOM   22599 C  CG2   . VAL A 1 4516 ? 178.519 171.389 198.153 1.00 105.83 ? 4516 VAL A CG2   1 
ATOM   22600 N  N     . PRO A 1 4517 ? 181.319 167.843 198.752 1.00 92.05  ? 4517 PRO A N     1 
ATOM   22601 C  CA    . PRO A 1 4517 ? 182.353 167.633 199.782 1.00 96.35  ? 4517 PRO A CA    1 
ATOM   22602 C  C     . PRO A 1 4517 ? 183.529 168.593 199.693 1.00 100.84 ? 4517 PRO A C     1 
ATOM   22603 O  O     . PRO A 1 4517 ? 184.120 168.925 200.731 1.00 103.61 ? 4517 PRO A O     1 
ATOM   22604 C  CB    . PRO A 1 4517 ? 182.795 166.180 199.547 1.00 101.07 ? 4517 PRO A CB    1 
ATOM   22605 C  CG    . PRO A 1 4517 ? 182.290 165.822 198.178 1.00 101.40 ? 4517 PRO A CG    1 
ATOM   22606 C  CD    . PRO A 1 4517 ? 181.048 166.621 197.978 1.00 93.58  ? 4517 PRO A CD    1 
ATOM   22607 N  N     . GLU A 1 4518 ? 183.913 169.031 198.490 1.00 105.00 ? 4518 GLU A N     1 
ATOM   22608 C  CA    . GLU A 1 4518 ? 184.996 170.004 198.395 1.00 102.50 ? 4518 GLU A CA    1 
ATOM   22609 C  C     . GLU A 1 4518 ? 184.613 171.307 199.078 1.00 100.56 ? 4518 GLU A C     1 
ATOM   22610 O  O     . GLU A 1 4518 ? 185.476 172.001 199.628 1.00 106.89 ? 4518 GLU A O     1 
ATOM   22611 C  CB    . GLU A 1 4518 ? 185.376 170.259 196.932 1.00 103.65 ? 4518 GLU A CB    1 
ATOM   22612 C  CG    . GLU A 1 4518 ? 184.365 171.055 196.094 1.00 105.96 ? 4518 GLU A CG    1 
ATOM   22613 C  CD    . GLU A 1 4518 ? 183.044 170.340 195.836 1.00 106.70 ? 4518 GLU A CD    1 
ATOM   22614 O  OE1   . GLU A 1 4518 ? 182.342 170.739 194.883 1.00 105.85 ? 4518 GLU A OE1   1 
ATOM   22615 O  OE2   . GLU A 1 4518 ? 182.708 169.374 196.550 1.00 107.93 ? 4518 GLU A OE2   1 
ATOM   22616 N  N     . ALA A 1 4519 ? 183.322 171.641 199.075 1.00 91.74  ? 4519 ALA A N     1 
ATOM   22617 C  CA    . ALA A 1 4519 ? 182.864 172.812 199.811 1.00 95.42  ? 4519 ALA A CA    1 
ATOM   22618 C  C     . ALA A 1 4519 ? 183.001 172.601 201.313 1.00 100.09 ? 4519 ALA A C     1 
ATOM   22619 O  O     . ALA A 1 4519 ? 183.309 173.542 202.049 1.00 104.23 ? 4519 ALA A O     1 
ATOM   22620 C  CB    . ALA A 1 4519 ? 181.422 173.138 199.432 1.00 93.57  ? 4519 ALA A CB    1 
ATOM   22621 N  N     . TYR A 1 4520 ? 182.789 171.369 201.787 1.00 98.34  ? 4520 TYR A N     1 
ATOM   22622 C  CA    . TYR A 1 4520 ? 183.071 171.054 203.187 1.00 93.98  ? 4520 TYR A CA    1 
ATOM   22623 C  C     . TYR A 1 4520 ? 184.547 171.233 203.511 1.00 95.15  ? 4520 TYR A C     1 
ATOM   22624 O  O     . TYR A 1 4520 ? 184.898 171.797 204.556 1.00 101.76 ? 4520 TYR A O     1 
ATOM   22625 C  CB    . TYR A 1 4520 ? 182.632 169.624 203.501 1.00 93.30  ? 4520 TYR A CB    1 
ATOM   22626 C  CG    . TYR A 1 4520 ? 182.879 169.188 204.931 1.00 93.64  ? 4520 TYR A CG    1 
ATOM   22627 C  CD1   . TYR A 1 4520 ? 184.047 168.523 205.280 1.00 96.44  ? 4520 TYR A CD1   1 
ATOM   22628 C  CD2   . TYR A 1 4520 ? 181.950 169.442 205.929 1.00 93.76  ? 4520 TYR A CD2   1 
ATOM   22629 C  CE1   . TYR A 1 4520 ? 184.280 168.120 206.580 1.00 93.92  ? 4520 TYR A CE1   1 
ATOM   22630 C  CE2   . TYR A 1 4520 ? 182.176 169.043 207.233 1.00 91.92  ? 4520 TYR A CE2   1 
ATOM   22631 C  CZ    . TYR A 1 4520 ? 183.343 168.383 207.551 1.00 90.44  ? 4520 TYR A CZ    1 
ATOM   22632 O  OH    . TYR A 1 4520 ? 183.573 167.984 208.847 1.00 92.03  ? 4520 TYR A OH    1 
ATOM   22633 N  N     . ILE A 1 4521 ? 185.423 170.739 202.635 1.00 89.59  ? 4521 ILE A N     1 
ATOM   22634 C  CA    . ILE A 1 4521 ? 186.857 170.890 202.856 1.00 88.31  ? 4521 ILE A CA    1 
ATOM   22635 C  C     . ILE A 1 4521 ? 187.222 172.365 202.928 1.00 94.13  ? 4521 ILE A C     1 
ATOM   22636 O  O     . ILE A 1 4521 ? 187.957 172.799 203.825 1.00 102.06 ? 4521 ILE A O     1 
ATOM   22637 C  CB    . ILE A 1 4521 ? 187.642 170.164 201.748 1.00 94.21  ? 4521 ILE A CB    1 
ATOM   22638 C  CG1   . ILE A 1 4521 ? 187.265 168.683 201.715 1.00 96.88  ? 4521 ILE A CG1   1 
ATOM   22639 C  CG2   . ILE A 1 4521 ? 189.135 170.330 201.951 1.00 97.92  ? 4521 ILE A CG2   1 
ATOM   22640 C  CD1   . ILE A 1 4521 ? 187.498 167.970 203.023 1.00 96.39  ? 4521 ILE A CD1   1 
ATOM   22641 N  N     . THR A 1 4522 ? 186.693 173.159 201.997 1.00 102.07 ? 4522 THR A N     1 
ATOM   22642 C  CA    . THR A 1 4522 ? 186.957 174.594 201.985 1.00 103.35 ? 4522 THR A CA    1 
ATOM   22643 C  C     . THR A 1 4522 ? 186.404 175.272 203.236 1.00 98.50  ? 4522 THR A C     1 
ATOM   22644 O  O     . THR A 1 4522 ? 187.030 176.186 203.786 1.00 104.63 ? 4522 THR A O     1 
ATOM   22645 C  CB    . THR A 1 4522 ? 186.361 175.207 200.716 1.00 105.27 ? 4522 THR A CB    1 
ATOM   22646 O  OG1   . THR A 1 4522 ? 187.092 174.745 199.573 1.00 107.00 ? 4522 THR A OG1   1 
ATOM   22647 C  CG2   . THR A 1 4522 ? 186.422 176.715 200.763 1.00 103.31 ? 4522 THR A CG2   1 
ATOM   22648 N  N     . ALA A 1 4523 ? 185.234 174.831 203.705 1.00 98.80  ? 4523 ALA A N     1 
ATOM   22649 C  CA    . ALA A 1 4523 ? 184.631 175.434 204.888 1.00 102.44 ? 4523 ALA A CA    1 
ATOM   22650 C  C     . ALA A 1 4523 ? 185.467 175.178 206.134 1.00 103.27 ? 4523 ALA A C     1 
ATOM   22651 O  O     . ALA A 1 4523 ? 185.716 176.101 206.916 1.00 104.85 ? 4523 ALA A O     1 
ATOM   22652 C  CB    . ALA A 1 4523 ? 183.210 174.906 205.078 1.00 100.49 ? 4523 ALA A CB    1 
ATOM   22653 N  N     . THR A 1 4524 ? 185.916 173.938 206.339 1.00 108.75 ? 4524 THR A N     1 
ATOM   22654 C  CA    . THR A 1 4524 ? 186.773 173.670 207.493 1.00 105.73 ? 4524 THR A CA    1 
ATOM   22655 C  C     . THR A 1 4524 ? 188.124 174.366 207.349 1.00 111.06 ? 4524 THR A C     1 
ATOM   22656 O  O     . THR A 1 4524 ? 188.709 174.816 208.345 1.00 113.28 ? 4524 THR A O     1 
ATOM   22657 C  CB    . THR A 1 4524 ? 186.958 172.165 207.700 1.00 106.83 ? 4524 THR A CB    1 
ATOM   22658 O  OG1   . THR A 1 4524 ? 187.925 171.665 206.773 1.00 109.94 ? 4524 THR A OG1   1 
ATOM   22659 C  CG2   . THR A 1 4524 ? 185.645 171.422 207.528 1.00 108.87 ? 4524 THR A CG2   1 
ATOM   22660 N  N     . ARG A 1 4525 ? 188.634 174.465 206.116 1.00 124.76 ? 4525 ARG A N     1 
ATOM   22661 C  CA    . ARG A 1 4525 ? 189.842 175.244 205.858 1.00 121.44 ? 4525 ARG A CA    1 
ATOM   22662 C  C     . ARG A 1 4525 ? 189.688 176.675 206.349 1.00 122.43 ? 4525 ARG A C     1 
ATOM   22663 O  O     . ARG A 1 4525 ? 190.527 177.180 207.106 1.00 125.87 ? 4525 ARG A O     1 
ATOM   22664 C  CB    . ARG A 1 4525 ? 190.152 175.227 204.360 1.00 122.94 ? 4525 ARG A CB    1 
ATOM   22665 C  CG    . ARG A 1 4525 ? 191.582 175.580 203.982 1.00 123.42 ? 4525 ARG A CG    1 
ATOM   22666 C  CD    . ARG A 1 4525 ? 191.639 176.233 202.611 1.00 119.43 ? 4525 ARG A CD    1 
ATOM   22667 N  NE    . ARG A 1 4525 ? 192.979 176.694 202.272 1.00 121.41 ? 4525 ARG A NE    1 
ATOM   22668 C  CZ    . ARG A 1 4525 ? 193.837 176.007 201.528 1.00 128.05 ? 4525 ARG A CZ    1 
ATOM   22669 N  NH1   . ARG A 1 4525 ? 193.524 174.822 201.030 1.00 128.32 ? 4525 ARG A NH1   1 
ATOM   22670 N  NH2   . ARG A 1 4525 ? 195.038 176.521 201.279 1.00 129.80 ? 4525 ARG A NH2   1 
ATOM   22671 N  N     . GLN A 1 4526 ? 188.613 177.343 205.929 1.00 116.57 ? 4526 GLN A N     1 
ATOM   22672 C  CA    . GLN A 1 4526 ? 188.400 178.728 206.330 1.00 118.35 ? 4526 GLN A CA    1 
ATOM   22673 C  C     . GLN A 1 4526 ? 188.126 178.835 207.825 1.00 120.18 ? 4526 GLN A C     1 
ATOM   22674 O  O     . GLN A 1 4526 ? 188.507 179.824 208.456 1.00 126.25 ? 4526 GLN A O     1 
ATOM   22675 C  CB    . GLN A 1 4526 ? 187.260 179.344 205.519 1.00 122.34 ? 4526 GLN A CB    1 
ATOM   22676 C  CG    . GLN A 1 4526 ? 187.169 180.859 205.635 1.00 125.09 ? 4526 GLN A CG    1 
ATOM   22677 C  CD    . GLN A 1 4526 ? 188.377 181.565 205.046 1.00 125.31 ? 4526 GLN A CD    1 
ATOM   22678 O  OE1   . GLN A 1 4526 ? 188.980 181.091 204.085 1.00 121.81 ? 4526 GLN A OE1   1 
ATOM   22679 N  NE2   . GLN A 1 4526 ? 188.739 182.703 205.627 1.00 122.87 ? 4526 GLN A NE2   1 
ATOM   22680 N  N     . TYR A 1 4527 ? 187.484 177.822 208.410 1.00 112.38 ? 4527 TYR A N     1 
ATOM   22681 C  CA    . TYR A 1 4527 ? 187.257 177.811 209.853 1.00 113.92 ? 4527 TYR A CA    1 
ATOM   22682 C  C     . TYR A 1 4527 ? 188.575 177.822 210.617 1.00 112.58 ? 4527 TYR A C     1 
ATOM   22683 O  O     . TYR A 1 4527 ? 188.783 178.647 211.517 1.00 110.13 ? 4527 TYR A O     1 
ATOM   22684 C  CB    . TYR A 1 4527 ? 186.413 176.587 210.224 1.00 115.81 ? 4527 TYR A CB    1 
ATOM   22685 C  CG    . TYR A 1 4527 ? 186.258 176.312 211.708 1.00 113.66 ? 4527 TYR A CG    1 
ATOM   22686 C  CD1   . TYR A 1 4527 ? 187.217 175.588 212.406 1.00 112.30 ? 4527 TYR A CD1   1 
ATOM   22687 C  CD2   . TYR A 1 4527 ? 185.143 176.756 212.404 1.00 111.05 ? 4527 TYR A CD2   1 
ATOM   22688 C  CE1   . TYR A 1 4527 ? 187.076 175.327 213.754 1.00 112.94 ? 4527 TYR A CE1   1 
ATOM   22689 C  CE2   . TYR A 1 4527 ? 184.993 176.499 213.754 1.00 111.15 ? 4527 TYR A CE2   1 
ATOM   22690 C  CZ    . TYR A 1 4527 ? 185.963 175.783 214.424 1.00 111.89 ? 4527 TYR A CZ    1 
ATOM   22691 O  OH    . TYR A 1 4527 ? 185.822 175.524 215.768 1.00 110.17 ? 4527 TYR A OH    1 
ATOM   22692 N  N     . VAL A 1 4528 ? 189.484 176.912 210.265 1.00 121.91 ? 4528 VAL A N     1 
ATOM   22693 C  CA    . VAL A 1 4528 ? 190.768 176.849 210.959 1.00 120.48 ? 4528 VAL A CA    1 
ATOM   22694 C  C     . VAL A 1 4528 ? 191.588 178.102 210.678 1.00 123.71 ? 4528 VAL A C     1 
ATOM   22695 O  O     . VAL A 1 4528 ? 192.274 178.626 211.567 1.00 126.29 ? 4528 VAL A O     1 
ATOM   22696 C  CB    . VAL A 1 4528 ? 191.523 175.566 210.568 1.00 128.50 ? 4528 VAL A CB    1 
ATOM   22697 C  CG1   . VAL A 1 4528 ? 192.926 175.566 211.161 1.00 127.58 ? 4528 VAL A CG1   1 
ATOM   22698 C  CG2   . VAL A 1 4528 ? 190.747 174.345 211.032 1.00 126.17 ? 4528 VAL A CG2   1 
ATOM   22699 N  N     . ALA A 1 4529 ? 191.524 178.612 209.444 1.00 131.90 ? 4529 ALA A N     1 
ATOM   22700 C  CA    . ALA A 1 4529 ? 192.252 179.833 209.111 1.00 132.34 ? 4529 ALA A CA    1 
ATOM   22701 C  C     . ALA A 1 4529 ? 191.751 181.016 209.929 1.00 132.96 ? 4529 ALA A C     1 
ATOM   22702 O  O     . ALA A 1 4529 ? 192.548 181.832 210.406 1.00 134.16 ? 4529 ALA A O     1 
ATOM   22703 C  CB    . ALA A 1 4529 ? 192.130 180.124 207.616 1.00 132.00 ? 4529 ALA A CB    1 
ATOM   22704 N  N     . GLN A 1 4530 ? 190.433 181.128 210.099 1.00 120.51 ? 4530 GLN A N     1 
ATOM   22705 C  CA    . GLN A 1 4530 ? 189.866 182.176 210.939 1.00 118.63 ? 4530 GLN A CA    1 
ATOM   22706 C  C     . GLN A 1 4530 ? 190.284 182.001 212.392 1.00 124.59 ? 4530 GLN A C     1 
ATOM   22707 O  O     . GLN A 1 4530 ? 190.591 182.983 213.078 1.00 126.64 ? 4530 GLN A O     1 
ATOM   22708 C  CB    . GLN A 1 4530 ? 188.344 182.170 210.815 1.00 117.41 ? 4530 GLN A CB    1 
ATOM   22709 C  CG    . GLN A 1 4530 ? 187.622 182.981 211.875 1.00 119.87 ? 4530 GLN A CG    1 
ATOM   22710 C  CD    . GLN A 1 4530 ? 186.119 182.943 211.701 1.00 122.72 ? 4530 GLN A CD    1 
ATOM   22711 O  OE1   . GLN A 1 4530 ? 185.612 182.398 210.722 1.00 122.69 ? 4530 GLN A OE1   1 
ATOM   22712 N  NE2   . GLN A 1 4530 ? 185.397 183.521 212.654 1.00 122.53 ? 4530 GLN A NE2   1 
ATOM   22713 N  N     . ALA A 1 4531 ? 190.298 180.758 212.879 1.00 121.19 ? 4531 ALA A N     1 
ATOM   22714 C  CA    . ALA A 1 4531 ? 190.704 180.515 214.260 1.00 118.36 ? 4531 ALA A CA    1 
ATOM   22715 C  C     . ALA A 1 4531 ? 192.149 180.938 214.496 1.00 117.87 ? 4531 ALA A C     1 
ATOM   22716 O  O     . ALA A 1 4531 ? 192.462 181.560 215.518 1.00 113.29 ? 4531 ALA A O     1 
ATOM   22717 C  CB    . ALA A 1 4531 ? 190.510 179.042 214.614 1.00 119.98 ? 4531 ALA A CB    1 
ATOM   22718 N  N     . ASN A 1 4532 ? 193.043 180.617 213.561 1.00 131.54 ? 4532 ASN A N     1 
ATOM   22719 C  CA    . ASN A 1 4532 ? 194.454 180.960 213.684 1.00 130.37 ? 4532 ASN A CA    1 
ATOM   22720 C  C     . ASN A 1 4532 ? 194.806 182.280 213.007 1.00 131.79 ? 4532 ASN A C     1 
ATOM   22721 O  O     . ASN A 1 4532 ? 195.970 182.694 213.054 1.00 132.75 ? 4532 ASN A O     1 
ATOM   22722 C  CB    . ASN A 1 4532 ? 195.324 179.835 213.122 1.00 128.63 ? 4532 ASN A CB    1 
ATOM   22723 C  CG    . ASN A 1 4532 ? 195.149 178.532 213.876 1.00 131.30 ? 4532 ASN A CG    1 
ATOM   22724 O  OD1   . ASN A 1 4532 ? 194.863 178.528 215.074 1.00 132.65 ? 4532 ASN A OD1   1 
ATOM   22725 N  ND2   . ASN A 1 4532 ? 195.323 177.416 213.178 1.00 130.34 ? 4532 ASN A ND2   1 
ATOM   22726 N  N     . SER A 1 4533 ? 193.832 182.949 212.386 1.00 138.17 ? 4533 SER A N     1 
ATOM   22727 C  CA    . SER A 1 4533 ? 194.032 184.256 211.754 1.00 137.35 ? 4533 SER A CA    1 
ATOM   22728 C  C     . SER A 1 4533 ? 195.184 184.227 210.748 1.00 138.67 ? 4533 SER A C     1 
ATOM   22729 O  O     . SER A 1 4533 ? 196.067 185.087 210.753 1.00 140.25 ? 4533 SER A O     1 
ATOM   22730 C  CB    . SER A 1 4533 ? 194.251 185.345 212.808 1.00 137.16 ? 4533 SER A CB    1 
ATOM   22731 O  OG    . SER A 1 4533 ? 193.039 185.660 213.472 1.00 133.67 ? 4533 SER A OG    1 
ATOM   22732 N  N     . TRP A 1 4534 ? 195.168 183.224 209.876 1.00 142.28 ? 4534 TRP A N     1 
ATOM   22733 C  CA    . TRP A 1 4534 ? 196.157 183.084 208.818 1.00 144.05 ? 4534 TRP A CA    1 
ATOM   22734 C  C     . TRP A 1 4534 ? 195.474 183.150 207.458 1.00 143.76 ? 4534 TRP A C     1 
ATOM   22735 O  O     . TRP A 1 4534 ? 194.275 183.422 207.348 1.00 141.33 ? 4534 TRP A O     1 
ATOM   22736 C  CB    . TRP A 1 4534 ? 196.940 181.770 208.950 1.00 144.29 ? 4534 TRP A CB    1 
ATOM   22737 C  CG    . TRP A 1 4534 ? 197.751 181.665 210.204 1.00 143.91 ? 4534 TRP A CG    1 
ATOM   22738 C  CD1   . TRP A 1 4534 ? 198.350 182.686 210.882 1.00 144.54 ? 4534 TRP A CD1   1 
ATOM   22739 C  CD2   . TRP A 1 4534 ? 198.068 180.467 210.922 1.00 143.29 ? 4534 TRP A CD2   1 
ATOM   22740 N  NE1   . TRP A 1 4534 ? 199.012 182.198 211.982 1.00 144.12 ? 4534 TRP A NE1   1 
ATOM   22741 C  CE2   . TRP A 1 4534 ? 198.855 180.838 212.029 1.00 143.06 ? 4534 TRP A CE2   1 
ATOM   22742 C  CE3   . TRP A 1 4534 ? 197.760 179.116 210.737 1.00 144.24 ? 4534 TRP A CE3   1 
ATOM   22743 C  CZ2   . TRP A 1 4534 ? 199.337 179.909 212.948 1.00 143.36 ? 4534 TRP A CZ2   1 
ATOM   22744 C  CZ3   . TRP A 1 4534 ? 198.238 178.195 211.650 1.00 143.84 ? 4534 TRP A CZ3   1 
ATOM   22745 C  CH2   . TRP A 1 4534 ? 199.018 178.595 212.741 1.00 143.95 ? 4534 TRP A CH2   1 
ATOM   22746 N  N     . SER A 1 4535 ? 196.257 182.902 206.414 1.00 146.78 ? 4535 SER A N     1 
ATOM   22747 C  CA    . SER A 1 4535 ? 195.738 182.875 205.056 1.00 147.48 ? 4535 SER A CA    1 
ATOM   22748 C  C     . SER A 1 4535 ? 195.582 181.437 204.573 1.00 145.82 ? 4535 SER A C     1 
ATOM   22749 O  O     . SER A 1 4535 ? 196.204 180.507 205.093 1.00 143.18 ? 4535 SER A O     1 
ATOM   22750 C  CB    . SER A 1 4535 ? 196.650 183.651 204.106 1.00 147.64 ? 4535 SER A CB    1 
ATOM   22751 O  OG    . SER A 1 4535 ? 196.153 183.611 202.780 1.00 145.87 ? 4535 SER A OG    1 
ATOM   22752 N  N     . LEU A 1 4536 ? 194.730 181.267 203.560 1.00 144.21 ? 4536 LEU A N     1 
ATOM   22753 C  CA    . LEU A 1 4536 ? 194.435 179.930 203.055 1.00 147.38 ? 4536 LEU A CA    1 
ATOM   22754 C  C     . LEU A 1 4536 ? 195.674 179.266 202.470 1.00 148.66 ? 4536 LEU A C     1 
ATOM   22755 O  O     . LEU A 1 4536 ? 195.938 178.088 202.737 1.00 149.22 ? 4536 LEU A O     1 
ATOM   22756 C  CB    . LEU A 1 4536 ? 193.320 179.998 202.012 1.00 146.99 ? 4536 LEU A CB    1 
ATOM   22757 C  CG    . LEU A 1 4536 ? 191.954 180.469 202.512 1.00 147.97 ? 4536 LEU A CG    1 
ATOM   22758 C  CD1   . LEU A 1 4536 ? 191.758 181.955 202.246 1.00 146.25 ? 4536 LEU A CD1   1 
ATOM   22759 C  CD2   . LEU A 1 4536 ? 190.844 179.654 201.867 1.00 146.98 ? 4536 LEU A CD2   1 
ATOM   22760 N  N     . GLU A 1 4537 ? 196.452 180.004 201.676 1.00 146.81 ? 4537 GLU A N     1 
ATOM   22761 C  CA    . GLU A 1 4537 ? 197.614 179.417 201.018 1.00 146.42 ? 4537 GLU A CA    1 
ATOM   22762 C  C     . GLU A 1 4537 ? 198.729 179.051 201.988 1.00 146.42 ? 4537 GLU A C     1 
ATOM   22763 O  O     . GLU A 1 4537 ? 199.637 178.307 201.605 1.00 144.49 ? 4537 GLU A O     1 
ATOM   22764 C  CB    . GLU A 1 4537 ? 198.149 180.369 199.946 1.00 143.55 ? 4537 GLU A CB    1 
ATOM   22765 C  CG    . GLU A 1 4537 ? 197.160 180.653 198.828 1.00 144.35 ? 4537 GLU A CG    1 
ATOM   22766 C  CD    . GLU A 1 4537 ? 197.734 181.563 197.762 1.00 145.30 ? 4537 GLU A CD    1 
ATOM   22767 O  OE1   . GLU A 1 4537 ? 198.830 181.259 197.246 1.00 146.47 ? 4537 GLU A OE1   1 
ATOM   22768 O  OE2   . GLU A 1 4537 ? 197.089 182.582 197.437 1.00 144.31 ? 4537 GLU A OE2   1 
ATOM   22769 N  N     . GLU A 1 4538 ? 198.686 179.547 203.222 1.00 150.48 ? 4538 GLU A N     1 
ATOM   22770 C  CA    . GLU A 1 4538 ? 199.665 179.185 204.237 1.00 149.52 ? 4538 GLU A CA    1 
ATOM   22771 C  C     . GLU A 1 4538 ? 199.267 177.944 205.024 1.00 150.26 ? 4538 GLU A C     1 
ATOM   22772 O  O     . GLU A 1 4538 ? 199.997 177.548 205.938 1.00 147.49 ? 4538 GLU A O     1 
ATOM   22773 C  CB    . GLU A 1 4538 ? 199.884 180.355 205.201 1.00 150.87 ? 4538 GLU A CB    1 
ATOM   22774 C  CG    . GLU A 1 4538 ? 200.055 181.703 204.521 1.00 149.80 ? 4538 GLU A CG    1 
ATOM   22775 C  CD    . GLU A 1 4538 ? 199.709 182.861 205.436 1.00 148.76 ? 4538 GLU A CD    1 
ATOM   22776 O  OE1   . GLU A 1 4538 ? 199.264 182.606 206.575 1.00 149.29 ? 4538 GLU A OE1   1 
ATOM   22777 O  OE2   . GLU A 1 4538 ? 199.879 184.025 205.017 1.00 146.85 ? 4538 GLU A OE2   1 
ATOM   22778 N  N     . LEU A 1 4539 ? 198.136 177.324 204.695 1.00 146.05 ? 4539 LEU A N     1 
ATOM   22779 C  CA    . LEU A 1 4539 ? 197.619 176.171 205.420 1.00 144.69 ? 4539 LEU A CA    1 
ATOM   22780 C  C     . LEU A 1 4539 ? 197.739 174.922 204.559 1.00 140.91 ? 4539 LEU A C     1 
ATOM   22781 O  O     . LEU A 1 4539 ? 197.263 174.900 203.419 1.00 141.07 ? 4539 LEU A O     1 
ATOM   22782 C  CB    . LEU A 1 4539 ? 196.162 176.394 205.828 1.00 140.73 ? 4539 LEU A CB    1 
ATOM   22783 C  CG    . LEU A 1 4539 ? 195.950 177.301 207.039 1.00 141.05 ? 4539 LEU A CG    1 
ATOM   22784 C  CD1   . LEU A 1 4539 ? 194.490 177.304 207.458 1.00 138.53 ? 4539 LEU A CD1   1 
ATOM   22785 C  CD2   . LEU A 1 4539 ? 196.840 176.858 208.187 1.00 142.45 ? 4539 LEU A CD2   1 
ATOM   22786 N  N     . CYS A 1 4540 ? 198.368 173.886 205.108 1.00 139.63 ? 4540 CYS A N     1 
ATOM   22787 C  CA    . CYS A 1 4540 ? 198.588 172.633 204.405 1.00 142.52 ? 4540 CYS A CA    1 
ATOM   22788 C  C     . CYS A 1 4540 ? 197.801 171.513 205.072 1.00 142.00 ? 4540 CYS A C     1 
ATOM   22789 O  O     . CYS A 1 4540 ? 197.337 171.638 206.209 1.00 141.54 ? 4540 CYS A O     1 
ATOM   22790 C  CB    . CYS A 1 4540 ? 200.078 172.272 204.364 1.00 141.52 ? 4540 CYS A CB    1 
ATOM   22791 S  SG    . CYS A 1 4540 ? 200.706 171.531 205.887 1.00 145.38 ? 4540 CYS A SG    1 
ATOM   22792 N  N     . LEU A 1 4541 ? 197.654 170.410 204.345 1.00 128.52 ? 4541 LEU A N     1 
ATOM   22793 C  CA    . LEU A 1 4541 ? 196.919 169.245 204.818 1.00 125.91 ? 4541 LEU A CA    1 
ATOM   22794 C  C     . LEU A 1 4541 ? 197.845 168.277 205.537 1.00 127.50 ? 4541 LEU A C     1 
ATOM   22795 O  O     . LEU A 1 4541 ? 198.912 167.925 205.021 1.00 127.16 ? 4541 LEU A O     1 
ATOM   22796 C  CB    . LEU A 1 4541 ? 196.220 168.529 203.660 1.00 128.64 ? 4541 LEU A CB    1 
ATOM   22797 C  CG    . LEU A 1 4541 ? 194.918 169.140 203.147 1.00 127.15 ? 4541 LEU A CG    1 
ATOM   22798 C  CD1   . LEU A 1 4541 ? 194.057 169.531 204.331 1.00 123.08 ? 4541 LEU A CD1   1 
ATOM   22799 C  CD2   . LEU A 1 4541 ? 195.177 170.337 202.245 1.00 127.02 ? 4541 LEU A CD2   1 
ATOM   22800 N  N     . GLU A 1 4542 ? 197.432 167.853 206.727 1.00 125.71 ? 4542 GLU A N     1 
ATOM   22801 C  CA    . GLU A 1 4542 ? 198.032 166.727 207.423 1.00 129.64 ? 4542 GLU A CA    1 
ATOM   22802 C  C     . GLU A 1 4542 ? 196.926 165.753 207.798 1.00 125.77 ? 4542 GLU A C     1 
ATOM   22803 O  O     . GLU A 1 4542 ? 195.935 166.136 208.428 1.00 122.10 ? 4542 GLU A O     1 
ATOM   22804 C  CB    . GLU A 1 4542 ? 198.801 167.177 208.668 1.00 127.83 ? 4542 GLU A CB    1 
ATOM   22805 C  CG    . GLU A 1 4542 ? 199.847 166.177 209.144 1.00 127.88 ? 4542 GLU A CG    1 
ATOM   22806 C  CD    . GLU A 1 4542 ? 200.985 165.992 208.152 1.00 127.94 ? 4542 GLU A CD    1 
ATOM   22807 O  OE1   . GLU A 1 4542 ? 200.808 165.241 207.169 1.00 124.86 ? 4542 GLU A OE1   1 
ATOM   22808 O  OE2   . GLU A 1 4542 ? 202.059 166.596 208.357 1.00 129.57 ? 4542 GLU A OE2   1 
ATOM   22809 N  N     . VAL A 1 4543 ? 197.097 164.494 207.405 1.00 115.03 ? 4543 VAL A N     1 
ATOM   22810 C  CA    . VAL A 1 4543 ? 196.051 163.485 207.500 1.00 110.10 ? 4543 VAL A CA    1 
ATOM   22811 C  C     . VAL A 1 4543 ? 196.525 162.367 208.415 1.00 114.07 ? 4543 VAL A C     1 
ATOM   22812 O  O     . VAL A 1 4543 ? 197.628 161.837 208.238 1.00 112.63 ? 4543 VAL A O     1 
ATOM   22813 C  CB    . VAL A 1 4543 ? 195.677 162.932 206.114 1.00 110.23 ? 4543 VAL A CB    1 
ATOM   22814 C  CG1   . VAL A 1 4543 ? 194.505 161.980 206.224 1.00 110.87 ? 4543 VAL A CG1   1 
ATOM   22815 C  CG2   . VAL A 1 4543 ? 195.349 164.073 205.169 1.00 110.26 ? 4543 VAL A CG2   1 
ATOM   22816 N  N     . ASN A 1 4544 ? 195.693 162.014 209.391 1.00 111.29 ? 4544 ASN A N     1 
ATOM   22817 C  CA    . ASN A 1 4544 ? 195.952 160.903 210.296 1.00 108.89 ? 4544 ASN A CA    1 
ATOM   22818 C  C     . ASN A 1 4544 ? 194.815 159.902 210.165 1.00 109.09 ? 4544 ASN A C     1 
ATOM   22819 O  O     . ASN A 1 4544 ? 193.649 160.254 210.374 1.00 111.74 ? 4544 ASN A O     1 
ATOM   22820 C  CB    . ASN A 1 4544 ? 196.083 161.387 211.741 1.00 106.97 ? 4544 ASN A CB    1 
ATOM   22821 C  CG    . ASN A 1 4544 ? 196.748 162.743 211.842 1.00 111.70 ? 4544 ASN A CG    1 
ATOM   22822 O  OD1   . ASN A 1 4544 ? 196.254 163.732 211.300 1.00 115.54 ? 4544 ASN A OD1   1 
ATOM   22823 N  ND2   . ASN A 1 4544 ? 197.876 162.799 212.539 1.00 110.96 ? 4544 ASN A ND2   1 
ATOM   22824 N  N     . VAL A 1 4545 ? 195.150 158.665 209.818 1.00 107.22 ? 4545 VAL A N     1 
ATOM   22825 C  CA    . VAL A 1 4545 ? 194.173 157.593 209.684 1.00 106.00 ? 4545 VAL A CA    1 
ATOM   22826 C  C     . VAL A 1 4545 ? 194.273 156.722 210.929 1.00 108.15 ? 4545 VAL A C     1 
ATOM   22827 O  O     . VAL A 1 4545 ? 195.282 156.044 211.148 1.00 107.83 ? 4545 VAL A O     1 
ATOM   22828 C  CB    . VAL A 1 4545 ? 194.400 156.774 208.407 1.00 103.63 ? 4545 VAL A CB    1 
ATOM   22829 C  CG1   . VAL A 1 4545 ? 193.460 155.582 208.372 1.00 104.65 ? 4545 VAL A CG1   1 
ATOM   22830 C  CG2   . VAL A 1 4545 ? 194.200 157.646 207.182 1.00 104.26 ? 4545 VAL A CG2   1 
ATOM   22831 N  N     . THR A 1 4546 ? 193.223 156.739 211.746 1.00 119.14 ? 4546 THR A N     1 
ATOM   22832 C  CA    . THR A 1 4546 ? 193.184 155.979 212.985 1.00 118.50 ? 4546 THR A CA    1 
ATOM   22833 C  C     . THR A 1 4546 ? 191.797 155.382 213.159 1.00 117.97 ? 4546 THR A C     1 
ATOM   22834 O  O     . THR A 1 4546 ? 190.837 155.785 212.498 1.00 118.34 ? 4546 THR A O     1 
ATOM   22835 C  CB    . THR A 1 4546 ? 193.534 156.847 214.203 1.00 119.16 ? 4546 THR A CB    1 
ATOM   22836 O  OG1   . THR A 1 4546 ? 192.825 158.090 214.126 1.00 118.82 ? 4546 THR A OG1   1 
ATOM   22837 C  CG2   . THR A 1 4546 ? 195.030 157.122 214.258 1.00 118.32 ? 4546 THR A CG2   1 
ATOM   22838 N  N     . THR A 1 4547 ? 191.703 154.408 214.059 1.00 131.66 ? 4547 THR A N     1 
ATOM   22839 C  CA    . THR A 1 4547 ? 190.417 153.809 214.379 1.00 134.09 ? 4547 THR A CA    1 
ATOM   22840 C  C     . THR A 1 4547 ? 189.501 154.839 215.031 1.00 134.66 ? 4547 THR A C     1 
ATOM   22841 O  O     . THR A 1 4547 ? 189.953 155.769 215.704 1.00 135.10 ? 4547 THR A O     1 
ATOM   22842 C  CB    . THR A 1 4547 ? 190.597 152.608 215.306 1.00 133.76 ? 4547 THR A CB    1 
ATOM   22843 O  OG1   . THR A 1 4547 ? 190.689 153.059 216.663 1.00 134.93 ? 4547 THR A OG1   1 
ATOM   22844 C  CG2   . THR A 1 4547 ? 191.861 151.842 214.945 1.00 131.04 ? 4547 THR A CG2   1 
ATOM   22845 N  N     . SER A 1 4548 ? 188.195 154.666 214.817 1.00 132.14 ? 4548 SER A N     1 
ATOM   22846 C  CA    . SER A 1 4548 ? 187.226 155.628 215.332 1.00 131.92 ? 4548 SER A CA    1 
ATOM   22847 C  C     . SER A 1 4548 ? 187.250 155.682 216.854 1.00 133.08 ? 4548 SER A C     1 
ATOM   22848 O  O     . SER A 1 4548 ? 187.135 156.762 217.445 1.00 131.54 ? 4548 SER A O     1 
ATOM   22849 C  CB    . SER A 1 4548 ? 185.825 155.280 214.829 1.00 132.06 ? 4548 SER A CB    1 
ATOM   22850 O  OG    . SER A 1 4548 ? 184.874 156.233 215.272 1.00 133.66 ? 4548 SER A OG    1 
ATOM   22851 N  N     . GLN A 1 4549 ? 187.392 154.526 217.506 1.00 148.66 ? 4549 GLN A N     1 
ATOM   22852 C  CA    . GLN A 1 4549 ? 187.422 154.494 218.965 1.00 149.87 ? 4549 GLN A CA    1 
ATOM   22853 C  C     . GLN A 1 4549 ? 188.641 155.231 219.509 1.00 149.99 ? 4549 GLN A C     1 
ATOM   22854 O  O     . GLN A 1 4549 ? 188.526 156.043 220.435 1.00 150.05 ? 4549 GLN A O     1 
ATOM   22855 C  CB    . GLN A 1 4549 ? 187.407 153.047 219.455 1.00 149.38 ? 4549 GLN A CB    1 
ATOM   22856 C  CG    . GLN A 1 4549 ? 186.335 152.184 218.811 1.00 150.86 ? 4549 GLN A CG    1 
ATOM   22857 C  CD    . GLN A 1 4549 ? 186.468 150.721 219.182 1.00 151.15 ? 4549 GLN A CD    1 
ATOM   22858 O  OE1   . GLN A 1 4549 ? 185.555 150.129 219.757 1.00 150.34 ? 4549 GLN A OE1   1 
ATOM   22859 N  NE2   . GLN A 1 4549 ? 187.611 150.130 218.854 1.00 150.21 ? 4549 GLN A NE2   1 
ATOM   22860 N  N     . GLY A 1 4550 ? 189.816 154.963 218.945 1.00 141.27 ? 4550 GLY A N     1 
ATOM   22861 C  CA    . GLY A 1 4550 ? 191.037 155.591 219.409 1.00 141.05 ? 4550 GLY A CA    1 
ATOM   22862 C  C     . GLY A 1 4550 ? 191.377 156.863 218.662 1.00 141.56 ? 4550 GLY A C     1 
ATOM   22863 O  O     . GLY A 1 4550 ? 192.455 156.974 218.070 1.00 139.69 ? 4550 GLY A O     1 
ATOM   22864 N  N     . ALA A 1 4551 ? 190.466 157.832 218.682 1.00 144.51 ? 4551 ALA A N     1 
ATOM   22865 C  CA    . ALA A 1 4551 ? 190.640 159.082 217.958 1.00 144.25 ? 4551 ALA A CA    1 
ATOM   22866 C  C     . ALA A 1 4551 ? 190.347 160.261 218.872 1.00 144.83 ? 4551 ALA A C     1 
ATOM   22867 O  O     . ALA A 1 4551 ? 189.356 160.257 219.609 1.00 144.59 ? 4551 ALA A O     1 
ATOM   22868 C  CB    . ALA A 1 4551 ? 189.731 159.141 216.729 1.00 143.76 ? 4551 ALA A CB    1 
ATOM   22869 N  N     . THR A 1 4552 ? 191.214 161.270 218.817 1.00 141.95 ? 4552 THR A N     1 
ATOM   22870 C  CA    . THR A 1 4552 ? 191.034 162.510 219.559 1.00 142.14 ? 4552 THR A CA    1 
ATOM   22871 C  C     . THR A 1 4552 ? 191.093 163.674 218.582 1.00 140.71 ? 4552 THR A C     1 
ATOM   22872 O  O     . THR A 1 4552 ? 192.038 163.779 217.795 1.00 140.10 ? 4552 THR A O     1 
ATOM   22873 C  CB    . THR A 1 4552 ? 192.104 162.678 220.644 1.00 141.60 ? 4552 THR A CB    1 
ATOM   22874 O  OG1   . THR A 1 4552 ? 193.406 162.603 220.050 1.00 141.57 ? 4552 THR A OG1   1 
ATOM   22875 C  CG2   . THR A 1 4552 ? 191.970 161.590 221.699 1.00 139.21 ? 4552 THR A CG2   1 
ATOM   22876 N  N     . LEU A 1 4553 ? 190.087 164.543 218.635 1.00 124.85 ? 4553 LEU A N     1 
ATOM   22877 C  CA    . LEU A 1 4553 ? 189.990 165.691 217.740 1.00 122.93 ? 4553 LEU A CA    1 
ATOM   22878 C  C     . LEU A 1 4553 ? 190.377 166.949 218.509 1.00 122.37 ? 4553 LEU A C     1 
ATOM   22879 O  O     . LEU A 1 4553 ? 189.714 167.317 219.485 1.00 122.07 ? 4553 LEU A O     1 
ATOM   22880 C  CB    . LEU A 1 4553 ? 188.582 165.814 217.164 1.00 120.86 ? 4553 LEU A CB    1 
ATOM   22881 C  CG    . LEU A 1 4553 ? 188.107 164.679 216.258 1.00 121.37 ? 4553 LEU A CG    1 
ATOM   22882 C  CD1   . LEU A 1 4553 ? 187.048 163.843 216.957 1.00 122.13 ? 4553 LEU A CD1   1 
ATOM   22883 C  CD2   . LEU A 1 4553 ? 187.576 165.231 214.946 1.00 120.38 ? 4553 LEU A CD2   1 
ATOM   22884 N  N     . ASP A 1 4554 ? 191.445 167.606 218.069 1.00 125.89 ? 4554 ASP A N     1 
ATOM   22885 C  CA    . ASP A 1 4554 ? 191.849 168.881 218.640 1.00 123.96 ? 4554 ASP A CA    1 
ATOM   22886 C  C     . ASP A 1 4554 ? 191.148 170.008 217.882 1.00 125.18 ? 4554 ASP A C     1 
ATOM   22887 O  O     . ASP A 1 4554 ? 190.194 169.782 217.133 1.00 127.44 ? 4554 ASP A O     1 
ATOM   22888 C  CB    . ASP A 1 4554 ? 193.371 169.019 218.627 1.00 124.76 ? 4554 ASP A CB    1 
ATOM   22889 C  CG    . ASP A 1 4554 ? 194.002 168.453 217.372 1.00 126.34 ? 4554 ASP A CG    1 
ATOM   22890 O  OD1   . ASP A 1 4554 ? 195.165 168.002 217.442 1.00 126.14 ? 4554 ASP A OD1   1 
ATOM   22891 O  OD2   . ASP A 1 4554 ? 193.345 168.472 216.314 1.00 127.87 ? 4554 ASP A OD2   1 
ATOM   22892 N  N     . ALA A 1 4555 ? 191.610 171.244 218.085 1.00 127.77 ? 4555 ALA A N     1 
ATOM   22893 C  CA    . ALA A 1 4555 ? 190.943 172.394 217.481 1.00 129.74 ? 4555 ALA A CA    1 
ATOM   22894 C  C     . ALA A 1 4555 ? 190.991 172.340 215.957 1.00 129.89 ? 4555 ALA A C     1 
ATOM   22895 O  O     . ALA A 1 4555 ? 190.062 172.801 215.284 1.00 127.49 ? 4555 ALA A O     1 
ATOM   22896 C  CB    . ALA A 1 4555 ? 191.574 173.690 217.990 1.00 128.05 ? 4555 ALA A CB    1 
ATOM   22897 N  N     . CYS A 1 4556 ? 192.063 171.785 215.394 1.00 131.24 ? 4556 CYS A N     1 
ATOM   22898 C  CA    . CYS A 1 4556 ? 192.259 171.763 213.951 1.00 130.77 ? 4556 CYS A CA    1 
ATOM   22899 C  C     . CYS A 1 4556 ? 191.788 170.468 213.298 1.00 130.68 ? 4556 CYS A C     1 
ATOM   22900 O  O     . CYS A 1 4556 ? 191.902 170.329 212.076 1.00 132.74 ? 4556 CYS A O     1 
ATOM   22901 C  CB    . CYS A 1 4556 ? 193.733 172.004 213.620 1.00 134.05 ? 4556 CYS A CB    1 
ATOM   22902 S  SG    . CYS A 1 4556 ? 194.891 170.983 214.562 1.00 138.02 ? 4556 CYS A SG    1 
ATOM   22903 N  N     . SER A 1 4557 ? 191.258 169.524 214.069 1.00 117.43 ? 4557 SER A N     1 
ATOM   22904 C  CA    . SER A 1 4557 ? 190.879 168.216 213.549 1.00 119.86 ? 4557 SER A CA    1 
ATOM   22905 C  C     . SER A 1 4557 ? 189.403 168.197 213.180 1.00 119.57 ? 4557 SER A C     1 
ATOM   22906 O  O     . SER A 1 4557 ? 188.584 168.849 213.836 1.00 119.45 ? 4557 SER A O     1 
ATOM   22907 C  CB    . SER A 1 4557 ? 191.171 167.114 214.569 1.00 120.66 ? 4557 SER A CB    1 
ATOM   22908 O  OG    . SER A 1 4557 ? 192.554 166.808 214.611 1.00 120.92 ? 4557 SER A OG    1 
ATOM   22909 N  N     . PHE A 1 4558 ? 189.073 167.454 212.126 1.00 109.35 ? 4558 PHE A N     1 
ATOM   22910 C  CA    . PHE A 1 4558 ? 187.698 167.205 211.722 1.00 103.29 ? 4558 PHE A CA    1 
ATOM   22911 C  C     . PHE A 1 4558 ? 187.554 165.740 211.342 1.00 104.87 ? 4558 PHE A C     1 
ATOM   22912 O  O     . PHE A 1 4558 ? 188.507 165.118 210.865 1.00 107.07 ? 4558 PHE A O     1 
ATOM   22913 C  CB    . PHE A 1 4558 ? 187.283 168.101 210.551 1.00 101.33 ? 4558 PHE A CB    1 
ATOM   22914 C  CG    . PHE A 1 4558 ? 187.197 169.556 210.905 1.00 100.93 ? 4558 PHE A CG    1 
ATOM   22915 C  CD1   . PHE A 1 4558 ? 185.993 170.116 211.293 1.00 101.99 ? 4558 PHE A CD1   1 
ATOM   22916 C  CD2   . PHE A 1 4558 ? 188.319 170.364 210.851 1.00 104.79 ? 4558 PHE A CD2   1 
ATOM   22917 C  CE1   . PHE A 1 4558 ? 185.909 171.454 211.619 1.00 104.21 ? 4558 PHE A CE1   1 
ATOM   22918 C  CE2   . PHE A 1 4558 ? 188.241 171.703 211.176 1.00 105.30 ? 4558 PHE A CE2   1 
ATOM   22919 C  CZ    . PHE A 1 4558 ? 187.034 172.248 211.561 1.00 105.98 ? 4558 PHE A CZ    1 
ATOM   22920 N  N     . GLY A 1 4559 ? 186.361 165.191 211.555 1.00 88.95  ? 4559 GLY A N     1 
ATOM   22921 C  CA    . GLY A 1 4559 ? 186.126 163.777 211.326 1.00 84.50  ? 4559 GLY A CA    1 
ATOM   22922 C  C     . GLY A 1 4559 ? 185.585 163.500 209.932 1.00 86.59  ? 4559 GLY A C     1 
ATOM   22923 O  O     . GLY A 1 4559 ? 184.614 164.111 209.493 1.00 90.04  ? 4559 GLY A O     1 
ATOM   22924 N  N     . VAL A 1 4560 ? 186.234 162.563 209.244 1.00 88.10  ? 4560 VAL A N     1 
ATOM   22925 C  CA    . VAL A 1 4560 ? 185.811 162.109 207.924 1.00 84.11  ? 4560 VAL A CA    1 
ATOM   22926 C  C     . VAL A 1 4560 ? 185.669 160.595 207.967 1.00 90.07  ? 4560 VAL A C     1 
ATOM   22927 O  O     . VAL A 1 4560 ? 186.573 159.896 208.436 1.00 93.59  ? 4560 VAL A O     1 
ATOM   22928 C  CB    . VAL A 1 4560 ? 186.802 162.523 206.818 1.00 87.54  ? 4560 VAL A CB    1 
ATOM   22929 C  CG1   . VAL A 1 4560 ? 186.157 162.376 205.452 1.00 87.36  ? 4560 VAL A CG1   1 
ATOM   22930 C  CG2   . VAL A 1 4560 ? 187.278 163.949 207.032 1.00 90.01  ? 4560 VAL A CG2   1 
ATOM   22931 N  N     . THR A 1 4561 ? 184.541 160.090 207.478 1.00 89.07  ? 4561 THR A N     1 
ATOM   22932 C  CA    . THR A 1 4561 ? 184.257 158.665 207.472 1.00 87.38  ? 4561 THR A CA    1 
ATOM   22933 C  C     . THR A 1 4561 ? 183.921 158.206 206.059 1.00 91.62  ? 4561 THR A C     1 
ATOM   22934 O  O     . THR A 1 4561 ? 183.466 158.986 205.219 1.00 93.83  ? 4561 THR A O     1 
ATOM   22935 C  CB    . THR A 1 4561 ? 183.094 158.316 208.411 1.00 88.14  ? 4561 THR A CB    1 
ATOM   22936 O  OG1   . THR A 1 4561 ? 181.894 158.940 207.940 1.00 88.73  ? 4561 THR A OG1   1 
ATOM   22937 C  CG2   . THR A 1 4561 ? 183.382 158.795 209.822 1.00 90.32  ? 4561 THR A CG2   1 
ATOM   22938 N  N     . GLY A 1 4562 ? 184.159 156.922 205.804 1.00 95.56  ? 4562 GLY A N     1 
ATOM   22939 C  CA    . GLY A 1 4562 ? 183.801 156.313 204.542 1.00 97.12  ? 4562 GLY A CA    1 
ATOM   22940 C  C     . GLY A 1 4562 ? 184.813 156.464 203.428 1.00 100.48 ? 4562 GLY A C     1 
ATOM   22941 O  O     . GLY A 1 4562 ? 184.568 155.961 202.325 1.00 102.31 ? 4562 GLY A O     1 
ATOM   22942 N  N     . LEU A 1 4563 ? 185.932 157.143 203.670 1.00 85.17  ? 4563 LEU A N     1 
ATOM   22943 C  CA    . LEU A 1 4563 ? 186.963 157.267 202.649 1.00 78.16  ? 4563 LEU A CA    1 
ATOM   22944 C  C     . LEU A 1 4563 ? 187.537 155.896 202.315 1.00 82.84  ? 4563 LEU A C     1 
ATOM   22945 O  O     . LEU A 1 4563 ? 187.835 155.101 203.211 1.00 88.29  ? 4563 LEU A O     1 
ATOM   22946 C  CB    . LEU A 1 4563 ? 188.070 158.207 203.120 1.00 78.60  ? 4563 LEU A CB    1 
ATOM   22947 C  CG    . LEU A 1 4563 ? 187.705 159.688 203.229 1.00 76.22  ? 4563 LEU A CG    1 
ATOM   22948 C  CD1   . LEU A 1 4563 ? 188.948 160.525 203.472 1.00 81.40  ? 4563 LEU A CD1   1 
ATOM   22949 C  CD2   . LEU A 1 4563 ? 186.981 160.153 201.979 1.00 79.58  ? 4563 LEU A CD2   1 
ATOM   22950 N  N     . LYS A 1 4564 ? 187.691 155.620 201.023 1.00 78.56  ? 4564 LYS A N     1 
ATOM   22951 C  CA    . LYS A 1 4564 ? 188.174 154.332 200.543 1.00 79.22  ? 4564 LYS A CA    1 
ATOM   22952 C  C     . LYS A 1 4564 ? 189.537 154.522 199.895 1.00 79.01  ? 4564 LYS A C     1 
ATOM   22953 O  O     . LYS A 1 4564 ? 189.695 155.375 199.015 1.00 83.85  ? 4564 LYS A O     1 
ATOM   22954 C  CB    . LYS A 1 4564 ? 187.189 153.712 199.551 1.00 82.24  ? 4564 LYS A CB    1 
ATOM   22955 C  CG    . LYS A 1 4564 ? 185.805 153.462 200.123 1.00 83.80  ? 4564 LYS A CG    1 
ATOM   22956 C  CD    . LYS A 1 4564 ? 185.819 152.316 201.119 1.00 83.82  ? 4564 LYS A CD    1 
ATOM   22957 C  CE    . LYS A 1 4564 ? 184.409 151.924 201.524 1.00 86.17  ? 4564 LYS A CE    1 
ATOM   22958 N  NZ    . LYS A 1 4564 ? 183.748 152.984 202.333 1.00 86.37  ? 4564 LYS A NZ    1 
ATOM   22959 N  N     . LEU A 1 4565 ? 190.513 153.731 200.329 1.00 76.29  ? 4565 LEU A N     1 
ATOM   22960 C  CA    . LEU A 1 4565 ? 191.847 153.746 199.745 1.00 70.86  ? 4565 LEU A CA    1 
ATOM   22961 C  C     . LEU A 1 4565 ? 191.945 152.622 198.720 1.00 82.79  ? 4565 LEU A C     1 
ATOM   22962 O  O     . LEU A 1 4565 ? 191.701 151.456 199.048 1.00 89.71  ? 4565 LEU A O     1 
ATOM   22963 C  CB    . LEU A 1 4565 ? 192.909 153.592 200.831 1.00 73.48  ? 4565 LEU A CB    1 
ATOM   22964 C  CG    . LEU A 1 4565 ? 194.362 153.849 200.432 1.00 79.12  ? 4565 LEU A CG    1 
ATOM   22965 C  CD1   . LEU A 1 4565 ? 194.554 155.296 200.027 1.00 78.78  ? 4565 LEU A CD1   1 
ATOM   22966 C  CD2   . LEU A 1 4565 ? 195.292 153.489 201.576 1.00 84.41  ? 4565 LEU A CD2   1 
ATOM   22967 N  N     . GLN A 1 4566 ? 192.303 152.970 197.487 1.00 83.74  ? 4566 GLN A N     1 
ATOM   22968 C  CA    . GLN A 1 4566 ? 192.311 152.032 196.369 1.00 81.26  ? 4566 GLN A CA    1 
ATOM   22969 C  C     . GLN A 1 4566 ? 193.743 151.592 196.092 1.00 81.84  ? 4566 GLN A C     1 
ATOM   22970 O  O     . GLN A 1 4566 ? 194.596 152.418 195.755 1.00 86.87  ? 4566 GLN A O     1 
ATOM   22971 C  CB    . GLN A 1 4566 ? 191.690 152.663 195.126 1.00 74.88  ? 4566 GLN A CB    1 
ATOM   22972 C  CG    . GLN A 1 4566 ? 190.336 153.296 195.366 1.00 78.04  ? 4566 GLN A CG    1 
ATOM   22973 C  CD    . GLN A 1 4566 ? 189.196 152.362 195.022 1.00 87.92  ? 4566 GLN A CD    1 
ATOM   22974 O  OE1   . GLN A 1 4566 ? 188.373 152.029 195.874 1.00 91.71  ? 4566 GLN A OE1   1 
ATOM   22975 N  NE2   . GLN A 1 4566 ? 189.140 151.934 193.766 1.00 88.27  ? 4566 GLN A NE2   1 
ATOM   22976 N  N     . GLY A 1 4567 ? 193.998 150.293 196.221 1.00 81.45  ? 4567 GLY A N     1 
ATOM   22977 C  CA    . GLY A 1 4567 ? 195.287 149.725 195.890 1.00 82.74  ? 4567 GLY A CA    1 
ATOM   22978 C  C     . GLY A 1 4567 ? 196.346 149.835 196.963 1.00 85.64  ? 4567 GLY A C     1 
ATOM   22979 O  O     . GLY A 1 4567 ? 197.499 149.468 196.706 1.00 87.03  ? 4567 GLY A O     1 
ATOM   22980 N  N     . ALA A 1 4568 ? 196.002 150.325 198.150 1.00 83.80  ? 4568 ALA A N     1 
ATOM   22981 C  CA    . ALA A 1 4568 ? 196.975 150.461 199.224 1.00 83.18  ? 4568 ALA A CA    1 
ATOM   22982 C  C     . ALA A 1 4568 ? 196.270 150.253 200.556 1.00 87.61  ? 4568 ALA A C     1 
ATOM   22983 O  O     . ALA A 1 4568 ? 195.049 150.381 200.664 1.00 91.13  ? 4568 ALA A O     1 
ATOM   22984 C  CB    . ALA A 1 4568 ? 197.671 151.824 199.179 1.00 82.26  ? 4568 ALA A CB    1 
ATOM   22985 N  N     . THR A 1 4569 ? 197.062 149.920 201.572 1.00 97.70  ? 4569 THR A N     1 
ATOM   22986 C  CA    . THR A 1 4569 ? 196.586 149.772 202.939 1.00 96.65  ? 4569 THR A CA    1 
ATOM   22987 C  C     . THR A 1 4569 ? 197.370 150.707 203.847 1.00 93.43  ? 4569 THR A C     1 
ATOM   22988 O  O     . THR A 1 4569 ? 198.594 150.817 203.732 1.00 96.08  ? 4569 THR A O     1 
ATOM   22989 C  CB    . THR A 1 4569 ? 196.726 148.329 203.435 1.00 96.16  ? 4569 THR A CB    1 
ATOM   22990 O  OG1   . THR A 1 4569 ? 198.112 147.967 203.477 1.00 93.72  ? 4569 THR A OG1   1 
ATOM   22991 C  CG2   . THR A 1 4569 ? 195.979 147.372 202.522 1.00 95.23  ? 4569 THR A CG2   1 
ATOM   22992 N  N     . CYS A 1 4570 ? 196.660 151.377 204.750 1.00 98.98  ? 4570 CYS A N     1 
ATOM   22993 C  CA    . CYS A 1 4570 ? 197.255 152.355 205.654 1.00 100.30 ? 4570 CYS A CA    1 
ATOM   22994 C  C     . CYS A 1 4570 ? 197.393 151.731 207.037 1.00 103.41 ? 4570 CYS A C     1 
ATOM   22995 O  O     . CYS A 1 4570 ? 196.392 151.484 207.717 1.00 102.28 ? 4570 CYS A O     1 
ATOM   22996 C  CB    . CYS A 1 4570 ? 196.409 153.625 205.708 1.00 100.05 ? 4570 CYS A CB    1 
ATOM   22997 S  SG    . CYS A 1 4570 ? 197.148 154.973 206.655 1.00 113.50 ? 4570 CYS A SG    1 
ATOM   22998 N  N     . ASN A 1 4571 ? 198.633 151.478 207.452 1.00 107.02 ? 4571 ASN A N     1 
ATOM   22999 C  CA    . ASN A 1 4571 ? 198.928 150.972 208.787 1.00 105.09 ? 4571 ASN A CA    1 
ATOM   23000 C  C     . ASN A 1 4571 ? 199.901 151.925 209.464 1.00 105.94 ? 4571 ASN A C     1 
ATOM   23001 O  O     . ASN A 1 4571 ? 200.967 152.218 208.915 1.00 108.11 ? 4571 ASN A O     1 
ATOM   23002 C  CB    . ASN A 1 4571 ? 199.501 149.551 208.732 1.00 106.98 ? 4571 ASN A CB    1 
ATOM   23003 C  CG    . ASN A 1 4571 ? 200.385 149.319 207.520 1.00 109.70 ? 4571 ASN A CG    1 
ATOM   23004 O  OD1   . ASN A 1 4571 ? 201.090 150.219 207.066 1.00 108.37 ? 4571 ASN A OD1   1 
ATOM   23005 N  ND2   . ASN A 1 4571 ? 200.351 148.102 206.991 1.00 109.07 ? 4571 ASN A ND2   1 
ATOM   23006 N  N     . ASN A 1 4572 ? 199.528 152.406 210.652 1.00 109.60 ? 4572 ASN A N     1 
ATOM   23007 C  CA    . ASN A 1 4572 ? 200.340 153.358 211.412 1.00 109.66 ? 4572 ASN A CA    1 
ATOM   23008 C  C     . ASN A 1 4572 ? 200.647 154.605 210.586 1.00 110.47 ? 4572 ASN A C     1 
ATOM   23009 O  O     . ASN A 1 4572 ? 201.755 155.144 210.622 1.00 110.09 ? 4572 ASN A O     1 
ATOM   23010 C  CB    . ASN A 1 4572 ? 201.630 152.704 211.914 1.00 109.22 ? 4572 ASN A CB    1 
ATOM   23011 C  CG    . ASN A 1 4572 ? 201.370 151.446 212.719 1.00 110.28 ? 4572 ASN A CG    1 
ATOM   23012 O  OD1   . ASN A 1 4572 ? 201.614 150.334 212.251 1.00 110.41 ? 4572 ASN A OD1   1 
ATOM   23013 N  ND2   . ASN A 1 4572 ? 200.873 151.617 213.938 1.00 110.52 ? 4572 ASN A ND2   1 
ATOM   23014 N  N     . ASN A 1 4573 ? 199.648 155.061 209.829 1.00 102.93 ? 4573 ASN A N     1 
ATOM   23015 C  CA    . ASN A 1 4573 ? 199.755 156.218 208.941 1.00 101.84 ? 4573 ASN A CA    1 
ATOM   23016 C  C     . ASN A 1 4573 ? 200.848 156.048 207.891 1.00 102.56 ? 4573 ASN A C     1 
ATOM   23017 O  O     . ASN A 1 4573 ? 201.436 157.034 207.436 1.00 99.81  ? 4573 ASN A O     1 
ATOM   23018 C  CB    . ASN A 1 4573 ? 199.982 157.513 209.731 1.00 100.71 ? 4573 ASN A CB    1 
ATOM   23019 C  CG    . ASN A 1 4573 ? 198.888 158.533 209.497 1.00 102.01 ? 4573 ASN A CG    1 
ATOM   23020 O  OD1   . ASN A 1 4573 ? 197.863 158.232 208.885 1.00 101.80 ? 4573 ASN A OD1   1 
ATOM   23021 N  ND2   . ASN A 1 4573 ? 199.103 159.751 209.978 1.00 102.02 ? 4573 ASN A ND2   1 
ATOM   23022 N  N     . LYS A 1 4574 ? 201.130 154.811 207.496 1.00 106.46 ? 4574 LYS A N     1 
ATOM   23023 C  CA    . LYS A 1 4574 ? 202.101 154.512 206.455 1.00 103.37 ? 4574 LYS A CA    1 
ATOM   23024 C  C     . LYS A 1 4574 ? 201.441 153.654 205.387 1.00 106.01 ? 4574 LYS A C     1 
ATOM   23025 O  O     . LYS A 1 4574 ? 200.730 152.694 205.701 1.00 109.79 ? 4574 LYS A O     1 
ATOM   23026 C  CB    . LYS A 1 4574 ? 203.326 153.795 207.030 1.00 102.56 ? 4574 LYS A CB    1 
ATOM   23027 C  CG    . LYS A 1 4574 ? 204.205 154.680 207.897 1.00 101.38 ? 4574 LYS A CG    1 
ATOM   23028 C  CD    . LYS A 1 4574 ? 205.446 153.938 208.360 1.00 106.26 ? 4574 LYS A CD    1 
ATOM   23029 C  CE    . LYS A 1 4574 ? 206.195 154.726 209.420 1.00 106.75 ? 4574 LYS A CE    1 
ATOM   23030 N  NZ    . LYS A 1 4574 ? 206.732 156.004 208.877 1.00 105.57 ? 4574 LYS A NZ    1 
ATOM   23031 N  N     . LEU A 1 4575 ? 201.676 154.002 204.126 1.00 91.56  ? 4575 LEU A N     1 
ATOM   23032 C  CA    . LEU A 1 4575 ? 201.026 153.329 203.011 1.00 87.26  ? 4575 LEU A CA    1 
ATOM   23033 C  C     . LEU A 1 4575 ? 201.870 152.165 202.512 1.00 88.77  ? 4575 LEU A C     1 
ATOM   23034 O  O     . LEU A 1 4575 ? 203.078 152.300 202.303 1.00 94.66  ? 4575 LEU A O     1 
ATOM   23035 C  CB    . LEU A 1 4575 ? 200.766 154.307 201.866 1.00 85.46  ? 4575 LEU A CB    1 
ATOM   23036 C  CG    . LEU A 1 4575 ? 199.728 155.403 202.105 1.00 84.00  ? 4575 LEU A CG    1 
ATOM   23037 C  CD1   . LEU A 1 4575 ? 199.116 155.822 200.786 1.00 86.07  ? 4575 LEU A CD1   1 
ATOM   23038 C  CD2   . LEU A 1 4575 ? 198.651 154.942 203.071 1.00 88.74  ? 4575 LEU A CD2   1 
ATOM   23039 N  N     . SER A 1 4576 ? 201.219 151.021 202.321 1.00 88.21  ? 4576 SER A N     1 
ATOM   23040 C  CA    . SER A 1 4576 ? 201.854 149.833 201.773 1.00 89.79  ? 4576 SER A CA    1 
ATOM   23041 C  C     . SER A 1 4576 ? 201.055 149.356 200.571 1.00 90.48  ? 4576 SER A C     1 
ATOM   23042 O  O     . SER A 1 4576 ? 199.823 149.300 200.618 1.00 93.78  ? 4576 SER A O     1 
ATOM   23043 C  CB    . SER A 1 4576 ? 201.950 148.717 202.819 1.00 90.73  ? 4576 SER A CB    1 
ATOM   23044 O  OG    . SER A 1 4576 ? 202.547 149.189 204.014 1.00 90.19  ? 4576 SER A OG    1 
ATOM   23045 N  N     . LEU A 1 4577 ? 201.760 149.020 199.494 1.00 89.52  ? 4577 LEU A N     1 
ATOM   23046 C  CA    . LEU A 1 4577 ? 201.092 148.541 198.292 1.00 90.29  ? 4577 LEU A CA    1 
ATOM   23047 C  C     . LEU A 1 4577 ? 200.404 147.211 198.569 1.00 93.69  ? 4577 LEU A C     1 
ATOM   23048 O  O     . LEU A 1 4577 ? 200.962 146.327 199.224 1.00 96.91  ? 4577 LEU A O     1 
ATOM   23049 C  CB    . LEU A 1 4577 ? 202.097 148.395 197.151 1.00 90.33  ? 4577 LEU A CB    1 
ATOM   23050 C  CG    . LEU A 1 4577 ? 202.543 149.706 196.500 1.00 89.89  ? 4577 LEU A CG    1 
ATOM   23051 C  CD1   . LEU A 1 4577 ? 203.533 149.443 195.377 1.00 91.92  ? 4577 LEU A CD1   1 
ATOM   23052 C  CD2   . LEU A 1 4577 ? 201.343 150.489 195.993 1.00 88.47  ? 4577 LEU A CD2   1 
ATOM   23053 N  N     . SER A 1 4578 ? 199.181 147.072 198.065 1.00 96.36  ? 4578 SER A N     1 
ATOM   23054 C  CA    . SER A 1 4578 ? 198.351 145.913 198.351 1.00 97.98  ? 4578 SER A CA    1 
ATOM   23055 C  C     . SER A 1 4578 ? 197.720 145.384 197.073 1.00 96.32  ? 4578 SER A C     1 
ATOM   23056 O  O     . SER A 1 4578 ? 197.577 146.106 196.083 1.00 97.57  ? 4578 SER A O     1 
ATOM   23057 C  CB    . SER A 1 4578 ? 197.250 146.250 199.361 1.00 96.15  ? 4578 SER A CB    1 
ATOM   23058 O  OG    . SER A 1 4578 ? 196.217 145.282 199.325 1.00 99.84  ? 4578 SER A OG    1 
ATOM   23059 N  N     . ASN A 1 4579 ? 197.346 144.109 197.110 1.00 102.78 ? 4579 ASN A N     1 
ATOM   23060 C  CA    . ASN A 1 4579 ? 196.635 143.468 196.014 1.00 104.01 ? 4579 ASN A CA    1 
ATOM   23061 C  C     . ASN A 1 4579 ? 195.124 143.513 196.189 1.00 106.28 ? 4579 ASN A C     1 
ATOM   23062 O  O     . ASN A 1 4579 ? 194.403 142.916 195.383 1.00 108.50 ? 4579 ASN A O     1 
ATOM   23063 C  CB    . ASN A 1 4579 ? 197.097 142.016 195.862 1.00 105.38 ? 4579 ASN A CB    1 
ATOM   23064 C  CG    . ASN A 1 4579 ? 198.534 141.908 195.393 1.00 108.96 ? 4579 ASN A CG    1 
ATOM   23065 O  OD1   . ASN A 1 4579 ? 199.361 141.257 196.031 1.00 112.16 ? 4579 ASN A OD1   1 
ATOM   23066 N  ND2   . ASN A 1 4579 ? 198.839 142.549 194.270 1.00 105.43 ? 4579 ASN A ND2   1 
ATOM   23067 N  N     . ALA A 1 4580 ? 194.630 144.189 197.221 1.00 98.51  ? 4580 ALA A N     1 
ATOM   23068 C  CA    . ALA A 1 4580 ? 193.201 144.362 197.422 1.00 96.42  ? 4580 ALA A CA    1 
ATOM   23069 C  C     . ALA A 1 4580 ? 192.715 145.597 196.676 1.00 95.86  ? 4580 ALA A C     1 
ATOM   23070 O  O     . ALA A 1 4580 ? 193.415 146.610 196.591 1.00 96.99  ? 4580 ALA A O     1 
ATOM   23071 C  CB    . ALA A 1 4580 ? 192.869 144.483 198.909 1.00 93.76  ? 4580 ALA A CB    1 
ATOM   23072 N  N     . ILE A 1 4581 ? 191.503 145.501 196.128 1.00 88.93  ? 4581 ILE A N     1 
ATOM   23073 C  CA    . ILE A 1 4581 ? 190.977 146.580 195.298 1.00 89.14  ? 4581 ILE A CA    1 
ATOM   23074 C  C     . ILE A 1 4581 ? 190.756 147.838 196.130 1.00 86.86  ? 4581 ILE A C     1 
ATOM   23075 O  O     . ILE A 1 4581 ? 191.183 148.934 195.752 1.00 89.32  ? 4581 ILE A O     1 
ATOM   23076 C  CB    . ILE A 1 4581 ? 189.685 146.132 194.592 1.00 86.91  ? 4581 ILE A CB    1 
ATOM   23077 C  CG1   . ILE A 1 4581 ? 190.017 145.254 193.385 1.00 87.72  ? 4581 ILE A CG1   1 
ATOM   23078 C  CG2   . ILE A 1 4581 ? 188.866 147.336 194.156 1.00 83.79  ? 4581 ILE A CG2   1 
ATOM   23079 C  CD1   . ILE A 1 4581 ? 190.964 145.904 192.401 1.00 87.94  ? 4581 ILE A CD1   1 
ATOM   23080 N  N     . SER A 1 4582 ? 190.097 147.699 197.278 1.00 88.34  ? 4582 SER A N     1 
ATOM   23081 C  CA    . SER A 1 4582 ? 189.796 148.840 198.130 1.00 85.17  ? 4582 SER A CA    1 
ATOM   23082 C  C     . SER A 1 4582 ? 190.048 148.474 199.584 1.00 88.92  ? 4582 SER A C     1 
ATOM   23083 O  O     . SER A 1 4582 ? 189.851 147.331 200.005 1.00 96.48  ? 4582 SER A O     1 
ATOM   23084 C  CB    . SER A 1 4582 ? 188.348 149.313 197.952 1.00 84.54  ? 4582 SER A CB    1 
ATOM   23085 O  OG    . SER A 1 4582 ? 188.163 149.926 196.689 1.00 93.65  ? 4582 SER A OG    1 
ATOM   23086 N  N     . THR A 1 4583 ? 190.484 149.469 200.352 1.00 80.28  ? 4583 THR A N     1 
ATOM   23087 C  CA    . THR A 1 4583 ? 190.679 149.323 201.789 1.00 81.97  ? 4583 THR A CA    1 
ATOM   23088 C  C     . THR A 1 4583 ? 189.983 150.484 202.478 1.00 85.39  ? 4583 THR A C     1 
ATOM   23089 O  O     . THR A 1 4583 ? 190.340 151.644 202.251 1.00 89.33  ? 4583 THR A O     1 
ATOM   23090 C  CB    . THR A 1 4583 ? 192.166 149.291 202.155 1.00 81.57  ? 4583 THR A CB    1 
ATOM   23091 O  OG1   . THR A 1 4583 ? 192.761 148.096 201.636 1.00 80.52  ? 4583 THR A OG1   1 
ATOM   23092 C  CG2   . THR A 1 4583 ? 192.341 149.320 203.665 1.00 82.20  ? 4583 THR A CG2   1 
ATOM   23093 N  N     . ALA A 1 4584 ? 188.995 150.174 203.312 1.00 90.23  ? 4584 ALA A N     1 
ATOM   23094 C  CA    . ALA A 1 4584 ? 188.192 151.203 203.959 1.00 88.94  ? 4584 ALA A CA    1 
ATOM   23095 C  C     . ALA A 1 4584 ? 188.983 151.843 205.093 1.00 90.97  ? 4584 ALA A C     1 
ATOM   23096 O  O     . ALA A 1 4584 ? 189.454 151.148 206.000 1.00 91.59  ? 4584 ALA A O     1 
ATOM   23097 C  CB    . ALA A 1 4584 ? 186.887 150.607 204.482 1.00 88.56  ? 4584 ALA A CB    1 
ATOM   23098 N  N     . LEU A 1 4585 ? 189.128 153.161 205.040 1.00 92.01  ? 4585 LEU A N     1 
ATOM   23099 C  CA    . LEU A 1 4585 ? 189.780 153.893 206.117 1.00 90.51  ? 4585 LEU A CA    1 
ATOM   23100 C  C     . LEU A 1 4585 ? 188.824 154.010 207.298 1.00 95.87  ? 4585 LEU A C     1 
ATOM   23101 O  O     . LEU A 1 4585 ? 187.694 154.478 207.120 1.00 99.31  ? 4585 LEU A O     1 
ATOM   23102 C  CB    . LEU A 1 4585 ? 190.205 155.276 205.643 1.00 88.54  ? 4585 LEU A CB    1 
ATOM   23103 C  CG    . LEU A 1 4585 ? 191.191 155.316 204.474 1.00 87.59  ? 4585 LEU A CG    1 
ATOM   23104 C  CD1   . LEU A 1 4585 ? 191.615 156.745 204.184 1.00 87.54  ? 4585 LEU A CD1   1 
ATOM   23105 C  CD2   . LEU A 1 4585 ? 192.401 154.443 204.760 1.00 91.36  ? 4585 LEU A CD2   1 
ATOM   23106 N  N     . PRO A 1 4586 ? 189.223 153.592 208.505 1.00 98.65  ? 4586 PRO A N     1 
ATOM   23107 C  CA    . PRO A 1 4586 ? 188.293 153.611 209.644 1.00 98.12  ? 4586 PRO A CA    1 
ATOM   23108 C  C     . PRO A 1 4586 ? 187.753 154.998 209.955 1.00 94.70  ? 4586 PRO A C     1 
ATOM   23109 O  O     . PRO A 1 4586 ? 186.536 155.212 209.952 1.00 94.47  ? 4586 PRO A O     1 
ATOM   23110 C  CB    . PRO A 1 4586 ? 189.145 153.072 210.801 1.00 99.27  ? 4586 PRO A CB    1 
ATOM   23111 C  CG    . PRO A 1 4586 ? 190.262 152.326 210.144 1.00 97.65  ? 4586 PRO A CG    1 
ATOM   23112 C  CD    . PRO A 1 4586 ? 190.545 153.062 208.874 1.00 94.12  ? 4586 PRO A CD    1 
ATOM   23113 N  N     . LEU A 1 4587 ? 188.648 155.946 210.221 1.00 98.42  ? 4587 LEU A N     1 
ATOM   23114 C  CA    . LEU A 1 4587 ? 188.254 157.322 210.491 1.00 99.73  ? 4587 LEU A CA    1 
ATOM   23115 C  C     . LEU A 1 4587 ? 189.396 158.241 210.095 1.00 99.88  ? 4587 LEU A C     1 
ATOM   23116 O  O     . LEU A 1 4587 ? 190.522 158.077 210.573 1.00 103.32 ? 4587 LEU A O     1 
ATOM   23117 C  CB    . LEU A 1 4587 ? 187.893 157.523 211.965 1.00 102.73 ? 4587 LEU A CB    1 
ATOM   23118 C  CG    . LEU A 1 4587 ? 187.629 158.972 212.379 1.00 103.05 ? 4587 LEU A CG    1 
ATOM   23119 C  CD1   . LEU A 1 4587 ? 186.358 159.491 211.737 1.00 102.84 ? 4587 LEU A CD1   1 
ATOM   23120 C  CD2   . LEU A 1 4587 ? 187.541 159.087 213.887 1.00 102.02 ? 4587 LEU A CD2   1 
ATOM   23121 N  N     . THR A 1 4588 ? 189.101 159.205 209.231 1.00 91.46  ? 4588 THR A N     1 
ATOM   23122 C  CA    . THR A 1 4588 ? 190.106 160.103 208.680 1.00 91.64  ? 4588 THR A CA    1 
ATOM   23123 C  C     . THR A 1 4588 ? 190.023 161.451 209.384 1.00 94.38  ? 4588 THR A C     1 
ATOM   23124 O  O     . THR A 1 4588 ? 188.979 162.112 209.345 1.00 97.77  ? 4588 THR A O     1 
ATOM   23125 C  CB    . THR A 1 4588 ? 189.911 160.272 207.174 1.00 98.27  ? 4588 THR A CB    1 
ATOM   23126 O  OG1   . THR A 1 4588 ? 189.762 158.984 206.563 1.00 103.18 ? 4588 THR A OG1   1 
ATOM   23127 C  CG2   . THR A 1 4588 ? 191.099 160.983 206.560 1.00 97.39  ? 4588 THR A CG2   1 
ATOM   23128 N  N     . GLN A 1 4589 ? 191.118 161.854 210.019 1.00 113.51 ? 4589 GLN A N     1 
ATOM   23129 C  CA    . GLN A 1 4589 ? 191.224 163.159 210.657 1.00 109.24 ? 4589 GLN A CA    1 
ATOM   23130 C  C     . GLN A 1 4589 ? 192.068 164.062 209.770 1.00 111.64 ? 4589 GLN A C     1 
ATOM   23131 O  O     . GLN A 1 4589 ? 193.196 163.707 209.413 1.00 118.05 ? 4589 GLN A O     1 
ATOM   23132 C  CB    . GLN A 1 4589 ? 191.850 163.051 212.047 1.00 108.97 ? 4589 GLN A CB    1 
ATOM   23133 C  CG    . GLN A 1 4589 ? 191.241 161.989 212.938 1.00 114.65 ? 4589 GLN A CG    1 
ATOM   23134 C  CD    . GLN A 1 4589 ? 191.928 161.911 214.286 1.00 116.33 ? 4589 GLN A CD    1 
ATOM   23135 O  OE1   . GLN A 1 4589 ? 192.439 162.910 214.792 1.00 116.72 ? 4589 GLN A OE1   1 
ATOM   23136 N  NE2   . GLN A 1 4589 ? 191.951 160.721 214.871 1.00 113.99 ? 4589 GLN A NE2   1 
ATOM   23137 N  N     . LEU A 1 4590 ? 191.527 165.223 209.418 1.00 105.19 ? 4590 LEU A N     1 
ATOM   23138 C  CA    . LEU A 1 4590 ? 192.244 166.196 208.606 1.00 112.35 ? 4590 LEU A CA    1 
ATOM   23139 C  C     . LEU A 1 4590 ? 192.520 167.438 209.446 1.00 112.51 ? 4590 LEU A C     1 
ATOM   23140 O  O     . LEU A 1 4590 ? 191.621 167.957 210.116 1.00 109.94 ? 4590 LEU A O     1 
ATOM   23141 C  CB    . LEU A 1 4590 ? 191.466 166.522 207.328 1.00 109.27 ? 4590 LEU A CB    1 
ATOM   23142 C  CG    . LEU A 1 4590 ? 190.007 166.994 207.292 1.00 105.00 ? 4590 LEU A CG    1 
ATOM   23143 C  CD1   . LEU A 1 4590 ? 189.828 168.451 207.694 1.00 108.85 ? 4590 LEU A CD1   1 
ATOM   23144 C  CD2   . LEU A 1 4590 ? 189.421 166.743 205.910 1.00 103.51 ? 4590 LEU A CD2   1 
ATOM   23145 N  N     . ARG A 1 4591 ? 193.773 167.882 209.437 1.00 130.23 ? 4591 ARG A N     1 
ATOM   23146 C  CA    . ARG A 1 4591 ? 194.227 169.019 210.221 1.00 125.73 ? 4591 ARG A CA    1 
ATOM   23147 C  C     . ARG A 1 4591 ? 194.844 170.054 209.294 1.00 126.86 ? 4591 ARG A C     1 
ATOM   23148 O  O     . ARG A 1 4591 ? 195.342 169.716 208.216 1.00 127.93 ? 4591 ARG A O     1 
ATOM   23149 C  CB    . ARG A 1 4591 ? 195.255 168.596 211.272 1.00 125.00 ? 4591 ARG A CB    1 
ATOM   23150 C  CG    . ARG A 1 4591 ? 194.722 167.660 212.338 1.00 124.84 ? 4591 ARG A CG    1 
ATOM   23151 C  CD    . ARG A 1 4591 ? 195.848 167.162 213.227 1.00 126.86 ? 4591 ARG A CD    1 
ATOM   23152 N  NE    . ARG A 1 4591 ? 196.976 168.086 213.242 1.00 128.59 ? 4591 ARG A NE    1 
ATOM   23153 C  CZ    . ARG A 1 4591 ? 197.694 168.374 214.319 1.00 128.14 ? 4591 ARG A CZ    1 
ATOM   23154 N  NH1   . ARG A 1 4591 ? 197.432 167.823 215.492 1.00 127.31 ? 4591 ARG A NH1   1 
ATOM   23155 N  NH2   . ARG A 1 4591 ? 198.702 169.235 214.215 1.00 127.00 ? 4591 ARG A NH2   1 
ATOM   23156 N  N     . TRP A 1 4592 ? 194.805 171.313 209.713 1.00 122.16 ? 4592 TRP A N     1 
ATOM   23157 C  CA    . TRP A 1 4592 ? 195.419 172.404 208.967 1.00 125.90 ? 4592 TRP A CA    1 
ATOM   23158 C  C     . TRP A 1 4592 ? 196.432 173.102 209.863 1.00 125.69 ? 4592 TRP A C     1 
ATOM   23159 O  O     . TRP A 1 4592 ? 196.081 173.616 210.930 1.00 126.55 ? 4592 TRP A O     1 
ATOM   23160 C  CB    . TRP A 1 4592 ? 194.368 173.376 208.433 1.00 123.64 ? 4592 TRP A CB    1 
ATOM   23161 C  CG    . TRP A 1 4592 ? 193.077 172.716 208.050 1.00 123.43 ? 4592 TRP A CG    1 
ATOM   23162 C  CD1   . TRP A 1 4592 ? 192.158 172.147 208.883 1.00 123.01 ? 4592 TRP A CD1   1 
ATOM   23163 C  CD2   . TRP A 1 4592 ? 192.604 172.486 206.719 1.00 126.21 ? 4592 TRP A CD2   1 
ATOM   23164 N  NE1   . TRP A 1 4592 ? 191.123 171.617 208.155 1.00 128.91 ? 4592 TRP A NE1   1 
ATOM   23165 C  CE2   . TRP A 1 4592 ? 191.376 171.808 206.822 1.00 127.11 ? 4592 TRP A CE2   1 
ATOM   23166 C  CE3   . TRP A 1 4592 ? 193.093 172.803 205.450 1.00 125.91 ? 4592 TRP A CE3   1 
ATOM   23167 C  CZ2   . TRP A 1 4592 ? 190.634 171.440 205.706 1.00 125.80 ? 4592 TRP A CZ2   1 
ATOM   23168 C  CZ3   . TRP A 1 4592 ? 192.352 172.435 204.344 1.00 123.72 ? 4592 TRP A CZ3   1 
ATOM   23169 C  CH2   . TRP A 1 4592 ? 191.135 171.767 204.479 1.00 122.71 ? 4592 TRP A CH2   1 
ATOM   23170 N  N     . VAL A 1 4593 ? 197.688 173.116 209.419 1.00 136.13 ? 4593 VAL A N     1 
ATOM   23171 C  CA    . VAL A 1 4593 ? 198.791 173.720 210.148 1.00 136.85 ? 4593 VAL A CA    1 
ATOM   23172 C  C     . VAL A 1 4593 ? 199.524 174.661 209.204 1.00 139.56 ? 4593 VAL A C     1 
ATOM   23173 O  O     . VAL A 1 4593 ? 199.328 174.636 207.987 1.00 141.25 ? 4593 VAL A O     1 
ATOM   23174 C  CB    . VAL A 1 4593 ? 199.761 172.666 210.723 1.00 137.59 ? 4593 VAL A CB    1 
ATOM   23175 C  CG1   . VAL A 1 4593 ? 199.069 171.832 211.790 1.00 136.26 ? 4593 VAL A CG1   1 
ATOM   23176 C  CG2   . VAL A 1 4593 ? 200.291 171.776 209.611 1.00 136.64 ? 4593 VAL A CG2   1 
ATOM   23177 N  N     . LYS A 1 4594 ? 200.369 175.507 209.785 1.00 154.08 ? 4594 LYS A N     1 
ATOM   23178 C  CA    . LYS A 1 4594 ? 201.115 176.477 208.995 1.00 153.80 ? 4594 LYS A CA    1 
ATOM   23179 C  C     . LYS A 1 4594 ? 202.073 175.770 208.044 1.00 154.86 ? 4594 LYS A C     1 
ATOM   23180 O  O     . LYS A 1 4594 ? 202.678 174.753 208.394 1.00 154.01 ? 4594 LYS A O     1 
ATOM   23181 C  CB    . LYS A 1 4594 ? 201.882 177.424 209.917 1.00 152.71 ? 4594 LYS A CB    1 
ATOM   23182 C  CG    . LYS A 1 4594 ? 202.550 178.580 209.196 1.00 152.49 ? 4594 LYS A CG    1 
ATOM   23183 C  CD    . LYS A 1 4594 ? 201.520 179.592 208.726 1.00 152.27 ? 4594 LYS A CD    1 
ATOM   23184 C  CE    . LYS A 1 4594 ? 202.180 180.892 208.304 1.00 153.46 ? 4594 LYS A CE    1 
ATOM   23185 N  NZ    . LYS A 1 4594 ? 202.992 180.723 207.068 1.00 154.28 ? 4594 LYS A NZ    1 
ATOM   23186 N  N     . GLN A 1 4595 ? 202.206 176.313 206.837 1.00 158.04 ? 4595 GLN A N     1 
ATOM   23187 C  CA    . GLN A 1 4595 ? 203.101 175.726 205.849 1.00 159.73 ? 4595 GLN A CA    1 
ATOM   23188 C  C     . GLN A 1 4595 ? 204.554 176.004 206.210 1.00 160.92 ? 4595 GLN A C     1 
ATOM   23189 O  O     . GLN A 1 4595 ? 204.934 177.141 206.504 1.00 159.15 ? 4595 GLN A O     1 
ATOM   23190 C  CB    . GLN A 1 4595 ? 202.793 176.278 204.457 1.00 159.05 ? 4595 GLN A CB    1 
ATOM   23191 C  CG    . GLN A 1 4595 ? 201.589 175.641 203.783 1.00 158.64 ? 4595 GLN A CG    1 
ATOM   23192 C  CD    . GLN A 1 4595 ? 201.869 175.243 202.347 1.00 160.45 ? 4595 GLN A CD    1 
ATOM   23193 O  OE1   . GLN A 1 4595 ? 202.881 174.606 202.052 1.00 162.18 ? 4595 GLN A OE1   1 
ATOM   23194 N  NE2   . GLN A 1 4595 ? 200.971 175.618 201.443 1.00 158.35 ? 4595 GLN A NE2   1 
ATOM   23195 N  N     . THR A 1 4596 ? 205.371 174.953 206.186 1.00 169.67 ? 4596 THR A N     1 
ATOM   23196 C  CA    . THR A 1 4596 ? 206.796 175.064 206.461 1.00 169.19 ? 4596 THR A CA    1 
ATOM   23197 C  C     . THR A 1 4596 ? 207.648 175.004 205.202 1.00 171.05 ? 4596 THR A C     1 
ATOM   23198 O  O     . THR A 1 4596 ? 208.877 175.080 205.304 1.00 171.67 ? 4596 THR A O     1 
ATOM   23199 C  CB    . THR A 1 4596 ? 207.238 173.963 207.433 1.00 168.31 ? 4596 THR A CB    1 
ATOM   23200 O  OG1   . THR A 1 4596 ? 206.989 172.679 206.849 1.00 169.01 ? 4596 THR A OG1   1 
ATOM   23201 C  CG2   . THR A 1 4596 ? 206.476 174.075 208.745 1.00 167.38 ? 4596 THR A CG2   1 
ATOM   23202 N  N     . ASN A 1 4597 ? 207.024 174.876 204.028 1.00 177.90 ? 4597 ASN A N     1 
ATOM   23203 C  CA    . ASN A 1 4597 ? 207.691 174.806 202.721 1.00 178.09 ? 4597 ASN A CA    1 
ATOM   23204 C  C     . ASN A 1 4597 ? 208.973 173.976 202.773 1.00 178.17 ? 4597 ASN A C     1 
ATOM   23205 O  O     . ASN A 1 4597 ? 210.033 174.375 202.285 1.00 178.49 ? 4597 ASN A O     1 
ATOM   23206 C  CB    . ASN A 1 4597 ? 207.951 176.208 202.154 1.00 176.61 ? 4597 ASN A CB    1 
ATOM   23207 C  CG    . ASN A 1 4597 ? 208.710 177.112 203.110 1.00 176.22 ? 4597 ASN A CG    1 
ATOM   23208 O  OD1   . ASN A 1 4597 ? 209.852 176.836 203.478 1.00 175.82 ? 4597 ASN A OD1   1 
ATOM   23209 N  ND2   . ASN A 1 4597 ? 208.071 178.201 203.520 1.00 176.46 ? 4597 ASN A ND2   1 
ATOM   23210 N  N     . THR A 1 4598 ? 208.860 172.789 203.364 1.00 176.19 ? 4598 THR A N     1 
ATOM   23211 C  CA    . THR A 1 4598 ? 209.970 171.850 203.453 1.00 175.11 ? 4598 THR A CA    1 
ATOM   23212 C  C     . THR A 1 4598 ? 209.931 170.792 202.358 1.00 175.91 ? 4598 THR A C     1 
ATOM   23213 O  O     . THR A 1 4598 ? 210.689 169.819 202.429 1.00 176.28 ? 4598 THR A O     1 
ATOM   23214 C  CB    . THR A 1 4598 ? 209.985 171.172 204.826 1.00 175.99 ? 4598 THR A CB    1 
ATOM   23215 O  OG1   . THR A 1 4598 ? 208.692 170.619 205.103 1.00 177.38 ? 4598 THR A OG1   1 
ATOM   23216 C  CG2   . THR A 1 4598 ? 210.348 172.174 205.912 1.00 175.36 ? 4598 THR A CG2   1 
ATOM   23217 N  N     . GLU A 1 4599 ? 209.064 170.957 201.365 1.00 169.98 ? 4599 GLU A N     1 
ATOM   23218 C  CA    . GLU A 1 4599 ? 208.929 170.033 200.224 1.00 170.38 ? 4599 GLU A CA    1 
ATOM   23219 C  C     . GLU A 1 4599 ? 208.503 168.671 200.781 1.00 168.40 ? 4599 GLU A C     1 
ATOM   23220 O  O     . GLU A 1 4599 ? 207.686 168.612 201.712 1.00 166.74 ? 4599 GLU A O     1 
ATOM   23221 C  CB    . GLU A 1 4599 ? 210.207 170.023 199.407 1.00 170.18 ? 4599 GLU A CB    1 
ATOM   23222 C  CG    . GLU A 1 4599 ? 210.563 171.365 198.791 1.00 168.76 ? 4599 GLU A CG    1 
ATOM   23223 C  CD    . GLU A 1 4599 ? 211.860 171.319 198.007 1.00 169.33 ? 4599 GLU A CD    1 
ATOM   23224 O  OE1   . GLU A 1 4599 ? 211.959 170.501 197.068 1.00 169.44 ? 4599 GLU A OE1   1 
ATOM   23225 O  OE2   . GLU A 1 4599 ? 212.780 172.099 198.330 1.00 170.36 ? 4599 GLU A OE2   1 
ATOM   23226 N  N     . LYS A 1 4600 ? 209.025 167.573 200.244 1.00 156.61 ? 4600 LYS A N     1 
ATOM   23227 C  CA    . LYS A 1 4600 ? 208.680 166.233 200.687 1.00 156.92 ? 4600 LYS A CA    1 
ATOM   23228 C  C     . LYS A 1 4600 ? 209.883 165.570 201.345 1.00 154.72 ? 4600 LYS A C     1 
ATOM   23229 O  O     . LYS A 1 4600 ? 211.027 166.006 201.191 1.00 153.72 ? 4600 LYS A O     1 
ATOM   23230 C  CB    . LYS A 1 4600 ? 208.189 165.376 199.515 1.00 156.95 ? 4600 LYS A CB    1 
ATOM   23231 C  CG    . LYS A 1 4600 ? 207.097 166.024 198.678 1.00 156.54 ? 4600 LYS A CG    1 
ATOM   23232 C  CD    . LYS A 1 4600 ? 205.924 166.466 199.538 1.00 156.35 ? 4600 LYS A CD    1 
ATOM   23233 C  CE    . LYS A 1 4600 ? 204.997 167.395 198.772 1.00 154.40 ? 4600 LYS A CE    1 
ATOM   23234 N  NZ    . LYS A 1 4600 ? 203.857 167.861 199.608 1.00 153.17 ? 4600 LYS A NZ    1 
ATOM   23235 N  N     . LYS A 1 4601 ? 209.606 164.500 202.088 1.00 148.00 ? 4601 LYS A N     1 
ATOM   23236 C  CA    . LYS A 1 4601 ? 210.634 163.718 202.758 1.00 149.68 ? 4601 LYS A CA    1 
ATOM   23237 C  C     . LYS A 1 4601 ? 211.175 162.594 201.882 1.00 151.74 ? 4601 LYS A C     1 
ATOM   23238 O  O     . LYS A 1 4601 ? 211.674 161.594 202.414 1.00 152.61 ? 4601 LYS A O     1 
ATOM   23239 C  CB    . LYS A 1 4601 ? 210.086 163.147 204.068 1.00 148.60 ? 4601 LYS A CB    1 
ATOM   23240 C  CG    . LYS A 1 4601 ? 211.092 163.101 205.206 1.00 148.59 ? 4601 LYS A CG    1 
ATOM   23241 C  CD    . LYS A 1 4601 ? 210.610 162.193 206.326 1.00 149.27 ? 4601 LYS A CD    1 
ATOM   23242 C  CE    . LYS A 1 4601 ? 209.239 162.619 206.829 1.00 148.32 ? 4601 LYS A CE    1 
ATOM   23243 N  NZ    . LYS A 1 4601 ? 208.785 161.791 207.980 1.00 148.16 ? 4601 LYS A NZ    1 
ATOM   23244 N  N     . ALA A 1 4602 ? 211.059 162.728 200.557 1.00 140.88 ? 4602 ALA A N     1 
ATOM   23245 C  CA    . ALA A 1 4602 ? 211.490 161.721 199.590 1.00 137.64 ? 4602 ALA A CA    1 
ATOM   23246 C  C     . ALA A 1 4602 ? 210.705 160.423 199.750 1.00 138.10 ? 4602 ALA A C     1 
ATOM   23247 O  O     . ALA A 1 4602 ? 211.003 159.424 199.087 1.00 136.81 ? 4602 ALA A O     1 
ATOM   23248 C  CB    . ALA A 1 4602 ? 212.994 161.457 199.706 1.00 136.99 ? 4602 ALA A CB    1 
ATOM   23249 N  N     . SER A 1 4603 ? 209.702 160.429 200.630 1.00 127.19 ? 4603 SER A N     1 
ATOM   23250 C  CA    . SER A 1 4603 ? 208.846 159.271 200.854 1.00 125.68 ? 4603 SER A CA    1 
ATOM   23251 C  C     . SER A 1 4603 ? 207.398 159.693 201.068 1.00 123.85 ? 4603 SER A C     1 
ATOM   23252 O  O     . SER A 1 4603 ? 206.656 159.029 201.799 1.00 125.43 ? 4603 SER A O     1 
ATOM   23253 C  CB    . SER A 1 4603 ? 209.336 158.447 202.047 1.00 124.54 ? 4603 SER A CB    1 
ATOM   23254 O  OG    . SER A 1 4603 ? 209.244 159.188 203.251 1.00 123.33 ? 4603 SER A OG    1 
ATOM   23255 N  N     . VAL A 1 4604 ? 206.982 160.792 200.444 1.00 111.32 ? 4604 VAL A N     1 
ATOM   23256 C  CA    . VAL A 1 4604 ? 205.634 161.328 200.585 1.00 112.43 ? 4604 VAL A CA    1 
ATOM   23257 C  C     . VAL A 1 4604 ? 204.953 161.276 199.226 1.00 113.48 ? 4604 VAL A C     1 
ATOM   23258 O  O     . VAL A 1 4604 ? 205.494 161.778 198.233 1.00 116.30 ? 4604 VAL A O     1 
ATOM   23259 C  CB    . VAL A 1 4604 ? 205.652 162.763 201.140 1.00 112.02 ? 4604 VAL A CB    1 
ATOM   23260 C  CG1   . VAL A 1 4604 ? 204.322 163.449 200.884 1.00 111.20 ? 4604 VAL A CG1   1 
ATOM   23261 C  CG2   . VAL A 1 4604 ? 205.973 162.751 202.624 1.00 114.56 ? 4604 VAL A CG2   1 
ATOM   23262 N  N     . VAL A 1 4605 ? 203.768 160.673 199.183 1.00 92.99  ? 4605 VAL A N     1 
ATOM   23263 C  CA    . VAL A 1 4605 ? 202.996 160.517 197.957 1.00 85.33  ? 4605 VAL A CA    1 
ATOM   23264 C  C     . VAL A 1 4605 ? 201.739 161.368 198.057 1.00 84.05  ? 4605 VAL A C     1 
ATOM   23265 O  O     . VAL A 1 4605 ? 201.007 161.302 199.051 1.00 89.60  ? 4605 VAL A O     1 
ATOM   23266 C  CB    . VAL A 1 4605 ? 202.653 159.036 197.698 1.00 87.20  ? 4605 VAL A CB    1 
ATOM   23267 C  CG1   . VAL A 1 4605 ? 202.105 158.383 198.957 1.00 88.91  ? 4605 VAL A CG1   1 
ATOM   23268 C  CG2   . VAL A 1 4605 ? 201.653 158.913 196.563 1.00 89.75  ? 4605 VAL A CG2   1 
ATOM   23269 N  N     . THR A 1 4606 ? 201.496 162.179 197.029 1.00 82.44  ? 4606 THR A N     1 
ATOM   23270 C  CA    . THR A 1 4606 ? 200.316 163.039 196.973 1.00 85.03  ? 4606 THR A CA    1 
ATOM   23271 C  C     . THR A 1 4606 ? 199.199 162.266 196.284 1.00 89.75  ? 4606 THR A C     1 
ATOM   23272 O  O     . THR A 1 4606 ? 199.146 162.188 195.055 1.00 95.82  ? 4606 THR A O     1 
ATOM   23273 C  CB    . THR A 1 4606 ? 200.624 164.341 196.243 1.00 83.48  ? 4606 THR A CB    1 
ATOM   23274 O  OG1   . THR A 1 4606 ? 201.727 164.998 196.879 1.00 88.79  ? 4606 THR A OG1   1 
ATOM   23275 C  CG2   . THR A 1 4606 ? 199.415 165.260 196.269 1.00 80.12  ? 4606 THR A CG2   1 
ATOM   23276 N  N     . LEU A 1 4607 ? 198.307 161.693 197.078 1.00 79.84  ? 4607 LEU A N     1 
ATOM   23277 C  CA    . LEU A 1 4607 ? 197.218 160.868 196.568 1.00 72.53  ? 4607 LEU A CA    1 
ATOM   23278 C  C     . LEU A 1 4607 ? 196.017 161.734 196.221 1.00 76.23  ? 4607 LEU A C     1 
ATOM   23279 O  O     . LEU A 1 4607 ? 195.553 162.505 197.068 1.00 83.23  ? 4607 LEU A O     1 
ATOM   23280 C  CB    . LEU A 1 4607 ? 196.810 159.826 197.595 1.00 68.15  ? 4607 LEU A CB    1 
ATOM   23281 C  CG    . LEU A 1 4607 ? 197.904 158.836 197.978 1.00 76.44  ? 4607 LEU A CG    1 
ATOM   23282 C  CD1   . LEU A 1 4607 ? 198.222 158.988 199.442 1.00 81.49  ? 4607 LEU A CD1   1 
ATOM   23283 C  CD2   . LEU A 1 4607 ? 197.455 157.424 197.681 1.00 80.90  ? 4607 LEU A CD2   1 
ATOM   23284 N  N     . PRO A 1 4608 ? 195.497 161.649 195.001 1.00 65.89  ? 4608 PRO A N     1 
ATOM   23285 C  CA    . PRO A 1 4608 ? 194.251 162.351 194.688 1.00 64.84  ? 4608 PRO A CA    1 
ATOM   23286 C  C     . PRO A 1 4608 ? 193.087 161.767 195.469 1.00 68.16  ? 4608 PRO A C     1 
ATOM   23287 O  O     . PRO A 1 4608 ? 193.029 160.565 195.737 1.00 80.85  ? 4608 PRO A O     1 
ATOM   23288 C  CB    . PRO A 1 4608 ? 194.081 162.121 193.184 1.00 67.47  ? 4608 PRO A CB    1 
ATOM   23289 C  CG    . PRO A 1 4608 ? 194.818 160.854 192.917 1.00 66.53  ? 4608 PRO A CG    1 
ATOM   23290 C  CD    . PRO A 1 4608 ? 195.977 160.835 193.872 1.00 68.48  ? 4608 PRO A CD    1 
ATOM   23291 N  N     . VAL A 1 4609 ? 192.149 162.636 195.834 1.00 64.88  ? 4609 VAL A N     1 
ATOM   23292 C  CA    . VAL A 1 4609 ? 190.925 162.229 196.514 1.00 65.14  ? 4609 VAL A CA    1 
ATOM   23293 C  C     . VAL A 1 4609 ? 189.784 162.477 195.539 1.00 64.02  ? 4609 VAL A C     1 
ATOM   23294 O  O     . VAL A 1 4609 ? 189.403 163.630 195.300 1.00 64.82  ? 4609 VAL A O     1 
ATOM   23295 C  CB    . VAL A 1 4609 ? 190.701 162.984 197.832 1.00 65.76  ? 4609 VAL A CB    1 
ATOM   23296 C  CG1   . VAL A 1 4609 ? 189.247 162.881 198.274 1.00 63.56  ? 4609 VAL A CG1   1 
ATOM   23297 C  CG2   . VAL A 1 4609 ? 191.632 162.459 198.911 1.00 73.88  ? 4609 VAL A CG2   1 
ATOM   23298 N  N     . TYR A 1 4610 ? 189.260 161.405 194.954 1.00 76.92  ? 4610 TYR A N     1 
ATOM   23299 C  CA    . TYR A 1 4610 ? 188.164 161.514 194.008 1.00 71.71  ? 4610 TYR A CA    1 
ATOM   23300 C  C     . TYR A 1 4610 ? 186.832 161.390 194.741 1.00 77.34  ? 4610 TYR A C     1 
ATOM   23301 O  O     . TYR A 1 4610 ? 186.774 161.248 195.964 1.00 86.29  ? 4610 TYR A O     1 
ATOM   23302 C  CB    . TYR A 1 4610 ? 188.301 160.465 192.908 1.00 71.15  ? 4610 TYR A CB    1 
ATOM   23303 C  CG    . TYR A 1 4610 ? 189.497 160.680 192.009 1.00 70.35  ? 4610 TYR A CG    1 
ATOM   23304 C  CD1   . TYR A 1 4610 ? 189.470 161.640 191.008 1.00 69.88  ? 4610 TYR A CD1   1 
ATOM   23305 C  CD2   . TYR A 1 4610 ? 190.650 159.924 192.160 1.00 74.71  ? 4610 TYR A CD2   1 
ATOM   23306 C  CE1   . TYR A 1 4610 ? 190.558 161.844 190.183 1.00 69.41  ? 4610 TYR A CE1   1 
ATOM   23307 C  CE2   . TYR A 1 4610 ? 191.742 160.120 191.338 1.00 78.27  ? 4610 TYR A CE2   1 
ATOM   23308 C  CZ    . TYR A 1 4610 ? 191.691 161.081 190.353 1.00 75.21  ? 4610 TYR A CZ    1 
ATOM   23309 O  OH    . TYR A 1 4610 ? 192.776 161.280 189.532 1.00 74.56  ? 4610 TYR A OH    1 
ATOM   23310 N  N     . LEU A 1 4611 ? 185.740 161.445 193.980 1.00 84.26  ? 4611 LEU A N     1 
ATOM   23311 C  CA    . LEU A 1 4611 ? 184.421 161.405 194.596 1.00 83.73  ? 4611 LEU A CA    1 
ATOM   23312 C  C     . LEU A 1 4611 ? 183.807 160.012 194.529 1.00 88.78  ? 4611 LEU A C     1 
ATOM   23313 O  O     . LEU A 1 4611 ? 183.251 159.530 195.521 1.00 92.63  ? 4611 LEU A O     1 
ATOM   23314 C  CB    . LEU A 1 4611 ? 183.504 162.427 193.929 1.00 81.03  ? 4611 LEU A CB    1 
ATOM   23315 C  CG    . LEU A 1 4611 ? 182.083 162.498 194.479 1.00 86.12  ? 4611 LEU A CG    1 
ATOM   23316 C  CD1   . LEU A 1 4611 ? 182.105 162.830 195.959 1.00 89.95  ? 4611 LEU A CD1   1 
ATOM   23317 C  CD2   . LEU A 1 4611 ? 181.293 163.533 193.716 1.00 86.99  ? 4611 LEU A CD2   1 
ATOM   23318 N  N     . ASN A 1 4612 ? 183.899 159.350 193.378 1.00 87.70  ? 4612 ASN A N     1 
ATOM   23319 C  CA    . ASN A 1 4612 ? 183.333 158.020 193.202 1.00 84.43  ? 4612 ASN A CA    1 
ATOM   23320 C  C     . ASN A 1 4612 ? 184.329 157.175 192.416 1.00 88.44  ? 4612 ASN A C     1 
ATOM   23321 O  O     . ASN A 1 4612 ? 185.441 157.615 192.108 1.00 92.11  ? 4612 ASN A O     1 
ATOM   23322 C  CB    . ASN A 1 4612 ? 181.963 158.103 192.518 1.00 81.40  ? 4612 ASN A CB    1 
ATOM   23323 C  CG    . ASN A 1 4612 ? 181.941 159.105 191.385 1.00 86.10  ? 4612 ASN A CG    1 
ATOM   23324 O  OD1   . ASN A 1 4612 ? 182.988 159.538 190.905 1.00 92.31  ? 4612 ASN A OD1   1 
ATOM   23325 N  ND2   . ASN A 1 4612 ? 180.745 159.484 190.952 1.00 85.18  ? 4612 ASN A ND2   1 
ATOM   23326 N  N     . PHE A 1 4613 ? 183.923 155.947 192.084 1.00 85.04  ? 4613 PHE A N     1 
ATOM   23327 C  CA    . PHE A 1 4613 ? 184.815 155.023 191.394 1.00 84.00  ? 4613 PHE A CA    1 
ATOM   23328 C  C     . PHE A 1 4613 ? 185.152 155.477 189.981 1.00 85.49  ? 4613 PHE A C     1 
ATOM   23329 O  O     . PHE A 1 4613 ? 186.164 155.033 189.428 1.00 91.57  ? 4613 PHE A O     1 
ATOM   23330 C  CB    . PHE A 1 4613 ? 184.197 153.624 191.356 1.00 85.62  ? 4613 PHE A CB    1 
ATOM   23331 C  CG    . PHE A 1 4613 ? 182.762 153.606 190.913 1.00 91.72  ? 4613 PHE A CG    1 
ATOM   23332 C  CD1   . PHE A 1 4613 ? 181.738 153.564 191.843 1.00 93.52  ? 4613 PHE A CD1   1 
ATOM   23333 C  CD2   . PHE A 1 4613 ? 182.438 153.624 189.567 1.00 90.09  ? 4613 PHE A CD2   1 
ATOM   23334 C  CE1   . PHE A 1 4613 ? 180.416 153.546 191.439 1.00 92.84  ? 4613 PHE A CE1   1 
ATOM   23335 C  CE2   . PHE A 1 4613 ? 181.119 153.606 189.157 1.00 89.91  ? 4613 PHE A CE2   1 
ATOM   23336 C  CZ    . PHE A 1 4613 ? 180.107 153.566 190.094 1.00 90.73  ? 4613 PHE A CZ    1 
ATOM   23337 N  N     . THR A 1 4614 ? 184.334 156.345 189.383 1.00 80.95  ? 4614 THR A N     1 
ATOM   23338 C  CA    . THR A 1 4614 ? 184.609 156.812 188.031 1.00 83.37  ? 4614 THR A CA    1 
ATOM   23339 C  C     . THR A 1 4614 ? 185.834 157.713 187.964 1.00 84.06  ? 4614 THR A C     1 
ATOM   23340 O  O     . THR A 1 4614 ? 186.377 157.914 186.872 1.00 89.87  ? 4614 THR A O     1 
ATOM   23341 C  CB    . THR A 1 4614 ? 183.396 157.554 187.469 1.00 82.67  ? 4614 THR A CB    1 
ATOM   23342 O  OG1   . THR A 1 4614 ? 183.162 158.742 188.235 1.00 89.46  ? 4614 THR A OG1   1 
ATOM   23343 C  CG2   . THR A 1 4614 ? 182.161 156.669 187.521 1.00 81.68  ? 4614 THR A CG2   1 
ATOM   23344 N  N     . ARG A 1 4615 ? 186.279 158.253 189.101 1.00 74.80  ? 4615 ARG A N     1 
ATOM   23345 C  CA    . ARG A 1 4615 ? 187.442 159.141 189.157 1.00 77.39  ? 4615 ARG A CA    1 
ATOM   23346 C  C     . ARG A 1 4615 ? 187.282 160.321 188.203 1.00 77.41  ? 4615 ARG A C     1 
ATOM   23347 O  O     . ARG A 1 4615 ? 188.225 160.727 187.522 1.00 86.26  ? 4615 ARG A O     1 
ATOM   23348 C  CB    . ARG A 1 4615 ? 188.736 158.377 188.867 1.00 77.76  ? 4615 ARG A CB    1 
ATOM   23349 C  CG    . ARG A 1 4615 ? 188.995 157.223 189.818 1.00 75.51  ? 4615 ARG A CG    1 
ATOM   23350 C  CD    . ARG A 1 4615 ? 190.468 156.867 189.872 1.00 69.70  ? 4615 ARG A CD    1 
ATOM   23351 N  NE    . ARG A 1 4615 ? 190.700 155.645 190.632 1.00 71.42  ? 4615 ARG A NE    1 
ATOM   23352 C  CZ    . ARG A 1 4615 ? 191.894 155.218 191.018 1.00 78.43  ? 4615 ARG A CZ    1 
ATOM   23353 N  NH1   . ARG A 1 4615 ? 192.994 155.890 190.726 1.00 77.75  ? 4615 ARG A NH1   1 
ATOM   23354 N  NH2   . ARG A 1 4615 ? 191.985 154.088 191.712 1.00 79.60  ? 4615 ARG A NH2   1 
ATOM   23355 N  N     . ALA A 1 4616 ? 186.072 160.873 188.150 1.00 70.03  ? 4616 ALA A N     1 
ATOM   23356 C  CA    . ALA A 1 4616 ? 185.780 161.995 187.267 1.00 77.71  ? 4616 ALA A CA    1 
ATOM   23357 C  C     . ALA A 1 4616 ? 185.852 163.335 187.986 1.00 80.84  ? 4616 ALA A C     1 
ATOM   23358 O  O     . ALA A 1 4616 ? 186.139 164.359 187.357 1.00 81.00  ? 4616 ALA A O     1 
ATOM   23359 C  CB    . ALA A 1 4616 ? 184.398 161.820 186.633 1.00 82.51  ? 4616 ALA A CB    1 
ATOM   23360 N  N     . ASP A 1 4617 ? 185.596 163.352 189.291 1.00 91.07  ? 4617 ASP A N     1 
ATOM   23361 C  CA    . ASP A 1 4617 ? 185.592 164.575 190.082 1.00 91.83  ? 4617 ASP A CA    1 
ATOM   23362 C  C     . ASP A 1 4617 ? 186.734 164.499 191.086 1.00 92.48  ? 4617 ASP A C     1 
ATOM   23363 O  O     . ASP A 1 4617 ? 186.901 163.482 191.766 1.00 96.71  ? 4617 ASP A O     1 
ATOM   23364 C  CB    . ASP A 1 4617 ? 184.247 164.759 190.789 1.00 94.06  ? 4617 ASP A CB    1 
ATOM   23365 C  CG    . ASP A 1 4617 ? 184.155 166.065 191.574 1.00 99.22  ? 4617 ASP A CG    1 
ATOM   23366 O  OD1   . ASP A 1 4617 ? 183.089 166.711 191.501 1.00 97.52  ? 4617 ASP A OD1   1 
ATOM   23367 O  OD2   . ASP A 1 4617 ? 185.119 166.445 192.272 1.00 98.94  ? 4617 ASP A OD2   1 
ATOM   23368 N  N     . LEU A 1 4618 ? 187.511 165.576 191.177 1.00 77.64  ? 4618 LEU A N     1 
ATOM   23369 C  CA    . LEU A 1 4618 ? 188.616 165.672 192.125 1.00 80.65  ? 4618 LEU A CA    1 
ATOM   23370 C  C     . LEU A 1 4618 ? 188.181 166.596 193.256 1.00 81.70  ? 4618 LEU A C     1 
ATOM   23371 O  O     . LEU A 1 4618 ? 187.726 167.717 193.009 1.00 88.17  ? 4618 LEU A O     1 
ATOM   23372 C  CB    . LEU A 1 4618 ? 189.869 166.200 191.433 1.00 84.77  ? 4618 LEU A CB    1 
ATOM   23373 C  CG    . LEU A 1 4618 ? 191.090 166.545 192.288 1.00 87.91  ? 4618 LEU A CG    1 
ATOM   23374 C  CD1   . LEU A 1 4618 ? 191.363 165.474 193.333 1.00 83.53  ? 4618 LEU A CD1   1 
ATOM   23375 C  CD2   . LEU A 1 4618 ? 192.304 166.768 191.407 1.00 88.84  ? 4618 LEU A CD2   1 
ATOM   23376 N  N     . ILE A 1 4619 ? 188.321 166.132 194.498 1.00 86.26  ? 4619 ILE A N     1 
ATOM   23377 C  CA    . ILE A 1 4619 ? 187.840 166.914 195.634 1.00 83.88  ? 4619 ILE A CA    1 
ATOM   23378 C  C     . ILE A 1 4619 ? 188.993 167.675 196.283 1.00 85.73  ? 4619 ILE A C     1 
ATOM   23379 O  O     . ILE A 1 4619 ? 188.978 168.909 196.357 1.00 91.09  ? 4619 ILE A O     1 
ATOM   23380 C  CB    . ILE A 1 4619 ? 187.114 166.007 196.642 1.00 84.56  ? 4619 ILE A CB    1 
ATOM   23381 C  CG1   . ILE A 1 4619 ? 185.769 165.564 196.069 1.00 80.17  ? 4619 ILE A CG1   1 
ATOM   23382 C  CG2   . ILE A 1 4619 ? 186.859 166.753 197.929 1.00 83.94  ? 4619 ILE A CG2   1 
ATOM   23383 C  CD1   . ILE A 1 4619 ? 184.888 166.709 195.627 1.00 83.23  ? 4619 ILE A CD1   1 
ATOM   23384 N  N     . PHE A 1 4620 ? 190.005 166.956 196.758 1.00 80.16  ? 4620 PHE A N     1 
ATOM   23385 C  CA    . PHE A 1 4620 ? 191.221 167.580 197.276 1.00 77.69  ? 4620 PHE A CA    1 
ATOM   23386 C  C     . PHE A 1 4620 ? 192.349 166.556 197.192 1.00 80.83  ? 4620 PHE A C     1 
ATOM   23387 O  O     . PHE A 1 4620 ? 192.212 165.511 196.548 1.00 90.17  ? 4620 PHE A O     1 
ATOM   23388 C  CB    . PHE A 1 4620 ? 191.016 168.115 198.700 1.00 77.59  ? 4620 PHE A CB    1 
ATOM   23389 C  CG    . PHE A 1 4620 ? 190.815 167.047 199.742 1.00 80.78  ? 4620 PHE A CG    1 
ATOM   23390 C  CD1   . PHE A 1 4620 ? 189.610 166.377 199.851 1.00 79.53  ? 4620 PHE A CD1   1 
ATOM   23391 C  CD2   . PHE A 1 4620 ? 191.826 166.737 200.634 1.00 87.42  ? 4620 PHE A CD2   1 
ATOM   23392 C  CE1   . PHE A 1 4620 ? 189.424 165.405 200.814 1.00 78.32  ? 4620 PHE A CE1   1 
ATOM   23393 C  CE2   . PHE A 1 4620 ? 191.643 165.768 201.600 1.00 84.52  ? 4620 PHE A CE2   1 
ATOM   23394 C  CZ    . PHE A 1 4620 ? 190.442 165.101 201.689 1.00 77.69  ? 4620 PHE A CZ    1 
ATOM   23395 N  N     . THR A 1 4621 ? 193.476 166.860 197.834 1.00 78.30  ? 4621 THR A N     1 
ATOM   23396 C  CA    . THR A 1 4621 ? 194.655 166.007 197.794 1.00 79.08  ? 4621 THR A CA    1 
ATOM   23397 C  C     . THR A 1 4621 ? 195.163 165.762 199.207 1.00 82.55  ? 4621 THR A C     1 
ATOM   23398 O  O     . THR A 1 4621 ? 194.978 166.589 200.104 1.00 84.03  ? 4621 THR A O     1 
ATOM   23399 C  CB    . THR A 1 4621 ? 195.777 166.625 196.947 1.00 84.25  ? 4621 THR A CB    1 
ATOM   23400 O  OG1   . THR A 1 4621 ? 196.204 167.857 197.541 1.00 90.54  ? 4621 THR A OG1   1 
ATOM   23401 C  CG2   . THR A 1 4621 ? 195.299 166.888 195.528 1.00 79.41  ? 4621 THR A CG2   1 
ATOM   23402 N  N     . VAL A 1 4622 ? 195.814 164.614 199.397 1.00 86.27  ? 4622 VAL A N     1 
ATOM   23403 C  CA    . VAL A 1 4622 ? 196.331 164.213 200.697 1.00 89.28  ? 4622 VAL A CA    1 
ATOM   23404 C  C     . VAL A 1 4622 ? 197.804 163.854 200.561 1.00 92.40  ? 4622 VAL A C     1 
ATOM   23405 O  O     . VAL A 1 4622 ? 198.285 163.491 199.486 1.00 94.27  ? 4622 VAL A O     1 
ATOM   23406 C  CB    . VAL A 1 4622 ? 195.548 163.023 201.294 1.00 92.02  ? 4622 VAL A CB    1 
ATOM   23407 C  CG1   . VAL A 1 4622 ? 194.199 163.478 201.808 1.00 89.68  ? 4622 VAL A CG1   1 
ATOM   23408 C  CG2   . VAL A 1 4622 ? 195.383 161.923 200.263 1.00 93.02  ? 4622 VAL A CG2   1 
ATOM   23409 N  N     . ASP A 1 4623 ? 198.550 164.006 201.657 1.00 102.56 ? 4623 ASP A N     1 
ATOM   23410 C  CA    . ASP A 1 4623 ? 200.015 163.760 201.591 1.00 102.97 ? 4623 ASP A CA    1 
ATOM   23411 C  C     . ASP A 1 4623 ? 200.403 162.657 202.581 1.00 103.80 ? 4623 ASP A C     1 
ATOM   23412 O  O     . ASP A 1 4623 ? 201.072 162.976 203.581 1.00 104.47 ? 4623 ASP A O     1 
ATOM   23413 C  CB    . ASP A 1 4623 ? 200.802 165.050 201.835 1.00 103.45 ? 4623 ASP A CB    1 
ATOM   23414 C  CG    . ASP A 1 4623 ? 200.679 166.052 200.700 1.00 105.63 ? 4623 ASP A CG    1 
ATOM   23415 O  OD1   . ASP A 1 4623 ? 201.276 167.140 200.814 1.00 108.95 ? 4623 ASP A OD1   1 
ATOM   23416 O  OD2   . ASP A 1 4623 ? 199.992 165.734 199.710 1.00 102.70 ? 4623 ASP A OD2   1 
ATOM   23417 N  N     . PHE A 1 4624 ? 199.999 161.415 202.308 1.00 104.22 ? 4624 PHE A N     1 
ATOM   23418 C  CA    . PHE A 1 4624 ? 200.407 160.280 203.175 1.00 102.82 ? 4624 PHE A CA    1 
ATOM   23419 C  C     . PHE A 1 4624 ? 201.884 159.970 202.917 1.00 104.74 ? 4624 PHE A C     1 
ATOM   23420 O  O     . PHE A 1 4624 ? 202.400 160.363 201.852 1.00 108.94 ? 4624 PHE A O     1 
ATOM   23421 C  CB    . PHE A 1 4624 ? 199.529 159.057 202.904 1.00 105.16 ? 4624 PHE A CB    1 
ATOM   23422 C  CG    . PHE A 1 4624 ? 198.114 159.176 203.410 1.00 107.52 ? 4624 PHE A CG    1 
ATOM   23423 C  CD1   . PHE A 1 4624 ? 197.854 159.304 204.764 1.00 109.71 ? 4624 PHE A CD1   1 
ATOM   23424 C  CD2   . PHE A 1 4624 ? 197.043 159.172 202.532 1.00 103.00 ? 4624 PHE A CD2   1 
ATOM   23425 C  CE1   . PHE A 1 4624 ? 196.554 159.415 205.229 1.00 108.63 ? 4624 PHE A CE1   1 
ATOM   23426 C  CE2   . PHE A 1 4624 ? 195.743 159.284 202.997 1.00 101.52 ? 4624 PHE A CE2   1 
ATOM   23427 C  CZ    . PHE A 1 4624 ? 195.501 159.405 204.345 1.00 106.39 ? 4624 PHE A CZ    1 
ATOM   23428 N  N     . GLU A 1 4625 ? 202.539 159.290 203.861 1.00 112.24 ? 4625 GLU A N     1 
ATOM   23429 C  CA    . GLU A 1 4625 ? 203.968 158.918 203.685 1.00 113.91 ? 4625 GLU A CA    1 
ATOM   23430 C  C     . GLU A 1 4625 ? 204.060 157.430 203.335 1.00 114.62 ? 4625 GLU A C     1 
ATOM   23431 O  O     . GLU A 1 4625 ? 203.536 156.609 204.112 1.00 118.62 ? 4625 GLU A O     1 
ATOM   23432 C  CB    . GLU A 1 4625 ? 204.764 159.236 204.951 1.00 114.55 ? 4625 GLU A CB    1 
ATOM   23433 C  CG    . GLU A 1 4625 ? 206.242 158.912 204.831 1.00 115.23 ? 4625 GLU A CG    1 
ATOM   23434 C  CD    . GLU A 1 4625 ? 207.097 159.403 205.986 1.00 116.46 ? 4625 GLU A CD    1 
ATOM   23435 O  OE1   . GLU A 1 4625 ? 206.536 160.013 206.918 1.00 117.64 ? 4625 GLU A OE1   1 
ATOM   23436 O  OE2   . GLU A 1 4625 ? 208.323 159.178 205.949 1.00 116.85 ? 4625 GLU A OE2   1 
ATOM   23437 N  N     . ILE A 1 4626 ? 204.703 157.103 202.211 1.00 106.04 ? 4626 ILE A N     1 
ATOM   23438 C  CA    . ILE A 1 4626 ? 204.881 155.676 201.811 1.00 107.25 ? 4626 ILE A CA    1 
ATOM   23439 C  C     . ILE A 1 4626 ? 205.667 154.968 202.917 1.00 106.49 ? 4626 ILE A C     1 
ATOM   23440 O  O     . ILE A 1 4626 ? 206.505 155.629 203.558 1.00 104.67 ? 4626 ILE A O     1 
ATOM   23441 C  CB    . ILE A 1 4626 ? 205.585 155.572 200.445 1.00 110.30 ? 4626 ILE A CB    1 
ATOM   23442 C  CG1   . ILE A 1 4626 ? 206.978 156.203 200.479 1.00 111.81 ? 4626 ILE A CG1   1 
ATOM   23443 C  CG2   . ILE A 1 4626 ? 204.723 156.171 199.345 1.00 106.49 ? 4626 ILE A CG2   1 
ATOM   23444 C  CD1   . ILE A 1 4626 ? 207.537 156.524 199.115 1.00 108.77 ? 4626 ILE A CD1   1 
ATOM   23445 N  N     . ALA A 1 4627 ? 205.402 153.678 203.132 1.00 113.07 ? 4627 ALA A N     1 
ATOM   23446 C  CA    . ALA A 1 4627 ? 206.065 152.941 204.233 1.00 115.51 ? 4627 ALA A CA    1 
ATOM   23447 C  C     . ALA A 1 4627 ? 207.262 152.150 203.703 1.00 120.40 ? 4627 ALA A C     1 
ATOM   23448 O  O     . ALA A 1 4627 ? 207.321 151.918 202.481 1.00 121.14 ? 4627 ALA A O     1 
ATOM   23449 C  CB    . ALA A 1 4627 ? 205.071 152.024 204.898 1.00 116.05 ? 4627 ALA A CB    1 
ATOM   23450 N  N     . THR A 1 4628 ? 208.183 151.767 204.591 1.00 133.88 ? 4628 THR A N     1 
ATOM   23451 C  CA    . THR A 1 4628 ? 209.340 150.923 204.187 1.00 133.62 ? 4628 THR A CA    1 
ATOM   23452 C  C     . THR A 1 4628 ? 209.994 151.486 202.922 1.00 132.59 ? 4628 THR A C     1 
ATOM   23453 O  O     . THR A 1 4628 ? 210.248 152.705 202.884 1.00 128.53 ? 4628 THR A O     1 
ATOM   23454 C  CB    . THR A 1 4628 ? 208.913 149.465 203.974 1.00 130.24 ? 4628 THR A CB    1 
ATOM   23455 O  OG1   . THR A 1 4628 ? 208.067 149.405 202.825 1.00 132.31 ? 4628 THR A OG1   1 
ATOM   23456 C  CG2   . THR A 1 4628 ? 208.194 148.883 205.171 1.00 127.54 ? 4628 THR A CG2   1 
ATOM   23457 N  N     . LYS A 1 4629 ? 210.248 150.625 201.932 1.00 133.73 ? 4629 LYS A N     1 
ATOM   23458 C  CA    . LYS A 1 4629 ? 210.947 151.062 200.695 1.00 133.94 ? 4629 LYS A CA    1 
ATOM   23459 C  C     . LYS A 1 4629 ? 209.945 151.166 199.541 1.00 133.66 ? 4629 LYS A C     1 
ATOM   23460 O  O     . LYS A 1 4629 ? 210.391 151.206 198.377 1.00 135.92 ? 4629 LYS A O     1 
ATOM   23461 C  CB    . LYS A 1 4629 ? 212.057 150.067 200.349 1.00 132.85 ? 4629 LYS A CB    1 
ATOM   23462 C  CG    . LYS A 1 4629 ? 211.600 148.624 200.186 1.00 130.23 ? 4629 LYS A CG    1 
ATOM   23463 C  CD    . LYS A 1 4629 ? 212.720 147.681 199.805 1.00 131.44 ? 4629 LYS A CD    1 
ATOM   23464 C  CE    . LYS A 1 4629 ? 213.855 147.674 200.806 1.00 132.47 ? 4629 LYS A CE    1 
ATOM   23465 N  NZ    . LYS A 1 4629 ? 214.941 146.752 200.398 1.00 134.19 ? 4629 LYS A NZ    1 
ATOM   23466 N  N     . GLU A 1 4630 ? 208.648 151.214 199.852 1.00 117.01 ? 4630 GLU A N     1 
ATOM   23467 C  CA    . GLU A 1 4630 ? 207.624 151.370 198.787 1.00 117.07 ? 4630 GLU A CA    1 
ATOM   23468 C  C     . GLU A 1 4630 ? 208.030 152.543 197.889 1.00 117.69 ? 4630 GLU A C     1 
ATOM   23469 O  O     . GLU A 1 4630 ? 208.210 153.654 198.421 1.00 119.89 ? 4630 GLU A O     1 
ATOM   23470 C  CB    . GLU A 1 4630 ? 206.241 151.587 199.402 1.00 114.32 ? 4630 GLU A CB    1 
ATOM   23471 C  CG    . GLU A 1 4630 ? 205.750 150.408 200.223 1.00 117.02 ? 4630 GLU A CG    1 
ATOM   23472 C  CD    . GLU A 1 4630 ? 205.462 149.149 199.424 1.00 119.74 ? 4630 GLU A CD    1 
ATOM   23473 O  OE1   . GLU A 1 4630 ? 206.395 148.627 198.783 1.00 120.08 ? 4630 GLU A OE1   1 
ATOM   23474 O  OE2   . GLU A 1 4630 ? 204.304 148.692 199.448 1.00 118.52 ? 4630 GLU A OE2   1 
ATOM   23475 N  N     . ASP A 1 4631 ? 208.172 152.297 196.584 1.00 104.63 ? 4631 ASP A N     1 
ATOM   23476 C  CA    . ASP A 1 4631 ? 208.582 153.362 195.629 1.00 103.45 ? 4631 ASP A CA    1 
ATOM   23477 C  C     . ASP A 1 4631 ? 207.409 154.325 195.424 1.00 103.92 ? 4631 ASP A C     1 
ATOM   23478 O  O     . ASP A 1 4631 ? 206.315 153.849 195.069 1.00 103.95 ? 4631 ASP A O     1 
ATOM   23479 C  CB    . ASP A 1 4631 ? 209.051 152.749 194.307 1.00 101.74 ? 4631 ASP A CB    1 
ATOM   23480 C  CG    . ASP A 1 4631 ? 209.502 153.762 193.268 1.00 106.63 ? 4631 ASP A CG    1 
ATOM   23481 O  OD1   . ASP A 1 4631 ? 209.490 154.968 193.575 1.00 106.55 ? 4631 ASP A OD1   1 
ATOM   23482 O  OD2   . ASP A 1 4631 ? 209.860 153.333 192.153 1.00 109.46 ? 4631 ASP A OD2   1 
ATOM   23483 N  N     . PRO A 1 4632 ? 207.587 155.651 195.610 1.00 96.89  ? 4632 PRO A N     1 
ATOM   23484 C  CA    . PRO A 1 4632 ? 206.515 156.610 195.347 1.00 93.80  ? 4632 PRO A CA    1 
ATOM   23485 C  C     . PRO A 1 4632 ? 206.070 156.460 193.888 1.00 93.03  ? 4632 PRO A C     1 
ATOM   23486 O  O     . PRO A 1 4632 ? 204.895 156.609 193.620 1.00 92.18  ? 4632 PRO A O     1 
ATOM   23487 C  CB    . PRO A 1 4632 ? 207.168 157.980 195.579 1.00 88.82  ? 4632 PRO A CB    1 
ATOM   23488 C  CG    . PRO A 1 4632 ? 208.657 157.706 195.530 1.00 91.78  ? 4632 PRO A CG    1 
ATOM   23489 C  CD    . PRO A 1 4632 ? 208.816 156.299 196.065 1.00 94.06  ? 4632 PRO A CD    1 
ATOM   23490 N  N     . ARG A 1 4633 ? 207.014 156.165 192.992 1.00 94.65  ? 4633 ARG A N     1 
ATOM   23491 C  CA    . ARG A 1 4633 ? 206.659 155.939 191.567 1.00 90.76  ? 4633 ARG A CA    1 
ATOM   23492 C  C     . ARG A 1 4633 ? 205.690 154.756 191.481 1.00 91.42  ? 4633 ARG A C     1 
ATOM   23493 O  O     . ARG A 1 4633 ? 204.597 154.935 190.915 1.00 99.13  ? 4633 ARG A O     1 
ATOM   23494 C  CB    . ARG A 1 4633 ? 207.908 155.661 190.729 1.00 94.67  ? 4633 ARG A CB    1 
ATOM   23495 C  CG    . ARG A 1 4633 ? 209.017 156.690 190.891 1.00 96.98  ? 4633 ARG A CG    1 
ATOM   23496 C  CD    . ARG A 1 4633 ? 210.081 156.624 189.810 1.00 96.38  ? 4633 ARG A CD    1 
ATOM   23497 N  NE    . ARG A 1 4633 ? 210.656 155.304 189.583 1.00 100.15 ? 4633 ARG A NE    1 
ATOM   23498 C  CZ    . ARG A 1 4633 ? 210.017 154.278 189.030 1.00 99.78  ? 4633 ARG A CZ    1 
ATOM   23499 N  NH1   . ARG A 1 4633 ? 209.061 154.493 188.144 1.00 96.96  ? 4633 ARG A NH1   1 
ATOM   23500 N  NH2   . ARG A 1 4633 ? 210.349 153.040 189.353 1.00 99.40  ? 4633 ARG A NH2   1 
ATOM   23501 N  N     . SER A 1 4634 ? 206.079 153.596 192.021 1.00 89.19  ? 4634 SER A N     1 
ATOM   23502 C  CA    . SER A 1 4634 ? 205.183 152.446 191.991 1.00 90.58  ? 4634 SER A CA    1 
ATOM   23503 C  C     . SER A 1 4634 ? 203.776 152.838 192.419 1.00 89.98  ? 4634 SER A C     1 
ATOM   23504 O  O     . SER A 1 4634 ? 202.789 152.333 191.873 1.00 95.70  ? 4634 SER A O     1 
ATOM   23505 C  CB    . SER A 1 4634 ? 205.726 151.330 192.883 1.00 94.67  ? 4634 SER A CB    1 
ATOM   23506 O  OG    . SER A 1 4634 ? 206.973 150.855 192.407 1.00 101.31 ? 4634 SER A OG    1 
ATOM   23507 N  N     . PHE A 1 4635 ? 203.664 153.735 193.402 1.00 82.26  ? 4635 PHE A N     1 
ATOM   23508 C  CA    . PHE A 1 4635 ? 202.351 154.237 193.795 1.00 82.31  ? 4635 PHE A CA    1 
ATOM   23509 C  C     . PHE A 1 4635 ? 201.688 154.994 192.653 1.00 77.22  ? 4635 PHE A C     1 
ATOM   23510 O  O     . PHE A 1 4635 ? 200.495 154.809 192.386 1.00 81.27  ? 4635 PHE A O     1 
ATOM   23511 C  CB    . PHE A 1 4635 ? 202.476 155.136 195.025 1.00 80.33  ? 4635 PHE A CB    1 
ATOM   23512 C  CG    . PHE A 1 4635 ? 202.483 154.391 196.327 1.00 82.09  ? 4635 PHE A CG    1 
ATOM   23513 C  CD1   . PHE A 1 4635 ? 203.572 153.623 196.699 1.00 84.55  ? 4635 PHE A CD1   1 
ATOM   23514 C  CD2   . PHE A 1 4635 ? 201.400 154.468 197.185 1.00 79.02  ? 4635 PHE A CD2   1 
ATOM   23515 C  CE1   . PHE A 1 4635 ? 203.577 152.940 197.899 1.00 82.74  ? 4635 PHE A CE1   1 
ATOM   23516 C  CE2   . PHE A 1 4635 ? 201.400 153.789 198.384 1.00 83.27  ? 4635 PHE A CE2   1 
ATOM   23517 C  CZ    . PHE A 1 4635 ? 202.489 153.024 198.742 1.00 80.98  ? 4635 PHE A CZ    1 
ATOM   23518 N  N     . TYR A 1 4636 ? 202.445 155.851 191.966 1.00 81.21  ? 4636 TYR A N     1 
ATOM   23519 C  CA    . TYR A 1 4636 ? 201.868 156.624 190.869 1.00 81.49  ? 4636 TYR A CA    1 
ATOM   23520 C  C     . TYR A 1 4636 ? 201.428 155.718 189.726 1.00 78.43  ? 4636 TYR A C     1 
ATOM   23521 O  O     . TYR A 1 4636 ? 200.349 155.909 189.154 1.00 80.06  ? 4636 TYR A O     1 
ATOM   23522 C  CB    . TYR A 1 4636 ? 202.868 157.664 190.362 1.00 80.47  ? 4636 TYR A CB    1 
ATOM   23523 C  CG    . TYR A 1 4636 ? 203.456 158.567 191.426 1.00 76.67  ? 4636 TYR A CG    1 
ATOM   23524 C  CD1   . TYR A 1 4636 ? 202.804 158.778 192.635 1.00 81.52  ? 4636 TYR A CD1   1 
ATOM   23525 C  CD2   . TYR A 1 4636 ? 204.666 159.211 191.217 1.00 81.00  ? 4636 TYR A CD2   1 
ATOM   23526 C  CE1   . TYR A 1 4636 ? 203.347 159.601 193.603 1.00 85.52  ? 4636 TYR A CE1   1 
ATOM   23527 C  CE2   . TYR A 1 4636 ? 205.213 160.037 192.177 1.00 85.51  ? 4636 TYR A CE2   1 
ATOM   23528 C  CZ    . TYR A 1 4636 ? 204.549 160.230 193.368 1.00 85.17  ? 4636 TYR A CZ    1 
ATOM   23529 O  OH    . TYR A 1 4636 ? 205.092 161.052 194.327 1.00 84.43  ? 4636 TYR A OH    1 
ATOM   23530 N  N     . GLU A 1 4637 ? 202.253 154.728 189.379 1.00 78.97  ? 4637 GLU A N     1 
ATOM   23531 C  CA    . GLU A 1 4637 ? 201.942 153.840 188.265 1.00 73.21  ? 4637 GLU A CA    1 
ATOM   23532 C  C     . GLU A 1 4637 ? 200.738 152.952 188.548 1.00 77.21  ? 4637 GLU A C     1 
ATOM   23533 O  O     . GLU A 1 4637 ? 199.924 152.719 187.648 1.00 83.50  ? 4637 GLU A O     1 
ATOM   23534 C  CB    . GLU A 1 4637 ? 203.158 152.978 187.927 1.00 77.64  ? 4637 GLU A CB    1 
ATOM   23535 C  CG    . GLU A 1 4637 ? 204.180 153.671 187.040 1.00 83.22  ? 4637 GLU A CG    1 
ATOM   23536 C  CD    . GLU A 1 4637 ? 205.502 152.932 186.988 1.00 88.25  ? 4637 GLU A CD    1 
ATOM   23537 O  OE1   . GLU A 1 4637 ? 205.552 151.768 187.437 1.00 92.96  ? 4637 GLU A OE1   1 
ATOM   23538 O  OE2   . GLU A 1 4637 ? 206.492 153.515 186.497 1.00 83.68  ? 4637 GLU A OE2   1 
ATOM   23539 N  N     . ARG A 1 4638 ? 200.605 152.453 189.774 1.00 70.20  ? 4638 ARG A N     1 
ATOM   23540 C  CA    . ARG A 1 4638 ? 199.532 151.533 190.128 1.00 64.88  ? 4638 ARG A CA    1 
ATOM   23541 C  C     . ARG A 1 4638 ? 198.183 152.222 190.280 1.00 66.90  ? 4638 ARG A C     1 
ATOM   23542 O  O     . ARG A 1 4638 ? 197.197 151.554 190.608 1.00 71.79  ? 4638 ARG A O     1 
ATOM   23543 C  CB    . ARG A 1 4638 ? 199.882 150.790 191.421 1.00 64.65  ? 4638 ARG A CB    1 
ATOM   23544 C  CG    . ARG A 1 4638 ? 200.969 149.743 191.245 1.00 74.81  ? 4638 ARG A CG    1 
ATOM   23545 C  CD    . ARG A 1 4638 ? 201.275 149.017 192.541 1.00 73.12  ? 4638 ARG A CD    1 
ATOM   23546 N  NE    . ARG A 1 4638 ? 200.149 148.223 193.014 1.00 69.65  ? 4638 ARG A NE    1 
ATOM   23547 C  CZ    . ARG A 1 4638 ? 200.245 146.972 193.441 1.00 72.74  ? 4638 ARG A CZ    1 
ATOM   23548 N  NH1   . ARG A 1 4638 ? 201.405 146.337 193.461 1.00 75.20  ? 4638 ARG A NH1   1 
ATOM   23549 N  NH2   . ARG A 1 4638 ? 199.151 146.342 193.860 1.00 76.19  ? 4638 ARG A NH2   1 
ATOM   23550 N  N     . GLY A 1 4639 ? 198.114 153.529 190.053 1.00 74.22  ? 4639 GLY A N     1 
ATOM   23551 C  CA    . GLY A 1 4639 ? 196.855 154.248 190.136 1.00 76.59  ? 4639 GLY A CA    1 
ATOM   23552 C  C     . GLY A 1 4639 ? 196.257 154.312 191.524 1.00 77.84  ? 4639 GLY A C     1 
ATOM   23553 O  O     . GLY A 1 4639 ? 195.028 154.290 191.666 1.00 77.91  ? 4639 GLY A O     1 
ATOM   23554 N  N     . VAL A 1 4640 ? 197.097 154.386 192.557 1.00 72.76  ? 4640 VAL A N     1 
ATOM   23555 C  CA    . VAL A 1 4640 ? 196.599 154.508 193.921 1.00 65.08  ? 4640 VAL A CA    1 
ATOM   23556 C  C     . VAL A 1 4640 ? 195.917 155.860 194.087 1.00 66.09  ? 4640 VAL A C     1 
ATOM   23557 O  O     . VAL A 1 4640 ? 196.382 156.879 193.559 1.00 72.03  ? 4640 VAL A O     1 
ATOM   23558 C  CB    . VAL A 1 4640 ? 197.741 154.305 194.930 1.00 67.09  ? 4640 VAL A CB    1 
ATOM   23559 C  CG1   . VAL A 1 4640 ? 198.708 155.477 194.914 1.00 75.78  ? 4640 VAL A CG1   1 
ATOM   23560 C  CG2   . VAL A 1 4640 ? 197.187 154.094 196.326 1.00 64.33  ? 4640 VAL A CG2   1 
ATOM   23561 N  N     . ALA A 1 4641 ? 194.789 155.868 194.792 1.00 72.09  ? 4641 ALA A N     1 
ATOM   23562 C  CA    . ALA A 1 4641 ? 194.007 157.083 194.984 1.00 76.16  ? 4641 ALA A CA    1 
ATOM   23563 C  C     . ALA A 1 4641 ? 193.051 156.868 196.151 1.00 73.68  ? 4641 ALA A C     1 
ATOM   23564 O  O     . ALA A 1 4641 ? 193.075 155.827 196.814 1.00 84.81  ? 4641 ALA A O     1 
ATOM   23565 C  CB    . ALA A 1 4641 ? 193.263 157.462 193.697 1.00 70.50  ? 4641 ALA A CB    1 
ATOM   23566 N  N     . VAL A 1 4642 ? 192.203 157.862 196.400 1.00 57.36  ? 4642 VAL A N     1 
ATOM   23567 C  CA    . VAL A 1 4642 ? 191.232 157.833 197.486 1.00 59.56  ? 4642 VAL A CA    1 
ATOM   23568 C  C     . VAL A 1 4642 ? 189.860 158.162 196.918 1.00 63.99  ? 4642 VAL A C     1 
ATOM   23569 O  O     . VAL A 1 4642 ? 189.708 159.123 196.156 1.00 74.16  ? 4642 VAL A O     1 
ATOM   23570 C  CB    . VAL A 1 4642 ? 191.605 158.823 198.610 1.00 59.42  ? 4642 VAL A CB    1 
ATOM   23571 C  CG1   . VAL A 1 4642 ? 190.529 158.844 199.681 1.00 62.60  ? 4642 VAL A CG1   1 
ATOM   23572 C  CG2   . VAL A 1 4642 ? 192.953 158.468 199.209 1.00 62.59  ? 4642 VAL A CG2   1 
ATOM   23573 N  N     . LEU A 1 4643 ? 188.861 157.365 197.287 1.00 73.86  ? 4643 LEU A N     1 
ATOM   23574 C  CA    . LEU A 1 4643 ? 187.484 157.584 196.869 1.00 70.60  ? 4643 LEU A CA    1 
ATOM   23575 C  C     . LEU A 1 4643 ? 186.636 157.965 198.072 1.00 76.71  ? 4643 LEU A C     1 
ATOM   23576 O  O     . LEU A 1 4643 ? 186.806 157.413 199.164 1.00 83.80  ? 4643 LEU A O     1 
ATOM   23577 C  CB    . LEU A 1 4643 ? 186.895 156.342 196.199 1.00 73.45  ? 4643 LEU A CB    1 
ATOM   23578 C  CG    . LEU A 1 4643 ? 187.651 155.779 194.999 1.00 74.65  ? 4643 LEU A CG    1 
ATOM   23579 C  CD1   . LEU A 1 4643 ? 186.837 154.677 194.352 1.00 74.31  ? 4643 LEU A CD1   1 
ATOM   23580 C  CD2   . LEU A 1 4643 ? 187.969 156.877 194.000 1.00 73.84  ? 4643 LEU A CD2   1 
ATOM   23581 N  N     . CYS A 1 4644 ? 185.719 158.911 197.865 1.00 77.14  ? 4644 CYS A N     1 
ATOM   23582 C  CA    . CYS A 1 4644 ? 184.853 159.355 198.949 1.00 77.37  ? 4644 CYS A CA    1 
ATOM   23583 C  C     . CYS A 1 4644 ? 183.690 158.402 199.194 1.00 82.43  ? 4644 CYS A C     1 
ATOM   23584 O  O     . CYS A 1 4644 ? 183.023 158.516 200.228 1.00 84.78  ? 4644 CYS A O     1 
ATOM   23585 C  CB    . CYS A 1 4644 ? 184.323 160.758 198.656 1.00 78.71  ? 4644 CYS A CB    1 
ATOM   23586 S  SG    . CYS A 1 4644 ? 185.523 162.078 198.942 1.00 95.18  ? 4644 CYS A SG    1 
ATOM   23587 N  N     . THR A 1 4645 ? 183.434 157.472 198.280 1.00 93.14  ? 4645 THR A N     1 
ATOM   23588 C  CA    . THR A 1 4645 ? 182.341 156.519 198.448 1.00 92.31  ? 4645 THR A CA    1 
ATOM   23589 C  C     . THR A 1 4645 ? 182.578 155.245 197.643 1.00 85.06  ? 4645 THR A C     1 
ATOM   23590 O  O     . THR A 1 4645 ? 183.377 155.227 196.708 1.00 87.96  ? 4645 THR A O     1 
ATOM   23591 C  CB    . THR A 1 4645 ? 180.991 157.129 198.030 1.00 92.05  ? 4645 THR A CB    1 
ATOM   23592 O  OG1   . THR A 1 4645 ? 179.937 156.204 198.323 1.00 93.15  ? 4645 THR A OG1   1 
ATOM   23593 C  CG2   . THR A 1 4645 ? 180.983 157.439 196.544 1.00 87.78  ? 4645 THR A CG2   1 
HETATM 23594 P  PB    . ADP B 2 .    ? 188.709 181.222 175.768 1.00 94.68  ? 4701 ADP A PB    1 
HETATM 23595 O  O1B   . ADP B 2 .    ? 188.856 181.124 174.271 1.00 75.78  ? 4701 ADP A O1B   1 
HETATM 23596 O  O2B   . ADP B 2 .    ? 187.333 180.836 176.246 1.00 77.61  ? 4701 ADP A O2B   1 
HETATM 23597 O  O3B   . ADP B 2 .    ? 189.808 180.511 176.513 1.00 82.68  ? 4701 ADP A O3B   1 
HETATM 23598 P  PA    . ADP B 2 .    ? 189.982 183.849 175.654 1.00 76.78  ? 4701 ADP A PA    1 
HETATM 23599 O  O1A   . ADP B 2 .    ? 191.320 183.190 175.635 1.00 73.67  ? 4701 ADP A O1A   1 
HETATM 23600 O  O2A   . ADP B 2 .    ? 189.498 184.508 174.405 1.00 67.80  ? 4701 ADP A O2A   1 
HETATM 23601 O  O3A   . ADP B 2 .    ? 188.888 182.780 176.129 1.00 78.58  ? 4701 ADP A O3A   1 
HETATM 23602 O  "O5'" . ADP B 2 .    ? 189.928 184.899 176.863 1.00 76.31  ? 4701 ADP A "O5'" 1 
HETATM 23603 C  "C5'" . ADP B 2 .    ? 190.388 184.461 178.164 1.00 68.52  ? 4701 ADP A "C5'" 1 
HETATM 23604 C  "C4'" . ADP B 2 .    ? 190.266 185.602 179.142 1.00 69.63  ? 4701 ADP A "C4'" 1 
HETATM 23605 O  "O4'" . ADP B 2 .    ? 191.331 185.491 180.120 1.00 65.96  ? 4701 ADP A "O4'" 1 
HETATM 23606 C  "C3'" . ADP B 2 .    ? 190.438 187.005 178.553 1.00 74.18  ? 4701 ADP A "C3'" 1 
HETATM 23607 O  "O3'" . ADP B 2 .    ? 189.850 187.986 179.396 1.00 72.61  ? 4701 ADP A "O3'" 1 
HETATM 23608 C  "C2'" . ADP B 2 .    ? 191.961 187.125 178.554 1.00 69.63  ? 4701 ADP A "C2'" 1 
HETATM 23609 O  "O2'" . ADP B 2 .    ? 192.424 188.453 178.438 1.00 79.99  ? 4701 ADP A "O2'" 1 
HETATM 23610 C  "C1'" . ADP B 2 .    ? 192.280 186.514 179.915 1.00 65.24  ? 4701 ADP A "C1'" 1 
HETATM 23611 N  N9    . ADP B 2 .    ? 193.611 185.928 179.991 1.00 58.63  ? 4701 ADP A N9    1 
HETATM 23612 C  C8    . ADP B 2 .    ? 193.962 184.645 179.656 1.00 67.49  ? 4701 ADP A C8    1 
HETATM 23613 N  N7    . ADP B 2 .    ? 195.236 184.395 179.824 1.00 66.98  ? 4701 ADP A N7    1 
HETATM 23614 C  C5    . ADP B 2 .    ? 195.761 185.588 180.298 1.00 62.21  ? 4701 ADP A C5    1 
HETATM 23615 C  C6    . ADP B 2 .    ? 197.065 185.967 180.669 1.00 66.91  ? 4701 ADP A C6    1 
HETATM 23616 N  N6    . ADP B 2 .    ? 198.113 185.152 180.616 1.00 67.19  ? 4701 ADP A N6    1 
HETATM 23617 N  N1    . ADP B 2 .    ? 197.247 187.237 181.101 1.00 72.70  ? 4701 ADP A N1    1 
HETATM 23618 C  C2    . ADP B 2 .    ? 196.186 188.052 181.151 1.00 74.46  ? 4701 ADP A C2    1 
HETATM 23619 N  N3    . ADP B 2 .    ? 194.920 187.807 180.830 1.00 74.00  ? 4701 ADP A N3    1 
HETATM 23620 C  C4    . ADP B 2 .    ? 194.768 186.542 180.405 1.00 63.96  ? 4701 ADP A C4    1 
HETATM 23621 P  PG    . ATP C 3 .    ? 159.605 190.241 182.021 1.00 74.03  ? 4702 ATP A PG    1 
HETATM 23622 O  O1G   . ATP C 3 .    ? 160.546 189.218 182.555 1.00 63.65  ? 4702 ATP A O1G   1 
HETATM 23623 O  O2G   . ATP C 3 .    ? 160.146 190.995 180.807 1.00 70.44  ? 4702 ATP A O2G   1 
HETATM 23624 O  O3G   . ATP C 3 .    ? 158.218 189.688 181.690 1.00 72.35  ? 4702 ATP A O3G   1 
HETATM 23625 P  PB    . ATP C 3 .    ? 160.093 192.560 183.830 1.00 67.80  ? 4702 ATP A PB    1 
HETATM 23626 O  O1B   . ATP C 3 .    ? 160.747 192.120 185.077 1.00 74.61  ? 4702 ATP A O1B   1 
HETATM 23627 O  O2B   . ATP C 3 .    ? 161.005 193.205 182.790 1.00 69.26  ? 4702 ATP A O2B   1 
HETATM 23628 O  O3B   . ATP C 3 .    ? 159.334 191.375 183.105 1.00 60.60  ? 4702 ATP A O3B   1 
HETATM 23629 P  PA    . ATP C 3 .    ? 158.509 195.039 183.634 1.00 73.15  ? 4702 ATP A PA    1 
HETATM 23630 O  O1A   . ATP C 3 .    ? 158.355 195.104 182.167 1.00 72.24  ? 4702 ATP A O1A   1 
HETATM 23631 O  O2A   . ATP C 3 .    ? 159.543 195.995 184.223 1.00 72.64  ? 4702 ATP A O2A   1 
HETATM 23632 O  O3A   . ATP C 3 .    ? 158.907 193.584 184.108 1.00 58.43  ? 4702 ATP A O3A   1 
HETATM 23633 O  "O5'" . ATP C 3 .    ? 157.131 195.286 184.362 1.00 63.45  ? 4702 ATP A "O5'" 1 
HETATM 23634 C  "C5'" . ATP C 3 .    ? 156.993 195.098 185.786 1.00 58.09  ? 4702 ATP A "C5'" 1 
HETATM 23635 C  "C4'" . ATP C 3 .    ? 155.615 195.543 186.201 1.00 61.10  ? 4702 ATP A "C4'" 1 
HETATM 23636 O  "O4'" . ATP C 3 .    ? 155.705 196.308 187.420 1.00 62.65  ? 4702 ATP A "O4'" 1 
HETATM 23637 C  "C3'" . ATP C 3 .    ? 154.911 196.470 185.220 1.00 62.94  ? 4702 ATP A "C3'" 1 
HETATM 23638 O  "O3'" . ATP C 3 .    ? 153.499 196.408 185.385 1.00 65.63  ? 4702 ATP A "O3'" 1 
HETATM 23639 C  "C2'" . ATP C 3 .    ? 155.468 197.839 185.613 1.00 66.03  ? 4702 ATP A "C2'" 1 
HETATM 23640 O  "O2'" . ATP C 3 .    ? 154.551 198.885 185.314 1.00 67.79  ? 4702 ATP A "O2'" 1 
HETATM 23641 C  "C1'" . ATP C 3 .    ? 155.639 197.694 187.130 1.00 62.46  ? 4702 ATP A "C1'" 1 
HETATM 23642 N  N9    . ATP C 3 .    ? 156.847 198.324 187.649 1.00 58.31  ? 4702 ATP A N9    1 
HETATM 23643 C  C8    . ATP C 3 .    ? 158.132 198.124 187.220 1.00 65.21  ? 4702 ATP A C8    1 
HETATM 23644 N  N7    . ATP C 3 .    ? 159.029 198.825 187.870 1.00 68.06  ? 4702 ATP A N7    1 
HETATM 23645 C  C5    . ATP C 3 .    ? 158.280 199.537 188.795 1.00 55.46  ? 4702 ATP A C5    1 
HETATM 23646 C  C6    . ATP C 3 .    ? 158.635 200.468 189.790 1.00 66.72  ? 4702 ATP A C6    1 
HETATM 23647 N  N6    . ATP C 3 .    ? 159.891 200.857 190.032 1.00 64.76  ? 4702 ATP A N6    1 
HETATM 23648 N  N1    . ATP C 3 .    ? 157.643 200.992 190.541 1.00 70.28  ? 4702 ATP A N1    1 
HETATM 23649 C  C2    . ATP C 3 .    ? 156.386 200.609 190.305 1.00 71.69  ? 4702 ATP A C2    1 
HETATM 23650 N  N3    . ATP C 3 .    ? 155.933 199.742 189.398 1.00 68.00  ? 4702 ATP A N3    1 
HETATM 23651 C  C4    . ATP C 3 .    ? 156.934 199.238 188.670 1.00 55.21  ? 4702 ATP A C4    1 
HETATM 23652 P  PB    . ADP D 2 .    ? 135.891 173.881 172.262 1.00 80.09  ? 4703 ADP A PB    1 
HETATM 23653 O  O1B   . ADP D 2 .    ? 136.126 174.960 171.235 1.00 67.76  ? 4703 ADP A O1B   1 
HETATM 23654 O  O2B   . ADP D 2 .    ? 136.200 172.482 171.788 1.00 70.09  ? 4703 ADP A O2B   1 
HETATM 23655 O  O3B   . ADP D 2 .    ? 136.431 174.205 173.633 1.00 70.00  ? 4703 ADP A O3B   1 
HETATM 23656 P  PA    . ADP D 2 .    ? 133.276 174.092 171.259 1.00 81.95  ? 4703 ADP A PA    1 
HETATM 23657 O  O1A   . ADP D 2 .    ? 132.652 175.459 171.395 1.00 63.62  ? 4703 ADP A O1A   1 
HETATM 23658 O  O2A   . ADP D 2 .    ? 133.932 173.694 169.960 1.00 69.59  ? 4703 ADP A O2A   1 
HETATM 23659 O  O3A   . ADP D 2 .    ? 134.299 173.872 172.481 1.00 69.80  ? 4703 ADP A O3A   1 
HETATM 23660 O  "O5'" . ADP D 2 .    ? 132.146 172.998 171.586 1.00 71.61  ? 4703 ADP A "O5'" 1 
HETATM 23661 C  "C5'" . ADP D 2 .    ? 131.247 173.196 172.671 1.00 57.95  ? 4703 ADP A "C5'" 1 
HETATM 23662 C  "C4'" . ADP D 2 .    ? 129.964 172.424 172.407 1.00 56.46  ? 4703 ADP A "C4'" 1 
HETATM 23663 O  "O4'" . ADP D 2 .    ? 129.213 172.292 173.615 1.00 58.98  ? 4703 ADP A "O4'" 1 
HETATM 23664 C  "C3'" . ADP D 2 .    ? 129.103 173.166 171.404 1.00 62.70  ? 4703 ADP A "C3'" 1 
HETATM 23665 O  "O3'" . ADP D 2 .    ? 128.914 172.368 170.233 1.00 66.69  ? 4703 ADP A "O3'" 1 
HETATM 23666 C  "C2'" . ADP D 2 .    ? 127.774 173.390 172.089 1.00 66.73  ? 4703 ADP A "C2'" 1 
HETATM 23667 O  "O2'" . ADP D 2 .    ? 126.721 172.862 171.279 1.00 75.69  ? 4703 ADP A "O2'" 1 
HETATM 23668 C  "C1'" . ADP D 2 .    ? 127.843 172.640 173.409 1.00 60.19  ? 4703 ADP A "C1'" 1 
HETATM 23669 N  N9    . ADP D 2 .    ? 127.401 173.517 174.520 1.00 58.03  ? 4703 ADP A N9    1 
HETATM 23670 C  C8    . ADP D 2 .    ? 128.091 173.734 175.655 1.00 65.52  ? 4703 ADP A C8    1 
HETATM 23671 N  N7    . ADP D 2 .    ? 127.425 174.577 176.481 1.00 67.27  ? 4703 ADP A N7    1 
HETATM 23672 C  C5    . ADP D 2 .    ? 126.276 174.912 175.871 1.00 60.27  ? 4703 ADP A C5    1 
HETATM 23673 C  C6    . ADP D 2 .    ? 125.113 175.768 176.193 1.00 65.51  ? 4703 ADP A C6    1 
HETATM 23674 N  N6    . ADP D 2 .    ? 125.048 176.450 177.361 1.00 72.57  ? 4703 ADP A N6    1 
HETATM 23675 N  N1    . ADP D 2 .    ? 124.119 175.847 175.283 1.00 70.06  ? 4703 ADP A N1    1 
HETATM 23676 C  C2    . ADP D 2 .    ? 124.171 175.175 174.120 1.00 68.57  ? 4703 ADP A C2    1 
HETATM 23677 N  N3    . ADP D 2 .    ? 125.195 174.381 173.764 1.00 62.33  ? 4703 ADP A N3    1 
HETATM 23678 C  C4    . ADP D 2 .    ? 126.260 174.208 174.582 1.00 58.31  ? 4703 ADP A C4    1 
HETATM 23679 P  PB    . ADP E 2 .    ? 142.785 150.678 151.790 1.00 89.84  ? 4704 ADP A PB    1 
HETATM 23680 O  O1B   . ADP E 2 .    ? 141.420 150.598 152.426 1.00 72.97  ? 4704 ADP A O1B   1 
HETATM 23681 O  O2B   . ADP E 2 .    ? 143.009 151.903 150.940 1.00 78.27  ? 4704 ADP A O2B   1 
HETATM 23682 O  O3B   . ADP E 2 .    ? 143.928 150.349 152.718 1.00 77.75  ? 4704 ADP A O3B   1 
HETATM 23683 P  PA    . ADP E 2 .    ? 141.879 149.562 149.402 1.00 80.79  ? 4704 ADP A PA    1 
HETATM 23684 O  O1A   . ADP E 2 .    ? 140.458 149.850 149.815 1.00 68.97  ? 4704 ADP A O1A   1 
HETATM 23685 O  O2A   . ADP E 2 .    ? 142.570 150.474 148.419 1.00 76.86  ? 4704 ADP A O2A   1 
HETATM 23686 O  O3A   . ADP E 2 .    ? 142.780 149.469 150.730 1.00 72.54  ? 4704 ADP A O3A   1 
HETATM 23687 O  "O5'" . ADP E 2 .    ? 141.931 148.060 148.831 1.00 79.28  ? 4704 ADP A "O5'" 1 
HETATM 23688 C  "C5'" . ADP E 2 .    ? 141.288 147.740 147.602 1.00 73.15  ? 4704 ADP A "C5'" 1 
HETATM 23689 C  "C4'" . ADP E 2 .    ? 141.287 146.231 147.408 1.00 68.18  ? 4704 ADP A "C4'" 1 
HETATM 23690 O  "O4'" . ADP E 2 .    ? 140.699 145.588 148.539 1.00 65.57  ? 4704 ADP A "O4'" 1 
HETATM 23691 C  "C3'" . ADP E 2 .    ? 140.470 145.836 146.192 1.00 67.29  ? 4704 ADP A "C3'" 1 
HETATM 23692 O  "O3'" . ADP E 2 .    ? 141.328 145.318 145.172 1.00 76.72  ? 4704 ADP A "O3'" 1 
HETATM 23693 C  "C2'" . ADP E 2 .    ? 139.520 144.755 146.662 1.00 70.83  ? 4704 ADP A "C2'" 1 
HETATM 23694 O  "O2'" . ADP E 2 .    ? 139.731 143.559 145.909 1.00 75.71  ? 4704 ADP A "O2'" 1 
HETATM 23695 C  "C1'" . ADP E 2 .    ? 139.856 144.512 148.122 1.00 64.16  ? 4704 ADP A "C1'" 1 
HETATM 23696 N  N9    . ADP E 2 .    ? 138.616 144.512 148.932 1.00 65.99  ? 4704 ADP A N9    1 
HETATM 23697 C  C8    . ADP E 2 .    ? 138.306 145.409 149.883 1.00 72.78  ? 4704 ADP A C8    1 
HETATM 23698 N  N7    . ADP E 2 .    ? 137.104 145.133 150.448 1.00 73.69  ? 4704 ADP A N7    1 
HETATM 23699 C  C5    . ADP E 2 .    ? 136.626 144.028 149.850 1.00 65.72  ? 4704 ADP A C5    1 
HETATM 23700 C  C6    . ADP E 2 .    ? 135.406 143.198 149.969 1.00 64.94  ? 4704 ADP A C6    1 
HETATM 23701 N  N6    . ADP E 2 .    ? 134.436 143.505 150.863 1.00 68.26  ? 4704 ADP A N6    1 
HETATM 23702 N  N1    . ADP E 2 .    ? 135.295 142.126 149.156 1.00 66.56  ? 4704 ADP A N1    1 
HETATM 23703 C  C2    . ADP E 2 .    ? 136.254 141.813 148.265 1.00 71.37  ? 4704 ADP A C2    1 
HETATM 23704 N  N3    . ADP E 2 .    ? 137.383 142.523 148.103 1.00 65.79  ? 4704 ADP A N3    1 
HETATM 23705 C  C4    . ADP E 2 .    ? 137.627 143.620 148.855 1.00 64.94  ? 4704 ADP A C4    1 
HETATM 23706 MG MG    . MG  F 4 .    ? 160.254 192.935 180.656 1.00 45.69  ? 4705 MG  A MG    1 
# 
